Entry Entry Name Active site Binding site Catalytic activity Cofactor Kinetics Transit peptide Signal peptide Post-translational modification Modified residue Uniquename Beta strand Helix Turn Propeptide Chain Glycosylation Disulfide bond Lipidation Sequence C6Y4D0 DPB3_SCHPO SPCC16C4.22; STRAND 26..28; /evidence="ECO:0007829|PDB:5Y27"; STRAND 61..63; /evidence="ECO:0007829|PDB:5Y27" HELIX 12..19; /evidence="ECO:0007829|PDB:5Y27"; HELIX 30..57; /evidence="ECO:0007829|PDB:5Y27"; HELIX 65..74; /evidence="ECO:0007829|PDB:5Y27"; HELIX 76..81; /evidence="ECO:0007829|PDB:5Y27" TURN 82..86; /evidence="ECO:0007829|PDB:5Y27" CHAIN 1..87; /note="DNA polymerase epsilon subunit C"; /id="PRO_0000389112" MEKTYGKTVLPLSRVKRIIKQDEDVHYCSNASALLISVATELFVEKLATEAYQLAKLQKRKGIRYRDVEDVVRKDDQFEFLSDLFSI G2TRN4 ERH_SCHPO SPAC19G12.17; STRAND 9..16; /evidence="ECO:0007829|PDB:6S2W"; STRAND 17..19; /evidence="ECO:0007829|PDB:6AKJ"; STRAND 24..30; /evidence="ECO:0007829|PDB:6S2W"; STRAND 67..75; /evidence="ECO:0007829|PDB:6S2W"; STRAND 80..83; /evidence="ECO:0007829|PDB:6S2W" HELIX 20..22; /evidence="ECO:0007829|PDB:6S2W"; HELIX 31..44; /evidence="ECO:0007829|PDB:6S2W"; HELIX 56..65; /evidence="ECO:0007829|PDB:6S2W"; HELIX 86..99; /evidence="ECO:0007829|PDB:6S2W" TURN 76..79; /evidence="ECO:0007829|PDB:6S2W" CHAIN 1..104; /note="Enhancer of rudimentary homolog 1"; /id="PRO_0000416492" MSPPPAESHIILLIQQGSDPKTRIWSDHCSLRSAIEYIVGVYQTNQAVSEKESIDVSRFFNFFDEIYDCVPLVYDRHFRAYIPHEKQWLLHHAQEYLTAARQIP O00102 UBC7_SCHPO ACT_SITE 90; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; PTM: Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation. {ECO:0000250|UniProtKB:Q02159}. SPBP16F5.04; STRAND 25..28; /evidence="ECO:0007829|PDB:6OP8"; STRAND 37..43; /evidence="ECO:0007829|PDB:6OP8"; STRAND 54..60; /evidence="ECO:0007829|PDB:6OP8"; STRAND 71..76; /evidence="ECO:0007829|PDB:6OP8"; STRAND 87..89; /evidence="ECO:0007829|PDB:6OP8" HELIX 5..20; /evidence="ECO:0007829|PDB:6OP8"; HELIX 32..34; /evidence="ECO:0007829|PDB:6OP8"; HELIX 92..94; /evidence="ECO:0007829|PDB:6OP8"; HELIX 117..129; /evidence="ECO:0007829|PDB:6OP8"; HELIX 139..147; /evidence="ECO:0007829|PDB:6OP8"; HELIX 149..166; /evidence="ECO:0007829|PDB:6OP8" TURN 49..52; /evidence="ECO:0007829|PDB:6OP8"; TURN 63..66; /evidence="ECO:0007829|PDB:6OP8"; TURN 101..103; /evidence="ECO:0007829|PDB:6OP8" CHAIN 1..166; /note="Ubiquitin-conjugating enzyme E2-18 kDa"; /id="PRO_0000082553" MSKAMALRRLMKEYKELTENGPDGITAGPSNEDDFFTWDCLIQGPDGTPFEGGLYPATLKFPSDYPLGPPTLKFECEFFHPNVYKDGTVCISILHAPGDDPNMYESSSERWSPVQSVEKILLSVMSMLAEPNDESGANIDACKMWREDREEYCRVVRRLARKTLGL O00103 UBC11_SCHPO ACT_SITE 113; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPCC1259.15c; CHAIN 1..176; /note="Ubiquitin-conjugating enzyme E2-20 kDa"; /id="PRO_0000082566" MDSDMQNQNPHTNSKNSSSAGMAVDGHSVTKRLRSELMSLMMSNTPGISAFPDSDSNLLHWAGTITGPSDTYYEGLKFKISMSFPANYPYSPPTIIFTSPMWHPNVDMSGNICLDILKDKWSAVYNVQTILLSLQSLLGEPNNASPLNAQAAELWSKDPIEYKRLLMQRYKEIDEI O13282 TAF5_SCHPO MOD_RES 256; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC5E4.03c; CHAIN 1..643; /note="Transcription initiation factor TFIID subunit 5"; /id="PRO_0000051259" MSATNGPQPQDLNRIVLDYLAKKGYSRTEAMLRLEASGSGVSVEEKLKSIEETPDAYTHTYTILRDWVDSSLELYKAELHRILFPIFVHSYLNLLSQDHYEAAKQFYELFKDDHTDLHDFDVKNLKSLSLPSHVAEDRTAQQYRQNKYQLHFSRITFDLLLHFLFENVSNGGSIIIKLINQHIDIHIVPGRPTVLENAKVINEQEGITGQSFERGDAQLQPVKLQQMPMDKEMEKIVEMDLEEEDMMHQNDPNNQSPKLLKEFRKLHEPNAEDAPSRDYIPLPPHKGVDILSEVEAVKDWSKRLHLGPRASLPSVCMYTFHHTNNNMNCAEFSPDSTMIACGFQESYIRLWSIKADKKSLPKSTSVEDSDGSVRLLSHSGPVYGTTFSPDNKYLLSCSEDASARLWSVDTKTALVAYKGHTGPVWDVAFGPFGHYFATASHDQTAQLWSCDHIYPLRVFAGHLSDVDCVTFHPNSAYVLTGSSDKTCRLWDVHRGHSVRVFNGHTQPVTAVAIAPDGHTMASADSEGLIHLWDIGTGRRIKTMRGHRGNIYSLSFSRESTVLVSGGSDCTVRAWDVFKTNYNNPVSSSLTGSVVTPFSAKTSTFNEVNWSTSPDQMVALYTKQTPIFNVSFTRRNLCLAISVS O13286 SRW1_SCHPO PTM: Phosphorylated by cdc2-cdc13-CDK complex. This targets srw1 for proteolysis which in turn promotes cdc13 turnover. Dephosphorylated during G1 arrest. {ECO:0000269|PubMed:10921878, ECO:0000269|PubMed:18257517}. MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:10921878"; MOD_RES 98; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:10921878"; MOD_RES 177; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:10921878"; MOD_RES 187; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 214; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:10921878" SPAC144.13c; CHAIN 1..556; /note="WD repeat-containing protein srw1"; /id="PRO_0000051228" MDEFDGFTRPTSSNSSANRNSNNSMNRVENNNSNSDSANTVDSRGDAHTRMRQGFEKSFPSSPNKKRPRTNEGDRFIPSRDASTELWTGFTKVEGPLTPVKKKQSVADRNFTTLLRSELFGSNDETFNNSPIATPNTTIGVSTPRTDSGIDDIELTQRTPPSSSHTSSSILQNTPVTPSRKIFHYLSPRDRNKSSYGKKAQYQDNPNRTIYSLSPVRSITKDLISASRLEGRELPSIPYRVLDAPGLAGDFYLNLLDWGQCNMLAVALASRVYLWSGISSEVTVMHNFYPTDTVTSLRWVQRGTHLAVGTHNGSVEIWDAATCKKTRTMSGHTERVGALSWNDHVLSSGGRDNHILHRDVRAPEHYFRVLTAHRQEVCGLEWNSNENLLASGGNDNALMVWDKFEEKPLYSFHNHIAAVKAITWSPHQRGILASGGGTADRTIKLWNTQRGSMLHNIDTGSQVCNLLWSKQTNEFISTHGFMENEVALWNYPSVSRVGTLKGHTDRVLYLAMSPNGENIVTGAADETLRFWKLFDSKSKHSASTMSSPFDPTMKIR O13290 DYHC_SCHPO BINDING 1890..1897; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 2169..2176; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 2174..2181; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 2520..2527; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC1093.06c; CHAIN 1..4196; /note="Dynein heavy chain, cytoplasmic"; /id="PRO_0000114642" MDKNDNSQCQLSTVSDEILIFLKKLLSLSVSDNLDDICETIALQSTFVDTFRSFINDEYYTVIYLYGSPCLTSSPTSPDSCTFGNMTFQWTSLLQDVFSGTSAFAIFKRFPLTDTPLTLQNMLYINQLPILKGGHKSNEIPERPINAIFLYTKYVMSCYFTAYLAMESVDDRSTIDLNSPSKGKELELTCQKFADFERSFTFFCREYQNSDTILQHHPLILSTIKHAEENNLDLSVRLLPSKVLSDSEFYKSLSNLVNVWLKTTRSLIKLFHDQISKTALEEFNFWQFYYRSLSRLNDQLHSRPVLFVLDILAFGKRFHTIASFNSETNIQCFVDKVGKIDALFKEISLDIFLSSSTLESLQLSAALLYSTFSKKWRNTGYPETRVLDFINFITEDLLKLISRLLPALGALSLSNVDFSHRTAVSSDILSLCYIRLKDFLRISGSLKEEQSYYGLKNSIKQIKAFENKLKYIQSFHEKHQQLIGALSEVYGLTHLTELEILEHLNKKEHVFNILTVFKDLQSLNVLDISLKGVNAWNSLETSYYNCMTVLEDEVIAQLKSLLQYSKTSSQMFTTLMRFQPLFFRTRVRTSISDCLHLLVNRIKQELDLLKTRFTEDVSDTELIAMNELRNLPMASSAIIWATQLKNRLHEYTKNINIIFGEDWNNFPDGFELKVECITLQKRLDTNLIFTNWINDVSSRNLNFDFDSKIFYLTQSESAESPLRLSVSIDFDPCSFCKEIRTLAHLGYNIPSQLMELASCLQRIQLIAMCLIDSVQSFNDVSFEISKTEEERFLLQEYELAVRQHIVTGLFISWNDFIVGNLSTPPKCAIGKRNFLKNIHPNVENYAYQFSSLTSLLMNKRNAISHTYMQIQEQLFQLDICEYSGDIFLTIQRKLQDLIDLLYVNGYSNLPPFVRALNLRFQDLLISRCRKFLSFFKTTILTSGNENNDLKSKFSSDMYEKLRGFLKPTNLTIQRNIIEFDPPVYRKKEDSIYLLDMCLQSVVNIPLLSIKTTAQRNCTLIGFFPVINRLESEILGIFESLLFHFDSILGYQNYWKKVEPFLNLNSLNLLLKSELFQLDQCYSLSLYLIHLKSEVDEIGKVTDFKIFSVNNTEFKSQVYLYLREWINALFDRFTFLLGKESEHLLNELDDTHSSLSTVDFTVNNTESLINSLKIFKKAGCYKLNVEHKIITYQNYEMTFNDCDAFSEFNFSLLKDITSKWKDLLESFECRRLKLENNKDEILRNFSEFAKRVNTETLSLISEWCASSLSLIKANYDEFSSTVDDFLFRFSKATEQCLMVKYIKKDLEIEIEESCDFSIQTEEIHLYKKFKDVISSNLEFIVEIKNTRWKLFDTATLSVQTTHQINALESVHTSFQHFKLFTNTKQSLNQLKDCTLLLQKLKSCPLKPVHWISLFEITKSTEQLDFEKLLVSDILGIDLQAHESFITTLLNSAVVEANLENQFNEVHSFWKNSYFSFKSFKGRNYIVVGCQELIDAVEKNMDSLNLIKTSRHFKDGDMNITDLQSKMKIIVKFLNIWKEIQQIWTHLSAIFYESTYIQQLLPELAASFFNSSKTYMHLVTLLKERSYLYKVSNIPSLLESAAKLSTTLEDSKKSLLKYFELQRHKISRLYFLGDDDLMELISNPCDPFVINKQIIKLYPGIRSLIVDTENTNINGCTTNEGNELLFDNPICLLDNTQPLHWISSLEPFLKATLFQLFSTSFQQIRDFYYNKSRNVFCKEWFLRYPSQITLLSLRCTLCHEIETGIADCCLDAVFNFINDGISSLVLLADENELSIKKKVTLMFNELLHFKETVGLLCKNSFNNYFWSREVKAFYREDHDDEAVVIKMFSLEFIYAFEYSELDDPIVYTDLTRNCFSVLLHSIASNLGGSPIGPAGTGKTETVKAVSAYLGKNVFVFNCDNAFNYKTIQRILSGLAQIGTYICFDEFNRLDSGTLSAISYDIQRIQSLVSHSDGLCQSPILLDAPTIFVTMNPGYLGRFKLPSNLKKLFRPIWMGSPDNKKICEILFLSFGFKESSLLSQVLDSFFLCCSGSLSNCLHYDFGLRAMKVVIKAAKRIKGFLKKKNTICQELEILWYAIREVLYPSLIYQDIPLFFKAEESYFNFPAVKANAFIDPDNFEVNIEQTLSKNFFGNNQYLKLKIMQLYQMSEAYNGIILLGKTGSGKSQIFRILQSALLNIGIDCIVYVISPKALTKESLFGSMNMDTREWTDGVFTKLLRKTRDSCYYKRYMFVFDDELSPEWVEAMNSLLDDNKTLTLSNGERIALQPYVKIFFEADSVASLTRATISRCGLICISNIDDNILSSTDKMLSFTSGATNYPLGSSNDEFSTVFSKVLTDEVMMNLISSCYKFSVDLQHIMNFTKQRFFTTFYSLLDQTKLFTRSSNITESLSFKELCNYLKKKICYILAWCCTGDTDAKSRERFTHWLMQNASVDLPEIKDFEHVSILDFDVSLETQSWYPIAGKTLKSSALKYAGNTVIPTLDTVRYAEFLNFSLTKNRCVIFCGPPGSGKSMLMLGTLRSRQDVEVIALNFSISTSSKSVVSFLEQSTVYYRSTGMTIMCPKNHEKVLVLFCDEINLPRSRNCLAEDVICFLRHMLEHQGFWHPLHKEWVTIKNIFVCGACNPSTDIGRNDFPERFLRRTVLIFVDYPESYSLVTIYNALLEKSALINQYKTIILNIVKASVKFYQVLRENFKSSTQGYVYTPRDLTRWLISFKNYAESYAETNNLSLIKVWYHEACRVLLDRLVSQKECSWGMTELQKVIVTDFGEFEVSVIFEKQIIFTDILKNGLEFLDFASLRPKLESLYKKFYSSHPNNTLVFVDETITHILRFHRILNNSGMHALLQGSVGLGQKAVVEFVCWLNSFSLFELQKNQTYSIEDFEDNLKSILILAGTTNCKACLAINESIAGVPGFLDLLNNLLTNSEVSNFFDQNDWAEIKKNLNKLNEFQPLKFDSEESVTEIFMNNVFQNLCVVFYVYTSADVDFQTNSLSPALLNRCTIDYYHSWDYHSMLQIANEVLQETISLNALDHDNPNLKNIKGSSIYDAVAQAVVNTHTSIVWEFKHLGKTSYFSCLHFIRFLNTFCLIFGRDANKLSKEKSRIENGFKKIKETSQGIDKFKEALSDQQNVLFSKTKTANDRLQCIIQTKQAVEAKKVYSLQAEASLQKKSFLLNEKKNSVMKEVSYAKPAVIEARKSVSDIKKAHLIELRSLSRPPMAIRITMEVVCKLLGFSATDWKNVQQLLKRDDFIPKILNYNLEKELSINLRRKIEQDYFSNPIFTFDSVNRASKACGPLLLWIKSICNYSKVLEKLEPLNSEVDRLKLEQKNAEECIQETIAACKDLDEKLLQLQEEYASMISEIHSMELQMDEVKCKMQRSIEVITDLSIERNEWSGFLNLYPKRMWNLVGESLMEASFVVYAGNLDPSMRIFLRNKCEPIISSFGFPISKSAVRTNIERCVQTSIESKYYKNLTDYSLENIYIIQENKSPLLIIDPSSQILDILPSLYKGKASDLISFSNKSFQNQIKLALLSGSAIIIKDAELWDVSIEPLLKPEFFTGSGEVQTTFAKDTITITLPLNIIFFSEVQSNELENKASKFMNVVNFTLSISLLETQMLKSVISVQEPGVFKQKDNCFTLKLSIERQIRSLQEQLLKTLCSSNENIVGTDEIVVLLKNLKEKHETIRLAYSESQSINRKVDELIRRYKLSIKSFLSVVVVFQHFISLKKSYSFSFNFIWSTFHQMLNVVLENRNQDFKSLIMDALRDLIRRCFLYIFPEDRVLFLFLLMFFFFPKETESLRKLLIVNGKTLELEQSYLNFFETCSDSNERGGLESLFFKTHASNIQNFCTEVLANTHCEEDCLKLLYDLWSSAFKVEFSNIKYDFLKIINDESESRMPTIVYLMENCEIDSLLQNAKIPQNIKKLTVSLGSAENESLADSYLKLASTEPLWLFINNIHLSTPWAEKLPSKMSNHLHKNSRIVCLSEIHNQLPHQLLCISRSIVFNKQTSFKNNLLNLLELLPTMTHTLPHNRFRLFFFLSWLHATLAEIYCFTCSSWKEPCYFDDSDFYFGTKILCNILYRNVHLEEFSWGTFKDLLLNVVYGPKVSASSDFIALDKILKRLIAQFKTQISSNILLTDNFKFILPYEITFSSAKEVIGQLPDEIPPGWLDIPENSKRKRTDIYFSMCI O13298 PHD1_SCHPO ACT_SITE 158; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:9781677}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000269|PubMed:9781677}; SPAC3G9.07c; CHAIN 1..434; /note="Histone deacetylase phd1"; /id="PRO_0000114725" MDTPETSTPYEQVEKGSFFSFRPQKKRVTYHLDEQVGNYHYGDKHPMKPHRITITNHLVMGYGLHNKMSVFSPRMATFGEMSEFHREDYLDFLKRVTPDNAEQFADKFQQFNIGDDCPVFDGTYEFSQRSAGASLDASRKLVQGQTDIAINWSGGLHHAKRGEASGFCYVNDIVLAILNMLRFFPRVLYIDIDIHHGDGVQQAFYESDRVLTVSFHKYNGDFFPATGNFDENGVKGGKYFALNVPLEDGIGDEQYTSLFKSIIEPTINTFQPSAIVLQCGADSLGYDRLGVFNLSIHAHGECVRFTRSFNIPMLVVGGGGYTLRNVARAWCYETSICVNEQIPSELPRETLYYEFFAPDYTLHPRLTTKIENKNTPKALEDLRIRALEQLRYLGGAPSVQMQQIPPDLTGHLEEEDERLNDEYLDKAVDVRVRG O13310 ORB6_SCHPO ACT_SITE 216; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 99..107; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 122; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC821.12; CHAIN 1..469; /note="Serine/threonine-protein kinase orb6"; /id="PRO_0000086455" MDKNDYLHFERNPSLFPKSTLDKVQKTKKYIEHYYKVAVDHAVERNQRRINLEQRLATERGSEERKNRQLRASGEKESQFLRFRRTRLSLEDFSTIKVIGKGAFGEVRLVQKLDTGKIYAMKSLLKTEMFKRDQLAHVKAERDLLVESDSPWVVSLYYAFQDSLYLYLIMEFLPGGDLMTMLINYDTFSEDVTRFYMAECVLAIADVHRMGYIHRDIKPDNILIDRDGHIKLSDFGLSTGFYKQDQSASYMKPRTGNTVKRGQMVDAIWLTMSSKDKMATWKKNRRVMAYSTVGTPDYIAPEIFLQQGYGQDCDWWSLGAIMFECLIGWPPFCSENSHETYRKIINWRETLTFPNDIHLSIEARDLMDRLMTDSEHRLGRGGAIEIMQHPFFTGIDWDHIRETAAPFIPNLKSITDTHYFPVDELEQVPEQPVTQQPASVDPQTLEQTNLAFLGYTYKKFNYLTMKGAL O13326 CYSD_SCHPO CATALYTIC ACTIVITY: Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:57844; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-homocysteine; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:58199; EC=2.5.1.49; Evidence={ECO:0000250|UniProtKB:P06106}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6526818}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.5 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:6526818}; KM=11.1 mM for O-succinyl-L-homoserine {ECO:0000269|PubMed:6526818}; KM=10.4 mM for L-homoserine {ECO:0000269|PubMed:6526818}; KM=0.053 mM for H(2)S {ECO:0000269|PubMed:6526818}; Vmax=15.5 umol/min/mg enzyme for O-acetyl-L-homoserine {ECO:0000269|PubMed:6526818}; Vmax=6.2 umol/min/mg enzyme for O-succinyl-L-homoserinee {ECO:0000269|PubMed:6526818}; Vmax=2.5 umol/min/mg enzyme for L-homoserine {ECO:0000269|PubMed:6526818}; MOD_RES 210; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P06721" SPBC428.11; CHAIN 1..429; /note="Homocysteine synthase"; /id="PRO_0000114778" MPVESEHFETLQLHAGQEPDAATSSRAVPIYATTSYVFRDCDHGGRLFGLQEPGYIYSRMMNPTADVFEKRIAALEHGAAAIATSSGTSALFMALTTLAKAGDNIVSTSYLYGGTYNLFKVTLPRLGITTKFVNGDDPNDLAAQIDENTKAVYVESIGNPMYNVPDFERIAEVAHAAGVPLMVDNTFGGGGYLVRPIDHGADIVTHSATKWIGGHGTTIGGVIVDSGKFDWKKNSKRFPEFNEPHPGYHGMVFTETFGNLAYAFACRTQTLRDVGGNANPFGVFLLLQGLETLSLRMERHVQNAFALAKYLEKHPKVNWVSYPGLESHVSHKLAKKYLKNGYGAVLSFGAKGGPDQSRKVVNALKLASQLANVGDAKTLVIAPAYTTHLQLTDEEQISAGVTKDLIRVAVGIEHIDDIIADFAQALEVA O13339 TERT_SCHPO BINDING 590; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; BINDING 742; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"; BINDING 743; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00405" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:24793650}; SPBC29A3.14c; CHAIN 1..988; /note="Telomerase reverse transcriptase"; /id="PRO_0000054931" MTEHHTPKSRILRFLENQYVYLCTLNDYVQLVLRGSPASSYSNICERLRSDVQTSFSIFLHSTVVGFDSKPDEGVQFSSPKCSQSELIANVVKQMFDESFERRRNLLMKGFSMNHEDFRAMHVNGVQNDLVSTFPNYLISILESKNWQLLLEIIGSDAMHYLLSKGSIFEALPNDNYLQISGIPLFKNNVFEETVSKKRKRTIETSITQNKSARKEVSWNSISISRFSIFYRSSYKKFKQDLYFNLHSICDRNTVHMWLQWIFPRQFGLINAFQVKQLHKVIPLVSQSTVVPKRLLKVYPLIEQTAKRLHRISLSKVYNHYCPYIDTHDDEKILSYSLKPNQVFAFLRSILVRVFPKLIWGNQRIFEIILKDLETFLKLSRYESFSLHYLMSNIKISEIEWLVLGKRSNAKMCLSDFEKRKQIFAEFIYWLYNSFIIPILQSFFYITESSDLRNRTVYFRKDIWKLLCRPFITSMKMEAFEKINENNVRMDTQKTTLPPAVIRLLPKKNTFRLITNLRKRFLIKMGSNKKMLVSTNQTLRPVASILKHLINEESSGIPFNLEVYMKLLTFKKDLLKHRMFGRKKYFVRIDIKSCYDRIKQDLMFRIVKKKLKDPEFVIRKYATIHATSDRATKNFVSEAFSYFDMVPFEKVVQLLSMKTSDTLFVDFVDYWTKSSSEIFKMLKEHLSGHIVKIGNSQYLQKVGIPQGSILSSFLCHFYMEDLIDEYLSFTKKKGSVLLRVVDDFLFITVNKKDAKKFLNLSLRGFEKHNFSTSLEKTVINFENSNGIINNTFFNESKKRMPFFGFSVNMRSLDTLLACPKIDEALFNSTSVELTKHMGKSFFYKILRSSLASFAQVFIDITHNSKFNSCCNIYRLGYSMCMRAQAYLKRMKDIFIPQRMFITDLLNVIGRKIWKKLAEILGYTSRRFLSSAEVKWLFCLGMRDGLKPSFKYHPCFEQLIYQFQSLTDLIKPLRPVLRQVLFLHRRIAD O13351 PMT3_SCHPO SPBC365.06; PROPEP 112..117; /evidence="ECO:0000255"; /id="PRO_0000035962" CHAIN 1..111; /note="Ubiquitin-like protein pmt3/smt3"; /id="PRO_0000035961" MSESPSANISDADKSAITPTTGDTSQQDVKPSTEHINLKVVGQDNNEVFFKIKKTTEFSKLMKIYCARQGKSMNSLRFLVDGERIRPDQTPAELDMEDGDQIEAVLEQLGGCTHLCL O13370 DED1_SCHPO BINDING 213..220; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 54; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 55; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 59; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 63; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 128; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 312; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1795.11; CHAIN 1..636; /note="ATP-dependent RNA helicase ded1"; /id="PRO_0000055042" MSDNVQQQVDSVGSVTEKLQKTNISRPRKYIPPFARDKPSAGAAPAVGDDESVSSRGSSRSQTPSEFSSNYGGRREYNRGGHYGGGEGRQNNYRGGREGGYSNGGGYRNNRGFGQWRDGQHVIGARNTLLERQLFGAVADGTKVSTGINFEKYDDIPVEVSGGDIEPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVPVDQDAGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVVHVEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELLQEANQECPSFLIAMARESSFGGNGRGGRYSGRGGRGGNAYGARDFRRPTNSSSGYSSGPSYSGYGGFESRTPHHGNTYNSGSAQSWW O13601 RSP1_SCHPO SPBC11B10.05c; CHAIN 1..494; /note="DnaJ-related protein rsp1"; /id="PRO_0000071131" MARTAFHDEFVDYYTILGAESTSSYVEIRQQYLKLVLRYHPDRNPGREAEVLPQFQLIQKAHEVLKDPKLRELFDQRRLLEAGRPDGVLRFRPKKSGPKNDISTKVASKVSVTMATKFAEKKKKQDRENVDSKDNNITNFSLHRSFSASGKMEKNNSFKEVSTSKSYISSGYLHPKTSPIFKKNGYATENVVDPISSSPRFKGPNYNKFNAKLYLESLREKRRTYTPLSEISNGLNSNGVENSSITKSSPRSSSSSNNERFKDTSEESIIFTSPNTPEHPSVYQTDITPEIKLEHSDNNSPSKPEIPFRHPTSKPLPPKPLSRSKSSSLSRNQTRSQLNDLSAENDSTSNSTEYDDQLQSILRSLAIEGDDDEVAKVLPKPPSVPTIQAPIPPEAPRNLTNASVDSYLNSFEMYQRRWSSYSIIYTQYAFQWQIFKNKCFQLDLMNTPGQSRLIDNWKEGSQAIQLFYAYEQMHLRALEELQSLKESLFASFGI O13648 ANM3_SCHPO BINDING 230; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 239; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 263; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 285; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 314; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" SPBC8D2.10c; CHAIN 1..543; /note="Ribosomal protein arginine N-methyltransferase rmt3"; /id="PRO_0000351450" MLVKPMACYFEIWTRKVTTIEDFSLAIANRFKQMGSHSDSEVDWDNEEEVWEDEVHEFCCLFCDSTFTCLKDLWSHCKEAHNFDFYQVKQQNNLDFYACIKLVNYIRSQVKEGKTPDLDKLSDILRSDEYMISVLPDDSVLFSLGDELDSDFEDDNTLEIEVENPADVSKDAEIKKLKLQNQLLISQLEEIRKDKMNELTSQTTDQLSVTPKKADNDSYYFESYAGNDIHFLMLNDSVRTEGYRDFVYHNKHIFAGKTVLDVGCGTGILSMFCAKAGAKKVYAVDNSDIIQMAISNAFENGLADQITFIRGKIEDISLPVGKVDIIISEWMGYALTFESMIDSVLVARDRFLAPSGIMAPSETRLVLTATTNTELLEEPIDFWSDVYGFKMNGMKDASYKGVSVQVVPQTYVNAKPVVFARFNMHTCKVQDVSFTSPFSLIIDNEGPLCAFTLWFDTYFTTKRTQPIPEAIDEACGFTTGPQGTPTHWKQCVLLLRNRPFLQKGTRVEGTISFSKNKKNNRDLDISVHWNVNGKADSQSYVLN O13666 ERG3B_SCHPO CATALYTIC ACTIVITY: Reaction=episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46560, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23929, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52972; EC=1.14.19.20; Evidence={ECO:0000250|UniProtKB:P32353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561; Evidence={ECO:0000250|UniProtKB:P32353}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045}; SPBC27B12.03c; CHAIN 1..329; /note="Delta(7)-sterol 5(6)-desaturase erg32"; /id="PRO_0000117026" MDVVLQYADKYVFDTFYGKIAESFDSSSSFANTAVNSTTLGLAEKVNFAITSGLLDRNNVWRQFTSLFLITWIMGTLSYFLSASFAYYVYFDREEARRHPKFLKNQEHLELMVALKNLPGMAILTAPWFLAEIRGYGYVYDKLDEYGYFYLFFSIALFLLFSDFLIYWIHRALHHRWLYAPLHKLHHKWIVPTPYSSHAFHYLDGYSQSLPYHMFPFFFPLNKYVYLLLFGSVNYWTVLIHDGKYFSNNAVVNGAAHHAAHHMYFNYNYGQFFTLFDRLCSSYRQPDQELFDAELRNEKLQEQRIRFMETVQYTVEGKDDRTYASKKDN O13684 PCS1_SCHPO SPAC11E3.03; CHAIN 1..261; /note="Monopolin complex subunit pcs1"; /id="PRO_0000058266" MRKNNMQTSKDSELKEQAKGKSSKLIHKLPKQRTRISQGQMHSTQDFVNNEDQDAYSVRENENELHINNSGMSELNKKLQLPNVELSTLSHTQEQEFNELNKLIRKINELQEFYLLEDLAKPVTNAGADADDTIVKDLKKELENEKKANHSLKNELLKTREQIKNYSKINILIKELFGLEVADCIEDEDGYRFNCKNTGRRGTLEYQLLLDDQNFTFTPRLNVQTDEELMKHLPDYLLEEIIFTKEQGKLFSARLMKALQD O13685 UBC13_SCHPO ACT_SITE 86; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPAC11E3.04c; CHAIN 1..148; /note="Ubiquitin-conjugating enzyme E2 13"; /id="PRO_0000082564" MALPKRIIKEIETLTRDPPPGIVAAPTEDNLRYFKITMEGPQQSAYEGGKFHLELFLPDEYPMMPPNVRFLTKIYHPNVDKLGRICLSTLKKDWSPALQIRTVLLSIQALMGAPNPDDPLDNDVAKIWKENEPQAIANAREWTKKYAV O13688 NSE6_SCHPO SPAC11E3.08c; CHAIN 1..522; /note="Non-structural maintenance of chromosome element 6"; /id="PRO_0000079254" MNASNNISKFPDLDNSSKLIDHILDSDDSEELDELPDISSLVPSARAQSRKQYLKNDSSNSSTYRWNIDLLSSTATIDDSVAKRRKLAVQNLLQYDSTQTFQTGDEIDELIGKSVGSNVLNVLRSNPIYDDDLRYEYCSNSKARVPDWNTLKAECLKDNDLEFNEGIIPTTFGDLLSAKLVPLDIALSICSLQFFRSLGDTTCSEWIANLEKIFYSYKSSSNNLNQIVRFIFETTADMIGIDLAKRQVPIQLERTSASENLKSNLKIKVINFLKCCGTLYRFSDDTVRFEMIQDACRILIDNQVGSFCKWQFSQFMELPISLNPDFLISNIHKVSESPRVWVTILSSLSRSCQKFRKKIAFTLFVGKQSKNDDSDFSSLCQRLDEISASCNNDYTTLLYQIRTFGYAVDEKHFKTNERLECLLEKLRKIDLTISGSTDHLLLSRCEVKDCIHRLFMVLYYLNTNSAPELERIIESDLPNNNKQKDRYFKDKTSNLSMKENKSFSAKKVKKGKKKNKRQAYKR O13692 GAS5_SCHPO ACT_SITE 159; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 261; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 88; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 158; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 159; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 200; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 205; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 300; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135" SIGNAL 1..22; /evidence="ECO:0000255" PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. SPAC11E3.13c; PROPEP 486..510; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000377427" CHAIN 23..485; /note="1,3-beta-glucanosyltransferase gas5"; /id="PRO_0000010492" CARBOHYD 147; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 216; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 252; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 318; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 337; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 397; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 491; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 70..99; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 214..353; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 232..264; /evidence="ECO:0000250|UniProtKB:Q06135" LIPID 485; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVTISKNYETLKEKYASAANYTGDGDYSSSPATLTCPADDSYFTSFPLPTMPSEAKGFIESGAGQPLGFNAPSNQEFSANATALVSPGPHSVSTTINTNIVQATISQSSTSGSSSGSSSASTTASSSSVSSGSSISSGSSSMSTSYTSASGSSAHSSGSSSGSSSATSSASTFNLSRFYVFAGILAISGLVFA O13710 SMC5_SCHPO BINDING 51..58; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC14C4.02c; STRAND 466..469; /evidence="ECO:0007829|PDB:5MG8"; STRAND 487..492; /evidence="ECO:0007829|PDB:5MG8"; STRAND 512..515; /evidence="ECO:0007829|PDB:5MG8"; STRAND 569..573; /evidence="ECO:0007829|PDB:5MG8"; STRAND 593..595; /evidence="ECO:0007829|PDB:5MG8"; STRAND 597..600; /evidence="ECO:0007829|PDB:5MG8"; STRAND 603..609; /evidence="ECO:0007829|PDB:5MG8"; STRAND 617..623; /evidence="ECO:0007829|PDB:5MG8" HELIX 411..432; /evidence="ECO:0007829|PDB:5MG8"; HELIX 437..448; /evidence="ECO:0007829|PDB:5MG8"; HELIX 450..452; /evidence="ECO:0007829|PDB:5MG8"; HELIX 461..464; /evidence="ECO:0007829|PDB:5MG8"; HELIX 470..472; /evidence="ECO:0007829|PDB:5MG8"; HELIX 473..485; /evidence="ECO:0007829|PDB:5MG8"; HELIX 493..506; /evidence="ECO:0007829|PDB:5MG8"; HELIX 524..526; /evidence="ECO:0007829|PDB:5MG8"; HELIX 533..538; /evidence="ECO:0007829|PDB:5MG8"; HELIX 545..548; /evidence="ECO:0007829|PDB:5MG8"; HELIX 553..562; /evidence="ECO:0007829|PDB:5MG8"; HELIX 565..567; /evidence="ECO:0007829|PDB:5MG8"; HELIX 577..584; /evidence="ECO:0007829|PDB:5MG8"; HELIX 637..688; /evidence="ECO:0007829|PDB:5MG8" CHAIN 1..1076; /note="Structural maintenance of chromosomes protein 5"; /id="PRO_0000119019" MDGLRPSKRRKSNPLYSDYALGSIVRIKLVNFVTYDYCELFPGPYLNLIIGPNGTGKSTIVSAICIGLGWPPKLLGRAKEAREFIKYGKNTATIEIEMKYRDDETVTITRQISQDKSSSFSINREACATSSITSLMDTFNVQLNNLCHFLPQDRVAEFAQLDPYSRLMETERAIDHEGLLPAHEKLIDLRKREREILQNKNQGQSTLNSLKDRQQALEKEVNIFKEREKIKSYIEMLGLAKMLVIYREKTNVFNQLRADKKKLKKDLKDLVEEFQPILDKGEELRSDLKLKDDTFNDYSSASMELNTSNLRARASFSNFMENEKKLYEKVNTNRTLLRNANLTLNEAQQSVKSLTERQGPRPSDNGVQDLQEKMQEVNAEKLQHENEKLESSHELGSIRTLKAQKLIDLDNIKRELSYYNDATKRKLDFMSSAPGWEDAYQTYQLLKEYESAFEAPAYGPIYMNLKCKEKGFAALIEGFFRTDTFRTFIMSNYNDYLKLMDLITSKTKYTPTIREFSSERKKKIEDFEPPCSREKLQSFGFDGYVIDFLEGPEVVLVALCHMLKIHQIPIAKRELPPASVNALNNFRLANGDPVLKTYLAGSSIHLVFRSAYGDREITRRTDPLPSRSIYFSENVEMDLVKRKEEQLNAQLSQLENLQNEERKLQEKVNEHESLLSRTNDILSTLRKERDEKLIPIHEWQQLQERIEHQTLLLRQREKVPEQFAAEIEKNEDIRKENFEALMNSVLKVKENSIKATNNFEKMLGSRLNVIEAKYKLEKHEMDANQVNARLTEVQDRLKDITDKLASAREDAMSLYGSVVDSLQTQSSDRQTAITELNEEFATSSEVDNKISIEETKLKFMNVNSYVMEQYDARKKEIEELESKMSDFDQSVEELQDEMNSIKEDWVSKLEENVQCISDRFSKGMSGMGYAGEVRLGKSDDYDKWYIDILVQFREEEGLQKLTGQRQSGGERSVSTIMYLLSLQGLAIAPFRIVDEINQGMDPRNERVVHRHIVNSVCDNAVSQYFLVTPKLLPDLTYHRNLKVLCICNGAWLPATFRTSLSTYFEKLKKSALISSS O13712 MUG61_SCHPO BINDING 605..612; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC14C4.05c; CHAIN 1..844; /note="Meiotically up-regulated gene 61 protein"; /id="PRO_0000116682" MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGVTNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPFETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNTTSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLVGLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKFDSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWHQEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFGLKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVYLKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAAITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSIQLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL O13716 AGN1_SCHPO CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59; SIGNAL 1..20; /evidence="ECO:0000305" PTM: Not glycosylated. SPAC14C4.09; CHAIN 21..424; /note="Glucan endo-1,3-alpha-glucosidase agn1"; /id="PRO_0000012111" MKLVLFLVLLFSALINLTNADKMVVAHFIVGNTYPYTVSNWEEDIQDAIAVGIDGFALNMGSDAWQVERIEDAYDAAASVSSDFKLFISFDMSIISADADFIEGVVRRFADKPNQLYYDGKVFVSTFAGETDTFGYSDVSTGWDSAVKEPLASAGYPIYFVPSWTSLGQGALEESVADGFLSWNAWPTTDADMNDNDDIGYQNLANSLGKLYVAPVSPWFYTHLSYKNWAYKSDWLIIDRWNEMLSVQPDMIEVLTWNDYGESHYIGNIQGALPAGSEGYVDGFDHTAWRYLMSPYISAYKLGLSEPYINFESLFYWYRPTPKSATATADSLSYPSGGDYMEDEIFVLVYLLQSAEVTVTCGSTTQTFSGVPGVNQFTIPMETNASPSFTVARQGGTLASGTGPEIVDSLSIYNFNAYTGVLYF O13734 SGO2_SCHPO MOD_RES 7; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 240; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 292; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 335; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC15A10.15; CHAIN 1..647; /note="Shugoshin-2"; /id="PRO_0000055452" MSKASLSPNVEDLKKKQIRQYKEIIRISKAQSIRIKELQLENERLLSENIDLRTTAINLEEQLETVQNENEENKTKLAALLNRFHEETDNFLSKLSLCQQEIQDTFKPVEANLAYDVDTDSEDLDEESVVKDTEEIIEQAQHDVSLRNLSGIEDENIIDDGETAINEQKKREANVFSDTQSAPQLKSGKALPADFENPYNLSNSKPVNNNNEDRVEAVTSENKSIDSAPQEKNHEYEIVSPKSLSNKINNQAAAQRRTEEDNANGVAQEENEGSQEAHFHSRIQSDTVIQSTPTKRKWDVDIQNKQINLASAATNVTGYVSETDSRPNRANSLDSAVLLVQSSNKSNRNGHHISDPNLNSSISLKFAPEDTAHNSLTSQENVGPQVTTTSLSNMTVAESPRTDTPREINGLVDSSVTNGNEKFSVEIMNDSNKIGLNPKSFTDEEREILTLFRNPPMRLSSEPPSSNGFSIAHPNNSPLRPPSLQGILNAEDRPYEIEPSRSSFATNDTGSYNNLELLSSVTNLKSPNENDRVTKTQSRRETKVKRRRKARIQETSEESTVVNEPNEKPDGRSRRERKKVNYALPGLRTKLRRNFDLPSDHVKAKKTRRAPKNSENDSATKTETANITSEAPTTSEVTLENSETLNL O13736 SLA1_SCHPO MOD_RES 309; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 311; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 312; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 454; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 573; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 577; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 927; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 929; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16E8.01; CHAIN 1..1420; /note="Actin cytoskeleton-regulatory complex protein sla1"; /id="PRO_0000303944" MANLPIIGIYKVLYSYEPQEINPGEEIPENEREISIVEDEIVCLLEKGEDDWYLVKRNVNSNDDDEEIGIVPSNYITEAEPSTKMKALYDYTQQSVDEISFQADQTLDCYGDTDSDWILVGFNNNFGLAPRNYVEGMDASSAPASQEPSASGVNAPTVSAPNSMVSPPPSFQPPSAAAPATSLPSDYNPPPPPPPPPAVEDQAADANEPDDYYSSGRAVSPEIPPTYTPKQADPLPAPPPPPPPTLPPQSTNTSQLPMPSRNVNNLGSQVNIPPPPATPSQPPRPPTNASTRSTGTSSSMAHSYDSPPSPSSPSDAYGDPNQHLKLRTDSHDDSRAYDSSSSMGNPAYEKWEVREVVGKKKKRTGILAINNKSIVLTFTKTMDAAQVWPVTDLVNYSSERKHVFIEFNSDSGITSLHLHASSNTNADNIIRALGDVAGSARAAGLREIAAASGSPMPKLPSDSALHRLNAASDAAGVNGGRTGDYEMSTVYGDRSARAEDHKPKDSSAGQKMGTVLYDFIAEAADELTVKANMRVVIVNDTASSDWWKCSVDGKEGVVPSNFIKPDTEGDAKSPPSSSKSGQGSSLSRRASKHESKHKRDSKHEARPESKHESHRESKSAEKDKKDKKDKKEDSKRSRSHSVSKPDSSKLRTWTDRTGAFKVEAEFLGYSDDKIHLHKTNGVKISVPSAKMSYKDLDYVELMTGKKVYSRTERKKDTQKQSHDHGHSHSKSHDREKEKEKKKDREHRKHRETEEEDEGPPPQPARPESTRPALAPPSSSHSNDKYDVIQERPKISYDWFDFFLRCGVDFTVCNRYTHNFNNEHLDEACIPSLNPDTLRTLGLKEGDIIRVMNHVNELNGVSTKPASAITPETKSTVNQIMSGGEALAAPVAVPAPIPAPVAEPAPPAAPAKEVVEKAPSPPATRPKSTTPQKFDDDAWANKPVTEPPVRASSVTVEPARVTESMNKMNISEEAKKPEAPSRPRTAPIPEPEEQKKAPVEKKDAEKSVQAPIPAQPTGNITIQNAYFTAPQPMAADPFQSPLYVQPTGFQPPPSALPIQPTGYMQPIPVQATGYQPLMVQPTGLQPHMTGVMPQVTGVMPQMTGVVPQMTGVMPQMTGVQVQKTGAMPQQPVNYGYQVAGMQPQATGIISQPTGIRAQATGIMTQPTGLHTQATGMMQPTGMQPQATGIMPQATGMMQPTGMQPQVTGIMPQSMPMQPQMTGVQVQKTGMVAQPMLSQYTGYQQNYTPTAMPAADGYGMQPSMNDTQAYYNMNAQTPVNYGFAGGQDTSFGYEQQQMYSPMQQQQQQYYGTEMQPDMGYQQPMMSNYYDPMQMQQQTPYGYNQTGMEGYSEYGYAQPAGNMANPMSYDPVSNASLYMPSDYNQQTQPANYYDSSFGGAQGANEAGKKASIYQATPDNPFGF O13759 CSX1_SCHPO MOD_RES 42; /note="Phosphoserine; by MAPK sty1"; /evidence="ECO:0000269|PubMed:14633985, ECO:0000269|PubMed:18257517"; MOD_RES 54; /note="Phosphoserine; by MAPK sty1"; /evidence="ECO:0000269|PubMed:14633985, ECO:0000269|PubMed:18257517"; MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 291; /note="Phosphoserine; by MAPK sty1"; /evidence="ECO:0000269|PubMed:14633985"; MOD_RES 455; /note="Phosphoserine; by MAPK sty1"; /evidence="ECO:0000269|PubMed:14633985" SPAC17A2.09c; CHAIN 1..632; /note="RNA-binding post-transcriptional regulator csx1"; /id="PRO_0000081536" MSIDCLYRRSSLFDTSFVPLHSSIPATSKMSASNSDVNAPISPVVDEGKSELVSPTLERLVAPFNCSPSSTPLQDVAGVGSKMSDTLWMGDLEPWMDATFIQQLWASLNEPVNVKVMRSKASSSETLISYCFVQFSSSAAAERALMKYNNTMIPGAHCTFKLNWATGGGIQHNNFVSRDPEFSIFVGDLLPTTEDSDLFMTFRSIYPSCTSAKIIVDPVTGLSRKYGFVRFSSEKEQQHALMHMQGYLCQGRPLRISVASPKSRASIAADSALGIVPTSTSNRQPNQDLCSMDPLNTTVFVGGLASNLSEKDLQVCFQPFGRILNIKIPFGKGCGFVQYSEKSAAEKAINTMQGALVGTSHIRLAWGHNTLPVSALSQSQSQVSDEGFDRTLSANQIFGMNQSVIGANSGSSNSSGSSLKSAPVSPRTAAAQSLLPNSVVSSINGMNSVNFSTISPPPLSRSASISPTLSGSGSGLTPLSSHFPSAATGLVGGQVYPQSSVLQSSKINGSAKVQPSVKLPEWLQPFSGNNHNSFATQDLLTRVSSLKLVDDEQPASLNGSAFQARASRPWNLGRERQSSLIDLRHELEQNENGLEKSGFGLNLRGRLPPRSYSTFNCTGQYLQPSLRLSRDS O13766 MDE10_SCHPO ACT_SITE 230; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 229; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 233; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 239; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000305" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SIGNAL 1..15; /evidence="ECO:0000255" PTM: Glycosylated. {ECO:0000269|PubMed:14871934}. SPAC17A5.04c; CHAIN 16..512; /note="Zinc metalloprotease mde10"; /id="PRO_0000029210" CARBOHYD 35; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 432; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 246..254; /evidence="ECO:0000250"; DISULFID 374..394; /evidence="ECO:0000250" MRLVLLFSCVLAVSSYAEIILAHSDENLLSRTKNNLSKWNENRLYDYGSKSTMSLPVSSLFPALQTLWIGVVADCSYVTHFTSRMEAKKHIFQEFEGVSTLYEDSFNINVQIHSLILPSAHDCSANVVDRPEISMSPRISIEEKLEIFSKWKYESPGNNVFEAISPHERESFPSEPQVSVLFTSSVKRSPHGVSWFATICSETHIENEWHVGPLSVVSAYPNDRLVVAHEIGHILGLIHDCNKKSCGDHSEACCPLSSSLCDAQELYIMNPSNSYTYANLRFSDCSILQLHSLVEKKYVSLSCLSKPSEKSVLRLGTCGNGIVEDGEECDCGEDCENNPCCDGKTCKLTKGSLCDDQQDACCYQCHFKNAGTLCRQSTNPCDKPEFCTGISSKCPVDENWDDGRICQDSLGMGSCASGVCTSASRQCKKLTNFSSLSCHSDSCKVSCQNEDGTCFISAKDYIDGTRCRGGLCYNGVCVPIEGSSASWSKQPSLFCASGTMLISLAVIAWFFW O13768 ERCC3_SCHPO BINDING 348..355; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:15937491}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:15937491}; SPAC17A5.06; CHAIN 1..804; /note="General transcription and DNA repair factor IIH helicase/translocase subunit XPB"; /id="PRO_0000101993" MSLKRKNNAREGTPDEDLEEYSDYSDVDNYGEEDDDSYKPAPRIRINNNKTKAQTTTNSNEARQSGISAMFGQNDFSNLLGLKLDHTARPLWINPIDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIAVLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDNVEDKKDITNDSSKETAEKSSSDELFSAVVGLQEEEDDEDAVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRNDNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNPKKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYASKAERLELLQEVLLQNEEAADLDDGEDTSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSANKQLKKDSKEHHALFRKHLYTKRR O13788 SSR1_SCHPO BINDING 236; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 239; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 260; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 263; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" SPAC17G6.10; CHAIN 1..527; /note="SWI/SNF and RSC complexes subunit ssr1"; /id="PRO_0000349432" MSNVTENKHDLHENGVPDSAQPMELDVSKKEDTEPEVRDEAKEFLLSQLPQVEVPEWAQWFDFSKVHEIEKKQNPEFFDGKNTSKTPEVYKEYRDFMISTFRLNSKVYLTFTACRRNLAGDVCAVLRVHRFLEQWGLINYNVNPDTRPSKIGPPSTSHFQILADTPRGLVPLLPPPSSSIPRSKAVTIEDPSIVRTNIYDPSLDDVLKGKGSTPNQKPSLSNLHENNIDQSDSPQHCYCCGNKFNESYYQSQTAQKYNVCISCYQQNRFPSPTTIADYKEVAIQNKIEDDDTWTAQELVLLSEGVEMYSDDWAKVASHVNTKSVEECILKFLNLPSSDKALFKMDKVHTNPVVDSLQGKNPILSVVSFLAKMVPPSSFTQKSSAKEEESDKVKGESVYPKPESESYDVEMNGKSLEDSDSLSELYLTNEEKKMASIIKDSVNVQIKLIESKLSHFDYLDQHIRLKSQELDAFAQATYREKLYMKRECQNARKKIEQQLQSKDTAANGLPVQSSAETSVIPASSMSPS O13790 CUL1_SCHPO PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}. SPAC17G6.12; CHAIN 1..767; /note="Cullin-1"; /id="PRO_0000119808" MTTLNTNDKDLPIVKKYDSLNGTWDFLKTGVSQIFERLDEGMTITKYMELYTAIHNYCADASKTITVDNFNDQTANVLGEALYNNLVLYLEEYLARLRKECISQTNHEEQLAAYAKYWTRFTTSARFINHLFGYLNRYWVKLKNRFTETLVYDIYTLCLVSWHHHVFSHIRDSLLQNLLYMFTKKRLYEPTDMKYVEVCVDSITSLSFDKTDMTKPNLSSYKTFFETNFIENTKNFYAKESSEYLASHSITDYLKKAEIRLAEEEELVRLYLHESTLKPLLEATEDVLIAQHEEVLHNDFARMLDQNCSEDIIRMYRLMSRTPNGLQPLRQTFEEFVKRSGFAAVAKIVPQVGGEADVDPKEYMEMLLSTYKASKELVNTAFHGDTDFTKSLDTAFRELVNRNVVCQRSSSRSPELLAKYADSILRKSNKNVDIDDVEDCLSSIIIIFRYVEDKDVFQNFYTKLLAKRLVNGTSNSQDAESSMLSKLKEVCGFEYTSKLQRMFQDISLSQEITEAFWQLPQSRAGNIDFSALVLGTSFWPLSPNNVNFHLPEELVPLYEGFQNYYYSCHNGRKLSWLFHLSKGEIKARINPQTNVTYVFQVSTYQMGVLLLYNHRDSYTYEELAKITGLSTDFLTGILNIFLKAKVLLLGDNDKLGDPNSTYKINENFRMKKIRVQLNLPIRSEQKQESLETHKTIEEDRKLLLQSAIVRIMKARRTLKHVVLVKETIDQIKSRFTPKVSDIKQCIDMLIEKEYLERQGRDEYIYLA O13795 POF8_SCHPO SPAC17G6.17; STRAND 294..299; /evidence="ECO:0007829|PDB:6TZN"; STRAND 322..324; /evidence="ECO:0007829|PDB:6TZN"; STRAND 328..332; /evidence="ECO:0007829|PDB:6TZN"; STRAND 338..346; /evidence="ECO:0007829|PDB:6TZN"; STRAND 384..387; /evidence="ECO:0007829|PDB:6TZN" HELIX 306..320; /evidence="ECO:0007829|PDB:6TZN"; HELIX 347..359; /evidence="ECO:0007829|PDB:6TZN"; HELIX 390..400; /evidence="ECO:0007829|PDB:6TZN" CHAIN 1..402; /note="La-related protein 7 homolog"; /id="PRO_0000119975" MFVPRQLNVRKIKAFTGKENNSIADGNNNKLKDEHYKHNEASKEPSHSISGGLMLNQQDRQLIEPLNPDFLSAVDSILEIYFHRERQKEKVHLAFLIQQDDFWKGIRPNPTQNNLKYALSYVTNALFHFDNSSHMVIRNENIVLPLDIPLYDRIIYVEPVPATLSNKSLLLAGKLRKYLKEFLPYVDAIGTPEGYAFVILYKKVDQSALSKLPVPPGWVLLTRKEWTNREEKYFENQLHLVKASSSDVSNSSNSFPENRYPKLTKVEKQMTKSVSKTSQTDKDEDNLDFTKNLLTRIKNLHPLTNKSTIHSLLSYVFSRQTQNIACEPMYIDYRKDETEAIIRWKTPLHAETCINAFRTQERKQNSHDDIRAHRKKGSSRPFLIAELITGEEEKNYWRMLKK O13799 YE02_SCHPO BINDING 147..154; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" MOD_RES 41; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17H9.02; CHAIN 1..1030; /note="Uncharacterized helicase C17H9.02"; /id="PRO_0000102099" MSENSTDSKNFQFSEGSRESSNDELKVLLRDTETKEDEKSSFSNSEEESIIENLSDSSVNKEYAKNSLKLSDAVSESKYLNPLLKDKRHDRSFALHKVVVPDDYDYIPLNKHIPSDPPAKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFGDVGLMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNALQFARWISEIHKQPCHVVYTDYRPTPLQHFIYPQGADGIYMLVDEKNKFKTENFKKVLEVLDHSTRQENYSKSSKKVKKSSSLERIINMVLSNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELVTEIFDSAINQLSEEDRGLRQFEEMRSLLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDTKGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLMRIEEISPEDILKKSFYQFQNMESLPLIKEELMQLKNEETSINIPNETAVKEFHDLKLQLEKYGEEIQKVMTHPDNCLPYLQSGRLIQIKLGGIIFPWGVLVNVIKREFDPNTREQVAPHETYVLDVLLPISSNSMSNHKVNPSILVPPRPNETPLYEIVSVLLTAVCNISSIRIYMPRELNSNESKLRAYRRVNEVIEEFKEIPYLDPLEHMHIESSTLSLSLRKLEILEPKLFDSPYYKDSKHRAEYHEFRKKLNLRAQIKDISTKITNTEAIIQLRELKIRQRVLRRLGFCTLENVIDIKGRVACEITSGDELLLVELIFQGFFNQMPPEEIAAALSCFVYEDKSEVSTLNLKEPFKKMYLTIIEAAKRIATVSLESKLQFNESDYLHQFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVRTFRRLDELLKQLEHAAIVLGNNELKEKSVLTEQKLHRDIIFSASLYL O13801 DRI1_SCHPO MOD_RES 184; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 437; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17H9.04c; CHAIN 1..604; /note="RNA-binding protein involved in heterochromatin assembly dri1"; /id="PRO_0000314102" MSKLPSPTMPLPESVGDLVVLHFETNLDDHGISIGRAPCEIHEICWVILDGKTLEKQHCESCSIREDSSRHGICGSASSLTEAIFTLDNSIQERLNFQGKPFTFVVMNGRELRVLLPKEARDQGITLPSYMRHPRLFDLSSEYAKWQIRMGAVPPYTITLSHIFGKLDVDSLPPITESKAIELSPSDAPYITKGLTQCWRLANATTLLLRKAEKDSRGHSLPSVLTQPINCQADARSFYAERSKIVHVAGLTNDVTQLELESWFTNHGVHPVALWTLKTPEPYKSTGTGFVLFASHEDAADALAFNGYCLGDRMLEIIPSSTKVLDKASDILIPFPSSKNRPRPGDWNCPMCGFSNFQRRTSCFRCSFPGPTHVSAATGSNTFSPDFPYGNSYGNGSSHFIANYGGSVHHSNENTMQSDLQHQNGNNAVNHHHSSRSFGGNVPFRAGDWKCGSEGCGYHNFAKNVCCLRCGASRATAAVVADHASGPVNGSYSHNSYSHIPPVMSTSPPNHSVYPYSQLSINSVTANHGQNFGGQNGGNVSRFDDHGRFKEVSRPSVTTDQGDWLCECGFTNFRRRSNCLRCNAPHYSNMQIPASLPSDFNAYV O13807 DDB1_SCHPO SPAC17H9.10c; CHAIN 1..1072; /note="DNA damage-binding protein 1"; /id="PRO_0000079843" MTYVTYLHKPSSIRNAVFCKFVNASSWNVIVAKVNCLEVYSYENNRLCLITSANIFAKIVNVKAFKPVSSPTDHIIVATDSFRYFTLFWDANDNTVSNGIKIQDCSERSLRESQSGPLLLVDPFQRVICLHVYQGLLTIIPIFKSKKRFMTSHNNPSLHDNFSVRIQELNVVDIAMLYNSSRPSLAVLYKDSKSIVHLSTYKINVREQEIDEDDVVCHDIEEGKLIPSENGGVFVFGEMYVYYISKDIQVSKLLLTYPITAFSPSISNDPETGLDSSIYIVADESGMLYKFKALFTDETVSMELEKLGESSIASCLIALPDNHLFVGSHFNNSVLLQLPSITKNNHKLEILQNFVNIAPISDFIIDDDQTGSSIITCSGAYKDGTLRIIRNSINIENVALIEMEGIKDFFSVSFRANYDNYIFLSLICETRAIIVSPEGVFSANHDLSCEESTIFVSTIYGNSQILQITTKEIRLFDGKKLHSWISPMSITCGSSFADNVCVAVAGGLILFFEGITEVGRYQCDTEVSSLCFTEENVVYVGLWSADIIMLTYCQDGISLTHSLKLTDIPRSIVYSQKYGDDGGTLYVSTNNGYVLMFNFQNGQVIEHSLRRNQLGVAPIILKHFDSKEKNAIFALGEKPQLMYYESDKLVITPLSCTEMLNISSYVNPSLGVNMLYCTNSYISLAKMSEIRSLNVQTVSVKGFPRRICSNSLFYFVLCMQLEESIGTQEQRLLSFLRVYEKNTLSEIAHHKFNEYEMVESIILMNDDKRVVVGTGFNFPDQDAPDSGRLMVFEMTSDNNIEMQAEHKVQGSVNTLVLYKHLIVAGINASVCIFEYEHGTMHVRNSIRTPTYTIDISVNQDEIIAADLMKSITVLQFIDDQLIEVARDYHPLWATSVEILSERKYFVTEADGNAVILLRDNVSPQLSDRKKLRWYKKFYLGELINKTRHCTFIEPQDKSLVTPQLLCATVDGSLMIVGDAGMSNTPLLLQLQDNIRKVIPSFGGLSHKEWKEYRGENETSPSDLIDGSLIESILGLREPILNEIVNGGHEGTKLDISVQDLKSIIENLEKLHP O13816 SCC3_SCHPO SPAC17H9.20; CHAIN 1..962; /note="Cohesin subunit psc3"; /id="PRO_0000120192" MSESVTTGSDDDGGDRESSPVMLSQSFDPMSSSSNSSSEENSDDDYEKTISSKKRHPRPNSKGVNVKRSRRNAIVEEDPQEEIFNNLFAFLLDQKVDTMDIAVSWFADYAKDNQSALANLINFILKCCGCNRAINVFDVQDQDSASATLSQIQLSVERTSTRDYPLNSKNLKFRNFRKRLTGLLSNFVSQLSIRNYLYNSTVFEDIMSWVVAMSSSTMRPIRHTATVFCLNIMTFLCEKSKELLNEHAIATKQLEKEEKRSRVNRNRINELNNSLGEIVKQQDTLTTYLNDYFDSVFVHRYRDVEPKIRVDCLQELGVWINTVPSIFFSGSYLRYLGWMLSDINTTVRLTVVKVLRKFFETDSFIGGLRHFSSRFKERILEMSCVDADIGVRVASIRLCNAMRTCGFLENSEILKVLKLILDINPRVQREAVLFLCKVVDESVNEKIDLWGEEDYILKAFSQTSLTTFSVHWIKFSQMCKLLEEVRLSYQSSFDYDTLLRIFQKNGNFITPITQALLNACEIDSIYQSWEDISNFVLFDNYTSTLKDPIDSILSFCKLNDFQESILLQLLSASIQTVCNNNFITPKTVHNKQAAETTNDQNKDKDLLYLNLLPYINSITERNSASPTLLHDSLRLLFSMDLTEMTDPQLSRHFELLINNLKKFFLTNNDLQIIQGCTILFLRLDSIPALKEDLKLLVTDICDQTVTEFLKNFGSFNIQDAVITKDEFVIFEACLTRIEGCTSLKDFSDYPEFDIIYERLVSLLSRVPNSYEDTLKFSAINTLQSLLFWFFLRKDNPADEEKKKDDETKVFNCLINIMNNDSSKILQLQAARTFLETVIMKEGVKASHYNDDNRVSEEHNFLKPQFLDALLKILEGWLYTYAKVGQFPFKRLTQASSPHTQISLDKNPLNRRLLEHVCCDLTSKLLIVVSLSNTITPEFSQQFCELRGHYGPKLSAIVDEFLN O13820 ERG5_SCHPO BINDING 461; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+); Xref=Rhea:RHEA:33467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18249, ChEBI:CHEBI:52972, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.19.41; Evidence={ECO:0000305|PubMed:18310029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33468; Evidence={ECO:0000305|PubMed:18310029}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; SPAC19A8.04; CHAIN 1..543; /note="C-22 sterol desaturase ERG5"; /id="PRO_0000334491" MEMNQTETLIPAARNVIRVLGYEIEYSKWTICFALLAVCIAYDQISYQMQKGHIPGPRFKIPFMGSFLDSMKPTFEKYNAKWQTGPLSCVSVFHKFVVIASERDLARKILNSPSYVQPCVVDAGKKILKHTNWVFLDGRDHIEYRKGLNGLFTTRALASYLPAQEAVYNKYFKEFLAHSKDDYAQYMIPFRDINVATSCRTFCGYYISDDAIKHIADEYWKITAAMELVNFPIVLPFTKVWYGIQSRKVVMRYFMKAAAESRKNMEAGNAPACMMEEWIHEMIETRKYKSENKEGAEKPSVLIREFSDEEISLTFLSFLFASQDATSSAMTWLFQLLADHPDVLQKVREEQLRIRKGDIDVPLSLDLMEKMTYTRAVVKECLRLRPPVLMVPYRVKKAFPITPDYTVPKDAMVIPTLYGALHDSKVYPEPETFNPDRWAPNGLAEQSPKNWMVFGNGPHVCLGQRYAVNHLIACIGKASIMLDWKHKRTPDSDTQMIFATTFPQDMCYLKFSPFDASTVDWKNSKEAFSNEAVSAATVETESA O13821 VPS27_SCHPO BINDING 176; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 179; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 192; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 195; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 200; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 203; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 222; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 225; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" SPAC19A8.05c; CHAIN 1..610; /note="Vacuolar protein sorting-associated protein 27"; /id="PRO_0000292523" MSRWWNSNSQFASDIEKATSETLPAGSEEISLYLEISDQIRSKSVDPKFAMRILKSRIDHSNPNVQIMALKLTDTCVKNGGSGFLLEIASREFMDNLVSILRSPAGIDEDVKMVILRYIQSWALAVPDTNSPLSYIIHVYQNLKDGDYEFPEPSQNITSKFLDTETPPDWTDSEVCLRCRTPFTFTNRKHHCRNCGGVFCNQCSSKTLSLPHLGINQPVRVCDSCYSLRTKPKGSKSRARNERKFHAKTRKTPSKPVTNNEDEDIKRAIELSLKEMPQSREPPSYERPSEANVVISQDQHLTEDEDEELKRAIAISLEEAQKSSQKDDNVTAPNNMNISYPSVPAHTVSTDIRSSPFSGRPSDNPSTLISTADADNITLYATLVQKLKKLPPGSIFTEYQLQELHENMGVMRTRMMRSLGETMSKYNGLIQALQKLQTCMRLNDALIEQRLSSTYAHHYIDSSMDSNRSIEPEPDVISTVRNSSTIPQASSSSVPKIVVDSSPVTENPPSHSDVMGQKDTISSYYSTDTDVSANVMGNRHDEVVFSDTASGEKNTKLNIDESTNYYNTDSIDKVGEPFDEISSGYDDLMNGNDKQGNDIPEVQEASLIEL O13826 RFP1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; SPAC19A8.10; CHAIN 1..254; /note="E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1"; /id="PRO_0000056333" MQFNGSNGIDESSVIDLTRSPSPPVETSISSTNIIDLDAIPDDSFPSSPVLSPRRRRMNRRRNERSRNFPSNHLSYLEDMIYLGPQVSTRRSSSRRDLMGMIARTFPEFSSVNSLSPSLFQLIVNRMRFDAIHPEWTNGSDDEYFSNHFEESYDDFTSSLENIKQSYKPPGPPKSGFTRSFNNDTLMVCPRCQEPLGTSKSKEKSALWATKCGHVYCGSCAKVLKTSKRSQSKCLVNDCGRYLNTKNAMWELFY O13828 DCP2_SCHPO BINDING 167; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; BINDING 220; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616" COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; SPAC19A8.12; STRAND 54..56; /evidence="ECO:0007829|PDB:2A6T"; STRAND 98..104; /evidence="ECO:0007829|PDB:5J3T"; STRAND 110..115; /evidence="ECO:0007829|PDB:5J3T"; STRAND 117..120; /evidence="ECO:0007829|PDB:5J3T"; STRAND 126..129; /evidence="ECO:0007829|PDB:5J3T"; STRAND 132..134; /evidence="ECO:0007829|PDB:5J3T"; STRAND 161..166; /evidence="ECO:0007829|PDB:5J3T"; STRAND 169..176; /evidence="ECO:0007829|PDB:5J3T"; STRAND 189..192; /evidence="ECO:0007829|PDB:5N2V"; STRAND 195..200; /evidence="ECO:0007829|PDB:5J3T"; STRAND 208..210; /evidence="ECO:0007829|PDB:5KQ1"; STRAND 245..247; /evidence="ECO:0007829|PDB:2QKM"; STRAND 272..274; /evidence="ECO:0007829|PDB:4A54" HELIX 8..19; /evidence="ECO:0007829|PDB:5J3T"; HELIX 25..28; /evidence="ECO:0007829|PDB:5J3T"; HELIX 31..47; /evidence="ECO:0007829|PDB:5J3T"; HELIX 49..52; /evidence="ECO:0007829|PDB:5J3T"; HELIX 61..69; /evidence="ECO:0007829|PDB:5J3T"; HELIX 73..75; /evidence="ECO:0007829|PDB:5J3T"; HELIX 76..81; /evidence="ECO:0007829|PDB:5J3T"; HELIX 83..90; /evidence="ECO:0007829|PDB:5J3T"; HELIX 136..148; /evidence="ECO:0007829|PDB:5J3T"; HELIX 201..203; /evidence="ECO:0007829|PDB:5J3T"; HELIX 223..240; /evidence="ECO:0007829|PDB:5J3T"; HELIX 255..265; /evidence="ECO:0007829|PDB:2QKM" TURN 2..5; /evidence="ECO:0007829|PDB:5KQ4"; TURN 20..22; /evidence="ECO:0007829|PDB:5J3T"; TURN 153..155; /evidence="ECO:0007829|PDB:5J3T"; TURN 205..207; /evidence="ECO:0007829|PDB:5KQ4"; TURN 218..222; /evidence="ECO:0007829|PDB:5J3T" CHAIN 1..741; /note="mRNA decapping complex subunit 2"; /id="PRO_0000373871" MSFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRAQNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGAIMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFDCSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNLMDLPTFKKNKPQTMKNKFYMVIPFLAPLKKWIKKRNIANNTTKEKNISVDVDADASSQLLSLLKSSTAPSDLATPQPSTFPQPPVESHSSFDIKQKILHLLNEGNEPKSPIQLPPVSNLPLNPPIQSSNSRLSHDNNSFDPFAYLGLDPKNPSASFPRVVSQNNMLTNKPVLNNHFQQSMYSNLLKDQNSVQHLFAASDMPSPMELPSPSTVYHQVFYPPTSTSVSSYGLGKTPQPAYGSSSPYVNGHQTQQISSLPPFQSQTQFLARNSDNSGQSYNSEGDSNSKRLLSMLSQQDTTPSSSTLSKEANVQLANLFLTPNSLETKKFSDNSQGEEISDNLHGESCNNPNANSVHSAQLLQALLHPSATETKEETPKKTSDSLSLLTLLKSGLPTPANDLQNKSQNNERKASSQVKELEVKNYSKSTDLLKKTLRIPRNDEPLEAANQFDLLKVSPQQKSEVPPKRNELSQSKLKNRKKKENSETNKNHVDMSPGFVKILKRSPLADQKKEDTQESDFKGSDDHFLSYLQSVVSSNSNGLH O13833 CID1_SCHPO BINDING 90; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT"; BINDING 101; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4FHY"; BINDING 103; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4FHY"; BINDING 168; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHW"; BINDING 171; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU"; BINDING 172; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU"; BINDING 193; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT"; BINDING 197; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4NKT"; BINDING 211; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT"; BINDING 212; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU"; BINDING 336; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU"; BINDING 340; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4FHX" CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:19430462, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0000269|PubMed:25712096}; CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:12218190, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:22885303}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17353264}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for UTP {ECO:0000269|PubMed:22885303}; KM=312 uM for ATP {ECO:0000269|PubMed:22885303}; Note=Mutation of His-336 to Asn decreases the Km for ATP to 65 uM and increases the Km for UTP to 45 uM. {ECO:0000269|PubMed:22885303}; SPAC19D5.03; STRAND 84..89; /evidence="ECO:0007829|PDB:4UD4"; STRAND 97..99; /evidence="ECO:0007829|PDB:4FH3"; STRAND 102..107; /evidence="ECO:0007829|PDB:4UD4"; STRAND 131..137; /evidence="ECO:0007829|PDB:4UD4"; STRAND 140..147; /evidence="ECO:0007829|PDB:4UD4"; STRAND 159..164; /evidence="ECO:0007829|PDB:4UD4"; STRAND 226..228; /evidence="ECO:0007829|PDB:4UD4"; STRAND 288..290; /evidence="ECO:0007829|PDB:4EP7"; STRAND 292..294; /evidence="ECO:0007829|PDB:4UD4"; STRAND 310..313; /evidence="ECO:0007829|PDB:4UD5"; STRAND 319..322; /evidence="ECO:0007829|PDB:4UD5"; STRAND 325..329; /evidence="ECO:0007829|PDB:4EP7"; STRAND 331..333; /evidence="ECO:0007829|PDB:4UD4"; STRAND 364..367; /evidence="ECO:0007829|PDB:4UD4" HELIX 42..55; /evidence="ECO:0007829|PDB:4UD4"; HELIX 59..79; /evidence="ECO:0007829|PDB:4UD4"; HELIX 90..93; /evidence="ECO:0007829|PDB:4UD4"; HELIX 115..127; /evidence="ECO:0007829|PDB:4UD4"; HELIX 166..181; /evidence="ECO:0007829|PDB:4UD4"; HELIX 185..198; /evidence="ECO:0007829|PDB:4UD4"; HELIX 204..206; /evidence="ECO:0007829|PDB:4UD4"; HELIX 211..224; /evidence="ECO:0007829|PDB:4UD4"; HELIX 256..258; /evidence="ECO:0007829|PDB:4UD4"; HELIX 268..281; /evidence="ECO:0007829|PDB:4UD4"; HELIX 301..304; /evidence="ECO:0007829|PDB:4UD4"; HELIX 338..341; /evidence="ECO:0007829|PDB:4UD4"; HELIX 344..361; /evidence="ECO:0007829|PDB:4UD4"; HELIX 370..374; /evidence="ECO:0007829|PDB:4UD4" TURN 234..236; /evidence="ECO:0007829|PDB:4UD4"; TURN 285..287; /evidence="ECO:0007829|PDB:4UD4" CHAIN 1..405; /note="Terminal uridylyltransferase cid1"; /id="PRO_0000120312" MNISSAQFIPGVHTVEEIEAEIHKNLHISKSCSYQKVPNSHKEFTKFCYEVYNEIKISDKEFKEKRAALDTLRLCLKRISPDAELVAFGSLESGLALKNSDMDLCVLMDSRVQSDTIALQFYEELIAEGFEGKFLQRARIPIIKLTSDTKNGFGASFQCDIGFNNRLAIHNTLLLSSYTKLDARLKPMVLLVKHWAKRKQINSPYFGTLSSYGYVLMVLYYLIHVIKPPVFPNLLLSPLKQEKIVDGFDVGFDDKLEDIPPSQNYSSLGSLLHGFFRFYAYKFEPREKVVTFRRPDGYLTKQEKGWTSATEHTGSADQIIKDRYILAIEDPFEISHNVGRTVSSSGLYRIRGEFMAASRLLNSRSYPIPYDSLFEEAPIPPRRQKKTDEQSNKKLLNETDGDNSE O13836 DXO_SCHPO BINDING 33; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O70348"; BINDING 93..95; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O70348"; BINDING 150; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000269|PubMed:19194460"; BINDING 182; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O70348"; BINDING 199; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O70348"; BINDING 201; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000269|PubMed:19194460"; BINDING 239; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000269|PubMed:19194460"; BINDING 240; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000269|PubMed:19194460"; BINDING 241; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O70348"; BINDING 263; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O70348" CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000269|PubMed:28283058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881; Evidence={ECO:0000269|PubMed:28283058}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphosphoguanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282, ChEBI:CHEBI:172876, ChEBI:CHEBI:172877; Evidence={ECO:0000250|UniProtKB:P53063}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929; Evidence={ECO:0000250|UniProtKB:P53063}; CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H(+); Xref=Rhea:RHEA:78683, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:138282, ChEBI:CHEBI:167618; Evidence={ECO:0000269|PubMed:19194460}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78684; Evidence={ECO:0000269|PubMed:19194460}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:19194460}; Note=Divalent metal cation. {ECO:0000269|PubMed:19194460}; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19D5.06c; STRAND 2..6; /evidence="ECO:0007829|PDB:6WUI"; STRAND 22..29; /evidence="ECO:0007829|PDB:6WUI"; STRAND 35..39; /evidence="ECO:0007829|PDB:6WUI"; STRAND 43..45; /evidence="ECO:0007829|PDB:3FQG"; STRAND 88..93; /evidence="ECO:0007829|PDB:6WUI"; STRAND 111..117; /evidence="ECO:0007829|PDB:6WUI"; STRAND 124..127; /evidence="ECO:0007829|PDB:6WUI"; STRAND 154..156; /evidence="ECO:0007829|PDB:3FQG"; STRAND 180..189; /evidence="ECO:0007829|PDB:6WUI"; STRAND 192..200; /evidence="ECO:0007829|PDB:6WUI"; STRAND 202..205; /evidence="ECO:0007829|PDB:6WUI"; STRAND 237..243; /evidence="ECO:0007829|PDB:6WUI"; STRAND 271..277; /evidence="ECO:0007829|PDB:6WUI"; STRAND 281..290; /evidence="ECO:0007829|PDB:6WUI"; STRAND 335..340; /evidence="ECO:0007829|PDB:6WUI"; STRAND 345..350; /evidence="ECO:0007829|PDB:6WUI" HELIX 7..9; /evidence="ECO:0007829|PDB:6WUI"; HELIX 73..81; /evidence="ECO:0007829|PDB:6WUI"; HELIX 94..102; /evidence="ECO:0007829|PDB:6WUI"; HELIX 134..137; /evidence="ECO:0007829|PDB:3FQD"; HELIX 141..152; /evidence="ECO:0007829|PDB:6WUI"; HELIX 159..161; /evidence="ECO:0007829|PDB:3FQD"; HELIX 164..168; /evidence="ECO:0007829|PDB:3FQD"; HELIX 170..172; /evidence="ECO:0007829|PDB:3FQD"; HELIX 234..236; /evidence="ECO:0007829|PDB:6WUI"; HELIX 251..266; /evidence="ECO:0007829|PDB:6WUI"; HELIX 293..298; /evidence="ECO:0007829|PDB:6WUI"; HELIX 299..301; /evidence="ECO:0007829|PDB:6WUI"; HELIX 309..328; /evidence="ECO:0007829|PDB:6WUI" TURN 54..61; /evidence="ECO:0007829|PDB:6WUI"; TURN 103..105; /evidence="ECO:0007829|PDB:6WUI"; TURN 119..121; /evidence="ECO:0007829|PDB:6WUI" CHAIN 1..352; /note="Decapping nuclease din1"; /id="PRO_0000079900" MLREFSFYDVPPAHVPPVSEPLEIACYSLSRDRELLLDDSKLSYYYPPPLFSDLNTGFPNRFHPPKSDPDPISIVKDVLMTKGIQMNSSFLTWRGLITKIMCAPLDPRNHWETYLVMDPTSGIIMMEERTRSETSYANQDRMCYWGYKFEAISTLPEIWDACSRDQIEQRDNQDVVPDEQYCSIVKINIGKSKLILAGEVDCIWDKKPCSAKESDVHSDDGTIEEDASNAENPNLHYVELKTSKKYPLENYGMRKKLLKYWAQSFLLGIGRIIIGFRDDNGILIEMKELFTHQIPKMLRPYFKPNDWTPNRLLVVLEHALEWIKQTVKQHPPSTEFTLSYTGGSKLVLRQII O13837 GABAT_SCHPO BINDING 142..143; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P80147"; BINDING 199; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P80147"; BINDING 357; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P80147" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19; Evidence={ECO:0000269|PubMed:17355287}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P17649}; MOD_RES 333; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P80147" SPAC19D5.07; CHAIN 1..474; /note="4-aminobutyrate aminotransferase"; /id="PRO_0000120380" MSSTATVTESTHFFPNEPQGPSIKTETIPGPKGKAAAEEMSKYHDISAVKFPVDYEKSIGNYLVDLDGNVLLDVYSQIATIPIGYNNPTLLKAAKSDEVATILMNRPALGNYPPKEWARVAYEGAIKYAPKGQKYVYFQMSGSDANEIAYKLAMLHHFNNKPRPTGDYTAEENESCLNNAAPGSPEVAVLSFRHSFHGRLFGSLSTTRSKPVHKLGMPAFPWPQADFPALKYPLEEHVEENAKEEQRCIDQVEQILTNHHCPVVACIIEPIQSEGGDNHASPDFFHKLQATLKKHDVKFIVDEVQTGVGSTGTLWAHEQWNLPYPPDMVTFSKKFQAAGIFYHDLALRPHAYQHFNTWMGDPFRAVQSRYILQEIQDKDLLNNVKSVGDFLYAGLEELARKHPGKINNLRGKGKGTFIAWDCESPAARDKFCADMRINGVNIGGCGVAAIRLRPMLVFQKHHAQILLKKIDELI O13838 NUP40_SCHPO MOD_RES 88; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 92; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19E9.01c; CHAIN 1..371; /note="Nucleoporin nup40"; /id="PRO_0000204872" CARBOHYD 11; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 169; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 242; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 349; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSSSFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFTMSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGMLINDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQPRNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF O13839 FIN1_SCHPO ACT_SITE 151; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 10..18; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 33; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC19E9.02; CHAIN 1..722; /note="G2-specific protein kinase fin1"; /id="PRO_0000085952" MEKYKILECIGHGSFGRIYKVQRLKDGALLAQKEIHFGNITRQEKQYIADEVNILRNLKHPNIVQYCGEELNRSAQVINLYMEYCGHGDLANLIQRYKEEKKRFTEQEVLKFFTQLLLALYRCHYGENAPACDSQWPREIFHPKQSVLHRDIKPANIFLDENNSVKLGDFGLSKLLDNTRVFTQSYVGTPYYMSPEIIRSSPYSAKSDVWALGCVIFEICMLTHPFEGRSYLELQRNICQGNLSCWDHHYSDDVFLLIRHCLEVNSDLRPTTYQLLRSPILSDIRSKLESERVVLEQSDLLHKKHQMLIQLENDLQFREQRLSARESELENVIASRLAQREEILRRELEKQLRDMDARYQRHMQTVVNSMQKMRVTSPVDHNEQPESSTAEMFVDCTIEASQSPLLHIPKLGISKPLQTLSCPGFTLTTQQPILKRPTLRKELSSRALHTTATLMKYRANASSLRTTPIDKDGQITSLQQKNGTSNQVADCMNKLLHTSLDGKKLSPSELCNKFSDGEGLPNRKVSKLSVESDETAVSASSGESVPTDSTLTDTKSKSVFVHPPSPQSLYVEKLEKLNIRSDEVSKPSKASKTLHGYALPSLASPYDVHAEEKIARENEMDGNFKTMKINQHPDEYVLRTPKKIQLLEGQKRSPVKQLGRLGYNKLRRSAMDNAGLELRKAASTSNYTSLQSRTLPGSWRDDEEEIPRPFLRKMLDARMMRA O13842 CDA1_SCHPO SPAC19G12.03; CHAIN 1..320; /note="Putative polysaccharide deacetylase"; /id="PRO_0000172745" MYETRDLTGNAGKPVDTNPWPNNSKIAVSFVVNYEEGGERSLLYEDEGFETFLTEAGLMPFPNRPVRERSIESCFEYGSRCGFWRILNLFKKHKVPFTCWAIGQAVEKNPVVVGAMEEAGCEVGSHSHRWINYEGVPPETEYEHIKKSVQAIQKASPSNSAPRSWYTGRASLNTRKLVCQVYKDLGLPQPFDSDEYNDDYPYWVADPLASKPGAEDDKGLLIVPYTLEVNDMKYAVAPGFCNSDDFYTYARDAFDVLYEEGLEGAPKMMTIGLHCRLTGRPGRFRGLQKLMEHITSKEGVWVATREQIAQAWSAKHPYKA O13848 I3ACR_SCHPO ACT_SITE 54; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q76L36"; ACT_SITE 109; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q76L36" BINDING 49; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 143; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 165; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 196; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 201; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 239; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 240; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 241; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 242; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 243; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 246; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36" CATALYTIC ACTIVITY: Reaction=indole-3-ethanol + NAD(+) = H(+) + indole-3-acetaldehyde + NADH; Xref=Rhea:RHEA:14873, ChEBI:CHEBI:15378, ChEBI:CHEBI:17890, ChEBI:CHEBI:18086, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.190; Evidence={ECO:0000269|PubMed:16813561}; CATALYTIC ACTIVITY: Reaction=indole-3-ethanol + NADP(+) = H(+) + indole-3-acetaldehyde + NADPH; Xref=Rhea:RHEA:17037, ChEBI:CHEBI:15378, ChEBI:CHEBI:17890, ChEBI:CHEBI:18086, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.191; Evidence={ECO:0000269|PubMed:16813561}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34 uM for NADP {ECO:0000269|PubMed:16813561}; KM=53.3 uM for NAD {ECO:0000269|PubMed:16813561}; SPAC19G12.09; CHAIN 1..284; /note="NAD/NADP-dependent indole-3-acetaldehyde reductase"; /id="PRO_0000339120" MLIAAMGPKIPVPAYGVGTALFKKEKGEINRTIVDSVKNALAAGFIHIDCAEVYGNEEEVGVALKEANVPRSKLFITSKVMHNVDNIPEALNESLRKLGTDYLDLYLLHSPIPFYEKKIPISEGWKAMETALGTGLVHSVGVSNFRIPDLEELLKTSTITPRVNQIEFHPQVYKAAKPLVEFCQSKGIIVEGYGPLSPLVRDAQGPVAEFTKSLESKYHVSDTQILLKWAYSKGVIPITTTSKIERMKECLNFDSFTLDKADIDELGTLGVQHHKRTFMKHMDE O13849 CBPY_SCHPO ACT_SITE 715; /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"; ACT_SITE 921; /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"; ACT_SITE 978; /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" BINDING 924; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 979; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074}; SIGNAL 1..18; /evidence="ECO:0000255" SPAC19G12.10c; PROPEP 19..521; /evidence="ECO:0000255"; /id="PRO_0000004295" CHAIN 522..1002; /note="Carboxypeptidase Y"; /id="PRO_0000004296" CARBOHYD 659; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 627..880; /evidence="ECO:0000250"; DISULFID 776..789; /evidence="ECO:0000250"; DISULFID 799..822; /evidence="ECO:0000250"; DISULFID 806..815; /evidence="ECO:0000250"; DISULFID 844..851; /evidence="ECO:0000250" MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPFKHHELEEHEGPEHHRGPEDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHQGPKEKHNERPEQNMQSSHELLVIEAFADLINSVPVEEIAEEFSRFLDTLGIEYYGNIPVHIQENAPKDSSIPPLFEFDDDLELSDLTPEQFAYLEMLKAEGIDPMTAFRDQSHPAKPSNAQPADSSRPYAVFSQEENGEHVNLKAFPDHTLRVKDSKPESLGIDTVKQYTGYLDVEDDRHLFFWFFESRNDPENDPVVLWLNGGPGCSSLTGLFMELGPSSINIETLKPEYNPHSWNSNASVIFLDQPINTGFSNGDDSVLDTVTAGKDVYAFLNLFFAKFPQYAHLDFHIAGESYAGHYIPQFAKEIMEHNQGANFFVASGYEMEKQYINLKSVLIGNGLTDPLVQYYFYGKMACESPYGPIMSQEECDRITGAYDTCAKLITGCYQTGFTPVCIGASLYCNNAMIGPFTKTGLNIYDIREECRDQEHLCYPETGAIESYLNQEFVQEALGVEYDYKGCNTEVNIGFLFKGDWMRKTFRDDVTAILEAGLPVLIYAGDADYICNYMGNEAWTDALEWAGQREFYEAELKPWSPNGKEAGRGKSFKNFGYLRLYEAGHMVPFNQPEASLEMLNSWIDGSLFA O13853 ITS3_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; PTM: Phosphorylated by casein kinase I. Phosphorylation inactivates the enzyme. {ECO:0000269|PubMed:9873063}. SPAC19G12.14; CHAIN 1..742; /note="Phosphatidylinositol 4-phosphate 5-kinase its3"; /id="PRO_0000185484" MKIDSNGIVNPHSITNEIPSYDEKQAVDLNGNAFAPNGTFQKKDLISHKNDFERTMRHDVLHTNPKIEVRSETHIYEPNDSLFKENQDFPSNPTAHSPSSSSNDSVITATGVPDGILRDSPIVSALEPPSSNSSSSPQLQNLKHQLSSPQPSRAPIDRSSSNPVTSSQQPPNDRSTLSSSQKAKRPLKRSYSEKNSSNAEPSGSRSGDRGTNVSTSGSLLDGIPPDIGSASWAEAVKQKRVNMRRRREELDDECVLVGTRVSEGHENYVTAYNMLTGIRVGVSRCQAKMDRELTPADFTARHKFTFDITGNELTPSAKYDFKFKDYAPWVFRHLRQLFHLDAADYLVSLTSKYILSELDSPGKSGSFFYFSRDYRFIIKTIHHSEHKFLREILYDYYEHVKNNPNTLISQFYGLHRVKLPFGRKIHFVVMNNLFPPHRDIHQTFDLKGSTLGRELDENQPCQSPMCTMKDTNWIRRNMHLQFGPLKRQIFLTQVKADIDMLSSLGIMDYSLLVGIHDLSRGNRDKIRNSILSVYDPNVSQHRVPSINGNESHSNVHVIRQVVNSTGPVSLDQSCNLLPTDQFVERRNFMFYSDDGGFQATDENNEPGNFIFYIGIIDLLTKYSYVKRVEHLWKGINHSDSVISAVPPAEYASRFYKFVESSIKPTLLVLKPFPLKPQDGQRVNKQQSVNAGNVRTNNKHGSLNNNTAPSSRNAKSTSAHKSPKTEHRFPFPCRNVTTNTSSS O13877 RPAB5_SCHPO BINDING 7; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19458260, ECO:0007744|PDB:3H0G"; BINDING 10; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19458260, ECO:0007744|PDB:3H0G"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19458260, ECO:0007744|PDB:3H0G"; BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19458260, ECO:0007744|PDB:3H0G" SPAC1B3.12c; CHAIN 1..71; /note="DNA-directed RNA polymerases I, II, and III subunit RPABC5"; /id="PRO_0000121341" MIIPIRCFSCGKVIGDKWDTYLTLLQEDNTEGEALDKLGLQRYCCRRMILTHVDLIEKLLCYNPLSKQKNL O13881 CLR2_SCHPO SPAC1B3.17; STRAND 3..7; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 31..33; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 122..124; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 132..135; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 141..145; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 157..161; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 236..241; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 244..256; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 277..283; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 289..293; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 298..300; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 322..329; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 337..339; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 342..344; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 366..373; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 376..379; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 383..386; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 389..391; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 400..408; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 412..425; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 459..465; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 471..476; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 480..483; /evidence="ECO:0007829|PDB:5IKJ" HELIX 13..15; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 39..56; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 64..71; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 128..130; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 172..184; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 190..192; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 196..199; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 200..202; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 203..224; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 267..274; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 295..297; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 301..303; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 311..313; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 314..319; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 334..336; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 393..395; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 450..458; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 477..479; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 507..511; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 513..515; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 520..529; /evidence="ECO:0007829|PDB:5IKJ" TURN 345..347; /evidence="ECO:0007829|PDB:5IKJ"; TURN 530..532; /evidence="ECO:0007829|PDB:5IKJ" CHAIN 1..537; /note="Cryptic loci regulator 2"; /id="PRO_0000089869" MPAITCVWSDGRSDTWPNVNGHSRTRSVPSLKPLPHQDSKNLLYRQICGRLLAQHVFGGAGSTQPILNQLCKRLSTGNPNNTNASTVVTAPEKNVVSARHVRPNPKSSKDTLEKQPKYSSQIYLTDSFENYYLASLPTNYQLYQRDSNRENGNGKREFWLYGHPSGRPFRSVNDFLHHLYWLISDLTRNESTCCCVLCSGNMTRVRKNLQKENERMFHECKDDTYTWPSSYRLGEVVWIDINNELIPAIIVARNLINYESNQMDAVKLISDTFVEPYQYHCKQLGNSRYYFDMAAADIEPWSRHPLDLQKQEHLVAHSICQTWNLFGIFQPLEGIDMEEPKFHDENYSIPLTVLPTFGGESNSLDDHFYGIFRGAEKLWINDLCVISTSSLPSVLQKTSFMYISDIYVNEDDIVCFQGSLWTQIDKNALDYNDSADNIDEHKDDLKELPRRLQMVSKLSNTYFRCLHDKSVEYVCPFADVLGRWYEPWFVKGDLNYTSEVKERTSSRLSAVGSENWVDDDFYEYLLSEIDMVSAVVM O13889 E2AK1_SCHPO ACT_SITE 491; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 230..238; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 253; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. SPAC20G4.03c; CHAIN 1..704; /note="Eukaryotic translation initiation factor 2-alpha kinase 1"; /id="PRO_0000085949" MLGTSTKCSKRDCNYAKENISRIMPTIGLGYKQNFEKKTADTQSSCKLLLVALLESFCKHSDQTPEQSKQMFLYVAHSLQNSGIIDFEFSEELEPIRNAYADSLHNLLSKAFRSTLPMSSTKDSKKSRYSSPDGVLAKTASFLSVLSDGGYEDDVMNVKPSVNVLSNRLNHLPVEALESCFPQTTLESSTFADFCEHKDGTGNLSFSNFDSFPTVQRSRYASDFEELELLGKGGYGSVYKARNKFDGVEYALKKIPLRLRSFSTSSNIFRESRTLARLNHPNVIRFFSSWVELLPSSEKQIEEEPLASADETLSQSADIDNFMFDMDTGLLQHTYPSSVQILFQEDSVADDLTPCYSTKNSTCNLTDLFKKEADQDYAESHDCSSTTSQVDTLGKLAPTKSASEMLLMDSFLSEREEDECSNIPSFDQQPLCLYIQMALCEETLEKHINRRNKHIHGVMSKGLRNCYILLFARILEGVLYLHDAMHLVHRDLKPRNIFLSSGVHSEPCSVCLPNFSDEDNVEVSNAYEPVNQRTLCVVPKIGDFGLVLSQSDNLEEGTNSSAESSFVGTSTYAAPELFSKHMRSVMNNNSSTDIYALGILFFELLYPFNTRMERASAIANLKKGIFPHDFLDSMPEEASLIRSMLSSSNKRPTAAQLLTSNLFHDLVVNELHVYQALLEDAEKRNNNLKAELNILRVLNPNYDC O13892 EDC4L_SCHPO MOD_RES 671; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 673; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 674; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1075; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC20G4.08; HELIX 936..948; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 951..960; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 964..970; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 975..981; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 984..996; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 1002..1018; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 1024..1026; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 1030..1044; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 1045..1047; /evidence="ECO:0007829|PDB:4Q2S"; HELIX 1050..1069; /evidence="ECO:0007829|PDB:4Q2S" TURN 1027..1029; /evidence="ECO:0007829|PDB:4Q2S" CHAIN 1..1076; /note="Enhancer of mRNA-decapping protein 4-like protein pdc1"; /id="PRO_0000116694" MNEQDLLNSLRRDLNLPNLGKSHDGSEAVESTFPEKKESSLSAQQPHVDDQRSSLLSLLNAGLNASNQSPSNSGPKYYASHSSSTDALLQAFRDGAKPSGTASGADVKRSDSESTEATSNERPFNPVSAANLERLLMSSTGPQTPINGELKSNDSQDTAFQSSRNMPSDTSVASPDYSHSQSSSPIANYQESGNSEEPHKAEEQQQLSIYQLDNPGSGNYVWETVISPDKFETSTFAKCERNDIAIINRELDAQDNQLIHTNEDFIAYAVHREPIIRVIEISTGKSFLLHNNSPNKFVSVAWGNDSVIKNRLMAIDTTGQVLIFAVDIATSTSEIIFQLSGAQSLSDPIKSRFHWYPKSSTRFAVALSKHIIFFDLDLLNNISFPIPRSINAIQQLPCFLIDTGISAKEYDFSYDGTVFATVDKDALIKIYTVPTTFPSTPDKRPVPSEVSPIAIFTTRMERGPSKNYEKPINLRFISTPGTNNSRYLVIVYVMNQLITLFDLYSKRNIQTFRFNNRPTAATTTSFSQFSVDNERSTLLVGNPPSNSIYFFLFAKDETVSEQAPIYNSTYELILASLNTSEPVPADAKFSVIVAKKFEKAACISFTACKILESEDKYCIVVSNTDGYEYYSIPTSILDKTGKTVRSLESVQNYDADIGGTIDLTERHSTASPSTVNSGFSTPRSQATGFSKKKKDKGERFETKDKSSSVLSPSSYSASTFDAIPMDSIVSNILASLEKSVHKNYESLRSQLLEYKAANEKHTEAILSVVSSTLTENTGKILESVVEKSMQVALKEEIANSVRNALKNNLEKIESFLENSIAELQNSVREDFDKQTSSLAQLRYSIQNVAHAQKESEVKYNELNEQVKTLEGYVETVLEKFNDLKIENKVPETAPDVVPSSYPPAAESNVSVSSDTSTKDVEKQEPSSAEQPAQGIAESLRRLKEYVKAGSVKECVAEWCNMPSVAGFDVLSEISYDRMLENCSNLLLLTFIYHISLLDSVDDDRLSKRMEYISRICLNIDVNDPKVETVVHPVLTLTREALLRQSEFFSPIFKRRLVVLLRALDGKISEISVASSN O13898 PMT1_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; EC=2.4.1.109; CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; EC=2.4.1.109; MOD_RES 451; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22A12.07c; CHAIN 1..893; /note="Dolichyl-phosphate-mannose--protein mannosyltransferase 1"; /id="PRO_0000121499" CARBOHYD 370; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 443; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 665; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 720; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMDVYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIFDNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLWNLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVTIRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHKPIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQREVTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFYEQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHYLPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDNLSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASEAAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQEENVAESAQARVE O13899 CRLS1_SCHPO CATALYTIC ACTIVITY: [Mitochondrial hydrolase]: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-diacyl-sn-glycerol = a cardiolipin + CMP + H(+); Xref=Rhea:RHEA:32931, ChEBI:CHEBI:15378, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; EC=2.7.8.41; Evidence={ECO:0000305|PubMed:29958934}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q07560}; TRANSIT 1..24; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: [Isoform 1]: Proteolytically cleaved, presumably during its import into the mitochondrion by mitochondrial processing peptidase. {ECO:0000269|PubMed:29958934}. SPAC22A12.08c; CHAIN 25..595; /note="Cardiolipin synthase (CMP-forming) / mitochondrial hydrolase fusion protein"; /evidence="ECO:0000255"; /id="PRO_0000318105"; CHAIN 25..?; /note="Mitochondrial hydrolase"; /evidence="ECO:0000269|PubMed:29958934"; /id="PRO_0000458745"; CHAIN ?..595; /note="Cardiolipin synthase (CMP-forming)"; /evidence="ECO:0000269|PubMed:29958934"; /id="PRO_0000458746" MLHTINYRSWHLAARQLGRSTFRKFTTESSTKSPIADVCFAFDSIDGVLIRGGRGLKEGTKTLKFLQKNNIPFILLTNGGGMHESVRAQRLSKTLSVSLTEDDFCQSHTPFRALADKYKHVLVLGGKDNSVRETAEKYGFKSVINELDVIAKLGTPFWPFTSFNEEDIKDAKDFDVTRPIEAVFTYVDPVRLGLDLQLVMELGQSKNGVLGTVSKTANEGPDIYFSNADLIWPNEYPLPRLGQGAFAICCESVFKELTGKDLRNTKYGKPHKLTYDYAKNILMKKHKTLGITNPPKEIFMVGDNPESDIRGANNYGWTSILVRTGIFQGDNSPKYSAKHVSDNVWEGVRWALSKHVPAAKLNKSMGEVRGFHTSSRVLNTVTKSNNSKPIQRPLRENIFTLPNLLTFSRLLSAPLIAYLYIYDYTKAAACFFLYAGFTDLVDGYIARKFDLGSIAGTVLDPLADKTLMTCLTICLAVRETMPLTLASLIIGRDVLLVSAVSYLRYKSLPAPKTFRRFFDFAIPTTELKPTRISKWNTALQLLLLGLLITEPILPFDASFAKSPLFYIVGCTTIASGASYCISRNTFRNIGKSKLQ O13902 DAK1_SCHPO ACT_SITE 221; /note="Tele-hemiaminal-histidine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00814" BINDING 53..56; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 104; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 109; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 413..416; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 458..459; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 512..513; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 565..567; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216; EC=2.7.1.29; Evidence={ECO:0000269|PubMed:10091325}; CATALYTIC ACTIVITY: Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378, ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216; EC=2.7.1.28; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.01 mM for dihydroxyacetone {ECO:0000269|PubMed:10091325}; KM=0.63 mM for ATP {ECO:0000269|PubMed:10091325}; Vmax=29.4 mmol/min/mg enzyme {ECO:0000269|PubMed:10091325}; SPAC22A12.11; CHAIN 1..580; /note="Dihydroxyacetone kinase 1"; /id="PRO_0000121520" MDKHFINDPEVLVLDGLKSLADMNKTLTVHEEGKFIYFHDYNKKNVSVISGGGAGHEPTHSSFVGKGMLTAAVSGSIFASPSSKQIYTGIKQVESEAGTLVICKNYTGDILHFGMALEKQRTAGKKAELIAVADDVSVGRKKSGKVGRRGLSGTVLVHKIAGAAAARGLPLEAVTTIAKAAIDNLVSIGASLAHVHVPGHEPIAKEDEMKHDEMELGMGIHNEPGCKRISPIPSIDDLIAQMLKQMLDQSDKDRAYVKIEGDDEVVLLMNNLGGLSMLEFSAISHKVKEALAKEYKINPVRIFAGPFTTSLNGLGFGITLLRTTDRVKVEGEEYSLVDLIDQPVEAIGWPLCQPSDLKSKNKIGNVSIEEGQKDVKSPVTVDKEKVRQAIVNSMENLIKAEPKITKFDTMAGDGDCGTTLKRGAEGVLKFVKSDKFSDDPIRIVRDIADVIEDNMDGTSGALYAIFFHGFAKGMKDTLEKSKDISSKTWAAGLKVALDTLFKYTPARPGDSTMCDALVPFVETFVKTNDLNAAVEEARKGADATADMQAKLGRAVYVGDDVKVPDAGALGVVAIVEGFTK O13911 PNK1_SCHPO BINDING 263..270; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=a 3'end (2'-deoxyribonucleotide 3'-phosphate)-DNA + H2O = a 3'-end 2'-deoxyribonucleotide-DNA + phosphate; Xref=Rhea:RHEA:14113, Rhea:RHEA-COMP:13863, Rhea:RHEA-COMP:13864, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:138147, ChEBI:CHEBI:138148; EC=3.1.3.32; Evidence={ECO:0000269|PubMed:11729194}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14114; Evidence={ECO:0000305|PubMed:11729194}; CATALYTIC ACTIVITY: Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + ADP + H(+); Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412, ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78; Evidence={ECO:0000269|PubMed:11729194}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15670; Evidence={ECO:0000305|PubMed:11729194}; MOD_RES 8; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C11.04c; CHAIN 1..408; /note="Bifunctional polynucleotide phosphatase/kinase"; /id="PRO_0000058477" MSSKKRKSPPQESLTSYFEKSSKSSKKYGSQNKDSDSSSTCLQQKIEIQWSITDSLYIAKYGKLKKTKKFIAFDLDGTLIKTKSGRVFSKDAADWTWWHPSVVPKLKALYQDNYSLVIFSNQNGIPRKPSAGHTFQMKIRAIFESLDLPIVLYAAILKDKFRKPLTGMWNSFLKDVNRSIDLSFIKYVGDAAGRPGDHNSTDLKFAENIGIKFETPEQFFLGHSFVPPNFESFHPKNYLVRNSSSHPYHFKKSEHQEIVVLVGFPSSGKSTLAESQIVTQGYERVNQDILKTKSKCIKAAIEALKKEKSVVIDNTNPTIESRKMWIDIAQEFEIPIRCIHLQSSEELARHNNVFRYIHHNQKQLPEIAFNSFKSRFQMPTVEEGFTNVEEVPFKCLKDYEDTWNYWYE O13917 HPRT_SCHPO ACT_SITE 114; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 110..118; /ligand="GMP"; /ligand_id="ChEBI:CHEBI:58115"; /evidence="ECO:0000250"; BINDING 154; /ligand="GMP"; /ligand_id="ChEBI:CHEBI:58115"; /evidence="ECO:0000250"; BINDING 181..187; /ligand="GMP"; /ligand_id="ChEBI:CHEBI:58115"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; Evidence={ECO:0000250|UniProtKB:Q04178}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; Evidence={ECO:0000250|UniProtKB:Q04178}; CATALYTIC ACTIVITY: Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8; Evidence={ECO:0000250|UniProtKB:Q04178}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; Evidence={ECO:0000250|UniProtKB:Q04178}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein. {ECO:0000250}; SPAC23C11.13c; CHAIN 1..206; /note="Hypoxanthine-guanine phosphoribosyltransferase"; /id="PRO_0000116674" MDPVRLYYSYNDIHKMCAQQAEKILETFRPDVIIAIGGGGFIPARILRTFLKKKGSKNIPIQAIGLSLYEELVSDSPEEVPGLEVKRTQWLDFSTLGMVDLVGKNILIVDEVDDTRTTLHYALRELQRDVAEQAKKLNREGEKTTFGIFVVHNKVKPKNAQLDKEILDKYYFTGCNTPDCWIMYPWEAQDIEEHDSHVAKMGDLKP O13919 PST2_SCHPO MOD_RES 641; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 643; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C11.15; CHAIN 1..1075; /note="Paired amphipathic helix protein pst2"; /id="PRO_0000121542" MEQTLAILKNDNSTLVAEMQNQLVHDFSPNGTALPELDIKAFVQKLGQRLCHRPYVYSAFMDVVKALHNEIVDFPGFIERISVILRDYPDLLEYLNIFLPSSYKYLLSNSGANFTLQFTTPSGPVSTPSTYVATYNDLPCTYHRAIGFVSRVRRALLSNPEQFFKLQDSLRKFKNSECSLSELQTIVTSLLAEHPSLAHEFHNFLPSSIFFGSKPPLGSFPLRGIQSSQFTLSNISDLLSQSRPDNLSPFSHLSNESSDFFKNVKNVLTDVETYHEFLKLLNLYVQGIIDRNILVSRGFGFLKSNSGLWRSFLSLTSLSPEEFLSVYNSACSDFPECGPSYRLLPVEERNISCSGRDDFAWGILNDDWVSHPTWASEESGFIVQRKTPYEEAMTKLEEERYEFDRHIEATSWTIKSLKKIQNRINELPEEERETYTLEEGLGLPSKSIYKKTIKLVYTSEHAEEMFKALERMPCLTLPLVISRLEEKNEEWKSVKRSLQPGWRSIEFKNYDKSLDSQCVYFKARDKKNVSSKFLLAEADILRSQAKLHFPLRSRSAFEFSFVYDNEIVLFDTCYMVCTYIVCNSPSGLKKVEHFFKNILPLHFGLEKDKFSIFLDQVFRGPDYDVNAPNIVGNKPVRRKRSNSITQLTEFVKQPKINGQRESRSAAAARKKEESGNKSQSNSQNSLSDESGNVTPVSKKQLSQPAAAIKASLKYPSHPDSLLEHQDHAGDTENEMHDDVDKEQFGYSSMYVFFRLFNLLYERLYELQRLEDQVSIIQQRIIPNPVSQKQKIWRDRWNDLSDVPDEKTHYENTYVMILRLIYGIVDQSAFEDYLRFYYGNKAYKIYTIDKLVWSAAKQVHHIVSDGKYKFVTSLVEQNSSASPKKNYDDFLYRLEIEKLLNPDEILFRFCWINKFKSFGIKIMKRANLIVDQSLDTQRRVWKKYVQNYRIQKLTEEISYKNYRCPFLCRNIEKERTVEQLVSRLQTKLLRSAELVSGLQAKLCLDSFKLLYLPRTEDSYIDASYLRLRDTDFLDCQNKRKQRWRNRWESLLKSVRGTSDNTAEVNFDADINALFIP O13924 HASP_SCHPO ACT_SITE 305; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" BINDING 162..170; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 184; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC23C4.03; CHAIN 1..488; /note="Serine/threonine-protein kinase haspin homolog hrk1"; /id="PRO_0000352813" MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY O13928 RHO3_SCHPO BINDING 20..27; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P61586"; BINDING 67..71; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P20171"; BINDING 125..128; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P61586" PTM: Palmitoylated by the erf2-erf4 complex. {ECO:0000269|PubMed:23843742}. MOD_RES 202; /note="Cysteine methyl ester"; /evidence="ECO:0000250|UniProtKB:P62745" SPAC23C4.08; PROPEP 203..205; /note="Removed in mature form"; /evidence="ECO:0000250|UniProtKB:P62745"; /id="PRO_0000281272" CHAIN 1..202; /note="GTP-binding protein rho3"; /id="PRO_0000198942" LIPID 202; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P62745" MSSCFGSKKKPIYRKIVILGDGAAGKTSLLNVFTKGYFPQVYEPTIFENYIHDIFVDGNSIELSLWDTAGQEEYDQLRSLSYSDTHVIMICFAVDSRDSLENVITKWLPEVSSNCPGVKLVLVALKCDLRGADEEQVDHSKIIDYEEGLAAAKKINAVRYLECSAKLNRGVNEAFTEAARVALAAQPRGTKDGADESHGTGCIIA O13935 TRM4B_SCHPO ACT_SITE 323; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" BINDING 167..173; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 208; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 235; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 270; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" CATALYTIC ACTIVITY: Reaction=cytidine(49) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(49) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54140, Rhea:RHEA-COMP:13804, Rhea:RHEA-COMP:13805, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192, ECO:0000305|PubMed:30646830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54141; Evidence={ECO:0000269|PubMed:23074192, ECO:0000305|PubMed:30646830}; CATALYTIC ACTIVITY: Reaction=cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(50) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61488, Rhea:RHEA-COMP:15838, Rhea:RHEA-COMP:15839, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:30646830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61489; Evidence={ECO:0000305|PubMed:30646830}; CATALYTIC ACTIVITY: Reaction=cytidine(60) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(60) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51160, Rhea:RHEA-COMP:12902, Rhea:RHEA-COMP:12905, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51161; Evidence={ECO:0000269|PubMed:23074192}; CATALYTIC ACTIVITY: Reaction=cytidine(61) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(61) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51164, Rhea:RHEA-COMP:12903, Rhea:RHEA-COMP:12906, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51165; Evidence={ECO:0000269|PubMed:23074192}; CATALYTIC ACTIVITY: Reaction=cytidine(62) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(62) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51172, Rhea:RHEA-COMP:12904, Rhea:RHEA-COMP:12907, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51173; Evidence={ECO:0000269|PubMed:23074192}; SPAC23C4.17; CHAIN 1..685; /note="Multisite-specific tRNA:(cytosine-C(5))-methyltransferase trm4b"; /id="PRO_0000317151" MGKRNKKVTQGKRAYNDKSEIVLENKQFEGYYKKQNLFRGKPNDEFDSFMEYMRKPLPTTFRICGYRHHAFELKNHFEKYYVPSLKNVVHEGQTIPPPTVLPWYPDGLAYIVDAQKDVIRKSPPLKRLQRFLVSENEAGNINRQEAVSMLPPLFLDVEPHHVILDMCAAPGSKTAQLIEAVYKKANIKDAAHDSKNLKSVEGLVIANDADPKRAQMLVHQINRLNSPNILVVNHDASTMPNIYVKGSSPSDGLNVIEEKKILKFDRILADVPCSGDGTFRKNLSLWREWSANSAFSLHPLQLRILIRGLQLLKVGGCLVYSTCSINPIENEAVVTAALKATGGAVSLVDVSKKLPLLKRDPGLLSWKVLDDSLNEFQSPAENTNDKIELTESMWPLPEEEMSKLHIERCARLYPHMQNTGGFFVAVLQKTDPINSRSFDPKKYTASMEILPPENKRQRTEKGVDEASNSTLTKSGNSYFDEEPFVYINPDDTSIKTIVDFYGIDPSFPRDQFFVRNQSGIPVRSIYFACSLFKEIIEANTNRVKFVHGGVRFFVKQEISQLLKDFSLKANKDICNFRIHSNGVNIISPFLNEKHFYDAGLKDLKILVKNEYPHVEQFSESGMLKKEFEKMPLGCNILRVDAQTKDGALMDMLILQPIWRSPTSCNLMLARKEKQNLSLELFGMDV O13936 SPT5_SCHPO MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C4.19; CHAIN 1..990; /note="Transcription elongation factor spt5"; /id="PRO_0000238565" MDTNSPKSIDKDANSTEVDAAEQDAASVKINSTRASPNGSDLLNDDSEAAKITTNEKQSSPVDSHNESPNDTTINKGEDGNENEVDNVNNNDKKEDEDNVEENEEEADANEEEEEDEEDDEEDEEDEDESGGGRRKRARHDRRNQFLDIEAEVDEDEEELEDEEDEIGREDGFIEEEVGADYVGDDRRHRELDRQRQELQSVDAERLAEEYREKYGRSQTVVGDTSNVPQRLLLPSVNDPNIWAVRCKIGKEKDIVFTIMRKAMDLQYTSSPLEIISAFQRDSLVGYIYVEARKQSHVLDALNGVLNVYTNNMILVPIKEMPDLLKVQKQVVELLPGAYVRIRRGKYAGDLAQVDNLSENGLTARVRIVPRIDYSDGLKRKNSATRPQARLFNESEAFKSNPSKFSKRGPRLFLFNNEEFEDGFLVKDIRISSLITEGVNPTLDEVSKFNPNNEDLDLSSLALSVKGGHAEFQPGDHVEVYVGEQTGVSGVVENVRGSVITMVSSDGLRLDVPSRGLRKRFRHGDYVKVIAGKYKDDTGMVVRISKDEVTFLSDTLMTELTVFSRDLGEASSAQAVNSAYELHDLVQLDVNTVACIFSVDRDTYKVIDQNGGVRTVLASQITMRHSNRRGVATDRNGAEIRIGDKVKEVGGEGKQGTILHIYRAFVFLHNRDIAENNGVFSARSRNVATIAAKGARISADLTKMNPALSNGPALPPVANLKRTIGRDKAIGATVRIRRGPMKGLLGVIKDTTDANARVELHTGNKMVTIPKENLLYTTKTGELISYTEFIERSRGIRPGSISTADGPNVPNWAQGARTPAVANGSRTPAWNTGSRTPAWNSGSKTPAWNSGSRTPAWNSGNKTPAWNAGSRTPAWNSGNKTPAWNVGNKTPAWNSGAKTPAWNAGNKTPSWNNGTKTPAWNANQTPMVANGTNTSWGQTPAYGGFSETNWDTEDNSKPYTAPTPGAWAAPTPGGWDDEEGDSPKYVPPSP O13953 EAF3_SCHPO SPAC23H4.12; CHAIN 1..337; /note="Chromatin modification-related protein eaf3"; /id="PRO_0000088780" MAVSYKVNERVLCFHGPLLYEAKIVDTEMKGDVTTYLIHYKGWKNSWDEWVEQDRILQWTEENLKTQKELKNAAISTRQKPTSKKSASSTSKHDSTGVKTSGKRSRESSTVTVDGDSHELPSRIKTQKSESPIPQQVKRDGTTDAKNEETTKPENNEKDDFEEEPPLPKHKISVPDVLKLWLVDDWENITKNQQLIAIPRNPTVRAAIAAFRESKISHLNNEIDVDVFEQAMAGLVIYFNKCLGNMLLYRFERQQYLEIRQQYPDTEMCDLYGVEHLIRLFVSLPELIDRTNMDSQSIECLLNYIEEFLKYLVLHKDEYFIKEYQNAPPNYRSLVGV O13958 SSN3_SCHPO ACT_SITE 140; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 11..19; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 36; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; SPAC23H4.17c; CHAIN 1..369; /note="Serine/threonine-protein kinase srb10"; /id="PRO_0000086580" MKDGYKIIGFISSGTYGKVYKAVSSNSNDKRLFAIKKFKAESKQVSSNAQQTGVSQSAIREMMLCREIQHENIVSLVQVLLKDGTISMVFEYAEHDLLQIIHFHSRSRTRQIPPSILKSILWQIINGVAYLHENWIMHRDLKPANIMITATGKVKIGDLGLGRLIRDPILPFYSSDRVVVTIWYRAPELLLGAHDYTPAIDVWAIGCIYGEMLALSPLFKGDEIKMEDKKVVPFQSTQMLRIMELLGTPTEERWPGLKNYPEYYQLSSFEVRYWNNLLPQWYQTVKNRDPQGLDLLMKMLQYDPKSRITAKQALEHVFFTSDKLWTTSPFLNQPIHYPERRISEDDSEVSSKRVLSTSLRSESKRFKGN O13959 RBX1_SCHPO BINDING 41; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 52; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 55; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 67; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 74; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 81; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 93; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 96; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" SPAC23H4.18c; CHAIN 1..107; /note="RING-box protein pip1"; /id="PRO_0000056021" MEDEMQIDKKEVEIEQKPPRFEIKKWNAVALWQWDIVVDNCAICRNHIMDLCIECQANTDSAAAQECTVAWGTCNHAFHFHCISRWLNTRNVCPLDNREWEFQRYGH O13961 NDC1_SCHPO SPAC1786.03; CHAIN 1..601; /note="Nuclear envelope protein ndc1"; /id="PRO_0000079566" MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVMLKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYFSHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRIAYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIATEELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHEEINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQNEALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAANALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS O13978 AT101_SCHPO SPAC25H1.03; STRAND 3..12; /evidence="ECO:0007829|PDB:4YK8"; STRAND 40..43; /evidence="ECO:0007829|PDB:4YK8"; STRAND 46..49; /evidence="ECO:0007829|PDB:4YK8"; STRAND 78..85; /evidence="ECO:0007829|PDB:4YK8"; STRAND 103..113; /evidence="ECO:0007829|PDB:4YK8"; STRAND 139..141; /evidence="ECO:0007829|PDB:4YK8"; STRAND 157..160; /evidence="ECO:0007829|PDB:4YK8" HELIX 16..29; /evidence="ECO:0007829|PDB:4YK8"; HELIX 54..73; /evidence="ECO:0007829|PDB:4YK8"; HELIX 90..93; /evidence="ECO:0007829|PDB:4YK8"; HELIX 119..137; /evidence="ECO:0007829|PDB:4YK8" TURN 13..15; /evidence="ECO:0007829|PDB:4YK8"; TURN 94..96; /evidence="ECO:0007829|PDB:4YK8" CHAIN 1..184; /note="Autophagy-related protein 101"; /id="PRO_0000278502" MTNTVTIELKIGYKYAAEVVKAVLGVILFHRQFSTVPARTIDVLDITVPTLVGAELNEQLATKAAEFIDTIRNEAGANGQMILLLYERSPKKSWFGKGNTIPWEQWILHTTILEEGDSYQESSLSLEAAVEQIVQAVNLRSLSYLPPVAMDSGNYPYEIVTPTSTEGWGSLLKRMIIENVSGGD O13983 HRQ1_SCHPO BINDING 333..340; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:22064477}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q05549}; SPAC23A1.19c; CHAIN 1..1063; /note="ATP-dependent helicase hrq1"; /id="PRO_0000353818" MSQTPIKKEESNDQDDKFEFKKYINEGKLPLKADNPKKKPQLGTIQANQPIPSIFDNLFNLFKVINTTYTFLYLRNSLTITFPLLNSSVKQSLKKELTIGDLSQLREICPQIIELNYKSLASLALEINKNVYTDLNPELYTGSTVSQSSEYVLVIELLETQERSSKRRRREGPTMKANIQRQKLDFNNLKKAIELRNQKFLQGIKEYIKKCQLTELDPTQQLLTQSRKNQPVPPDSPSIPNDSIENCNLNTKACSIEELLNEIASESSYEGQIVQEALHTYPAVEAQYGALSRPLSQELINALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTLKNIRVDTFDGDTPLESRESIIRSANIIFTNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIAEYFGNSQYRFVSCSATIEDPLQHMKKIFGVDNIKLINYTSSPSGSKKFVMWNPPYVDPKHPDDGKKSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELKTKQKGDLLSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVETFPVDQFYLKHPILIHTQPNAELTLDLTNEVLLASHLQCAAYELPINIRSDEKFFGNQIQDICEANLEMVEESYRPHPKYLPFPASQVRIRSVSEDMFTLVDVTNDKNVILELLEPFRVALTAYEGAVYVYQGKTFIIRLLNINKRIITAHQVDVEWSTLQRDFTDVDPVRSLMKKTMHGSTNIYFGAVKATLHVFGYFKVNKQKDILDVVDITDHPVEIDSRGFWIDVPWHIIEVLSLKKINGAASIHAAQHALLSLMPIFISNSGNDIRTECKAGEKEYKEAKSERRRPSRLIFYDNCGDSSGAGLCNKAYEHTDELITMAIERIESCDCKVREGCPGCITSSKFEGGVCSGEVLDKVGALILLKMLLCQHVNLDIYADGPEIDSYHALRTLIPSC O13988 POT1_SCHPO SPAC26H5.06; STRAND 18..22; /evidence="ECO:0007829|PDB:1QZG"; STRAND 25..28; /evidence="ECO:0007829|PDB:1QZG"; STRAND 41..57; /evidence="ECO:0007829|PDB:1QZG"; STRAND 65..72; /evidence="ECO:0007829|PDB:1QZG"; STRAND 78..80; /evidence="ECO:0007829|PDB:1QZH"; STRAND 83..93; /evidence="ECO:0007829|PDB:1QZG"; STRAND 104..115; /evidence="ECO:0007829|PDB:1QZG"; STRAND 118..131; /evidence="ECO:0007829|PDB:1QZG"; STRAND 138..140; /evidence="ECO:0007829|PDB:7CUH"; STRAND 212..224; /evidence="ECO:0007829|PDB:5USB"; STRAND 229..234; /evidence="ECO:0007829|PDB:5USB"; STRAND 258..260; /evidence="ECO:0007829|PDB:5USN"; STRAND 263..267; /evidence="ECO:0007829|PDB:5USB"; STRAND 284..294; /evidence="ECO:0007829|PDB:5USB"; STRAND 300..304; /evidence="ECO:0007829|PDB:5USB"; STRAND 315..319; /evidence="ECO:0007829|PDB:5USB"; STRAND 378..380; /evidence="ECO:0007829|PDB:7CUI"; STRAND 405..419; /evidence="ECO:0007829|PDB:7CUI"; STRAND 424..429; /evidence="ECO:0007829|PDB:7CUI"; STRAND 433..443; /evidence="ECO:0007829|PDB:7CUI"; STRAND 449..455; /evidence="ECO:0007829|PDB:7CUI"; STRAND 519..527; /evidence="ECO:0007829|PDB:7CUI"; STRAND 546..554; /evidence="ECO:0007829|PDB:7CUI" HELIX 8..16; /evidence="ECO:0007829|PDB:1QZG"; HELIX 30..33; /evidence="ECO:0007829|PDB:1QZG"; HELIX 148..150; /evidence="ECO:0007829|PDB:7CUH"; HELIX 156..173; /evidence="ECO:0007829|PDB:1QZG"; HELIX 204..206; /evidence="ECO:0007829|PDB:5USB"; HELIX 270..275; /evidence="ECO:0007829|PDB:5USB"; HELIX 310..312; /evidence="ECO:0007829|PDB:4HJ7"; HELIX 324..326; /evidence="ECO:0007829|PDB:5USB"; HELIX 327..336; /evidence="ECO:0007829|PDB:5USB"; HELIX 390..394; /evidence="ECO:0007829|PDB:7CUI"; HELIX 421..423; /evidence="ECO:0007829|PDB:7CUI"; HELIX 456..463; /evidence="ECO:0007829|PDB:7CUI"; HELIX 473..475; /evidence="ECO:0007829|PDB:7CUI"; HELIX 477..491; /evidence="ECO:0007829|PDB:7CUI"; HELIX 494..504; /evidence="ECO:0007829|PDB:7CUI"; HELIX 508..510; /evidence="ECO:0007829|PDB:7CUI"; HELIX 511..514; /evidence="ECO:0007829|PDB:7CUI"; HELIX 542..544; /evidence="ECO:0007829|PDB:7CUI" TURN 247..249; /evidence="ECO:0007829|PDB:4HIO"; TURN 276..278; /evidence="ECO:0007829|PDB:5USB"; TURN 430..432; /evidence="ECO:0007829|PDB:7CUI" CHAIN 1..555; /note="Protection of telomeres protein 1"; /id="PRO_0000121732" MGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTSSARQNQTGLSYPSVSFSLLSQITPHQRCSFYAQVIKTWYSDKNFTLYVTDYTENELFFPMSPYTSSSRWRGPFGRFSIRCILWDEHDFYCRNYIKEGDYVVMKNVRTKIDHLGYLECILHGDSAKRYNMSIEKVDSEEPELNEIKSRKRLYVQNCQNGIEAVIEKLSQSQQSENPFIAHELKQTSVNEITAHVINEPASLKLTTISTILHAPLQNLLKPRKHRLRVQVVDFWPKSLTQFAVLSQPPSSYVWMFALLVRDVSNVTLPVIFFDSDAAELINSSKIQPCNLADHPQMTLQLKERLFLIWGNLEERIQHHISKGESPTLAAEDVETPWFDIYVKEYIPVIGNTKDHQSLTFLQKRWRGFGTKIV O13995 DAP1_SCHPO BINDING 138; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413" MOD_RES 108; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC25B8.01; CHAIN 1..166; /note="Cytochrome P450 regulator dap1"; /id="PRO_0000121746" MASTQVVFIVTLFLYLLITRWRRKNEKSFIASEEPKQPEWRDYTPAELKEYNGSKNSLVFLAIKGTVYNVTMGSKFYGPQGPYSAFAGHDASRGLAKNSFDDEFIPDSDAEELDDCSDLNDEERQALNDWKAFFDQKYQAVGRLISPREARAAATISETEEKVAHN O14003 RFC3_SCHPO BINDING 63..70; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC27E2.10c; CHAIN 1..342; /note="Replication factor C subunit 3"; /id="PRO_0000121755" MSIEKGKGRAMDIDLPLGSESTLPWVEKYRPANLEDVVSHKDIISTLEKFISSNRVPHMLFYGPPGTGKTSTILACARKIYGPNYRNQLMELNASDDRGIDAVREQIKNFASTRQIFASTFKMIILDEADAMTLAAQNALRRVIEKYTKNVRFCIICNYINKISPAIQSRCTRFRFQPLPPKEIEKTVDHVIQSEHCNIDPDAKMAVLRLSKGDMRKALNILQACHAAYDHIDVSAIYNCVGHPHPSDIDYFLKSIMNDEFVIAFNTISSIKQQKGLALQDILTCIFEALDELEIKPNAKIFILDQLATIEHRMSFGCSEKIQLSAMIASIKTGVDLAAKVN O14008 CAM2_SCHPO SPAC29A4.05; CHAIN 1..143; /note="Myosin 1 light chain cam2"; /id="PRO_0000334492" MPASKEQTDEMKEAFVLYDIDKDGLIPTSHVGSVLRSLGINVTDAELAKLSNELGDAIDEKKFMSFVSNKLRETESEEEYIKAFRVFDKDNSGYIETAKFADYMKTLGEKLSDNEVQLMVQEADPTNSGSFDYYDFVQRIMAK O14011 PRP19_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P32523}; SPAC29A4.08c; CHAIN 1..488; /note="Pre-mRNA-processing factor 19"; /id="PRO_0000050950" MFCSISGETPKEPVISRVSGNVYEKRLIEQVIRETSKDPVTQQECTLEDLVPVKVPDFVRPRPPSATSLPALLSLFQEEWDSVALEQFELRRNLTETKQELSTALYSLDAALRVISRLTKERDEAREALAKFSDNIGTVSSKTIEVQEVEMGESDDQLKTSLRSTVEKTFQELSSKRKRTKLQPKWATDDAVSQLLQATPSTILENLETESTTSFFPSPENSSFVLCLHKDELLCLDIQSNSTLKIFEGSALACCWLTSSKIAVATADAISIFEFPVSSSGLQSVGEPTSSIPIDEKVNFLQAHPSGEYLLAASNEKCYIFSLKSQVYNITVAQHITSLAVHPDGNLFVAGLENGELRFFETSSGNELTKFGPHSSPVKTLQFGENGYWLVVTTNDDSDIFIWDLRKSELVQKIPLQTKVAAVSLDITSQLLVSSDGETLYVHIYVKSSKSWRCMSQTHVSSISNLVWLNELHQLLFSTSNGAILRLG O14019 HAL4_SCHPO ACT_SITE 481; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 357..365; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 385; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 238; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 241; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 299; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29A4.16; CHAIN 1..636; /note="Serine/threonine-protein kinase hal4"; /id="PRO_0000085986" MGEKDKLHEISSKFASLGLGSLKSTPKARETTEPPPPSSQQPPSTPNGKEAASPSALKQNVRPSLNSVQQTPASIDAVASSSNVSLQSQQPLSKPVVSSKPNQTTAMPPPSNNPSRHVSSTSNKPAAVSPNPAAHHAELPSGSVPPSASVSRANSTATTTPHKAGVVSNPAAANVHVLSVAASPNPSTPSNGPAPVSTTATPSRNPVTRLQRIFSQNSVSRQNSRTGRGAAVANTEETNSTGGSETGGAANSSSTSNPSSAKWSRFTVYDDASHTHQLRPARRQEKLGKMLKDFLAGNSKKREEERIAKEAADAQHQLSLVQSWINGYGQEKLADKKDPAKVSASFVEKYGRCQEVIGRGAFGVVRIAHKVDPQNSGSETLYAVKEFRRKPAESQKKYTKRLTSEFCISSSLRHPNVIHTLDLIQDGKGDYCEVMELCSGGDLYTLIMAAGRLEPMEADCFFKQLMRGVDYLHDMGVAHRDLKPENLLLTVSGSLKITDFGNGECFRMAWEKEAHMTCGLCGSAPYIAPEEYTESEFDPRAVDVWACGVIYMAMRTGRHLWRVAKKSEDEYYSRYLMDRKNESGYEPIEMLERSRCRNTLYNILHPNPTYRLTAKQIMKSEWVRSITLCEAGNAGL O14021 PRW1_SCHPO SPAC29A4.18; CHAIN 1..431; /note="RbAp48-related WD40 repeat-containing protein prw1"; /id="PRO_0000051170" MAVSAVPHPSKQAQASEEGINQEKCINEEYKIWKKNSPFLYDLIITRALEWPCMSLQWYPEQQIFAEHGYTEQKMFLGVRADVGKYLLAVASIQLPYLNQTVPPTTMEGASAGDESSLRVNISNLYSHPESVCSAKLMPQDDSCVATVGNYHNDVLVFDKESFESYSSASESPLKPKYRLTKHTQPCTSVCWNFLSKGTLVSGSQDATLSCWDLNAYNESDSASVLKVHISSHEKQVSDVRFHYKHQDLLASVSYDQYLHVHDIRRPDASTKPARSVHAHSGPIHSVAFNPHNDFILATCSTDKTIALWDLRNLNQRLHTLEGHEDIVTKISFSPHEEPILASTSADRRTLVWDLSRIGEDQPAEEAQDGPPELLFMHGGHTSCTIDMDWCPNYNWTMATAAEDNILQIWTPSRSIWGNEQLEEDATAYLS O14022 CTA5_SCHPO ACT_SITE 480; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250" BINDING 838; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 842; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; SPAC29A4.19c; CHAIN 1..1096; /note="Cation-transporting ATPase 5"; /id="PRO_0000046353" MDSIELKQLVPENDSEPGTPRQLLFQHYDISNEETIGIKPFKSIPAKVYILRVTEILTLGLLHLILTWLPEFRLKWIEAPCSNEDVEFVAISDPSGTSSIEKVSSICLKNDIQTSSFVLPSGKTRYFEYKKLRFYLEPLNLQWVLMPLETSAYSLVTSTPAYIQNGLDTFTIAKLRQVYGSNSLVSTKKSIVTILLNEVLHPFYLFQAVSVLIWLCDSFVFYSCCIVFISSYSIFLSVKESKESENRIHSIIGAPQPVTVIRNQVKQTVLADDLVIGDLLYFSNLDLKTCPVDGILFSSSCLLDESMVTGESVPARKFPLEDNSLDSWMIASCNIFSPHLIHAGTKFLKIDSTPSTPCLISVVRTGFRSNKGQLIRNLLYPNLRPSQLYLDSMSFLKTMAILSFVSIVFIAIYLNLYNASFGHVVLRSLDVLTILVPPALPATLSVGIANSIARLSRALIYTTSPESIHNAGCLSTFVFDKTGTLTENSVQLSCVYVKSGSNGLLKQVDADSLSLDSTKLNAHAYRVATCSQSLELVGNELVGDPLEVTLFTQFNGTFCATIRASNTPHPPLFSVSNSFDGPSQIFSIYKALEFDPVLRRMSVICSTSTERSLMLFTKGAPESILAISSQQSIPSNVQEVIHTLSSKGFRIIAFASKNLITPLQELIHLSRSTLESNVTFQGLFVLESPLRESSKDVISSLLRSKMEVSICSGDSLFTSVFVAKHCGALDSCNFIYTAELADSGDDCPQIHFEKIDLQTQNFQPIPDGFSLKDVILEKDSSLCMDGKLLQRLLTMLSFNEIKILLSKLRVLARMSPFDKATYVELCQKYGCKVGFCGDGANDCIALKQADVGVSLSDSEACAAASFVSKKKSIKDVFNVLLEGRCSLILSHRCFQYMVLCAIVQFSGVFFLYLKNYNFNDNQFLFMDLLIIFPLSAAMSYFDPAQNLTSNRPNSTLFGKGRVKDLGIQSVLIWLSHGLLTLILHELNWVELPEWQLEKSNTKNVLVTSIFLLSSLQYLGICIGINQSSEFLSPIWKKKTYVCLCTTIGLCNIYLCFANENHIISRCLQITRLPTLYRFIILFMGVISCCLTSILNM O14023 ELP3_SCHPO BINDING 96; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000250|UniProtKB:Q02908"; BINDING 106; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000250|UniProtKB:Q02908"; BINDING 109; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000250|UniProtKB:Q02908"; BINDING 161; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"; BINDING 472..475; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"; BINDING 495..497; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"; BINDING 528; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74882; EC=2.3.1.311; Evidence={ECO:0000250|UniProtKB:D5VRB9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; Evidence={ECO:0000250|UniProtKB:D5VRB9}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q02908}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908}; SPAC29A4.20; CHAIN 1..544; /note="Elongator complex protein 3"; /id="PRO_0000310360" MSTSSLAFLKAKACAEIVAELIASENQNKVINLNALKMRISKKHQLSESPRLTDIIAAIPPDAYLKESLMRKLRAKPVRTASGIAVVAVMCKPHRCPHIAMTGNVCVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLRSLGHTVDKVEYIIMGGTFMSLPESYRHTFIANLHNALSGATTEDLDEAVKFSEQSETKCVGITIETRPDYCLDQHLDEMLRYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCETFQLAKDTGYKVVTHMMPDLPNVGMERDIFQFQEYFENPAFRTDGLKLYPTLVIRGTGLYELWKTGRYKNYTPNALVDLIARILALVPPWTRIYRIQRDIPMPLVSSGVETGNLRELALNRMRDLGTKCRDIRAREVGMQEVHHKIHPEQVELLRRDYTANGGWETFLSYEDPKQDILIGLLRLRQCSDKTYRPEFTSQPTSLVRELHVYGSAVPVHSRDPKKFQHQGFGTLLLEEAERIAKYEHGSKKISVISGVGVRKYYQKLGYTLDGPYMSKWL O14026 SET2_SCHPO CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359; Evidence={ECO:0000250|UniProtKB:P46995, ECO:0000255|PROSITE-ProRule:PRU00901}; MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 545; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 594; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 596; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 783; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 785; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 787; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 789; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 793; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29B12.02c; CHAIN 1..798; /note="Histone-lysine N-methyltransferase, H3 lysine-36 specific"; /id="PRO_0000269792" MQTASSLSVLTPLNEENVDRKSSWSKDTIAVQAVGSSPSSSSSHDFESKEDAEGMNKDESAPSPSTSSPSSASSRSQSKYVRKEALPPQLFHHLDSAKDKALTTFEEIQECQYASANIGKPPENEAMICDCRPHWVDGVNVACGHGSNCINRMTSIECTDEDNVCGPSCQNQRFQRHEFAKVDVFLTEKKGFGLRADANLPKDTFVYEYIGEVIPEQKFRKRMRQYDSEGIKHFYFMMLQKGEYIDATKRGSLARFCNHSCRPNCYVDKWMVGDKLRMGIFCKRDIIRGEELTFDYNVDRYGAQAQPCYCGEPCCVGYIGGKTQTEAQSKLPENVREALGIEDEEDSWENITARRQRRKKGIDETSKIIEEVQPTPLTSESATKVIGVLLQTKDDLLTRKLMERIFLTSDPSVCRSIIALRGYNIFGLMLKKFSIDIEFILRSIKTMLSWPRLTRNKIQDSNIEPVVQEFCDHENEEVKDHAKTLLKEWESLEIAYRIPRRKPGQVAPQSTNAEPSNNQSNPPLRDQEPQRGDKGDIKSAINNSTEDLSKKHPALHSSRPSDSRSRSKFGNDYQSHSKHNLFRKNSFPKRRRLSNSDTPSETTTPNNEQEQVSNQANKVDLNKIISAAMESVNQKNVLKAQKEEEERIAQQKREEKRRLAYEESLKRHAKKLHEKKTKSSQDATIDHHLTSHSPESIAFKAVLAKFFANKTARYQEKLGKAEFKLRVKKMTEIILKKHIQLVLSKKEKALPDELSDSQQRKLRVWAFRYLDTVVSRSGTATTTPTDSPSIGESPKKAA O14031 PGT1_SCHPO BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63 uM for glutathione {ECO:0000269|PubMed:18662319}; MOD_RES 93; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29B12.10c; CHAIN 1..851; /note="Glutathione transporter 1"; /id="PRO_0000315922" CARBOHYD 32; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 77; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 109; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 256; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 452; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 464; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 691; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 843; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTARNSASIPTSIRKTSENEVSGDETPAGVGNLSTKTASKTSLTFRQSSSDESTSSYSGNHHNINIQHHPNRPFRTNSSSFSPNDYSISESPSKSKKDGVHVSAVQLDNETDSEVESEVEELERELEAIEDSVYPEVRAAVNPTDDVNLPVNTWRTWVLTTIFVIVFAAVNQFFSLRYPALSISFIVAQLILFPLGKLLNLLPNWKIGYGRFSFYLNSSPFNVKEHAAITIAVSLTSSTAYATNILSAQTSFYKQNLSWGYKILIVLTSQMLGYGFAGLTRRWIVYPAAMIWPQTLVSTVLFRTLHGNSGNDIGVLKNNRISANGWTISRYRFFAYVMIGSFVFYWFPGFIFKGLSYFTVLCWIWPKNRVVNQLFGYNSGLGILPLTFDWQQVVYNSNPLASPWWVICNTFGSVVLIFWIVVPILYYKGVWFSNYLPMLSSSTFDHTGVSYNSSRVLNSDYSFNHTKYESYSPLYMPMSYSMSTALNFAAVTAIFTHCALYNGKDIWQRLWKESGKDECIHRKLMRNYKEAPQWWYATLFIVVFGLTIFTVRYYDTQCPVWALIVALLIFIVNFIPQGVLEGITNQHVGLNIITELIGGYILPGKPLANLMIKLYGFIPMRQGLEFSRDLKLAQYMKIPPRILFFVQLFATILGGITQVAVQEWMNYHIPGICTTSQSNGFTCPNGRSIYNASLIWGAIGPAKMFSKGKPYYPLIFFFLIGAVAPFITWGLRKRFPKSWIGKLNAPVLFTGPGNIPPATGINYSSWAIVGFIFNYVIRKRAIHWWRKYNYVLAAAMDSGVAVAGVVIFLCVSYPGGKITWWGNTVYTKTYDWKSVPYRSLGPNETFGYTNW O14036 SMD2_SCHPO SPAC2C4.03c; CHAIN 1..115; /note="Small nuclear ribonucleoprotein Sm D2"; /id="PRO_0000122212" MADLVDKPRSELSEIELARLEEYEFSAGPLSVLQQAVKNHDQVLINCRNNKKLLARVKAFDRHSNMVLENVKEMWTEKKRTASGKKGKAINKDRFISKMFLRGDGVVLVVRIPSA O14040 DI3L2_SCHPO BINDING 453; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03045"; BINDING 462; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03045" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03045}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03045}; SPAC2C4.07c; STRAND 332..335; /evidence="ECO:0007829|PDB:4RO1"; STRAND 345..348; /evidence="ECO:0007829|PDB:4RO1"; STRAND 351..355; /evidence="ECO:0007829|PDB:4RO1"; STRAND 372..376; /evidence="ECO:0007829|PDB:4RO1"; STRAND 387..393; /evidence="ECO:0007829|PDB:4RO1"; STRAND 441..443; /evidence="ECO:0007829|PDB:4RO1"; STRAND 449..453; /evidence="ECO:0007829|PDB:4RO1"; STRAND 462..468; /evidence="ECO:0007829|PDB:4RO1"; STRAND 470..481; /evidence="ECO:0007829|PDB:4RO1"; STRAND 531..541; /evidence="ECO:0007829|PDB:4RO1"; STRAND 551..557; /evidence="ECO:0007829|PDB:4RO1"; STRAND 561..564; /evidence="ECO:0007829|PDB:4RO1"; STRAND 625..629; /evidence="ECO:0007829|PDB:4RO1"; STRAND 635..640; /evidence="ECO:0007829|PDB:4RO1"; STRAND 670..672; /evidence="ECO:0007829|PDB:4RO1"; STRAND 674..678; /evidence="ECO:0007829|PDB:4RO1"; STRAND 739..742; /evidence="ECO:0007829|PDB:4RO1"; STRAND 759..761; /evidence="ECO:0007829|PDB:4RO1"; STRAND 843..848; /evidence="ECO:0007829|PDB:4RO1"; STRAND 853..857; /evidence="ECO:0007829|PDB:4RO1"; STRAND 862..866; /evidence="ECO:0007829|PDB:4RO1"; STRAND 909..912; /evidence="ECO:0007829|PDB:4RO1"; STRAND 917..920; /evidence="ECO:0007829|PDB:4RO1" HELIX 360..363; /evidence="ECO:0007829|PDB:4RO1"; HELIX 395..410; /evidence="ECO:0007829|PDB:4RO1"; HELIX 435..439; /evidence="ECO:0007829|PDB:4RO1"; HELIX 483..485; /evidence="ECO:0007829|PDB:4RO1"; HELIX 492..500; /evidence="ECO:0007829|PDB:4RO1"; HELIX 516..519; /evidence="ECO:0007829|PDB:4RO1"; HELIX 565..573; /evidence="ECO:0007829|PDB:4RO1"; HELIX 577..580; /evidence="ECO:0007829|PDB:4RO1"; HELIX 591..612; /evidence="ECO:0007829|PDB:4RO1"; HELIX 645..665; /evidence="ECO:0007829|PDB:4RO1"; HELIX 687..695; /evidence="ECO:0007829|PDB:4RO1"; HELIX 705..715; /evidence="ECO:0007829|PDB:4RO1"; HELIX 721..734; /evidence="ECO:0007829|PDB:4RO1"; HELIX 743..745; /evidence="ECO:0007829|PDB:4RO1"; HELIX 749..751; /evidence="ECO:0007829|PDB:4RO1"; HELIX 773..783; /evidence="ECO:0007829|PDB:4RO1"; HELIX 794..831; /evidence="ECO:0007829|PDB:4RO1"; HELIX 859..861; /evidence="ECO:0007829|PDB:4RO1" TURN 364..369; /evidence="ECO:0007829|PDB:4RO1"; TURN 420..424; /evidence="ECO:0007829|PDB:4RO1"; TURN 520..523; /evidence="ECO:0007829|PDB:4RO1"; TURN 613..616; /evidence="ECO:0007829|PDB:4RO1"; TURN 666..668; /evidence="ECO:0007829|PDB:4RO1"; TURN 683..686; /evidence="ECO:0007829|PDB:4RO1"; TURN 716..718; /evidence="ECO:0007829|PDB:4RO1"; TURN 755..758; /evidence="ECO:0007829|PDB:4RO1"; TURN 768..770; /evidence="ECO:0007829|PDB:4RO1"; TURN 784..787; /evidence="ECO:0007829|PDB:4RO1" CHAIN 1..927; /note="DIS3-like exonuclease 2"; /id="PRO_0000314756" MDLKPNIRRKEKRNLLKGEAALEKKGSIDRKTKNKAYPSTTHDPHQNDDSNIPGLGSGLLERIKDIVQRPTDTQLKGQDSNHKKASLTETKTEKAKVKPKAKKKNSKEKISKSSKQDEHKTDVHKESVSKLSKNLESRNNRDENSAKREKNNSHQVEADTNNATEMVSSNAKKSVYPLYYDSATVKKGLKSGTLFKGTLRILENHRSAFACMEDIPDFYVDGPIARNRAFHNDVVIVEPVMNNDSPTEKSNFLQNGVEKVKIKDHDDELGGAMEHLERLEIKSVASFKGDSRTRARVVAIEKRAEISKIVGILRAPGWSLKNVEYVSKKSSYAIFIPKDKRLPFITIHKNDLSDLSGENWIENILKHHDQLFSVEITRWSIYSRYPMGVLGEKLGNITDVEAYTNALLLENGISSSPFSDEVLNCLPPDDWIISHEEIKKRRDLRNELIITIDPETARDLDDAVSCRALDNGTYEVGVHIADVTHFVKPDSALDKEAASRATTVYLVQKAIPMLPPLLCERLCSLNPNVERLAFSVFWKLDSNGKEIGKRWFGKTVIKTCARLAYSEAQGVIEGKSWDDAVGKPIGGTHTPKDVETSILTLCEISRKLRKDRFAKGAVEINSTELKFQLDEYGMPNKCEVYEQTDANHLIEEFMLLANRSVAEHISKNFSNNSLLRRHASPKEKQINEFCHFLKSMNFDFDASSSAAFNASMVRLRSTFNEELVELFENMAVRSLNRAEYFCTGDFGEKTDWHHYALSFNHYTHFTSPIRRYPDIIVHRLLERSLKNTSPGIDKKNCSLVAAHCNEKKEKSTTVQEDSQQLFLSVYIAEYCKKHDKKSMPVQAFATRISGNSIDVYISEYGISNRVDLSSDDRIKSFIVAPDDSSVKITLFDDSQKTIALTDRFQVYLYSDYSRTFFSIRCSLVSLN O14050 MSY2_SCHPO SPAC2C4.17c; CHAIN 1..840; /note="Mechanosensitive ion channel protein Msy2"; /id="PRO_0000316597" MNEHRREPHRRSGYQDDSAFTNTEKLVDELDHNVEPEQLLEKNRTDFKLMYVIVKFYRWFNNLSFITRWITIWFPLAGALVIPLAVGVSPYPNAKLGGVRIFWIFVWLEVAWGGFWVSRVIARLLPYILYPLMGILPFTMYKYTVILTALEMPLAIFFCSIVCVCTFSPIMIGKGNFTSTTVTTTTSATATPTASASSNAVESVFVTKTAASVPSWIKVITKILGAAVVTSIVLLLEKIFLHFIGFHYHEVQYQYRITDNKRNTAVLAKLLTAALDAPYHDSPRVRRQDYLLGLIDTRSMSESKGSGNGKLRKVKKISKNAKRIFSKTRNAISTAFTDMLGKHAKDLTPEQEFILETIRSKKKCLALARKIWYSLVPEGEDCFQKEDLIGLIPDDEINDIFHILDNDYSRTVTLDEMEQFTREISIEFRSISSSLRDVDLALGKLDRVGLGVVGIIAVLTFISFLDTSFATILAAFGTTLLSLSFVFSTSAQELMSSIIFLFSKHPFDISDVVIVNNIKYEVVSLSLLFTVFRTMGGSTVQAPNSLLNTLFIENLRRSQPQSETITIVSPFATDFKQLERLRDLLLTFVKENERDFRPIIDLNVSDFSTLDSLKFTVTYYYKSNWQNVSLQCVRRNKFMCALKNAIATTNLPAVADPVRGSPDYPFVIEQYNLERPEYSKTASRPQFSDISSTASSNSLSNKPGFAHSESRNYHTHDEDNSSDDNHKREDRGHLPAQYLRQSVATWQIPNLISAIEAYDSQNESSQENATYTVVESNGNANGDNTATNSQGATDNGQTTTNTTQNNVDNTQATTDNTQANTDNMQVAIDYSQNMDGQIQY O14063 IMA1_SCHPO SPCC962.03c; CHAIN 1..542; /note="Importin subunit alpha-1"; /id="PRO_0000120743" MSASSRFIPEHRRQNYKGKGTFQADELRRRRETQQIEIRKQKREENLNKRRNLVDVQEPAEETIPLEQDKENDLELELQLPDLLKALYSDDIEAQIQATAKFRKALSKETNPPIQKVIDAGVVPRFVEFLSHENNLLKFEASWALTNVASGSSNQTHVVVEANAVPVFVSLLSSSEQDVREQAVWALGNIAGDSPMCRDHVLQCGVLEPLLNIIESNRRLSMLRNSTWTLSNMCRGKNPQPDWNSISQVIPVLSKLIYTLDEDVLVDALWAISYLSDGANEKIQAIIDAGIPRRLVELLMHPSAQVQTPALRSVGNIVTGDDVQTQVIINCGALSALLSLLSSPRDGVRKEACWTISNITAGNSSQIQYVIEANIIPPLIHLLTTADFKIQKEACWAISNATSGGARRPDQIRYLVEQGAIKPLCNLLACQDNKIIQVALDGIENILRVGELDRANNPDKINLYAVYVEDAGGMDLIHECQNSSNSEIYQKAYNIIEKFFGEEDEIEELEPETVGDTFTFGTTQEPAGDFQFSATNAEDMAM O14064 BIR1_SCHPO BINDING 163; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"; BINDING 166; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"; BINDING 183; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"; BINDING 190; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00029" PTM: Phosphorylated by ark1. {ECO:0000269|PubMed:11950927}. SPCC962.02c; CHAIN 1..997; /note="Protein bir1"; /id="PRO_0000122387" MKPITSSSKRRWNRFRREMCNYSKRLDTFQKKKWPRAKPTPETLATVGFYYNPISESNSEERLDNVTCYMCTKSFYDWEDDDDPLKEHITHSPSCPWAYILSSKNNPNQNPQAAALTKCREQTFVDKVWPYTNRPDYHCEPSVMAASGFVYNPTADAKDAAHCLYCDINLHDWEPDDDPYTEHKRRRADCVFFTWKDPNSLSPTKLSFLSTSNIDPEDLTEDNSILPVSPTRDSTKSHKTLNFSPSRKNNLNARPLTMSLYTNTSEEKDSQPTRAPQSPTKPVLLTAPRRKNKSPKKSKPAVFKPVKPIFSDEDEDDDDLTASQPFSKGICNDSMQVAKKNFTEEIPLKEDEKDNELEHLVSPATSVHTTVSDITGHQSVTDESDEQNNCMSTPPKIEIESKIEEEISVVSKSKEISSSVSSVGKEQNHTEKQVAIETPEQQKVEKEDEHLNLQGSFIEESTKQPISSKPSTSSPDMTDAATGGRVSSSSFRDKILQTNFSPRSTIDSFSNISKKRNSEEANDENDETNLKIPIPEKKRKFQEVLQSKNILVSSTEDSHEPVKVTEDSQTAIHVSKFEDLENKSMESEQSLQLLSESENDDKPLIDLIPLLAIKRKDNLVSGVLEKGKSTSTSKTKFDTSIVDFIEKPKTEISEVLPEEKRKAICDESQTVRVSIDRGVTKTRDVSSPVSDEKSENVNHEEANSGHTVMNVHSSLDPQPIVQPNELESGSYLKDLPDRNVGNSEKVTFQEDDINSPKLQSKNNQTVEAVNTETSDKLQEKEANHELENIEKIEEKLTEVDKVSLSDAFPDQEIKNSRTSVQNGTRSVSKNTPEKETKVDKIDNVSKKDVETSPGSCETSSAFAKTYAEKEVTSINLPSVRKPLDESYYDHSISPFDPLCQSSFLAPQTPVKSKHALPLVEANAPPWEPIDFSSLLESPVPNPVEPNKLSEKELDMTVEQWIKFMYAKCAKEFEEACEEKIEWLLEEGKRAEEYIQNL O14072 ATC4_SCHPO ACT_SITE 485; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:P39986" BINDING 485..487; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39986"; BINDING 485; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P39986"; BINDING 487; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P39986"; BINDING 587; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 644; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39986"; BINDING 710; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39986"; BINDING 824..828; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39986"; BINDING 824; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P39986" CATALYTIC ACTIVITY: Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90782, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39986}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39986}; SPACUNK4.07c; CHAIN 1..1211; /note="Endoplasmic reticulum transmembrane helix translocase"; /id="PRO_0000046350" MGSKALITSPDISSGQLYIKLPTFFHLYVWPFALFVYPYIGYVYQNKLYSEEVRYLTYIAVGTIHALFWLAGEWNTKVYCLMTCRKTDKVEQATHILVTPSKIGESSSVEPITKLVLPDSQTIQYSFSFQRKRFIYEPEKGCFANITFPMDEPSTIGTLKKSTGLTNIQSEIFLYRYGKNCFDIPIPTFGTLFKEHAVAPFFVFQIFCCVLWCLDDYWYFSLFSMFMIIALECSVVWQRQRTLTEFRTMSIKPYEIQVYRNKHWFPISTEDLLPNDVVSVLHNKEDSGLPCDLLLLSGSCVVNEAMLSGESTPLVKESIELRPEEAVIDVDELDKNAVLFGGTRVLQVTQSPFCKLKTPDNGVPAIVLRTGFETSQGSLVRTMVFSSEKVTANNRESLYFILFLLVFAIAASGYVWHVGSKTERSRYKLMLDCVMIITSVVPSELPMELSMAVNASLGALSKYYIYCTEPFRIPLSGHLDICCFDKTGTLTEEHMVVQGIAGVNRKDPYSLEKLSDASNDAILAIATAHTLVLLEQEGETPKVVGDPMEKATVENLGWSIEKKNFVSAPEGSVFYKGKVQIIRNFQFSSALKRQSSVSNVRVSGGSFKTFVSVKGAPEVIATMLREVPKDYEKIYKDYGRKGSRVLALGYKYFKNYIPENQVSDLSRESIESDLVFAGFLIFTSPLKEDARQTVQMLNNSSHRCMMITGDNPLTAVYVAEQVGIVEKPTLVLDIKHENEKILEWKSTDDTINLPMNPHKSLEASLYEKYDLCITGRALSQIINPDVIMSIFTHAWVYARVSPSQKEFMISTLKHNGYITLMCGDGTNDVGALKQAHVGVALLNASEEDMLEMQERARNQKLMGVYEKQIQLAKRFNLPTPPVPPALCHAFPPGPNNPHREKTQEGLNKVLEDLETKKASDVQLTEAEKAAERRANLANKMFDTLANASDDEAPKLKLGDASVAAPFTSKLAVVSSITNIVRQGRCTLVALVQMHKILALNCLITAYSLSVLHLDGIKFGDTQYTISGMLMSVCFYCVSRARPLETLSKERPQAGIFNTYIIGSVLGQFAIHIVTLIYITRVVYLYEDPLEKVDLEETFKPSLLNTAIYLLQLIQQVSTFAINYQGRPFREALSENKGMYYGLLGIAFVAIAGVTEFSPELNAKLQLVKMAYNFQIQLLATMVVDYAACWIIEELMKKYFRDNKPKEIVLRN O14079 MDB1_SCHPO MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 283; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPACUNK4.14; STRAND 2..5; /evidence="ECO:0007829|PDB:4S3H"; STRAND 8..11; /evidence="ECO:0007829|PDB:4S3H"; STRAND 14..20; /evidence="ECO:0007829|PDB:4S3H"; STRAND 27..29; /evidence="ECO:0007829|PDB:4S3H"; STRAND 34..41; /evidence="ECO:0007829|PDB:4S3H"; STRAND 44..52; /evidence="ECO:0007829|PDB:4S3H"; STRAND 54..56; /evidence="ECO:0007829|PDB:4S3H"; STRAND 68..73; /evidence="ECO:0007829|PDB:4S3H"; STRAND 80..82; /evidence="ECO:0007829|PDB:4S3H"; STRAND 85..90; /evidence="ECO:0007829|PDB:4S3H"; STRAND 388..393; /evidence="ECO:0007829|PDB:7P0J"; STRAND 421..424; /evidence="ECO:0007829|PDB:7P0J"; STRAND 426..428; /evidence="ECO:0007829|PDB:7P0J"; STRAND 445..447; /evidence="ECO:0007829|PDB:7P0J"; STRAND 494..497; /evidence="ECO:0007829|PDB:7P0J"; STRAND 523..525; /evidence="ECO:0007829|PDB:7P0J"; STRAND 537..539; /evidence="ECO:0007829|PDB:7P0J"; STRAND 542..544; /evidence="ECO:0007829|PDB:7P0J"; STRAND 558..560; /evidence="ECO:0007829|PDB:7P0L" HELIX 398..406; /evidence="ECO:0007829|PDB:7P0J"; HELIX 433..441; /evidence="ECO:0007829|PDB:7P0J"; HELIX 449..457; /evidence="ECO:0007829|PDB:7P0J"; HELIX 463..466; /evidence="ECO:0007829|PDB:7P0J"; HELIX 471..477; /evidence="ECO:0007829|PDB:7P0J"; HELIX 499..504; /evidence="ECO:0007829|PDB:7P0J"; HELIX 508..519; /evidence="ECO:0007829|PDB:7P0J"; HELIX 530..532; /evidence="ECO:0007829|PDB:7P0J"; HELIX 546..553; /evidence="ECO:0007829|PDB:7P0J"; HELIX 563..570; /evidence="ECO:0007829|PDB:7P0J"; HELIX 575..578; /evidence="ECO:0007829|PDB:7P0J" TURN 489..492; /evidence="ECO:0007829|PDB:7P0J"; TURN 505..507; /evidence="ECO:0007829|PDB:7P0J" CHAIN 1..624; /note="DNA damage response protein Mdb1"; /id="PRO_0000116712" MEIQFGNQRCRMVNSGGFLATDGSHLKEMETDDVLVEFLNIEHQLFIRNIRAIVKIADTTVLPSASDKKLLYYVFDETRVRINDTPVIFSKLEEDNANVNEGSKMGVMTVPNTPQKPNLQQQKFEAINANEDQIDYSSNLEQNYNSLIRQGSDQVIPLSRFASEKSALELEKELFSERIPESQSAAEPVLKVENSENDLDEKLVLDGQHVEGDHSSDTEEEVVSEDQKQLNKTDDESTFIESHQIYIQGETKSPSSVSQSLSGDPSLKPAEVFDRKQSAEINSPIEKDVNPQQNISDSSIKNNSIHSDEVNPEVRPDLTPSNENEESKRSAPEIALKEKESTSQDESNREAEEAPISTNYSFPSSSLEDQPDKNVQSSAVENKNKHTNLVTSSFNLTKPMKSFIRRNGLRVQESVTDETDFVILGSPPLRRTHKFLLATSLGIPLVSSQYLTDCIKSGKVLDFRSYKYKDEEAEAKWGFRLDDIHRRTCFNGKRLYITKAIRDSMVGDSIHGLYSILETSGAEIVGDIKRAQEKDTIILAQPDNDQEGRNMSATGLNVYKIELVALSILRDRIDFDEFLIDYDADSPTKVIGKRNVSKASRTGQGRKRSSRSSWNKPSAKEQRT O14089 IMB2_SCHPO SPAC2F3.06c; CHAIN 1..910; /note="Importin subunit beta-2"; /id="PRO_0000120769" MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVSSLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICEDSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVCQALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLLLLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAALDVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLGRYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVLILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNTLYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYCFDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIGRLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKILQGSVELFNGKASWQASPEVLAQIQAQYGV O14092 HEM1_SCHPO ACT_SITE 377; /evidence="ECO:0000250|UniProtKB:P18079" BINDING 152; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 265; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 284; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 317; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 345; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 374; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 406; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 407; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P18079"; BINDING 492; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P18079" CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000250|UniProtKB:P09950}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P09950}; TRANSIT 1..25; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 377; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P18079" SPAC2F3.09; CHAIN 26..558; /note="5-aminolevulinate synthase, mitochondrial"; /id="PRO_0000001243" MERVVKLAAKHCPFVSKADPSALRRMAGAGLIRAGARCPVVRHALPVAAATGADVSRGFKSDSKQMAMEPSLDEIHLKAGVVNTGSRTCRHADAVKAAAEAATTTPVTKKHQMPKHYASDLNGVGPATTPRFDYDTFYREELDKKHRDKSYRYFNNINRLAKEYPLAHLADPNTRVEVWCSNDYLNMGGHKKIREAMHQCIETYGGGAGGTRNIAGHNQHAVRLEKSLADLHQKPAALVFGSCYVANDATLSTLGRKLPNCIFLSDEMNHASMINGIRNSRCEKIIFKHNDLVDLEAKLASLPLNRPKIIAFESVYSMSGNVAPISEICDLAKKYGAITFLDEVHAVGMYGPRGAGVAEETPGLLSRVDIITGTLAKSYGCVGGYIAASSTLVDMIRSLAPGFIFTTSLPPHVMVGALTAVEHLKVSNVEREQQRSAVRRVKQSLSEIGIPVLSNDTHIVPAMVGDAHLAKLASDSLLHDHNIYVQSINFPTVSVGTERLRITPTPAHNTEHYVQSLTNAMNDVWSKFNINRIDGWEKRGIDVGRLCKFPVLPFTTTH O14098 CTK1_SCHPO ACT_SITE 399; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P24941, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 283..291; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P24941, ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 306; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P24941, ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000250|UniProtKB:Q03957}; MOD_RES 56; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 104; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 109; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F3.15; CHAIN 1..593; /note="CTD kinase subunit alpha"; /id="PRO_0000338603" MSYSKSTIYRRQGTEPNSHFRRTVEEKSQLSGTNEESLGGHTLSSNAFKNNSSSISPSSSAKDPREQRKRTFPLNDTHSSRARQHERPFRSRKSRRRKGKKAFSPRPGSPPSPSFYRSGSQKRARNLTTKDYFAKRSESSSSASVSPISPSANRNDSKRQASSFRRSPPSSVHMKPSAFNGRKVSRRPSSSPPPIPSIPHETTSSDTQKKSSVSSGFPENKHGKFHFHIPNERRSRFDQPPSKRMALTSTARESVPAPLPSPPSGPIYTYTYPKPAYEKIDQIGEGTYGKVYKAINTVTGDLVALKRIRLEQEKDGFPITTVREVKILQRLRHKNIVRLLEIMVEKSSVYMVFEYMDHDLTGVLLNSQLHFTPGNIKHLSKQIFEALAYLHHRGVLHRDIKGSNILLNNNGDLKFADFGLARFNTSSKSANYTNRVITLWFRPPELLLGETAYDTAVDIWSAGCIVMELFTGKPFFQGRDEISQLEVIYDMMGTPDVHSWPEVKNLPWYELLKPVEEKKSRFVETFKEILSPAAIDLCQKLLALNPFCRPSAHETLMHEYFTSESPPPEPAVILKNMQGSWHEWESKKRKSKR O14111 PSD3_SCHPO ACT_SITE 769; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03209"; ACT_SITE 825; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03209"; ACT_SITE 912; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03209"; ACT_SITE 912; /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03209" BINDING 343; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 346; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 349; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03209}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03209}. MOD_RES 912; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000255|HAMAP-Rule:MF_03209" SPAC31G5.15; CHAIN 1..967; /note="Phosphatidylserine decarboxylase proenzyme 3"; /id="PRO_0000303954"; CHAIN 1..911; /note="Phosphatidylserine decarboxylase 3 beta chain"; /evidence="ECO:0000305"; /id="PRO_0000416837"; CHAIN 912..967; /note="Phosphatidylserine decarboxylase 3 alpha chain"; /evidence="ECO:0000305"; /id="PRO_0000416838" MPFTKSCRSANTLRKGIKNGKLILKIIVNDIDNVESCLSGDESNDSKKSSASFYMKLKYGSYRALADNILSTDENRKEDIAVFDVPLPNGLQIDTFTLCLYRKSKWKKQIVGEAYIGIQALLLSTNPDETCKYPVISPPSGRNKENQSPSHQICNLSLKWIIYDPEDADADSKTLAKAWLQQIKMNQTSIDPMSNISKSLKELEVDNVESDLEDSSFIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETGLYSFNIETSSPSQDTSSKAEDSPTVQKIADDFSSAVGKDLRTDIIEQIIPLTLCCKHDFSTPRDVKLSFKAMFFPIAALRQKFWRVMLAQYGDIEDGHIGKLGMYAVLDTLGSNIPNSMVDDIYTELSSKNHDDTSDSITVDEAVICLERLVDLVCHQDQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDSRNFPSKLYLVYLSNCPLCLKFKLSKVNQQKATVHLATCASHDWKRVDRLMMTSYVSLNQAQRRWFSKAFAKVVYGSSKVGSTSATTLVQNRQTGQIQEEKMNAYVRIGIRLLYRGIRNRRIEGSKVKKILRSLTLKQGMKYDSPISVKEIKPFIRFFDLNMNEVDMPVGGFKTFNEFFYRKLKPGSRPCAFPDNPDILVSPADSRIVAYECIEKATTYWIKGTEFTVERLLGYSNEAQRFVGGSICISRLAPQDYHRFHSPVNGCIGPITKIEGQYYTVNPMAIRSYLDVFGENVRVLIPIDSNEFGKVMLVAVGAMMVGSTVLTVDEGKIVQRSDELGYFKFGGSTVITLFEPNVTSFDEDLLRNSKTKIETLVKMGERIGQKIDPNKPTDAEDHSKSDS O14113 SDE2_SCHPO PTM: The N-terminal UBL (ubiquitin-like) propeptide is cleaved at Gly-84 by the deubiquitinating enzymes ubp5 and ubp15; the resulting mature sde2 associates with spliceosomes. {ECO:0000269|PubMed:28947618, ECO:0000269|PubMed:36095128}.; PTM: Polyubiquitinated; ubiquitination is partially dependent on ubr11. {ECO:0000269|PubMed:28947618}. SPAC31G5.18c; PROPEP 1..84; /note="UBL"; /evidence="ECO:0000305|PubMed:28947618, ECO:0000305|PubMed:36095128"; /id="PRO_0000457161" CHAIN 85..263; /note="Splicing regulator sde2"; /id="PRO_0000352831" MECKTVFLNGDFLKNSVNVNLNRLATVETLLRHVLGDSYETVLERAYLTHQSRIVHPDIQLCKLEGKSTSAHLNLTLCTRVLGGKGGFGSQLRAAGGRMSKKRNEQENQDSCRDLDGNRLGTIRQAKELSEYLAKKPAETRAKKEAKKQKLNKVLAADSSSSRFDDHEYLEDLEQSVSNVRDAFQNSLLYRRGSTSASSFSSGSNGATTDEPAEKEARNNNSSINSWSRRMQASESSNEAEGEDSESQTSKSLYEWDDPLYGL O14114 ATD2_SCHPO BINDING 309..314; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000269|PubMed:31848341, ECO:0007744|PDB:6JQ0" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31848341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000269|PubMed:31848341}; SPAC31G5.19; CHAIN 1..1190; /note="ATPase histone chaperone abo1"; /id="PRO_0000310281" MKEEASEHGGSADETQELSPVSDSSDEMPNNAKRRRRSQSMIANKRIHQAFQEDEGDEDWEEEEHKPKAKRRYNTRSNESFSEGDDEPFEVSESSALEDELSDSEDSFIRSVRSKPKYKPGTRRSTRLRNRRSQDEEESEEEHRPILRERTSRINYSVPLAFPPVDEMDGDPSSQVNQSRSRKTHSELAITKLLRQQVSSFMPYIDSSGSESESDNTRIKKSSAKTIKALTDPANSGGPPDFGRIREKSDLADSDPLGVDSSLSFESVGGLDNYINQLKEMVMLPLLYPEIFQRFNMQPPRGVLFHGPPGTGKTLMARALAAACSSENKKVSFYMRKGADCLSKWVGEAERQLRLLFEEAKSTQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMESRGQVIIIGATNRPDAVDPALRRPGRFDREFYFPLPDRDARKKIIEIHTRNWDPPVPEWLCSMLAEKSKGYGGADLRALCTEAALNSIKRTYPQLYRSTKRLQIDPKTIKVKVKDFVMSMKRMIPSSERSSISPSKPLSPELKPLLNEAFQDIEKTLQKLMPVASKLNPLEEVMYDDPKENDFEYQQRLETFETLRIYKPRFLICGRKGLGQTALGPAILQQYEGVHVQSFDMSTLLQDSTQSIETSIIHLFLEVRRHTPSIIYIPDIDNWLNVLPLTAITTFSSMLERLDFSDQILFLALSSSPLSELHPQLREWFSSKQSVYSLQYPTRDSIIAFFQPILELIKASPTELPGGIPRKRRVLPELPLAPDPPPFTSQKITLKQTKQADMRLLNKLKIKLNALLGSLRARYRKFKKPLIDFNDIYCVDPETGHSYRSREECHYEFVDDVVKQIGSDQKFSMMSLEEIEKRTWDNCYCTPKQFVHDIKLILRDALQLEDSETIKRAQEMYANVLLGVEDMEDDQFSQRCERMALREAERRKLRHGKLQKHLDETKADMQFTSEKPSVDESITEVDDAIKDGPPVLAETLTNSLMEDVGPENVDMDIEDNEIFTNQSTMSVPSMLVENEESPKPDEYIDQKDKVQSPLLNGKSPVGVPSEAALRVSTDVSTNISSNGRADIPVDTLITSPADVPNNAPTDAHNITSADGHIENIEQEVVFPDLVFDEDRLTPLKQLLIDSTTGFTVDQLLHLHSFLYQIIWNTKSEWNRNSVVDECERAVKEFMINALQ O14122 CUL4_SCHPO PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}. SPAC3A11.08; CHAIN 1..734; /note="Cullin-4"; /id="PRO_0000119810" MPPEAKRIVVKGFDPRKSRQRQETYYVTMIDRLNMALQVVMAGLGLKTGYQELYSGVENLTRADQASRCFNILQHHMSSGIQLLKDSAESFIQLEGTETDTNACTVVVGCWNKWLERVEIVQNIFYYMDKTFLSHHPDYPTIEELSLSLFREKLMAVKNIQIPFLNSLLQSFENLHSSKSTDHAYLQDAMLMLHRTEMYSSVFVPMYLVMLSRFYDTESSQKIQELPLEEYLEYAMSSLEREDAYVEKFDIVRDKKSIRETVQRCLITSHLDTLTKGISQFIEKRDAHSCKLLYALLQFNHETEYLIQPWSDCLVDVGFKLVNDESKDDTLVQELLSFHKFLQVVVDESFLHDETLSYAMRKAFETFINGAKGSQREAPARLIAKYIDYLLRVGEQASGGKPLKEVFSEILDLFRYIASKDIFEAYYKLDIAKRLLLNKSASAQNELMLLDMLKKTCGSQFTHSLEGMFRDVNISKEFTSSFRHSKAAHNLHRDLYVNVLSQAYWPSYPESHIRLPDDMQQDLDCFEKFYLSKQVGKKISWYASLGHCIVKARFPLGNKELSISLFQACVLLQFNNCLGGEGISYQDLKKSTELSDIDLTRTLQSLSCARIRPLVMVPKSKKPSPDTMFYVNEKFTDKLYRVKINQIYLKEERQENSDVQEQVVRDRQFELQASIVRVMKQKEKMKHDDLVQYVINNVKDRGIPLVSDVKTAIEKLLEKEYLEREDNDIYTYVT O14129 RAD55_SCHPO BINDING 51..58; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC3C7.03c; CHAIN 1..350; /note="DNA repair protein rhp55"; /id="PRO_0000122955" MLSSQHRLVTQPAIRAYEAFSAPGFGFNSKLLDDAFGGSGLKRGYISEVCGAPGMGKTSLALQITANALLSGSRVIWVETCQPIPMERLRQLLDNHVPSSQDEEEKCDTDELLNLLDVVYAPNLVNILAFLRNFDQEKHLKEIGLLIIDNLSMPIQLAYPTSPEDYAYLRLRRNTSKKSSLSDSSQKENTLTLNKENEFSSKDDSNFAFHNSSTKTTINRRKKAIGTISSLLSKITSSCYVAIFVTTQMTSKVVSGIGAKLIPLLSTNWLDNLSYRLILYSRHSTEESKDGQSRPSHQLLRYAFMAKQPPAHSAESELAFQLTSTGIQDYQSIPTNSSQRRKRSILECES O14139 HRP3_SCHPO BINDING 400..407; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" MOD_RES 1250; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1285; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G6.01; CHAIN 1..1388; /note="Chromodomain helicase hrp3"; /id="PRO_0000080242" MSTSAIALALSSSKAIEQLDHVQTETPNLKQEMSESPSNSGVASKRKLQSTEWLDPELYGLRRSGRTRSNPGRYVDTDDQEDVFPSKHRKGTRNGSSFSRHRTIRDLDDEAESVTSEESESDDSSYGGTPKKRSRQKKSNTYVQDEIRFSSRNSKGVNYNEDAYFESFEEEEEEEMYEYATEVSEEPEDTRAIDVVLDHRLIEGHDGSTPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIKQVILLDREIREDPTTTREDIEAMDIEKERKRENYEEYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQEREESALSPSRGTNYGNSRPKYRKLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSQISLLNIVVELKKASNHPYLFDGVEESWMQKINSQGRRDEVLKGLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLLSKDTIEEDVLERARRKMILEYAIISLGVTDKQKNSKNDKFSAEELSAILKFGASNMFKAENNQKKLEDMNLDEILEHAEDHDTSNDVGGASMGGEEFLKQFEVTDYKADVSWDDIIPLTEREKFEEEDRLREEEEALKQEIELSSRRGNRPYPSSAVESPSYSGTSERKSKKQMLKDEVLLEKEIRLLYRAMIRYGSLEHRYNDIVKYADLTTQDAHVIKKIAADLVTASRKAVSAAEKDLSNDQSNNKSSRKALLITFKGVKNINAETLVQRLNDLDILYDAMPTSGYSNFQIPMHVRSVHGWSCQWGPREDSMLLSGICKHGFGAWLEIRDDPELKMKDKIFLEDTKQTDNSVPKDKENKEKKVPSAVHLVRRGEYLLSALREHHQNFGIKSSPAISTNGKTQPKKQTANRRQSGKPNVKSAQKIESATRTPSPAISESRKKPSSKDTKIETPSREQSRSQTASPVKSEKDDGNVSLNAEQKARCKELMYPVRKHMKRLRKDSSGLGRAELVKLLTECLTTIGKHIEKTVNDTPSEEKATVRKNLWMFACYFWPKEEVKYTSLISMYEKMK O14140 SEM1_SCHPO SPAC3G6.02; CHAIN 1..71; /note="26S proteasome complex subunit rpn15"; /id="PRO_0000122969" MSRAALPSLENLEDDDEFEDFATENWPMKDTELDTGDDTLWENNWDDEDIGDDDFSVQLQAELKKKGVAAN O14147 CHL1_SCHPO BINDING 44..51; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 255; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074"; BINDING 273; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074"; BINDING 283; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074"; BINDING 319; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.; EC=5.6.2.3; Evidence={ECO:0000250|UniProtKB:Q96FC9}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.3; Evidence={ECO:0000250|UniProtKB:Q96FC9}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P18074}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P18074}; SPAC3G6.11; CHAIN 1..844; /note="ATP-dependent DNA helicase chl1"; /id="PRO_0000351016" MCHSKEVKFKTNFHHPYTPYDIQLEFMRSLYSSISDGKIGIFESPTGTGKSLSLICASLTWLDEHGGVLLEDNEKSNDNKSNTSSKIPDWVLEQDLKIQKDLVKETHARLEQRLEEIRKRNQSRKNQMSNNSTTYHRETKRRNINAEASTSDNCNNSNTSVDPMDEYLVTAEYTMPSTSEQSEDLFNNGYSSKVSELLRKLSPDNEKPPIVQKIYFTSRTHSQLQQLVQEIKKLNNQTFSTPIRVVSLASRKNLCINNEVRKLRPTSALNEKCIELQGSAHKCPFLQDNTQLWDFRDEALAEIMDIEELVELGQRLKVCPYYGTREAVDSAQIVTLPYPLLLQESARNALNLTLKDNICIIDEAHNLIDAICSMHSSSISFRQVCIAETQLQQYFLRFEKRLNGNNRMHIKQLIKVVYNLKSFFLNCLETNTNSKVINVDSLLVSNGADQINLHHLSEYLNVSKLARKVDGYTKYMHSLGTQELESLNDLRSERFSNGNGYEEDPYTPVLMQLESFLLNIANPAPEGKLFYEKQTGDNPYLKYLLLDPSKHVEILTEQCRSVNLAGGTMSPIDDFITLLFSDEQSRILPFSCDHIVPPENITTILVSQGPAGVPFEFTHKRKDDENLLKDLGRTFQNFISIIPDGVVVFFPSFAFLQQAVKVWEMNGITNRLNAKKPLFIESKDFGDNPLDTFEHYKQSVDAGLSGMLFSVIGGRLSEGINFSDKLGRAVMVVGMPFPNSQDVEWQAKVSYVEEKAKEKGINAKQASQEFYENTCMRAVNQSIGRAIRHRDDYASIILLDSRYNRSSIQRKLPNWLSKNIHSSPNFGPAIRQLATFFRAKKMCD O14148 INO80_SCHPO BINDING 867..874; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P53115}; MOD_RES 179; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 518; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29B12.01; CHAIN 1..1604; /note="Chromatin-remodeling ATPase INO80"; /id="PRO_0000350963" MDPSRETFDGSTRDSYKPPNGAEMMGQSELNTQNRIPYNTSANNRNWQIPLYWQQRGNEFQASPPPPLGYVTPEYGATGTPVNANNASRVDYATTAANVPEEYANDYSSELAYIHNVNDMPHVDGLSNHSPATQPDLFETPAQSDPILFSSYPHAAQARVDPSISKDLYNMVPRPDANTVSPHAARSASSLPVPKEASETPFRDASTDLFDEHAHAAPMHSSISISTLLSDSDRYEPHVSLTENISPVMAPSIDARLSQTILRGLPPAQKLSPNSSQSQITHNRRKHKLPLNATTNNSVVLTPDTSPLLDSDEVVSDDDSNEQQTMMMKFNYLQHLRNKRDEAVHAEKRRLLDIRGSIHDRLVCRYENRYNKLHASEYNHHHDWAVRQAIREEVAAVEAAKIRADEEKKKKEREEQVRLLQESADKDAEMNEASTATSENEDLKDDLSLADLSSKKTANSQATENNNTPSKAKVKAESKVRSKAKSDKSRAKLSSDTNKDSEKNDNNDASLQSAGVASDGESSPETPLTKASKSKKAKASKLANDTSKNANGETKSTPKKSKKKTSKAQQEANSTTAEGKEKLSGDSTETGNSTNKEASTEDTKANATASAPNKKKKTVETLQQQVIKEIARKEIPRVYKIIQQNQYNRSTNARKTSQLCGREARRWQFRTIKNNKDMQTKAKRAMRETMVFWKRNERVERDLRKKAEREALDRAKKEEELRESRRQARKLDFLITQTELYSHFVGRKMDREQDLPSATNTASVSEINFDSDEEEDIRRLAVESAQEAVQKAREHSQLFDANRQQSPNNSSSDMNEGEMNFQNPTLVNAFEVKQPKMLMCKLKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSISVMAYLAETHNIWGPFLVIAPASTLHNWQQEITRFVPKLKCIPYWGSTKDRKILRKFWCRKNMTYDENSPFHVVVTSYQLVVLDAQYFQSVKWQYMILDEAQAIKSSSSSRWKSLLAFKCRNRLLLTGTPIQNTMQELWALLHFIMPSLFDSHNEFSEWFSKDIESHAQSNTQLNEQQLKRLHMILKPFMLRRVKKNVQSELGEKIEKEVYCDLTQRQKILYQALRRQISIAELLEKAILGGDDTVASIMNLVMQFRKVCNHPDLFEREDVRSPLSLATWSKSIYINREGNFLDVPYNTRNFITFSIPRLLYEQGGILSVPGLNTSRGFETKYLYNLMNIWNPEYTNDSIKSNPEGSPFSWLRFVDESPQTLFQTFQNPVVHYLDEAEASSSLKEEQLCRQEFCYGKDYSNVRKMLLLPKSITKVDVLGSDFKEDSPFYHLTHVLEESDSQLDLTLLDSVLVQRASAPPIDIYCPGSRQFTVLQSRFQRDHLWSHYLYQPLKGEEDLIINNQAVSKLPIPRKPLLPSFGIAKGSYSNVRIPSMLRFIADSGKLSKLDKLLVELKANDHRVLIYFQMTRMIDLMEEYLTFRQYKYLRLDGSSKISQRRDMVTEWQTRPELFVFLLSTRAGGLGINLTAADTVIFYDSDWNPSIDSQAMDRAHRIGQQKQVTVYRFITRGTIEERIVIRAKEKEEVQKVVISGGETRPTKQMDLKGNSREMVSWLLEE O14156 PP2C4_SCHPO BINDING 92; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 92; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 308; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 347; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; SPAC4A8.03c; CHAIN 1..383; /note="Protein phosphatase 2C homolog 4"; /id="PRO_0000057773" MSIRFLKRLRAPLYIQNAYCSKNYFYRSFIQYYSPSNGPYLKISMNKAPQSLGLCTARGDSPTNQDRMAYGYLNNLKDTTNRDSPFFYGLFDGHGGTECSEFLSTNLGKIIENQDLNDTEKILKEVHSVGGYMAGLKPPFSLRTVLQSRDEDLLWRARLYYSFLQADMDYLTNYARPSPDSAVPGAVGTVAIITSKNNLSYWESDSYIIHLAHVGDTRALLCDSRTGRAHRLTFQHHPADVEEARRLRRYNMGFSRDSFGQKRFAWVANTRSFGDGYKLKKLGVVAEPQLTSIHSLRDDWSFLTLLSDGITDVVSDDEVVDIIKLSESPQDAANNIIRYAQNVGAVDDITCLVVRLPGWKKRTINDFTKNLRLEKSAYHPRRS O14157 MYO3_SCHPO BINDING 182..189; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 1421; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4A8.05c; CHAIN 1..2104; /note="Myosin type-2 heavy chain 2"; /id="PRO_0000123481" MSYLSKNGSNDNNNIIKKLVDAEKHCNAVKDASFDERTWIWIPDSKESFVKAWIVEDLGEKYRVKLERDGSERIVDGFDAEKVNPPKFDMVDDMAALTCLNEPSVVNNLTQRYEKDLIYTYSGLFLVAVNPYCHLPIYGDDVVRKYQSKQFKETKPHIFGTADAAYRSLLERRINQSILVTGESGAGKTETTKKVIQYLTSVTDASTSDSQQLEKKILETNPVLEAFGNAQTVRNNNSSRFGKFIRIEFSNNGSIVGANLDWYLLEKSRVIHPSSNERNYHVFYQLLRGADGSLLESLFLDRYVDHYSYLKNGLKHINGVDDGKEFQKLCFGLRTLGFDNNEIHSLFLIIASILHIGNIEVASDRSGQARFPSLTQIDQLCHLLEIPVDGFVNAALHPKSKAGREWIVTARTREQVVHTLQSLAKGLYERNFAHLVKRLNQTMYYSQSEHDGFIGVLDIAGFEIFTFNSFEQLCINFTNEKLQQFFNHYMFVLEQEEYTQERIEWDFIDYGNDLQPTIDAIEKSEPIGIFSCLDEDCVMPMATDATFTEKLHLLFKGKSDIYRPKKFSSEGFVLKHYAGDVEYDTKDWLEKNKDPLNACLAALMFKSTNSHVSSLFDDYSSNASGRDNIEKKGIFRTVSQRHRRQLSSLMHQLEATQPHFVRCIIPNNLKQPHNLDKSLVLHQLRCNGVLEGIRIAQTGFPNKLFYTEFRARYGILSQSLKRGYVEAKKATITIINELKLPSTVYRLGETKVFFKASVLGSLEDRRNALLRVIFNSFSARIRGFLTRRRLYRFNHRQDAAILLQHNLRQLKLLKPHPWWNLFLHLKPLLGTTQTDEYLRRKDALINNLQNQLESTKEVANELTITKERVLQLTNDLQEEQALAHEKDILVERANSRVEVVHERLSSLENQVTIADEKYEFLYAEKQSIEEDLANKQTEISYLSDLSSTLEKKLSSIKKDEQTISSKYKELEKDYLNIMADYQHSSQHLSNLEKAINEKNLNIRELNEKLMRLDDELLLKQRSYDTKVQELREENASLKDQCRTYESQLASLVSKYSETESELNKKEAELVIFQKEITEYRDQLHKAFQNPEKTHNINDVKSGPLNSDENIYSTSSTTLSILKDVQELKSLHTKEANQLSERIKEISEMLEQSIATEEKLRRKNSELCDIIEALKYQIQDQETEIISLNADNLDLKDTNGVLEKNASDFIDFQGIKSRYEHKISDLLNQLQKERCKVGLLKQKTENRSVTQHTLDGNSPHPSFEEKHSGDPLKRIDGNNDDRKIDNKLLKTISKSLDALQLTVEEELSNLYSLSKDLSFTDISGHIPNSIRKLEKGLSTLSELKERLNASNSDRPSPDIFKDTQAIMNSRKLLSNPNSDAQSGLISSLQKKLYNPESNMEFTGLKPLSPSKISNLPSSQPGSPSKRSGKMEALIRNFDQNSSIPDPFIVNQRNSVLQTEFEKINLKLKEATKSGILDNKDLSKFSELIQSLLKENEELKNLTTSNLGSDDKMLDFAPLLEDVPNNTRNQIKGFVEKAISSKRAIAKLYSASEEKLFSTEKALREITKERDRLLHGLQGPSVPTSPLKAPTASQLIIPNFDGSITNYSGEEETEWLQEEVNIMKIKELTSTVNKYREQLAMVQSLNEHAESSLSKAERSKNYLTGRLQEVEELARGFQTTNADLQNELADAVVKQKEYEVLYVEKSNDYNTLLLQKEKLMKQIDEFHVIRVQDLEEREKKDQLLFQRYQKELNGFKVQLEEEREKNLRIRQDNRHMHAEIGDIRTKFDELVLEKTNLLKENSILQADLQSLSRVNNSSSTAQQNAQSQLLSLTAQLQEVREANQTLRKDQDTLLRENRNLERKLHEVSEQLNKKFDSSARPFDEIEMEKEVLTLKSNLAQKDDLLSSLVERIKQIEMFALKTQKDSNNHREENLQLHRQLGVLQKEKKDLELKLFDLDLKTYPISTSKDVRMLQKQISDLEASFAASDIERIKGIDECRNRDRTIRQLEAQISKFDDDKKRIQSSVSRLEERNAQLRNQLEDVQASETQWKFALRRTEHALQEERERVKSLETDFDKYRSLLEGQRVKRSESRLSMRSNRSPSVLR O14164 EIF3C_SCHPO MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:18257517"; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:18257517"; MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:18257517"; MOD_RES 19; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:18257517"; MOD_RES 20; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:18257517"; MOD_RES 667; /note="Phosphothreonine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:18257517" SPAC4A8.16c; CHAIN 1..918; /note="Eukaryotic translation initiation factor 3 subunit C"; /id="PRO_0000123529" MSRFFKGGSSDSDAESVDSSEENRLTSSRLKKQDDSSSEEESSEEESASSSESESSEEESESEESEVEVPKKKAVAASEDSESDSESSEEEEETESEEDSEVSDESESESESESESEEESESEEESDESERSGPSSFLKKPEKEEAKPAGLKFLRGESSEESSDEEEGRRVVKSAKDKRYEEFISCMETIKNAMSSNNWIVVSNEFDHLNKVSQKCKEAGRNPPPYIEFLSALDQKLESADKAFIKSLDAANGRAFNALKQRVRKNNRQFQSDIDRYRKDPEGFMKPAELNEIPKPAGKAGQDEVIVDGVATRGIVAPTEGLGKPEEITPADIFKYLRAIFEARGKKSTDRSEQIRLLEKLSTIAVTDYQRLRVKVALLAVRFDINTGSGQYMPIDQWNAALTELHSILDIFDANPKIVIVEQVEDENEEEEEAIAAAENNNGVIQVQGSVVSFLERLDDEFTRSLQMIDPHTPEYIDRLKDETSLYTLLVRSQGYLERIGVVENTARLIMRRLDRVYYKPEQVIRANEEVAWRSFPPTFDLTITPRATTTTPDILIHSLCVYLYNNGVSLLRTRAMLCHIYHEALQNRFYKARDMLLMSHLQDSVHAADIATQILHNRTMVQIGLCAFRNGMVQETQYALQDISTTGRVKELLGQGIQAPKFGQFTPDQDRLDKQLVLPFHMHINLELLECVYLTCSMLMEIPAMAAASSTASDSRKRVISRPFRRMLEYIDRQLFVGPPENTREYIMQASKALADGEWRRCEEFIHAIKIWSLMPDADKIKQMLSEKIREEGLRTYLLAYAAFYDSVSLEFLATTFDLPVQRVTVIVSRLLSKREIHAALDQVHGAIIFERVEINKLESLTVSLSEKTAQLNEANEKLYEQKTQHTNPQENRRRDKGGSVKRRNERTENRNRSDMN O14170 POP2_SCHPO SPAC4D7.03; CHAIN 1..703; /note="WD repeat-containing protein pop2"; /id="PRO_0000051140" MSLSRCPTDNSSSRINSSVPLINSSSPATPPESFDPQVFPSSLIHGDNLLPQDDQIASDPRSESNSCNGNTSSSLPCTDSYQYPLKHSCTPSFLRKFNESIENVSYKCLDHSPPDSVPGDFSISLVPQRNFLYSHSSLPPKIISIDRNNRIKLDNSISSNSDNFPPSPKVDTSNTVSPGSKPISEDLEDLNLQSIVQTFEDLPEGIQSYAFFQLLRSCNRQSMRLLLNECEPLLKKDILSNLPFSIVQSILLNLDIHSFLSCRLVSPTWNRILDVHTSYWKHMFSLFGFQINENDWKYANPNLNRPPFLHNDQISDDYFPEIFKRHFLNRKRWLFPSIPPSHLSFPIHVPNFMITSLLLHKDRIITTSGSGTIQIHNAITGVLEARLEGHKEGVWAVKIHENTLVSGSIDKTVRVWNIEKAKCTHIFRGHISIIRCLEILVPSRLIRHGVEIVEPDQPYIVSGSRDHTLRVWKLPKNTDPPYLPDNTNSIDRWEKNPYFVHTLIGHTDSVRTISGYGDILVSGSYDSSIRIWRVSTGECLYHLRGHSLRIYSVLYEPERNICISGSMDKSIRVWDLSTGTCKYVLEGHDAFVTLLNVFQNRLISGSADSTIRIWDLNTGKPLMVLPSNSGYISSFVSDEHKIISGNDGSVKLWDVRTGKLLRFLLTDLTKIWHVDFDAMRCVAAVQRDDQAYLEVINFSGSRP O14174 SPT20_SCHPO SPAC4D7.10c; CHAIN 1..473; /note="SAGA complex subunit spt20"; /id="PRO_0000116700" MERNNGLGDYTYRYHGKELSLDDFQNKQGIESSDDAFLSKIYENVSNFNVPRKLHDIEHKFSKEEPSLILHIHKFHFRFEQQDGAFTYNGPVKSILQYIRMELIPPDCLEVFRNSDVKFYDGCLTVRIIDHRQSPSADQTVQPQPGSTNQQQQNNTNPINNQPEDTKPNTNSPPVYHTVLRPTPETLWQDLCLLSESFANSLSDEAVLTLESNILLASEAPLFLTPAKSKAEMIQFMNQLADSAPPCTRKKPQGSAQLADEEAERLEKENLLLLMDDQRKRDFQPTFQRLQFIENVRRKRAILQQRQMQMQQQQKAQQQQSPKAQQPPAHLVQSAPVQRKTTPKIQRLPPSSIQIPPPKPMQKFPANAASSESPPNATGNFLPSGPVPANEPMLKRESVDLIKIRQLAILFQQRASQLKARGATREQITEILNRQAIAAGTDLATVMTVARNLHFQQLQMRQQQQQQQMKAER O14187 SPP42_SCHPO MOD_RES 2015; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4F8.12c; CHAIN 1..2363; /note="Pre-mRNA-splicing factor spp42"; /id="PRO_0000290646" MASLPPGNPPPPPPPPGFEPPSQPPPPPPPGYVKKRKNKTPAQSGNLEKQLNERARKWRASQKSKFGVKRKQGYVQTEKADLPPEHLRKIMKDRGDMSSRKFRADKRSYLGALKYLPHAVLKLLENMPMPWEEYREVKVLYHVTGAITFVNESPRVIEPHFIAQWGTMWMMMRREKRDRKNFKRLRFPPFDDEEPPFSIDQLLDLEPLEAIRMDLDEEDDAPVMDWFYENKALEDTPHVNGPTYRRWKLNLPQMANLHRLGYQLLSDLRDDNYFYLFNDNSFFTAKALNVAIPGGPKFEPLYKDEAPEMEDWNEFNDIYKLIIRHPIKTEYRIAFPYLYNSRARSVALSEYHQPSNVFVPPEDPDLPAFFWDPIINPITSRQLTLHELDTSPEDSAIEEDPNFEIPFDPFFHSEDIEFEHTASALILLWAPHPFNKRSGATKRAQDVPLIKHWYLEHCPPNQPVKVRVSYQKLLKSHVMNKLHMAHPKSHTNRSLLRQLKNTKFFQSTSIDWVEAGLQVCRQGYNMLQLLIHRKGLTYLHLDYNCNLKPTKTLTTKERKKSRFGNAFHLMREILRLTKLIVDSHVQYRLGNIDAYQLADGLHYIFNHVGQLTGMYRYKYRLMRQIRACKDFKHLIYYRFNTGPVGKGPGCGFWAPSWRVWLFFLRGIVPLLERWLGNLLARQFEGRHSTGVAKQITKQRVDSHQDLELRAAVMNDILDMIPEGIRQGKSKTILQHLSEAWRCWKANIPWKVPGLPAPIENMILRYVKSKADWWTSVAHFNRERIRRGATVDKTVAKKNLGRLTRLWLKAEQERQHNYLKDGPYVTADEAVAIYTTFVHWLESRRFQPIPFPPLSYKHDTKLLVLALERLKEAYSVKGRLNQSQREELALVEQAYDNPHEMLSQIKRRLLTMRTFKEVGIEFMDMYSHLIPVYSVDPMEKICDAYLDQYLWFEADRRHLFPSWVKPSDSEPPPLLVYKWCQGINNLTDVWETSNGECNVLMETRLSKVFEKVDLTLLNRLMSLLMDTNLASYASAKNNVVLSYKDMSHTNSYGLVRGLQFSSFIWQFYGLVLDLLILGLQRATEIAGPADAPNDFLHFKDQATETSHPIRLYTRYIDKVYIMFRFTDEESRDLIQRFLNENPDPTNSNVVNYSKGKKNCWPRDARMRLMKHDVNLGRAVFWEIRNRLPRSLTTLEWEDTFPSVYSKDNPNLLFSMTGFEVRILPKIRQNEEFSLKDGVWNLTDNRTKQRTAQAFIRVTEDGINQFGNRIRQILMSSGSTTFTKIANKWNTALIALMTYYREAAISTPELLDLLVKCESKIQTRVKISLNSKMPSRFPPAVFYSPKELGGLGMLSMGHVLIPQSDLRWSKQTDTGITHFRSGMTTNGEHLIPNLYRYIQPWESEFIDSQRVWAEYAMKRQEALQQNRRLTLEDLEDSWDRGIPRINTLFQKDRHTLAYDKGWRVRTEFKQYQLLKNNPFWWTSQRHDGKLWQLNNYRVDVIQALGGVEGILEHTMFKATGFPSWEGLFWEKASGFEESMKFKKLTNAQRSGLNQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGIMMHGKIPTLKISLIQIFRSHLWQKIHESVVWDLCQVLDQELESLQIETVQKETIHPRKSYKMNSSCADILLLAAYKWNVSRPSLLNDNRDVLDNTTTNKYWIDVQLRFGDYDSHDIERYTRAKFLDYSTDAQSMYPSPTGVLIGIDLCYNMHSAYGNWIPGMKPLIQQSMNKIMKANPALYVLRERIRKGLQLYASEPQEQYLSSSNYAELFSNQIQLFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKVIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPRQIIVTRKGMLDPLEVHLLDFPNITIKGSELQLPFQAIIKLDKINDLILRATEPQMVLFNLYDDWLQSVSSYTAFSRLILILRALNVNTEKTKLILRPDKSIITKENHVWPNLDDQQWLDVEPKLRDLILADYAKKNNINVASLTNSEVRDIILGMTITAPSLQRQQIAEIEKQGRENAQVTAVTTKTTNVHGDEMVVTTTSAYENEKFSSKTEWRNRAISSISLPLRTKNIYVNSDNISETFPYTYILPQNLLRKFVTISDLRTQVAGYMYGKSPSDNPQIKEIRCIALVPQLGSIRNVQLPSKLPHDLQPSILEDLEPLGWIHTQSSELPYLSSVDVTTHAKILSSHPEWDTKAVTLTVSYIPGSISLAAYTVSKEGIEWGSKNMDINSDEAIGYEPSMAEKCQLLLSDRIQGFFLVPEEGVWNYNFNGASFSPKMTYSLKLDVPLPFFALEHRPTHVISYTELETNDRLEEDMPDAFA O14188 IQG1_SCHPO SPAC4F8.13c; STRAND 94..96; /evidence="ECO:0007829|PDB:1P5S" HELIX 33..55; /evidence="ECO:0007829|PDB:1P2X"; HELIX 62..64; /evidence="ECO:0007829|PDB:1P2X"; HELIX 65..68; /evidence="ECO:0007829|PDB:1P2X"; HELIX 73..82; /evidence="ECO:0007829|PDB:1P2X"; HELIX 100..113; /evidence="ECO:0007829|PDB:1P2X"; HELIX 118..120; /evidence="ECO:0007829|PDB:1P2X"; HELIX 124..127; /evidence="ECO:0007829|PDB:1P2X"; HELIX 133..148; /evidence="ECO:0007829|PDB:1P2X"; HELIX 167..179; /evidence="ECO:0007829|PDB:1P2X"; HELIX 187..189; /evidence="ECO:0007829|PDB:1P2X" TURN 69..71; /evidence="ECO:0007829|PDB:1P2X"; TURN 149..151; /evidence="ECO:0007829|PDB:1P2X" CHAIN 1..1489; /note="Ras GTPase-activating-like protein rng2"; /id="PRO_0000056665" MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEFSKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTSGLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSISRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIPLFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLEKLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAILLRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVKNFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKINTLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVIKLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCTIENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETLQSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTVKVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS O14194 GGT2_SCHPO ACT_SITE 420; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 147; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 438; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 440; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 459; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 462; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 490..491; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 512..513; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000305|PubMed:15920625}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}. SPAC56E4.06c; CHAIN 1..419; /note="Glutathione hydrolase 2 heavy chain"; /evidence="ECO:0000250"; /id="PRO_0000247900"; CHAIN 420..611; /note="Glutathione hydrolase 2 light chain"; /evidence="ECO:0000250"; /id="PRO_0000247901" CARBOHYD 138; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 153; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 297; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 396; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSPTDTTPLLYSWDDQSRHQDPDWHKLRNYHGAWYRRISRRRFSQFIFAFGLMTLFVLVYSISSNLHTPTQFTGHKVRGRRGAVASEVPVCSDIGVSMLADGGNAVDAAIASTFCIGVVNFFSSGIGGGGFMLIKHPNETAQSLTFREIAPGNVSKHMFDKNPMLAQVGPLSIAIPGELAGLYEAWKSHGLLDWSKLLEPNVKLAREGFPVTRAMERVLKLPEMAHLLKDPIWQPILMPNGKVLRAGDKMFRPAYAKTLEIIANKGIEPFYRGELTNSMVKFIQDNGGIVTVEDFGNYSTVFADALHTSYRGHDVYTCTLPTSGPALIEGLNILDGYPLNTPSLAFPKRLHLEVEAMKWLSAGRTQFGDPDFLPLDHLDVVSKLLSKEFASQIRNNISLSKTYPWEHYNPSYDLPISHGTTHVSTVDSNNLAVSITSTVNLLFGSQLMDPVTGVVFNDQMDDFSIPGASNAFNLSPSPWNFIEPFKRPQSSSAPTILTDINGDFEMALGASGGSRIVTAVLDSIIKRIDMDYDIESMVASARPHHQLLPDILILESGFSKSVATRMKKYGHKVWRLKQHDTPLSQIQAVTRHHSEYYGMSDPRKYGQAAAY O14213 EPR1_SCHPO MOD_RES 344; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6B12.08; CHAIN 1..380; /note="ER-phagy receptor 1"; /id="PRO_0000278521" MNNPFKDMDCYEILQVNHDSDLQEIKANYRKLALQYHPDRNPGIEDYNEIFSQINAAYNILSNDDKRKWHEKDYLRNQYSVQIEDVLQHLQTIEKIPFESTSAFVERLRQDEKIAGSTDDLPTLGDTTWLWTYAKPIYQKWLRFSTKKSFEWEALYNEEEESDAATRRLMKRQNQRQIQYCIQRYNELVRDLIGKACDLDPRRKNVVKLSDGERYNSLQEASRKQSERDRRQYQETFKNQSIASWTIIDQEETSSDDESLSKEIVNSNPIMCMVCNKNFRSQNQLENHENSKKHKKNLRKMNQEIKKHAKEAQKNAESNKQPEDAPSESPYSNKVSSSDFYTRSFEEIEKTFTFVEISDNEFYTASEDGFLNEDDKLDQD O14214 TRM10_SCHPO ACT_SITE 207; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:24081582" BINDING 183; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:24081582"; BINDING 203; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:24081582"; BINDING 207..211; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:24081582"; BINDING 215; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:24081582"; BINDING 229; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:24081582"; BINDING 241..243; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:24081582" CATALYTIC ACTIVITY: Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221; Evidence={ECO:0000269|PubMed:24081582}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.2 uM for tRNA(Gly) {ECO:0000269|PubMed:24081582}; Note=kcat is 0.16 min(-1) for tRNA(Gly) (m1G9)-methylation. {ECO:0000269|PubMed:24081582}; MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6B12.09; STRAND 96..100; /evidence="ECO:0007829|PDB:4JWH"; STRAND 134..138; /evidence="ECO:0007829|PDB:4JWH"; STRAND 160..164; /evidence="ECO:0007829|PDB:4JWH"; STRAND 180..183; /evidence="ECO:0007829|PDB:4JWH"; STRAND 188..190; /evidence="ECO:0007829|PDB:4JWH"; STRAND 199..203; /evidence="ECO:0007829|PDB:4JWH"; STRAND 225..228; /evidence="ECO:0007829|PDB:4JWH"; STRAND 237..239; /evidence="ECO:0007829|PDB:4JWF" HELIX 104..106; /evidence="ECO:0007829|PDB:4JWH"; HELIX 109..128; /evidence="ECO:0007829|PDB:4JWH"; HELIX 142..152; /evidence="ECO:0007829|PDB:4JWH"; HELIX 155..158; /evidence="ECO:0007829|PDB:4JWH"; HELIX 169..172; /evidence="ECO:0007829|PDB:4JWH"; HELIX 174..179; /evidence="ECO:0007829|PDB:4JWH"; HELIX 208..210; /evidence="ECO:0007829|PDB:4JWG"; HELIX 214..222; /evidence="ECO:0007829|PDB:4JWH"; HELIX 245..258; /evidence="ECO:0007829|PDB:4JWH"; HELIX 261..268; /evidence="ECO:0007829|PDB:4JWH" TURN 232..234; /evidence="ECO:0007829|PDB:4JWH" CHAIN 1..304; /note="tRNA (guanine(9)-N1)-methyltransferase"; /id="PRO_0000060518" MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN O14215 PRI1_SCHPO ACT_SITE 66; /evidence="ECO:0000255"; ACT_SITE 131; /evidence="ECO:0000255"; ACT_SITE 133; /evidence="ECO:0000255" BINDING 131..133; /ligand="a ribonucleoside 5'-triphosphate"; /ligand_id="ChEBI:CHEBI:61557"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 131; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 131; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 131; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 131; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 133; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 133; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 133; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 133; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 143; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 144; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 150; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 153; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 182..188; /ligand="a ribonucleoside 5'-triphosphate"; /ligand_id="ChEBI:CHEBI:61557"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 333; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 333; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P49642"; BINDING 342..345; /ligand="a ribonucleoside 5'-triphosphate"; /ligand_id="ChEBI:CHEBI:61557"; /evidence="ECO:0000250|UniProtKB:P49642" CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.102; Evidence={ECO:0000250|UniProtKB:P49642}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49642}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P49642}; SPAC6B12.10c; CHAIN 1..454; /note="DNA primase small subunit"; /id="PRO_0000046735" MTVQIDELDDKDLDEIIANGTLDGAKQGAVDSETMIQYYRHLFPWKYLFQWLNHGPVVTNDFAHREFAFTLPNDAYIRYLSFSNWEELKKEALNLCPSRFEVGPVYSANPRDRKTIRKSTFHPLKKELVFDIDMTDYDDVRTCCSKTNICEKCWPFITIAVQVLDICFHEDFGFKHILWVYSGRRGIHAWICDEIACSLDDRSRRMIASYLQVVVGNPQGGVRLINNLKRPLHPHLTRSLNILKSAFVKIVLEDQDPWASKEGAENLLKLLPDKDLASALRKKWEVDPERSSKNKWSDIDTVLASGSIASISPSVIAIAKQDIVLTYLYPRLDVEVSRHLNHLLKSPFCVHPGTSRVCVPIDIERMDSFNPLKVPTVNDLLQELDKNSQNDNGHGPTMETNTTENQKDNARGQSNKGHGFSTSLNPYTLYFKSFSSQLFKETVGNKRKHENLEF O14216 SLD2_SCHPO PTM: Phosphorylated by cdc2 at the onset of S-phase. {ECO:0000269|PubMed:11937031, ECO:0000269|PubMed:18257517}. MOD_RES 60; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:11937031"; MOD_RES 74; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:11937031"; MOD_RES 87; /note="Phosphoserine; by cdc2"; /evidence="ECO:0000269|PubMed:11937031"; MOD_RES 99; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:11937031"; MOD_RES 154; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:11937031"; MOD_RES 183; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6B12.11; CHAIN 1..337; /note="DNA replication regulator sld2"; /id="PRO_0000116666" MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQNYSSYKLKKRKFRRHRS O14222 FSV1_SCHPO SPAC6F12.03c; CHAIN 1..247; /note="Syntaxin-like protein fsv1"; /id="PRO_0000210268" MSNLLLIIDSVSQKIRDRRKLEEFGQNPDEEIESSLKDVRQELQKLNEEQSRLEKNAQIPEYRVRESEAFLIRMQRRLESAEEEFEKQRRASSIPADGTSAFSANPQVASTNNKLTPLPSLQKTTSSSEGSDIEMEAMYPVDGNDPDPINVNVLAQMHQQMLNEQEESLGGIEASVQRQKRMGYAMNTELSEQNVLLDNMNNDADRIERRFDHAKNRLNKVSRKAKQYPRCFIILLLCALLLLVASI O14227 RDP1_SCHPO CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; SPAC6F12.09; CHAIN 1..1215; /note="RNA-dependent RNA polymerase 1"; /id="PRO_0000097211" MAVSLNDFISVKLKRYSRESPWERLRVPYRNKKQKKWASVHNNEAQLHSANKRNDNCLIQRSSTWRLGDMITLVIKDIPVTWLSNEGGKLYNLWEPLHDYGTIEFMKINEPLNGQTSTTAIVQFAPPPKVPFWEPNGKINVKGVDLAVQIDITAHRSHISRQVFSKNSFRSDQLVKIPLSSFKLGQVYDERIVPLFGVDCGITVTESNLLVYFNFKKLCVLFDASFDKQIETFRLDFDFHSIIGDVGTDYYDDHISLVFRFRFSPLIFRKSKNATESRVQTFWTASHLWRRHYDILPFNVSPTTASPIELLNCHNAPIGRCNVLVLSFSIRDESDKDDIAFLLHNLEKFNLKSQLDKVVFHLVPDYKHRCSLINDKEIEEEIAYLLQACLSKNLLSEIDLPIILANLKKLSKERAKKFLRLILTSKTALINPSELDFTKSFVFYDLSSASSIHIKKLYVTPTTLRIVEDSLEAGNRVIRNFKDFANRFMRVQITDEYYKQKIRGGSDGFRNEKLYSRIQQLLTYGIKVGNQIYEFLAFGNSQLREHGAYFFASGSDLNAKQIREWMGDFSEINSVSKYAARMGQCFSTTKEINRFCVDISLQDDIVRNNHCFTDGVGMASLSVIRRLSLEVKNHDMFPSAFQFRMGGYKGVLSLAPPTKLEYHQGNLVFPRRSQDKFKSFHSTLEVIKISRFSNAHLNMQLITLLEGLGVEKTVFLELTRSQLSKMNESINSKQKSILMLRDNVDEYHSTLIIADFIQAGFLERDDAFTENLLNLYYEWVLRLIKEKQKVSVPKGAYLLGVADETGTLKGHYDDAVLSVPEIFIQITDTSTSFGSYSTGKLKTRVIVGLCIVARNPSLHPGDVRVCKAVRCDELMHLKNVIVFPTTGDRSIPAMCSGGDLDGDEYTVIWDQRLLPKIVNYPPLLESSPKKSIDFLEGKPLIDSVKEFFVNYIKYDSLGLISNAWKAWAHDHDNNPEGIFGNVCLELAEMHSKAVDFAKSGVACKMQAKYHPKRYPDFMQKTKTRSFRSETAVGKIFRYAARFQRESGRPATYNPIMNTVYDPCMKLPRFKTEYLNVAEEVKKHYDNDLRSIMARFDISTEYEVYTAFILFKDDLAKTVNEYGLREEVSFQFDLLKKKYTQEYLEKCALSNQSAFDSSEYEERINSAVAATYDVTYDQRVKSVGNGTTEVLISFPYLFSSRLCQLSRKAMLTANNF O14230 ERG20_SCHPO BINDING 50; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 53; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 88; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 95; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 95; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 99; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 99; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 104; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 105; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 192; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 193; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 232; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 249; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 258; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250|UniProtKB:Q12051" CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000305|PubMed:17596513}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409; Evidence={ECO:0000305|PubMed:17596513}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000305|PubMed:17596513}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362; Evidence={ECO:0000305|PubMed:17596513}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; SPAC6F12.13c; CHAIN 1..347; /note="Farnesyl pyrophosphate synthase"; /id="PRO_0000123951" MSAVDKRAKFESALPVFVDEIVNYLKTINIPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEILLGHPLDEAAYMKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMPGVGNIAINDAFMVESAIYFLLKKHFRQESCYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLSKFSLQKHSFIVIYKTAFYSFYLPVALAMHLAGVATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKIGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEKRVKAVFEELNIRGEFENYEESEVSEIKKLIDGVDESTGLKKSIFTTFLGKIYKRNK O14232 MTR4_SCHPO BINDING 220..227; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPAC6F12.16c; CHAIN 1..1117; /note="ATP-dependent RNA helicase mtr4"; /id="PRO_0000102098" MFGGELDDAFGVFEGKVPKSLKEESKNSQNSQNSQKIKRTLTDKNASNQEQGTKKLESSVGEQESATKRAKIENLKDNQDLIPNNDVNGIHINNSAVADTKHKPKIGDIAADDISNEVSIKNEGDTIPEATVADSFEQEASLQVAGKVGMTEAKSSTEEVVELRHQVRHQVSIPPNYDYVPISKHKSPIPPARTYPFTLDPFQAVSIACIERQESVLVSAHTSAGKTVVAEYAVAQSLRDKQRVIYTSPIKALSNQKYRELLAEFGDVGLMTGDVTINPDATCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDKERGVVWEETIILLPDKSHFVFLSATIPNAMQFAEWITKIHRQPCHVVYTDFRPTPLQHYLFPSGSDGIHLVVDEKSNFREENFQRAMSALMEKQGDDPAAMATKGNAKKGKTGKGGVKGPSDIYKIVKMIMVKNYNPVIVFSFSKRECEALALQMSKLDMNDQTERDLVTTIFNNAVNQLSEKDRELPQIEHILPLLRRGIGIHHSGLLPILKEVIEILFQEGLLKVLFATETFSIGLNMPAKTVVFTNVRKFDGKTFRWISGGEYIQMSGRAGRRGLDDRGIVILMIDEKMDPPVAKSMLKGEADRLDSAFHLSYNMILNLLRVEGISPEFMLERCFFQFQNSLEVPKLEAKLEESQQHYDSFTILDERPLEEYHTLKTQLERYRTDVRTVVNHPNFCLSFLQGGRLVRVKVGNEDFDWGVVVNVSKRPLPKGQSNEYLPQESYIVHTLVMVASDTGPLRIRSGHLPEVHPPAAEDKGKFEVVPFLLSSLDGIAHIRVFLPNDLKSQGQKLTVGKALSEVKRRFPEGITLLDPVENMNIKEPTFIKLMKKVNILESRLLSNPLHNFSELEEKYAEYLRKLALLEEVKDLKKKLSKARSIMQLDELNSRKRVLRRLGFTTSDDVIEVKGRVACEISSGDGLLLTELIFNGMFNDLTPEQCAALLSCLVFQEKSEVENQRMKEELAGPLKILQEMARRIAKVSKESKQELNEEEYVNSFKPSLMEVVYAWAHGASFAQICKMTDVYEGSLIRMFRRLEELIRQMVDAAKVIGNTSLQQKMEDTIACIHRDIVFSASLYL O14243 SNX4_SCHPO BINDING 60; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250|UniProtKB:Q3UR97"; BINDING 62; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250|UniProtKB:Q96L94"; BINDING 86; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250|UniProtKB:Q96L94"; BINDING 105; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250|UniProtKB:Q6P4T1" MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6F6.12; CHAIN 1..401; /note="Sorting nexin-4"; /id="PRO_0000213817" MSDSVNLDEPSTNSTHFLQCLVTEPRKELQGSRDTHVSYLIITKTNLSIFTRAECKVRRRFSDFVKLQEILSRMNEDCVVPPLPAKHKLEYIKGGRFSDNFINRRAKLLNRYITRCALHPVLHQSPHFIAFLENPNWNNYVRFFIQPKLNNTSKLDEISDSLLNAFSKLKEEPTEFDIQRDHVQQFMFGISNLEGSIQKLLRLEKALESDYEDVSIQFDRLASLDQALDVPIESIQNALQQTGTEYANLTEKLTLLLDTIKDVESYAHSLKELLKRRDQKQQDVEALQEYSAKLSLERDKISSGGSNGFSLSKTLDDLRGIDHNDTRLKRLEHVQSELQAVEQAIQEASAVHDAFNQRVREESKLFDSVRQSEMLSAISDYANVHVEFFTNIRDLWIRVKQ O14246 TPZ1_SCHPO SPAC6F6.16c; HELIX 188..190; /evidence="ECO:0007829|PDB:7CUI"; HELIX 196..198; /evidence="ECO:0007829|PDB:7CUI"; HELIX 202..211; /evidence="ECO:0007829|PDB:7CUI"; HELIX 441..465; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 480..484; /evidence="ECO:0007829|PDB:5WE0"; HELIX 490..505; /evidence="ECO:0007829|PDB:5WE0" CHAIN 1..508; /note="Protection of telomeres protein tpz1"; /id="PRO_0000304008" MSNCLKHPWLENGLLNLIKNADVLPIRVFKCQPLQIFEYIRYEHPIRCKLSDTEFYIEAEFSSQSISDLNNFTEKRITSLRGGIVTLGNFLIHLIPSQSGIIPWIQVESFNFQGCEGAVFGNPKAITTSALFNALLQSPYLAALANEFNRSIKEGSSYQEASLSQQEKPNDNTSNSRDIKNNIQFHWKNMTSLSIEECIIPKGQQLILEKESEENTTHGIYLEERKMAQGLHNSVSETPEVKQEDNDEDLDAYSWSSSTDSAGEIPSLPTNRKILEKIAEKPPPFESPLEDDETPDQTNEHEANQVNVSQLPLNPRGSGISGRPVESTEQLNSSLTIERSQSIQSTDSKQRVETQSHRRSKIEIFDAQDELFDRSICTTIDDSTGKLLNAEETPIKTGDLHSTSASSVISCTPPAINFTSDICNEQIELEYKRKPIPDYDFMKGLETTLQELYVEHQSKKRRLELFQLTNNHQKNSEACEMCRLGLPHGSFFELLRDWKKIEEFRNKS O14261 ATG11_SCHPO MOD_RES 548; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 550; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 552; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC7D4.04; CHAIN 1..926; /note="Taz1-interacting factor 1"; /id="PRO_0000072418" MRFRLNDSFSGKSWTIDNVQWTPQNLVAWIMELNIGLSDEAKLLLPNGMSLNETVLNSESDVVIYVLDQNLLTFTYDGDKIPSIPSLKGQPISNVLTGIIADSSSDQWKDKISKCLSLLSDILESSSKIHNQLSVCHDEYSTSIVSPEVAMNYLQRRQSGMKDLLFVFYERLDRVSVSDLLHDFLALPTGSLPITPLKILSTNWTKLDSWLNSISARYAEAQKRVQQCIGAANSIIVSPFKEVPSIKEGDDAYYHLRSVAQDAANILQEILKIESTSTTSQIKPKCNYETEITDCMEKLQSNLSELKSSRKSSLISLKSFWLSFYKVSLRYDALYEYLRQIAEELDRSKFVLSQSRNIFSLYIDILMEALRRTEWQESYNVSHDSSLPLDQEKELSLRKSWLSHFSNLLFNHGQLKYLPVLTRDEISNYLLNIQAHPNYQTFHQMLSNRLSEYLGFPGSPREAVSNTVQANNSLHEKLAMYQNRCNNLEAMLSHQNGFNYNINNDGLSPNAPHPPINEQSNSSQPFYRVSPSIVPLNVIRKLTNRKTSFTDSHILRLQDEVNQLRNELDLVNKRNEDLLIELQGKEEKIQYLETENEEVLQKYENLQEELSSTRKLLTKNEAAVAEQQSNEEMHSNEPNILNLYSVFEGKVDSLQELYNAFKLQLTSLKQKGEYATLAKDAEAVQHIIEERDYALAEKADLLKLSENRKEQCKILTQKLYTIVFRCNELQSVLRECVTQPGFDSDNERDGHASIPDRQIEFNSKDLQYLYWMDGEDADRNFQEFLNRMSSLDFDSFHNFVVSVLTQAHNHELRWKREFQSNRDKALKAILDSQSKVSLRNFKQGSLVLFLPTRRTAGNKKVWAAFNVNAPHYYLNTQPHLKLESRDWMLGRVTSIEDRTADDSTDKWLRLPSGTIWHLVEAIDERF O14283 PRR1_SCHPO MOD_RES 221; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 418; /note="4-aspartylphosphate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00169" SPAC8C9.14; CHAIN 1..539; /note="Transcription factor prr1"; /id="PRO_0000124594" MPSSNGSSDFVRKLFNMLEEPEYRHILRWSDSGDSFIVLDTNEFTKTILPRHFKHSNFASFVRQLNKYDFHKVRHEEGAPSIYGEGAWEFRHDDFQLHHKDLLDNIKRKAPSKRNLANENTAPVIENLKQQVDSILDFQKLLDRNLSGLATSYQTILLKMFELKRGIESRDLLMSSIISYLCDLEGSTQRQANPGAMFVPSHPLQELLNAYQALAKGQVATTSPQQIPNQIQQASAATTASSKMTVDTNLGTAQPSLYNTPSSDYELANQEKPADSMASAASLNTPLSSNDHSLNPHAHGSYPMYEKFQPIQHPNPGSFTTHLDSNASMAKSFSQISNDSLAKASSVATSMSQMGAAVPTTGLWKRQPRILLVEDDELSRRMTIKFLTSFDCQVDVAVDGIGAVNKANAGGFDLILMDFILPNLDGLSVTCLIRQYDHNTPILAITSNISMNDAVTYFNHGVTDLLVKPFTKLTLLQLLKKQLLNLLQADNSINMSDVPSTKEAKDDKAPVTFYLENDAPMYPQQMLQDPIQADLQHPH O14285 SPC34_SCHPO SPAC8C9.17c; CHAIN 1..164; /note="DASH complex subunit spc34"; /id="PRO_0000211553" MSDLLNYLQSIAATSEKLLEPENPNAARFTDAVLHTHAITDLIRDTQKEELIAAEFKSLPKDWSERLASENPADYVACIEELLDIYPMQGGREYLETLVEKYNLHMSGIENLENVLLEQKEQLQQLEKRQTDQVSARENILQRETSEIQRLEREIEKVKQLIQS O14286 ATM1_SCHPO BINDING 288..292; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:P40416"; BINDING 351..354; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:P40416"; BINDING 401; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:P40416"; BINDING 452; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9NP58"; BINDING 476..487; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC15A10.01; CHAIN 29..693; /note="Iron-sulfur clusters transporter atm1, mitochondrial"; /id="PRO_0000093469" MLERCPWKLISSPRNIPARSFLNSRGTYLVLRKSNILPLQHILRFSNFASKQCFPLRNGNNSASKALWNNKSKEKEPLNTSVKLASDVPDDKNVTGQMIVKDMLQYIWPKGKTNLKVRVVSALALLVAAKILNVQVPFYFKSIIDTMNTTLVQEVGALWSTVGAVVLGYGFARIFSTVFQELRNSVFAIVSQSAIRSVSSNVYQHLLNLDMNFHLSKQTGSITRAMDRGTKGISFILSSMVLHIIPITLEIAMVSGILTYKYGPSFSAIAATTVALYALFTVRTTSWRTVFRRQANAADSKASAAAIESLINYEAVKTFNNESYEMSRYEKHLSAYEKANVKVASSLAFLNSGQAIIFSTALTLMMYMGCRGIVTSNLTVGDLVMINQLVFQLSIPLNFLGSVYREMRQAFTDMEQLFSLKRINIQVKEAPDARDLVLKGGSIQFDNVHFSYNPNRPILNGCSFNIPAGAKVAFVGASGCGKSTILRLLFRFYDTDSGKILIDNQRLDQITLNSLRKAIGVVPQDTPLFNDTILYNIGYGNPKASNDEIVEAAKKAKIHDIIESFPEGYQTKVGERGLMISGGEKQRLAVSRLLLKNPEILFFDEATSALDTNTERALLRNINDLIKGSHKTSVFIAHRLRTIKDCDIIFVLEKGRVVEQGSHEQLMAKNSVYTSMWHSQESPFGESNKSGDA O14295 PLR1_SCHPO ACT_SITE 52; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal; Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65; Evidence={ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 mM for pyridoxal {ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982}; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10438489}. MOD_RES 292; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9E9.11; CHAIN 1..333; /note="Pyridoxal reductase"; /id="PRO_0000124683" MPIVSGFKVGPIGFGLMGLTWKPKQTPDEEAFEVMNYALSQGSNYWDAGEFYGVDPPTSNLDLLARYFEKYPENANKVFLSVKGGLDFKTLVPDGNPDFVSKSVENVIAHLRGTKKLDLFQCARVDPNVPIETTMKTLKGFVDSGKISCVGLSEVSAETIKRAHAVVPIAAVEVEYSLFSRDIETNGIMDICRKLSIPIIAYSPFCRGLLTGRIKTVEDLKEFAKSFPFLEYLDRFSPDVFAKNLPFLQAVEQLAKKFGMTMPEFSLLFIMASGNGLVIPIPGSTSVSRTKSNLNALNKSLSPEQFKEAKEVLSKYPIYGLRYNEQLAGTLSV O14299 WIS4_SCHPO ACT_SITE 1161; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 1043..1051; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 1066; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; SPAC9G1.02; CHAIN 1..1401; /note="MAP kinase kinase kinase wis4"; /id="PRO_0000086818" MGLEHTFYPAEDRFEPLLEHSEPVNFVPKENAKSYVRQGFASPHQSLMDNLVDSTESTKRSENFVSHIPLTPSHSGQSEKLMSTRTSHSPYISPTMSYTNHSPANLTRNSSFNHQHYSTTLRSPPSMRGRGIDVNSSHYPHISRPRTSSDSQKMYTRAPVDYYYIQENPYFNNIDQDSISDKSLPSTNQSLHHSEEDTESDNDFSESIHPEFDIDVFYKVSNILYDESDLQDPEKRERLEWHSMLSSVLKGDVMQTEKRRLRLTEPDGHSGTYISEVWLGLQAWLHGRLNADQAEVIRKSREGVEPVLREVIDFQIQDEETTKPPLEQVTEILEKVEQCKQFYISSREMEENVPLSASKEFNYKLNALISWSNVMESIQVETLVLQKWVGNDEFDLTMRTPQFNYDGVENTSSFVERIFRQSGLQRTFEQRTLTTLNRIIHQAKQTISENAQAFEEMKLPTYEDKLLPLVRFPIKLLEEALRLRLAYAKKIKGPNFLIVDSMLDDFKIALSVAVRIKREYIKIASPSPGWSLPTNVDEDYDNVLLDSLKFYFKLLTLKLSSGNKNLYFKEIDFLENEWAFLNEHIYWINGGDIHMAGQFSYLSNSLLLNVHRYVESHLNGPTERTAASLTNWYSTLLKNTQIRFRKILRFSETLNSRFENASDFVISEGHLPDLVNRLSTTGHFLAYTANLERDGVFVIADHTLSENPEALKALLFSKDISNLETIQQNCSYVLILCPVHPIVWKGRIEKVDVPDFSVDLKTNRVRIIASNKREHLQAAKSVFQSISGDLVTLAVECRSSITRVYKEFIRLSKLCMRISSTVVDCVSAVREACSGVNCHDLIYHVFSFAAEFGQRILRFLSFDSYWQTKLKRKITSLAVEWISFICDECDLMDRKTFRWGVGALEFLMLMIRGNNILLIDDAMFLKIREKVGKSMAFLLTHFDVLGAKSKVAAKLQRESTEVSSSPRLTSFGDVEEEALSIQLLQKETMLRIDELEIERNNTLLERLAIGHVLDDSVFRNRDFIKLASSFSNITIRWQQGHFVRSGMFGDVYTGVNMETGDLLAVKEIKLQDSRTFRSTVDQIHNEMTVLERLNHPNVVTYYGVEVHREKVYIFMEFCQGGSLADLLAHGRIEDENVLKVYVVQLLEGLAYIHSQHILHRDIKPANILLDHRGMIKYSDFGSALYVSPPTDPEVRYEDIQPELQHLAGTPMYMAPEIILGTKKGDFGAMDIWSLGCVILEMMTGSTPWSEMDNEWAIMYHVAAMHTPSIPQNEKISSLARDFIEQCFERDPEQRPRAVDLLTHPWITDFRKKTIITMPPATITKKTSLSHTITEEKTAQLLAGRHDDSKAETDSLAASYKEESALPVASNVGLRQPNELRIDSINLPPAIVTPDTINYSVD O14302 CYK3_SCHPO MOD_RES 213; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9G1.06c; CHAIN 1..886; /note="cytokinesis protein 3"; /id="PRO_0000116705" MSIPKQLPCMVRALYAWPGEREGDLKFTEGDLIECLSIGDGKWWIGRHINTNTQGIFPSNFVHCLDIPTVRPGSSMSRTSASSFRYSSPQKSSIDTPITSSDQGLTPDLVGSSNALNKPTRESDSLKHQKSHPMLNSLGSSLSLKKSVSRPPSSMSRTNLDVSSRWDNTADNDSQIDAQDLSRSTPSPLRSAMENVLQSLNAMGKKSFSRANSPLLRLTKSTTTSKETDFIPVPPAHGSTSMTSRSKLDDSTDNSSKPRTSLQPGESPMKSSRDISRKPSMASSVLSPSDYFPQHRRFQSAPAPIPRPVSTLIPLTQVRTTASNVIKPRPQTTERPSTAQSFRKGGGFLKKTFKKLLRRGSSKRKPSLQPTPPVSYPAHNVPQKGVRPASPHTLKSVKDDLKRTKTYTKAEFAAKREEIFNKLSMPVYEPLKDLSECIGNVLADGEPVQFSVGTNIHNMNFSAIDKQIRSIIPQRVQVSPAVLAKNYLAPGQTTALAQMRAVFIYISERITFTNQTLDNDELRTSTQVISEGQGTPFEVALLVKEMLQALDLWCEVIEGYLKSPDDIYYTRDININHAWNVVTFDNEVRLIDASFASPTHPQQALKSSSSNDFYFLMKPNECIFTHVPENPDQQFIMPDLSMPIVMALPWVSSVYFTLGLKLRKFNTSILHLNDLEVLQIEFLAPKDIECVAEVDALSALAPTADVSQCYKYTLTQAFWETPDIRVMRVKAVMPANNRAAVLRIYAGRLGVSSPVRTAPHPMAMSLPFVHHGKNKALEFVTRHPVPHCPSVDLYINSPQCGTLHSGVEYKFNVSAYACQPSTSISNTRLAIQTPTGNIVRLREERSGNGVIFFSLSLTINETGEYRALILAEKIGRWVVYATWQAV O14305 SID1_SCHPO ACT_SITE 129; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" BINDING 15..23; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 38; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC9G1.09; CHAIN 1..471; /note="Serine/threonine-protein kinase sid1"; /id="PRO_0000086653" MYPLNANSYTLLRKLGSGSFGVVWKARENVSGDIIAIKQIDLETGIDDITDIEQEVFMLSNCNSSNVIQYYGCFVDGYTLWILMEHMDGGSVSGLLKMGRLNEQVISIILREVLYGLNYLHGQNKIHRDIKAANILLSSSTGNVKLADFGVAAQLSNAASRRHTFVGTPFWMAPEVIQQTSYGLAADIWSLGITAIEMANGIPPRATMHPMRVIFEIPQSEPPKLDDHFSPTFRDFVSCCLDLNPNMRWSAKELLQHPFIKSAGTVKDIIPLLVQKENKLFDDSDQSVLEETINNTLKPFEEPIAEGNADIEDWTFETVKKSDSTVLGNTSIPKNSIISSQNKEELPSSIKYLEKTIMSDQATPHPFSKSLSEKGSSYHKSLTSDFAMKHYIKSTIRSMLLNDKLSATQRSSLESFYTSFISLDKNLSSKFVNQITPDNRLHHKKQKRSPISQLLFSRWLEETEKRRSLNG O14310 NP106_SCHPO MOD_RES 217; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 221; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 237; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1739.14; CHAIN 1..933; /note="Nucleoporin npp106"; /id="PRO_0000124786" MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLAESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEFMEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTTNIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSSSAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLMRSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHRVSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFERAISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPAYQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGDYDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVVKVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYRTISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL O14313 PMP20_SCHPO ACT_SITE 43; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000250|UniProtKB:P38013" SPCC330.06c; CHAIN 1..156; /note="Peroxisomal membrane associated protein 20"; /id="PRO_0000056609" DISULFID 43; /note="Interchain; in linked form"; /evidence="ECO:0000269|PubMed:20356456" MVAVGSTLPKVTLWENKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQVPGYIANEKQFAAKGISGIYVVAVNDVFVTKAWKKSFDGGEQSGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLSSL O14327 PAB2_SCHPO SPBC16E9.12c; CHAIN 1..166; /note="Polyadenylate-binding protein 2"; /id="PRO_0000081721" MSDQDALDTQEKELLEMKERVAEMEAEAAKLRAMQEQLDNETEALRNDKESIDAQSVYVGNVDYSVTPEELQSHFASCGSVNRVTILCDKFTGHPKGFAYIEFSEPSLVPNALLLNGSMLHERPLKVTPKRTNVPGMSRGRGRGRGRGRGRGRGGYRGRARGFAPY O14333 PSD1_SCHPO ACT_SITE 157; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; ACT_SITE 287; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; ACT_SITE 401; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; ACT_SITE 401; /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208}; TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208" PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208}. MOD_RES 401; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208" SPBC16E9.18; CHAIN 19..437; /note="Phosphatidylserine decarboxylase proenzyme 1, mitochondrial"; /id="PRO_0000353844"; CHAIN 19..400; /note="Phosphatidylserine decarboxylase 1 beta chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; /id="PRO_0000353845"; CHAIN 401..437; /note="Phosphatidylserine decarboxylase 1 alpha chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; /id="PRO_0000353846" MLKFHRNVKPQFGAFARYSSLGKHNSRKRVGIIRLAYGLTGIGLVGLAGFAWAQDRHEKTYQKKGVQVEGPWQFYVLTTLPLRTLSRWWGYVNRIEIPLWMRVPAFGLYSKIFGCNLTEADPDDVRQYKNLAEFFTRKLKPGARVIDPDAPIVIPADGKILNYGVIEGGQLEQVKGITYSLDALLGDEKLARLKRSHAIPSPDHIPHIRQEEFAKLNGIHYSLQDLMGHDHGERPSHVKDASAQHIDLLSSTKVAAKSQFTLFGSRETNCLYYAVIYLAPGDYHRFHSPTDWVVERRRHFSGELFSVSPFMARRLGNLFILNERVALMGRYKYGFMSMIPVGATNVGSIRIKFDKDLCTNQFGKLGPVGTFDEAVYTSSSSILHGHPLLRGDEVGNFELGSTVVLVFEAPADFEFLVKQGQKVRVGLPLGRVVPSSH O14343 KLP5_SCHPO BINDING 144..151; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" SPBC2F12.13; CHAIN 1..883; /note="Kinesin-like protein 5"; /id="PRO_0000125388" MSRQSSITVTVRVRPFSTAESANLIASSDRLSFGTSSSLRNPGSGRQIRRVVKVLDGRVLVFDPPDETTATLSATNRRLSTSQQSLARLSRKSNNSAGFGRDLRYAFDRVFDETATQQQVYERTARPLLDNILDGFNATIFAYGATGCGKTHTISGTMQDPGLIYLTLKELFERMDHLRDEKIFDLRLSYLEIYNETIRDLLVSPTPNQAKPLNLREDADRRITVPGLTSLSPESLEEIIDIIMKGNANRTMSPTEANAASSRSHAVLQVTLIQKPRTAGINEDHTLATLSIIDLAGSERATATKLRGSRLFEGANINKSLLALGNCINALCDPHRRAHVPYRDSKLTRLLKFSLGGNCRTVMIVCVSPSSVHYEETHNTLKYANRAKNIKTEVLRNMISVDRHVSQYVKAIVELREQISELENRLAQIDLSSQSNGSDQDAVTQSFAHESKLAEARNLLRMTFEETLPLQNDTINKVEKVKHFDDSIRVLKYWLSCYERILPNSADERVFLVRSKLESLLTRRAEIIADIDPELVYQKFQRSVSHIINTYKQEGATMYADVLQDEVDLLKSIIENQVLDAQNKVDEFTPVLESLLRSSFKASSLLKEGGMQELFSILEKWLLGIGLGEKPNISVLSESYKLNSTSDDSRTINRDRVHSFPTQPLLNNNLPRMFFVKSPKKPVVFSKRSPKKRVRFDDSMSTSDSGASAYNSPIQTSKLKNMNFFNTMHMPSTPAHKRPENKNQIDVEINLTSPVSPMLEDKPEPGLLIKSPLEKKQEVNSESTQLDQLLAEDSSTDDVSLPHLDTIDLDGSPVPKVPDLNFSRANMDSPTFILNNEAIHNFDFSKPKTRQSLSSLTTLHLSNPANIIRKSLSMAENEEEKAT O14350 SWI3_SCHPO SPBC30D10.04; CHAIN 1..181; /note="Swi1-interacting protein swi3"; /id="PRO_0000072350" MSTAASDSGVEKLVEENKREEVKKNEEEKEFDLGLEENPDSVKKPRKRLAKFDEERLISENGIPKLRKMMRKVKLKGKGHEAKDLKQLLGMYHIWTHELYPRATFDDSISYLKTLGKHRSVKVRRRGWINEIAVENGSDSNASLFTGPSSNSLVNLTSGDPYVQDTADDAFVAQDNDTQLE O14352 LSM4_SCHPO SPBC30D10.06; STRAND 13..19; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 24..32; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 38..46; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 53..61; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 66..71; /evidence="ECO:0007829|PDB:6PPQ" HELIX 3..9; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 63..65; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 73..81; /evidence="ECO:0007829|PDB:6PPQ" TURN 10..12; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..121; /note="Probable U6 snRNA-associated Sm-like protein LSm4"; /id="PRO_0000125570" MLPLTLLNATQGRPILVELKNGETFNGHLENCDNYMNLTLREVIRTMPDGDKFFRLPECYIRGNNIKYLRIQDEVLSQVAKQQAQQRENRGSRFRGRGQRGRGNYGHTAPNRRGRGRGGHM O14356 TOR1_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:12805221}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:12805221}; PTM: Phosphorylation at Thr-1972 in the ATP-binding region by AKT1 strongly reduces kinase activity. {ECO:0000269|PubMed:24247430}. MOD_RES 1972; /note="Phosphothreonine; by PKB/AKT1"; /evidence="ECO:0000269|PubMed:24247430" SPBC30D10.10c; CHAIN 1..2335; /note="Serine/threonine-protein kinase tor1"; /id="PRO_0000088812" MEYFSDLKNKNESIQLAAADQLKEFVHSSTKELSGESLARFNNDINRRIFELIHSHDSHERFGGILAIGKLIEFESEGDVTNLSRYANYLRMTLPSTDWHSMELSAKVLGHLAASGGTLAAEFVEFEVQRAFEWLQGDRQEQKRMAAILIIKALAQNSPTLVYLYISEIFQNLWTGLRDPKPLIRETAADALGASLDVVCQREAKVQLQCFNEVLLQAEHGLRQSSVEYLHGSLLAYKELFEKSGSFIREHYTEFCDLALRLREHRDNSIRRCIVFLLPTLSEYNPKKFQQRYLDSFMVYLLSHIRKDKEKSLAFEAIGRIAMAVNEAMIPYLQNILKVIRDTLTAKVREKTQYEKPVFECIGMLAAAVKLELLEDSRSLLGLIFSCELSVHLRQALVKMAENIPPLLAPIQERLLNMVSQILTGKNFEIRTNDTYTPSFTNIYSAREPDQRSKSTESIILALETLGTFNFTGYSLISFIQESVLSYLENDNSEIRIAAARTCCQVFARDPICRKTNPLAVESVAEVLEKLLTLGIADSDPKIRETVLSLLDERFDRHLAHPDNIRCLFIALNDEVFSIREIAIIIIGRLALYNPAHVMPSLRKTIIQLLSDMEYSGNSRQKEESAQLLKLLVSKARTLIKPYIQSIIHVILPKAADTSPGVSSAIISALGELASVEGEDMPVDVRGSFMKLILVNLQDQSSTLKRLASLKCLRKLCGRSGYVIQPYLDYPPLLGALIGILQSEQPTPIRREVLRTLGVLGALDPYTYLTTEEVSDDLQSSHNNAHGVPQISAAQYPSLENYAMVAVVTLIGILKDSSLSMHHSSVVQAVMHICSQMGSKSTVFLPQVVPTFLQVMQSLSASSAEFYFQQLTTLTSIIGPNIRDYVSDIFNLSKVFWESTTSLLLVILELIDAIAIALQDEFKFYLPQILSCMLKAFSLDNTSSRSVSYKVLQSFVIFGSNIEEYMHLVLPVIIRSFERDTIPLGFRKSALKCIAQLFQSVNFSDHASRIIHPLVRMLGKSNGDLRAVIMDTLCAIVSQLGYDYSIFIPMVNKVLVSHKISHPAYELLVSRLLKGEPLPKDVVVKEFKPRPSTKPFSTQDEVLTKLPVDQASLKAAWESSQKLTRDDWQDWIRRISIELLKESPSSALRSCSTLAGIYHPLARDLFNVSFLSCWDELTESNKKNLVKSIELAMNAPNISVEILQTLLNLAEYMEREDHTLPIPIKVISAHASKCNVYAKALHYTELQFVQETKEEVSISTIESLITINNHLQQSDAAVGMLQYTKEHKQFSLKETWYEKLHRWDDALAAYEHREREGDSSFEINIGKLRCYYALGDWDHLSELAQKAWVTSEQEHREAIAPLAAAAAWGLGQWNLISEYVSAMDRDPQDKEFFSAISAVHLGQYNKAYGHIERHRDILVNDLSSIIGESYNRAYGIMVKSQMLSELEEIIDYKKNMQYENNLDSLKKTWRKRLEGCQKNVDVWHNTLRFRALVLSPQDSPEMWIKLADLCRRSDRLKLSNQCLTYLMGRDPSNAYPLDSLKLLNPHVVYTYLKYLWATDQKNIAVSELEEFTSYLSSKHGYKMGDSSKLVDILASSSVSSEERSFLARCFHKLGKWKKSLQDSVNQESVRDILNCYFYATLFDKSWYKAWHSWALANFEVVGYYEQTEHGVTQDMYEQYIVPAIKGFFHSSVLNQKNSLQDILRLLNLWFKFGEHSDVAAAIVEGFSNVPMDTWLEVIPQLIARIHTSSSSVRASVHQLLSDIGRVHPQALVYSLTVSSKSTNPQQKHSAKSIMDSMLSHSDTLVRQALLVSQELIRVAILWHELWYEGLEEASQAYFSDHDISLMIDIVKPLHETLEKGPSTLSEISFAQTFGYDLRKARSYWQKFLQDGDPTELNQSWDLYYQVFRRIQKQLPRIKHLELQYVSPKLLDACDLELAVPGTYGHNKPVIRISHFHHTFEVISSKQRPRRLTIHGSDGKDYQYVLKGHEDLRQDERVMQLFGLCNTLLTTDSETFKRRLNIERYTVIPLSPNSGLLGWVPHSDTLHFLIKEFRSKRNILLNLEHRMMLQMAPDCDSLTLLQKLEVFEYVMANTDGYDLYHVLWLKSRSSEAWLDRRTSYTQSLAVMSMVGYILGLGDRHPSNLMMDRYSGKIIHIDFGDCFEVAMHREKFPEKIPFRLTRMLINAMEVSGIQGTYKITCELVMRVLRSNTESLMAVLEAFVYDPLINWRLMTKSSFGASTTLRPTSSSVEEKGRSYTHRARHADYAALSETNGVNAEGLNERSIQVLKRVSNKLTGKDFDLKEQLPVKAQVEKLIQQATAPENLCRCYVGWCSFW O14368 HSP16_SCHPO SPBC3E7.02c; STRAND 14..16; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 24..26; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 39..43; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 45..53; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 62..67; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 70..77; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 85..93; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 98..105; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 116..120; /evidence="ECO:0007829|PDB:3W1Z"; STRAND 123..131; /evidence="ECO:0007829|PDB:3W1Z" HELIX 59..61; /evidence="ECO:0007829|PDB:3W1Z"; HELIX 80..83; /evidence="ECO:0007829|PDB:3W1Z"; HELIX 112..114; /evidence="ECO:0007829|PDB:3W1Z" TURN 4..6; /evidence="ECO:0007829|PDB:3W1Z" CHAIN 1..143; /note="Heat shock protein 16"; /id="PRO_0000126003" MSLQPFFGFPPTVNDLFSDFVSYSPRLNNQIPGELSPSIDVHEGKDTVSVDVELPGVKKEDVQVHYDSGKLTISGEVVNERKNESTEGNQRWSERRFGSFSRTITIPAKIDADRIEANFSNGLLTVTLPKVEKSQTKKQIAIK O14370 BCA1_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9483807}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9483807}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9483807}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; TRANSIT 1..47; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 256; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPBC428.02c; CHAIN 48..427; /note="Branched-chain-amino-acid aminotransferase, mitochondrial"; /id="PRO_0000001280" MSLMFLRRAGNIKGRNIRFALQRGSVGYSQQSSEACKNFLNTTQLRTMVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMILPGVTRDSILEICRERLAPKGWKITEGKYSMKEVAQASKEGRLLEVFGAGTAALVSPVKAINYKGTEYEIPMPEGQEAGPITSEISKWILDIQYGKEPNNPWSVPALP O14417 MAD2_SCHPO SPBC20F10.06; STRAND 42..47; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 50..55; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 80..89; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 95..105; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 149..158; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 167..169; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 179..187; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 189..199; /evidence="ECO:0007829|PDB:4AEZ" HELIX 14..33; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 39..41; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 58..76; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 118..137; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 138..140; /evidence="ECO:0007829|PDB:4AEZ" TURN 90..92; /evidence="ECO:0007829|PDB:4AEZ" CHAIN 1..203; /note="Mitotic spindle checkpoint component mad2"; /id="PRO_0000126114" MSSVPIRTNFSLKGSSKLVSEFFEYAVNSILFQRGIYPAEDFKVVRKYGLNMLVSVDEEVKTYIRKIVSQLHKWMFAKKIQKLILVITSKCSGEDLERWQFNVEMVDTADQFQNIGNKEDELRVQKEIQALIRQITATVTFLPQLEEQCTFNVLVYADKDSEVPTDWVDSDPRILRDAEQVQLRSFSTSMHKIDCQVAYRVNP O14463 TRX1_SCHPO ACT_SITE 30; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 33; /note="Nucleophile"; /evidence="ECO:0000250" SPAC7D4.07c; CHAIN 2..103; /note="Thioredoxin-1"; /id="PRO_0000120043" DISULFID 30..33; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" MVKQVSDSSEFKSIVCQDKLVVVDFFATWCGPCKAIAPKFEQFSNTYSDATFIKVDVDQLSEIAAEAGVHAMPSFFLYKNGEKIEEIVGANPAKLEASIKANL O14470 SSR2_SCHPO BINDING 193; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 196; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 216; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 219; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 306; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23H3.10; CHAIN 1..503; /note="SWI/SNF and RSC complexes subunit ssr2"; /id="PRO_0000197084" MTLDQVRIPFLVEQTYPIIVPSYAGWFDMSKIHDIERRSNPEFFNGKSPLKTPSIYKDYRDFMINSYRLEPNEYLTVTACRRNLVGDVCAIIRVHAFLEQWGLINYQIDPETRPAFRLPPISGHVQAISNTPIVTQEMLAQHPPPSTVGGSSSQEFVKLEEKHYSPSLNAMEQTSPKEEDEKSDKVPRVDKVCFTCGVNCSQTWYHNLKNKKYDICPNCYKQGRFSSSFNSSDFLCMDAIDFNHDEEKPWSNQETLLLLEAIETYGDDWNQIALHVGSRTKEQCLIHFLQIPIEDPYRQKLQGDFSPFKKGFLPFDENENPVLSTLTYLASIVQQGMKERKQNESVKQGETSFGNSEFKNPLERVAYYALKSAAQKAKLIAAFENRQLRRLVFSLIQAQLEKLQLKMKVLEQLEKMCSLELSELDLRGKNLLLSRLSTKKMLLAFNKKLEEAVNLGGEDGLKIIDDLMSTEHAEALLTFEMPTATTVSPLSKQYPDKFRTIAL O36015 TRM7_SCHPO ACT_SITE 164; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03162" BINDING 53; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03162"; BINDING 55; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03162"; BINDING 83; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03162"; BINDING 99; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03162"; BINDING 124; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03162" CATALYTIC ACTIVITY: Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_03162, ECO:0000305|PubMed:25404562}; SPAC4F10.03c; CHAIN 1..285; /note="tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase"; /id="PRO_0000155589" MGRSSKDKRDAYYRLAKEQGWRARSAFKLLQLNEQFNLFEGAKRVVDLCAAPGSWSQVLSRELLKNIDTSIAADEKPMIVAVDLQPMAPIDGVCTLQLDITHPNTLSIILSHFGNEPADLVVSDGAPDVTGLHDLDEYIQAQILLAAFNLAVCVLKPGGKFVAKIFRGRDVSLLYSQLRLMFRKVSCAKPRSSRASSIESFVVCEDFNPPSNFQPDLTKPLCVIDPTNAHEIAPFIACGDLDGYDADATYPVEINMKKATLDVIQPPTAPPYKRAIELKHSKMMS O36019 ATG13_SCHPO PTM: Phosphorylated (PubMed:17295836). Dephosphorylated under depletion of nitrogen (PubMed:17295836). {ECO:0000269|PubMed:17295836}. SPAC4F10.07c; STRAND 80..82; /evidence="ECO:0007829|PDB:4YK8"; STRAND 109..113; /evidence="ECO:0007829|PDB:4YK8"; STRAND 150..157; /evidence="ECO:0007829|PDB:4YK8"; STRAND 211..215; /evidence="ECO:0007829|PDB:4YK8"; STRAND 222..224; /evidence="ECO:0007829|PDB:4YK8"; STRAND 238..242; /evidence="ECO:0007829|PDB:4YK8"; STRAND 246..248; /evidence="ECO:0007829|PDB:4YK8"; STRAND 251..261; /evidence="ECO:0007829|PDB:4YK8" HELIX 36..57; /evidence="ECO:0007829|PDB:4YK8"; HELIX 77..79; /evidence="ECO:0007829|PDB:4YK8"; HELIX 86..97; /evidence="ECO:0007829|PDB:4YK8"; HELIX 167..185; /evidence="ECO:0007829|PDB:4YK8"; HELIX 189..199; /evidence="ECO:0007829|PDB:4YK8" TURN 102..104; /evidence="ECO:0007829|PDB:4YK8" CHAIN 1..758; /note="Autophagy protein 13"; /id="PRO_0000116723" MPRLNTQLPRMYSAPPGHSKAVSTELNKDLSSVGGRSAKLGQVIHHCFYKTGLIILESRLNVFGTSRPRESSKNNKWFNLEIVETELYAEQFKIWKNIELSPSRKIPPMVLHTYLDISDLSKNQTLSVSDGTHSHAINFNNMSTMKIVLERWIVNLDGEALSTPLELAVLYKKLVVLFRSLYTYTHLMPLWKLKSKIHKLRAHGTSLKVGCALSTDDVLSNDFLPISAPISSSLGSSIATFSFSPVGTPAGDFRISVQYRKNCHFEVHDSDALLSNQLLSADKHQLAASNNSQDFEDGKQYDQPPPSFATRLAKQSDPNSLLQSEIQHLASIESITAQAAPLVTIHPFKSPSLSASPGSNFDNMSISPKVAVNRYIHRGPSATSLNKFSMISDAASKSRAKLPPLTSGSLKLNTLDISNTPNLRRFSSSFGPRERKESFSSRNRLPLVNHPIRSIFKHNVSENPITDHSEHAVYDSEFASKDDLSGFIQLLDSHAHHLNASEGSKSSGSFPGKVQTLTSGISPVAHPHNSLGSSNEIFDIDTYNHSIDNSGSRFTEAVKHNLGNSSHSIMRHHTLGTLRSRPSFSEKSTFPAPLTSISQASTFQGDNRSPSTVIPHTQTEVPSANDTSKQLASLHDMRKSQSPICARSATSAGLPRFEYHTSLSKSLEHSSTPASLQATKTPSPSFVLEPGIPQEYKKHFDNLSEERRQCLTPSTPTYEYYNEHNPNYDDDLLFTMTDMTLEPHDVSAIRLGSPKSDD O36023 SPN1_SCHPO BINDING 102..109; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 139; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 165; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 244..252; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 317; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC4F10.11; CHAIN 1..469; /note="Septin homolog spn1"; /id="PRO_0000173503" MASMVLADGMPTVKDDSTRSRGSDVDSFTSTDNVTQINVEAAISENKNEEKPIQDNSEQEFNPHVSIIQRQLNGYVGFASLPNQWHRRCVRQGFNFNVLVLGESGSGKSTLVNTLLNRDVYPPTQKSLTGDFGVNPEPTVMINSSAVEIVENGISLQLNVIDTPGFGDFIDNTDCWQPVLTDIEGRYDQYLELEKHNPRSTIQDPRVHACIFFIQPTGHAISAMELRVMLALHEKVNIIPIIAKADTLTDDELNFTKEMILRDIQYHNIRIFFPPTYETDDPESVAENADIMSRIPFAIIASNTFVVNNEGKRVRGRRYPWGVVEVDNEEHSDFPKLREMLIRTHLEELKEQTNKLYEAYRTERLLSSGISQDHSVFREVNPSAKLEEERALHEEKLMKMEAEMKTIFSQKVQEKEDRLKQSENELRTRHREMKAALEKQKADLIDHKNRLMQAKAAAENEKSKRKFFK O36027 WSP1_SCHPO MOD_RES 386; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4F10.15c; CHAIN 1..574; /note="Actin-binding protein wsp1"; /id="PRO_0000189003" MPPSSSITQEDKATIRKYIPKSTNKIIAAAVVKLYVAYPDPNKWNYTGLCGALVLSYDTTAKCCWFKLVDVVNNSGIIWDQELYQNMDYRQDRTFFHSFELDKCLAGFSFANETDAQKFYKKVLDKGCHPESIENPVLSFITRKGSSRHAPNNSNIQPPSAAPPVPGKENYNAVGSKSPNEPELLNSLDPSLIDSLMKMGISQDQIAENADFVKAYLNESAGTPTSTSAPPIPPSIPSSRPPERVPSLSAPAPPPIPPPSNGTVSSPPNSPPRPIAPVSMNPAINSTSKPPLPPPSSRVSAAALAANKKRPPPPPPPSRRNRGKPPIGNGSSNSSLPPPPPPPRSNAAGSIPLPPQGRSAPPPPPPRSAPSTGRQPPPLSSSRAVSNPPAPPPAIPGRSAPALPPLGNASRTSTPPVPTPPSLPPSAPPSLPPSAPPSLPMGAPAAPPLPPSAPIAPPLPAGMPAAPPLPPAAPAPPPAPAPAPAAPVASIAELPQQDGRANLMASIRASGGMDLLKSRKVSASPSVASTKTSNPPVEAPPSNNLMDALASALNQRKTKVAQSDEEDEDDDEWD O36028 ATCZ_SCHPO ACT_SITE 600; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0" BINDING 600; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 600; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 601; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 602; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 602; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 724; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 765; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 767; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P32660"; BINDING 770; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 788; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 822; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 823; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 902; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 903; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 904; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1009; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1015; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1035; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 1038; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 1039; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1039; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q8NB49"; BINDING 1298; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"; /ligand_id="ChEBI:CHEBI:57262"; /evidence="ECO:0000250|UniProtKB:G0S196" CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:P32660}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; SPAC4F10.16c; CHAIN 1..1367; /note="Phospholipid-transporting ATPase C4F10.16c"; /id="PRO_0000343137" MPSLINFDAISSLKSSLHGLSICAFNHLHHVPQHNGSLAHEGPTNQTDYSSRHHESQFSQEAHAEQRSRDDEEANSFEGSCNNSDQSWTSRVTSKKNEAGTESGDASVRRIYVTSIPEEHRHLPSQWFPSNKIRTTKYTPVSFIPKNLWNQFKNIANAFFLFVTLLQCIPLFCPEHLGLSFIPLSVILLTTAIKDGIEDYRRCVLDKKFNNTLTWKLVGFNNANALGEHIGLWRKLKKFISHTVADMSYCLKNSGISSGLATLTVDNISHRHSLESDSAFTLSSVSQDSLEIHEIGNSGPSNSFSVIQEQSTGSSNAKFERVCRKSLLVGDIVKVLADEAIPADLLILSTENSNGVCYVETKNLDGETNLKDKYALCSTKCCKSEYRCSAASFWVECEQPHADLYSLNGVVKAPGAVQSPSESTNGRKIHEEPFSISNVLLCGCTLRNSKWVIGLVLYTGSETRIQKNRGLTPSKRSRITRDLNWTIILNFLLLFAMCLFSGVLRSIYSAQNNSARVFELSKNSNTAPAHGIISIFTSLILFQNLVPISLYITMDIVRSIQSYFIFSDREMYDEKLDCPCSPKSWNISDDLGQIEYIFSDKTGTLTQNIMSFKKCSINGIRYGKSHNEDTCIKKRRNLNYNENLSCKVDLDKKKMLETLSLSDSPNPESITFISSKFVDHLQSNENYIQTEACFEFFKALALCHSVVTDVQDETLIYNAQSPDEEALVKVARDFGFTLLNTKNRRYTIRIRGENKNFRVLDIIPFTSTRKRMSVIIRDEDGIIHLICKGADTVIFPRLSSGQNNIIEKTKKHLASFSSEGFRTLCIARRTIDKQDYLEWKVNFNEANSAIHERNEKVSKVSEMIEQELELLGGTAIEDKLQENVPETIALLAIAGIKLWVLTGDKVETAINIGYSCNLLDPNMTIFRIDANSFGALEEVEAFIRNTLCFNFGYMGTDEEFRFLLKDHSPPSPKHAIVIDGDALNFVLSEQVSFLFLMLCKQCKTVLCCRVSPSQKAAVVALVKKSLNVVTLAIGDGANDVSMIQEADVGVGIKGVEGQAASMSADYAIGQFSFLGRLLLVHGRWDYKRMSQMISFFFYKNVIWTFILFWYQFYNEFDGNYIFDYTYVMLFNLLFTSLPVIIAGCFDQDVDASVSMKNPSLYQRGILGLEWNGKRFWSYMLDGIYQSLVCFGVALFVFKFGDFVSWTGRNIECIEDIGLFISSPTIFVINIFILMNQERLNLISLITWMFSIGVFWIWTFIYSEVGPSYAFHKSASRTCQTFGFWCVTVLTIALCLLPRFSYICLQKLFYPRDIDLLRRRLCAKSDDETSSSSSFATDIEMCEQCNDPLSSKKNSGIVTSVSFDDSNK O42634 DMC1_SCHPO BINDING 120..127; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305"; BINDING 223; /ligand="dsDNA"; /ligand_id="ChEBI:CHEBI:4705"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 223; /ligand="ssDNA"; /ligand_id="ChEBI:CHEBI:9160"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 226; /ligand="ssDNA"; /ligand_id="ChEBI:CHEBI:9160"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 229; /ligand="dsDNA"; /ligand_id="ChEBI:CHEBI:4705"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 229; /ligand="ssDNA"; /ligand_id="ChEBI:CHEBI:9160"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 235; /ligand="dsDNA"; /ligand_id="ChEBI:CHEBI:4705"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 235; /ligand="ssDNA"; /ligand_id="ChEBI:CHEBI:9160"; /evidence="ECO:0000250|UniProtKB:Q14565"; BINDING 304; /ligand="ssDNA"; /ligand_id="ChEBI:CHEBI:9160"; /evidence="ECO:0000250|UniProtKB:Q14565" SPAC8E11.03c; CHAIN 1..332; /note="Meiotic recombination protein dmc1"; /id="PRO_0000122916" MEEFAEGNDDEQMIFSDIEDLTAHGIGMTDIIKLKQAGVCTVQGVHMSTKRFLLKIKGFSEAKVDKLKEAASKMCPANFSTAMEISQNRKKVWSISTGSEALNGILGGGIQSMSITEVFGEFRCGKTQMSHTLCVTAQLPRDMGGAEGKVAFIDTEGTFRPDRIKAIAERFGVDADQAMENIIVSRAYNSEQQMEYITKLGTIFAEDGQYRLLIVDSIMALFRVDYSGRGELSERQQKLNIMLARLNHISEEFNVAVFVTNQVQADPGAAMMFASNDRKPVGGHVMAHASATRLLLRKGRGEERVAKLNDSPDMPEAECSYVITPGGIADVS O42649 SMC3_SCHPO BINDING 32..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305" PTM: Acetylation at Lys-105 and Lys-106 by ECO1 is important for genome stability and S phase sister chromatid cohesion. {ECO:0000250}. MOD_RES 105; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 106; /note="N6-acetyllysine"; /evidence="ECO:0000250" SPAC10F6.09c; CHAIN 1..1194; /note="Structural maintenance of chromosomes protein 3"; /id="PRO_0000119014" MYITKIVIQGFKSYKDYTVIEPLSPHHNVIVGRNGSGKSNFFAAIRFVLSDAYTHLSREERQALLHEGPGATVMSAYVEVTFANADNRFPTGKSEVVLRRTIGLKKDEYSLDKKTVSKTEVINLLESAGFSRSNPYYIVPQGRVTSLTNAKDSERLELLKEVAGTQIYENRRAESNKIMDETIQKSEKIDELLQYIEERLRELEEEKNDLAVYHKKDNERRCLEYAIYSREHDEINSVLDALEQDRIAALERNDDDSGAFIQREERIERIKAEITELNHSLELLRVEKQQNDEDYTNIMKSKVALELQSSQLSRQIEFSKKDESSKLNILSELESKISEKENELSEILPKYNAIVSEADDLNKRIMLLKNQKQSLLDKQSRTSQFTTKKERDEWIRNQLLQINRNINSTKENSDYLKTEYDEMENELKAKLSRKKEIEISLESQGDRMSQLLANITSINERKENLTDKRKSLWREEAKLKSSIENVKDDLSRSEKALGTTMDRNTSNGIRAVKDIAERLKLEGYYGPLCELFKVDNRFKVAVEATAGNSLFHIVVDNDETATQILDVIYKENAGRVTFMPLNKLRPKAVTYPDASDALPLIQYLEFDPKFDAAIKQVFSKTIVCPSIETASQYARSHQLNGITLSGDRSDKKGALTAGYRDYRNSRLDAIKNVKTYQIKFSDLQESLEKCRSEIESFDQKITACLDDLQKAQLSLKQFERDHIPLKDELVTITGETTDLQESMHHKSRMLELVVLELHTLEQQANDLKSELSSEMDELDPKDVEALKSLSGQIENLSHEFDAIIKERAHIEARKTALEYELNTNLYLRRNPLKAEIGSDNRIDESELNSVKRSLLKYENKLQIIKSSSSGLEEQMQRINSEISDKRNELESLEELQHEVATRIEQDAKINERNAAKRSLLLARKKECNEKIKSLGVLPEEAFIKYVSTSSNAIVKKLHKINEALKDYGSVNKKAYEQFNNFTKQRDSLLARREELRRSQESISELTTVLDQRKDEAIERTFKQVAKSFSEIFVKLVPAGRGELVMNRRSELSQSIEQDISMDIDTPSQKSSIDNYTGISIRVSFNSKDDEQLNINQLSGGQKSLCALTLIFAIQRCDPAPFNILDECDANLDAQYRSAIAAMVKEMSKTSQFICTTFRPEMVKVADNFYGVMFNHKVSTVESISKEEAMAFVEG O42661 SMD1_SCHPO SPAC27D7.07c; CHAIN 1..117; /note="Small nuclear ribonucleoprotein Sm D1"; /id="PRO_0000122205" MKLVRFLMKLTNETVSIELKNGTIVHGTITSVDMQMNTHLKAVKMTVKGREPVPVETLSIRGNNIRYYILPDSLPLDTLLIDDSTKPKQKKKEVVRGRGRGRGRGTRGRGRGASRGF O42667 SSM4_SCHPO MOD_RES 460; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 606; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC27D7.13c; CHAIN 1..670; /note="Microtubule-associated protein ssm4"; /id="PRO_0000083532" MSYLSVGDEVLIRGELGIVRFAGSTDFESGIWLGVELLNGKGKNDGSVKGKRYFSCEKGKGIFVRACSSNVMKRPSVVKSRKKGSENISNFMEKTKAIKQKSRREPSKFERSLARPLCITPIDSSTPTKTATFYTSSTTENLDELNFSTEELSSFDTTLLNSDTSKLSGLDDSSFMEEEFVWQVDNVLQECEKKFTPHSKGSYLKENLKSELRKGRLDELMCENTALKEKIDKLNKELEKVEPQLTFLRSKNSIEKPRNFRREKFLKKFLAMQKEIKYLRKRKLQIRKIPNYKYSDRSLNSKTPKSQDNWTTQVTPSSLLGVSEVSKVLQLKQVQVDITELVKIPKNPFSEKLTISNVNRYLNIVPGSLDLQFSLTNENFVHWNSTVYQELLNLKSNNSSVDGVKTRRQLLEENALLSHKVLKLTEEIQDLETLNQLNTEIEARQSEKLNEVQEETQRLSQLLISSQPALTEVKHLKLCLSDSQEELLQLNAKLEKANIVIDELNSAKLKLSKQVEEESSMKDDLTEMNQRLKEQIESYENEVNSEITSRTLKEFETLKTQYEKNLCNLREQLKTARMKLADKYPQGDNTSENIDWLKHSLRDSNTENSIPSPLTFACKEIRKLVADIKPVSVEKQLALNWKKDIERPSFHHNQQLFNYCQLTDILSKKC O42709 MCM10_SCHPO SPBC1347.10; CHAIN 1..593; /note="DNA replication licensing factor mcm10"; /id="PRO_0000096280" MHDPFIAEENDLDLEEKRLQRQLNEIQEKKRLRSAQKEASSENAEVIQVPRSPPQQVRVLTVSSPSKLKSPKRLILGIDKGKTGKDVSLGKGPRGPLPKPFHERLAEARNQERKRSDKLKTMKKNRKQSFQRKRNILEDGKSEEEKFPMKCDEIDPYSRQAIVIRYISDEVAKENIGGNQVYLIHQLLKLVRAPKFEAPEVDNYVVMGIVASNSGTRETVNGNKYCMLTLTDLKWQLECFLFGKAFERYWKIQSGTVIALLNPEVLKPKNPDIGRFSLKLDSEYDVLLEIGRSKHLGYCSSRRKSGELCKHWLDKRAGDVCEYHVDLAVQRSMSTRTEFASSMATMHEPRARREKRFRGQGFQGYFAGEKYSAIPNAVAGLYDAEDAVQTERERKERYKKQRAQAEREREILVRLSKRCCASSSSSSNSNNLSTGMSMRTLGHQYLNLQGSGVKNLHDKGNPTALSKDSEIDSSTKKPSVLASFNASIMNPKSSLPSFSNSAILGTNDAASGTPVPQDTTSTKVSPAVVFTSSPRIFSPQSLRKIGFDPTHSADASTTHSTATGLSRSGSLKNIKFRYEFTESDDEDDLEIVP O42832 SPB1_SCHPO ACT_SITE 158; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03163" BINDING 57; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03163"; BINDING 59; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03163"; BINDING 77; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03163"; BINDING 93; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03163"; BINDING 118; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03163" CATALYTIC ACTIVITY: Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000255|HAMAP-Rule:MF_03163}; MOD_RES 362; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1687.11; STRAND 47..53; /evidence="ECO:0007829|PDB:8ETC"; STRAND 71..79; /evidence="ECO:0007829|PDB:8ETC"; STRAND 87..92; /evidence="ECO:0007829|PDB:8ETC"; STRAND 112..117; /evidence="ECO:0007829|PDB:8ETC"; STRAND 149..160; /evidence="ECO:0007829|PDB:8ETC"; STRAND 176..179; /evidence="ECO:0007829|PDB:8ETC"; STRAND 185..187; /evidence="ECO:0007829|PDB:8ETC"; STRAND 193..201; /evidence="ECO:0007829|PDB:8ETC"; STRAND 255..257; /evidence="ECO:0007829|PDB:8ETC"; STRAND 275..278; /evidence="ECO:0007829|PDB:8ETC"; STRAND 281..283; /evidence="ECO:0007829|PDB:8ETC"; STRAND 293..295; /evidence="ECO:0007829|PDB:8ETC"; STRAND 305..308; /evidence="ECO:0007829|PDB:8ETC"; STRAND 757..760; /evidence="ECO:0007829|PDB:8ETC"; STRAND 769..771; /evidence="ECO:0007829|PDB:8ETC"; STRAND 777..782; /evidence="ECO:0007829|PDB:8ETC" HELIX 15..23; /evidence="ECO:0007829|PDB:8ETC"; HELIX 28..40; /evidence="ECO:0007829|PDB:8ETC"; HELIX 58..66; /evidence="ECO:0007829|PDB:8ETC"; HELIX 97..107; /evidence="ECO:0007829|PDB:8ETC"; HELIX 127..148; /evidence="ECO:0007829|PDB:8ETC"; HELIX 165..175; /evidence="ECO:0007829|PDB:8ETC"; HELIX 209..212; /evidence="ECO:0007829|PDB:8ETC"; HELIX 214..217; /evidence="ECO:0007829|PDB:8ETC"; HELIX 228..233; /evidence="ECO:0007829|PDB:8ETC"; HELIX 258..263; /evidence="ECO:0007829|PDB:8ETC"; HELIX 267..273; /evidence="ECO:0007829|PDB:8ETC"; HELIX 284..291; /evidence="ECO:0007829|PDB:8ETC"; HELIX 297..304; /evidence="ECO:0007829|PDB:8ETC"; HELIX 311..328; /evidence="ECO:0007829|PDB:8ETC"; HELIX 456..470; /evidence="ECO:0007829|PDB:8ETC"; HELIX 640..645; /evidence="ECO:0007829|PDB:8ETC"; HELIX 661..669; /evidence="ECO:0007829|PDB:8ETC"; HELIX 763..765; /evidence="ECO:0007829|PDB:8ETC"; HELIX 787..795; /evidence="ECO:0007829|PDB:8ETC" TURN 246..248; /evidence="ECO:0007829|PDB:8ETC"; TURN 471..474; /evidence="ECO:0007829|PDB:8ETC"; TURN 650..653; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..802; /note="AdoMet-dependent rRNA methyltransferase spb1"; /id="PRO_0000155601" MGKSQKKTAKGRLDKWYKLAKEQGYRSRAAFKLVQLNQKYSFLEKAKVIIDLCAAPGGWLQVASKTCKPGSLIVGVDLAPIKPIPNCHTFVEDITSDKCRSQLRGYLKTWKADVVLHDGAPNVGSAWLQDAYGQAQLVLMSMKLACEFLVAGGTFVTKVFRSRDYNNLLWVFKQLFNKVEATKPPSSRNVSAEIFVVCRGYKAPKKLDPRFTDPRTVFEEVQEPVTNVDAKVFHPEKRKRSREGYADDDYTLHKTVLASEFVTANDPIQILGTSAEIVFPKDDEECQRLYNLDVTTEEILLCCSDLQVLGKKEFRDILRWRLKIRDEMGIGKKVEDEQKTVVEEIPEMDEEERLDQELQDLSEAERVKLKRERRKANQRKQREIVRMQMGMLAPMDIGLEHEAMGEDSLFGLATAEKHGLKELENGTLPVTESVDEEVSTDNEVEYDSDDERDRLEADLDSMYSDYTKRKAESDVKYRVKKARGDLDDEEWNGIDNGTESDDSQIAETNFATPDKDRLTTSLLDKGSTKDGLSRKARMFFDQDIFDGIEDADADVEIMSMNRAAIKKREAELASQNNDDGSKGDQSEDSNDHIEVVPVASAHDEDDDWNSDSDNDENNVEIVTAEAMTLAQDIASRRKSKADLIDEGYNRWSFQSKEGLPDWFLDEETTVNKPNKPITKEAVLALREKMKALNARPIKKVLEAQGRKKMRTIKRLQRVAKKAEGISESGDMTESEKAKEISRLVSRATKSKPKAKPTLVVAKGPNKGLKSRPKGVKGKYKMVDSRMKKDLRAQKRLAKKGRR O42844 KCC2_SCHPO ACT_SITE 188; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 71..79; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 94; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:12135745}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:12135745}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12135745}; PTM: Autophosphorylated. {ECO:0000269|PubMed:12135745, ECO:0000269|PubMed:18257517}. MOD_RES 252; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23A1.06c; CHAIN 1..504; /note="Calcium/calmodulin-dependent protein kinase type II"; /id="PRO_0000086104" MSILAGFKNLLKHSKSSKGRSNASKSVDVSVNRDVAAYTELAAKNVNAGGDEEIRVANYPGLEKYQLIENLGDGAFSQVYKAYSIDRKEHVAVKVIRKYEMNKKQRQGVFKEVNIMRRVKHKNVVNLFDFVETEDFYHLVMELAEGGELFHQIVNFTYFSENLARHIIIQVAEAVKHLHDVCGIVHRDIKPENLLFQPIEYLPSQNYTPPSLEPNKLDEGMFLEGIGAGGIGRILIADFGFSKVVWNSKTATPCGTVGYAAPEIVNDELYSKNVDMWAMGCVLHTMLCGFPPFFDENIKDLASKVVNGEFEFLSPWWDDISDSAKDLITHLLTVDPRERYDIHQFFQHPWIKGESKMPENFTYKPKLHGTPGGPKLSLPRSLVSKGEIDIPTTPIKSATHPLLSSYSEPKTPGVSSVHEAMGVAYDIRRLNHLGFSPEQLSKKSMNTGSIKELILDEETTTDDDDYIISSFPLNDTLGSEGKDPFSLNLKESSLYSRRSAKRVN O42860 BUB3_SCHPO PTM: Phosphorylated by bub1. {ECO:0000269|PubMed:15509783}. SPAC23H3.08c; CHAIN 1..320; /note="Mitotic checkpoint protein bub3"; /id="PRO_0000234560" MNFSKTLLKNSKDGISSVIFSPSVKNELIAGCWDGSLLHYQISENPELLGKYDLSSPILSLEYTDEKTALVGNLDGTVTTLDLNTRNHEFLGNHGKGVSCISKLRLENCFISGSWDKSFRVWDVRVKQPVEGQDIGKKIFASSSRDNILVLGCSERENLVYDIRNLKLPFQRRPSSFKYMTRSVCCNQNFEGFVSSSIEGRTSVEYINPSQEAQSKNFTFKCHRQIQKDYDIVYPVNDLKFHPIHQTLATAGGDGVVAFWDIQVRKRLRVLNPSKINISSISFNVDGSMLAIATCAQEEAAGNIYVHALESNFAAPKLKS O42861 FFT3_SCHPO BINDING 412..419; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; MOD_RES 213; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 617; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC25A8.01c; CHAIN 1..922; /note="ATP-dependent helicase fft3"; /id="PRO_0000074383" MDGKRKIEHTADGTHYDATSNVKRKPIFPPFIADSLSEATEKANVMGGGMNSRLQILSEMSKRVQATAPISSLEHFKQLSDISPSFTSSANSINQPYNYSGSLENLVPTPSAGTPSQFMDAQNPYGAVYNALSQFSETEPKMPSYMDDEEASDSLPLSLSSQSLSSQVTNQKPAPHRLTMRERYAANNLTNGLQFTLPLSSRKTYEPEADDDSNDDMYSDDDSNADRWASRIDTAALKEEVLKYMNRCSTQDLADMTGCTLAEAEFMVAKRPFPDLESALVVKQPRPVIPKGRRGRREKTPLGPRLVGICMEIMRGYFVVDALIRQCEQLGGKIQRGIEAWGLSNTATSDEGETSLVNFDQMKSFGTPANSSFITTPPASFSPDIKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELYYGSQVEREEIRERINSNKDSYNVMLTTYRLAATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKKSPESDFERALLSEQRVSRAKMMMAPFVLRRKKSQVLDALPKKTRIIEFCEFSEEERRRYDDFASKQSVNSLLDENVMKTNLDTNANLAKKKSTAGFVLVQLRKLADHPMLFRIHYKDDILRQMAKAIMNEPQYKKANELYIFEDMQYMSDIELHNLCCKFPSINSFQLKDEPWMDATKVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESINVFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIALDATLSGNAETVEAEDDDD O42862 ATG14_SCHPO SPAC25A8.02; CHAIN 1..390; /note="Autophagy-related protein 14"; /id="PRO_0000304106" MLHVNKCQLCETRRPSICESCLKKQLYDFYHKRDEFSRDIESELEKVAKLKSESFSLKGKITQKEELTYRLQNLAASLNEKKSLSCDLHSRKQLIEDDLSNRKKSINIASQKLAGLSHSTSDYFSKEYLTAYRRSELLQNKLHEYQKKLITRVLDMYQLHWQRDLVLNTQGCTQKSAQMGSEFNPDSIDSSLAYRLSKLSMGNSKSDLSHSDNETGHFYSNFFSQVMELNASVTISGIPVCIRSKEKMFLNPDCALTLSFICIFLAQYTSIPLPCPLQLPSPDQKPMTSFSSEQMLYIMYNIVWISWNCGIFSFPRGITQSQLFELMQYTGFWLVQLRTKPLTSQKPDWHYKMGMDFDLFHRLYLARLPIPINYSSLRSRSSSKPYQLIS O42868 SSU72_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; SPAC3G9.04; CHAIN 1..197; /note="RNA polymerase II subunit A C-terminal domain phosphatase ssu72"; /id="PRO_0000255612" MAPKTNLQISVICASNQNRSMEAHNVLKNAGYQVDSFGTGSAVRLPGPSIDKPNIYQFGYPYDEIYKELEAQDSRLYTANGLLKMLDRNRRIKRAPCRWQDQDSIYNIVITCEERCYDAICEDLYRRGETLNRPVYLINVDIKDNHEEASVGGKAILDLVNKLTEAQDKLEELFPSIMADFQSNHPKLPVLYTIHFF O42872 RRP41_SCHPO SPAC3G9.10c; CHAIN 1..242; /note="Exosome complex component ski6"; /id="PRO_0000139961" MSHFEILSLEGLRNDGRRWDEMRNFQCRIGIEPSENGSAFIELGNTKVLCIVDGPSEPVIKSKARADRTFVNVEINIASFSTIDVKKRFKSDRRIQLQCLALQNTFEEIIQTELYPRSQISVYLHVLQDDGAVMASCINATTLALIDAGIPVKDFVCCSTAGIVESDMLLDLNSLEESALSWLTVAVLGNIKKVVYMQLETSMHLDYLESVMNMAIAGSEHIYNTMQSAVRQSAKPALASLS O42874 STU1_SCHPO MOD_RES 599; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1221; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G9.12; CHAIN 1..1462; /note="Protein peg1"; /id="PRO_0000272294" MADKDAQDFLKFLKSNASTDEKTRCLDTLRSFFNKNNIPNADLGLFVECFRLALTTVNPLLLRSSVACFETFLRRLRAQYPTWLKFRVPMLKNLVIDHIASRDLQKRVLNILIDLWHFNPSEIEKSLIHLSTTSKSAETRIQCFKWFVLAHNAHLSFDVKSLRPALYINLENANPSVREEAKEVLLLIYKNLSTSAKMQFITDVETTSGLRREILQSLVEELSLISSSSEVIIVQNSASSFQPAPFMTAVATLYPGVELENVKPLLANFSKQLEQDSASMLPAFEGRETEQNWSVRQDSVLRLRQYLRGNACIDYLPELLSVLKTLLPGILLALLSLRTTLSSSAIQLIKEMAIILKSNIDPFLELILPNLLKVCSVTKKLASQAANVTFAAILVNCGVLSRNLSFISLAAHDTNAQLRVFSSNWIFMLISLSPELKNLASLQTNLKAFEKLICRGLADSNSQVREVYRKSFWKLSEYFPSVQEELTNTLEPSVLKQLHLANPNRQAASFNFSGPKRAPIRPLSNLRSFSKSQKEETSSNSSNSSGTRRLGLPQRATPASRERVLPYTRSQAFHSTSLPPSLPSGHSPSIAIPSKRSVSATIKDESKTFELLKNIQRKYELILSGSSVDLPSAEFLSSNLTDALYSGSSICYSLIFSHSLLDLTFQYVDIASLLSQFLLCVYDPSNVGHSFALASFPYVKSHYDAHKYFPIVFDVLMNISNMAPHVKVFPFNTNQKRLIIHGCLLWLKEISDTKLNQLENKPFFVTDKLRYYSSKILAMTAKTKLTSKNWIPLSGLLFSLRAHDTFMFDGLLDRLNEESRTKLVSSWSKQDAFDYSKSSTHQEHLSKNLPTLNTSSSSNSSQTDLLVPHGKGETKETEMQSPIESKEGLLSKDTHIESPQGTSLEKENEEEGKNPVESNCSEESLDDHNIDQTLVNKKETLAQDSESLLQKNNALNEKGFENQFGLSSSAAKVLNKDTLDHVSGPISNSVSSSFKDFTRTPFKEINGERETGFELTSYVNALSKKDDINVQKTENVDESVGLNAMFMDNVNQDSLNSVDQSSGKDKLLLTSSTPNKPTTFFMPANEEILGSPAKDYDIHDQSYSVHELHSENMRENVGQSSLIYNNRDYMNTPMNDFSLSFSEIKGGILESPVESPMTGTISPIDADESVLHDIPAYESLNKSESNKYQEQAYSTPLHHTLNVLPKNKWILSRMHKMENGSPINVDKNLDDAVAALEAAVKELNDGSVNTKTLKFCIKVCKETPSMLYHSHGLLPAILHYIESNNSAMHISDCLILLHEFLVQGYQGVDMHTYHNIICILIEKAEKCKDEPVILAGIEDNITLIAEIADLQGLYEFTQQRLQSLNTETGEKSAPLLLMLLSAILMRLKDLEFLETKDLLRHVVLKYIDHTNPEIRKATFNVCLAVNTIVNNVDETFSILGGLNEGQRLLFMHYLKMKSDEKN O42893 TREA_SCHPO ACT_SITE 457; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P13482"; ACT_SITE 652; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P13482" BINDING 97; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P32356"; BINDING 99; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P32356"; BINDING 101; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P32356"; BINDING 103; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P32356"; BINDING 108; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P32356"; BINDING 283; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P13482"; BINDING 290..291; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P13482"; BINDING 327; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P13482"; BINDING 336..338; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P13482"; BINDING 336; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 455; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P13482" CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000269|PubMed:12153582, ECO:0000305|PubMed:12943532}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12943532}; MOD_RES 47; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 49; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 50; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC660.07; CHAIN 1..735; /note="Cytosolic neutral trehalase"; /id="PRO_0000173797" MPSKFSSKYVDTEAISNDDDNPFATAKSYYSKDTDLSTRVSAGRPRTLSTSMEASAAPTIPELKNLRRRGSLDEHKQPRKFLVDVDKTLNALLESEDTDRNMQITIEDTGPKVVSLGSASSGGYRLYELRGTYQLSNLLQELTLAKDYGRRYILLDERRLNENPVNRLSRLIKGTFWDALTRRIDASVLDVICRDTKDRSGSHVNRIYVPKAEQEMYEYYVRAAKERPYLNLQVEYLPEEITPEWVRDVNDKPGLLALAMEKYQDDEGNTHLRGVPFVVPGGRFNELYGWDSYFESLGLLVDDRVDLAKGMVENFIFEITYYGKILNANRTYYLLRSQPPFLTDMALRVYERIKNEEGSLDFLHRAFSATIKEYHTVWTATPRLDPKTGLSRYRPGGLGIPPETEASHFEHLLRPYMEKYHMTLEEFTHAYNYQQIHEPALDEYFVHDRAVRESGHDTTYRLEKVCADLATVDLNSLLYKYETDISHVILEYFDDKFVLPNGTIETSAIWDRRARARRAAMEKYLWSEADSMWYDYNTKLETKSTYESATAFWALWAGVATPRQAAKFVDVSLPKFEVAGGIVAGTKRSLGKVGLDNPSRQWDYPNGWSPQQILAWYGLIRYGYEEETRRLVYRWLYTITKSFVDFNGIVVEKYDLTRPVDPHRVEAEYGNQGVNIKGVAREGFGWVNASYEVGLTFCNSHMRRALGACTTPDVFFAGIKEESLPAFENLSIHKN O42900 PPK19_SCHPO ACT_SITE 146; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 30..38; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 52; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 957; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 958; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC119.07; CHAIN 1..1706; /note="Serine/threonine-protein kinase ppk19"; /id="PRO_0000256820" MGIQLSTIQTPQFHELFEEELPEYHNERSLGDSHFLRTFRMQDRKGYDVLIKVFVNKLPEISLSSIVNLLKEEQENISYRVPNAVPYIKTLVTLRAAYLVRPYVTHNLYDRISTRPFLELTEKKWIMFQLLKGISDCHRLGVCHGDIKSENILITSWNWAYLSDFSSFKPTYLPEDNPADYGYFFDTSSRRVCNIAPERFVPASQLQPAPLSPAMDIFSLGCVFAELLLEESPLFTLSQLFSYKAHGSYDLQSVLEQIEDKSTQNMILSMLDRDPSQRLSADAYLQKYRGTVFPACFYDTLYDYCIGLVDPSGILSAKQPNDACSLYGSRIDDIYRDIMPPNNNDISNLMHTPHEYNGIDSYSVPLFTTLDEFYNKNPAAKNWYLRLYNTMQEKKGFEDKEQGSTPAPSPSVIEDISSIETDENHLYGAAVLLPIVLSTIRHVNTRESKINALSLVQILSRNICDESKLDTVLPFVMTLLRDQYADVRISALITITRLVSNVTSIAPINAFLFQEYLFPDLQHFLFDMNSRTRATYASCLPILAKQASKFLNLAQSLRNAGILSFPESEYENINHGKAELLFETGRHDLVVTVERHVSTLLADSSSIVRRSLLNALAPLCVFFGKAKSNDLILSHLITYLNDTDWMLRCAFFESITGLSIFIGPRSVDEYILPLMLQALVDPEPAVLESVLGSFSGLIELHLFEKLVVVDILQLVLPLVAVPNAYIRRAALSVIYSAYQSFDDIDRDCIVTPLLRPYLMSNLCDINSLEKLDQFILPMVSDSVWSTLTRWYEESENSSFWKCDKDASYSSLDVSNDSLLGRTKNLQKREIMHHAEVYTHKKISLTGHVIITSTEMLELSEDDQKWADIIKEMGVDVKHLWVLANLRDYVKKTKINLNGINYKRQSGLRELNTYPNAPLHILPETIFWNPERPPSSSIANETFLDRNSYAESIQTSRSYNDDLIARDPIAYVGTDMTNAFGTTTKPKDVSQSDIKVDINRESNSDNGETITGTHDVYRQTDNPEIKLPSDTASSKVDTHNPTVTQPTDDTGGLNSYNTENPLLTNNTLEPSSVEAIVSSKDSDKHAKESKGKSLAPLISSRVSTNDTTNVAGIRSQRSFTTHIDLKKLTTRQNGAKKSSYTGTNPCVLNYLNKIYAEAAASTLNVGAAVSPSWASNIPLRRRTKVSAKAANKIVQTHEWHPEGSRVAQIYLGSLLDGGTKKVLVSPDSSFFVTLGSDGVVRAWQLVESVRHISTMRCECRLSYGHTRRNGERNRFSVVNGCFLGNTYAFASVTQDGSVEVHRLDVNNQRHTLISAGRIPNLDFSDSVTSMEASTFHDGSIRLVVVTKWSRIVYLDVGMMRVLSSDQLPLQCGSATSVVVSEGCNWALIGTTKGWLLLWDLRFGTLSCSWHMPARIDQMHLLLDVTKKRSNVNEYTSGNNNSPVTKVPGSSSTSSSSTQPINSTIPINPLENHGMLNSFGSTTVSISFSVLTNLDNKEVNLEDAVPASHRSASGIVNFDVEKGKTEEVFLENWNSSLTSPIPVSVGIDAFNEKKKFDIDSGNDMGLRDLNTKFDSPWPCISSPIYRYRGPSAGSVEREPLFLIAASGSPHAFIWNPHNVSASSSVTNDSESSKLSLIHNKPPIYQKVSEQQNVRPKSSGVSRPLLFLQQQKNLPSENRLHPIVDMAFLYQPYAIVLIVDAFGSLELWT O42916 ALE1_SCHPO ACT_SITE 363; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16A3.10; CHAIN 1..509; /note="Lysophospholipid acyltransferase"; /id="PRO_0000315633" MAYLIDIPFEYFSSFLGVHPDQLKLLFCFLSAYPFAGILKRLPSAPWIRNLFSISIGLFYLIGVHHLYDGVLVLLFDALFTYFVAAFYRSSRMPWIIFIVILGHTFSSHVIRYIYPSENTDITASQMVLCMKLTAFAWSVYDGRLPSSELSSYQKDRALRKIPNILYFLGYVFFFPSLLVGPAFDYVDYERFITLSMFKPLADPYEKQITPHSLEPALGRCWRGLLWLILFITGSSIYPLKFLLTPKFASSPILLKYGYVCITAFVARMKYYGAWELSDGACILSGIGYNGLDSSKHPRWDRVKNIDPIKFEFADNIKCALEAWNMNTNKWLRNYVYLRVAKKGKRPGFKSTLSTFTVSAMWHGVSAGYYLTFVSAAFIQTVAKYTRRHVRPFFLKPDMETPGPFKRVYDVIGMVATNLSLSYLIISFLLLNLKESIHVWKELYFIVHIYILIALAVFNSPIRSKLDNKIRSRVNSYKLKSYEQSMKSTSDTDMLNMSVPKREDFENDE O42917 ESO1_SCHPO BINDING 540; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"; BINDING 543; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"; BINDING 555; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"; BINDING 559; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01255" SPBC16A3.11; CHAIN 1..872; /note="N-acetyltransferase eso1"; /id="PRO_0000173994" MELGKSKFSWKDLQYCDKAGTQNSPLRVVAHIDQDAFYAQVESVRLGLDHSVPLAVQQWQGLIAVNYAARAANISRHETVTEAKKKCPELCTAHVKTWKAGESEAKYHENPNPNYYKTCLDPYRHESVKILNIIKKHAPVVKKASIDECFIELTSDVKRIVLEEYPYLKIPSEDSNVALPQAPVLLWPAEFGMVIEEEVVDRTKEDYERDWDDVFLFYAAKIVKEIRDDIYLQLKYTCSAGVSFNPMLSKLVSSRNKPNKQTILTKNAIQDYLVSLKITDIRMLGGKFGEEIINLLGTDSIKDVWNMSMDFLIDKLGQTNGPLVWNLCHGIDNTEITTQVQIKSMLSAKNFSQQKVKSEEDAINWFQVFASDLRSRFLELEGMRRPKTICLTVVSRFLRKSRSSQIPMNVDISTQFIVEATSKLLRQLQQEFDVYPISNLSISFQNIIEVDRNSRGIEGFLKKSNDEIYMSTSVSPSIEGRAKLLNENMRENNSFELSSEKDIKSPKRLKRGKGKGIFDMLQQTAVSKPTENSADETYTCEECEQKITLSERNEHEDYHIALSISRKERYNNLVPPSHDKPKQVKPKTYGRKTGSKHYAPLSDETNNKRAFLDAFLGNGGNLTPNWKKQTPKAISNSSDNMTQLHLDLANSTVTCSECSMEYNSTSEEDILLHSRFHSRVLGGVTVSFQCSPIYRVNYGLSSDCIYSINSESSLIDQRKAEEALSFVNNELSSEPIETIGVDKYTTFLFISDKKCVGLLLAERISSAYIVDELELNNNNSTSSAVYIKNENLRKGFVLGISRIWVSASRRKQGIASLLLDNALKKFIYGYVISPAEVAFSQPSESGKQFIISWHRSRNNGSSKSLRYAVYES O42930 VPS10_SCHPO SIGNAL 1..33; /evidence="ECO:0000255" SPBC16C6.06; CHAIN 34..1466; /note="Vacuolar protein sorting/targeting protein 10"; /id="PRO_0000316211" CARBOHYD 465; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 545; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 986; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFFLTKILPLRGRIFPMFGCLLLIVSLITGCIASPAAEVAETVFDSKPVDFMTFKDSTNTLFLNAEFGDVYLSQDNGQSWRNGVISGQVCPIKKLIKHSFENSRVFALTECDTVYYSYDNGENWDYFTIDHPISITQLPFHFHAKNPDYVIFNNQYCSSSGTWVGKICKPDLYYTKDGFQSDPEPMPVGSSYCIFADSSEKMVVSSEEQIICISLNPNSAARPPFSHHIVYSDDWFQSIVPVQLHNFLGSDGAYGILSTGSFLVAALIDAATRKLFVYVSQDGYYWEEALKFHKGFEFDAFTILPSTEYSFFIDSLDSHPNNPTGILYSLDSESNTFVIRQMNTNRYVDGYTDFMLIDYLDGLQFVNVVENVDEIEVDPQVDKVLSSRITFDGGKTWSTVASPESSCNSMKQCSLHLFLDPHVSHASIASSKFAPGILLASGSVGDRLLSENQMDLFVSEDGGRNWTLSRDGMHLFAMSGFGSIFFASEYLDVINEVYYSLDHGQSWVTVTLDKTIVPIKLFASEDPYAEIFYLLAMTDDGEQSNYSLFSFNFGKFLPKECQFSNSESNKNDFEKWYTRYANGSPICSEMGKKEFFWRKKATSVCSVPKSITDLHGSFDACECTDEDYECNTQFISNDQGECKLLDFIGSLLCASEDLDTFQKIPYRLVPGNKCTPNKRDSHREPQTFNCDSFNEPGTEITSFLYDFDEKIVDVVYLEGTVPEENTFLIGISVNSHVYFSEDEGKTWDKFSKEEFSSVLPHAYNKNSVYMVTSKNIVYFTTNRGKNFYKFKAPSPPNQNGKSLFSFHPSRPAWLLYAGSENCEKNPFADDCRDVVFVSLDFGDTWSRLPSNLEYCSWAKAEKLVVDDTLIFCIRQNTNDPFKKELISSIDFFEYEQDEILNDVVGFMIEDEYVIVAVQDEEGTSLSLDVSINGLNFASCSFPAYLNVHPKQAYTILDSQTHSLFIHVTTNTHLGSEWGDILKSNSNGTYFMTSLANVNRDSVGYVDFERLEGIQGIALANIVSNTKELTDGGTKKLQTLITFNDGLDWSYLNLVGGEKIVPKCGKNCYLHLHGYTERNQFSDPTSTNAAVGLIIGVGSFSPFLIPYEESQTFISRDAGVTWYRIFDSPHLWAFLDSGSIIIAVESISPTNVIKYSADEGRTWQEYQFSEKSKVVVDVSTKPSGVGHQVLLLTTDDENAPISSVLIDFDALYRRTCVFDEENSEESDFVRWVPTDISGKPLCLRGRISSFYRKSIHKKCRVGSSLLVKEEVLSKCECTRADFECDYNYRRLKDGTCVLVSGLQPPDTREEQCSVDDAFEWRQPTGYKRTPLTECEGGVPLDAGTLHPCPGKEDDYYKAHPKPGGWSIFLTIIFSILLAAVAGCILYYYSRRFLKGAIRLGSDSATENPLESGISYTRGAFSSIPIFFSALYQSVRSLFIRSTPTNGEFENAAFLQNYEIDDDDEESV O42934 CHP2_SCHPO SPBC16C6.10; STRAND 328..336; /evidence="ECO:0007829|PDB:6FTO"; STRAND 342..348; /evidence="ECO:0007829|PDB:6FTO"; STRAND 353..357; /evidence="ECO:0007829|PDB:6FTO"; STRAND 377..379; /evidence="ECO:0007829|PDB:6FTO" HELIX 358..364; /evidence="ECO:0007829|PDB:6FTO"; HELIX 366..374; /evidence="ECO:0007829|PDB:6FTO" TURN 325..327; /evidence="ECO:0007829|PDB:6FTO" CHAIN 1..380; /note="Chromo domain-containing protein 2"; /id="PRO_0000080239" MVKSADLDLMNSIISESDENFSPPPFTVEEAENSINNKSSTASLESPQNGSWHPSLYGLSVPEKTHIQNSLDLYSHGNSGSQKTHNVSFSCEIRKVKSSKLSPISNMEDSEDKKEEDESSSYKNEFKSSSSASVSSNFEKTSGSDDHNSQSPVPLNEGFEYIASSGSEDKNSDEEFAVEMILDSRMKKDGSGFQYYLKWEGYDDPSDNTWNDEEDCAGCLELIDAYWESRGGKPDLSSLIRLTRSRARSSNEASYVEKDESSNSDDSISYKRRRSRNAANRITDYVDSDLSESSMKEKQSKIEKYMKSDKSSKNFKPPFQKKSWEDLVDCVKTVQQLDNGKLIAKIKWKNGYVSTHDNIIIHQKCPLKIIEYYEAHIKFT O42938 PFKA_SCHPO ACT_SITE 345; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184" BINDING 204; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 267..268; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 297..300; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 298; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 343..345; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 380; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 387..389; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 444; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 472; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 478..481; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 655; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 712..716; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 750; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 757..759; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 817; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 843; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 849..852; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184"; BINDING 918; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /ligand_note="allosteric activator; ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03184" CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11015725}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.025 mM for ATP (without effector) {ECO:0000269|PubMed:11015725}; KM=0.027 mM for ATP (with 2.6 uM fructose 2,6-bisphosphate) {ECO:0000269|PubMed:11015725}; KM=0.63 mM for fructose 6-phosphate (without effector) {ECO:0000269|PubMed:11015725}; KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP) {ECO:0000269|PubMed:11015725}; KM=0.17 mM for fructose 6-phosphate (with 2.6 uM fructose 2,6-bisphosphate) {ECO:0000269|PubMed:11015725}; PTM: The N-terminus is blocked. MOD_RES 43; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 45; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 167; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 171; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 175; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 600; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 602; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16H5.02; CHAIN 1..942; /note="ATP-dependent 6-phosphofructokinase"; /id="PRO_0000112043" MSGETVHGISCYSVVANTEDTYNQTLDFYQKLGFKKVASFGTSDSDNARVCNESLREDWMHVAGNNSAESVTIKFRLVPGELSLSPAAEDSEWRGQKSSLVFYYPNLLDLLKQLSADAIKYQAFPNEKKPDEVYVEDPLGNLIGFSDRYNPFAHANLKKSEESGAASNLESGLATPVVETLKKATTSDKPAGVKKKIAVMTSGGDSPGMNAVVRAVARIAIHRGCDAFAIYEGYEGLVQGGDMIKQLQWGDVRGWLAEGGTLIGTARCMAFRERPGRLRAAKNLISAGIDSIIVCGGDGSLTGADIFRSDWPGLVKELEDTKAITPEQAKLYRHLTIVGLVGSIDNDMSSTDVTIGAFSSLHRICEAVDSISSTAISHSRAFIVEVMGRHCGWLAVLAALATGADFVFIPERPAEVGKWQDELCNSLSSVRKLGKRKSIVIVAEGAIDSELNHISPEDIKNLLVERLHLDTRVTTLGHVQRGGIPCAYDRMLATLQGVDAVDAVLASTPDTPSPMIAINGNKINRKPLMEAVKLTHEVADAIEKKQFAHAMELRDPEFADYLHTWEGTTFIEDESHFVPKDERMRVAIIHVGAPAGGMNSATRAAVRYCLNRGHTPLAIDNGFSGFLRHDSIHELSWIDVDEWCIRGGSEIGTNRDTPDLDMGFTAFKFQQHKIDALIIIGGFEAFTALSQLESARVNYPSFRIPMAIIPATISNNVPGTEFSLGCDTCLNAVMEYCDTIKQSASASRRRVFVCEVQGGRSGYIATVGGLITGASAIYTPEDGISLDMLRKDIDHLKATFALEAGRNRAGQLILRNECASKVYTTEVIGNIISEEAHKRFSARTAVPGHVQQGGNPTPMDRARAARLAMRAIRFFETCRANDLGNDPSSAVVIGIRGTGVSFSSVADVENNETEIEMRRPKNAWWRDMHNLVNILAGKTFAD O42995 MIS19_SCHPO SPBC27B12.02; STRAND 58..62; /evidence="ECO:0007829|PDB:6S29" HELIX 79..97; /evidence="ECO:0007829|PDB:6S29"; HELIX 104..111; /evidence="ECO:0007829|PDB:6S29" CHAIN 1..112; /note="CENP-A recruiting complex protein mis19"; /id="PRO_0000116509" MDLMPLEKARAIEIAFDNVFHNTKIPDNLQQFDAILKRLERRRFIPTENQKPRVYETELLVLRFREFGVKDNHNHPINLHSLRSKSLIRAQGKKLDLHNRVFLRRNVRAVKM O42998 SIP1_SCHPO MOD_RES 45; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 48; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27B12.08; CHAIN 1..1919; /note="Pof6 interactor protein 1"; /id="PRO_0000372352" MSLASLPLEKLTKVADVDKRETIYIDLLNYEKQLRNLNKNTREDSLQTNLNPLLSLIKKYGNFIAYPTRKLLSNCIIALLKGLEGYHQHRVLLYFVDSIHEKKDYIEIINVLSVLTSCLEEYGNQINQQETFIRFFFKYSKTNLSYGVRSIALDGLSKCIETSIQSTNEDLIKEIWKCIKSNLNTSSTNVLLSALRCAYYILGSSRLRNSELEWFKSFLFKKSSIDNSLLHSSLGRCFSALASAQADKSIEAAANAVPSTPADDENNEEVENRSTTRRFDETESFRHALRILVENYHSKHAKYESSKAVLVFAVKHLFLMQRPSFVSLNYTTIVDIILLHQSHSTSKEWLSSLEQYHCTYLFRDVIGRRFLDQSSELQGIEILLKRVLEPYLKDQSKISEIAVKTAMASTADILSRSKGSATALYSQLLDTTLQILYLGKDSLKNEVAWLLRCLLSVMPSPLMPTLLALFNRLELEFKHLRSKPKEVSPKLNVGIFNNLTLSLMSIYVAAEENPLYVASSIFSKLFNFSLDLIKSSSKLDLLAAQAQIKTGWRLLSAYVSFGPSFTRMQLSQLLILWKNALSRVPSKIHSQNFMETNADMFNRFEALQCLLSFLEYNKILFTPDVRKRVIIFLNNCLKFYKAFSLTKRLEITMPIPASDYSHLELRSLLLARIFQCFFELSQLSGMSLDDQELLSTTVSTIAELSSLQGYDTADEIVQAKAFTSPRVIPGIGSRFYAQPEEEFQTTMDDILPCYICESSSDSLSVISRSNSAKLPYVPPSLTSLIDNAIQLFASMFCHQPPKVMESTLEIMVASVTNLKSGRDILRYKAVTANTLFSIYGFLSAFDNKKVTLPDKVVSLMIELLENLTAVNDPKLIPYISKSYAFLAYLYQSKPTSVLDTIIKRAAESGDPNCRAVLILAVGHILKKVGSGVPQTTLITAYQLLKVFNTDSNDLVRECSIRASSVSLGSIAKTIPSVLTAQTRILLSYMLLPECDIDVQLLKKRNSLFFPSTLFANYLDCLINELGPNLRSDSSTSHFAFDLAHQLLLLSRDTGDNIIHVYKCYQHLYLFTPLETNSDFFIRELCGNIIDLKQPKRREISIEVLYQILLQNHEFSESCYKRHFDRLIWQSLDTTPDNKLLKNILYIWLNDYKDSDIHSWVNILLFLVGIKNTSSSERSNEQDIQNNLDEDTVSLAYGTSENASNPLFQKNYRWQTQFYAATCLKTCISEVMAENKEPAKYLISRISDLVRAAFVLSTSDNFYLKQGGFELLDTIITDFSNVMDPDFDDVSLLDQFQAQISSAFSSAFVDDSSPEIVAMSLNIASNFIGTGLLKTESQAAKILNLLKEALESSLPERAGFEENRHFKYDSKYFLRIATLSAWASLLVHSANVSYLKEFLSSNIRRLSSHWIMALRGYSRLQFGPSLVKDFVADTSFTRVQSINPKILLNIYEKSWLNIAESLTILLSTDANLIYGILSGDELSLSEEDVFFQDNINYASNRYSFNFFLFSVCFQSLLIPSTLQGFRNPVFRIMRIMTEVLTEELCTKVLYDHNVFPEVVDLLVRLILTEDWETKASIVIFVKKLALANPAHNDLKFCETDSVTSMEPTVSESVEMLFQLVKILTLALTVRVPGLRSDPAESATNKKASEFVILCFNAFLDVSNIFPAIVRVDLFATAMHVYEVIMDDQQLLKNSKQELLAALRKLLSTMVEQNDHTCTTLIYTLFEHLLNIYKETINDSDKKEKNETAFMSMVLVLTLAAPILDSEQLVVHDFLEELFSSLKSSEEDFALRTRCVTSLMLVNSKHPSMSALCRFIIYKSVTMLQNGEVLKSGDYVTEFIPALLDMHVHIPEEKKKSFLSMSIPIAAHFSILVEHADARKRIGEKLLKIMAIQPDEAKAIIQQLSPRQKKCVEEILIQNVE O43001 SYJ1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000269|PubMed:11348594}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15316017}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57.8 uM for Ins(1,4,5)P3 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=10.9 uM for Ins(2,4,5)P3 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=75.9 uM for Ins(2,4)P2 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=5860 uM for p-nitrophenyl phosphate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=182 uM for 3-O-methylfluorescein phosphate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=530 uM for magnesium ions {ECO:0000269|PubMed:15316017}; KM=12 uM for manganese ions {ECO:0000269|PubMed:15316017}; KM=6.39 uM for nickel ions {ECO:0000269|PubMed:15316017}; KM=14.5 uM for cobalt ions {ECO:0000269|PubMed:15316017}; SPBC2G2.02; STRAND 553..566; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 583..585; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 589..596; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 635..643; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 646..653; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 660..669; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 680..688; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 691..699; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 731..740; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 745..747; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 778..780; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 816..823; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 825..831; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 836..839; /evidence="ECO:0007829|PDB:1I9Z"; STRAND 842..853; /evidence="ECO:0007829|PDB:1I9Z" HELIX 536..547; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 548..551; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 577..580; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 611..627; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 654..659; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 707..720; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 724..726; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 749..757; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 761..765; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 769..775; /evidence="ECO:0007829|PDB:1I9Z"; HELIX 855..876; /evidence="ECO:0007829|PDB:1I9Z" CHAIN 1..1076; /note="Inositol-1,4,5-trisphosphate 5-phosphatase 1"; /id="PRO_0000209736" MQCLLREKPRSLALVNKDHALMFHSVPQNKNSLSVCVAEFTALSEKPLEGFRKISSHRIYGTLGLIELEGSNFLCVISGASEVARVRDKERVFRIMEVCFYSVNRSNWDHIRQENYSPDIPDGYDTDTQGYDSYKYAAEPFSSLRKLLTNGSFYFSLDFDITTRLQLRTSQTMTEPQYDSMHTQFMWNEFMLRQLIKFRSHLNGDEKSALDGCRFFTCAIRGFASTEQFKLGIQTIRLSLISRLSSLRAGTRFLSRGVDDDGNVANFVETETILDSSKYCVSYCQVRGSIPIFWEQEGVQMFGQKIDITRSLEATRAAFEKHFTSLIEEYGPVHIINLLGTGSGERSLSERLRQHIQLSPEKDLIHLTEFDYHSQIRSFEDANKIRPMIYSDAETFGFYFENNEGQSIVVQDGVFRTNCLDCLDRTNVIQNLVSRVFLEQVMIYTRQNAGYDFWQVHSTIWANNGDALARIYTGTGALKSSFTRKGKLSIAGALNDLSKSVGRMYINNFQDKGRQETIDLLLGRLIDQHPVILYDPIHEYVNHELRKRENEFSEHKNVKIFVASYNLNGCSATTKLENWLFPENTPLADIYVVGFQEIVQLTPQQVISADPAKRREWESCVKRLLNGKCTSGPGYVQLRSGQLVGTALMIFCKESCLPSIKNVEGTVKKTGLGGVSGNKGAVAIRFDYEDTGLCFITSHLAAGYTNYDERDHDYRTIASGLRFRRGRSIFNHDYVVWFGDFNYRISLTYEEVVPCIAQGKLSYLFEYDQLNKQMLTGKVFPFFSELPITFPPTYKFDIGTDIYDTSDKHRVPAWTDRILYRGELVPHSYQSVPLYYSDHRPIYATYEANIVKVDREKKKILFEELYNQRKQEVRDASQTSYTLIDIAGSVAGKPNLIPHLPANGVDKIKQPSSERSKWWFDDGLPAKSIAAPPGPEYRLNPSRPINPFEPTAEPDWISNTKQSFDKKSSLIDSIPALSPAPSSLARSSVSSQRSSTSIIPIKPNKPTKPDHLVAPRVKPLLPPRSGSSSSGVPAPNLTPVNVPPTPPPRKSSASQRSGDLLASSPEESSISWKPLV O43007 C1TM_SCHPO BINDING 84..88; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P11586"; BINDING 131..133; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P11586"; BINDING 202..204; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P11586"; BINDING 227; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P11586"; BINDING 299..303; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P11586"; BINDING 405..412; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616" CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000250|UniProtKB:P09440}; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000250|UniProtKB:P09440}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; EC=6.3.4.3; Evidence={ECO:0000250|UniProtKB:P09440}; TRANSIT 1..55; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC2G2.08; CHAIN 56..972; /note="C-1-tetrahydrofolate synthase, mitochondrial"; /id="PRO_0000315627" MNVMVSFNQLRNYFLESNSLRPSKWLFQSYGTSSSANILNGKLLARKLQRSVAEEVQALKAKDRNFKPALAIVQVGKREDSNVYVRMKEKAARLVGIDFKYCPFPETIQMPALLHELKKLNDDHTVHGVLVQLPLPKHLNERTVTESITPPKDVDGFGAFNIGLLAKNDATPIHYPCTPKGIMELLKDNKISVAGLNAVVLGRSDIVGNPISYLLRKDNATVTVCHSKTKDLIQHISNADLVIAALGKPEFVRGEWLKPGSVVVDVGINAVQRNGKRVLVGDVHFESASKVASSITPVPGGVGPMTVAMLMENIVNAAKIARTENIYRKIDLNPLELKKPVPSDIEIANSQEPKLISNLAKEMGIYDTELENYGNYKAKVNLAVYERLKHRKDGNYVVVSGITPTPFGEGKSTVVAGLVQAMGHLGKLGIACVRQPSQGPTFGVKGGAAGGGYAQFIPMDDFNLHMTGDIHAVTAANNLLVAALETRMFHENTQSDAALIKRLIPVKNGRRVIPRGLIGRWNRICASHNMDPEDVNNASPELLKEFVRLNVDPDTIECNRVLDVNDRFLRSIEVGKASTEKGHVRKTSFDISVASECMSILALSCDLNDMHSRLSRMVIANDKYGNAITAGDLGVSGALTVLLKDAIKPNLMQTLEGTPAFVHAGPFANISIGASSIIADKIALKLAGTESFDRPEDAGYVVTEAGFASDMGMEKFFNIKCRYSKLVPNTVVLVTTVKALKLHGGGPKLKPGAPIPEEYLVENLDLVKNGCSNMVKHIQNCHKFNIPVVVAINSYKTDSSKEHEIIREAALQAGAVDAVPSDHWAQGGKGAIELAKSVMTACDQSSNSKFRLLYDSETSIEDKVNVIAKEMYGANGVEFSSLAKERINTFIKQGFGNLPICMAKTQYSLSHNPEFRNVPKNFTVPIRDMRLNAGAGFIYPLAAEIQTIPGLPTAPAYLNIDICENGEIVGLS O43029 FAP1_SCHPO CATALYTIC ACTIVITY: Reaction=L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-carboxylate; Xref=Rhea:RHEA:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58769, ChEBI:CHEBI:61185; EC=1.5.3.7; Evidence={ECO:0000269|PubMed:16233628}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16233628}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.07 mM for L-pipecolate {ECO:0000269|PubMed:16233628}; KM=33.5 mM for L-proline {ECO:0000269|PubMed:16233628}; Vmax=46.1 umol/min/mg enzyme for L-pipecolate {ECO:0000269|PubMed:16233628}; Vmax=9.45 umol/min/mg enzyme for L-proline {ECO:0000269|PubMed:16233628}; SIGNAL 1..20; /evidence="ECO:0000255" SPBC354.15; CHAIN 21..412; /note="L-pipecolate oxidase"; /evidence="ECO:0000255"; /id="PRO_0000347274" CARBOHYD 105; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 142; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVKNTSVIIVGAGVFGLSAALELTKRGGYTIKILDRAPPPVIDGSSVDANRIIRSDYADAVYCSMGIDALEEWRTNPLFKEQFYGSGLMFVGRDNVEYRDMSLENLTKMGVSAAKFQTTEELRKLFPKWIGELNDGEAGYANFSSGWANAEQSVKSVVNYLAHAGVSFISGPEGTVEELITEENVVKGVRTTTGAYMAEKLIFATGAWTASLLPNDHTRFLATGQPVAYIKLTPEEYIRFLTNPVYLDFDTGFYIFPPTPDGYLKFARHGYGFTRMQNLKSGKVESVPPKKPLVSPILPKEAELDLRRNLQRTYGEEISQRPFYKTRICYYTDTADAEFVFDYHPDYENLFVCTGGSGHGFKFFPILGKYSIGCMFRELEEPLLKKWRWKKENLEFAALDHSRAGPSRQELS O43035 ATG3_SCHPO ACT_SITE 227; /note="Glycyl thioester intermediate"; /evidence="ECO:0000250" BINDING 1..10; /ligand="1,2-diacylglycero-3-phosphoethanolamine"; /ligand_id="ChEBI:CHEBI:57613"; /evidence="ECO:0000250" SPBC3B9.06c; CHAIN 1..275; /note="Autophagy-related protein 3"; /id="PRO_0000213584" MAQRLTSAFLNWREHITPASKTSDFENTGMISPEEFVLAGDYLVSKFPTWSWECGDRIRGFLPKDKQYLVTRHVFCVQRNINIGVNEEWVDIETDDTRNKDDDQDDDAISSIHSDTSDIASAERLKGQSKELSDSGPLPLKDEEDDDQMVSPVIKEDEGRYYDLYIVYDKYYRTPRLFLRGWNAGGQLLTMKDIYEDVSGEHAGKTVTMEPFPHYHSHNTMASVHPCKHASVLLKLIKQHRERNDPIRVDQYMVLFLKFVSTMLPYFEIDYTIQA O43043 SCAP_SCHPO SPBC3B9.15c; STRAND 569..573; /evidence="ECO:0007829|PDB:4YHC"; STRAND 585..589; /evidence="ECO:0007829|PDB:4YHC"; STRAND 598..603; /evidence="ECO:0007829|PDB:4YHC"; STRAND 609..614; /evidence="ECO:0007829|PDB:4YHC"; STRAND 619..623; /evidence="ECO:0007829|PDB:4YHC"; STRAND 628..633; /evidence="ECO:0007829|PDB:4YHC"; STRAND 644..647; /evidence="ECO:0007829|PDB:4YHC"; STRAND 651..657; /evidence="ECO:0007829|PDB:4YHC"; STRAND 659..666; /evidence="ECO:0007829|PDB:4YHC"; STRAND 671..677; /evidence="ECO:0007829|PDB:4YHC"; STRAND 686..692; /evidence="ECO:0007829|PDB:4YHC"; STRAND 697..699; /evidence="ECO:0007829|PDB:4YHC"; STRAND 701..709; /evidence="ECO:0007829|PDB:4YHC"; STRAND 712..721; /evidence="ECO:0007829|PDB:4YHC"; STRAND 726..735; /evidence="ECO:0007829|PDB:4YHC"; STRAND 740..747; /evidence="ECO:0007829|PDB:4YHC"; STRAND 752..758; /evidence="ECO:0007829|PDB:4YHC"; STRAND 763..769; /evidence="ECO:0007829|PDB:4YHC"; STRAND 772..777; /evidence="ECO:0007829|PDB:4YHC"; STRAND 791..795; /evidence="ECO:0007829|PDB:4YHC"; STRAND 800..804; /evidence="ECO:0007829|PDB:4YHC"; STRAND 806..813; /evidence="ECO:0007829|PDB:4YHC"; STRAND 818..824; /evidence="ECO:0007829|PDB:4YHC"; STRAND 834..839; /evidence="ECO:0007829|PDB:4YHC"; STRAND 841..843; /evidence="ECO:0007829|PDB:4YHC"; STRAND 846..858; /evidence="ECO:0007829|PDB:4YHC"; STRAND 864..869; /evidence="ECO:0007829|PDB:4YHC"; STRAND 876..886; /evidence="ECO:0007829|PDB:4YHC"; STRAND 899..902; /evidence="ECO:0007829|PDB:4YHC"; STRAND 909..914; /evidence="ECO:0007829|PDB:4YHC"; STRAND 919..922; /evidence="ECO:0007829|PDB:4YHC"; STRAND 926..939; /evidence="ECO:0007829|PDB:4YHC"; STRAND 992..1002; /evidence="ECO:0007829|PDB:4YHC"; STRAND 1007..1018; /evidence="ECO:0007829|PDB:4YHC"; STRAND 1027..1031; /evidence="ECO:0007829|PDB:4YHC"; STRAND 1034..1039; /evidence="ECO:0007829|PDB:4YHC"; STRAND 1042..1049; /evidence="ECO:0007829|PDB:4YHC" HELIX 580..584; /evidence="ECO:0007829|PDB:4YHC"; HELIX 635..637; /evidence="ECO:0007829|PDB:4YHC"; HELIX 782..784; /evidence="ECO:0007829|PDB:4YHC"; HELIX 796..798; /evidence="ECO:0007829|PDB:4YHC"; HELIX 904..906; /evidence="ECO:0007829|PDB:4YHC" TURN 624..627; /evidence="ECO:0007829|PDB:4YHC"; TURN 667..670; /evidence="ECO:0007829|PDB:4YHC"; TURN 814..817; /evidence="ECO:0007829|PDB:4YHC"; TURN 859..861; /evidence="ECO:0007829|PDB:4YHC"; TURN 873..875; /evidence="ECO:0007829|PDB:4YHC"; TURN 895..898; /evidence="ECO:0007829|PDB:4YHC"; TURN 1003..1006; /evidence="ECO:0007829|PDB:4YHC" CHAIN 1..1086; /note="Sterol regulatory element-binding protein cleavage-activating protein"; /id="PRO_0000315874" CARBOHYD 94; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 168; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 454; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRIFTLGKGRISRGYARQVNPSLFAKYSYCIANNPWYFILVFTLLSITGIYSSLVAYQQSLYDQSLARWSAWYAESINAEANVITKQLYLLGTNTSVFSEDYLSNAYRWETSFHQYLAEYGYPCIRDEKSCVTISPIPKYYGKVDPVAQYSYTKGLPENEREVNKLRNDTIAEGFDSLSAFVITYFLKPEQVDTFHVVLKKFISETPNLYASLLDTSPTTVVARIPDLTVIYRWYLWVGFGVGLFAYLYLSLVRLHDIRAKFGLTATIFIQSGTAYFSTCSLLYFFERTGPICPWPMAYYIIIFMDIENSFRLLRAVIASPQTKRVPSRIMEGFSSTIIASFSSLLKKLLTLFVLSFFVYPLVQEFCLFLACSFVVSFLLHGSFFLAVLSVDIRRLELQDFLDSNSSNRNSKWWVPYLEYVRFMWSPWIIDNLGTVSFHMYVIYLQLQSSTDINGSWRLASPNIRFLITLYHRLGRILRERKLFPLITTGWFGDPTFLEALKEKTMAENLVIALYRPVILDTVNRRDYTNVYNSFHDRRVWRWSTFFSILFAIDFAVGLLVKALLRGWSDHDELSTDTTLHEEKFRIEPVPVHHQLDILKIAVSENYKTFASVGLDRCLVVWDLRQWCTKLVLSKEQMPRTLKAIALDPQGNYVSLFSKDTLFILNVESPCLMLQHSYHCKPNSKLNVFWMPGTHKDDEWKNFELVVVESSGEIQVFSLTIEIEGADIALVEKFQLSSPIIKSISIVSPTANRIACLTESGEVTVYSKKGPVWSPKILSQNKNYLTETKKDIYGIAMADILFLARDSGVDMIDLKNDELLHSFTLPPIKVNTFSVGVSNSRFVNGQFRVSSISFCFTHAVTEKVLYYYYGNECNESYIILNKWDQQPNLVDVHDPDNSLACLTFDELQENIHEVEDASECVMSSDGLYIFGMRRKSSSGICPTADEKNEDNGFTLRNRKLRTGHYNWTSYVPLLDSYMQDMEHKKNTHSGGETQVWEVWMYSQSEKKHRCKSLKMYNSLIIADPGPSLAVSDRCVAIVLGNYVALVGYGSEIFRDFYQIRNSDEMDRILRRKRKNLQRKRSGTIGC O43052 RGA1_SCHPO MOD_RES 690; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3F6.05; CHAIN 1..1150; /note="Rho-type GTPase-activating protein 1"; /id="PRO_0000075898" MSQRDAKKDGLLYTTNGVSPTPPKRIPVPSRQNKIEENSTTKNFPHSRHTSTVAGTEGGSSLSRRHTSAESRKALPNQQQLAQSGLLNKEEQQSLKRSDTSVFPKAVRKVSSSKICASCGQVISGQYVRALGNIYHLECFRCHDCNSLVASKFFPIDDPTLNKQVPLCETDYFRRLDLLCASCGMALRGYYITALNKKFHIEHFTCSLCYTVFGPNDSYYEYEGKVYCHYHYSTLFAARCCGCDGPILRQFVEVYRNGVSQNWHVPCHMIYKFWNVKLCQKTSIETSKKKDSELSQSQLRKREKHLEQKIFHIWHALSYFEEYTASCISDMLLLVSNGEFTKSVICAQKFIRYIEILFKGIDSLETILSSFHAKSMPYVREAKLLCKKLVSIFALLAKCHNSDIRDVAIVQDFLSLFTGLAHYLKLLIRISLTGGLRLEQDHACKHALPQFLQTVEEARFVDQEGYDSSSFDMPLNLANASSDLCYVCHSALEEDCVLLGEIRCHIGCLSCTKCKYNNRENYDWARWNNQTKQIECYLCYTESSNVSNDEPHPSFEYVSRLSQYIYLLRIALVRLYTILMENNDSSQRKPLSVDPKQENVSSTVETAKQAETTASSDSFRKYANTLNDLRHLKSSRNRKATSNETQSSSNSTETSKLSKNVSESGKDKSPHWHSHGGSITGKSIVEQASSPLERRMDAFDENRAFTLDDIPKVISEQRNREHRPNAFRHMPSYTDPSYRKNSGAIYDKNDGTQKGLTPKSEDAPIRYLSDLSNLELLFTKHVAVLILHPLVRDYYSLDELMEMSDLRKGGFWEKFGKAFKGKDAEKKNVKKKGTFGVPLEILVERNNAQSTVGTGVGVKHIPAFIGNTLAAMKRKDMSVVGVFRKNGNIRRLKELSDMLDVSPDSIDYEQETPIQLAALLKKFLRELPDPLLTFKLFGLFITSSKLESEEERMRVLHLTICLLPKGHRDTMEVIFGFLYWVASFSHIDDEVGSKMDIHNLATVITPNILYSKSNDPVDESFLAIEAVHLLIENFEKFCEVPREISLLLDDPTLFYNNAAWTSKELYKRCEEIISQMSLDERNTPKHTASTKRKRQPIRRVTTNLTSDVPSGSEVADTNSLSSTTKDEASPNSDAQPKPQVKPQHAVIRDS O43058 SEP1_SCHPO MOD_RES 446; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4C3.12; CHAIN 1..663; /note="Forkhead protein sep1"; /id="PRO_0000091907" MNFNSTNPYYFTHEKNLNNASKYSELPIAYQEIPLQSLPPYPKVASKLKGVVAGGKENNIASFQKPSSKATRPYIPSYTRLTYSVPPLPIPPPSEQSLDTIIYRNPSVSSSQSQEPEEFFLPLDDGKKPPYSYAMLIGMSIIRSPDRRLTLSAIYDWISNTFSFYNKSNNGWQNSIRHNLSLNKAFMKIERPRNLPGKGHFWSIRPGHEEQFLKLKLRKPGVNSRPAPPVQDVTSSTKYGSSTGSSGFNTFNTSPHIFNQRHQYLQNYYTASLTNIPTISNVNATNFHPLHSQQPYVDTPGIDAPSDLEAKFSDLGVSSVVSVTSPLQSCTNSPSPPLSSPASSASPSESLRNESLGIKSAKSLGLNKDDAPVEGPPVSHLEKDVETPSVHDSVLGFNDTVTNLGKKGLKDGTTNTLQIPAVRLPSLPSSPTIKNPSGLLLKRSNSIDFPTPPKALCPKLFCFRDDIVADDYTKFSLLSPIRSDMSGISASPNTNLKEHRTRILQMLATPDAKQLSSLTSSDAEFWSVTPLKSSILRNGDASKQVTLSESPKGDSLLDGGSLSYFTNNISSVAGLETPSKLPMSKSFDTFEDDFLDPMDMLSFENHFSDFNSNRKVSPVKREVRRKYISSATTIHSSAAQDDTYLPSPTKRKMPLLRQTSTLF O43060 EIF3F_SCHPO MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:18257517" SPBC4C3.07; CHAIN 1..302; /note="Eukaryotic translation initiation factor 3 subunit F"; /id="PRO_0000347327" MALGTKHVLHLTKPSSRSSPLNIVIEPAVLFSILDHSTRKSENNQRVIGTLLGTRSEDGREIEIKSCFAVPHNESSEQVEVEMEYHRAMYHLHLKANPREVVVGWYATSPDLDAFSALIQNLYASPAEPGTAPLGTYPHPCVHLTVNTDVSSPLAIKTYVSSPVGITERLADSCAFVPTPFTIRDDEAVRSGLKAVAAPKNDPSRLASLFTDLQQLRRSTLELLSMIERVSDYVQNVIDGSSPANVAVGRYLMKCFSLIPCVEGQDFEKIFSSHLQDVLVVVYLANTLRTQVDIASRLNLLP O43068 MDE4_SCHPO SPBC6B1.04; CHAIN 1..421; /note="Monopolin complex subunit mde4"; /id="PRO_0000096323" MSTISTSTDSKLDNLGLSVTSRRNQILFYLSKALNLAHLLRSDSLQKSFLDALKQSATDSELLHKNLDEIKFLQNEKLNNEKLLEQEQNEANDYRLKVERLEHKISDYVQEINSLNSQLQIQKSNPEKHEDAVSQNRLRGSLDTVSSPSKTHKANKDEKATRLHLIIANLKKALKEKDAEVLNLQSHVSSKESELDRFKIKLETEESNWKVRLQVLESKLATQDRKLRMQKKSTERKSLLVSPRVSSPKLFSPSKQAIMGTRQPNATSGSPLSVTPFLQKTSTSIGLSSSPPQSSPSAQSSQPFSRDKYPHSMTVSPSNARYLKKHLDDTIPSNVSDINHNDHLKIPQSPSSLSPSKIPIRKKRKLKDTVSNCEFTEEDSESSFLLETIQPTKSTLRRSISPLKKRNDEINELKKGFTMKK O43069 ATG7_SCHPO ACT_SITE 521; /note="Glycyl thioester intermediate"; /evidence="ECO:0000250" SPBC6B1.05c; CHAIN 1..649; /note="Ubiquitin-like modifier-activating enzyme atg7"; /id="PRO_0000212820" MFVGKALQFQSFHSSIDATFWHQLSNYKVEKQKLDASPLTIHGKFNTYSRGNISIVFGEAPSNSNIKDCLAEGTLLNANTPQEFTNADVKKIREEIGEVLLNSIKNGVVSERPNELLRFLIFSYADIKAYKYHYWCLFPSFKETPHWIVKDLSPAESLIPSGPILSQIREFLSTADYYQRPFFLLIKSTLDEWTIAPLKELSHCVDKSLQFYLVAEDSVQLAEYPSWPVRNILAFAFIKFKLKVINLFLYRDGINSDTLSKSILIKVEADKDMILEAPLSIVGWERNGKGVLGPRVVNLSTVLDPFVLSESASTLNLSLMRWRLVPQLDLDRIQNSKCLLLGAGTLGCGVARNLLSWGVRHVTFVDYSTVSYSNPVRQSLFTFEDCKRKLPKAECAAQRLKEIYPNMFSTGYNISIPMLGHPIYEAGIEKTMHDYETLENLISTHDAIFLLTDTRESRWLPTVISTAMDKLLINSALGFDSWLVMRHGSVLQKENRLGCYFCNDIFAPSNSLVDRTLDQTCTVTRSGCANIATAIAVELFVSLLQHPNGHAAPVLNEDQTVLGELPHQIRGFLHNFSLMKISGMAYPQCSACSECIINEWNREKWMFVLRAINEPDYVEELCGLREVQALGEIAGTMEEWISDKESVIL O43070 NBS1_SCHPO MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC6B1.09c; STRAND 2..7; /evidence="ECO:0007829|PDB:3HUF"; STRAND 16..18; /evidence="ECO:0007829|PDB:3HUF"; STRAND 20..28; /evidence="ECO:0007829|PDB:3HUF"; STRAND 35..37; /evidence="ECO:0007829|PDB:3HUF"; STRAND 41..43; /evidence="ECO:0007829|PDB:3I0M"; STRAND 48..52; /evidence="ECO:0007829|PDB:3HUF"; STRAND 68..72; /evidence="ECO:0007829|PDB:3HUF"; STRAND 79..81; /evidence="ECO:0007829|PDB:3HUF"; STRAND 84..86; /evidence="ECO:0007829|PDB:3I0M"; STRAND 91..93; /evidence="ECO:0007829|PDB:3HUF"; STRAND 95..102; /evidence="ECO:0007829|PDB:3HUF"; STRAND 109..113; /evidence="ECO:0007829|PDB:3HUF"; STRAND 118..121; /evidence="ECO:0007829|PDB:3HUF"; STRAND 140..143; /evidence="ECO:0007829|PDB:3HUF"; STRAND 150..152; /evidence="ECO:0007829|PDB:3HUF"; STRAND 157..159; /evidence="ECO:0007829|PDB:3I0N"; STRAND 174..176; /evidence="ECO:0007829|PDB:3HUF"; STRAND 230..234; /evidence="ECO:0007829|PDB:3HUF"; STRAND 250..254; /evidence="ECO:0007829|PDB:3HUF"; STRAND 264..267; /evidence="ECO:0007829|PDB:3HUF"; STRAND 269..273; /evidence="ECO:0007829|PDB:3HUF"; STRAND 283..285; /evidence="ECO:0007829|PDB:3I0M"; STRAND 291..293; /evidence="ECO:0007829|PDB:3HUF"; STRAND 303..306; /evidence="ECO:0007829|PDB:3HUF"; STRAND 491..496; /evidence="ECO:0007829|PDB:4FBW" HELIX 57..62; /evidence="ECO:0007829|PDB:3HUF"; HELIX 123..134; /evidence="ECO:0007829|PDB:3HUF"; HELIX 163..170; /evidence="ECO:0007829|PDB:3HUF"; HELIX 178..184; /evidence="ECO:0007829|PDB:3HUF"; HELIX 190..193; /evidence="ECO:0007829|PDB:3I0N"; HELIX 195..197; /evidence="ECO:0007829|PDB:3I0N"; HELIX 198..209; /evidence="ECO:0007829|PDB:3HUF"; HELIX 219..222; /evidence="ECO:0007829|PDB:3HUF"; HELIX 238..246; /evidence="ECO:0007829|PDB:3HUF"; HELIX 257..259; /evidence="ECO:0007829|PDB:3I0N"; HELIX 275..279; /evidence="ECO:0007829|PDB:3I0N"; HELIX 294..302; /evidence="ECO:0007829|PDB:3HUF"; HELIX 314..319; /evidence="ECO:0007829|PDB:3HUF"; HELIX 478..486; /evidence="ECO:0007829|PDB:4FBK" TURN 8..13; /evidence="ECO:0007829|PDB:3HUF"; TURN 135..137; /evidence="ECO:0007829|PDB:3HUF"; TURN 223..228; /evidence="ECO:0007829|PDB:3HUF"; TURN 307..312; /evidence="ECO:0007829|PDB:3HUF" CHAIN 1..613; /note="DNA repair and telomere maintenance protein nbs1"; /id="PRO_0000096751" MWIIEAEGDILKGKSRILFPGTYIVGRNVSDDSSHIQVISKSISKRHARFTILTPSEKDYFTGGPCEFEVKDLDTKFGTKVNEKVVGQNGDSYKEKDLKIQLGKCPFTINAYWRSMCIQFDNPEMLSQWASNLNLLGIPTGLRDSDATTHFVMNRQAGSSITVGTMYAFLKKTVIIDDSYLQYLSTVKESVIEDASLMPDALECFKNIIKNNDQFPSSPEDCINSLEGFSCAMLNTSSESHHLLELLGLRISTFMSLGDIDKELISKTDFVVLNNAVYDSEKISFPEGIFCLTIEQLWKIIIERNSRELISKEIERLKYATASNSTPQKIIQPQRHIQKNIVDDLFSVKKPLPCSPKSKRVKTLENLSIMDFVQPKQMFGKEPEGYLSNQSNNGSAQNKKSGDNSEKTKNSLKSSSKKSANTGSGQGKTKVEYVSYNSVDKGNSSPFKPLELNVVGEKKANAEVDSLPSENVQESEDDKAFEENRRLRNLGSVEYIRIMSSEKSNANSRHTSKYYSGRKNFKKFQKKASQKAPLQAFLSLSEHKKTEVFDQDDTDLEPVPRLMSKVESIPAGASSDKSGKSSISKKSSNSFKELSPKTNNDEDDEFNDLKFHF O43085 DSC1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305}; SIGNAL 1..25; /evidence="ECO:0000255" SPBC947.10; CHAIN 26..695; /note="DSC E3 ubiquitin ligase complex subunit 1"; /id="PRO_0000310840" MDRRRWVPSTPVVTLLLLFMLFAPAPRLPSRNGESSEKSIKAEKRAFSEIKNATFLNIPERVEHSLTFPTEIWETRDGLFEEPVGKGDSHLNHTSVMTGNWNILPYPSFGKVSPNVTWHTTLRNIVMSQSGRFSANLYEYVDGNSDGISFVLNLENNNDTSVYHMTFHGDRVKPINVFLGSTDVTPNFGGVDVIPWLLKDSPYKDAPPLDGTEYFPLLQNRSLERIETRLQDAQTVGWSPLVFEEEEVTCSAFVFLHNKNTGLDKETLKAIENEFYHPQGVSTQKMPEVFVSGLVYSPDCNVAFTFSNTKGPRNFVLENHLVRFSSLYIFIVLSQIFVLLRQMRINSPSHVQRLSFLTIAMQAGLDAYIAIFFLSTNAVIEKGYLPFVSVAFLSLVPSVMFTMRYLALILRVQNSNMPPPAPRPVTNNSSNNNTNQSNASNENSPNAPSAANDNTETTTVNPPQEDDQPMTQHERDQRDWSAVCLRFYFIILVVCIASLYSAFWPVIYRFYFISALIFTSYSFWIPQIIQNVKQGTSRSFTWTYILGASVLRLYLPLAIFIDSELILGFPPKYFFALGLVLWMLFQVLVLLVQDTLGPRFFLPKKFFLSSPVYDYHPVIQQDDLEAFMRDANVCPICMQPIELVSTGSTLNPASMMVRRNYMLTPCHHLYHRQCLLQWMETRSICPVCRCHLPAV O43086 ELG1_SCHPO SPBC947.11c; CHAIN 1..920; /note="Telomere length regulation protein elg1"; /id="PRO_0000239057" MQIVGYLSADSQSNPDLKSENEAKEEKPIGRRHTMSPVPATSENKYFGKSPLSGSRKPRRSRSLHKERSYMRKFFDMDMEESKDFENDQSLLVTLKVSTSLGQKIENILHPKLSNDTNSTAFPPAKSSGEASDTNILVENINSQETVNSSPLVSELHYSNLADSPSNLRNTVTSMHPFFMSKSVKKNSEIKFVSEERGGTKPERLLDPLWPTPDSQSMLEYAGSIEPSVFWFPKKHLEEAILEETSHLSFKEVLSSTTANMITPLAEKNKTEVLQVTPSKLHTFALESLCFSPAPFIQKVLSRLLPSDPNVEMPMIPQILEKGLWVSKYAPSKTQDCCAFSQCLSKIADWLRSCRLTKPESSSVPPSSSISRSSTIHSCTSSKRNEDSLSESDFEPDIIEEEDDSDEFNPSVSRKKAKLTSSQFSNWMLVTGVTGIGKTSCLYAICRELNFEVVEIHPGMRRSGKELLERIGELTQSHIVDKSRLNNTPDILILLEEVDILFQDDRGFWQAVSTLIEKSKRPVVMTCNETDFLPSAFLQEDHIVQFQSISSALLTDYISSVLYADRCIISRNVVESISYRYGSDLRGILMQLNFWSLVNFPSLPSKDKQDDSHEPFIEATISAFDEGVGVYNPRIQTSEDLLQTYSEEQMGDIGLLFMPNLVNWRKVCVPKSEMEEKEAIMEKLIYSHQYADSLSYVDYRFSSQPTIYETYELMNDSASFEDMSLECRDNCANAFQDNLVGFPTISNPFHANAPPEPHELKLQYHSFCFINNLFSKSSLKAISSNDSIVPKALNNRELQLSALASTIGYKLDPDDVYNILSFLSFANSQVTSYTPPNSIDRPNDILILEVAPFVRCMRRYDRIRLNSYKLLLSSKGRSASHISRRGAASILRSAGYNYGRLQYLEGSDRILSTWFSTTLD O43091 DPS1_SCHPO BINDING 72; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 75; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 130; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:Q12051"; BINDING 137; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 137; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 141; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 141; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 146; /ligand="an all-trans-polyprenyl diphosphate"; /ligand_id="ChEBI:CHEBI:58914"; /evidence="ECO:0000250"; BINDING 147; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 229; /ligand="an all-trans-polyprenyl diphosphate"; /ligand_id="ChEBI:CHEBI:58914"; /evidence="ECO:0000250"; BINDING 230; /ligand="an all-trans-polyprenyl diphosphate"; /ligand_id="ChEBI:CHEBI:58914"; /evidence="ECO:0000250"; BINDING 267; /ligand="an all-trans-polyprenyl diphosphate"; /ligand_id="ChEBI:CHEBI:58914"; /evidence="ECO:0000250"; BINDING 284; /ligand="an all-trans-polyprenyl diphosphate"; /ligand_id="ChEBI:CHEBI:58914"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = all-trans-decaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:27802, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.91; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; SPBPJ4664.01; CHAIN 1..378; /note="Decaprenyl-diphosphate synthase subunit 1"; /id="PRO_0000123977" MIQYVYLKHMRKLWSLGKVRSTVLRFSTTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDRSVVGDKYIDDDDLRSFSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIADLVRGEFLQLKNTMDPSSLEIKQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAKDSLLCLPDSPARKALFALADKVITRKK O43114 ORC5_SCHPO BINDING 42..49; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC646.14c; CHAIN 1..455; /note="Origin recognition complex subunit 5"; /id="PRO_0000127095" MHLYQLEDELKKNVFCREDQIKKLSCLLFNKDCRVPSIVLYGVASTAKTFLLRTAFDLSKEENVWINLQDCFTVAHFWYRILIKVGVDKDIALKKGINISGFIYLLEQAMSKRDYHTFLVLDQIDDFAEASTILFSQLAQLPIVANIPNLSIIFVLHSHPAQYLGTLSIAVIFFPQYTQAEILEICQKTPPNLDFLDRSGDSVFEDEIELSVWMQYCSFLWSVFGVQCLNDYRSFRSVLDRYWPKFIQPIVEGDIHPADYAQLHKLAKNFLVSDATVTKRLHIINPTEIKNLLDSKSINLSLVSKYLLVSAFLASYNPSRLDAQFFSFSKTSKRRGRKRKQIQDEGVLFSKIPRTAGSKGRSAVKISQLTLGPKPFEVERLIAIYYAISSPVEKVLTADVFVQIATLASLKMILSASKGVLRSLDSPRYIVNVSREYVLKIADSLSFPLDSYLAG O59676 PDP1_SCHPO MOD_RES 252; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC29A3.13; STRAND 54..59; /evidence="ECO:0007829|PDB:2L89"; STRAND 61..63; /evidence="ECO:0007829|PDB:2L89"; STRAND 65..80; /evidence="ECO:0007829|PDB:2L89"; STRAND 82..84; /evidence="ECO:0007829|PDB:2L89"; STRAND 86..94; /evidence="ECO:0007829|PDB:2L89"; STRAND 99..103; /evidence="ECO:0007829|PDB:2L89"; STRAND 108..110; /evidence="ECO:0007829|PDB:2L89"; STRAND 123..125; /evidence="ECO:0007829|PDB:2L89" HELIX 105..107; /evidence="ECO:0007829|PDB:2L89"; HELIX 113..121; /evidence="ECO:0007829|PDB:2L89"; HELIX 128..137; /evidence="ECO:0007829|PDB:2L89"; HELIX 140..142; /evidence="ECO:0007829|PDB:2L89" TURN 95..98; /evidence="ECO:0007829|PDB:2L89" CHAIN 1..359; /note="PWWP domain-containing protein 1"; /id="PRO_0000303950" MNNARTNAKRRRLSSKQGGLSISEGKESNIPSVVEESKDNLEQASADDRLNFGDRILVKAPGYPWWPALLLRRKETKDSLNTNSSFNVLYKVLFFPDFNFAWVKRNSVKPLLDSEIAKFLGSSKRKSKELIEAYEASKTPPDLKEESSTDEEMDSLSAAEEKPNFLQKRKYHWETSLDESDAESISSGSLMSITSISEMYGPTVASTSRSSTQLSDQRYPLSSNFDHRGEAKGKGKQPLKNPQERGRISPSSPLNDQTKALMQRLLFFRHKLQKAFLSPDHLIVEEDFYNASKYLNAISDIPFLNYELITSTKLAKVLKRIAFLEHLENDELYDIRQKCKNLLYSWAMFLPNEPSIKGM O59701 CYSK_SCHPO BINDING 84; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P16703"; BINDING 190..194; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P16703"; BINDING 289; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P16703" CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-succinyl-L-serine = L-cysteine + succinate; Xref=Rhea:RHEA:53816, ChEBI:CHEBI:29919, ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:136856; Evidence={ECO:0000269|PubMed:28581482}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:17482430, ECO:0000269|PubMed:28581482}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P0ABK5}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for O-succinyl-L-serine {ECO:0000269|PubMed:28581482}; KM=0.33 mM for O-acetyl-L-serine {ECO:0000269|PubMed:28581482}; KM=0.34 mM for Na(2)S {ECO:0000269|PubMed:28581482}; Note=kcat is 2.8 sec(-1) with O-succinyl-L-serine as substrate. kcat is 1.5 sec(-1) with O-acetyl-L-serine as substrate. {ECO:0000269|PubMed:28581482}; TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 54; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P16703" SPBC36.04; CHAIN 30..351; /note="Cysteine synthase 1"; /id="PRO_0000167128" MATSGIQTKVPGIVSGFIGAIGRTPLIRLNTLSNETGCNILAKAEFQNPGGSVKDRAAYYVVRDAEKKGKLSRGGTIVEGTAGNTGIGLAHIARARGYKCVIYMPNTQSQAKIDTLKFLGAEVHPVPVAPFSNPLNYNHQARRHAESTPNASWTDQFDNVANLLSHYETTGPEIWDQTKGTVDGFTCSTGTGGTFAGVTKYLKEKSDGRVASFVADPPGSVLYSHIKTKGKHPDNKGSSFTEGIGQGRITGNVQPVYDLIDDAMKIPDEKSINMFFRLLDQEGLFLGGSSCLNVVAAVEMAKILGPGKTVVTILCDSGHKYATRLFSRSFLESKKLFDVIEPQYKKYIVLP O59702 CLR6_SCHPO ACT_SITE 138; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; SPBC36.05c; CHAIN 1..405; /note="Histone deacetylase clr6"; /id="PRO_0000114740" MGFGKKKVSYFYDEDVGNYHYGPQHPMKPHRVRMVHNLVVNYNLYEKLNVITPVRATRNDMTRCHTDEYIEFLWRVTPDTMEKFQPHQLKFNVGDDCPVFDGLYEFCSISAGGSIGAAQELNSGNAEIAINWAGGLHHAKKREASGFCYVNDIALAALELLKYHQRVLYIDIDVHHGDGVEEFFYTTDRVMTCSFHKFGEYFPGTGHIKDTGIGTGKNYAVNVPLRDGIDDESYESVFKPVISHIMQWFRPEAVILQCGTDSLAGDRLGCFNLSMKGHSMCVDFVKSFNLPMICVGGGGYTVRNVARVWTYETGLLAGEELDENLPYNDYLQYYGPDYKLNVLSNNMENHNTRQYLDSITSEIIENLRNLSFAPSVQMHKTPGDFTFENAEKQNIAKEEIMDERV O59703 GGPPS_SCHPO BINDING 55; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 58; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 93; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 100; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 100; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 104; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 104; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 109; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250"; BINDING 110; /ligand="isopentenyl diphosphate"; /ligand_id="ChEBI:CHEBI:128769"; /evidence="ECO:0000250|UniProtKB:P14324"; BINDING 196; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250"; BINDING 197; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250"; BINDING 236; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250"; BINDING 253; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250"; BINDING 262; /ligand="dimethylallyl diphosphate"; /ligand_id="ChEBI:CHEBI:57623"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; SPBC36.06c; CHAIN 1..351; /note="Geranylgeranyl pyrophosphate synthase"; /id="PRO_0000339411" MVNDFNEKNGIKKRLLDFFPVVLEGIREILESMQYFPEETEKLLYSIKRNTLGGKNNRGLAVLQSLTSLINRELEEAEFRDAALLGWLIEILQGCFLMADDIMDQSIKRRGLDCWYLVVGVRRAINESQLLEACIPLLIRKYFRNMPYYVDLLDTFREVTFLTELGQQEDLLSSRDGEASLRSFDLMKYDFIITYKTSFYSFYLPIKCALLLSRNSNQKAYDTTIKLSKLLGYYFQVQDDYLDCFGDYTVLGKVGMDIQDNKCTWLVCYAEKFASADQLNLLRAHYGKAGSENIAVIKQLYHELQIPELYHKFEDDMVDSISKEIDLIDESTGLKKCIFTKFFQLIYKRSR O59726 FNX2_SCHPO SPBC3E7.06c; CHAIN 1..577; /note="Vacuolar membrane amino acid uptake transporter fnx2"; /id="PRO_0000372714" MSNPRTKSPNTNRGQGLRSERSALLNDSLSSLNGNSSYDSIKDSSKNNKDVAEVNEYPRRPESSVSVVSNSPHRQDAATTNTVSTVSVSKVLPALLLGVVLAALDNTIVASTYTKIGAEFGKFSQVSWTATAYMISCTAFQPLFGKFCDIYGRKKTLLAAYCVFGIGCFLCGTSRSLWQLVAARAIAGIGGGGMNSTVSILMSDIVPLKQRGTYQGIINVFFAIGSSLGGPVGGYFADQYTWRIGFLIQVPLIAIAFLCVYFTLNLPHHNHVSFMTRFRKIDLKGLILLIIGVTTMTCAFTLGGNVREWNDPVVISLLIASSISYLSFVYVEAFVAFEPLAPMDVLTERTCLSSYLCNFFHSVANFGWIYGMPLFFQSIKNEGAEKSGIRLIPMIIGSSLGSLLGGAVISLTGNYKKITVGSYFFGSVAALFMLRYGYSNFNWEYAVYPFSGGLGNGIAVTTTLVAIIHASPSAFQASAIATSYLFRSNGCVLGVSISSSIVQTVLGIKLRKSLDFDVDELLHHLRKDISYVHRLPEEIRQTVLDALLGSIHYSFLFVSFMFFCAFVCSMFIKNRNL O59734 RUXF_SCHPO SPBC3E7.14; CHAIN 1..78; /note="Small nuclear ribonucleoprotein F"; /id="PRO_0000125543" MSFVPVNPKPFLQGLIGKPVLVRLKWGQEYKGTLQSVDSYMNLQLLNAEELVDGVKTGDLGEILIRCNNVLWVGESTV O59740 MOD5P_SCHPO MOD_RES 43; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 350; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC530.04; CHAIN 1..522; /note="Cell polarity protein mod5"; /id="PRO_0000351429" MSALSESPAIPSFWRPETSEISKKPRPNTTVGFQFDNRNVGTSAPSTPAIRRNNTDSFERGLSLPLPSSKQDTGSSVLDPDGDAYVNRYARPVTAGSIYIPSNYHKSFSPNTFSGFNVKRSASKSPKRSANGSTSEDISIEGSPSETAKGARSSFNSNFRTFDIGSERRRRILEASQDSSRPGRYSYRTKSASPALIDTSTLDSRLNFTMGRLERSIAQLSKNTMRAVSHLENPPKDITLPKLNVKNSAWPLQPYSPPANETPASSSSSAKARPVSVPDMSSPVPASSVEYESLKAAVTYSPSQNPKKVAETDSESRKSSFQSSYNDADRPFQVGAQTQSTPNRISRSDSPIVYDVDTHSEDNASTASSEAISQSMRSFQPQPNTGSPFPRFTSTNTEDEQESDIPQSDANDSTVNLNQPNYANLTPTPQVSPKRPTYSRSSPLPSASVPALGDGSPDPPAAPSIQNSLSVHESEMPPHVTRDYTQPAASATPVPKEKPSEKSEKPPKKKGSKLEKFCCILM O59747 PDF1_SCHPO ACT_SITE 125; /evidence="ECO:0000250"; ACT_SITE 245; /evidence="ECO:0000250"; ACT_SITE 298; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl diphosphate + H2O = a di-trans,poly-cis-dolichyl phosphate + H(+) + phosphate; Xref=Rhea:RHEA:14385, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19506, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57497, ChEBI:CHEBI:57683; EC=3.6.1.43; Evidence={ECO:0000250|UniProtKB:P53223}; SIGNAL 1..24; /evidence="ECO:0000255" PTM: Proteolytically cleaved, possibly by krp1. {ECO:0000269|PubMed:15075260}. SPBC530.12c; CHAIN 25..622; /note="Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1"; /id="PRO_0000349152"; CHAIN 25..?; /note="Palmitoyl-protein thioesterase"; /id="PRO_0000349153"; CHAIN ?..622; /note="Dolichyldiphosphatase"; /id="PRO_0000349154" CARBOHYD 223; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 260; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 396; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 106..138; /evidence="ECO:0000250" MLSCSSFLIFFLFSWVLLPMKSFAIPIISLDKVRLAINDGASEQLPVVIWHGLGDTPTSFTLTEVSQRVQKLTKGAVYAIRVGDNEFEDIKAGYLGKLEDQLDEVCDLIGNEDSLSNGFYALGLSQGGLFLRALAQTCDAAKIRSLITLGSPHSGINTIPGCSPTNLICKAVVHSILGLGIWHSWIQNHVVQAQYYRTEKQYDKYLENNKFLTHLNNEVLHDNYTRNIEKLKELDNLVAVSFERDDIVEPPYSTGFGWINETTGENIEMEDFVLYESLGLKDLVNQGKLETISFPGRHLQMRWGDFDALVLKYFKDEKEEKTELEESTRPSNFLSTYFVSPLVSAIDGTVDYLHGKSLFPEKRNFKELTMRKRSIVTPEDSEEVYPYISEFVAASNVSEEKGPKSFANLAFITIFSHFFYHIDDMWRSTLGLFSLIPQIIGIIYLTVMFTGRELDTFMQFGGQVVNEFINYVVKVSLKYPRPADIEYGVGYGMPSSHSQFMGFFSAYMIAWDYKYRRSQCFSMLSFAKYAIYLTLSTFVCSSRYLLDFHYLTQVVYGYMIGFGVGLFWVYLVGKLRSLGVTKWLLSLPPLQFFYIKDTIPHSKDNHKRQWLESKQFKNQKSN O59748 CTK2_SCHPO SPBC530.13; CHAIN 1..335; /note="CTD kinase subunit beta"; /id="PRO_0000310348" MAENENHVLSIRMSHPYYSEKEISRILSTRDPKENNLRMQAFAWISTLSKTLKFPVRTSGLAMLLYSRFQLFFPVNEIPLLECATACLVVASKIEDTAKKFRDILLAHYLQKHPGSEVDAHSQVCYKLIEENKKRILGLERMTLELICFDFRVRHPHNYMVKFAKSLKFSSSTASIAWNVCTDAYKTYTMLKYPAHIVAVASISIACKLQQLPQPIIPRSFFAPPALTEAVIADILDLYMHYQPHTCIGNMYTTEKLLGLCVDFQRAQKNSGRPQKPPQIDPHSSSLADEYRESNKRLQESKESCARFILDCDRKYFNTEFEKRMLEERRNKGTV O59751 KLP6_SCHPO BINDING 134..141; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" SPBC1685.15c; CHAIN 1..784; /note="Kinesin-like protein 6"; /id="PRO_0000125389" MKEGSSISVAVRVRPFTEREKGLLAETPKSKEFLGDGSLAVSNTSSNTFCTNGIRKIVRVLDDNVLIFDPPEENPLAKVQKSLLPAGKRFRDVRYAFDRLFGEEASQEDVYKGTTEPLLDSVLQGYNATVFAYGATGCGKTHTISGRPDDPGIIFLTMRALLDRVEGLKRTMNVDISVSYLEIYNEKIRDLLVQDPLSMEKPKSLNICEDAEQNVSVPGLSYFTPTNLEEVMEIIIRGNSNRTMSPTEANAVSSRSHAVLQIYITQTPKSGEKQEESESQNSHKVRSVFSFIDLAGSERASATKNRGKRLVEGANINRSLLALGNCINSLCEPRRRQHVPYRDSKLTRLLKFSLGGNCRTCMIVCISPSSEHYDETHNTLKYGNRAKNIKTKVSRNVVSVDRHVSEYVRTIYELRQKVSILQKRIAEESKQLALNKEVRKISSREIKMLDARSMLKNSFDGSRDLQKSLIEHVRTLRRIEDEITLTKMWISIAKESDAMSGHNIKSVETRLAKLYDQRSLITAKVNPEEICKTFQNSISHIVSSFKGEGADMYADMLQDDVDLLKSIIENQILDAKHESETFSSTSRKLIQNLFLLFPLLPGNAIDVNESLARAFDQLVGIVPSEPTIQVPNLIEKGKAPLLSMFEIPRSPSRFKARSPSKAARVLKKPLKKRVRFSEVPTTSSVPPVEIKNKDSKPKVEKSLDKHNMNNDRSFLVPSRDARNSLTSLSLHSNVAKNKSSHSSKWPTHTLSPIITTALKQPVRRISLVSQPLQKTGGTENTPNA O59755 CUT12_SCHPO SPBC649.05; CHAIN 1..548; /note="Spindle pole body-associated protein cut12"; /id="PRO_0000079567" MSETLNTPPTYAWVLKAFSSKLAGTVTKPVTKMSSYIEDAESDAELPQDAKEDLRPTETLTPLKSKAAQNGILKTPGTLQIKKTVNFKDISKDAATWNRPTKNNFLFTRLDDENPLMGHEEFKSPLLQSTPKPNINNPDNENKSKHDEFDNRYNININESYKNETKSNQRLGEDVPSKKKYPHSMDAEISKFKWDSNNNNDWSSLMKDCFRDVVNNNRKMKEIIKDVMIDTSQAFPSESLDEPDYTINLDAPRSSSGKYWKQKFSMLDSAHSDLELELTSIRERLESLILEKQEEINFWKQRCRALETEKIHNHQGQQSKYKGKEFVGNRFSQMRELYTAKPSPITTKVVSRPSQSDVREPQEQVPSKNLHRGADMSHLAAQMLTHSSKKSHTTNLIPSEGIISSTPISAASKVRMNLMQSNQTPTPAPFSIAAKKSHLPSKLSFPQDGGSLSSATTLQQLPKARVTPNVLSSLSSNLGKTNPTSVYQSKANVTTSADVEKPQVKVATSSRVDYDLKSPNQRTANAKKRLEERRRRRKLKLQELQLNS O59757 SPC7_SCHPO SPCC1020.02; CHAIN 1..1364; /note="Kinetochore protein spc7"; /id="PRO_0000290644" MPTSPRRNSIATTDNVIGRNKSRKRPHSLGGPGALQELKEHTNPAKGILKSYSSFSVDPAFTGDEDFNDIHTQINNTVIGISSNVMAASKRLQMEDLQQLSRETSRKSLNRRVSFASHARVRWYPKDHQSDSEKSTSNHSTPERTFASDAKNHSPKGPTTTSFSRNETQSSPHSHSASIISDGSDMDIASPIRSTESDMVSEALNAGHPPPSLYPENDDLSIQNPTKALPEAEKALDVHDATREQVNDREETNMDLTIQFQEADSFLSHSESIKGLSSSEQGTVYSLKASHDPSNQTQLSSPNKSSSPTSIEISDFSKNNENHDQSENKEEEEDMMLTRPIEIPQHFSPIARPLTSQEAIVDMDITSNNINLSPVSHFSNGLDLQNLEEAPMNLTRPINANPHLTNHSPNDLTNGEEEMDTTSAFNIENSHLTLLSPIRPSSRSMEEQIMDLTQPISSTNAPTHLNEDDLNQFTSNISSSSKPRKDNNKTANSSKPIPDSEDFMDITRPFNILSPSKEALSEEQPMELTSTVFPCENSTSHLEVEEAAMDETVAFQIRGNNVELPSADKENAEREEIPSYSDKSENFNTTSFTNHERSPNGNNNLKFSKDPNSSSPSRHVVATPTDKLGTRKRRLRYSTSSFDQSTLRRNRLATIRNARKSISTLNDRELLPVNFFEKKVNSGLYKSVERSENYRLGATPLTAEKPFTTEKPLSSLPEEVSRQPTDDKGEQVSNADVDSGLSKTERLTIQQTNEIKHVPTNTTSSVKLPQQPSNEDEKERITTADYADSTSLERLESQEPNRNELVQVGSSNAGNTTSVGMNEHEKSPVKLSKGVSNVDTSLGASTINTNILNQDSGPNEEIPVGNEPEFDTMPTLPNVEPISLSDFLKMTGIEFLDNLTIAKRRETLLPNAEENKKCSIQELLESFYIQFPLLELYKFSCQQLQDYIAEGKDFVTKIEEETLKENPLLFYEYRKASSDMRVLMDSQFLMMKTFARLQAKGDWYEWREGLMQGIKHELNLNLTGMQRSLTHLMDVANVIHPYAQEIQERYNGSITTVQTLKKQKEFANQYDSTLLAQAQEKLEKLKVEVERRRRLLSEKEERRKELAIKIEQVTNSCSDLELRTNAEQDFYAKNQDFEFDEIKRYEEQLLNLKNELGWTIVSLTAGGIKLATNNTALSPYSAEVTVEILRQNFQVNVDIACKFPNESNACSSNVLEHVASSFSKWHSKVFSRNLRLLKKYLNDVSICWEQIVYLVQDFQRLWYHWPFLSVENDDKSIIINVELYLRSVSSKVKVVFGLPIDTIYQTTEVGKFYASTSVAVKQMYAESEGDSYVSEVLNTLSEVVHCTSTYALSSACLTVWNKYS O59763 OCA2_SCHPO ACT_SITE 425; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P39009, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 308..316; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P00517, ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 331; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39009, ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q08732}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q08732}; MOD_RES 72; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1020.10; CHAIN 1..650; /note="Serine/threonine-protein kinase oca2"; /id="PRO_0000337145" MSVTPPNVQFNLNGDSDHKSDNSSSSLENKLDTELKITSPPRNPPQRLHPVDFSEHADTDDDMNHPLPRVQSPVHIKNHIDPKLAEDRYRSSAARHFEPISIPPSAITSEDEDDYHGSANSSTVLPPRTENALHAASPKPSGSTGYTSPALSQNSGSGGEGESDEGSFNTQHHRSPIFQAYPSSEDLVGDPNDPYRRTRRAPIKTNPHDIPSQFIFRKLGLHHGKHGHHGHSGSLSLKSLVPNHHDKHDKHDKHEKHHSSLDLRRFFKSHQKTDKEKKPSVSKSKSSANLQDDHFGLFKKYGKFGRMLGSGAGGSVRIMKRSSDGKIFAVKEFRARRPTETEREYARKVTAEFCIGSALHHTNIIETLDIVEENKKFYEVMEYAPYDMFSIVMSGKMTMPEVYCCFKQLLSGVAYLHSMGLAHRDLKLDNLVVDSNCFVKIIDFGSAVVFKYPFEADIVEATGVVGSDPYLAPETLVRKLYDPRAVDIWSSAIIFCCMALRRFPWKYPKLSDNSFRLFCMKQPSNDAESPSDILADIKKQRLVEQGCEPIRKTDESHSPNSKTDNSSTHKQELYGPWRLLRLLPRETRAVIAHMLELDPVKRYDIHRVFADNWINDISMCHMENGKVIHSPTHVHNLVASEESPAPPAKH O59767 MAD3_SCHPO SPCC1795.01c; HELIX 13..18; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 19..22; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 32..39; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 45..64; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 65..67; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 72..85; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 96..106; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 111..113; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 117..127; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 133..142; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 150..162; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 166..179; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 184..201; /evidence="ECO:0007829|PDB:4AEZ"; HELIX 203..205; /evidence="ECO:0007829|PDB:4AEZ" TURN 92..94; /evidence="ECO:0007829|PDB:4AEZ"; TURN 107..109; /evidence="ECO:0007829|PDB:4AEZ" CHAIN 1..310; /note="Mitotic spindle checkpoint component mad3"; /id="PRO_0000084548" MEPLDAGKNWVHMDVIEQSKENIEPRKAGHSASALAKSSSRNHTEKEVAGLQKERMGHERKIETSESLDDPLQVWIDYIKWTLDNFPQGETKTSGLVTLLERCTREFVRNPLYKDDVRYLRIWMQYVNYIDEPVELFSFLAHHHIGQESSIFYEEYANYFESRGLFQKADEVYQKGKRMKAKPFLRFQQKYQQFTHRWLEFAPQSFSSNTNSVNPLQTTFESTNIQEISQSRTKISKPKFKFSVYSDADGSGKDGQPGTWQTLGTVDQRRKENNISATSWVGEKLPLKSPRKLDPLGKFQVHCDEEVSKE O59790 ARK1_SCHPO ACT_SITE 212; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 95..103; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 118; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPCC320.13c; CHAIN 1..355; /note="Serine/threonine-protein kinase ark1"; /id="PRO_0000085634" MSDSKLADSLNCLSVSTPSTTANPGRQQLLRLAVSNQRQVNNVSLANGKENKRTSNSKFNSSLRKIEEPIAGVPSSAGPQWREFHIGMFEIGKPLGKGKFGRVYLAKEKKTGFIVALKTLHKSELVQSKIEKQVRREIEIQSNLRHKNILRLYGHFHDEKRIYLILEFAGRGELYQHLRRAKRFSEEVASKYIFQMANALSYLHKKHVIHRDIKPENILLGIDGEIKLSDFGWSVHAPSNRRTTLCGTLDYLPPEMVEGKEHTEKVDLWSLGVLTYEFLVGAPPFEDMSGHSATYKRIAKVDLKIPSFVPPDARDLISRLLQHNPEKRMSLEQVMRHPWIVKYKDSWTRKSSESS O59791 SRR_SCHPO ACT_SITE 57; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:19640845, ECO:0007744|PDB:2ZR8"; ACT_SITE 82; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:19640845, ECO:0007744|PDB:2ZR8" BINDING 32; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 33; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 52; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 79; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 84; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 87; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 119; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 176; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 183; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 184; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 185; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 186; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 187; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 208; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 208; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC, ECO:0007744|PDB:2ZPU, ECO:0007744|PDB:2ZR8"; BINDING 208; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 212; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 212; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC, ECO:0007744|PDB:2ZPU, ECO:0007744|PDB:2ZR8"; BINDING 212; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 214; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 214; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC, ECO:0007744|PDB:2ZPU, ECO:0007744|PDB:2ZR8"; BINDING 214; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 277; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4"; BINDING 308; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC"; BINDING 311; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9GZT4" CATALYTIC ACTIVITY: Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384, ChEBI:CHEBI:35247; EC=5.1.1.18; Evidence={ECO:0000269|PubMed:19640845}; CATALYTIC ACTIVITY: Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; Evidence={ECO:0000269|PubMed:19640845}; CATALYTIC ACTIVITY: Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18; Evidence={ECO:0000269|PubMed:19640845}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 mM for serine {ECO:0000269|PubMed:19640845}; Vmax=870 nmol/min/mg enzyme {ECO:0000269|PubMed:19640845}; PTM: Modification of the active site Lys by its substrate Ser to lysino-D-alanine reduces but does not abolish enzyme activity. MOD_RES 57; /note="Lysino-D-alanine (Lys); alternate"; /evidence="ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845"; MOD_RES 57; /note="N6-(pyridoxal phosphate)lysine; alternate"; /evidence="ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC" SPCC320.14; STRAND 41..47; /evidence="ECO:0007829|PDB:1V71"; STRAND 77..79; /evidence="ECO:0007829|PDB:1V71"; STRAND 100..105; /evidence="ECO:0007829|PDB:1V71"; STRAND 122..126; /evidence="ECO:0007829|PDB:1V71"; STRAND 151..154; /evidence="ECO:0007829|PDB:1V71"; STRAND 176..181; /evidence="ECO:0007829|PDB:1V71"; STRAND 183..185; /evidence="ECO:0007829|PDB:1V71"; STRAND 203..209; /evidence="ECO:0007829|PDB:1V71"; STRAND 256..260; /evidence="ECO:0007829|PDB:1V71"; STRAND 302..307; /evidence="ECO:0007829|PDB:1V71" HELIX 10..20; /evidence="ECO:0007829|PDB:1V71"; HELIX 33..39; /evidence="ECO:0007829|PDB:1V71"; HELIX 48..50; /evidence="ECO:0007829|PDB:1V71"; HELIX 52..54; /evidence="ECO:0007829|PDB:1V71"; HELIX 57..65; /evidence="ECO:0007829|PDB:1V71"; HELIX 70..75; /evidence="ECO:0007829|PDB:1V71"; HELIX 84..95; /evidence="ECO:0007829|PDB:1V71"; HELIX 110..118; /evidence="ECO:0007829|PDB:1V71"; HELIX 133..144; /evidence="ECO:0007829|PDB:1V71"; HELIX 155..161; /evidence="ECO:0007829|PDB:1V71"; HELIX 163..172; /evidence="ECO:0007829|PDB:1V71"; HELIX 186..198; /evidence="ECO:0007829|PDB:1V71"; HELIX 210..212; /evidence="ECO:0007829|PDB:1V71"; HELIX 214..221; /evidence="ECO:0007829|PDB:1V71"; HELIX 235..237; /evidence="ECO:0007829|PDB:1WTC"; HELIX 244..253; /evidence="ECO:0007829|PDB:1V71"; HELIX 262..275; /evidence="ECO:0007829|PDB:1V71"; HELIX 282..285; /evidence="ECO:0007829|PDB:1V71"; HELIX 286..293; /evidence="ECO:0007829|PDB:1V71"; HELIX 294..298; /evidence="ECO:0007829|PDB:1V71"; HELIX 314..321; /evidence="ECO:0007829|PDB:1V71" TURN 21..23; /evidence="ECO:0007829|PDB:1V71"; TURN 128..131; /evidence="ECO:0007829|PDB:1V71" CHAIN 1..323; /note="Serine racemase"; /id="PRO_0000185588" MSDNLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFLSQ O59836 HIM1_SCHPO BINDING 499; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"; BINDING 502; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"; BINDING 512; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"; BINDING 518; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600" PTM: Hyperphosphorylated at the G1/S and S-phases of the cell cycle. SPCC550.13; CHAIN 1..545; /note="Hsk1-interacting molecule 1"; /id="PRO_0000083978" MNLGRCPLAPRSANIVLPKHDAVSKQKEYRIEEKTNEAQREEIITWKDNREDEGEVKTDFEVVNNENIITTTPKHQTVITPKSYRKSVKRIKHDAPQNEDIPVMKGLAPINADTESKAESMAAGKVLGSKNSSQKARLQEWKRQYKKAFPHFRFYLDGCDPSVAHRVKKQIQQLGGHVETFFSGNVTHVATVRAIQDVSVKYAKQDVITKARQLNMKIWSMEKLCNRVLKTLMENDQCTTNAPTKQGNDLSYLLYVEKVQGTNERDLSVPRQDFVHFRGPYLYVHDIANIYKPILLREWQKPLPDRDVPWPTFRATSIGRCPFVPETKYRLSTSKSLVAKNDQQLLQRQSQEPSLILRANSMKASLPDISNTGISGMNTNTTYNTNINNTPQTAISGITQDTSPSIRTNCHHCLDDGMQASGIVQSNLTSAAMSNNSAIRSGSAASVPVVTINGRDIAELKKRIIQQKSGMIGKDYSYKAMLHNTSQRKIRVDAKPGYCENCREKFDNFESHIRSSRHRRFAENNDNFKDLDELFALVQRPLRPD O59855 HSP72_SCHPO MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250"; MOD_RES 36; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 339; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 417; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 546; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1739.13; CHAIN 2..647; /note="Probable heat shock protein ssa2"; /id="PRO_0000078380" MSKSIGIDLGTTYSCVGHFSNNRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTIFDAKRLIGRKFDDPEVQSDMKHWPFKVISKDGKPVLQVEYKGETKTFTPEEISSMVLMKMRETAEAYLGGKVTDAVVTVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDRSNQGESNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDSRLVNHFIQEFKRKNKKDITGNARAVRRLRTACERAKRTLSSSAQASIEIDSLFEGIDFYTSITRARFEELCADLFRKTMEPVERVLRDSKVDKASVNEIVLVGGSTRIPRVQKLVSDFFNGKEPCKSINPDEAVAYGAAVQAAVLTGDTSEKTQDLLLLDVAPLSMGIETAGGVMTPLIKRNTTIPTKKSEIFSTYSDNQPGVLIQVFEGERARTKDCNLLGKFELSGIPPAPRGVPQIEVTFDVDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDRMVAEAEKYKAEDEAESGRIQAKNHLESYAYSLRNSLDDPNLKDKVDASDKETVDKAVKETIEWLDSNTTAAKDEFEAKQKELESVANPIMAKIYQAGGAPGGMPGAAPGAAPGAAPGAAPGGDNGPEVEEVD O59858 GPX1_SCHPO ACT_SITE 36; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000250|UniProtKB:P40581" CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:18162174}; SPBC32F12.03c; CHAIN 1..158; /note="Glutathione peroxidase-like peroxiredoxin gpx1"; /id="PRO_0000066644" DISULFID 36..82; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:P40581" MSHFYDLAPKDKDGNPFPFSNLKGKVVLVVNTASKCGFTPQYKGLEALYQKYKDRGFIILGFPCNQFGNQEPGSDEEIAQFCQKNYGVTFPVLAKINVNGDNVDPVYQFLKSQKKQLGLERIKWNFEKFLVNRQGQVIERYSSISKPEHLENDIESVL O59868 ATC1_SCHPO ACT_SITE 329; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; MOD_RES 892; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC31E1.02c; CHAIN 1..899; /note="Calcium-transporting ATPase 1"; /id="PRO_0000046229" MSVQYDAFSVEQTCADLETDMYNGLSSLQEITRRNKVHGDNDLKVEDEENMVVQFLKQFVKDPLILLLFASSAISVTLGNIDDAISIALAIVIVVTVGFVQEYRSEQSLKALNNLVPHYCNVIRSGKTEHIVASKLVPGDLVILQIGDRVPADLRIVEATELEIDESNLTGENSPRKKSSEAISSNISLTERNNIAFMGTLVRHGHGRGIVVATGSDTEFGRVFLTMQQTEKPKTPLQNSMDDLGKQLSLISLIGIAVIVLVGFFQGKNWLEMLTIGVSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIIRRLPSVETLGSVNVICSDKTGTLTMNHMTVTKIYTCGMLAAFSLPESEHIELSVRRTVGIEKALLAAALCNNSKVHNKADSILDTTCPWAGFPVDVALIECSERFGLKDPRETYSRISEVSFSSERKYMSVAVQYNSSKMNFMKGATEQVLSSCAYFSDQDGVQHELTAEMKENIQRNEFEMAASGLRIIAVASGINTNKLVFHGLFGINDPPRPQVRESVQYLMTGGVRVIMITGDSVVTAISIARSLGMAIPSNDEEAIRNYALTGAQLDDLDSSSLRDAVSRVVVFARTTPQHKMKIVEALQSLGDVVAMTGDGVNDAPALKLADIGIAMGRQGTDVAKEAADMILTDDSFATILSAVEEGKGIFNNIKNFITFQLSTSVAALSLIAISSVFGFQNPLNAMQILWINILMDGPPAQSLGVESVDEDVMMKPPRPRNAPIISVQLLQRVLLSAFIIVTVTIVVFRVQMQDGNVTARDTTMTFTCFVFFDMFNALACRSETKSVFKLGIFSNRMFNIAVGGSLIGQALVVYASPFQRIFQTEAIGLKDVLILLACTSSVLWVDEIRKWYRRRKGLVRTKSNYLLRNV O59945 FIMB_SCHPO BINDING 29; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 31; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 35; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 40; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 66; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 68; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 70; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 75; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000305" SPBC1778.06c; HELIX 112..126; /evidence="ECO:0007829|PDB:1RT8"; HELIX 133..135; /evidence="ECO:0007829|PDB:1RT8"; HELIX 144..148; /evidence="ECO:0007829|PDB:1RT8"; HELIX 153..162; /evidence="ECO:0007829|PDB:1RT8"; HELIX 169..171; /evidence="ECO:0007829|PDB:1RT8"; HELIX 183..200; /evidence="ECO:0007829|PDB:1RT8"; HELIX 210..214; /evidence="ECO:0007829|PDB:1RT8"; HELIX 218..232; /evidence="ECO:0007829|PDB:1RT8"; HELIX 255..258; /evidence="ECO:0007829|PDB:1RT8"; HELIX 263..277; /evidence="ECO:0007829|PDB:1RT8"; HELIX 289..291; /evidence="ECO:0007829|PDB:1RT8"; HELIX 295..304; /evidence="ECO:0007829|PDB:1RT8"; HELIX 312..315; /evidence="ECO:0007829|PDB:1RT8"; HELIX 319..331; /evidence="ECO:0007829|PDB:1RT8"; HELIX 341..345; /evidence="ECO:0007829|PDB:1RT8"; HELIX 349..362; /evidence="ECO:0007829|PDB:1RT8"; HELIX 383..397; /evidence="ECO:0007829|PDB:1RT8"; HELIX 407..410; /evidence="ECO:0007829|PDB:1RT8"; HELIX 415..424; /evidence="ECO:0007829|PDB:1RT8"; HELIX 431..433; /evidence="ECO:0007829|PDB:1RT8"; HELIX 446..462; /evidence="ECO:0007829|PDB:1RT8"; HELIX 472..476; /evidence="ECO:0007829|PDB:1RT8"; HELIX 480..498; /evidence="ECO:0007829|PDB:1RT8"; HELIX 511..522; /evidence="ECO:0007829|PDB:1RT8"; HELIX 537..541; /evidence="ECO:0007829|PDB:1RT8"; HELIX 543..552; /evidence="ECO:0007829|PDB:1RT8"; HELIX 554..556; /evidence="ECO:0007829|PDB:1RT8"; HELIX 559..561; /evidence="ECO:0007829|PDB:1RT8"; HELIX 568..584; /evidence="ECO:0007829|PDB:1RT8"; HELIX 593..597; /evidence="ECO:0007829|PDB:1RT8"; HELIX 601..612; /evidence="ECO:0007829|PDB:1RT8" TURN 130..132; /evidence="ECO:0007829|PDB:1RT8"; TURN 149..151; /evidence="ECO:0007829|PDB:1RT8"; TURN 306..308; /evidence="ECO:0007829|PDB:1RT8"; TURN 332..334; /evidence="ECO:0007829|PDB:1RT8"; TURN 411..413; /evidence="ECO:0007829|PDB:1RT8"; TURN 523..525; /evidence="ECO:0007829|PDB:1RT8" CHAIN 1..614; /note="Fimbrin"; /id="PRO_0000073756" MLALKLQKKYPELTNEEILTLTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPEDFVGIFNVLKKGVEGTEVKKGRITIKGSSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDITLHPELYRLLEEDETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVLQRAEQVLQNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFNTHPGLEPLNEEEKPEIEPFDAEGEREARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASGDEMMRFKAVENCNYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTLHSLSRGGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAVIFILPEDIVAVRPRLVLHFIGSLMAV O60016 CLR4_SCHPO BINDING 260; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 260; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 262; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 268; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 268; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 276; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 278; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 307; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 307; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 311; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 313; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 317; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891"; BINDING 338..340; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:30051891"; BINDING 381; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"; BINDING 406; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"; BINDING 407..410; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:30051891"; BINDING 412; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:30051891"; BINDING 477..478; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000269|PubMed:30051891"; BINDING 477; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:30051891"; BINDING 479; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:30051891"; BINDING 484; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:30051891" CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; Evidence={ECO:0000269|PubMed:11283354}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:11283354, ECO:0000269|PubMed:30051891}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; EC=2.1.1.366; Evidence={ECO:0000269|PubMed:30051891}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:28143796}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28143796}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54200, Rhea:RHEA-COMP:13826, Rhea:RHEA-COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28143796}; CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367; Evidence={ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:11283354}; PTM: Autocatalytic methylation of specific lysine residues in an internal loop (autoregulatory loop) promote a conformational switch that enhances the H3K9me activity of clr4. {ECO:0000269|PubMed:30051891}. MOD_RES 127; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:30051891"; MOD_RES 127; /note="N6-methyllysine; alternate"; /evidence="ECO:0000269|PubMed:30051891"; MOD_RES 455; /note="N6,N6,N6-trimethyllysine; by autocatalysis; alternate"; /evidence="ECO:0000269|PubMed:30051891"; MOD_RES 455; /note="N6,N6-dimethyllysine; by autocatalysis; alternate"; /evidence="ECO:0000269|PubMed:30051891"; MOD_RES 455; /note="N6-methyllysine; by autocatalysis; alternate"; /evidence="ECO:0000269|PubMed:30051891"; MOD_RES 464; /note="N6-methyllysine"; /evidence="ECO:0000269|PubMed:30051891" SPBC428.08c; STRAND 14..17; /evidence="ECO:0007829|PDB:1G6Z"; STRAND 26..29; /evidence="ECO:0007829|PDB:1G6Z"; STRAND 40..42; /evidence="ECO:0007829|PDB:1G6Z"; STRAND 216..219; /evidence="ECO:0007829|PDB:1MVH"; STRAND 221..224; /evidence="ECO:0007829|PDB:1MVH"; STRAND 226..228; /evidence="ECO:0007829|PDB:6BOX"; STRAND 237..239; /evidence="ECO:0007829|PDB:1MVH"; STRAND 265..268; /evidence="ECO:0007829|PDB:1MVH"; STRAND 277..279; /evidence="ECO:0007829|PDB:1MVH"; STRAND 294..296; /evidence="ECO:0007829|PDB:1MVH"; STRAND 302..305; /evidence="ECO:0007829|PDB:1MVH"; STRAND 309..313; /evidence="ECO:0007829|PDB:6BOX"; STRAND 330..334; /evidence="ECO:0007829|PDB:1MVH"; STRAND 336..346; /evidence="ECO:0007829|PDB:1MVH"; STRAND 353..356; /evidence="ECO:0007829|PDB:1MVH"; STRAND 360..363; /evidence="ECO:0007829|PDB:1MVH"; STRAND 382..385; /evidence="ECO:0007829|PDB:1MVH"; STRAND 390..392; /evidence="ECO:0007829|PDB:1MVH"; STRAND 394..397; /evidence="ECO:0007829|PDB:1MVH"; STRAND 399..402; /evidence="ECO:0007829|PDB:1MVH"; STRAND 415..423; /evidence="ECO:0007829|PDB:1MVH"; STRAND 432..439; /evidence="ECO:0007829|PDB:1MVH"; STRAND 455..458; /evidence="ECO:0007829|PDB:1MVH" HELIX 44..47; /evidence="ECO:0007829|PDB:1G6Z"; HELIX 51..61; /evidence="ECO:0007829|PDB:1G6Z"; HELIX 196..214; /evidence="ECO:0007829|PDB:1MVH"; HELIX 254..256; /evidence="ECO:0007829|PDB:1MVH"; HELIX 322..324; /evidence="ECO:0007829|PDB:1MVH"; HELIX 364..371; /evidence="ECO:0007829|PDB:1MVH"; HELIX 404..407; /evidence="ECO:0007829|PDB:1MVH"; HELIX 470..472; /evidence="ECO:0007829|PDB:6BP4" TURN 32..35; /evidence="ECO:0007829|PDB:1G6Z"; TURN 62..65; /evidence="ECO:0007829|PDB:1G6Z"; TURN 273..275; /evidence="ECO:0007829|PDB:1MVH"; TURN 452..454; /evidence="ECO:0007829|PDB:6BOX" CHAIN 1..490; /note="Histone-lysine N-methyltransferase, H3 lysine-9 specific"; /id="PRO_0000186063" MSPKQEEYEVERIVDEKLDRNGAVKLYRIRWLNYSSRSDTWEPPENLSGCSAVLAEWKRRKRRLKGSNSDSDSPHHASNPHPNSRQKHQHQTSKSVPRSQRFSRELNVKKENKKVFSSQTTKRQSRKQSTALTTNDTSIILDDSLHTNSKKLGKTRNEVKEESQKRELVSNSIKEATSPKTSSILTKPRNPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAPAGTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRTIYDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG O60052 FNTA_SCHPO CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000269|PubMed:10617635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346; Evidence={ECO:0000269|PubMed:10617635}; CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.59; Evidence={ECO:0000269|PubMed:9781874}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21241; Evidence={ECO:0000269|PubMed:9781874}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29703}; SPAPB1A10.04c; CHAIN 1..294; /note="Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha"; /id="PRO_0000119753" MDPIDPELNEILDFTEYGPLTPIPQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNHTPSYIDNELEWLDEIAEDFQKNYQVWHHRQKILSLTKNYERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELLEKDIYNNSAWNHRFYVLFETSKVVSWSLEEELNYLKDKILFAPDNQSAWNYLCGVLDKSGPSKLDNLIANLRKNLPALHKPLLEFLAMYEPSSSEEIYQKLANEVDVPHAALWTWMSQRSNP O60060 CARA_SCHPO ACT_SITE 301; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 385; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 387; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" BINDING 88; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 272; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 274; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 302; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 305; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 343; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 345; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 346; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1" CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:P22572}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific small chain]: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:P22572}; TRANSIT 1..17; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC56F2.09c; CHAIN 18..415; /note="Carbamoyl phosphate synthase arginine-specific small chain"; /id="PRO_0000290599" MLRFLKPFPLRFGKRFYSKVPPVTNHERILPKQPSFPTAPAQNEIATLTIRNGPIFHGTSFGANRNVSGEAVFTTSPVGYVESLTDPSYKQQILIFTQPLIGNYGVPDCKKRDENGLLRHFESPHIQCAGVVVNDYATKYSHWTAVESLGEWCAREGVAAITGVDTRAIVTFLREQGSSLAKISIGEEYDANDDEAFINPEEVNLVSQVSTREPFFVSGGDGMLNIAVIDCGVKENILRSLVSRGASVTVFPFDYPIQNVASNYDGIFLTNGPGDPTHLTKTVNNLRELMNTYNGPIMGICMGHQLLALSTGAKTIKLKYGNRGHNIPALDIASGNCHITSQNHGYAVDASTLPAEWKATWTNLNDQSNEGIAHVSRPISSVQFHPEARGGPMDTFYLFDNYIKEAIKYQKSRTA O60070 ASH2_SCHPO BINDING 43; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 58; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 61; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 88; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" SPBC13G1.08c; CHAIN 1..652; /note="Set1 complex component ash2"; /id="PRO_0000059320" MLAHGSNDYGVSLKGNKTGSSPSKASSLNWNEPHTLNEQNTYCYCGKDRNLRFPDLQCSVCLNMFHLSCLSPPCTSMMGFSTNYQFVCKHCTEDGFERFERGVSAWKAITATAMANLVVKRYVETNPDVPVDSFNAEKMRNFQANTYFFKKKEDLIPFIEEHWQLLCPDREKVQTWQATLGSCLVANRDTYRAKDETMRNQNSEYALNNPNLFDFRSGYIFPFQRVGATVPKKRLVETETPPPSSSKLKEDYKDSKREMKRSNTPWSNASIKKNEVPTVPIRYKPPPWRDSDFETVPKLPIFYPNSSSPNFFSLSEIPFNRRGFRYSPCEAAKDLPNVMYREIELPPFTSRINWHDISTPVFIDHSALCATVEKGFRMARSNVFMTSGEWYFEIKIEKGGGDDGAHVRIGVSRREAPLDAPVGYDAYSYGLRDLGGQKVHMSRPRNFMDSFGTGDIIGLHISLPKPSFAQHTTLPSCHDRIPIRYKGQLYFEQPDYVPSKMMDELMIPSKHNRYIDLPYIPGSFIKVYKNGSYMGTAFENLLDFNPPNSINSNHYSFDDGSLGYYPSISMYGGGIARFQFGPQFSHRPLVLGSNVRPVSERYNEQIAEDVLCDILDEIDYAEDPNTSSVTIDVPQEPNAGITIIPEIKDITE O60094 DPO5_SCHPO MOD_RES 742; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 743; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC14C8.14c; CHAIN 1..959; /note="rDNA transcriptional regulator pol5"; /id="PRO_0000046471" MATKTQLELFTKLTSNDKAIRLSSAAQLIDSLSNEEELKYSLNRLTKGLSSGRESARIGFAVALTELLTRTKDIRATHVLDLLVKHNTASGNLKGQDERDFYFGLLFGLQSIVYSGILTHKESTIEDFQRVVDLLLQLSGKKNWLQDVCFYVIYKLVEQIPEISFSSNAFLAVNKLLQTPAVSKSTEGVGLFLCLTRVPDNVKSEEVAMANWEPAHPLHKSNLVTLSKIMRQADASETGGQNSAWKQKIPMVWKYIFEEYQRKTYSGLAPFHDFWAVVVDEGIFSSTSSLERKFWGFQIMELALDYVSSDNIGDIFSKNFLHCLINHLSDEDRYLYRAAKRVTSKLEKVSKQNPTLVYPIAIHLLGERGSLNFDRVTNTKLVEHILPLADEQGILQLFQLLLSYVKRCPEDIASDTKAVEWRRQWATDTMLSILRSKRSIKQEPWVRELLEIFIAYGYFEVPESEEVIPKFSEGTQNMFRLRLMSALSYLSSSAFQQSQTDHQLGDKNWPYVALNYLLELEKSPKNNLLISMDESVIEIVQKSLSVLHKVTKKIDKKAQHLQQLNAFQLLYSLVLLQVYAGDTDSIDVLEDIDNCYSKVFNKKSKRESTSNEPTAMEILTEVMLSLLSRPSLLLRKLVDMLFTSFSEDMNRESIHLICDVLKAKESVKDSEGMFAGEEVEEDAFGETEMDEDDFEEIDTDEIEEQSDWEMISNQDASDNEELERKLDKVLEDADAKVKDEESSEEELMNDEQMLALDEKLAEVFRERKKASNKEKKKNAQETKQQIVQFKVKVIDLIDNYYKTQPNNGLGFEFLIPLLEMILKTKHKVLEEKGQAVFRNRLSKLKWTEEKPSSKNVLEALKKVHVLCGKKASLGSTGSSISQLLLKLLADTPYLKEGVEVYLKSFLLWIQEPSKSHYNANIFHDFINWGAQQRLKHQQTSTAASSPQKTGHHENEKTNH O60119 SCS2_SCHPO MOD_RES 236; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 237; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 259; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 268; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16G5.05c; CHAIN 1..383; /note="Vesicle-associated membrane protein-associated protein scs2"; /id="PRO_0000314099" MSVECSGELFFYPPFTTMSKELISVHNPNPEPVIFKVKTTAPKHYCVRPNSGKIEPKSTVNVQVLLQAMKEEPAPDFKCRDKFLIQSMAIGDADTSNVENYHEFWTEMEKQGRSIFDRKIRCVYSTKQPPQSADKQVENTSTSNPPVSVEGSENLASSVGGPTAVGVSLDEAQNDFNGAKDHLSNGVNTVVPDSTFRSTFESAQIPDASVVQTVVTDADNGAASVKDTIVTAESASSKGADVARSKVQDIIDNEIPKPSESPRRSVSSTPPVHPPPPVPQNLSAVNEEFDTKKNDFDSKLPESTPAVEKVSENLGSETRESLQGAKPAAGAHSSDNALEQIKPSYSADPSSSTGASLTESPGIPPNIVIILCLIFFLIGYLFF O60126 TOP3_SCHPO ACT_SITE 330; /note="O-(5'-phospho-DNA)-tyrosine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01383" CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10131}; SPBC16G5.12c; CHAIN 1..622; /note="DNA topoisomerase 3"; /id="PRO_0000145197" MRVLCVAEKNSIAKSVASILGGGHVRRRDTRSKYVKNYDFSFNFGGNVGSSDVTMTSVSGHLTEASFPSEYSSWSSVPQDVLFDAQIITSVSKNAEVLADNIKKEARNAQYLYIWTDCDREGEHIGVEISNVARASNPSIQVIRADFNNLERSHIISAAKRPRDVSKNAADAVDARIELDFRLGAIFTRLQTIQLQKSFDILQNKIISYGPCQFPTLGFVVDRWQRVEDFVPETYWHLRFVDKRQGKTIQFNWERAKVFDRLTTMIILENCLECKTAKVVNITQKPKTKYKPLPLSTVELTKLGPKHLRISAKKTLELAENLYTNGFVSYPRTETDQFDSSMNLHAIIQKLTGAQEWDSYAEGLLAGDYRPPRKGKHNDRAHPPIHPVQMVHRSALPSQDHWKVYELITRRFLACCSDNAKGAETLVQVKMEEELFSKKGLLVTEKNYLEVYPYEKWESSDQLPEYRLHEEFQPHILDMMDSSTSSPSYITEPELIALMDANGIGTDATMAEHIEKVQEREYVIKRKKRGQGVTEFVPSSLGVALAKGYDEIGLEWSLTKPFLRKEMEVQLKNIENGQLNRNVLVHMILTQFRDVFHLTKQRFDCLKNSCRVYLMSHNEPQT O60129 FKH2_SCHPO PTM: Phosphorylated. Occurs periodically during mitosis. {ECO:0000269|PubMed:15302827, ECO:0000269|PubMed:15509866, ECO:0000269|PubMed:18257517}. MOD_RES 319; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 321; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 322; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 336; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 375; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 535; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 626; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16G5.15c; CHAIN 1..642; /note="Fork head protein homolog 2"; /id="PRO_0000091905" MTVRRLESKSEHISDDEERKEQLDYKKQMDVDTDRNIVLNGRLESQIAKLSVPPHEMRVVDDYSNSKNAERHSGEIQAYAKFAGSTWTYYVKKIRIILGREPANPSPKGKNEDLEVIDMNFGPSKVVSRKHAVVEYDLDDQTWNCSVYGRNGIKVDGKLFKNGETVKLTSGSILEVAGLQMMFVLPNAAEQKQTDESTIKEDAIKSEISAAVNDAAEYGDNKKPPYSYSVMIAQAILSSSECMMTLSNIYSWISTHYPYYRTTKSGWQNSIRHNLSLNKAFRKVPRKSGEQGKGMKWSIVPEFREEFIAKTRKTPRKRSPSSPVPLLAKKREGSPSLPIPILPKMKDTSIPAAEPASSTTSARDQTPSTPKDVGSPSTAETSAEEKQMETYKTPTHAALSDIISTHDYALDANSASQTKKAAFGSPIGSSTYPTSSPAPFWKYVAVPNPHDWPQVGSYDTISPYRNPVNSHLIYSQIQQSSPKKIDEQLHDLQGVDLVNGFEGISSWRESMVNKLRSSVSDSPTMNLANSNSKSSPVAVQRVSTLPQASANKQAKEMESKMSNSPTQKSKTEENNQAVRAILDASATMEKQYDLHRLPTPTSQTESASVPQIANPPNSQNLVKEKSPQQYIQVPQSNVKSSA O60132 TEA4_SCHPO MOD_RES 35; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 40; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1706.01; CHAIN 1..821; /note="Tip elongation aberrant protein Tea4"; /id="PRO_0000259412" MLHMNSASSADSMEIMESHFDPTQQNDSTIIESRYSPEEYLEQSFEIQRIISGENSEPQTVASQEISDSQEEDTTLTSSQFEDCGTEYNEVVEDDEFRSEDEDDFMDEEEEYALYEAELSSSPSIHEEVIDCNFVHAIRGFEATVEGQVDATKGDMMILLDDSNSYWWLVKMCKNLAIGYLPAEYIETPSERLARLNKYKNSETSNSQQSVTLPPLDIVEKTLEAPSPNFRIKRVTFTCSSNSSDDEMDSENDYEAMVNRTVAENGLEIEFSDSSDSSLSAEYRSESEDHVTDSPAYVDLTELEGGFNQFNSTSFQSTSPLGLEIVETEINGSSTTADSKNSHSPYSKFSSAYPDAENSNISKINISIAGNKELYGNATQSDPSLYSTWIANKHKTASSATVDSPLRRSLSVDAMQSNASFSSYSSTSNTDKSLRPSSYSAVSESSNFTHDVSRDNKEISLNAPKSIIVSQSDSFDTSNVTQDAPNDVEKEPISGQMPNNLSVQSLKQLEVYPIRHSVSIEMPSEKLLSPRLYSSSTPSSPTKGFQKDDEEDSENRKQADKVELSPSSLLRQMSLPVDSSSQSDAQCTTSSVYITAERKAFSQSSIDLSTLSNHHVNNEINRRSFAGGFTSLADELSEMRELLHESPAPLECNEEMVIPTPELDASSAIPSSSISHDEDLLPRKNTEESTSSSSFSSLITSPASLQYDENPFKQSVVAELNNNSSSVPFVDSAHASDIHAYDNDHVSTKNKEFNRRLREFILDPDSLSGLYWSVKSAGVRASRRVSRNIEGESVSSDLDDIFANVLKGLSDEMASLLNTNR O60158 BQT4_SCHPO SPBC19C7.10; STRAND 33..39; /evidence="ECO:0007829|PDB:5YCA"; STRAND 42..52; /evidence="ECO:0007829|PDB:5YCA"; STRAND 59..65; /evidence="ECO:0007829|PDB:5YCA"; STRAND 103..105; /evidence="ECO:0007829|PDB:5YC2"; STRAND 106..108; /evidence="ECO:0007829|PDB:5YCA" HELIX 16..18; /evidence="ECO:0007829|PDB:5YCA"; HELIX 26..31; /evidence="ECO:0007829|PDB:5YCA"; HELIX 73..80; /evidence="ECO:0007829|PDB:5YCA"; HELIX 86..99; /evidence="ECO:0007829|PDB:5YCA"; HELIX 115..124; /evidence="ECO:0007829|PDB:5YCA"; HELIX 128..136; /evidence="ECO:0007829|PDB:5YCA" TURN 54..56; /evidence="ECO:0007829|PDB:5YCA"; TURN 66..68; /evidence="ECO:0007829|PDB:5YCA" CHAIN 1..432; /note="Bouquet formation protein 4"; /id="PRO_0000317335" MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVNKGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITKLESEVYYEKRKVRALGGIAIGLGVGAILPFLF O60165 SPN7_SCHPO BINDING 25..32; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 86; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 166..174; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 224; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPBC19F8.01c; CHAIN 1..428; /note="Septin homolog spn7"; /id="PRO_0000173509" MNKGPRHRPKFLSKKGKKLRIMVAGSSYTSYQACINSLCSKQILEAETEIDPLKAHIDRILEIREFNADILEDEFHVDLTVIEVNGFGDKIDNSASFEVVTHYLESQFDQALIEESKIKRNSKFTDTRVDALLYFIAPRGHCLSEFDLEAMKRFSKRVNVIPVIGNSNAFTEEELKNFKDVIMKDLKQCNIKVFDFPWDPEEDEDEVIEDNKRLWESVPFAVSGGVSEEDEEGYQRIVKKFQWGTFVIDDPAHSDFLNLKTVLFISHLDILKSITKQTYYENYRTEKLSNDSPSNTSLSLQKQNSIVANEDKRSVNGSERTETRSSIDQSEMRTNVSDSTKSEELKKINSIKVDNTSSLKCDSYGNTKTKTNQLNCEQIGLEVISPKEFPHRTTSSRNSLPNNTTKELEMKKMDDLSHERYENLPFYR O60182 RFC1_SCHPO BINDING 362; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 374; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 416..423; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 519; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" MOD_RES 27; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23E6.07c; CHAIN 1..934; /note="Replication factor C subunit 1"; /id="PRO_0000121775" MSNSDIRSFFGGGNAQKKPKVSPTPTSPKPKRSLKKKRIVLSDDEDGTIENSKVPASKSKVQKRNESEDISHSLPSIVHEDDKLVGSDGVSTTPDEYFEQQSTRSRSKPRIISNKETTTSKDVVHPVKTENFANDLDTTSDSKPVVHQTRATRKPAQPKAEKSTTSKSKSHTTTATTHTSRSSKSKGLPRFSDEVSQALKNVPLIDVDSMGVMAPGTFYERAATTQTPGSKPVPEGNSDCLSGISFVITGILETLTRQEATDLIKQYGGKVTGAPSVRTDFILLGENAGPRKVETIKQHKIPAINEDGLFYLITHLPASGGTGAAAQAAQQKKEQEEKKILETVARMDDSNKKESQPSQIWTSKYAPTSLKDICGNKGVVQKLQKWLQDYHKNRKSNFNKPGPDGLGLYKAVLLSGPPGIGKTTAAHLVAKLEGYDVLELNASDTRSKRLLDEQLFGVTDSQSLAGYFGTKANPVDMAKSRLVLIMDEIDGMSSGDRGGVGQLNMIIKKSMIPIICICNDRAHPKLRPLDRTTFDLRFRRPDANSMRSRIMSIAYREGLKLSPQAVDQLVQGTQSDMRQIINLLSTYKLSCSEMTPQNSQAVIKNSEKHIVMKPWDICSRYLHGGMFHPSSKSTINDKLELYFNDHEFSYLMVQENYLNTTPDRIRQEPPKMSHLKHLELISSAANSFSDSDLVDSMIHGPQQHWSLMPTHALMSCVRPASFVAGSGSRQIRFTNWLGNNSKTNKLYRMLREIQVHMRLKVSANKLDLRQHYIPILYESLPVKLSTGHSDVVPEIIELMDEYYLNREDFDSITELVLPADAGEKLMKTIPTAAKSAFTRKYNSSSHPIAFFGSSDVLPMKGSAQREVPDVEDAIEAEDEMLEEASDSEAANEEDIDLSKDKFISVPKKPKKRTKAKAEASSSSSTSRRSRKKTA O60184 CYC8_SCHPO MOD_RES 893; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 895; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 897; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 898; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 992; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1059; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1061; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23E6.09; CHAIN 1..1102; /note="General transcriptional corepressor ssn6"; /id="PRO_0000106418" MPQSQVATASPSQNAQPNHGMGSKVLSSDPNASLPPQTAYYASPLHANSVSLPPSHLPRSTLHPLLSQQQQPAQQSPSLGPAQQNIQQPPSVSIASQPHYAEAIVPIQQVLQPQQYRQLPPNMVAATNAPQQHPQLQRMMPILSSNQPIQQLPLPNQASPYIPVPLQQQQQSQPQQQPQQQQHQQPQQPQPPQQPLQQQQQQRQLHSGIQQPVSTIVSQNGTYYSIPAVNHPMAGQPIAIAPVPAPNQAALPPIPPQALPANGTPNTLASPVTLPAANSAVQNAQPVPMTSSPAMAVVPQNKTAATSTLAAQQGANVLPPNAPESVRHLISLNEETWIQIGRLAELFDDQDKALSAYESALRQNPYSIPAMLQIATILRNREQFPLAIEYYQTILDCDPKQGEIWSALGHCYLMQDDLSRAYSAYRQALYHLKDPKDPKLWYGIGILYDRYGSHEHAEEAFMQCLRMDPNFEKVNEIYFRLGIIYKQQHKFAQSLELFRHILDNPPKPLTVLDIYFQIGHVYEQRKEYKLAKEAYERVLAETPNHAKVLQQLGWLCHQQSSSFTNQDLAIQYLTKSLEADDTDAQSWYLIGRCYVAQQKYNKAYEAYQQAVYRDGRNPTFWCSIGVLYYQINQYQDALDAYSRAIRLNPYISEVWYDLGTLYESCHNQISDALDAYQRAAELDPTNPHIKARLQLLRGPNNEQHKIVNAPPSNVPNVQTAKYINQPGVPYSNVPVAQLSGNWQPPHLPQAQLPSATGQSGVVQQPYQTQPSVTNNNVATQPVIASTVPVQTAAPSSQTAVPQTIHQSNAFTPRGKHASGSRNSISSTKSPQHKLSDQPRSRNNSISNVSHRERSNSVSSKSRETRTSASNESDPKKSTQRDSSKKLENSTVVSGSPSSSSKSDAAKSIKPQKPEPALKPVEGTADPKSTKRNHQETEKTADTDVSSTEPVKRQKTADVNDDVGEEEVKQSVSEQVDSAQLTSEPKSESLPKSPEEKSDDTSNDVTTENTNDINGDSNMDNVATVDKSTDAVDTSTATVAATTTTAEEELPQKESQERSSPSPENQDSTPLAPKSVSPKQAARTLDIDENYDDDEGEKETVSV O74113 CDC45_SCHPO SPAC17D4.02; CHAIN 1..638; /note="Cell division control protein 45 homolog"; /id="PRO_0000192818" MFIKRSDYASAYLKIKEASVSGGCTVQLFVALDPDALCACKLLSTLLKGDFISHKIRPVSGYRDLEQANKTLLEQNEDIKFIILLNCGTMVDLNNYLVSMEDVSIYVIDSHRPHNLNNIYIENNIFVFDDGDIEEDMNKIHDAWYAFNSHELSDEENSDSSNEREEEVEDDNRSVESYSSSDYQARSRRRFSEETTQRRAEIKEKRKKRKEFASILSEYYEKGSWYGESITNILFAVASMLGREDNDMLWLAIVGLTCLEIHCQSSKKYFNRSYSLLKDEVNRLNPSPLENQIVGRAHGKTPHDQSIRLEDEFRFMLVRHWSLYDSMLHSAYVGSRLHIWSEEGRKRLHKLLAKMGLSLVECKQTYIHMNMDLKKTLKSSLKRFAPFYGLDDVIFHSFTRTYGFKCTLSASDVSYAISALLEMGNTGVLLQSKTVARSPDMTEEEYLEKFENAQNQEWLHNFYDAYDALDDVDSLERALKLAMHLQRAIVRTGITLLEKRAIKTLRSFRFGLINEGPDLKIFMHPLALTKMSLWIAEAINEQEREFGKLRHLPLVLAAFVEEKNRYLIVGTSTSAFTSNEDDDDDDGHGHNRFGVAFQEVANMTSATLQMDCFEASVIECQKSDLGVFLESLSFKTLL O74135 CKI3_SCHPO ACT_SITE 134; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 21..29; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 44; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC1805.05; CHAIN 1..439; /note="Casein kinase I homolog 3"; /id="PRO_0000192863" MSTTSSHSNVVGVHYRVGKKIGEGSFGMLFQGVNLINNQPIALKFESRKSEVPQLRDEYLTYKLLMGLPGIPSVYYYGQEGMYNLLVMDLLGPSLEDLFDYCGRRFSPKTVAMIAKQMITRIQSVHERHFIYRDIKPDNFLIGFPGSKTENVIYAVDFGMAKQYRDPKTHVHRPYNEHKSLSGTARYMSINTHLGREQSRRDDLESMGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQVTPLKELCEGYPKEFLQYMIYARNLGYEEAPDYDYLRSLFDSLLLRINETDDGKYDWTLLNNGKGWQYSAAKQHVVQRRHTQGTNNRRQSTIPPYARTRQNLLSSPSKQTPVNNVVDASVATQKDGIPGKAASPQVQQQQQTSSAQQQQPQRVEQPAPQTTQPTQVDTQQAAKPAPSKEKSRKKFHLRLLSCCISKQE O74184 WAT1_SCHPO MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573" SPBC21B10.05c; CHAIN 1..314; /note="Target of rapamycin complex subunit wat1"; /id="PRO_0000051141" MSVQYPPQHSVLLVSSGYDHTIRFWEALSGICSRTIQHADSQVNRLCISPDKKFLAAAGNPHVRLYDINTSSQMPLMTFEGHTNNVTAIAFHCDGKWLATSSEDGTVKVWDMRAPSVQRNYDHKSPVNDLLIHPNQGELLSCDQSGRVRAWDLGENSCTHELIPEEDVPMSSITVGSDGSMLIAGNNKGNCYVWRMLNHQGASLLQPVVKFQAHQRYITRCVLSPDVKHLATCSADATVNIWSTEDMSFMLERRLQGHQRWVWDCAFSADSTYLVTASSDHVARLWELSSGETIRQYSGHHKAAVCVALNDYQI O74191 FKBP4_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:10544281}; MOD_RES 192; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 213; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 249; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1347.02; CHAIN 1..361; /note="FK506-binding protein 39 kDa"; /id="PRO_0000075315" MSLPIAVYSLSVKGKDVPAVEESTDASIHLTMASIDAGEKSNKPTTLLVKVRPRIPVEDEDDEELDEQMQELLEESQREFVLCTLKPGSLYQQPLNLTITPGDEVFFSASGDATIHLSGNFLVDEEDEEEEESDEDYDLSPTEEDLVETVSGDEESEEESESEDNSASEEDELDSAPAKKAQVKKKRTKDESEQEEAASPKKNNTKKQKVEGTPVKEKKVAFAEKLEQGPTGPAAKKEKQQASSNAPSSPKTRTLKGGVVVTDVKTGSGASATNGKKVEMRYIGKLENGKVFDKNTKGKPFAFILGRGEVIRGWDVGVAGMQEGGERKITIPAPMAYGNQSIPGIPKNSTLVFEVKLVRVH O74304 WIN1_SCHPO ACT_SITE 1244; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 1126..1134; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 1149; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; MOD_RES 224; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 226; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1006.09; CHAIN 1..1436; /note="MAP kinase kinase kinase win1"; /id="PRO_0000086816" MENILDPSVVNSHILENGSRRSSINPILDSELRDKTFEKAHRRSLTLLSSFTSSMLELPNNGKEENHRRPSVARSSSDRSKASAKEDLFSEAFRMAEQPPAEALTISTPVDPINIDELDRAYAVSPSDTSNLLHPPTSSSSIPIPIKNAGHSNLDHPIRPSLQSSISSNRIIKSPGIKEDDYMHRGRSISSPMIDVEHINSTAVPSKTKNLPEKPKRSHKLRNSITFAKIEDHPERKSQLRRLSSSLKCFDPEYDYNDPSLSIRRDSSTYYFSNVNETYDEEDSDLDSETSTVNWVQSVLNLPSLLSDDLMANPKNKERFEWQYMLTSVLTGDIVRSEKLRLRKIASSREGRNSDYSDNLWMEIWCWLTHRSVDSYRENLKHLRTGMVDVLLAIMNFHWDESNELTPIVAVDNMLQKLDKYERLYPSRRSILQEHSLYASESFQHKLDVLTAYSNVTHALEIQVNIIRSWVGNEEMDITKNTTNSINNVSQISNGPFVERFYRETGLIRAFEQRIMTNMNSVLSKVCNTIVTYADDLKSYGLPLIADDYMRLLSFPFRLIKEFLNLRLSCAENITSISLFTIDSLLDDLRNTMKVAVHIIQQHTVLIKPFRDDSKFVDENQSLNNILVASLKFYFNLLHRKVRNGCALLHFKETEILEGEWDFLLAVCPHIEHGFQIMSKSLSSLVGEILTNINRYLKDQLQGPDTDDSALITSFYIKVLDCVRIRFRKLMSFTRILKAHLENSCEYVIKENSLSLLIQRLEESNHVLTYTASIEHEGAYVIVPGHLVDSPNILREVLSMTFNKGDNNFESVPPYAVVLAPDSSICWNGHVTDLDIPEVSISIAPNCVRLVTLATANQLSVIEDYFISIVGDTVSLVDSAKANSSKINKQMTKIKRNSLKLALSLLDVIQTIRTRYHGMNCQNLIHYSFSYAIEFAQRLMRLSILDASSIGLIRRKMIQLAISWVGFIYEDCSPTDRNTFRWTVTALEFAMIMTYGSNILMIDKKSFEELKEKVGKCVALLLLHFDVMGTKHAGRSMDQQAGDIPARLVRNNSDRSRLSDNELASFVKEEVMHRIIELESNRRDRLYKSQLIGRVLDDTTKENRLLKELASSKSNITIRWQQGGLIGSGSFGTVYRAVNLDTGDLMAVKEVALHKPRISRPMIKRIKGEMLVLELFDHPNVVSYYGIEVHREKVNIFMELCQGSSLFEFLRYGRIEDELVIQVYVLQLLEGLAYIHSCGVSHQDVKPENILFDHNGIMKFTDFGSAKMSGSASTKIFEQLTQQEEEEFEKDSEFLQHLDQNRGYSLTGTPTYMAPELILGNPSERVGAMDIWSLGCVIVEMATGSPPWPRLDNHFSLMYHIAAHNPPIIPADDQLSPLGQNFLKRCFVSDPNQRATAAELLMDPWVYPLRAGTEFDLMNSSVVESAPSTNGAPLEL O74309 SLM9_SCHPO MOD_RES 406; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 421; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 422; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC15D4.03; CHAIN 1..807; /note="Histone transcription regulator slm9"; /id="PRO_0000051219" MHIFVPKLLENHQFSSISSSKDFVAVSAETNVYILSKDFFYPKSSEKRIIQSLNGHKTTHLSFDSPISCIRFTYDGSCLAVATEAGTFLYHSEKWDKAFQVLSGPAYEVCWSQQGHILATSWKQISIYVKDEGLRTETIVKKTEHADSNHQPAVSIEESKEAVESTSQSSEISFKLIKVIEGHHTFVGGLAFDPMGQFLASQSFDHTLKVWKLSTFGVEKSIAKPFEQMPTGNRFLRLSWSPDGAHIASVNAVNEGAYVIAIVQRDTWTYDINLVGHQGPLECATFNPYLYEDPFQKSIIASAAHDGCVSIWNTACARPMAVIHELSCSSFVDLQWSTSGFELYGVSLDGNLMLLQFEESEFGEKMDTIHYPDDLSYFNSSRSKAHVNKNAAADRTTSPTQGQPESPSKSILLRPPPSIASSPESKRRKCPKKFVARPPVPHPTSLYSQIRIGCPYLKPKLVISKSFGTLIVKNHNQLSLLKCTFSNLDGNDCSWFSYLPNAIVLANGTSVFWAVATEDSSIYIYSPAGRLLLPPVVVAATPCFLECCGDFLCCIVSTGLLYIWNIKNFEAIHSPVSTLPLFHSNFSVSKIARGPSIEQFFVTKQGHPVAIMSDGNAFAFIRDSSSWLRVSEGWWMIGSQYWGPLASESNEESPLGFLERCTDEEIIKAGRGRFLQRLVKALMLRQGYDNYEMLVSIRHLENRLMSSAKLDLEYDFRENLILYAKKIAEEGMKDKMDELCKELLGPLRIPHNGIDTVKVGNRLWSPTIAGNNKRNLLKDIIIHTAKYRDMQRITSQYSDLLRRSALL O74312 ATG9_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088; Evidence={ECO:0000250|UniProtKB:Q12142}; PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}. SPBC15D4.07c; STRAND 390..394; /evidence="ECO:0007829|PDB:7D0I"; STRAND 455..457; /evidence="ECO:0007829|PDB:7D0I"; STRAND 600..602; /evidence="ECO:0007829|PDB:7D0I"; STRAND 640..643; /evidence="ECO:0007829|PDB:7D0I"; STRAND 647..650; /evidence="ECO:0007829|PDB:7D0I" HELIX 183..195; /evidence="ECO:0007829|PDB:7D0I"; HELIX 198..223; /evidence="ECO:0007829|PDB:7D0I"; HELIX 253..287; /evidence="ECO:0007829|PDB:7D0I"; HELIX 302..312; /evidence="ECO:0007829|PDB:7D0I"; HELIX 336..343; /evidence="ECO:0007829|PDB:7D0I"; HELIX 345..355; /evidence="ECO:0007829|PDB:7D0I"; HELIX 373..382; /evidence="ECO:0007829|PDB:7D0I"; HELIX 384..387; /evidence="ECO:0007829|PDB:7D0I"; HELIX 396..398; /evidence="ECO:0007829|PDB:7D0I"; HELIX 401..403; /evidence="ECO:0007829|PDB:7D0I"; HELIX 404..410; /evidence="ECO:0007829|PDB:7D0I"; HELIX 412..425; /evidence="ECO:0007829|PDB:7D0I"; HELIX 427..447; /evidence="ECO:0007829|PDB:7D0I"; HELIX 449..452; /evidence="ECO:0007829|PDB:7D0I"; HELIX 461..464; /evidence="ECO:0007829|PDB:7D0I"; HELIX 472..480; /evidence="ECO:0007829|PDB:7D0I"; HELIX 483..489; /evidence="ECO:0007829|PDB:7D0I"; HELIX 496..520; /evidence="ECO:0007829|PDB:7D0I"; HELIX 538..555; /evidence="ECO:0007829|PDB:7D0I"; HELIX 565..576; /evidence="ECO:0007829|PDB:7D0I"; HELIX 581..583; /evidence="ECO:0007829|PDB:7D0I"; HELIX 591..599; /evidence="ECO:0007829|PDB:7D0I"; HELIX 603..623; /evidence="ECO:0007829|PDB:7D0I"; HELIX 626..628; /evidence="ECO:0007829|PDB:7D0I"; HELIX 629..638; /evidence="ECO:0007829|PDB:7D0I" TURN 297..299; /evidence="ECO:0007829|PDB:7D0I"; TURN 364..366; /evidence="ECO:0007829|PDB:7D0I"; TURN 644..646; /evidence="ECO:0007829|PDB:7D0I"; TURN 651..655; /evidence="ECO:0007829|PDB:7D0I" CHAIN 1..702; /note="Autophagy-related protein 9"; /id="PRO_0000119837" MFYQPAQNKKQYDDLADIEAQNNVPNTQEVLEAWQESLDSDEDESSPLEESNGFTISEHDDFVKSVPRKNNPTDLLYSGKLLDSDEPPSVHGNSSKVPSKHPSPSFPETTSLRNLQNGSKQKPALPNFNDPHFYNEDVTRSGHPNRSIYTQLPRNEFSNARVLWNRLSARDRVLWRWANVENLDSFLQQVYTYYTGKGLSCIIVHRLFQILTVSFVIGFTTFITSCIDWPAVTPHGSLAGVTKSQCIAQMSPITYLVLWLFLSFLLALWIYYLTDIPRLWQMREFYIHALKIATADMPTVSWQRVLYRLLKLKNVNALTAEDGRVVSLHNMKRLDAYAIANRIMRKDNYFIALINNGIINIELPLLHRRILTHTTEWNINWCIFNFVFDEQGQLRSAFRNPNSRKRLSEELRRRFIVAGFLNCLFAPIVAIYLVIHNFFRYFNEYHKNPGALSTRRYTPLALWTFREYNELQHFFDERINDSYAAASHYVSQFPDFNMIRLFKYISFILGSFTAILVIITVFDPELMVTFEITKDRSVLFYLGLFGSLIAVSRSIIPDETLVFAPEKALRRVITFTHYMPGWWSDNMHSKAVQQEFCSLYSYRIVNLLWEILGILLTPVLLFFTFPSCSQDIVDFFREHTINVEGVGYVCSYAVFQDNPPYESVASLVQSRKISPLIQNKPELSRISFYEQFNTEAPRRDLR O74327 AVT5_SCHPO SPBC1685.07c; CHAIN 1..420; /note="Vacuolar amino acid transporter 5"; /id="PRO_0000316193" MSGYSPLSSGPADVHIGKAGFFSSVINLANTILGAGILSLPNAFTKTGLLFGCLTIVFSAFASFLGLYFVSQCAARLPRGKASFAAVAKHTFPSLAVVFDASIAVKCFGVAVSYLVIVGDLMPQIAPSLGLSSPMFLRRQTWIVFALFVLTPLSFLKRLDSLRHTSVISLIALCYLVFIVLYHFIIGDTVKGEIRYFVPESGFGYLSVLPVFVFGFTCHQNAFSVINEVRNFSQGFVNFTMFTAIISSTLLYLLVAITGYLSFGSLASGNIIAMYDNTSIWIIGGKLAIVVLVLFSYPLQCHPCRNSVYQAIRRSYSAHDMSDGYHAVITLCILLFTHSLALLLSSLEMVLAFVGSTGSTFISFILPGSLYYFFSHKVASPGNSSPLQLRISRAFAAGLAIYGTVVMILCLNINIAKLSH O74352 HOB1_SCHPO MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 299; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC21D10.12; CHAIN 1..466; /note="Protein hob1"; /id="PRO_0000192954" MSWKGFTKALARTPQTLRSKFNVGEITKDPIYEDAGRRFKSLETEAKKLAEDAKKYTDAINGLLNHQIGFADACIEIYKPISGRASDPESYEQEGNAEGIEAAEAYKEIVYDLQKNLASEMDVINTRIVNPTGELLKIVKDVDKLLLKRDHKQLDYDRHRSSFKKLQEKKDKSLKDEKKLYEAETAFEQSSQEYEYYNEMLKEELPKLFALAQSFIAPLFQGFYYMQLNVYYVLYEKMSHCEIQYFDFNTDILESYERRRGDVKDRAEALTITKFKTAKPTYKRPGMGPGGKDATASSSSSFSSKREEAAAEPSSSTATDIPPPYSTPSVAGASDYSTPSAGYQTVQTTTTTTEAAAAQYPQAAFPPPPVMPQPAAAAVTTPVAAPVAAAAAAVPVPPPAPAPAAAPAAEHVVALYDYAAQAAGDLSFHAGDRIEVVSRTDNQNEWWIGRLNGAQGQFPGNYVQLE O74354 DNT1_SCHPO PTM: Phosphorylated by clp1. {ECO:0000269|PubMed:17538026, ECO:0000269|PubMed:18257517}. MOD_RES 174; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 306; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 513; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25D12.02c; CHAIN 1..599; /note="Nucleolar protein dnt1"; /id="PRO_0000303893" MRTTLRLHIIKDGEQDNQFMILFDPSSSISLLKEKVQETYKSLYPFESNINIRNIKNEESYDIPNEYLVGEIFPTNSKVIVESFSSPLKKLDGTMINFKEKNIQHDLDGVENDFATVQSASNGVHAINGKRTHPDESENPRKLPKKNFVEAIDANSPGFVYRPTSIRDRAYSISSNHDNESTLTEGIALKEIESPDKDRKADGIVNLSVTQEEDDNHQSFNSSLTPSQPTTYNRANFFSINDASSDSSSDAPLRTLSSPSRLRMKDNDRKYLVEHSPAALIKESETIDGIDDKSLRSSTREVSVESPNEDSVNDDSSSDVSDEKETEAKHEIRAPAIIVRETSSHPSTAVPSENDTTESENDTLSESSTTSISSSPSENSDTSDDLTKVDSPNKSLVNDNVSAKHDKESENGKSKFPPPSQTLVTTSTISAAGNEPSDEIGSENDSDSDSDSDSSVPLSQLQKKSQQRNSVSHEIQNRGTKGSPKEPKAKPSTERPETHRTLSYSRLSELSKTFSPEIREPSLTKKTAVSMQESKEEGRSDESSESEESGSSSDESDNSEKEDRSNPIPVEKRASTVLNTKKKRKAKRNSALAGLAALV O74360 RGA4_SCHPO MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 625; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 738; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 740; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC28E12.03; CHAIN 1..933; /note="Probable Rho-type GTPase-activating protein 4"; /id="PRO_0000075902" MNSGTTLHLDRLSLETPSERTCFCIKCWESVPSTSQVWFGGKCWHSDCFKCVNCNKKLDPSSEDFSQDDQKQIFCKLCVDICNGCSTPICEFNAVSNSQANHPCCSNCRAFINSNAFGKFKGQHYCLPCLRKQDEENQKAVMESASGFIPLRNIAQTAENTSLTGQNQGFQNPHFIASDSPSSVLSGRMQNTSSPTNSLRPQLKVQTNGYETPGDINSAKSYKDIQKDFLLKPKNSFVKTSPSPLANGPSFRSANASPFDSCDSFHSGSSIPIEPVSSRQSSVVNNNSVQQPVAYHAFVQSPTENGTLPQLPKNESVVNPPPLRRSSTMNYKSVSTTTSPSKYGYVSGRIALSPIHLRGALRDVTNKCNLKVPRNRNSLSNLDEYYVNGLESDETPTKARFPRYPTVFNKLDDKRLSSEPNGLKKRLTNSSNYEASPRAKSLNLSQVSLHQACEPEYNRSSLVRASDVFTSNVFDATEESANELAIRISELQAEVGTLLLEATSLASIIEQQTPVSPEAFKQELVADLNYRLDYLRKSFQPELSTLLLRRDALSTTVSKLQNAYSTVMEETAYLNVKNTELVSLNNQLERELAYLREQQHKKRTSSSFGIFNNDKKSNRTISTPSPRESFSRLQMVASSLGFRPKDNKDKESGGYNKRNSKIDLKKSFSKRFHWKRDSPHMSSTPSISEEHLASEEQEDFVPAVGHCKLCGKYSNELRAHYQDCVSSTIDRQYQSKKSESPVWALNPDDFDQNRLTLLRVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSEDISAVTSVFKQYLRNLPNPIITYDQYFPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDVIDMTVKNYSLAFLIDHVHEVFA O74365 SOL1_SCHPO MOD_RES 852; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 855; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC30B4.04c; CHAIN 1..865; /note="SWI/SNF chromatin-remodeling complex subunit sol1"; /id="PRO_0000318141" MNNQGFVPASDYPTAVSYPTQGQSYNTQEEQPAYPQRFSTSQGMYAAEYGNANMMNTSENEPNNLAHSQPFRQSPSTQRNLPNQSFDFASNGAWNGSGSVKYSSPMMPSSRIPFQQEKEAAMQQQQQQQQQQQLYQRQMQSREALLSQQIPPNQIGINAHPAVRQTPQPAPSPNTPSGNANQLTPAYAASFDKFMVSLISFMEKRGTPIKSYPQINNTPINLMMLYALVMRAGGSRQVSAHNFWPKISASLGFPSPDAISLLIQYYNSYLLPYEEAWLAAQQQQKSLQQAKANHSANVQSRPKNYPQKPVQTTPEAVHANGSMHGSLHSKSPSPAFTANRFSPAAPTTVSSERNAPPYPSAPTRPTPPTVQTSSSAAPVDSAEPVAYQPIKKPIDPMLGYPLNVAATYRLDESLLRLQMPSIVDLGTVNIQALCMSLQSTLEKEITYAMNVLLILTNDQKWMFPLSECQDVVDALIDVATQCLDNLLSVLPNEDLMEIADKRPSYRQLLYNCCVEISQFSREDFSNSLSENKTKDSINAIDVHNSEQNLLAVFVIFRNLSHFEANQNVLVQNPDFFPLLIRVVKSLNFHATSLLRSSRNTLDLHKDVLIVLCQLSQNFILPNVDVARHVLLFILSFSPFNRKKSKTILNDTLPTSIPSYTPATHPYAGPAINAYAKLLAKDANNKTNFQAIFDNNPKFLDSLFLLLASVVPKFNRHCLKICERRLPLLQQSFFCLAATVSYVKQSEQAANWCNIGEGFFVSMLRLLILLSGHPSLNPPSRVASQYPTTNPFRYVIQSGISTVRRLLSLVEAGNISLSSFPKSETLLAVLLAPTTETSFLKEISNLLDRTGDSDASLENTDDKSGI O74369 CSS1_SCHPO ACT_SITE 289; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 49; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPBC32F12.01c; CHAIN 1..424; /note="Inositol phosphosphingolipids phospholipase C"; /id="PRO_0000075691" MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLGITYQYMARERLHMRLRIAHLLISIPLIIGVHVAIAWCDPAWLKVIILFFTVMLTIAAVVNGFCIGLLFGRWEFNGLLEFVAELKEQKLLCKQYLVDHPLPFAKS O74372 DUO1_SCHPO SPBC32F12.08c; CHAIN 1..282; /note="DASH complex subunit duo1"; /id="PRO_0000215594" MTSELQQELQILRSFNYTIEKLTDGLSASKEKIKSFETSINNSNRLIQLWSSVLSQTEHTQNLILNSDWKGLSFDNEELERLQHQKMLQIQAEEQRKIELQQEQERLEQERRQKEEAIALQKQQQQRLLRSKDPKVRPARRAASSYVPSRPSHVPRSSSMNVRSRVSMATTSNPNSLRTPSSSFASHRQSAIPKSATSSAPTIPTSNLPSVASSIPNNGLNSSNRKSIISKTSSRLRPPSRVSNVPSVPQHPSTRSRTSTRETTQPPFTTNPSNRSKRTTLR O74384 ERFB_SCHPO ACT_SITE 212; /note="S-palmitoyl cysteine intermediate"; /evidence="ECO:0000250|UniProtKB:Q8VDZ4" CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000305|PubMed:23843742}; PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}. SPBC3H7.09; CHAIN 1..350; /note="Palmitoyltransferase erf2"; /id="PRO_0000212946" MSYEKHSDAKASRYAWNQPWNPFEVTLSDPTYPMNLEEKNQIPYRFQSVPDDVPEVPHIESRYKNLPGNNIYLCCGRLQMSSQYKAFLISLFALILPGVLFFIFSAFWLWHHVSPAVPITFAYLYALAVVSMFKCSTADPGILPRNAYSLTYNPAHPWSVIPEDRKVLVGSTRSDSVFVNTVYCHTCHLYRPPRASHCHLCDNCVEYLDHHCIWLNTCIGRRNYRYYFIFLLSVVLSALYLTGLGFYTSIGSFHESTDTNFAAHLRRPWAGVSFFLGIYGALGAILPGILFCYQCYLISVGQNVHEYLRAKSTETEDVHPFHDSIWLNFLVVLCRPKNVSYVRPTRKSYV O74420 WTF13_SCHPO SPCC162.04c; CHAIN 1..388; /note="Meiotic driver wtf13"; /id="PRO_0000193227" MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV O74423 ENT1_SCHPO MOD_RES 212; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 216; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 255; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 406; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC162.07; CHAIN 1..702; /note="Epsin-1"; /id="PRO_0000074523" MKAAVRSVKNFSKGYTDTQIKVRNATTNDSWGPSGTAMAEIAELTYDQNEMLEVMDIIDRRLNDKGKNWRHVFKSLSLLEYCLHNGSENVVRWAKDNIYIITTLREFVYVDDNGHDQGQNVRTKAKEITSLLEDEHALKEARGDSRERDRDRDRTRSSRFDDDDDDRAPYEESRLSRAPSRASRYDDDDRDHRSRRRSRSRRPGRSRSRRRSRRPSPSAEHNSAEENDPELQRVIEESKRQAEEDAKRRNMANDSEAELQKAIQLSKEEDEARQRHQREREQQEQAFMGNQQNAYQPVDFFGNPVQPQPTGFLQQQPTGFIRPQNTGFVQPQYTGFVQPQHTGFVQPQATGFMQPQRTGFVQPQATGFVQPQATGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFIQPQRTGFVQPQQNGFFNPQPTGYMQPQRTGMMQPQRTGFSQPFESNNPFPVMQPQRTGFGQTPNAPMMAPNHTGYVHPQPTGLQRQTTGYTGNNNPYSRPLQSQSTGILQQQQQQSAPRLEPTKTGSNNPFAQFSNLPSQSTAPATKPMKPVRTGDDRFSNIAQAISTGNPMGTDSFGNIGLTRVPTQHTGSKFTNSAGQTIQAQATGNTHNPFQSQQATGYYKQPMQQQQNMQQPYYNQQNYNYQNQQPMQGMQQQSMQPQVGSLIDL O74429 VIP1_SCHPO BINDING 42..43; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 123; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 197; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 204; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 223..224; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 223; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 248..251; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 258..260; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 260; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 274; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 276; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 321; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 333..335; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O43314"; BINDING 338..341; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O43314" CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q06685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460; Evidence={ECO:0000250|UniProtKB:Q06685}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q06685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277; Evidence={ECO:0000250|UniProtKB:Q06685}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58.18 uM for inositol hexakisphosphate {ECO:0000269|PubMed:25254656}; Vmax=450.5 nmol/min/ug enzyme {ECO:0000269|PubMed:25254656}; MOD_RES 19; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 706; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 720; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1672.06c; STRAND 34..39; /evidence="ECO:0007829|PDB:8E1J"; STRAND 63..66; /evidence="ECO:0007829|PDB:8E1J"; STRAND 84..88; /evidence="ECO:0007829|PDB:8E1J"; STRAND 109..112; /evidence="ECO:0007829|PDB:8E1J"; STRAND 140..143; /evidence="ECO:0007829|PDB:8E1J"; STRAND 145..148; /evidence="ECO:0007829|PDB:8E1J"; STRAND 175..179; /evidence="ECO:0007829|PDB:8E1J"; STRAND 182..185; /evidence="ECO:0007829|PDB:8E1J"; STRAND 188..200; /evidence="ECO:0007829|PDB:8E1J"; STRAND 207..209; /evidence="ECO:0007829|PDB:8E1J"; STRAND 218..225; /evidence="ECO:0007829|PDB:8E1J"; STRAND 228..233; /evidence="ECO:0007829|PDB:8E1J"; STRAND 245..249; /evidence="ECO:0007829|PDB:8E1J"; STRAND 259..265; /evidence="ECO:0007829|PDB:8E1J"; STRAND 269..273; /evidence="ECO:0007829|PDB:8E1J"; STRAND 294..296; /evidence="ECO:0007829|PDB:8E1J"; STRAND 316..325; /evidence="ECO:0007829|PDB:8E1J"; STRAND 328..337; /evidence="ECO:0007829|PDB:8E1J" HELIX 41..44; /evidence="ECO:0007829|PDB:8E1J"; HELIX 47..57; /evidence="ECO:0007829|PDB:8E1J"; HELIX 69..74; /evidence="ECO:0007829|PDB:8E1J"; HELIX 77..79; /evidence="ECO:0007829|PDB:8E1J"; HELIX 96..106; /evidence="ECO:0007829|PDB:8E1J"; HELIX 115..121; /evidence="ECO:0007829|PDB:8E1J"; HELIX 123..132; /evidence="ECO:0007829|PDB:8E1J"; HELIX 153..163; /evidence="ECO:0007829|PDB:8E1J"; HELIX 212..214; /evidence="ECO:0007829|PDB:8E1J"; HELIX 254..256; /evidence="ECO:0007829|PDB:8E1T"; HELIX 300..312; /evidence="ECO:0007829|PDB:8E1J"; HELIX 344..361; /evidence="ECO:0007829|PDB:8E1J" TURN 277..280; /evidence="ECO:0007829|PDB:8E1J" CHAIN 1..920; /note="Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase"; /id="PRO_0000270923" MIQNASHLTSIDTESSTRTASPVSSIVTPTKRNVVGICAMDAKARSKPCRNILNRIIAEGEFEAIVFGDNMILDEAVENWPACDYLICFYSSGFPLKKAEKYVELRKPFCVNDVVFQELLWDRRLVLNILDAIRVSTPQRLICSRDGGPKINKVLEEKLRRKFGIEITEVPTPEVKMLDEDTLSVDGKIIKKPYVEKPVYGEDHNIYIYFPKSVGGGGRKLFRKVANKSSDYDPDLCAPRTEGSFIYEEFMNVDNAEDVKVYTVGPHYSHAETRKSPVVDGIVRRNPHGKEIRFITNLSEEEKNMASKISIAFEQPVCGFDLLRVSGQSYVIDVNGWSFVKDNNDYYDNAARILKQMFHVAERHRRNRVPSVQEVLNPPPRESEAWRLKSLVGVLRHADRTPKQKFKFSFTSDPFVKLLQGHTEEVILRNEQLNSVLAATNLATELKCEDINKLKQLRLALETKKDLPGTKVQLKPAYSPEGKLLKLQLIIKWGGEFTHSARYQSKDLGEQFHKDLYIMNRDCLKDVEIYTSSERRVSASAEIFAMAFLEQETIPSDLLKVRKDLLDDSNAAKDTMDKVKKHLKSLLRVGDTARKEFTWPENMPKPCEVMQQVVQLMKYHRAVMRENFIILGPEVEQVQSRWCCNENPALFRERWEKLFSEFCDSEKADPSKVSELYDTLKYDALHNRQFLERIFTPYQYLKLPQSPSLIAKEPPQRTDSNGNLVGMTGANTNHTERPLEKLYELYDLAKVLFDFVSPQEYGIEPKEKLEIGLLTSVPLLRQIIHDIKEARDSDHASTRMYFTKESHIYTLLNCILESGLPMKLPRNQIPELDYLTQICFELFERTNPSGNKEFSVRITLSPGCYAQCPLDMNLDAKHCISVSPRRSLTRHLDLQQFITKTEDLCNSVHLPKRFIPVNIN O74435 CDC31_SCHPO BINDING 47; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 49; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 51; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 58; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 156; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 158; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 160; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 162; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 167; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SPCC1682.04; CHAIN 1..176; /note="Cell division control protein 31"; /id="PRO_0000073576" MFANARAKRRSRASSPTPARLGGYAPLRVEITEEQRQDINEAFKLFDSDKDNAIDYHELRAAMRALGFNAEKSEVLKILRDFDKTGKGYLQMEDFVRVMTEKIVERDPLEEIKRAFELFDDDETGKISLRNLRRVAKELNENIDDQELEAMIEEFDLDQDGEINEQEFIAIMMDEA O74441 CTL1_SCHPO SPCC1682.11c; CHAIN 1..574; /note="Choline transporter-like protein ctl1"; /id="PRO_0000350953" CARBOHYD 40; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 101; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 457; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 558; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFSDYASRFLAQSRFSSVDQRNFKYPTSRSNLQSVSIDRNSSIDSHETDLSAGSSSLHGLNSLIDSGSIHWQLREQEQSNSHISRNENELFSKENSIYNGNFSENLGVQPNPQTISHESVNEEYTELPYDAHLPSEQKVPDRKWGLTFGFLTLALFTYSFLMVWRTNPNIPPATSPYAAIQKAFPLFHKDAIICMMLSVIWLFCLVAIPRFLYFLLASVPLTMFAFAVYLLKASRIHLETSIQPKLMLLTGIILLVAPILLSYYVWRRRIHFETSFNIIRLACRVIADIPQITLIFISFLFSFYVLIFIWVRLFARLFLRGSTLVGSVWVLPRSSWVLASFYSLHFLWLCTFFHALQCAIISSIVSQWFFYRDTKSSATKTNLVSHFFYHVVSNQYGLCAFSSFLVVITKVPLHFLPTWLRHVSRIVYYMFSKTSASYVTSPLTLAYASIYSVPYMNASKALYQIEQLNRVGLRRRSYYFSKYTLLAARSLLAIGVGVTSWNYSIHENGVFYGYIVGLLGGFLAWLIIGAIEGGLSMIVDALLICSIIDISSCQGDPNGSHCFEAWQLFESNGY O74456 PEF1_SCHPO ACT_SITE 126; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 9..17; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 32; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; MOD_RES 13; /note="Phosphothreonine"; /evidence="ECO:0000250"; MOD_RES 14; /note="Phosphotyrosine"; /evidence="ECO:0000250" SPCC16C4.11; CHAIN 1..288; /note="Serine/threonine-protein kinase pef1"; /id="PRO_0000086505" MNYQRLEKLGEGTYAHVYKGQNRVTGEIVALKVIRIDADEGTPSTAIREISLMKELRHPNIMSLSDVLQTENKLMLVFEYMEKDLKKYMDTYGNQGALPPSQVKNFTQQLLKGISFCHENRVLHRDLKPQNLLINSRGELKLADFGLARSIGIPVNTFSNEVVTLWYRAPDVLLGSRVYSTSIDIWSVGCIMAEMATGRPLFAGSNNEDQLLKIFRLLGTPTEQSWPGISLLPEYKPTFPIYKAQDLAYLFPTFDPLGLDLLRRMLRLQPELRTTGQDALQHAWFLTA O74465 HRR1_SCHPO BINDING 393..400; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 94; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1739.03; CHAIN 1..999; /note="Helicase required for RNAi-mediated heterochromatin assembly 1"; /id="PRO_0000256155" MEQVQDEIWKLSTLDAWEMVNKNTEVVFDEIPEPETLSEMKRHPLYSNIFNADNNTTSFTEQIETSETSKTQDSEGNKVDKNLKENKSIRRKRSIDNDYELSNVKRNDITSGKNREFENEHHPASDTSSWRELPSIPTLEELTSKSVELPSNNIYGGYKSFEDYLSIHYRLLREDAVSPLRESVLRYKVNPNYITGSSLAVYDHVRIDGYTISSSVIAAKLSFSVRAKKKIKWATSRRLISGSLVLLSNDDFQTFRIGTVCARPLSGLNKHPHEIDVKFEDISISLDPREEYVMIEATSGYWEAYKHVLRSLQRLSASTFPMKDYLVHCKSNQETAKHIQNNPRIRINSILKNNSQKIVNALEPFGPGEYILDSSQLKAYQSMLTKRLSIIQGPPGTGKSFVTLKAIETLLENTHSHVLPILVACQTNHAVDQILIRLLHQGASVMRLGSRTKDPEIAAVTIFQKAKHTKHSFKAAYNEIRHKKQRLIKQITNIMHNFNLEFVTLSYLHSKGIITTSQLESLRNNTEWISSVAENGEKTEEELISIWLGDAKVELITPSEITDGFEEELQIDPEKLEEIQKEAEDSGALMEEELRGKFINLRCKYLFSKLTTLHEKEIDTLLTIPNIWDIPEYSRGIIYCRWLESAYAAAEKELNRLYRFYLKVDRERIGFSNKRAAILLRGANVIGMTTTGLNKYRDILERINPKICFIEEAADVLEGPIIPAVFPSLEQLVLIGDHKQLRPGCSTYALRQDPFNLSISMFERLVENDMEYTRLTMQRRMHPQIRRLVSSVYEDLSDYEITKYWPSIPGMGEIRRFFLTHSRIEDNDGFASKINLFEAQMLVQFAVYLINNGVEPQKITCLTFYAAQKDLIERLLSESLNREKHFIKVATVDGYQGEENDVVLLSLVRNNDRTEVGFLSSPHRVCVSLSRARRGLFIFGNAQLVAESNPLWWDAINTLMNDETIQGLGDHLPLFTKDGTIYVNDPVELLDVNMRLTRK O74469 YQC7_SCHPO SPCC1739.07; CHAIN 1..133; /note="Exosome complex protein C1739.07"; /id="PRO_0000339128" MDPEYSELFERLNKQLDNVEDVLKPLKDAESIFELAEGKSELEQAKLYITMSYAINSTLYSFYKLNGIDASERPVMQELQRVKNYISKIQQAEKNVNPKTEAVNTSNAAISSSSSNRPKVAKDAATRIIKHHT O74473 CDC11_SCHPO PTM: Phosphorylated by cdc7 and cdk1. Hyperphosphorylated during anaphase. Dephosphorylated by par1. {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:12546793, ECO:0000269|PubMed:15062098, ECO:0000269|PubMed:18257517}. MOD_RES 360; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 558; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1739.11c; CHAIN 1..1045; /note="Septation initiation network scaffold protein cdc11"; /id="PRO_0000339131" MEQLWLEHDLSEEWIPQPQEQGSDNSSEPPTTSNVNNTQSTGRGSSGTSTEHGTFKKGRNDAPDVPQWKQVNAKNPVARDIFARLDLENMFEESSKQSPPSKSPTKNPSKKSSNNSSRRSSSSVGKLSNVSNMQSSPSKDPFVSQDYEKESISSSQFSKKYSEGSLKSQQSNTRSNSVHEKQNTDHASNASSSSSVVSSPSLKPNNTSPLKLFQGASDPFTREHLNQLTQDVKSNSFENGEKQFSLPEPRRPQKPMRTTERKASLNTKDLYQEVEEVMARLRGRMPNSGRESTIFLPRKLSGLREEEEQDEISVEVSQEDSSNAFPSLSDQLHLKSLQSMKRVTSIFNDNDDSFPSASSSPQRQAYMTDKMPLREIDVGSSQSSSKTARLNSSPKSTLKTSSVKTRRSHSAQSSRKVSDYPNMVVITPADLPEGIDTTQGSMEFDRIHNRWRRKGHDSDLGFDFETDEDASLSHPERTILFKAASTRHQANNDPNNLEKQQPHSFPLRKQNVAQSEFPKHSLRDNSENAPQILSSFHDLSLQNESFDEMFNGRYENGSPIPFISSGSGLKSKADKDAEYSFSVSRQSIIQILSDVEPYEPFWKRIIQLDISRRHLDSLIGLSELCPSIEELTLEGNEIAYLTGCPVTIRDLNAVENRLSSLTSFSNLLNLQYLDISYNQLEDLTGLSSLIHLRELKVDSNHLWSLDGIQHLDGLLKLSACNNRIKELSFTNSNLHRLEELLLGNNEIEEIEEISSLQNLMVLQLDNNKLTNLKASQPMIHLRILRISNNAIHQLEVDQFPHLRTLYMDLNRFNRPPDIRRLKRLVNFSFRTQDPEASNFVIQPSLDIRNLYLSNNTFVTLDCKHMFLGVRYLELANVQLKEVPKYIATSMPNLRVLDLSHNYISDIESLKPLQMIHRLYLVGNRIKKMRNLCDILANLKQLNVLDLRMNPLNFNIYPVIDDSIYELSAASKYQQSINQKGHHRKEDPQKQWQEKELAFSSTLSEAWRTRRKMYAEAILLACPHLEWLDGSDVSQSSRAAFTKSSN O74475 FKS4_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000305|PubMed:15615781}; MOD_RES 965; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 969; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 971; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 976; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1840.02c; CHAIN 1..1955; /note="1,3-beta-glucan synthase component bgs4"; /id="PRO_0000121724" MSGNNENVSGITGHDAVSDDQYAYDSEVYDDQNAYQRQPADAYSNEEFLDQADYDSMYGEGYNGYDYPTGVTESYGDEYTPVDTASSGINQYSTEKGKFTRPSDEYESEYSDYNAQPSDANNFYNLRGDGRYNAYDPSSDSLANVYNSVPYGSSPYDFSNSSFVGNSGSGTPLDGDSGSFYADSANLTNREPYPAWTPENELPLTKEEIEDIFIDLTNKLGFQRDSMRNMYDFFMCLLDSRASRMTPDQALLTLHADYIGSDIANYKKWYFASQMDREDAVGLANVGIYGGKVTSIKEKGKFFSRNKKAPKVVKPPRKSRFKRKKKKEQPEEAEDEYIDVNTDDSLESAEYRWRSHMRSMTQFERAQQIALWLLLWGEANNVRFMPEVIAFLFKCAYDYIISPEAQNVTEPVPEGYYLDNIVSPLYQYMHDQQFEIINGKYVRRERPHDQLIGYDDINQLFWHAEGIARLIFEDGTRLIDIPASERFHRLPEVQWNRAFYKTYYESRSWFHLITNFNRIWVIHFGMFWYFTAFNSPTLYTKPFHQRDGPKPTGASQWAAVACTSVVSCIIMAAASLCEYLFVPRRFPGSKPIWKRLCIIVLIAIINLIPIVYIFGFSSKHQQRSGRRIAVGVVAFLMSIATYVYFSLVPLQSTFGKLSVKDSRKYLANKYFTSNFAPLKFDNQALSVIIWVCVFTCKFAESYFFLTLSIRDPIIVLSTMRPYLCSIYWAGSRLCFVQPRIILGIMYFTDLILFFLDTYLWYIIFNTIFSVLRSFVLGISILTPWRNIFSRMPQRIYGKILATNDMEIKYKPKILISQIWNAIVISMYREHLLSIDHVQRLLYHQVPAEEGRRTLRTPTFFVSQDDNIVHTTFFPANSEAERRLSFFAQSLATPIPEPVPVDNMPTFTVLIPHYAEKILLSLREIIREEDQLSRVTLLEYLKQLHPVEWDCFVKDTKILVEENAPYENDSVSEKEGTYKSKVDDLPFYCIGFKSAMPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNTDRLERELDRMARRKFKLVVSMQRYAKFTKEEYENAEFLLRAYPDLQIAYLDEDPPEEEGAEPQLFAALIDGHSEIMENERRRPKYRIRLSGNPILGDGKSDNQNMSLPFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEEMETDNVNPYSESARERNKHPVAILGAREYIFSENIGILGDVAAGKEQTFGTLFSRTLAQIGGKLHYGHPDFLNGIFMTTRGGVSKAQKGLHVNEDIYAGMNAMLRGGRIKHCEYFQCGKGRDLGFGSILNFNTKVGTGMGEQMLSREYYYLGTQLQLDRFLSFYFAHPGFHLNNMFIMLSVQLFMVVLINLGAIYHVVTVCYYNGNQKLSYDTSIVPRGCYQLGPVLSWLKRCVISIFIVFWISFIPLTVHELIERGVWRATKRFFKQIGSFSPLFEVFTCQVYSQAITSDLAYGGARYIGTGRGFATARLPFSILYSRFAVPSIYIGARFLMMLLFGTMTVWVAHLIYWWVSIMALCVAPFLFNPHQFDWNDFFVDYREFIRWLSRGNSRSHANSWIGYCRLTRTRITGYKRRVLGQPSDKISMDTPRAKFTNVFFSDVLIPALLAAGAIIPYFFINSQPGNPMFITDPNNPSPYVHDTKTGTNPILRLVIISLIPIAAGFGMSGFFGGMACCLGPAFGLCCKKFPSIFAAIAHTIQIFIFIAIFEVCWFLDGWSLPKTVLAFCAVTAIHRFIFKILTLLCLSREVKQDSANISWWSGKWYGKGYGYHAFTLPAREFVCKAIELNLFATDFFLGHLLLFFMLPVICIPYIDRWHSVLLFWLRPSRQIRPPIFSTKQNRLRKRIVRRYSALYFSILVIFLILIIVPLAAGAEIRQGLTASEAVAKGAVGWNQTNSSIGSGIIQPRDTNYTANYSFWYDRYHFEFNTTY O74476 IMB3_SCHPO SPCC1840.03; CHAIN 1..1095; /note="Importin subunit beta-3"; /id="PRO_0000120773" MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLPGDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVFRTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLADCLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDVAGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAEGAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVNFSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGKTMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKPDFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHDGVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVAAVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGNDTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLELPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTIITILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF O74499 LSM7_SCHPO SPCC285.12; STRAND 34..40; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 45..53; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 59..69; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 76..88; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 93..99; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 103..105; /evidence="ECO:0007829|PDB:6PPQ" HELIX 28..31; /evidence="ECO:0007829|PDB:6PPQ" TURN 71..73; /evidence="ECO:0007829|PDB:6PPQ"; TURN 90..92; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..113; /note="U6 snRNA-associated Sm-like protein LSm7"; /id="PRO_0000317308" MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE O74511 EKC1_SCHPO MOD_RES 411; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 418; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 419; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 425; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 459; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 468; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 491; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 493; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 494; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 711; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 713; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC663.01c; CHAIN 1..838; /note="Extragenic suppressor of kinetochore protein 1"; /id="PRO_0000046105" MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK O74518 CID12_SCHPO BINDING 77; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 79; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; MOD_RES 325; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 327; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 329; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC663.12; CHAIN 1..336; /note="Poly(A) RNA polymerase cid12"; /id="PRO_0000256156" MGKVLLELHSVPWNEEGLSDNARLYSFLEFVSPKIEELKYRKLLLEKLQTHIREVVLDAELQVYGSMYIGTTLSISDVDVSLKSPRVGELEKRRVTMVLRKYLDADADFHSSARVPRINLVDVSGIGVDLTFGNDKACRTAELQKAYNEEHPIFGRLLMLLKHWLFERDLENVHHGGIASCALSYMLIGWLEMRFHKKGIDSEVQPIRALLQKFFYFWGVEWTYELFVLRPLTGQIVPKLQKGWLNEVQPNLLSIEDPIDRNNDIGKQSFQISMIKAAFVASANELLSDKTWFSTFAITEDEMFLCKQFENVINTKRSLVEGYDSDTESDELQAGG O74536 SNF1_SCHPO ACT_SITE 156; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 40..48; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 63; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P06782}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P06782}; PTM: Phosphorylation at Thr-189 by ssp1 is required for nuclear entry in nutritionally stressed cells (PubMed:22375066). {ECO:0000269|PubMed:22375066}. MOD_RES 189; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:22375066"; MOD_RES 442; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC74.03c; STRAND 29..31; /evidence="ECO:0007829|PDB:3H4J"; STRAND 34..43; /evidence="ECO:0007829|PDB:3H4J"; STRAND 46..53; /evidence="ECO:0007829|PDB:3H4J"; STRAND 59..66; /evidence="ECO:0007829|PDB:3H4J"; STRAND 97..102; /evidence="ECO:0007829|PDB:3H4J"; STRAND 104..111; /evidence="ECO:0007829|PDB:3H4J"; STRAND 162..164; /evidence="ECO:0007829|PDB:3H4J"; STRAND 170..172; /evidence="ECO:0007829|PDB:3H4J"; STRAND 230..232; /evidence="ECO:0007829|PDB:3H4J"; STRAND 234..236; /evidence="ECO:0007829|PDB:3H4J"; STRAND 329..331; /evidence="ECO:0007829|PDB:3H4J"; STRAND 453..460; /evidence="ECO:0007829|PDB:2QRD"; STRAND 486..489; /evidence="ECO:0007829|PDB:2QR1"; STRAND 496..502; /evidence="ECO:0007829|PDB:2QRD"; STRAND 513..525; /evidence="ECO:0007829|PDB:2QRD"; STRAND 528..541; /evidence="ECO:0007829|PDB:2QRD" HELIX 67..72; /evidence="ECO:0007829|PDB:3H4J"; HELIX 77..86; /evidence="ECO:0007829|PDB:3H4J"; HELIX 118..125; /evidence="ECO:0007829|PDB:3H4J"; HELIX 130..149; /evidence="ECO:0007829|PDB:3H4J"; HELIX 199..201; /evidence="ECO:0007829|PDB:3H4J"; HELIX 206..208; /evidence="ECO:0007829|PDB:3H4J"; HELIX 210..226; /evidence="ECO:0007829|PDB:3H4J"; HELIX 256..263; /evidence="ECO:0007829|PDB:3H4J"; HELIX 270..272; /evidence="ECO:0007829|PDB:3H4J"; HELIX 276..279; /evidence="ECO:0007829|PDB:3H4J"; HELIX 283..286; /evidence="ECO:0007829|PDB:3H4J"; HELIX 291..293; /evidence="ECO:0007829|PDB:3H4J"; HELIX 306..314; /evidence="ECO:0007829|PDB:3H4J"; HELIX 320..326; /evidence="ECO:0007829|PDB:3H4J"; HELIX 338..351; /evidence="ECO:0007829|PDB:3H4J"; HELIX 462..476; /evidence="ECO:0007829|PDB:2QRD"; HELIX 492..495; /evidence="ECO:0007829|PDB:2QRD"; HELIX 504..508; /evidence="ECO:0007829|PDB:2QRD"; HELIX 562..575; /evidence="ECO:0007829|PDB:2QRD" TURN 54..56; /evidence="ECO:0007829|PDB:3H4J"; TURN 159..161; /evidence="ECO:0007829|PDB:3H4J"; TURN 178..183; /evidence="ECO:0007829|PDB:3H4J"; TURN 194..196; /evidence="ECO:0007829|PDB:3H4J"; TURN 545..547; /evidence="ECO:0007829|PDB:2OOX" CHAIN 1..576; /note="SNF1-like protein kinase ssp2"; /id="PRO_0000086669" MQPQEVDLMENSTMRNGARVLPPEAISKRHIGPYIIRETLGEGSFGKVKLATHYKTQQKVALKFISRQLLKKSDMHMRVEREISYLKLLRHPHIIKLYDVITTPTDIVMVIEYAGGELFDYIVEKKRMTEDEGRRFFQQIICAIEYCHRHKIVHRDLKPENLLLDDNLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVINGKLYAGPEVDVWSCGIVLYVMLVGRLPFDDEFIPNLFKKVNSCVYVMPDFLSPGAQSLIRRMIVADPMQRITIQEIRRDPWFNVNLPDYLRPMEEVQGSYADSRIVSKLGEAMGFSEDYIVEALRSDENNEVKEAYNLLHENQVIQEKSHLSKSKRVDSFLSVSPPAFSEYTSELQKKSKQELIDPTLEGPRWTVSDPPTYAKQTIDSNICVLVPTAEKNKLEMRTLADAASAVDTSQSTRKKSRRNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPVNGKYRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFMLDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKLFSA O74539 MAK3_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1795; /note="Phosphohistidine; by autocatalysis"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"; MOD_RES 2263; /note="4-aspartylphosphate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00169" SPCC74.06; CHAIN 1..2344; /note="Peroxide stress-activated histidine kinase mak3"; /id="PRO_0000081410" MYSQHELRNKVSLALSSLLRYTFELTPFFELYEADFAYALYAGFELATNRKVVGKFSFQNVHLENEYNILTEIAKDERASKFSPTPIEFTSFPHIDLSACIAYDFGHGAELSTSYAYFRENPAEFVRFCIAICKCIEYLHSKGMVHGEIRLDSFIPISSYDNVYMLTVGSGASYFHNCLQAHNWRKYSEDSESMSRILFISPEQTGRTSYSVGYRTDIYSLGVLFFHYLSDCSPYTGSFVQRIRSILTEPLPDISKSCPKLPHLIFKIIEKMTRKNPDERYTSCSGIVNDLEACLDDIDKGLILNDHVLEKTGRTSLFYLPCSIYGREHEIKLIRKILRNSPRAINHQDKKDLETFNPYYLNAIESESSSQSLSLSQRASEVMPLVILITGCEGIGESSLIQTICDRREGYMAITKFEVSQSIVYSAIVSAVAEFIRQILAEDQLLLNNFFEELKNKLESDLYLLDSVFDLVPEIRSLLQQFSTSSGNTRKTSLLGSNHSSYSDKLGSPTILSTSFSLARPYPEPALVSPSTERPPRSSFSAALMTLLNIIASFKKVTMVIENIHLADESSLIILQKIVYSDLPLTLMITCDKENDHVINRFRLANDRIHEIELKPLSFNAVNSYVQATLHRTDDGLARFSSYVYHISKGVPLLVRNVLLSIYENKIIYFDWKKNRWEVNYDEMYTLDNDYSEPDAFMTAKKKISKLNDSSRAILGWASLLGPSFSFATVKKLCKDTDNIELNVEALQSALREGIIYATSSDDTYTFSRSIYVKAMRDLLNEAKIQIMHACLIDVCLKNRDRYNIFDIAFHINAAFDFVKGDKRSVEYCHYLHLAAEEALKIGANQEALDLYNRCIKMIPHEIPEESDDSYIRCQLIGMYVGCAEAYWVNDNFDTASEMLKLAEEKACNNSEVFPARFLYSRILFEGVHIEECTQYVLSCLKPLGYELKRHSLEDSKSIISALIPRIIDKITKSSEESQSSTDDDDRRIFEILSFLYVGSVATSYFSETAEMAIDFGIAQVEFFLSTVVNSFSAFALVYFAILANSLLEPSEDILFIGNYGEKLNREAENPIIFSRTEYLYVQSLGFIDSTTKERRLTIDYLDRNCVTCSDKHVIISLLLVSSWEKFLTSNNYSNYLADFETTHAQIMEMKPWVGDTSLITQLKRFLMCLQDNIKLDLIKSKSFLSDHNIQLSSPAAQESAKLAFSLHGWINSWYLLALVMHGEWDMAISYGENFKREFKNALLTSSRVFGIFMFTWSLVNKMLICPEFTKQKKYYEQYKENLGFFDSLCIGDNECITRVYFLLLKACGLIMNGLNFEASVMLEEVISLTEKLELFLLQAFAFETVGSIFVSMELYTSATQYLEEAIRNYAALGVKQKARHLRDKFGDLLVSNNLQVSIDEATQTDFPLVFSPERSSIDINASSMRSEKASFEIPFPEEQIDDDVSPVAQDSSLEELLISLDIIDLTSVMRSCQTIASEIELTGLLSTMTQRMLEDSSANAAVIAIRDDVGFKIAAYRTGELNEVFAPPMPITEDQTYVPSRVINYVVHTQKALFSNNINHEFDLQQERWNIENHMGRSVIAIPLYQKKEVFAILYLQGPPSAFHSRHMSVLSILGAQASFAIVNISLFHKVKEATNVNTIIIKAQREALNLVQKSEAKYRSFVDTMPCLLSKLEFDEELRIELFGSFWKEYCGELNINDPNTWKEYVHLDDHLKLQDFLLSHLHNPLPFELEIRIKRKDGVYRWNLTRCTPTTNEKNRTSFLCATIDIDDQKKARATALELARLRSNFLANISHELRTPFSGFYGMLSLLDDTNLDSEQRDIVSAARISCEMLLRVINDLLNFSKLEAGKVTLESDLEFSLESVVCDCMQSVYSACAEKGINLSYNVSPDIPFFTAGDGMKIGQMLKSILDNSVKTVNNGFIRVRAFLAGSSKKNDRDQLQIAFIVEDTREESNAIFLANMINSLNRGCNDYLPMDLSGTALGMSTCLQLCKIMGGSVSVEVSQNNPTFKICYDLKIHELGKERYDIIATPLFQNLTEFNDLIKSKVAIRVSKTSTEYDNITTYLQAARKVLHVFKGLQDLASIFDLSPDSALLRCSVVVVDVYSMDDVKAVEKILKSYPDVHVIYLCCDPSRLNIEQELQKPSGRSFACKKRWGFLQMPCTRENFLKVTLQVFKSNEDTCNFYSYVNEYGESPKPDDDMDRLNKCVGSKILIAEDNPIVRMTLKKQLEHLGMDVDAAEDGKETLQIFESHPDNYYQVCFVDYHMPVYDGLEVTRRMRKIERKHGCAPLPIFALTADMQPTMETQFQEVGITHYLSKPFKKETLIKMLLQYLVNGTDGNANTS O74555 BBP_SCHPO MOD_RES 131; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC962.06c; CHAIN 1..587; /note="Branchpoint-bridging protein"; /id="PRO_0000256150" MLNSRSVGSTGSNNTPLGRRRFDEKPDSLPPLPDANGMSNGYRDSYKSNSRMDHRPDGYHDGRGRRAYRKHYWGHPTPIEEMLPSQMELETAVKSCMTMEQLELYSLNVRLEEITQKLRTGDVVPHHRERSPSPPPQYDNHGRRLNTREIRYKKKLEDERHRIIERAMKMVPGFRAPSDYRRPAKTQEKVYVPVKDYPEINFIGLLIGPRGHTLKDMEAKSGAKIAIRGKGSVKEGKGRSDPSVRGNMEEDLHCLVTADSEDKINHAIKLIDNVIQTAASVPEGQNDLKRNQLRQLATLNGTLRDDENQVCQNCGNVGHRRFDCPERINHTMNIVCRHCGSIGHIARDCPVRDQQPPMADSTADREYQSLMQELGGGSAISNGNGEPQKSIEFSESGAASPQAGHPPPWAAASTSVSSSTSSPAPWAKPASSAAPSNPAPWQQPAAPQSAPALSMNPSSLPPWQQPTQQSAVQPSNLVPSQNAPFIPGTSAPLPPTTFAPPGVPLPPIPGAPGMPNLNMSQPPMVPPGMALPPGMPAPFPGYPAVPAMPGIPGATAPPGAPGSYNTSESSNLNAPPGVSMPNGYSNR O74558 MOB2_SCHPO MOD_RES 46; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 48; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC970.04c; CHAIN 1..244; /note="Maintenance of ploidy protein mob2"; /id="PRO_0000193581" MFLLNSLSRITRGNRSKRHQNLSDASSSSGSFSKKSSTSQLVRTGSPSVEPTALYLQQPFVRTHLVKGNFSTIVSLPRFVDLDEWVALNVYELFTYLNHFYDVFATFCTVKTCPVMSAAANFDYTWLDNNRKPVHLPAPQYIEYVLAWIENRLHDQNVFPTKAGLPFPSNFLVIVKAIYKQMFRIFAHMYYAHYAEILHLSLEAHWNSFFAHFIAFGKEFQLLDKRDTAPLKDLIVVLENQGNI O74560 RAF2_SCHPO SPCC970.07c; CHAIN 1..636; /note="Rik1-associated factor 2"; /id="PRO_0000116561" MPPVRAEKKRKTDLIEQVCVTNKAGELVDLEDVLEYGPYSLTGILSSEKDEQEPLFDESIVLGYSIKISPVWTYNLKDVPEKETMSIWIVTPQRRYGILSPSSEYKAIYEQISEKNRLFYLIKTKFKDDMISGTLEDYDNYIEVLKEKLELPSCFQAILLVQKHIRFLLTQMVATSSLHVWSESPFFIRIRSSYEHLILQINKNIYNARQERKKSKLSSNNPSDNNTTMKSSLNQALTLINLPEQPFSISSPTATPQLGVVKRTSPLRFPLNDIWLSGLRIVDPNIESISLWKRIQVSTSPKHQRYISLQEVCSVIAQQLQITNLEALNKLSSHGETLLQIMHTAFTWRGTKLFNDIKHAIGFRSSVQQARSQFRGYCYDYLFMHCNNGEKTSLHLLRTLICMKLDFSNAQLAAKILFHFLLFDIGSGLSGSDYTYEQYINHSAVAFSFTEEIFEKNFVTVLPDFVKLFSISFGYWPAFSFYDELLKLLRNKYPKVYSSTPNLCDQVWLDRTNLFPCNRSTRSTLPYRPTKLLDLASASSCLSKKETDFKQDTGLYSYNLEKVEALKVSPDLQTGIWSCPVQNCLYFAVCDNPYKPSQVIYDHLLGHVDSKFIFKTPSNSVRSFTNKLEHIMYNIN O74562 SEC8_SCHPO MOD_RES 449; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 450; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC970.09; CHAIN 1..1073; /note="Exocyst complex component sec8"; /id="PRO_0000118941" MDTRGYSETKKGRYPVGKKSLESPNGYSNYGTSMDNELSSEYASRGMHIGDLENLVNEIEDEWKDLGREDYQPISTALELLDDSSFGRDYKSFLNVYDRISAALQTIAHTHKDDFTRGISAYGEIMEGIQKCNSRIIALKQSLEASQECIGNTNSKELQQTLARSSQYKKVISVLKELNEANQLFDNFHTLVDSKQYYHASDLIRRVWDELSRSDFDGILVVEQFKSRMTGLLSHLEDILSEELVSITFLKDAVAYPIVSYCSPNPLRETSNPYFLRDFLKNNANTSTLGQSEQLRYLEEALSLKLSDCLKMDYGRDSLRDIRIVLESLNLLGKLPNAISSLKSRTSAEMFTTVDSTSRAIVNKYSLGNNVSTVNPFSKSLYDIGLHAETDREHTMISEFLTNLFTKLRCVLMHYRGISEFMTKLETKTPKHASSSHKSSIMSVNSDPTSPKVSKFDTSDSTFPFDTLLQAFESEIRLMLKDYLISKEEYIENSGNFVVGTEMSIYNLPGENEEDKLFDVTNEIAVENKSNAFYARINELVNEKAPELILNKSNASVSTIELFSGSSKEIVRLAGHVVFVGPSVFHASSVLPQTVFFLEDSVSILKNPNIPPQFAVNFMKEFLRGSYIPQLYKFMSSHFDTIMKDVGAFQLHRDWKIYSKIPIFKCHVAIVQYFHDLQDYLPIVALNLVEFYELLHTLLVRFRNHCSDYLSDLCRTAVLKEYKHVNEDTEDVDDTVRVKLLHDDVTYPQFIKFLKQKNPSLEGLNELCRMENKRLLQYEDRAITSEVKLPVSVLSKDSDLVNSVSYLHNSMEWFLQRCFSRFMNGSRRMNVLQQNQANFGGDFLPIDNLLGNNSDLMKGAYKEVFDSLQRLQFDALLLIRMEVRLQYIHSINQSVNLPDYVVEYRGRPDASIMALNSTIVTTNLKLETCLNEWERRFVFQGLSELVDSSLYSIFYKIESMNRGSCLQMLKNMSAMIQILKTVKEIHGDVEFPKSSRVFGIYQNGAKKIIEHFIAAPKKELLPDVKQMVRIYYQRLMKDAKRNGRDDLYRQYQKKIGSVLTQFDNTVGGARKNP O74563 BRL2_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305}; SPCC970.10c; CHAIN 1..680; /note="E3 ubiquitin-protein ligase brl2"; /id="PRO_0000055855" MYQNGKPDAPTILGQKRELEDVEIQDDDIQEVSKEDLLKDVRVRSIQFDELESKIEGLQNLAEEKLKVLATLVSWWPEILQQFSVVFQGNELKDFESEGVFSILEKFPELSYFNDAVKNNKTKALSIIQKLLSTVDSSTNSVSRDPFSVLSIDDSALTEKLNTINLDIDKILDELDTTRSQLHSIIKLPDRSSSFTLQCINESVRPQSTKVKEEATTSSKGKDEEKKVSTVEQRTQLQQLSRLQDQQNGLMESRSQSLKILDSNVNEMDKLIMERENALNNVETTNLKKYSSFLALKEAVSMTSEQLRVLEHLLSECSHEINVLSQQSKNFNGVFESSYQPLINDLDHQISVMQNDEKRINNAKTELSLSLEKKLEAKKQKEKVYKDKLDELANLETMVLEKKKAVATREAANKIRLVDLNDLELQKDLSTYLSKELASTEKAFRLVKQQTVKSSHSHYQELITKFSVEKEKAEQKYFLTMKSTDSLHAEVKLLRQKYQKTNEIISKMLNSQDTAVHRIIEFEDQLARLSSVRNNSIKQSTTFQVKKSSQKSTIQNLEEKVSYLQQFMDKNNATLTDLEFQCSDLSSSIDILSKQDEEHEKEKRKLKDTGVSTSAEELKTFRAMCKCSVCNFERWKDRIISLCGHGFCYQCIQKRIETRQRRCPICGRGFGASDVIPIHL O74627 CG1C_SCHPO MOD_RES 300; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 302; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32F12.06; CHAIN 1..342; /note="Cyclin pch1"; /id="PRO_0000080426" MSEVIKSVPPGSQNTSQWIISKDQLVFTPSALDGIPLDQEEIQRSKGCNFIINVGLRLKLPQTALATANIYFHRFYLRFSLKNYHYYEVAATCIFLATKVEDSVRKLRDIVINCAKVAQKNSNVLVDEQTKEYWRWRDVILYTEEVLLEALCFDFTVEHPYPYVLSFIKKFVADDKNVTKVAWTYINDSTRSIACLLYSPKTIAAAAFQFALEKNEINLSTTTDGLPVWMEESQVSYEDVKGVLTLIDSLYKKINPSKQALPIDQKNGSHASSVAPGTPSSLASVSTQATPQHQNSSGRTDSFHSLNTETPSKSTVDDQILSTAAQPKKSSDTDKEMETEAS O74630 ATM_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPCC23B6.03c; CHAIN 1..2812; /note="Serine/threonine-protein kinase tel1"; /id="PRO_0000227706" MTSLNDIVNKLSSSKIKTRSDALQNLRSYIIYSRNGNSLNQEDALIIEKAIKRAFELEWQISANHGKRQISKASQEQKLQDISYLLRTCVESYILLFREPHILALLDIILRHTFTANGSICEVVCLNFSKALRLLLSHSPHLHHLRFSDWQSLVSYCCQAIEKLSIAEETYVSDSEEEPISQKNYQEISIWKSHDVIRVKQEVVELIYVMRSLVQWYAAPINFVSEQLLKFFEFFFYAYTEETDAHLPALQCLFQLCAYAIPNCNDYSASVVLLVFKILINSDKWKRLDLRLQLIQCLAISYPLWSNSETWDPHRSIRSFNLDLLNSSFFSLKNFLNFFGKRSSLSLANFRFHTVEPKNNIAKLYDPRLHLFFSLRHNSFFESYFIYFFLAKLILLKKTVLSLASTEQANKKQKTCSQIEELLLQAELANISASSFSLQLMVIITAISDNLTNDDLLSIQKMSLNFTEKKNELQSWSFFILFNICYNKAYSSMLTTSCKKEILAAASRGLLNSVTSPVCYQILTYFNMYRPLCFASIFPFIKQQFILFNDYSPMLSYEAIDYWKSLYILLNENLFVGQSSFKSVFLKWLKWHLYHLFSKEGELPFFSFTDSSIIIFDLLMMIFYRPLSLSYITTEIRSPFERNLFHLKEAWSPVTLRFPYTTDEICKQSTEGCYPFNSNHTIDCDSLQNVIKMLESSIDEISSASYDKDELDKETPSFEAVMIFSQISFLCGFLNCFIQKKGIHNVTPNNLVIFKNLFPEVLSFVKSNHSYDPIINCISTNLQFTISDEPKHLRYEIGSDLIRSTHFRDSNPLKTLVLYIMDMASKNVFIKPQEFDHDEYFSQEEEDIYRPENLIRNHQILGLMEGSLEQIRNTDLFILQKYIDYFSSHPHDSLINILHLYPIETFCFGMSAIGAYFLDVARTSEPIFYKCLEILAQKILMNYDYERDEVYLMIFIKIFQKCVHSKLQFTDATLKLIVKITKFIEKVFIETKFSSLSGRQTFLKFIFQLSPTSHVYSKFDYQKLISLTLKDSDVCVIYNFVDDLVIFLKKCDKTLIEGFVLPILSIKIEKSLYKGFCYLYLTLKVFLSISSNRSALLYQLLKLANSYETSTIFEPLLRKLHIQSANIKQLFRIYRLEIFWSFVSKDLSNTTNDFLEFPYKPIYFSLSDFLKENSDEIILVLILTKNITLAKLITSRMSVDFSEKYTQLIPVITTYTHLSEVENKKYSLRFNSIDEALDVELLNRSKAFLFCLEMLKEVKELGSTFKSISSTSFKVYSQLTIFANRVSFNNSTAIPFFSTKSVLWYCNRLFQELEGFSSIPSVIDLVLRRLAIQLHFATDEELQVTISFRLCAFLCFSDPFITSNYLVMIVLRIARQLLSIPCTQSLGLGIARFHLKKFKPTDFDYFFQLAEFCMDFLGFCYNTIGTKMEAIQDFYTWFDGYVTALLNFEYEGYGFLRCQINFVRSVMTTKNEWIEVSNKLFERGHFLKRIAMNNYLCLYFWQVLDACPRNVLHSLSLEIWKCYKAYDITEFPDSLKLFFSDIMGWNFFKSPEIADLNHYIPKTDPRLCDTKTYEESKLIIWKLICQKACSLLFKYDILLDSFIEDCIRMFFENGNHQELRKFLNFPKDSIIYDSDFKTLVSEEGSFQWVKLQPTNFDSLSNWTKEETLKLLNMMGKSSTTHSLKLLSTYMVGFSTSIIQYIIHLILLEFDFNGNNKKQKEYVTQLILSGLLNKNTNSIRKTCMNILLYLRRQLGHHALNPFEANYWVPINYSVAASTAYDCHLYEQSLLFLTIHNTKTDELDITLLSDILSQLPCPDAYYGIKRETSFKNILLKAVHEKRSPLAISYLDAANMYRSNEDEGTKMMFSNTLNNAGFFSLNEFYIDSLKANDAIDECSNEVYASAWRMQKWDIPPLSLDNKTTKDCLVFEVLHAVHNYAIYGNYLHLEEYINKKLLLINPNEEPDSLLFYALAYDLKFLIRCNQSQFNCDILQLLKENKQMSSQLHECFQLLLEIRNVLLSLLQSHKQLDLSDDLASFRKYYILELLKISESFLIVDNLQNAFSVAMLSDALYRKFDLADENLKHDIDFLSSKILWQRDEKIDAIGMLSESLSKTNSSIFPSISYAYLGNWLYTTKSEKTELVSKNYFEKSLSHMSHLNAKEKAKIYCMFAQFCDNNYSSPDLTEDFKRMEKLYFEKKNDIQQLERSIVNASNMKEEKMLKNHHSREMSSFIIDEREYLRMSTFRSKMLTQSITHYLKCLSESDENDVLISRCCTMWLSNSHLDELNNSLQHYLQNLPCKKFIPVFYQLAARLMNENSKFQQSLTSICYNVGRNHPYHSLHVLFSLVSNVPEIENLDAGSRYRAVKKILDLLKVNQGLSNLVTKLLCSFENYVSLAEWNPRSKVDSTSFSRFPGYKWFLKDAANYGLPPITMNVKVNDTGDYSNIPTVSSFDDTIHFASGINAPKVITCLGSNGHTYKQLVKGGNDDLRQDAVMEQVFEQVNGFLRSYRKTSQRNLSMRTYKVIPLALKTGVIEWVQDTIPLGEYLDSAHKVYHPKEWSLSTCRKLIAEKQMEDLETRLKVYDLVCRHYRPVFRHFFLESYADPVQWFTTQTNYARSTAVASVLGHVLGLGDRHGQNILIDKTSGEVIHIDLGIAFEQGKKLPVPECVPFRLTRDVVDGMGITGVEGVFRRCMEFTLETLRREEDSLLSVLEVLRYDPLFSWLISPLRRMKKQKMQLENFNQPESGNITTDASRDPKIQRNNVSGESEAERAILKVRQKLSSTLSVEASVGELIRIAQDPSYLALMFCGWSAFQ O74653 POB1_SCHPO MOD_RES 224; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 225; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 229; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 241; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 433; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 439; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 440; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 442; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 444; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 549; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1289.04c; CHAIN 1..871; /note="Protein pob1"; /id="PRO_0000058504" MASQRFVIALHSFPGKSSDELPLVEGRKYLLIKMDEEFGDGWWEGEDEQGNRGIFPASHVELISDERSDSSDSRRGKEDFSISTAEVTRSSLSSSRSTSSRSDKDSEKLYSNNSLSSSHSSILNGPLDSLSKPSVPSNFNSMFPSSKQEGPSPLLDNQPSSDLSNFNTIDADYNNASASTSAPATSASLKKVLSAEDSVRETITDIETALQNMSTSASRTPNDSSPLPYIENRPASSLAVSEKIQNVPNWSTEEVVEWLMNAGLGSVAPNFAENEITGEILLGLDSNVLKELNITSFGKRFEVLRKIQQLKDSYEQSLYEEYPQFAEPISVSQSSDSSSSIPKKSNDEAGGSPSKSSPTRPGFNDYVNRPTSVMPSLSNMIVSPDLDSSPSTDWNQYVIPPLATPSSRNSKSTQSAVPENVSRFDSNEPSATSPILKRSSPTDSISQNSGLPSRLTEPISSPSTSSIDVDKEGTSFPGLPYHSSKGNLYAPQPSSNVPTKFTGGASESSSVPPRPIPSAMKGKAPASAISIEALEELDPPKITTIDGESPSSISSRLPSSNLEQGSSSSVTKSPESMPDPSAKASSPVTSKGVSINEKSAVNNYATPLSKPQPKDTKGSKLGNTFVAPSPAASLPASPPVGTELKTRPTLRSVASSPLNKEPIGKRKSKRDIFGRQKVLPTGISEGLSNIPAKEAIKTADCHGWMRKRSDRYGVWKSRYFVLKGTRLSYYHSLNDASEKGLIDMTSHRVTKTDDIVLSGGKTAIKLIPPAPGAAKAAVMFTPPKVHYFTCENNEELHRWSSAFLKATVERDMSVPVLTTSRMPTISLSKAKELRTRPPSLLIDDENEANLTSSIGLKKNAKQKNKKSSKQK O74718 ERF3_SCHPO BINDING 245..252; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000305|PubMed:19417105, ECO:0007744|PDB:1R5N"; BINDING 384..387; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000305|PubMed:19417105, ECO:0007744|PDB:1R5N"; BINDING 428..429; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000305|PubMed:19417105, ECO:0007744|PDB:1R5N" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:19417105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:19417105}; MOD_RES 182; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 539; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC584.04; STRAND 226..228; /evidence="ECO:0007829|PDB:1R5N"; STRAND 237..245; /evidence="ECO:0007829|PDB:1R5B"; STRAND 310..312; /evidence="ECO:0007829|PDB:1R5B"; STRAND 314..320; /evidence="ECO:0007829|PDB:1R5B"; STRAND 341..348; /evidence="ECO:0007829|PDB:1R5B"; STRAND 359..361; /evidence="ECO:0007829|PDB:1R5N"; STRAND 377..384; /evidence="ECO:0007829|PDB:1R5B"; STRAND 386..388; /evidence="ECO:0007829|PDB:1R5N"; STRAND 421..425; /evidence="ECO:0007829|PDB:1R5B"; STRAND 434..436; /evidence="ECO:0007829|PDB:1R5O"; STRAND 470..472; /evidence="ECO:0007829|PDB:1R5B"; STRAND 475..487; /evidence="ECO:0007829|PDB:1R5B"; STRAND 490..494; /evidence="ECO:0007829|PDB:1R5B"; STRAND 497..502; /evidence="ECO:0007829|PDB:1R5B"; STRAND 506..514; /evidence="ECO:0007829|PDB:1R5B"; STRAND 520..525; /evidence="ECO:0007829|PDB:1R5B"; STRAND 529..536; /evidence="ECO:0007829|PDB:1R5B"; STRAND 546..548; /evidence="ECO:0007829|PDB:1R5B"; STRAND 550..552; /evidence="ECO:0007829|PDB:1R5B"; STRAND 556..566; /evidence="ECO:0007829|PDB:1R5B"; STRAND 573..575; /evidence="ECO:0007829|PDB:1R5B"; STRAND 579..585; /evidence="ECO:0007829|PDB:1R5B"; STRAND 590..594; /evidence="ECO:0007829|PDB:1R5B"; STRAND 601..603; /evidence="ECO:0007829|PDB:1R5O"; STRAND 621..630; /evidence="ECO:0007829|PDB:1R5B"; STRAND 642..646; /evidence="ECO:0007829|PDB:1R5B"; STRAND 648..650; /evidence="ECO:0007829|PDB:1R5B"; STRAND 652..661; /evidence="ECO:0007829|PDB:1R5B" HELIX 230..233; /evidence="ECO:0007829|PDB:1R5B"; HELIX 247..249; /evidence="ECO:0007829|PDB:1R5B"; HELIX 251..261; /evidence="ECO:0007829|PDB:1R5B"; HELIX 267..276; /evidence="ECO:0007829|PDB:1R5B"; HELIX 353..356; /evidence="ECO:0007829|PDB:1R5B"; HELIX 364..373; /evidence="ECO:0007829|PDB:1R5B"; HELIX 395..413; /evidence="ECO:0007829|PDB:1R5B"; HELIX 417..420; /evidence="ECO:0007829|PDB:1R5B"; HELIX 451..457; /evidence="ECO:0007829|PDB:1R5B"; HELIX 462..465; /evidence="ECO:0007829|PDB:1R5B"; HELIX 638..641; /evidence="ECO:0007829|PDB:1R5B" TURN 221..224; /evidence="ECO:0007829|PDB:1R5B"; TURN 389..393; /evidence="ECO:0007829|PDB:1R5O"; TURN 428..431; /evidence="ECO:0007829|PDB:1R5B"; TURN 440..442; /evidence="ECO:0007829|PDB:1R5B"; TURN 503..505; /evidence="ECO:0007829|PDB:1R5B"; TURN 634..636; /evidence="ECO:0007829|PDB:1R5B" CHAIN 1..662; /note="Eukaryotic peptide chain release factor GTP-binding subunit"; /id="PRO_0000091488" MASNQPNNGEQDEQLAKQTSKLSMSAKAPTFTPKAAPFIPSFQRPGFVPVNNIAGGYPYAQYTGQGQNSNSPHPTKSYQQYYQKPTGNTVDEDKSRVPDFSKKKSFVPPKPAIPKGKVLSLGGNTSAPKSTKPISISLGGTKAPTTTKPAAPAAQSKTETPAPKVTSESTKKETAAPPPQETPTKSADAELAKTPSAPAAALKKAAEAAEPATVTEDATDLQNEVDQELLKDMYGKEHVNIVFIGHVDAGKSTLGGNILFLTGMVDKRTMEKIEREAKEAGKESWYLSWALDSTSEEREKGKTVEVGRAYFETEHRRFSLLDAPGHKGYVTNMINGASQADIGVLVISARRGEFEAGFERGGQTREHAVLARTQGINHLVVVINKMDEPSVQWSEERYKECVDKLSMFLRRVAGYNSKTDVKYMPVSAYTGQNVKDRVDSSVCPWYQGPSLLEYLDSMTHLERKVNAPFIMPIASKYKDLGTILEGKIEAGSIKKNSNVLVMPINQTLEVTAIYDEADEEISSSICGDQVRLRVRGDDSDVQTGYVLTSTKNPVHATTRFIAQIAILELPSILTTGYSCVMHIHTAVEEVSFAKLLHKLDKTNRKSKKPPMFATKGMKIIAELETQTPVCMERFEDYQYMGRFTLRDQGTTVAVGKVVKILD O74736 ING2_SCHPO BINDING 251; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 253; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 264; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 269; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 275; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 278; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 291; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 294; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53" MOD_RES 181; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 183; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 197; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 198; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1709.11c; CHAIN 1..305; /note="Chromatin modification-related protein png2"; /id="PRO_0000362155" MGTSGIEIFAALNDFTDAIVSVPESVCGKFTSLKEIDAQVRDIRQNVIQEIGVVLKNEKNDELSGEERCERLQKTLKEILPYSDSKICLATDAMNNIKSCIDRLDAGFEYVELEIPQQLRLGYPDDRALMNYHSTVTPQTSERRRETRRHQNNQHSQQYSSQERSSSYNNFEDASSPQSSYHTPTKRRKNAVPRKSSSPPLSSTKHAPQSTERRPVRRSESRLKQTNGEPLVKHDTLDSSDISREGEQLYCYCQQVSYGQMIGCDNENCKREWFHLPCVGLVEPPKGIWYCKECEELAKSSESRQ O74752 MAS5_SCHPO BINDING 110; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 129..131; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 137; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 140; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 153; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 156; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 179; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 182; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 195; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 198; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 209..210; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 241..243; /ligand="substrate"; /evidence="ECO:0000250" MOD_RES 404; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPBC1734.11; PROPEP 405..407; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000396683" CHAIN 1..404; /note="Mitochondrial protein import protein mas5"; /id="PRO_0000314107" LIPID 404; /note="S-farnesyl cysteine"; /evidence="ECO:0000250" MVKETKLYEVLNVDVTASQAELKKAYRKLALKYHPDKNPNAGDKFKEISRAYEILADEEKRATYDRFGEEGLQGGGADGGMSADDLFASFFGGGMFGGGMPRGPRKGKDLVHTIKVTLEDLYRGKTTKLALQKKVICPKCSGRGGKEGSVKSCASCNGSGVKFITRAMGPMIQRMQMTCPDCNGAGETIRDEDRCKECDGAKVISQRKILTVHVEKGMHNGQKIVFKEEGEQAPGIIPGDVIFVIDQKEHPRFKRSGDHLFYEAHVDLLTALAGGQIVVEHLDDRWLTIPIIPGECIRPNELKVLPGQGMLSQRHHQPGNLYIRFHVDFPEPNFATPEQLALLEKALPPRKIESAPKNAHTEECVLATVDPTEKVRIDNNVDPTTATSMDEDEDEEGGHPGVQCAQQ O74757 HRD1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; MOD_RES 367; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17D11.02c; CHAIN 1..677; /note="ERAD-associated E3 ubiquitin-protein ligase hrd1"; /id="PRO_0000358324" MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLDMTPKRLPCGHILHFHCLRNWLERQQTCPICRRSVIGNQSSPTGIPASPNVRATQIATQVPNPQNTPTTTAVPGITNSSNQGDPQASTFNGVPNANSSGFAAHTQDLSSVIPRRIALRDGWTMLPIPGTRRIPTYSQSTSTTNPSATPTTGDPSNSTYGGPQTFPNSGNNPNFNRGIAGIVPPGWRLVSSNTQSLSTNSAMTSLYQNASSADNNLGSSLPNVVPLSRGLTQSNETSNTFPAASSNISSQLRELHTKIDELRETVSNFRADYNSIRTSLNQLEAASGINERIQTTSADSLLNSNGMSGTEGFENTQTSITTNDNQSSILTSSDQTSPFATDEDRQNSRNVQLETVDENF O74760 EIF3A_SCHPO MOD_RES 374; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:18257517"; MOD_RES 501; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:18257517"; MOD_RES 874; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:18257517"; MOD_RES 875; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:18257517"; MOD_RES 877; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:18257517" SPBC17D11.05; CHAIN 1..932; /note="Eukaryotic translation initiation factor 3 subunit A"; /id="PRO_0000123543" MAPPQGKPENVLRLADELIALDQHSSALQSLHETIVLKRSRNAQGFSLEPIMMRFIELCVHLRKGKIAKEGLYTYKNAVQNTSVTAIENVVKHFIELANKRVQEAQEKADKISVEYVDDLEATETPESIMMSLVSGDLSKSRTDRALVTPWLKFLWDAYRTVLDILRNNARLEVMYQLIANSAFQFCLKYQRKTEFRRLCELLRSHLGNASKFSNAPHSINLNDAETMQRHLDMRFSQLNVAVELELWQEAFRSIEDIHSLLTFSKRAPAAVMLGNYYRKLIKIFLVCDNYLLHAAAWNRYFTFTNVQKPATANFVILSALSIPIIDANKLSGPSIEAEDAKSKNARLALLLNLSKTPTRETLIKDAISRGVLSFCDQAIRDLYQILEVEFHPLSICKKLQPIIKRLAESNDTAQYIRPLQQVILTRLFQQLSQVYDSISLKYVMDLATFEEPYDFNPGQIEKFIMNGNKKGAFSIRLNHIENSISFSSDLFSNPIKSSDSVSLQSTPSELITSQLTRIAKSLSSVLMRFDTDFCLLRKQQAEAAYERAQAGVEQERKAVIAQRSLLELRRGQADTLATQREAELAAQRALKQKQESEAESLRVQEEINKRNAERIRREKEAIRINEAKKLAEELKAKGGLEVNAEDLEHLDADKLRAMQIEQVEKQNKSMNERLRVIGKRIDHLERAYRREAIPLWEEDAKQQAEHDREIFYEREKQRKEVQERKHEQAIKDKKAFAQFASYIHAYKQNIDDERDKAYQEAYAKAKNVIDAERERQRKEIFEQKLAEAIREAEEEAARAAEEEANRELHEQEEAQKRAIEERTRAAREAKEREQREMAEKLERQRRIQQERDEEISRKLAEKAAARRANIGASSPSPGAWRRGGASAGGVSRDSPRYSRGGYSRGSVPPRETLAPSKGAYVPPSRRNQQQQ O74774 HBS1_SCHPO BINDING 184..191; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32769"; BINDING 323..326; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32769"; BINDING 352..355; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32769" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P32769}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P32769}; SPBC25B2.01; STRAND 177..183; /evidence="ECO:0007829|PDB:3MCA"; STRAND 186..188; /evidence="ECO:0007829|PDB:3MCA"; STRAND 261..271; /evidence="ECO:0007829|PDB:3MCA"; STRAND 284..290; /evidence="ECO:0007829|PDB:3MCA"; STRAND 318..323; /evidence="ECO:0007829|PDB:3MCA"; STRAND 357..362; /evidence="ECO:0007829|PDB:3MCA"; STRAND 364..366; /evidence="ECO:0007829|PDB:3MCA"; STRAND 368..370; /evidence="ECO:0007829|PDB:3MCA"; STRAND 406..415; /evidence="ECO:0007829|PDB:3MCA"; STRAND 418..431; /evidence="ECO:0007829|PDB:3MCA"; STRAND 435..438; /evidence="ECO:0007829|PDB:3MCA"; STRAND 443..451; /evidence="ECO:0007829|PDB:3MCA"; STRAND 453..455; /evidence="ECO:0007829|PDB:3MCA"; STRAND 460..462; /evidence="ECO:0007829|PDB:3MCA"; STRAND 466..474; /evidence="ECO:0007829|PDB:3MCA"; STRAND 484..486; /evidence="ECO:0007829|PDB:3MCA"; STRAND 488..490; /evidence="ECO:0007829|PDB:3MCA"; STRAND 493..504; /evidence="ECO:0007829|PDB:3MCA"; STRAND 515..520; /evidence="ECO:0007829|PDB:3MCA"; STRAND 525..538; /evidence="ECO:0007829|PDB:3MCA"; STRAND 541..543; /evidence="ECO:0007829|PDB:3MCA"; STRAND 548..558; /evidence="ECO:0007829|PDB:3MCA"; STRAND 560..562; /evidence="ECO:0007829|PDB:3MCA"; STRAND 573..592; /evidence="ECO:0007829|PDB:3MCA" HELIX 168..171; /evidence="ECO:0007829|PDB:3MCA"; HELIX 190..202; /evidence="ECO:0007829|PDB:3MCA"; HELIX 303..312; /evidence="ECO:0007829|PDB:3MCA"; HELIX 325..328; /evidence="ECO:0007829|PDB:3MCA"; HELIX 332..346; /evidence="ECO:0007829|PDB:3MCA"; HELIX 354..356; /evidence="ECO:0007829|PDB:3MCA"; HELIX 377..380; /evidence="ECO:0007829|PDB:3MCA"; HELIX 387..392; /evidence="ECO:0007829|PDB:3MCA"; HELIX 476..478; /evidence="ECO:0007829|PDB:3MCA"; HELIX 569..572; /evidence="ECO:0007829|PDB:3MCA" TURN 347..349; /evidence="ECO:0007829|PDB:3MCA"; TURN 400..402; /evidence="ECO:0007829|PDB:3MCA"; TURN 439..442; /evidence="ECO:0007829|PDB:3MCA"; TURN 565..567; /evidence="ECO:0007829|PDB:3MCA" CHAIN 1..592; /note="Elongation factor 1 alpha-like protein"; /id="PRO_0000326088" MSRHRDVKNLDLDDYELDEEPGEEELTEEQEEEFRSAVATVRETLLGVPISEKEIADTVWYYYFDVEKSVNYLLQKASSKAGAKEKQNTDSQKEKKQNKSKEALADAKDPLDESSNGIKNLSLNKNDEPAFQTNGEVKMKNSSESDNQPEKKKIKKQNPTDLVSVPEIFEQSNPKPVVHLVVTGHVDSGKSTMLGRIMFELGEINSRSMQKLHNEAANSGKGSFSYAWLLDTTEEERARGVTMDVASTTFESDKKIYEIGDAPGHRDFISGMIAGASSADFAVLVVDSSQNNFERGFLENGQTREHAYLLRALGISEIVVSVNKLDLMSWSEDRFQEIKNIVSDFLIKMVGFKTSNVHFVPISAISGTNLIQKDSSDLYKWYKGPTLLSALDQLVPPEKPYRKPLRLSIDDVYRSPRSVTVTGRVEAGNVQVNQVLYDVSSQEDAYVKNVIRNSDPSSTWAVAGDTVTLQLADIEVNQLRPGDILSNYENPVRRVRSFVAEIQTFDIHGPILSGSTLVLHLGRTVTSVSLKIVTVNNKRSRHIASRKRALVRISFLDGLFPLCLAEECPALGRFILRRSGDTVAAGIVKELC O74791 GRN1_SCHPO BINDING 202..205; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P40010, ECO:0000255"; BINDING 276..283; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P40010, ECO:0000255"; BINDING 326..329; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P40010, ECO:0000255" SPBC26H8.08c; STRAND 5..7; /evidence="ECO:0007829|PDB:8ETJ" HELIX 13..30; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..470; /note="GTPase grn1"; /id="PRO_0000348611" MVSLKKKSKRRTTRLRSRIEKKAAESKRKQKRADKKNPQWKSRIPKDPGIPNSFPYKDKILAEIEEQKRIREEEKLARRASGQVDAAMEEEDAVDENGSLMISKIAEAAQASNPDDEEEFVMEEDNLGEAPLLVDSESYEASVKADTSRKAYDKEFKKVVEASDVILYVLDARDPEGTRSKDVERQVLASSAEEKRLIFVINKIDLVPSEVLNKWVTYLRNFFPTIPMRSASGSGNSNLKHQSASASSTISNLLKSLKSYSAKKKLKSSLTVGVIGYPNVGKSSVINALVNRSANGRSAPCPAGNVAGMTTSLREVKLDNKLRLVDSPGIVFPSSDSKDDLYRLVMLNAVSSTKVDDPVAVASYILQFLSRVPGQLERMFQRYELPPLLNTSDIDTATDFLVNIARKRGRLGRGGIPNLNAAANIVINDWHAGRIEWWAEPEVINEKNSSEVQDTQIVTEWAKEFDLNDF O74803 RHP23_SCHPO MOD_RES 84; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 364; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2D10.12; CHAIN 1..368; /note="UV excision repair protein rhp23"; /id="PRO_0000114903" MNLTFKNLQQQKFVISDVSADTKISELKEKIQTQQNYEVERQKLIYSGRILADDKTVGEYNIKEQDFIVCMVSRPKTSTSTPKSAASPAPNPPASVPEKKVEAPSSTVAESTSTTQTVAAAAPSNPDTTATSEAPIDANTLAVGAQRNVAVENMVEMGYERSEVERAMRAAFNNPDRAVEYLLTGIPEDILNRQREESAAALAAQQQQSEALAPTSTGQPANLFEQAALSENENQEQPSNTVGDDPLGFLRSIPQFQQLRQIVQQNPQMLETILQQIGQGDPALAQAITQNPEAFLQLLAEGAEGESALPSGGIQIQITQEESESIDRLCQLGFDRNIVIQAYLACDKNEELAANYLFEHGHESEDEP O74805 MYO51_SCHPO BINDING 159..166; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC2D10.14c; CHAIN 1..1471; /note="Myosin-51"; /id="PRO_0000123482" MSHARLSVGSECWVSNNNGHWDAARLIEIKDNGGGKVVATVAKSSGVLETVNYQQLQNRNIGQSESPSDLTNLPYLNEPSVLHALHNRYNNKQIYTYSGIVLVSINPYQNLPEFYNDNLIKHFHKDPEAAKVPHLYSIASSCYHALTTDSKNQTIIVSGESGAGKTVAAKYIMRYLTSVQGVDHNGVVKRSVENQVLATNPIMEAFGNAKTIRNDNSSRFGKYVTISFDENLLITGANVNTYLLERSRVVSLLKGERNYHIFYQLITGCTEEQRDKWFLESASSFNYLSQGNCDEISGVDDSNDFTITCRALSTIGISESRQEDVFCLLAALLHLGNIEVCATRNEAQIQPGDGYLQKAALLLGVDSSTLAKWIVKRQLKTRSETIITSSTLEHAISIRDSVAKYLYSALFLWIVHMINASLDHNKVKRAAYKYIGVVDIYGFEHFEKNSMEQFCINYANEKLQQEFNKHVFKLEQEEYVKEGLDWRLIEYSDNQGCISLIEDKLGILSLLDEECRLPSGNHQSFLQKLNNQLPTKHSQFYKKSRFNDGSFMVKHYALDVSYQVHDFLAKNSDAIPDEFISLLQNSKNEFITYLLDFYMQLVSSQNKNPRKTAISRKPTLSSMFKSSLSQLMTTVSSTNVHYIRCIKPNEEKLPWTFSPPMVLSQLRACGVFETIRISSLGFPARFSYEEFAHRFRILLSSKEWEEDNKKLTLNIVNSVIPHDNLNFQVGRSKIFFRSNVIGNFEEAHRATCSKSTVLLQSAIRGFFTRKEYQRTVKFIIKLQSVIMGWLTRQRFEREKIERAAILIQAHWRSYIQRKRYLSLIKCAIVIQSIVRKNIAYSRYINELRESSATLLAKFWRAYNARKTFRGLKKSVIALQCVSRSVLTRRYLRRLQDSAGRTSILYEKQKNLQASITEVSKQLKSNSKKVTVLRNKLNILNNSLSKWKCLIKKPSDFSEPVSMDFTSNDEQLVQLLQAESKLRQASQQLYMAAKKSELGFVQSQTARENLSNYYQALQMTVSEKFEYDTEQLPSRVLFYAMDRYFSIHKKLKQLLELVGVENASLLPNEVVNKQTKDLLYEKRVVFLKQIKQALTVSSLFNAVGYKDGVMRLLETDQNSLLFAGVVNFLIFAGISLDLKTQISEFLSQLCSYFTKIVDGTVIENDKTLDFYEKPLQAVLYWFATLHKIRSFLVHLLSINSHGKQSVVEDLWNPLILKFSKHFSNLENSFHSLVQKLLSCCTEGSINALLNSKCLPEFIDAADENTTPTGMNIYELIDRMNLIHKLLISSALQPNLLELTISHMLQHIGQRAFQTLIHGRSPYTWKSASQVSYNASLLINWCHQKGISYVNSSLLPLMQSPLVFCLRKNDANDLDVILSVCNLLSPFEVVCLLNRYQPCAGENPLPKSFSKAVEALSCKYKQSGFTNGKITNTNGHAIPIAASKNPLLSLENNHIYEELRLSELINLLAKATL O74808 CLR1_SCHPO SPBC2D10.17; STRAND 377..379; /evidence="ECO:0007829|PDB:5IKF"; STRAND 485..490; /evidence="ECO:0007829|PDB:5IKF"; STRAND 1212..1215; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 1227..1231; /evidence="ECO:0007829|PDB:5IKJ"; STRAND 1234..1238; /evidence="ECO:0007829|PDB:5IKJ" HELIX 364..372; /evidence="ECO:0007829|PDB:5IKF"; HELIX 387..395; /evidence="ECO:0007829|PDB:5IKF"; HELIX 404..408; /evidence="ECO:0007829|PDB:5IKF"; HELIX 411..413; /evidence="ECO:0007829|PDB:5IKF"; HELIX 417..426; /evidence="ECO:0007829|PDB:5IKF"; HELIX 432..434; /evidence="ECO:0007829|PDB:5IKF"; HELIX 447..464; /evidence="ECO:0007829|PDB:5IKF"; HELIX 469..478; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1163..1173; /evidence="ECO:0007829|PDB:5IKJ"; HELIX 1221..1226; /evidence="ECO:0007829|PDB:5IKJ" TURN 361..363; /evidence="ECO:0007829|PDB:5IKF"; TURN 396..399; /evidence="ECO:0007829|PDB:5IKF" CHAIN 1..1238; /note="Cryptic loci regulator protein 1"; /id="PRO_0000290637" MAEPDISSSETLTELQQLRLLYFFCFYHAAPFNVKTLVHSLIPPGALSYLLSTYDILRPWLMALRVREGPVNDISTIVQLYEEIVKTGFFINPPPFESYSQTLVARITTLGRPKLQVQQEAQSEVYQRASTNTQQQVSNVSHGNFKPNSSVNTEPNTSILSNSKYAGIKPFDFQSSSQNPGLVCEQKTFYQHQFRPFSNLPSNKSSPVKHVSPNVKNNSKKTASSVNSNHSSIPSSITKSNISSLDVYGSEKLISSGSQQPGHGMVQTTSDKVNASASLYDRSPSKKDITSSRNTSSYNLGSMRNPSTLKNAAHANPFEGLRFQGSSAVLKEGLNSTVKKTFFDNLNSEKVCPSVSPFLTPDNIASSILYSTASFSRSKPDRPRLNLSLELKLMQNELNKGQLKKQFKGDLRNLADWNNLSLVSSKFPSLPITNLRPDGSFLKHRRFNEEIAYNRQTLEKAIKQLDLSPDKVIQLREQNGVAVNGRVCYPTRNKHSEISAQSSSSLGVTKSLASEVYSSSTVDTISKLNTDKDNYLIKSKKEPIQQKSVSSETTLVKPSSTSSYIDTTNNVLKTNSSFKSSGLTSGPRNEKELLPEGIPTSHNNSETQAQTADVSNIAASADGIYNSDQEKPPEKLDVTKRAFGREIENSNEKELLTSTFLSPSAESQVCLAEIKTIRPGLVPKKQFSVDQNNVISDNTDCSLPKPSNSKLSSISSDGDASSNRMAVPDKSPFVHAAPNSKALTKDSFSTHISVSSLLHSDNEISPIDSTRKDYFTSKDSNLQTLKEDASSTKQAKDSGTNDFDKLISGNDVSKNNSGEEQSRSALKPLISGKLSSCESINLTKDISTVKRKEYFGIESTSSKQPFHDTGSIKIPAKRSFDTIDKDFRSSNIPFADKIKEDGGDKNVISSIHITTELPKSMPVEVPTNAGAQSDQSNVVDSESLNLRENISTSVADVSLSQAGNEAVLSKKACKPLVLIDPFEEKVLKAFNMLSKGYAEYRCQWEGCLANLHSLENFIKHVLLLHHPKSCSVVKCLWASCDMVLPSEEFEMHLRGHLNNIRLNCEVSNCKKCFSNYEDMFKHLQHSHLPFKFTPESFIKIRNGNVKEEARRTRNAYTQKSGEVECFMETCTPIAKPAPANWYPVPPPGFNSSLLSRLTQSNQSKDKIIAALAKRNVYKSFAGLYDSKGKNDNTGYDFDSNYARVGRHGSFILPVSKSVPTPSLLIEGSIVQRKNIKIE O74833 DNLI4_SCHPO ACT_SITE 281; /note="N6-AMP-lysine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" BINDING 279; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 281; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 282; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 286; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 341; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 341; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 378; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 438; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 438; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 443; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 460; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917"; BINDING 462; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P49917" CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49917}; SPCC1183.05c; CHAIN 1..913; /note="DNA ligase 4"; /id="PRO_0000059581" MDEAKETVFTKPQNHSSTLEFYDFVTTLLEPLSRIGKTRKSKTSNLDPYELKRKILLDYFNKWRQHVGPDLYPLLRLMLPDLDRERGSYGFKEFGLGKLFIRAMHLSPTSEDAKSLKNWRGSESKHTGDFSTMLQDILQRRAYRTFPGAFTVGDVNALLDQLADASSEDTRVNILEQFYRSLSPLELRWLIPILLKVRKYGTSEKFILSVFHPDAARLYRLCSSLKRICWELYDPSRSLDETETDVEVFSCFQPQLANFKKKDLHQTLEAMGNKPFWIEEKLDGERIQLHMSSGKFQFYSRNARSYTYAYGSSYFDEQSRLTQYIIGAFDKRISQIILDGEMVTWDPVLETVIPYGSLRSIFEDSSSHSSYSPYYVVFDILYLNGKSLVKYSLESRRRILEKVIVRESHRMSILPYKVGSTIEDIEAELRNVIQEGSEGLVIKKPSGSYHLGERMDDWIKVKPYYLQGFGEDLDCLILGGYFGRGKQSGKINSFLCGLRMDYTPKDHSEKFQSFVRVGGGFTYFDRDIIRKETEGKWLPWSSDALEYMELAGTKQDFEKPDMWIHPKDSLVLQIKAAEVVVSNRFKTNYTLRFPRLEKVRLDRSWKDALTINEFFTLKNAVEKQDNVSFHVNKKRKVSQKREKQKKFLYDEPTFKKEASPHSDVLKNLHFVVLPPTELHETKAGLQQIIIENGGLIHQGVGNFGKERLFLVADRVSTRVSIERSKNMCTIIRSQWVMDSVNNQRLMPQWSYLLFSKDEKYSWKTALESLSAKSLSNLLVELKQLDLSKEYSKISDDTSILNLTISKEEASFVGAFPFLKFTVFLDLKGIENSELYDVRMGQYRLTKCILLWNGATIEKDISSKKLTHVVMFVEDSTRLEQLTKACELYQIEPKFVNFEWVVNEWKKASTNILG O74839 MSY1_SCHPO MOD_RES 98; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1183.11; CHAIN 1..1011; /note="Mechanosensitive ion channel protein Msy1"; /id="PRO_0000372692" MSSPTSPTSSPGRHHWSNSKDGMPPEYTNQDPNSDQADNENSDAKAHQPQHSPQHSTENQGHTGTSDTSSLEMELSKLHPESKQRQLPHSPEHERSRSPIASVVSYRSHMTLEDENQIFNAEMAVRGSQSLQRRPTGRSVRGSMRRLSSHRSKSMRTSKSKKSGDYERTAENEEAAQEAENHLDNFGVVTFGTEAPIKAPDHPVTIFGRIFKFIQQRSFYLRSLIYIIPLGVLLLIPVFIGRFYHPQPPYRDELGHEYERHLHVGGVDLMWMAIWWEIIWLSIWAARYAAKVIPYFFAFFVSFISNNVTKWRCMAVALEFPITLFLWMLAVYVSFLPIMTRRHIGDYGVPDHVRVKLPWQQSANNVLITLFITSIMNLVEKVLMQLIAMSLHRREYESRILYNKFAINELARLYGYARQRSFDFKDAIHRAQADVFKFADHQHGKKRAAAARVAQNALNKTTYKAISAFNFATDMVNKVAGEITNREVEKSSSPKSVVLHLLKTTRGCQSLARCLFEALVNPENPDLVLDDFIPVYTDETGEVDNATLEACYSIFDRDLNGDITCEEIELACVEIGKERKSISASLRDLNDSISKLDGICMFIVAVITLFIFLYLIARNFSGVLTSAGTTLLGLSWLFSGSAQELLSSIIFVFVKHPYDVGDRVDVMINGTVTSAMVKEISIMSTEFRLLTGKVIQAPNSLLNTLWILNMRRSDGIADPVTVNLKFGTTLQQIEQLRIKIIDFLKEEKRDYKPDLLTEVTDLPDLYSMSLCVVFFHKYNFQDEVLRMRRRNMFMCALMTYMQELDIVSPIFNSPGKSKDSPMYVNFNNGSMEGVKLSGGNDGGGTENHRDSTVGGGILKNPKAYPYREPTPPGSSDSDTASVSKKRVDFSLGTRHLMPAFDDVADIGSKRLGRDSLPDAVIENAGTEAMRREAEERRRAEEEEYERSQQESSSNEENENASRTSGARFSFSSKASRLSARPSARTVPPLQHISIQDLREPNENNTSKSARL O74844 CENPQ_SCHPO SPCC1235.07; CHAIN 1..244; /note="Inner kinetochore subunit fta7"; /id="PRO_0000290642" MEMKRRVRAVRRDQIQKRWRPLEDKQRQEIIIIFRTCSRLVLNTIKSETRKSLAEEWFMNILLKIEAPLRNLPVPRKRKESILFSQLLSSNMQLEQQLYSDLDHINVLQQELKVETARLENEQKSYEEMKQNMAINNSRLADLKSKLHPYLKKGLKISHDNFSDSNDFSFQKKLNTEDSNTSKTSTLDMYKEKLKPFTKTMQIHANKTVQLSQTIQKATLLLQRLNNTKNIGLNKSSKLKIKNI O74846 SEC6_SCHPO SPCC1235.10c; CHAIN 1..752; /note="Exocyst complex component sec6"; /id="PRO_0000118930" MTAAASDDAVYNKVADILRQCEDFHRLSTHIERFEREQASLNMHVKTELEKHVEAVELGKLALHDAQTKRVKLLQELHNMLTLCESAREMVDEFPLISRMSRIYKNCYATKQMISQLNNLVKETDVIEDMLREDLELDSDMPNLLRAHYKLSKLREFREEALYQASLEGQSDLPITLENSFSNLNTLSDNFDRLVLNFCRNIFQLVKSGHIKTIVQIFKIVEAEESSDEVLKSIRDAKSSLPDSQDGPFLSLQGMTRQLRNFRLRVLEEFQGAAAENFQRAWVSYLEDGSGELNLDFIFEDLKVAFYVLPDLTPPSYNIAKTFASIYQECLVGLVTKAVSLDTPAAVYLYLINFHREYRKFFEENAPFSVDEVEPGLEDGKDGILVREYTRLFTQKIREWSDKLFQSSVDTFMKRESEPELDSDGNYGLQGTIIFFQMITQQINIISHTNNSDVVGIVLSSIMYIMQSMQDQWKSVMRSELSQQLSGNPESVPPGLMEYLLAVANDNLKCAGFMDNTLLNTFELITSEREEDLREAFGKTVDGYILISDIGVSQIVAIISNDVKPALTSLFQPNWYQSSNMKLIVDTFRDYIVDCIEHMVPGLFDVFLLEASNALTISYLRSIFNKNACFDGDNAIQQIRSDIALAIRVFGEYMAAEHLRSTFEPIEKLLLGMLDADVETVSEYFHLLKEAYWDAPLSLVEAVLQNRTDLEKSIIKKMIDIVRHENDSLQIDTSQQPTVFSQVTSLSGSSIL O74850 DGAT2_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:12963726}; CATALYTIC ACTIVITY: Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000269|PubMed:12963726}; SPCC1235.15; CHAIN 1..345; /note="Diacylglycerol O-acyltransferase 1"; /id="PRO_0000176219" MSEETSIPGIIASTPPISKDSRRNVSHWLQALAVFLHSVSLTLTASWYTVLWAFLPFWPFLIVYLIWLIYDDGFVTGKDRQKRWLRNAPPYRWFCHYFPIRLHKTTELDSEKNYIFGYHPHGIISLGAFGGFASEGADFSKLFPGINVSVLTLNSNFYVPVYRDYLMALNINSVSKKSCVSILSRKPGDSVLIVIGGAQESLLSRPGQNNLVLKKRFGFVKLAFLTGSSLVPCFAFGESDIFEQVDNNPRTRIYKFQEIVKKIAGFTVPFFYGRGLLNKTFGLMPWRKPINIVVGEPIDVPKKSHPTNQEIYEVHEEYIRRLEGLWNKYKDVFLPNRISELKLSA O74854 POF6_SCHPO SPCC18.04; CHAIN 1..872; /note="F-box protein pof6"; /id="PRO_0000119973" MKPSEAREHAIRKIKEYLERRHKQQFKALFGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKKLLLMNAWDVTLSRKLYYESQDGMSQANMSSNTSKGFHLQSSDKKYADSDRPKLSSSSLLSLPDQKIPFPVDYSTVQGKQVVLTVLDCVSQRVEFARLDYIKVWRALAPIYRNLAYASNTIDPIAFSAFRTPEEQSKVLKYLIRFGNSYPYGTYRQAMQNAILDMASLFEQACLDEFELGLHSRNLDLLRKFSHVLHDFSGPNAYVSMYLAKQTDFVRSFFHFDPYSLFISNNLEEIHINWNILESVVNDTIKLLESESKFSEATLPEPELVQVPYAKDILGNSLKDYVISICEHIGEEETELFLVFISGFYGLCKKFFSIPNGPALVDTIFQPQIDIFISQELHYFKTVGWSLVDQWDQKLEEKEDATECFFYKNVSQNTAKNNFLETFKNVMLLPVSLFTIPSENNSASNLAEKAIEQKEEEDPELSKLDAARFVPANIYVSKDRLKHLPTTELAAQAAVLDSKLEGISTMFSLELALKIVHLCKVSLARAKVFMGTSVPQDDDIKGLSKDLFVQLLRELGQGHLKHGFDRAIEHLSSFDPRRDFSSNTVEPVVKFLELINVGDMIQQMMDSFFNEEMSPICVKDDMFDPAIAEKKKFEQLLDERAAFGLHKGINVLIEHADFLLETKTPMNLFSDQTIGSITNTIEPTAAAKNVVQFLGFHMRILVGRADHEILDVFYKEVGMRLFDSLTRYIKSHKFSVDGGLKLLSDCNLYYEFIHSLHQSSLLPYFKTLKEIAHLFIIDGKNAEEIGKLATDTSRFSSAFHTEEVYEILHSRIDWLNIKYEVDKVIHGLACCIM O74856 CAF1_SCHPO BINDING 53; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; BINDING 53; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:19307292"; BINDING 55; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; BINDING 55; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:19307292"; BINDING 174; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; BINDING 243; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; BINDING 243; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:19307292" CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19307292}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:19307292}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19307292}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19307292}; Note=Binds 1 Zn(2+) ion per subunit. At lower physiological Zn(2+) concentrations, Mg(2+) replaces Zn(2+). The nature of the bound ion affects the speed of the RNA degradation reaction and, to a limited extent, base selectivity. {ECO:0000269|PubMed:19307292}; MOD_RES 302; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 304; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 306; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC18.06c; STRAND 24..28; /evidence="ECO:0007829|PDB:2P51"; STRAND 49..55; /evidence="ECO:0007829|PDB:2P51"; STRAND 68..70; /evidence="ECO:0007829|PDB:2P51"; STRAND 89..95; /evidence="ECO:0007829|PDB:2P51"; STRAND 106..112; /evidence="ECO:0007829|PDB:2P51"; STRAND 156..160; /evidence="ECO:0007829|PDB:2P51"; STRAND 165..170; /evidence="ECO:0007829|PDB:2P51"; STRAND 202..207; /evidence="ECO:0007829|PDB:2P51" HELIX 33..43; /evidence="ECO:0007829|PDB:2P51"; HELIX 71..84; /evidence="ECO:0007829|PDB:2P51"; HELIX 123..131; /evidence="ECO:0007829|PDB:2P51"; HELIX 136..142; /evidence="ECO:0007829|PDB:2P51"; HELIX 146..154; /evidence="ECO:0007829|PDB:2P51"; HELIX 172..183; /evidence="ECO:0007829|PDB:2P51"; HELIX 191..201; /evidence="ECO:0007829|PDB:2P51"; HELIX 208..212; /evidence="ECO:0007829|PDB:2P51"; HELIX 222..228; /evidence="ECO:0007829|PDB:2P51"; HELIX 240..259; /evidence="ECO:0007829|PDB:2P51"; HELIX 265..267; /evidence="ECO:0007829|PDB:2P51" TURN 30..32; /evidence="ECO:0007829|PDB:2P51"; TURN 44..46; /evidence="ECO:0007829|PDB:2P51"; TURN 116..118; /evidence="ECO:0007829|PDB:2P51"; TURN 213..216; /evidence="ECO:0007829|PDB:2P51" CHAIN 1..335; /note="Poly(A) ribonuclease pop2"; /id="PRO_0000362142" MTAMNSNFSYPALGVDGISSQISPIRDVWSTNLQQEMNLIMSLIERYPVVSMDTEFPGVVARPLGVFKSSDDYHYQTLRANVDSLKIIQIGLALSDEEGNAPVEACTWQFNFTFNLQDDMYAPESIELLTKSGIDFKKHQEVGIEPADFAELLIGSGLVLQEEVTWITFHSGYDFAYLLKAMTQIPLPAEYEEFYKILCIYFPKNYDIKYIMKSVLNNSKGLQDIADDLQIHRIGPQHQAGSDALLTARIFFEIRSRYFDGSIDSRMLNQLYGLGSTGSVLWHNNSSTPQIQFRDLPGAHPSPTPSNAGIPTTLTNTSSAPNFANSTFRFPPRVV O74859 APTX_SCHPO ACT_SITE 147; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:21984210, ECO:0000305|PubMed:26007660" BINDING 200; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:26007660, ECO:0007744|PDB:3SPD, ECO:0007744|PDB:3SPL, ECO:0007744|PDB:4XBA"; BINDING 203; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:26007660, ECO:0007744|PDB:3SPD, ECO:0007744|PDB:3SPL, ECO:0007744|PDB:4XBA"; BINDING 217; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:26007660, ECO:0007744|PDB:3SPD, ECO:0007744|PDB:3SPL, ECO:0007744|PDB:4XBA"; BINDING 221; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:26007660, ECO:0007744|PDB:3SPD, ECO:0007744|PDB:3SPL, ECO:0007744|PDB:4XBA" CATALYTIC ACTIVITY: Reaction=a 5'-end adenosine-5'-diphospho-5'-2'-deoxyribonucleoside-DNA + H2O = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + AMP + 2 H(+); Xref=Rhea:RHEA:52128, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:136413, ChEBI:CHEBI:456215; EC=3.6.1.71; Evidence={ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:24362567}; CATALYTIC ACTIVITY: Reaction=a 5'-end adenosine-5'-diphospho-5'-ribonucleoside-2'-deoxyribonucleotide-DNA + H2O = a 5'-end 5'-phospho-ribonucleoside-2'-deoxyribonucleotide-DNA + AMP + 2 H(+); Xref=Rhea:RHEA:52132, Rhea:RHEA-COMP:13182, Rhea:RHEA-COMP:13183, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136414, ChEBI:CHEBI:136415, ChEBI:CHEBI:456215; EC=3.6.1.71; Evidence={ECO:0000269|PubMed:21984210}; CATALYTIC ACTIVITY: Reaction=a 3'-end 2'-deoxyribonucleotide-3'-diphospho-5'-guanosine-DNA + H2O = a 3'-end 2'-deoxyribonucleotide 3'-phosphate-DNA + GMP + 2 H(+); Xref=Rhea:RHEA:52140, Rhea:RHEA-COMP:13186, Rhea:RHEA-COMP:13187, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115, ChEBI:CHEBI:136419, ChEBI:CHEBI:136420; EC=3.6.1.72; Evidence={ECO:0000269|PubMed:26007660}; SPCC18.09c; STRAND 51..54; /evidence="ECO:0007829|PDB:4XBA"; STRAND 56..62; /evidence="ECO:0007829|PDB:4XBA"; STRAND 67..76; /evidence="ECO:0007829|PDB:4XBA"; STRAND 133..140; /evidence="ECO:0007829|PDB:4XBA"; STRAND 142..145; /evidence="ECO:0007829|PDB:4XBA"; STRAND 148..153; /evidence="ECO:0007829|PDB:4XBA"; STRAND 174..176; /evidence="ECO:0007829|PDB:4XBA"; STRAND 206..208; /evidence="ECO:0007829|PDB:3SPD" HELIX 34..38; /evidence="ECO:0007829|PDB:4XBA"; HELIX 39..43; /evidence="ECO:0007829|PDB:4XBA"; HELIX 45..47; /evidence="ECO:0007829|PDB:4XBA"; HELIX 86..92; /evidence="ECO:0007829|PDB:4XBA"; HELIX 94..105; /evidence="ECO:0007829|PDB:4XBA"; HELIX 109..119; /evidence="ECO:0007829|PDB:4XBA"; HELIX 126..130; /evidence="ECO:0007829|PDB:4XBA"; HELIX 163..169; /evidence="ECO:0007829|PDB:4XBA"; HELIX 181..183; /evidence="ECO:0007829|PDB:4XBA"; HELIX 190..192; /evidence="ECO:0007829|PDB:4XBA"; HELIX 193..195; /evidence="ECO:0007829|PDB:4YKL"; HELIX 211..229; /evidence="ECO:0007829|PDB:4XBA" TURN 79..83; /evidence="ECO:0007829|PDB:4XBA"; TURN 106..108; /evidence="ECO:0007829|PDB:4XBA"; TURN 201..203; /evidence="ECO:0007829|PDB:4XBA" CHAIN 1..232; /note="Aprataxin-like protein"; /id="PRO_0000314650" MSVHKTNDAFKVLMNSAKEPIVEDIPKKYRKQSFRDNLKVYIESPESYKNVIYYDDDVVLVRDMFPKSKMHLLLMTRDPHLTHVHPLEIMMKHRSLVEKLVSYVQGDLSGLIFDEARNCLSQQLTNEALCNYIKVGFHAGPSMNNLHLHIMTLDHVSPSLKNSAHYISFTSPFFVKIDTPTSNLPTRGTLTSLFQEDLKCWRCGETFGRHFTKLKAHLQEEYDDWLDKSVSM O74866 RIFK_SCHPO ACT_SITE 96; /note="Nucleophile"; /evidence="ECO:0000305" BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105" CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; SPCC18.16c; STRAND 24..31; /evidence="ECO:0007829|PDB:1N08"; STRAND 34..36; /evidence="ECO:0007829|PDB:1N08"; STRAND 46..48; /evidence="ECO:0007829|PDB:1N08"; STRAND 62..71; /evidence="ECO:0007829|PDB:1N08"; STRAND 74..84; /evidence="ECO:0007829|PDB:1N08"; STRAND 93..99; /evidence="ECO:0007829|PDB:1N08"; STRAND 111..121; /evidence="ECO:0007829|PDB:1N08" HELIX 38..41; /evidence="ECO:0007829|PDB:1N08"; HELIX 50..52; /evidence="ECO:0007829|PDB:1N08"; HELIX 129..147; /evidence="ECO:0007829|PDB:1N08"; HELIX 150..153; /evidence="ECO:0007829|PDB:1N08"; HELIX 154..157; /evidence="ECO:0007829|PDB:1N08"; HELIX 159..161; /evidence="ECO:0007829|PDB:1N08" TURN 53..59; /evidence="ECO:0007829|PDB:1N08" CHAIN 1..163; /note="Riboflavin kinase"; /id="PRO_0000194151" MTVNLEEKRPEIVGPEKVQSPYPIRFEGKVVHGFGRGSKELGIPTANISEDAIQELLRYRDSGVYFGYAMVQKRVFPMVMSVGWNPYYKNKLRSAEVHLIERQGEDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNSMDRPSYSSYKKDPFFKV O74874 CCR4_SCHPO BINDING 387; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:O95551" CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPCC31H12.08c; CHAIN 1..690; /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"; /id="PRO_0000290617" MFNPRYTQGTIYPGAHPGLLTPDHQHAAILSVQNSPALENSNISEHWKQQIALATQSRSFSSPHQRAHNAAALARSGGPGFSMNYNARTGAFTGGPNAAGLSSLGGKYNTSSTTTTLTTSTTLNTSSGTTLNSTSKTTTSSVAVDDQKSKSDSKKERRDWTCLDLGGIGLRNVSTDLFKFSFLTELYINHNNLTRLPPEIGKLKNLVILDASGNSIKTIPPELGLLTELREVLLFDNMISVIPAELGTLFQLKILGIEGNPLQDVYKNQIMESGTAGLIAALRDGCPVGPPPPERGWEKLVSDDDDDVNDNVSTSVRDLTAADSNKPSTTSKNLKFTIMSYNVLCERYATSTLYGYTPSWALSWSYRKDLIMQELGGYNADIICLQEVDVENYDTFFAPQMSLKGYKGVHFPKSRVRTMNEVERRIVDGCATFFKTSKYVMHEKMVIEYNQAPSLRRQDIKLTSNMYNRVMTKDNISVITLLENKENGSRLIVANCHIHWDPQFRDVKVIQVAMLMDEIAQVATKFRNMPSKIPSDQLKDERPTYPEYLKIPILICGDFNSVQGSGVYDFLSSGSISQNHEDFMNNDYGEYTVNGRSHAFNLKSAYGESEALSFTNYTPGFKGAIDHIWYTGNSLEVTGLLKGVDKDYLSGVVGFPNAHFPSDHICLLAEFKVKQEKTPLPSSKFNNDKK O74880 MCES_SCHPO BINDING 92..93; /ligand="mRNA"; /ligand_id="ChEBI:CHEBI:33699"; /ligand_part="mRNA cap"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"; BINDING 96; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"; BINDING 118; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"; BINDING 140; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"; BINDING 168; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43148"; BINDING 191; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43148"; BINDING 196; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43148" CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-ProRule:PRU00895}; SPCC330.10; CHAIN 1..360; /note="mRNA cap guanine-N7 methyltransferase"; /id="PRO_0000303915" MSSSNSRVHEEQPPTENRRYARPTAQMNRVIEQQPRRRDYFQNNDNSGRRGYNRHENNGNAQDVVRSHYNARPDLGYKKRQFSPIIQLKRFNNWIKSVLIQKFAPHASDYPILVLDMGCGKGGDLIKWDKAGIDGYIGIDIAEVSVNQAKKRYREMHASFDALFYAGDCFSSSINELLPPDQRKFDVVSLQFCMHYAFESEEKVRVLLGNVSKCLPRGGVMIGTIPNSDVIVKHIKMLKPGEKEWGNDIYKVRFPESPPRSFRPPYGIQYYFYLEDAVTDVPEYVVPFEAFRAVAEGYNLELIWVKPFLDILNEEKNSETYGPLMDRMKVVDNEGHRGIGGQEKEAAGFYLAFAFEKRGI O74887 TPX1_SCHPO ACT_SITE 48; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000305|PubMed:24316080" CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:20356456}; PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin srx1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:15956211}. MOD_RES 105; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC576.03c; CHAIN 1..192; /note="Peroxiredoxin tpx1"; /id="PRO_0000351076" DISULFID 48; /note="Interchain (with C-169); in linked form"; /evidence="ECO:0000269|PubMed:24316080"; DISULFID 169; /note="Interchain (with C-30 in TRX1); transient"; /evidence="ECO:0000269|PubMed:24316080"; DISULFID 169; /note="Interchain (with C-48); in linked form"; /evidence="ECO:0000269|PubMed:24316080" MSLQIGKPAPDFKGTAVVNGAFEEIKLADYKGKWVFLGFYPLDFTFVCPTEIVAFSEAASKFAERNAQVILTSTDSEYSHLAFINTPRKEGGLGGINIPLLADPSHKVSRDYGVLIEDAGVAFRGLFLIDPKGVLRQITINDLPVGRSVDEALRLLDAFQFVEEHGEVCPANWHKGSDTIDTKNPEKYFSKH O74910 RAF1_SCHPO SPCC613.12c; STRAND 231..236; /evidence="ECO:0007829|PDB:4O9D"; STRAND 243..248; /evidence="ECO:0007829|PDB:4O9D"; STRAND 252..259; /evidence="ECO:0007829|PDB:4O9D"; STRAND 271..276; /evidence="ECO:0007829|PDB:4O9D"; STRAND 281..284; /evidence="ECO:0007829|PDB:4O9D"; STRAND 289..291; /evidence="ECO:0007829|PDB:4O9D"; STRAND 297..299; /evidence="ECO:0007829|PDB:4O9D"; STRAND 302..307; /evidence="ECO:0007829|PDB:4O9D"; STRAND 311..318; /evidence="ECO:0007829|PDB:4O9D"; STRAND 323..327; /evidence="ECO:0007829|PDB:4O9D"; STRAND 332..336; /evidence="ECO:0007829|PDB:4O9D"; STRAND 343..348; /evidence="ECO:0007829|PDB:4O9D"; STRAND 354..358; /evidence="ECO:0007829|PDB:4O9D"; STRAND 363..368; /evidence="ECO:0007829|PDB:4O9D"; STRAND 375..381; /evidence="ECO:0007829|PDB:4O9D"; STRAND 392..399; /evidence="ECO:0007829|PDB:4O9D"; STRAND 408..414; /evidence="ECO:0007829|PDB:4O9D"; STRAND 424..429; /evidence="ECO:0007829|PDB:4O9D"; STRAND 434..438; /evidence="ECO:0007829|PDB:4O9D"; STRAND 445..451; /evidence="ECO:0007829|PDB:4O9D"; STRAND 456..463; /evidence="ECO:0007829|PDB:4O9D"; STRAND 465..474; /evidence="ECO:0007829|PDB:4O9D"; STRAND 479..487; /evidence="ECO:0007829|PDB:4O9D"; STRAND 489..496; /evidence="ECO:0007829|PDB:4O9D"; STRAND 502..507; /evidence="ECO:0007829|PDB:4O9D"; STRAND 510..516; /evidence="ECO:0007829|PDB:4O9D"; STRAND 524..528; /evidence="ECO:0007829|PDB:4O9D"; STRAND 551..554; /evidence="ECO:0007829|PDB:4O9D"; STRAND 561..564; /evidence="ECO:0007829|PDB:4O9D"; STRAND 568..573; /evidence="ECO:0007829|PDB:4O9D"; STRAND 577..579; /evidence="ECO:0007829|PDB:4O9D"; STRAND 581..587; /evidence="ECO:0007829|PDB:4O9D"; STRAND 592..597; /evidence="ECO:0007829|PDB:4O9D"; STRAND 601..608; /evidence="ECO:0007829|PDB:4O9D"; STRAND 613..617; /evidence="ECO:0007829|PDB:4O9D"; STRAND 630..632; /evidence="ECO:0007829|PDB:4O9D" HELIX 226..228; /evidence="ECO:0007829|PDB:4O9D"; HELIX 384..388; /evidence="ECO:0007829|PDB:4O9D" TURN 277..280; /evidence="ECO:0007829|PDB:4O9D"; TURN 370..372; /evidence="ECO:0007829|PDB:4O9D"; TURN 401..404; /evidence="ECO:0007829|PDB:4O9D"; TURN 430..433; /evidence="ECO:0007829|PDB:4O9D"; TURN 475..478; /evidence="ECO:0007829|PDB:4O9D" CHAIN 1..638; /note="Rik1-associated factor 1"; /id="PRO_0000051497" MTNSSPRVKRRTDTQYLHSVSSKLPKVDFDTNNEEFFEEEFEIYDPFYRAELPCPKPSLSISKHSIAKVPSNVNKRLELQLLLTSGTFLPNSRPYLSERVRKHTHLLSNSITGDDKPSLIHVDFTPEECFILQEAKLKFGPVNSVQFNDAYSTHISPKLPGRAYEDCQKFEIDNPSLSPVDKHGAIILRTYKKNKKLLPDYLKSFYNAGSSYFQREQVHQLMDGESVFFLKPWKHFNETSGDTVCVAYNPLCEKFALGSTAQDGAYNRLGNLWIGDFHSETIQSLESHYKLNQVGEKEYSTISDLCFSKGNLFLYTGAFDNAVKVWDMEGNLCGIFNAPTDYIHKLALSDDDLLAVACKNGYGYLLSTDNSTGEILTSANLIYPEALEKGYSASLIEFSNFLGRSSDKVIIGYDSFHTSNNRGCLALFDASTASFVQKFNTADEAFTSLYMHPSQVGFVASSNTLSNGRVYYLDTRMYKVCLNFTTTQKDINHATISNSGILVTSSGTDNQTFVWDSRKPDKPLSLLKHGKTKMIHFDGANEEEVDAGINMAQWQPKGNLFVTGGSDGIVKVWDLRLNNPFIQNFTEMNSAITYGGFSEDASKLTVCCVGGDVNMYSLGNDNGNKFGEFRIIENRLLT O74919 RNC1_SCHPO PTM: Phosphorylated by pmk1. Phosphorylation causes enhancement of the RNA-binding activity. {ECO:0000269|PubMed:12931193}. MOD_RES 50; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:12931193" SPCC757.09c; CHAIN 1..398; /note="RNA-binding protein rnc1"; /id="PRO_0000334490" MAYNHFSIPKNIEEKENSFFDVTFQDEPDETTSTATGIAKVSIPTPKPSTPLSTLTNGSTIQQSMTNQPEPTSQVPPISAKPPMDDATYATQQLTLRALLSTREAGIIIGKAGKNVAELRSTTNVKAGVTKAVPNVHDRVLTISGPLENVVRAYRFIIDIFAKNSTNPDGTPSDANTPRKLRLLIAHSLMGSIIGRNGLRIKLIQDKCSCRMIASKDMLPQSTERTVEIHGTVDNLHAAIWEIGKCLIDDWERGAGTVFYNPVSRLTQPLPSLASTASPQQVSPPAAPSTTSGEAIPENFVSYGAQVFPATQMPFLQQPKVTQNISIPADMVGCIIGRGGSKISEIRRTSGSKISIAKEPHDETGERMFTITGTHEENEKALFLLYQQLEMEKDRRSH O74926 RBD2_SCHPO ACT_SITE 130; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872"; ACT_SITE 182; /evidence="ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872" CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872}; SPCC790.03; CHAIN 1..251; /note="Rhomboid-type serine protease 2"; /id="PRO_0000206191" MIFMILGRSKEFILKLPIWTQIITYIAILVYALSFFGISTGVLSLSWIGLLQKRQLYEIITYVTLHLSMLHIVFNFVSLLPAMSQFEKKQGTLACILVTVIPYTLFPGIMHLIVYHFFLRKDYVSIAGLSGWAFAFISASCVHSPQRLISFFNLFSIPAYCFPIIYLIMTTILVPKASFIGHASGAVMGYCTPFMLGSIPLKSWAQNVDPIFQSWVKNYHSFDQLSHAQLPIAEPLSTFSSFPGKGTRLGG O74944 POLK_SCHPO BINDING 136; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 226; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 492; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 495; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 509; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 513; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; SPCC553.07c; CHAIN 1..547; /note="DNA polymerase kappa"; /id="PRO_0000278522" MENAKDFIGETIKENGLLTIEDDGSSSSDEEATLKRRLAGPSVLKSGQENVNQKKINEIIYEASKGSKFFEAEQKRDRELRLRIEKVQVEVEKYQSKLRFDKAFQREWTIRQESVDTTVEDFRAKRDLTQIIVHVDCDAFYASIEELKNPKLKSLPMAVGKSVLCTANYVARKFGVRSAMPEFIARKICPDLVVIPLNLSEYAIKSKEIQNVLAQYDSNLCPASIDEFYMNLTSHLRLQELAFTVENITMVVEKIRKQVHEETGVTVSCGIAANKLLAKIASNKRKPNNQFFIPFDEIGISKFMNDLPVREVSGIGRVLEQQLLGLEIKTCGDIQRNLVILSYIFLPKSFQNLLRCSYGFGTTILDEYGESKRKTIGSEATFSSNLSSPSIIEYKLRLLVQNVSENLQKRGLVTNSIAIKYKTSEFQVHTKQKSIGQFIHSESDLLKPALQLLRQSYPMTIRLLGVRATKLVSKSRCLAMQLKFQSQNTVPCPVCQKNIENELGILNQHVDLCLNVETVKSLINTDHTANPTIKKRKSNTLDTYFLE O74954 CBF11_SCHPO SPCC736.08; CHAIN 1..613; /note="Transcription factor cbf11"; /id="PRO_0000363405" MGDYFAWDFANISGSNTSGSLNLNQLNLDNINNGLHNQEDGAGGRNENSERVGSGSPGSVSMQVLSLFSAVNSALATLEKSEEFPSVVKDEQSIFPAVAKASNSLDELAQNIIPAPSPPGFNRKRKTFDEDSSVEMIRRAISDHLDLLNNCCIGIANLNEDSVHKISLTRSGKPSQLVTVSCRHSSVIQKSYGSEKRYLCPPPMVYINGNYSSIFNQSFRTEISIMNDFGQCSQPISEEYTGQGCMIFRSLHISSLVAAKSKNLRLSLDMFSNVNNQLLSHLVTSSISIVSKPSKKGSKLKISNITLRSGSVVSLYNRINSQTVRTKYTSIEAGQFCLRGDRWVPLRINLLLPDENGKLKVCDDVDNPEPIKYGSIVELVDEATGTTSDPLIIRRVEKDHIAEEDGYVNQMHRIVLESAYPISNVRHLKIAEHSSLAYSNNISVRWFLGATSAQNRNASSEAILPIEWEAVGNLSSNEMTRVGDSVCWTIVGISHFDCTMMLPFNQNPVPTVTDYPYIEEPPEYLESSRSLQFKIGGYSVGLQIWLGVHGPLSYSFTAAADTSTMGTVTLGLSQISYDPSCAEQKYPLLFVIPGGIVIIGKCEILLTSSAFGN O74957 AGO1_SCHPO SPCC736.11; CHAIN 1..834; /note="Protein argonaute"; /id="PRO_0000194065" MSYKPSSEIALRPGYGGLGKQITLKANFFQIISLPNETINQYHVIVGDGSRVPRKQSQLIWNSKEVKQYFGSSWMNSVYDGRSMCWSKGDIADGTIKVNIGSESHPREIEFSIQKSSKINLHTLSQFVNSKYSSDPQVLSSIMFLDLLLKKKPSETLFGFMHSFFTGENGVSLGGGVEAWKGFYQSIRPNQGFMSVNVDISSSAFWRNDSLLQILMEYTDCSNVRDLTRFDLKRLSRKFRFLKVTCQHRNNVGTDLANRVYSIEGFSSKSASDSFFVRRLNGEEQKISVAEYFLENHNVRLQYPNLPCILVKNGAMLPIEFCFVVKGQRYTAKLNSDQTANMIRFAVQRPFERVQQIDDFVHQMDWDTDPYLTQYGMKIQKKMLEVPARVLETPSIRYGGDCIERPVSGRWNLRGKRFLDPPRAPIRSWAVMCFTSTRRLPMRGIENFLQTYVQTLTSLGINFVMKKPPVLYADIRGSVEELCITLYKKAEQVGNAPPDYLFFILDKNSPEPYGSIKRVCNTMLGVPSQCAISKHILQSKPQYCANLGMKINVKVGGINCSLIPKSNPLGNVPTLILGGDVYHPGVGATGVSIASIVASVDLNGCKYTAVSRSQPRHQEVIEGMKDIVVYLLQGFRAMTKQQPQRIIYFRDGTSEGQFLSVINDELSQIKEACHSLSPKYNPKILVCTTQKRHHARFFIKNKSDGDRNGNPLPGTIIEKHVTHPYQYDFYLISHPSLQGVSVPVHYTVLHDEIQMPPDQFQTLCYNLCYVYARATSAVSLVPPVYYAHLVSNLARYQDVTADDTFVETSEASMDQEVKPLLALSSKLKTKMWYM O74958 MMI1_SCHPO MOD_RES 176; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 178; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 230; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 231; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 263; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 265; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 311; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 312; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC736.12c; STRAND 104..108; /evidence="ECO:0007829|PDB:6AKJ"; STRAND 339..341; /evidence="ECO:0007829|PDB:6FPQ"; STRAND 348..357; /evidence="ECO:0007829|PDB:6FPQ"; STRAND 371..375; /evidence="ECO:0007829|PDB:6FPQ"; STRAND 389..397; /evidence="ECO:0007829|PDB:6FPQ"; STRAND 403..409; /evidence="ECO:0007829|PDB:6FPQ"; STRAND 414..417; /evidence="ECO:0007829|PDB:6FPQ"; STRAND 426..440; /evidence="ECO:0007829|PDB:6FPQ" HELIX 109..111; /evidence="ECO:0007829|PDB:6AKJ"; HELIX 113..117; /evidence="ECO:0007829|PDB:6AKJ"; HELIX 321..323; /evidence="ECO:0007829|PDB:6FPQ"; HELIX 360..369; /evidence="ECO:0007829|PDB:6FPQ"; HELIX 376..386; /evidence="ECO:0007829|PDB:6FPQ"; HELIX 443..450; /evidence="ECO:0007829|PDB:6FPQ"; HELIX 466..481; /evidence="ECO:0007829|PDB:6FPQ" TURN 99..102; /evidence="ECO:0007829|PDB:6AKJ"; TURN 398..400; /evidence="ECO:0007829|PDB:6FPQ" CHAIN 1..488; /note="RNA binding exosome specificity factor Mmi1"; /id="PRO_0000372616" MSNTNFSTSRSSKSIPELPNLEALRSLWPPPSLNESGDTRSVWTTHTGEPVASSVLSTSGSNNFSSPLKRPAPESHDAPIGRRLMVDDPRLIKHGKYDFSRHCTDYGHSYEWPYFRSLRRESMLYHTSGSYPESQPPYSSYSTDAPHYYHAGSESSAYYDSRSRLHGIQPPPKRRTLSPPPRRLADPVVVGSSRYVEEEVYRRPPYTLASEVPSSASAYQAGYSSYPVRSSPQLSHEDTRHGIASSGSTRYPFVPANTRASHSPSLLEPYAHSLPSSVAPVGAYPEKSSYLLSNSSNDSASRKEKPKARASTPPPLNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIAHAKKTSIWAVKKDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWIKTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR O74966 RUXG_SCHPO SPBC4B4.05; CHAIN 1..77; /note="Small nuclear ribonucleoprotein G"; /id="PRO_0000125551" MSKAGAPDLKKYLDRQVFVQLNGSRKVYGVLRGYDIFLNIVLEDSIEEKVDGEKVKIGSVAIRGNSVIMIETLDKMT O74971 ATG5_SCHPO PTM: Conjugated to atg12; which is essential for autophagy. SPBC4B4.10c; CHAIN 1..261; /note="Autophagy protein 5"; /id="PRO_0000219008" MNVDNNKGNIPELLWNGTISVRIDYEGNSLAYLANVPRQSYFAQILPNVQRLLAPSIPLSECWLDYNGVPLKWHWPVGLLFDLLTVFDPDTPRAPVLWRIQLRSGLFPTTKILQMETMDTFRTYFFNCLKESDYVRNGSSSGIIALSKAETDTYWNAILNHDYYDFRPIAIKILFSKSKFIPLKIYLGANAPIIQTSAPLGSSLGEFLNKRLPDLFPSCDKFLIVKPVIHGITIFLQSVLDELNRDFCYIDGFLHIVLMKV O74986 COM1_SCHPO PTM: Phosphorylated by tel1 in response to DNA damage; promoting interaction with nbs1 and recruitment to DSBs. {ECO:0000269|PubMed:18378696, ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577}. MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577"; MOD_RES 78; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577"; MOD_RES 79; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:19804755"; MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577"; MOD_RES 89; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577"; MOD_RES 114; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18378696"; MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:33836577"; MOD_RES 154; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:33836577"; MOD_RES 155; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:33836577"; MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18378696" SPCC338.08; HELIX 12..55; /evidence="ECO:0007829|PDB:4X01" CHAIN 1..294; /note="DNA endonuclease ctp1"; /id="PRO_0000278499" MNEEEHNKSVHWSIVYRQLGNLLEQYEVEIARLKSQLVLEKKLRIQVEKELESVKTKQISSSASSKVSSNTIQELDSTTDEDEIPGSDTVDEEDPSLNAPFSEKNQSVKIPPHSPTLPVQNASAFVKPISVPLGNVKEEKFLDTNPIGAESFESSDGEMHLRARSPEDMILLRETQPLAPLDINTLGVSDNRQKKGTEKKRPFEPEFLNDDVIRGNKRKALPAYECPDCQKFYELHGPVKESSVAPTWNDENRLGGGSLPNCKHQPLVQKVGRHRKLNIPKPIPNGFWESDFVD O74991 POF3_SCHPO SPCC338.16; CHAIN 1..577; /note="F-box/TPR repeat protein pof3"; /id="PRO_0000106362" MNNYQVKAIKEKTQQYLSKRKFEDALTFITKTIEQEPNPTIDLFELRAQVYEKSGQYSQAELDAKRMIHLNARNARGYLRLGKLLQLDGFDKKADQLYTQGLRMVHKMDPLRPVLKKVSQRLNERILRTRPVLDLFRILPREVLLCILQQLNFKSIVQCMQVCKHWRDCIKKEPSLFCCLDFSCASPRSVNSRDRNVMAVARYSVYSKDNIQEVIGLEKLGILTPTKALLRSVKSLKVYKTISPLHTQSTDKLYTIWTPFSELHYFYCATPITFSIASKILSCCKKLKQVELVDLIPDLIFDSMDWDKLFNAESVPLALKSLTFIRNQKFPFHHKEQQFLKDLLSASPYLEYLEASYQSDLVAAIKKYKINLRSLIIIDEGVSNTVKDLAFLPQSLTTLIVKPCNPASTILCPYLFPTNVRMESLINLELFLYLRLSQNDIDNVVKFLTSCYKLKKLVLHDSLALAPHFFEIFASLPELEHLEIPDNVALQNKHAIHITDCCPNLKYVNFSNSISLDGSGFIAVLRGLKELKRIDIINCDSVSRDAIDWARSKGMQVTVASSLPNSQPLGTKKIRLI O75001 MCM7_SCHPO BINDING 366; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /ligand_note="ligand shared with MCM3"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 406; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /ligand_note="ligand shared with MCM3"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 408; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /ligand_note="ligand shared with MCM3"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 409; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /ligand_note="ligand shared with MCM3"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 410; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /ligand_note="ligand shared with MCM3"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 511; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /ligand_note="ligand shared with MCM3"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 536; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /ligand_note="ligand shared with MCM4"; /evidence="ECO:0000250|UniProtKB:P33993"; BINDING 630; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /ligand_note="ligand shared with MCM4"; /evidence="ECO:0000250|UniProtKB:P33993" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P33993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P33993}; SPBC25D12.03c; CHAIN 1..760; /note="DNA replication licensing factor mcm7"; /id="PRO_0000194123" MALPTIDLKIPEYEECQHKITDFLSHFKQEQVQDGQQNQDISMSDAGDEPFLKSKYMDILQKISNRESNVINVDLNDLYEFDPSDTQLLHNIESNAKRFVELFSQCADALMPPPTVEINYRNEVLDVIMQQRVQRNENIDPEHKGFPPELTRGYDLYFRPVTRNKKPFSVRDLRGENLGSLLTVRGIVTRTSDVKPSLTVNAYTCDRCGYEVFQEIRQKTFLPMSECPSDECKKNDAKGQLFMSTRASKFLPFQEVKIQELTNQVPIGHIPRSLTVHLYGAITRSVNPGDIVDISGIFLPTPYTGFRAMRAGLLTDTYLECHYVSQIIKNYTNIEKTPQSEAAIAELNQGGNVYEKLAKSIAPEIYGHEDVKKALLLLLVGGVTKELGDGMRIRGDINICLTGDPGVAKSQLLKYISKVAPRGVYTTGRGSSGVGLTAAVMRDPVTDEMVLEGGALVLADNGICCIDEFDKMDESDRTAIHEVMEQQTISISKAGITTTLNARTSILAAANPLYGRYNPKVAPIHNINLPAALLSRFDILFLILDTPSRETDEHLAQHVTYVHMHNEQPKMDFEPLDPNMIRHYISSARQYRPVVPKDVCDYVTGAYVQLRQNQKRDEANERQFAHTTPRTLLAILRMGQALARLRFSNRVEIGDVDEALRLMSVSKSSLYDDLDPSSHDTTITSKIYKIIRDMLNSIPDVEGNERSLTLRAIRERVLAKGFTEDHLINTIQEYTDLGVLLTTNNGQTIMFLDPDLHMEN O75011 NAK1_SCHPO ACT_SITE 133; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 16..24; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. {ECO:0000305|PubMed:18257517}. MOD_RES 541; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17F3.02; CHAIN 1..652; /note="Serine/threonine-protein kinase nak1"; /id="PRO_0000086416" MENNTASSPYTKLELVGRGSYGAVYRGICNLTKETVAIKILNLDTDEDEVSDIQKEVAVLSELKQSDVENIIKYHGSYLVGTNLWIIMDYCHGGSVRTLMEAGPISEPCISLILRETLQALKFIHHAGIIHRDIKAANILVSMSGNVKLCDFGVAAELNINRRKRITFIGTPYWMAPEVIRDGQEYNVMADIWSLGITAYEIATGSPPHAKEDPFRAVYLIAHTAPPRLNGNFSALLKEFIASCLQDVPQRRLDSSELLKSKFIKQYSRMSISELTNVVKRYDTWQAAGGIPQTLLLGEEADDGSDPDQETSDTAASDDGWEFGTIKQGQSNVSSITGTSTSTTTAATSSTTVTGTVIPKSSTVHEPPSSNDSHPLLQLFKDSKISDDDSPSNAEGASTEDSKGEVSYSQIELPSLDSSNLSSKKSTIQSKHTKQAEDYDLFVGRTRSNSKTSSDQSIKRPLPRVVQRQKTSLGKRGISMSPMKPGLRMPSSFDLQSRSISMGAFEQLSTPLEAPAHKHSAVLQPLEVNRSISIPPPKSISPSILHKPSLESASSTPKISSCSSTPKPFNSKLRAHLPPLSIGSPAVQPLANDNYDSLGVRGLNMELFNDYPGNMHNIKSVLSLEIDIVLGEMDACLKSLECNLLNRKAYNE O94235 MPS1_SCHPO ACT_SITE 442; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 322..330; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 345; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; SPBC106.01; CHAIN 1..678; /note="Serine/threonine-protein kinase mph1"; /id="PRO_0000086389" MSKRNPPVTNIADLVSDSSLDEDSLSFLEELQDPELYFKNDTFSSKSSHSDGTVTGDTLRRQSSGATALERLVSHPRTKNFDLQGNGGQNSALKEVNTPAYQSMHHFEHLITPLPSTNASHSEVSLSAGVNDLNSNSEHDLLPKSVNKTPGSLSISRRRRIGRIGLGPPKRAEYTLTDPSKTSDTKNSTEADEDIEMKSREVSPASNSVAATTLKPLQLHNTPLQTSQEHPKPSFHPSQFESSFSPRVQFDHDVERRASELHSRPVTVFQEPQRSASQPYESHALSPKVAPLFDNSQATPIPKRQQDVVTVANLQFIKLGVVGKGGSSMVYRIFSPDNSRLYALKEVNFINADQTTIQGYKNEIALLRKLSGNDRIIKLYAAEVNDTLGQLNMVMECGETDLANLLMKNMKKPINLNFIRMYWEQMLEAVQVVHDQNIVHSDLKPANFLLVEGNLKLIDFGIAKAIGNDTTNIHRDSHIGTINYMAPEALTDMNAHTNSGVKLVKLGRPSDVWSLGCILYQMVYGRAPFAHLKMIQAIAAIPNEQYHIHFPEVALPANAVQEKEGSLPGVTVGPDLMDVMKRCLERDQRKRLTIPELLVHPFLNPLPSYLTPLAKKPLPVSGHTNNAHPLRLSTEISASQLSMIIERSVELSKHKRLNKELIDSMAYDCVSNLRKMPE O94236 EIF3D_SCHPO SPAC637.07; CHAIN 1..567; /note="Eukaryotic translation initiation factor 3 subunit D"; /id="PRO_0000123524" MATGFKLPELAPVKSAWGPPETEQIGGDIPYAPFSKGDRLGKIADWSVDQPKDGREQRGRQGAFAGRFRDQYQTYGYGASSIFGYQHSEDESSFSVIDRGSVNRTRTSARNGGTLLKVRGRGQNVQRGGRGGRYGSSGGRGAGDTVVSRSSGAGGARGRRFGWKDYDKHQRLRNASVTVGDDWQLLDEVEFSHLSKLNLAAAAPVTVDSYGYIYPYDKSFDKIHVKSEKPLQALDRVHYNPTTTEDPVIQKLALNSDANIFITDSILSLLMCSTRSVYPWDIVITHQSGKLFFDKREGGPFDYLTVNENAYDSPMDADNREGVNSPGALSVEATYINQNFCVQALRETEEEKYKLPHPNPFYNSKEQSEPLAAHGYIYRDVDLSLETDEKPVKLMVRTEVDGYVKNPANDVQYISIKALNEYDPKFTNVTGSVDWRSKLESQRGAVFATEMKNNSCKLARWTVEALLAGVDSMKVGFVSRSNARDAQHHGILGVVAYKPADLASQMNLSLSNGWGIVRTIADVCLKMPDGKYVLVKDPNRPILRLYSVPPNTFEEAAGPSLEASSTA O94244 HAT2_SCHPO MOD_RES 425; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1672.10; STRAND 41..48; /evidence="ECO:0007829|PDB:6S1R"; STRAND 56..64; /evidence="ECO:0007829|PDB:6S1R"; STRAND 68..77; /evidence="ECO:0007829|PDB:6S1R"; STRAND 83..85; /evidence="ECO:0007829|PDB:6S1R"; STRAND 87..97; /evidence="ECO:0007829|PDB:6S1R"; STRAND 122..132; /evidence="ECO:0007829|PDB:6S1R"; STRAND 136..140; /evidence="ECO:0007829|PDB:6S1R"; STRAND 143..150; /evidence="ECO:0007829|PDB:6S1R"; STRAND 156..160; /evidence="ECO:0007829|PDB:6S1R"; STRAND 166..170; /evidence="ECO:0007829|PDB:6S1R"; STRAND 175..178; /evidence="ECO:0007829|PDB:6S1R"; STRAND 185..190; /evidence="ECO:0007829|PDB:6S1R"; STRAND 197..202; /evidence="ECO:0007829|PDB:6S1R"; STRAND 207..211; /evidence="ECO:0007829|PDB:6S1R"; STRAND 219..221; /evidence="ECO:0007829|PDB:6S1R"; STRAND 223..225; /evidence="ECO:0007829|PDB:6S1R"; STRAND 228..231; /evidence="ECO:0007829|PDB:6S1R"; STRAND 238..243; /evidence="ECO:0007829|PDB:6S1R"; STRAND 250..255; /evidence="ECO:0007829|PDB:6S1R"; STRAND 260..264; /evidence="ECO:0007829|PDB:6S1R"; STRAND 275..277; /evidence="ECO:0007829|PDB:6S1R"; STRAND 284..289; /evidence="ECO:0007829|PDB:6S1R"; STRAND 291..293; /evidence="ECO:0007829|PDB:6S1L"; STRAND 294..301; /evidence="ECO:0007829|PDB:6S1R"; STRAND 306..310; /evidence="ECO:0007829|PDB:6S1R"; STRAND 316..321; /evidence="ECO:0007829|PDB:6S1R"; STRAND 328..333; /evidence="ECO:0007829|PDB:6S1R"; STRAND 340..345; /evidence="ECO:0007829|PDB:6S1R"; STRAND 350..354; /evidence="ECO:0007829|PDB:6S1R"; STRAND 374..378; /evidence="ECO:0007829|PDB:6S1R"; STRAND 385..390; /evidence="ECO:0007829|PDB:6S1R"; STRAND 394..396; /evidence="ECO:0007829|PDB:6S29"; STRAND 398..402; /evidence="ECO:0007829|PDB:6S1R"; STRAND 405..412; /evidence="ECO:0007829|PDB:6S1R" HELIX 13..40; /evidence="ECO:0007829|PDB:6S1R"; HELIX 152..154; /evidence="ECO:0007829|PDB:6S1R"; HELIX 161..163; /evidence="ECO:0007829|PDB:6S1L"; HELIX 214..216; /evidence="ECO:0007829|PDB:6S1R"; HELIX 355..357; /evidence="ECO:0007829|PDB:6S1R"; HELIX 364..369; /evidence="ECO:0007829|PDB:6S1R"; HELIX 414..417; /evidence="ECO:0007829|PDB:6S1R" TURN 101..103; /evidence="ECO:0007829|PDB:6S29"; TURN 418..420; /evidence="ECO:0007829|PDB:6S1L" CHAIN 1..430; /note="Histone acetyltransferase type B subunit 2"; /id="PRO_0000227743" MSEEVVQDAPLENNELNAEIDLQKTIQEEYKLWKQNVPFLYDLVITHALEWPSLTIQWLPDKKTIPGTDYSIQRLILGTHTSGNDQNYLQIASVQLPNFDEDTTEFTPSTIRRAQATGSYTIEISQKIPHDGDVNRARYMPQKPEIIATMGEGGNAYIFDTTCHDALTTGEALPQAVLKGHTAEGFGLCWNPNLPGNLATGAEDQVICLWDVQTQSFTSSETKVISPIAKYHRHTDIVNDVQFHPQHEALLASVSDDCTLQIHDTRLNPEEEAPKVIQAHSKAINAVAINPFNDYLLATASADKTVALWDLRNPYQRLHTLEGHEDEVYGLEWSPHDEPILASSSTDRRVCIWDLEKIGEEQTPEDAEDGSPELLFMHGGHTNRISEFSWCPNERWVVGSLADDNILQIWSPSRVIWGRDHVQVSPRDLE O94267 SPT16_SCHPO MOD_RES 444; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 445; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP8B7.19; STRAND 36..42; /evidence="ECO:0007829|PDB:3CB6"; STRAND 67..74; /evidence="ECO:0007829|PDB:3CB6"; STRAND 77..83; /evidence="ECO:0007829|PDB:3CB6"; STRAND 100..108; /evidence="ECO:0007829|PDB:3CB6"; STRAND 131..135; /evidence="ECO:0007829|PDB:3CB6"; STRAND 160..164; /evidence="ECO:0007829|PDB:3CB6"; STRAND 247..251; /evidence="ECO:0007829|PDB:3CB6"; STRAND 254..256; /evidence="ECO:0007829|PDB:3CB6"; STRAND 271..273; /evidence="ECO:0007829|PDB:3CB6"; STRAND 276..283; /evidence="ECO:0007829|PDB:3CB6"; STRAND 285..287; /evidence="ECO:0007829|PDB:3CB6"; STRAND 294..301; /evidence="ECO:0007829|PDB:3CB6"; STRAND 357..359; /evidence="ECO:0007829|PDB:3CB6"; STRAND 361..364; /evidence="ECO:0007829|PDB:3CB6"; STRAND 384..395; /evidence="ECO:0007829|PDB:3CB6"; STRAND 405..416; /evidence="ECO:0007829|PDB:3CB6"; STRAND 419..421; /evidence="ECO:0007829|PDB:3CB6" HELIX 8..23; /evidence="ECO:0007829|PDB:3CB6"; HELIX 25..30; /evidence="ECO:0007829|PDB:3CB6"; HELIX 53..62; /evidence="ECO:0007829|PDB:3CB6"; HELIX 84..87; /evidence="ECO:0007829|PDB:3CB6"; HELIX 91..94; /evidence="ECO:0007829|PDB:3CB6"; HELIX 112..127; /evidence="ECO:0007829|PDB:3CB6"; HELIX 144..153; /evidence="ECO:0007829|PDB:3CB6"; HELIX 157..159; /evidence="ECO:0007829|PDB:3CB6"; HELIX 166..174; /evidence="ECO:0007829|PDB:3CB6"; HELIX 178..197; /evidence="ECO:0007829|PDB:3CB6"; HELIX 199..209; /evidence="ECO:0007829|PDB:3CB6"; HELIX 215..223; /evidence="ECO:0007829|PDB:3CB6"; HELIX 224..227; /evidence="ECO:0007829|PDB:3CB6"; HELIX 229..232; /evidence="ECO:0007829|PDB:3CB6"; HELIX 235..237; /evidence="ECO:0007829|PDB:3CB6"; HELIX 244..246; /evidence="ECO:0007829|PDB:3CB6"; HELIX 304..323; /evidence="ECO:0007829|PDB:3CB6"; HELIX 330..344; /evidence="ECO:0007829|PDB:3CB6"; HELIX 346..351; /evidence="ECO:0007829|PDB:3CB6"; HELIX 367..369; /evidence="ECO:0007829|PDB:3CB6"; HELIX 432..435; /evidence="ECO:0007829|PDB:3CB6" TURN 88..90; /evidence="ECO:0007829|PDB:3CB6"; TURN 128..130; /evidence="ECO:0007829|PDB:3CB6"; TURN 154..156; /evidence="ECO:0007829|PDB:3CB6" CHAIN 1..1019; /note="FACT complex subunit spt16"; /id="PRO_0000245188" MAEYEIDEITFHKRLGILLTSWKNEEDGKTLFQDCDSILVTVGAHDDTNPYQKSTALHTWLLGYEFPSTLILLEKHRITILTSVNKANMLTKLAETKGAAADVNILKRTKDAEENKKLFEKIIEYIRATNKKVGVFPKDKTQGKFINEWDSIFEPVKSEFNLVDASLGLAKCLAIKDEQELANIKGASRVSVAVMSKYFVDELSTYIDQGKKITHSKFSDQMESLIDNEAFFQTKSLKLGDIDLDQLEWCYTPIIQSGGSYDLKPSAITDDRNLHGDVVLCSLGFRYKSYCSNVGRTYLFDPDSEQQKNYSFLVALQKKLFEYCRDGAVIGDIYTKILGLIRAKRPDLEPNFVRNLGAGIGIEFRESSLLVNAKNPRVLQAGMTLNLSIGFGNLINPHPKNSQSKEYALLLIDTIQITRSDPIVFTDSPKAQGDISYFFGEDDSSLEDGVKPRKPPTRGTATISSHKGKTRSETRDLDDSAEKRRVEHQKQLASRKQAEGLQRFAQGSVPSSGIEKPTVKRFESYKRDSQLPQAIGELRILVDYRAQSIILPIFGRPVPFHISTLKNASKNDEGNFVYLRLNFVSPGQIGGKKDELPFEDPNAQFIRSFTFRSSNNSRMSQVFKDIQDMKKAATKRETERKEFADVIEQDKLIEIKNKRPAHINDVYVRPAIDGKRLPGFIEIHQNGIRYQSPLRSDSHIDLLFSNMKHLFFQPCEGELIVLIHVHLKAPIMVGKRKTQDVQFYREVSDIQFDETGNKKRKYMYGDEDELEQEQEERRRRAQLDREFKSFAEKIAEASEGRIELDIPFRELAFNGVPFRSNVLLQPTTDCLVQLTDTPFTVITLNEIEIAHLERVQFGLKNFDLVFIFQDFRRPPIHINTIPMEQLDNVKEWLDSCDICFYEGPLNLNWTTIMKTVNEDPIAFFEEGGWGFLGAPSDDEGDDSVEEVSEYEASDADPSDEEEEESEEYSEDASEEDGYSESEVEDEESGEDWDELERKARQEDAKHDAFEERPSKKRHR O94272 ATG8_SCHPO PTM: The C-terminal 5 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. {ECO:0000250|UniProtKB:P38182}. SPBP8B7.24c; STRAND 28..35; /evidence="ECO:0007829|PDB:6AAF"; STRAND 48..52; /evidence="ECO:0007829|PDB:6AAF"; STRAND 77..80; /evidence="ECO:0007829|PDB:6AAF"; STRAND 105..111; /evidence="ECO:0007829|PDB:6AAF" HELIX 4..8; /evidence="ECO:0007829|PDB:6AAF"; HELIX 11..24; /evidence="ECO:0007829|PDB:6AAF"; HELIX 57..68; /evidence="ECO:0007829|PDB:6AAF"; HELIX 91..98; /evidence="ECO:0007829|PDB:6AAF" PROPEP 117..121; /note="Removed in mature form"; /evidence="ECO:0000250|UniProtKB:P38182"; /id="PRO_0000017237" CHAIN 1..116; /note="Autophagy-related protein 8"; /id="PRO_0000017236" LIPID 116; /note="Phosphatidylethanolamine amidated glycine"; /evidence="ECO:0000250|UniProtKB:P38182" MRSQFKDDFSFEKRKTESQRIREKYPDRIPVICEKVDKSDIAAIDKKKYLVPSDLTVGQFVYVIRKRIKLSPEKAIFIFIDEILPPTAALMSTIYEEHKSEDGFLYITYSGENTFGTVFPF O94276 YORS_SCHPO SPBP8B7.28c; STRAND 39..41; /evidence="ECO:0007829|PDB:2LUY"; STRAND 43..45; /evidence="ECO:0007829|PDB:2LUY"; STRAND 48..50; /evidence="ECO:0007829|PDB:2LUY"; STRAND 63..66; /evidence="ECO:0007829|PDB:2LUY"; STRAND 69..72; /evidence="ECO:0007829|PDB:2LUY"; STRAND 90..92; /evidence="ECO:0007829|PDB:2LUY"; STRAND 94..96; /evidence="ECO:0007829|PDB:2LUY"; STRAND 99..102; /evidence="ECO:0007829|PDB:2LUY"; STRAND 112..114; /evidence="ECO:0007829|PDB:2LUY" HELIX 35..37; /evidence="ECO:0007829|PDB:2LUY"; HELIX 56..60; /evidence="ECO:0007829|PDB:2LUY"; HELIX 107..111; /evidence="ECO:0007829|PDB:2LUY"; HELIX 118..121; /evidence="ECO:0007829|PDB:2LUY" TURN 51..53; /evidence="ECO:0007829|PDB:2LUY"; TURN 81..83; /evidence="ECO:0007829|PDB:2LUY" CHAIN 1..215; /note="Meiotic chromosome segregation protein P8B7.28c"; /id="PRO_0000352818" MDFKSRKYKIKKHPKDCKLHAKKYRGTLNSKGKNDNDCLIMCMRCRKVKGIDSYSKTQWSKTFTFVRGRTVSVSDPKVICRTCQPKQHDSIWCTACQQTKGINEFSKAQRHVLDPRCQICVHSQRNDGDDNLESDKFVDPFIGDDSDLDDDIYIHDKQTINSEYADDVSDNTDEERTESKGQQESNSAEEYDDDDSDEDRMEEIFQQFKKEKQIV O94282 CTU1_SCHPO SPBC2G5.03; CHAIN 1..335; /note="Cytoplasmic tRNA 2-thiolation protein 1"; /id="PRO_0000316593" MSNKLCQLCNERRPALVRPKTGQKICKECFYYVFETEIHNVIIENKLFVRGERVGIGASGGKDSTVLAYVMKLLNERYDYGLELYLISVDEGIRGYRDDSLDTVKRNQQQYGLPMKIVSYADLYDGWTMDNVVARIGTKNNCTYCGVFRRQALDRAALSLDIHHLVTGHNADDIAETILMNLLRGDVARLPRSTEITTQSDSSPTKRSKPFKYSYEKEIVLYAHYKKLDYFSTECTYSPEAFRGTARAMIKQLENIRPSSILDIIYSGESMQLASSVQEQLPQQTTCERCGFISSNRICKACMLLEGLNKGITGLGLGSDRKTKKLQSQIPACAE O94284 HMT2_SCHPO ACT_SITE 204; /note="Cysteine persulfide intermediate"; /evidence="ECO:0000250|UniProtKB:Q7ZAG8"; ACT_SITE 383; /note="Cysteine persulfide intermediate"; /evidence="ECO:0000250|UniProtKB:Q7ZAG8" BINDING 35..39; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:O67931" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10224084}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10224084}; TRANSIT 1..24; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC2G5.06c; CHAIN 25..459; /note="Sulfide:quinone oxidoreductase, mitochondrial"; /id="PRO_0000021446" MLTLNSTIKSVTGSFQSASMLARFASTHHKVLVVGGGSAGISVAHQIYNKFSKYRFANDQGKDTSLKPGEIGIVDGAKYHYYQPGWTLTGAGLSSVAKTRRELASLVPADKFKLHPEFVKSLHPRENKIVTQSGQEISYDYLVMAAGIYTDFGRIKGLTEALDDPNTPVVTIYSEKYADAVYPWIEKTKSGNAIFTQPSGVLKCAGAPQKIMWMAEDYWRRHKVRSNIDVSFYTGMPTLFSVKRYSDALLRQNEQLHRNVKINYKDELVEVKGSERKAVFKNLNDGSLFERPFDLLHAVPSMRSHEFIAKSDLADKSGFVAVDQSTTQSTKFPNVFAIGDCSGLPTSKTYAAITAQAPVMVHNLWSFVNGKNLTASYNGYTSCPLLTGYGKLILAEFLYKQEPKESFGRFSRFLDQTVPRRMFYHLKKDFFPFVYWNFAVRNGKWYGSRGLIPPHFPVN O94296 ATC3_SCHPO ACT_SITE 518; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0" BINDING 518; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 518; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 519; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 520; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 520; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 613; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 654; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 656; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P32660"; BINDING 659; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 677; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 710; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 711; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 790; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 791; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 792; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 883; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 889; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 909; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 912; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 913; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 913; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q8NB49"; BINDING 1103; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 1173; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 1177; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 1178; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 1189; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 1190; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250|UniProtKB:P39524" CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P39524}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; SPBC887.12; CHAIN 1..1258; /note="Phospholipid-transporting ATPase C887.12"; /id="PRO_0000314112" MARDVDNKQNAKRISRDEDEDEFAGESMVGRTLDNPFLGEDEFEDIFGSESQYISSSGQNSTNPFLADTRIENSPLGSESKANQLNKQGTNVNHIEIPLRDFNDPTQPESFLPPPKNTFTSRIKKIKNLFKKEKKQVKPEDLGPRQIILNDYSANHFLHNAVSTCKYSAFTFLPKFLKEQFSKYANLFFLFTAVVQQIPGITPVNRYTTIGPMLIVLSVSGIKEIMEDIKRKKQDQELNESPCYVLQGTGFVEKQWKDVVVGDIVKIVSETFFPADLVLLSSSEPEGLCYIETANLDGETNLKIKQALPETAGLLKPVELGQLSGEVKSEQPNNNLYTFDATLKLLPSDRELPLSPDQLLLRGAQLRNTPWVYGIVVFTGHESKLMKNTTETPIKRTSVEKQVNSQILFLLCIFVFLCFASSLGALIHRSVYGSALSYVKYTSNRAGMFFKGLLTFWILYSNLVPISLFVTFELVRYIQAQLISSDLDMYNEETDTPAACRTSSLVEELGQVGYIFSDKTGTLTRNQMEFRQCTIAGVAYADVIPEDRQFTSEDLDSDMYIYDFDTLKENLKHSENASLIHQFLLVLSICHTVIPEYDESTNSIKYQASSPDEGALVKGAASIGYKFLARKPHLVTVSIFGKDESYELLHICEFNSTRKRMSIVFRCPDGKIRLYVKGADTVIMERLASDNPYLQTTIHHLEDYATVGLRTLCIAMREVPEDEYQRWSTVFETAASSLVDRAQKLMDAAEEIEKDLILLGATAIEDRLQDGVPDTISTLQTAGIKIWVLTGDRQETAINIGMSCKLIDEDMGLVIVNEETKEATAESVMAKLSSIYRNEATTGNVESMALVIDGVSLTYALDFSLERRFFELASLCRAVICCRVSPLQKALIVKMVKRNTGEVLLAIGDGANDVPMIQAAHVGVGISGMEGLQAVRSSDFSISQFCYLKKLLLVHGSWCYQRLSKLILYSFYKNIALYMTQFWYAFCNAFSGQVIFESWSISLYNVLFTVLPPVVIGIFDQFVSAGQLFQYPQLYQLGQRSEFFNLKRFWSWITNGFYHSLLLFLCSIAVFYYDGPNKDGLASGHWVWGTTLYAAILATVLGKAALISNHWTQYTVIATLGSFLLWIVFMPIYAVAAPAIGFSKEYYGIIPHLYGNLKFWASLLVLPTIALMRDFVWKYSSRMYYPEEYHYVQEIQKYNVTDYRPRIVGFHKAIRKIRQMQRMRKQRGYAFSQGEEDQSRILDAYDTTHTRGAYGEMR O94313 CARB_SCHPO BINDING 208; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 248; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 254; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 255; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 285; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 287; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 292; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 318; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 319; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 320; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 361; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 361; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 361; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 375; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 375; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 375; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 375; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 375; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 377; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 377; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 784; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 823; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 825; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 830; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 855; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 856; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 857; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 858; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 898; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 898; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 898; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 917; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 917; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 917; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 917; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 917; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 919; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 919; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:Q7SH52}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial]: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:Q7SH52}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; SPBC215.08c; CHAIN 1..1160; /note="Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial"; /id="PRO_0000145089" MALWATSMRRAIPGISKAFLGSNRVLETAGVSQLSKHLLPQWSGVPHRKISASATNFNDKVKESNTPDANAYIRSGHIKAAEHEKVKKVVVVGSGGLSIGQAGEFDYSGAQAIKALRESSVHTILINPNIATIQSSHSLADEIYFLPVTAEYLTHLIERENPDGILLTFGGQTALNVGIQLDDMGVFARNHVKVLGTPISTLKTSEDRDLFAKALNEINIPIAESVAVSTVDEALQAAEKVSYPVIIRSAYSLGGLGSGFANNKEELQSMAAKSLSLTPQILVEKSLKGWKEVEYEVVRDAANNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEEYHMLRTAAIKIIRHLGVVGECNVQYALSPNSLEYRVIEVNARLSRSSALASKATGYPLAYTAAKIALGHTLPELPNAVTKTTTANFEPSLDYVVTKIPRWDLSKFQYVNREIGSSMKSVGEVMAVGRTFEESLQKALRQVDPSFLGFMAMPFKDLDNALSVPTDRRFFAVVEAMLNQGYSIDKIHDLTKIDKWFLSKLANMAKVYKELEEIGSLYGLNKEIMLRAKKTGFSDLQISKLVGASELDVRARRKRLDVHPWVKKIDTLAAEFPAHTNYLYTSYNASSHDIDFNEHGTMVLGSGVYRIGSSVEFDWCGVSCARTLRKLGHSTIMVNYNPETVSTDFDECERLYFEELSYERVMDIYEMETASGIVVSVGGQLPQNIALKLQETGAKVLGTDPLMIDSAEDRHKFSQILDKIGVDQPAWKELTSVAEASKFANAVGYPVLVRPSYVLSGAAMSVIRDESSLKDKLENASAVSPDHPVVITKFIEGARELDVDAVASKGKLLVHAVSEHVENAGVHSGDATIALPPYSLSEDILSRCKEIAEKVCKAFQITGPYNMQIILAQNPDKPDTPDLKVIECNLRASRSFPFVSKTLGVNFIDVATRSIIDQEVPAARDLMAVHRDYVCVKVPQFSWTRLAGADPYLGVEMSSTGEVACFGKDVKEAYWAALQSTQNFKIPLPGQGILLGGDRPELAGIAADLSKLGYKLYVANKDAAKLLQPTSAEVVEFPVKDKRALRAIFEKYNIRSVFNLASARGKNVLDQDYVMRRNAVDFNVTLINDVNCAKLFVESLKEKLPSVLSEKKEMPSEVKRWSEWIGSHDL O94316 SN114_SCHPO BINDING 148..155; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 216..220; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 270..273; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPBC215.12; CHAIN 1..984; /note="Pre-mRNA-splicing factor cwf10"; /id="PRO_0000363370" MMEEDLYDEFGNYIGPENEEDEEELFPQAPSPTIAQVPSFEEVIPDEELEDVERAEEMALSHLEPQNAVVLHEDKQYYPSAEEVYGSNVDIMVQEQDTQPLSQPIIEPIRHKRIAIETTNVPDTVYKKEFLFGLLTGTDDVRSFIVAGHLHHGKSALLDLLVYYTHPDTKPPKRRSLRYTDTHYLERERVMSIKSTPLTLAVSDMKGKTFAFQCIDTPGHVDFVDEVAAPMAISDGVVLVVDVIEGVMINTTRIIKHAILHDMPIVLVLNKVDRLILELRLPPNDAYHKLRHVIDEVNDNICQISKDLKYRVSPELGNVCFASCDLGYCFTLSSFAKLYIDRHGGIDVDLFSKRLWGDIYFDSKTRKFAKQSLDGSGVRSFVHFILEPLYKLHTLTISDEAEKLKKHLSSFQIYLKPKDYLLDPKPLLQLICASFFGFPVGFVNAVTRHIPSPRENAARKASQSYIGPINSSIGKAILEMSREESAPLVMHVTKLYNTVDANNFYAFARVYSGQVKKGQKVKVLGENYSLEDEEDMVVAHIAEICVPCARYRLHVDGAVAGMLVLLGGVDNSISKTATIVSDNLKDDPYIFRPIAHMSESVFKVAVEPHNPSELPKLLDGLRKTNKSYPLSITKVEESGEHTIFGTGEMYMDCLLYDLRTLYSEIEIRVSDPVARFCETAVDTSSIKCFSDTPNKKNRITMVVEPLEKGISNDIENGKVNINWPQKRISEFFQKNYDWDLLASRSIWAFGPDDRGTNILRDDTLSTDVDKNVLNSVKEYIKQGFQWGTREGPLCDETIRNVNFRLMDVVLAPEQIYRGGGQIIPTARRVCYSSFLTASPRLMEPVYMVEVHAPADSLPIIYDLLTRRRGHVLQDIPRPGSPLYLVRALIPVIDSCGFETDLRVHTQGQAMCQMVFDHWQVVPGDPLDKSIKPKPLEPARGSDLARDFLIKTRRRKGLVEDVSTTRYFDQEMIDSLKEAGVVLSL O94326 PIR2_SCHPO MOD_RES 28; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 30; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC725.08; STRAND 223..229; /evidence="ECO:0007829|PDB:7QY5"; STRAND 248..253; /evidence="ECO:0007829|PDB:7QY5"; STRAND 264..270; /evidence="ECO:0007829|PDB:7QY5"; STRAND 287..289; /evidence="ECO:0007829|PDB:7QY5"; STRAND 308..310; /evidence="ECO:0007829|PDB:7QY5"; STRAND 409..411; /evidence="ECO:0007829|PDB:7QY5"; STRAND 466..468; /evidence="ECO:0007829|PDB:7QY5"; STRAND 470..472; /evidence="ECO:0007829|PDB:7QY5"; STRAND 474..476; /evidence="ECO:0007829|PDB:7QY5"; STRAND 478..480; /evidence="ECO:0007829|PDB:7QY5"; STRAND 484..487; /evidence="ECO:0007829|PDB:7QY5" HELIX 72..74; /evidence="ECO:0007829|PDB:7QY5"; HELIX 81..91; /evidence="ECO:0007829|PDB:7QY5"; HELIX 106..128; /evidence="ECO:0007829|PDB:7QY5"; HELIX 132..138; /evidence="ECO:0007829|PDB:7QY5"; HELIX 142..144; /evidence="ECO:0007829|PDB:7QY5"; HELIX 152..170; /evidence="ECO:0007829|PDB:7QY5"; HELIX 210..220; /evidence="ECO:0007829|PDB:7QY5"; HELIX 235..243; /evidence="ECO:0007829|PDB:7QY5"; HELIX 278..283; /evidence="ECO:0007829|PDB:7QY5"; HELIX 312..314; /evidence="ECO:0007829|PDB:7QY5"; HELIX 317..337; /evidence="ECO:0007829|PDB:7QY5"; HELIX 344..354; /evidence="ECO:0007829|PDB:7QY5"; HELIX 368..383; /evidence="ECO:0007829|PDB:7QY5"; HELIX 398..401; /evidence="ECO:0007829|PDB:7QY5"; HELIX 422..439; /evidence="ECO:0007829|PDB:7QY5"; HELIX 441..443; /evidence="ECO:0007829|PDB:7QY5"; HELIX 447..449; /evidence="ECO:0007829|PDB:7QY5"; HELIX 454..465; /evidence="ECO:0007829|PDB:7QY5"; HELIX 488..497; /evidence="ECO:0007829|PDB:7QY5"; HELIX 500..517; /evidence="ECO:0007829|PDB:7QY5"; HELIX 526..528; /evidence="ECO:0007829|PDB:7QY5" TURN 99..105; /evidence="ECO:0007829|PDB:7QY5"; TURN 171..175; /evidence="ECO:0007829|PDB:7QY5"; TURN 258..260; /evidence="ECO:0007829|PDB:7QY5"; TURN 389..392; /evidence="ECO:0007829|PDB:7QY5"; TURN 402..404; /evidence="ECO:0007829|PDB:7QY5" CHAIN 1..609; /note="NURS complex subunit pir2"; /id="PRO_0000352817" MSEVHQESEVEYSRWKRERSPERSQRRSQSPPGEQSAYHRERSPLRKRGNYYDDRTRASGPYPTFTKPLIDPYTQTNAVSYERFIRWYSKENHISATTEDLYNSLHGTYNNYKQDLYARTARSFVESHCDEAWFEDSYWVDESQGRVLEVSENEKSYRRALYDKFMDRLDAGYYDDFQLPTAEDVIEKPSIPDNDTDDSILPSNDPQLSKWNQDSRNDAMENTLLVSHVLPNISVAQIHNALDGISFVQHFSLSTINLIKNDERSLWVHFKAGTNMDGAKEAVDGIQLDSNFTIESENPKIPTHTHPIPIFEIASSEQTCKNLLEKLIRFIDRASTKYSLPNDAAQRIEDRLKTHASMKDDDDKPTNFHDIRLSDLYAEYLRQVATFDFWTSKEYESLIALLQDSPAGYSRKKFNPSKEVGQEENIWLSDLENNFACLLEPENVDIKAKGALPVEDFINNELDSVIMKEDEQKYRCHVGTCAKLFLGPEFVRKHINKKHKDWLDHIKKVAICLYGYVLDPCRAMDPKVVSTSYVSLQILNKPYVGFRNINANYTFPTTSYSRRNDEEITSGASSQKSYSRQEPMIHRREFYRTYQDLDAPNQEVPELDY O94360 MOB1_SCHPO SPBC428.13c; CHAIN 1..210; /note="Maintenance of ploidy protein mob1"; /id="PRO_0000193580" MFGFSNKTAKTFRVRKTEAGTKHYQLRQYAEATLGSGSLMEAVKLPKGEDLNEWIAMNTMDFYTQINMLYGTITEFCTAASCPQMNAGPSYEYYWQDDKIYTKPTRMSAPDYINNLLDWTQEKLDDKKLFPTEIGVEFPKNFRKVIQQIFRRLFRIYAHIYCSHFHVMVAMELESYLNTSFKHFVFFCREFGLMDNKEYAPMQDLVDSMV O94363 RHB1_SCHPO BINDING 16; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 18; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 19; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 20; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 20; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 21; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 32; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 35; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 38; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 38; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 119; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 122; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382"; BINDING 150; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q15382" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q15382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:Q15382}; MOD_RES 182; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPBC428.16c; PROPEP 183..185; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281369" CHAIN 1..182; /note="GTP-binding protein rhb1"; /id="PRO_0000082712" LIPID 182; /note="S-farnesyl cysteine"; /evidence="ECO:0000250" MAPIKSRRIAVLGSRSVGKSSLTVQYVENHFVESYYPTIENTFSKNIKYKGQEFATEIIDTAGQDEYSILNSKHSIGIHGYVLVYSITSKSSFEMVKIVRDKILNHTGTEWVPIVVVGNKSDLHMQRAVTAEEGKALANEWKCAWTEASARHNENVARAFELIISEIEKQANPSPPGDGKGCVIA O94374 IMA2_SCHPO SPBC1604.08c; CHAIN 1..539; /note="Importin subunit alpha-2"; /id="PRO_0000290665" MESRYLSDRRSRFKSKGVFKADELRRQREEQQIEIRKQKREESLNKRRNLNAVLQNDIDVEEEADQSQVQMEQQMKDEFPKLTADVMSDDIELQLGAVTKFRKYLSKETHPPIDQVIACGVVDRFVQFLESEHHLLQFEAAWALTNIASGTTDQTRIVVDSGAVPRFIQLLSSPEKDVREQVVWALGNIAGDSSACRDYVLGNGVLQPLLNILQSSASDVSMLRNATWTLSNLCRGKNPPPNWSTISVAVPILAKLLYSEDVEIIVDACWAISYLSDGPNEKIGAILDVGCAPRLVELLSSPSVNIQTPALRSVGNIVTGTDAQTQIIIDCGALNAFPSLLSHQKENIRKEACWTISNITAGNTQQIQAIIESNLIPPLVHLLSYADYKTKKEACWAISNATSGGLGQPDQIRYLVSQGVIKPLCDMLNGSDNKIIQVALDAIENILKVGEMDRTMDLENINQYAVYVEEAGGMDMIHDLQSSGNNDIYLKAYSIIEKYFSDEDAVEDLAPETENGAFTFGNGPQAQGEFKFDSQDMAM O94383 SMC1_SCHPO BINDING 32..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305" SPBC29A10.04; CHAIN 1..1228; /note="Structural maintenance of chromosomes protein 1"; /id="PRO_0000119010" MGRLLRLEVENFKSYRGHQIIGPFEDFTSIIGPNGAGKSNLMDAISFVLGVKSSHLRSTNVKELIYRGKILQRDNTDFTDSSNPTTAYVKLMYELDNGEQREYKRAITPSGATEYKIDEEIVTFSEYCGSLQKENILVRARNFLVFQGDVETIASQSPLELSKLVEQISGSLEYKSEYDKSKDEQDKAVNLSAHSFNKKRGINAELRQYQEQKTEAERYQSQKEKRDSAQLVYLLWKLFHLEKSISSNMAEVTRLKADSIQLIERRDENTKEIEKLKEKEGSIRRNLLAFDRKVRKQEKLIASKRPELISIAEKALESKSNLRKIQRKAAEIEKDYSDQASTLQVLENQLTSLSAAEKEFLKDMQEKEQLKGLRLLPEDKEEYEGLRSEADKLNSNLLFKLQTLNRNIKVTSQSKDSLTSIVGDLESKIKSLHESVSSLDTERADLLAKINEKIESLELEKHDQQKKRLTYSELFHKTQELNEELQSCLQKILEASADRNESKQDAKKREALYALKRIYPEVKGRIIDLCTPTQKKYESAIAAALGKNFDAIVVETQAVAKECIDYIKEQRIGIMTFFPMDTIAASPVNQKFRGTHKGARLAIDVLNFESEYERVMISAVGNTLICDSMTVARDLSYNKRLNAKTVTLEGTVIHKTGLITGGSSNNRSAKHWDDHDFDLLTQTKDRLMHQIGEIEYQKSSCVITESDTVKLHSLESEISLLKDKYTVVSRSVEDKKKEIGHYESLIKEKQPHLSELEMELRNFVKSRDELQIQVEKVEEKIFSGFCKRIGISDIHTYDEIHRTFTQSFTQKQLEFTKQKSLLENRISFEKQRVSDTRLRLERMHKFIEKDQESIDNYEQNREALESEVATAEAELELLKEDFASENSKTEKILLAASEKKLVGKRLVSELTKLSGNITLLESEIDRYVSEWHAILRKCKLEDIDVPLREGSLTSIPIDDVSNSGDITMGEEPSEPVINFEKFGVEVDYDELDEELRNDGSESMASVLQEKLREYSEELDQMSPNLRAIERLETVETRLAKLDEEFAAARKAAKNAKERFNAVKQKRLQKFQAAFSHISEQIDPIYKELTKSPAFPLGGTAYLTLDDLDEPYLGGIKFHAMPPMKRFRDMDQLSGGEKTMAALALLFAIHSYQPSPFFVLDEIDAALDQTNVTKIANYIRQHASSGFQFVVISLKNQLFSKSEALVGIYRDQQENSSRTLSINLEGYVE O94395 KU70_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPCC126.02c; CHAIN 1..607; /note="ATP-dependent DNA helicase II subunit 1"; /id="PRO_0000255455" MENDEQIDETENFAIGKYAILFVIEVSPSMLDPVDEFTPSSLQMALICAYQLAAQRVITNPSDIMGVLLYGTESSTGRFANQMMLLDIDPPDAERIKSLQSFEKDFQFSKEKFKPCSCQVSLSSVLYHCSVIFTTKAENFEKRLFLITDNDHPAWDATERDIILQRAKDLRDLDIQVHPVFLDPPTHSFRINIFYSDFLYIVYGRQDVSNLVNRGQAQLQHMLNMITALQKPKRAHFHLKMDLGNDVRIGVEAFILLKRLESAKTNWVYAKGERFAVAVPQSKQVSFATKKELKKDEIRRSYSYGGSSVVFGSDELNKVRSFEPPTLRIIGFRDFSTLKPWHCLKPAVFLRPKDDEIIGSGAVFSAIHKKLLASNKIGIAWFVSRPNANPCFVAMLATPGSIHIRDDFELPLGIFLVQLPTADDIRSLPPINPNPISMPSNLIETMQRILRGMELRSYQPGKYNNPSLQWHYKVLQALALDEEIPTDFVDNTLPKYKAIQKRVGEYMGDVNNIVAEYRNDISDKNGIKEEEEDQGPIVKKARIEKSGKPIFAEDDRLKQLYIEGVLDKEIKALKVSQLKDILRDRGLRVSGKKADLLDNLTNYVKKL O94396 PUS1_SCHPO ACT_SITE 103; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P07649" CATALYTIC ACTIVITY: Reaction=a uridine in tRNA = a pseudouridine in tRNA; Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000269|PubMed:11095668}; CATALYTIC ACTIVITY: Reaction=uridine in snRNA = pseudouridine in snRNA; Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q12211}; CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q12211}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q12211}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q12211}; MOD_RES 518; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 519; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 525; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC126.03; CHAIN 1..534; /note="tRNA pseudouridine synthase 1"; /id="PRO_0000057528" MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADRLSVIRETLNQYVGVHNFHNFTVGQAFHQKNSNRVIRSFTASDPFMIGDTEWISCKVHGQSFMLHQIRKMIALAILVVRTGCPVERIQDAFKKTKINIPKGPGFGLLLESPFFKGYNEHKAPENNRDPIDFTKYEQKITAFKHAHIYDKIFLEEARKQVFHCFLSFIDSYNEEDFSYLSDIGITEKTQEVSSKLPDVLSSDEEEDSAENKDDLEG O94421 SNF22_SCHPO BINDING 894..901; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPCC1620.14c; CHAIN 1..1680; /note="SWI/SNF chromatin-remodeling complex subunit snf22"; /id="PRO_0000074360" MFAVQGNQKFPKGLTKDNIQSLYQQWQVMRNQGATEENNPEFAQISSILRMVQRAHYARMQQMRNQSSEFPDAENTNLRKQQDTLPTTGFNNLPEGKAGMQTLPGRPASNGPTPPNPGNGNVGLNNPSYMNSQASPNIMNAPLQRDTSVPPAPSMVHPHTNTNANSNNLKVYANQLSQQNTSNPTYHNAYDMASMMKNGSRMNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYNGYQNDAASFAHSKLPSSANPNTPFNSTATVDVGAAGSHFPYPQPSNLDAINAKTYFQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPRMSPSPSASALKTQSHVPSAKVPPTSKLNHAQLAMLKSQIVAYNCLNSPNGQVPPAVQQAIFGRVYGASNEVSPSMPFQQNVPQMSSVKKDTPTRDANMRTSKAPYIQNIPNQFQRRAYSATIPVKNESLAKPSVSPMPLQQSTGKTEVAKRAQFPTNVNYSSCVDPRTYVKTPIPFSKFSSSENLSLIPSLLPPSISWDDVFLSSEIAIACSIANRIDFLEKENRPKSVNKKILQQDKSKSMIELRCLRLLEKQRSLRETINSVIPHSDSLAAGNLRLMFRNVKRQTMQEANLVLALAEKQKTEHAMRQKEKLLTHLRSIMLHRKSIVTKVDKQNKAKTQRCKDIINFHAHLEKEEKKRIERSARQRLQALRADDEAAYLQLLDKAKDTRITHLLKQTDQYLENLTRAVRIQQSNIHSGNTSGKGSNSAELEAPISEEDKNLDYFKVAHRIHEEVEQPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVDGEKGKTGIKGLQNTVMQLKKICNHPFIFEDVERAIDPSGTNVDLLWRAAGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLITEKSIEENILSRAQYKLDLDGKVIQAGKFDNKSTPEEREAFLRSLLEHDGDDDHDLTYGELQDDELNELISRTDEELVLFKKLDKERAATDIYGKGKPLERLLTVNELPDFYKVEVDSFAVQSSSELEDQYLERKRRRRNSISYTELTLDELNTVDDPSSTLMPRKRGRPRKKTNSGSSLSTPLSQESSLARSGRKNTPSYKQKALRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVIEDLEKNNSLHAYEEEALNEEQASLVFLENSEAELPLDSGIVSAEDDKVITYEDSSSSYSE O94436 TAF14_SCHPO SPAC22H12.02; CHAIN 1..241; /note="Transcription initiation factor TFIID subunit 14"; /id="PRO_0000238606" MTTVKRTVRLITDQNVLPGGEAAVLNDQSFPVREWSIKLVCLNPQGEETDASFVDRVTYKLHPTFQNPTRTIRKPPFQIKEQGWGEFEMEIIIYYADKGGEHRFLHYLHFQQEHYHEDIELNINATRPGLLKALTATGEVPGYSDEGEEARKDKRKNESEVGAGKKKAKAKPVDMDKLAEGLQKLQEDDLLQVVQMVNENKTPDMYVRNDIEGGEFHIDLYTLPDNLLLLLYSFCAKRVTM O94446 ESA1_SCHPO ACT_SITE 355; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q08649" BINDING 320..324; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q08649"; BINDING 329..335; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q08649"; BINDING 359; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q08649" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:20299449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:20299449}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q08649}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; Evidence={ECO:0000250|UniProtKB:Q08649}; CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, ChEBI:CHEBI:144968; Evidence={ECO:0000269|PubMed:29192674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; Evidence={ECO:0000269|PubMed:29192674}; CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q08649}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; Evidence={ECO:0000250|UniProtKB:Q08649}; PTM: Autoacetylation at Lys-279 is required for proper function. {ECO:0000250|UniProtKB:Q08649}. MOD_RES 279; /note="N6-acetyllysine; by autocatalysis"; /evidence="ECO:0000250|UniProtKB:Q08649" SPAC637.12c; CHAIN 1..463; /note="Histone acetyltransferase mst1"; /id="PRO_0000051564" MSNDVDDESKIETKSYEAKDIVYKSKVFAFKDGEYRKAEILMIQKRTRGVVYYVHYNDYNKRLDEWITIDNIDLSKGIEYPPPEKPKKAHGKGKSSKRPKAVDRRRSITAPSKTEPSTPSTEKPEPSTPSGESDHGSNAGNESLPLLEEDHKPESLSKEQEVERLRFSGSMVQNPHEIARIRNINKICIGDHEIEPWYFSPYPKEFSEVDIVYICSFCFCYYGSERQFQRHREKCTLQHPPGNEIYRDDYISFFEIDGRKQRTWCRNICLLSKLFLDHKMLYYDVDPFLFYCMCRRDEYGCHLVGYFSKEKESSENYNLACILTLPQYQRHGYGKLLIQFSYELTKREHKHGSPEKPLSDLGLISYRAYWAEQIINLVLGMRTETTIDELANKTSMTTNDVLHTLQALNMLKYYKGQFIICISDGIEQQYERLKNKKRRRINGDLLADWQPPVFHPSQLRFGW O94449 RFC4_SCHPO BINDING 24; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 36; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 61..68; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 157; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 215; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" SPAC1687.03c; CHAIN 1..342; /note="Replication factor C subunit 4"; /id="PRO_0000121770" MSNAVSSSVFGEKNNSVAYELPWVEKYRPIVLDDIVGNEETIDRLKVIAKEGNMPHLVISGMPGIGKTTSILCLAHALLGPAYKEGVLELNASDERGIDVVRNRIKAFAQKKVILPPGRHKIIILDEADSMTAGAQQALRRTMEIYSNTTRFALACNQSNKIIEPIQSRCAILRYSRLTDQQVLQRLLNICKAEKVNYTDDGLAALIMTAEGDMRQAVNNLQSTVAGFGLVNGENVFRVADQPSPVAIHAMLTACQSGNIDVALEKLQGIWDLGFSAVDIVTNMFRVVKTMDSIPEFSRLEMLKEIGQTHMIILEGVQTLLQLSGLVCRLAKSQMKPESFII O94451 PLI1_SCHPO BINDING 321; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"; BINDING 323; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"; BINDING 344; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"; BINDING 347; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452" MOD_RES 395; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 396; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1687.05; CHAIN 1..727; /note="E3 SUMO-protein ligase pli1"; /id="PRO_0000218986" MNQANFLQELPNVLKRLETGLIIPQLKDILRVFGLRLSGTKAELITRIKQLIERIAIENNTTSWEALKKAIDGDVTSAVCILKYNTYQIYSAAAPIAPPSSASGNRSYSRPFAPVVHSRIRFRKSPFYDILEQFNAPFVVPACVGTRNTISFSFHVTPPALSKLLNDPKQYRVYLFSTPSETIGFGNCLMEFPTPQMELRINNQVAHANYRRLKGKPGTTNPADITDLVSKYAGPPGNNVVIYYMNSTKSYSVVVCFVKVYTIENLVDQIKSRKAESKEKIIERIKNDNQDADIIATSTDISLKCPLSFSRISLPVRSVFCKHIQCFDASAFLEMNKQTPSWMCPVCASHIQFSDLIIDGFMQHILESTPSNSETITVDPEGNWKLNTFDEPVESSEDEFVPKEKVIELSDGEGISTMANKSNDQPTRRASTHNSGPPAKRKRESLVIDLTISDDDENVATSTTESPSNATKENSLSRNVQSPNIDTAISNRSTNVRHGHPGFKDYTVENSPASRERSTSESAQSSVHMGYAGEGGLLSGALRAPSQQNNNNSNTQHSINLHTIVPSPYEPPLSVTPSTAITNLSIPESNRTNSSASSKSFTMNDLILPPLHLKNTTQTNNAHEDAQSSNLSQNHSLFYERIPQRPSYRIEKQNKGIYEDENEQSISAMPIPRAHPQLPKNLLSQTAGPLWDEQQDAQVDWNSELQSNNSYHNSGFEGTGNTFQSID O94457 ERG3A_SCHPO CATALYTIC ACTIVITY: Reaction=episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46560, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23929, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52972; EC=1.14.19.20; Evidence={ECO:0000305|PubMed:18310029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561; Evidence={ECO:0000305|PubMed:18310029}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045}; SPAC1687.16c; CHAIN 1..300; /note="Delta(7)-sterol 5(6)-desaturase erg31"; /id="PRO_0000117025" MDYLLNYADQYALDSIYNAVYPLARDNIVRQSISLFFLTWFGGMFLYLTFASLSYQFVFDKSLMDHPKFLKNQVFMEVLTALQNLPGMALLTVPWFLAELHGYSYLYDNISDYGLKYFLCSLPLFVMFSDFGIYWAHRFLHHRYVYPRLHKLHHKWIICTPYASHAFKSADGFLQSLPYHLFPFFFPLHKLTYLALFTFVNFWSIMIHDGKYISNNPIINGAAHHNGHHIYFNYNYGQFTTLFDRLGNSFRAPDEAWFDKDLRQNEDVLRVELMEYEAIRNEVEGDDDREYIANSAKKNH O94459 SCC4_SCHPO SPAC1687.18c; CHAIN 1..559; /note="MAU2 chromatid cohesion factor homolog"; /id="PRO_0000116739" MTGLNETDARILVTSRHLFLWPLAETYFKNAEKVLQDCGVCDSFGRLLSTGLQCLYSVLMDTKMEPRVELLTRKRICEVLLSHTVEYADVEAILNRALIIAEQHNLTEYKFSLQLLLSRVFCRTSPKAAKVLLTRCVREAEEYAKVAEIYHSNNQSNPHRWVYEFLLATLEFQNVSQVANSIHNYANHHKHQHLQLLAMILNQSLPMDEISTDSDQISILCLVTQIAQCLRKGEILLAREILPKIHSKLESETFVWPSSYIDFFIDDTSKISIKWMSINQLYLLIYLISGFCYISDSTSGRASRFLQEGLRITGDFKHQERCVLEYLESQKWINNITKDMKYYLIATYLSRSRLSKAERILQSTEDDQTGFLGILKGMYLQKRGDLKKAEVHYRETAKNFSFRTDTFIISTLNLINILEDSAAASRCLESIEPLCNKHEKKIFKLWLLVLKVIREGPQVHQSNVLPRVIQQSSEYANTQLQYISLTELSERFGKLEHAEKMAISALELAKKSKDELWCLISGRILEDFYRSVQKYDKMRQQALENSAYSKLIEDIYSFV O94466 RGA7_SCHPO MOD_RES 496; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 497; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23G7.08c; CHAIN 1..695; /note="Probable Rho-GTPase-activating protein 7"; /id="PRO_0000097315" MLSAPSSSTTPASPPTSPPNTTSSDDFAVLKEPKVEAILNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANHSLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYNRALDNKNTGDSQKKVGFFKPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTLLNGLTIRPQKPTPTNCGLQHALDNINANTDFVQYVLHASIKHEDNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFPNPSVASPAFPNSSTSNPSTAPASASPLASTLKPSTANDTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPPSSINSNRAASPFRPTSVSPQPSSPTKSLLFGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEDYENDVHAVADLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIKQATIPEISSFSRTIEILIDYCFTIFDYD O94477 MYO52_SCHPO BINDING 167..174; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 1065; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1072; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1919.10c; CHAIN 1..1516; /note="Myosin-52"; /id="PRO_0000123483" MTSGIYYKGLQCWIPDEQSQWIPGSIKDCRVEGEKAFLTVQDENENETVITVKPDDLNYEGRNGLPFLRSINSDADDLTDLSYLNEPSVLDALSTRYNQLQIYTYSGIVLIAVNPFQRLPNLYTHEIVRAYSEKSRDELDPHLYAIAEDSYKCMNQEHKNQTIIISGESGAGKTVSARYIMRYFASVQALIQSTDSNFHEAPQLTAVENEILATNPIMEAFGNSKTSRNDNSSRFGKYIQILFDGNATIIGAKIQTYLLERSRLVFQPNQERNYHIFYQILAGSSSEQLEKWKLVENSQEFNYLKQGNCSTIEGVNDKEEFKATVDALKTVGIDNDTCECIFSLLAALLHIGNIEVKHSRNDAYIDSKNENLINATSLLGVDPSSLVKWLTKRKIKMASEGILKPLNEFQAVVARDSVAKFLYASLFDWLVATINKALMYSADKSNQTAKSFIGVLDIYGFEHFKKNSFEQFCINYANEKLQQEFYRHVFKLEQEEYAAEGLNWSYIDYQDNQQCISMIESRLGILSLLDEECRMPTNSDENWVSKLNDAFSKPEFKNSYQKSRFGNKEFTIKHYALDVVYCAEGFIDKNRDTISDELLELFTNSDVPFVKDLVLFRLEQTAPPADTKKIKTKPKSNTLGSMFKSSLVSLMSTINETNAHYIRCIKPNEEKEAWKFDNQMVVSQLRACGVLETIKISCAGFPSRWTFDEFVSRYYMLVPSAVRTTESLTFSKAILEKHADPTKYQIGKTKIFFRSGVTPLLESARDKALKHAAHLLYEAFAVNYYRTRFLLSRKRVRSFQAVAHGFLSRRHTEYELLSSNIIKLQSLWRTALKRKEFIQTKNSILKVQSIIRGFLLRQTLEEKTKHDATLIIQSLWLTFKAHKHYKELQYYAVRIQSLWRMKLAKRQLTELKIESTKASHLKQVSYRLESRLFEISKQLDNSEQENNKFRERIAELESHLSNYAEAKLAQERELEQTRVLISDQSQDGELKELLEEKENALIMMEEEMRQVNDANTELLRVNATLKSQLKNYDMIIVEQTSQLKEKNRIIASLTKATKILNSASSIEQSRNSEEKSRRDSSLMEMRTQKEMLVLLMNDGLKHDLDKLTEYAGRTFTTLKTLLLKDNDVEAQKLDHLFLAKLLFIIISQMWKSNLCQESVALVERYCVHTLEYVFQKTSSANERPDIGFWVANTHALLAFVYTKQQAFKHSSAFTLLSTESHESVQTIFEMIESHLSKIFFEWVRQVNNFLKPLIVQAMIITGTNTDAGDENRKLRIKFFEKPKYKITDVIHVLNKVHDSCQAYKVNYEIYNALIRSIYRFINVEAFNSLFIDERGSWKRGTNISYNYHVLKDWCLESGVPEAYLQLEELLQTSKILQFVKDDPNYVARVRDFYALNFLQIKTLLHRYDYADYEAHVPKKTMSELSKNIVAEGINQREQLTYEVLDYRLQDSFEESPSLEKIKIPDDCNVTYLRRIIDLASAEESVEQALITVGNVADNDVQNSSDEENQVPNGIKV O94487 PPK35_SCHPO ACT_SITE 285; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 168..176; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 191; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPCC417.06c; CHAIN 1..624; /note="Serine/threonine-protein kinase ppk35"; /id="PRO_0000256830" MDLLGLKELDNNKLVSKAKENGVEFSDLFLLSSGYLRDRENASASVSSKNERMVLNEERQNCWTKRNDPKGLTYYQLLKPSEVEILSRPETRRKRMACQVFFLNYYISTIEYHKLRKERLEEFTACTSSLKQSKQKRLWKEHCGRERAFLRKKRTKIQCSHFDLLVKLGQGGYGSVWLAKKRNTHELLAMKMMKKSTLQQLNEVKHILNERDILTNTNSEWLVKLYYAFQDKEKVYLAMEYVPGGDFRTFLTTKGLLHENQTRFYLAEMVAAISAVHKLGYMHRDLKPENFLIDQKGHIKLSDFGLSTAIVTSNQVNRLQHALVSAVNPQRPYLTQKQRRNIYKALLEKNENKVNSVVGSPEYMAPEVVYGKKYDRTVDYWSLGCICYECLVGYPPFSGSTLQETWTNLYYWREMLQRPSKNENGIYDKKARSVSDEAWSFITKCLTEPTSRFQSTIEIQKHPFFKRLHWNGLRKRAVPPFVPRLENQLDTSYFDDFNDEQVLDAYKDVYEKQRKAEQKAKSNGVMNGNQRQFLGFTFKYRPNARKPLVGRHREKRQLRKEKPEKKNNSTKQKDLITVSHNKGTTAIEDLDEDKRSKTKGHKTKSSRVHRLLERKGKDLYEFLL O94488 MBO1_SCHPO MOD_RES 94; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1005; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1009; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC417.07c; CHAIN 1..1115; /note="Gamma tubulin complex adapter mto1"; /id="PRO_0000356169" MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLESRIKPDQSFNLSTPSPAPSNLITLQSRYSQALSELETTKRAFAALRKEKSKKTNYSVGAYNEDRNVLSNMLDNERREKEALLQELESLRVQLSKKVPMPAKNTDERVIETLQRSNELLRMDISMQNEALLLRKQENDRLVKQVEELTVALNSGKMNAIVEAESSKNELWDSMMVSRMKTQEQSIELTRLYKQLQDIEEDYENKLMRMEQQWREDVDQLQEYVEEITQELQDTKEVLSKSSKESDDYEEVVGKLRTEAEREIEKFEKTIRENEESISLFKEEVEKLTDEITQLSERYNDKCHEFDELQKRLQTLEEENNKAKEDSTSKTSNLLEQLKMTEAEVDSLRKENEENKQVIALKESELVKSNDNKLLLNEQIESLNDQLSQLKTEMESVTTSKESLADYLSNLKERHNDELDSLNKKLREFEGILSSNSSLKSEIEERNNQYVTLRENFDSLQNAIMETFDKQVTHCSVNHLVQQIRKLKDENKKDQSGTDKLMKKIYHCEQSLKEKTNSLETLVSEKKELKNLLDAERRSKKAIQLELENLSSQAFRRNLSGSSSPSERSQSRELKLLQASEKRLKEQVEERNSLIKNIVTRFTQLNTGSKPVNTNVEALTTISSMNQAVNMNFRELDKSIQEFKRKCQSMEREFKTELRKLDGVLEARSKRLSQLEERVKLLGAGSTSSIPNSPRASKRVSLDSEDKKLVPASPDKSAVQRGITALKRDAEGMSHIWQLRLREMEFQLKAEQEGRKRDKLGARERLQDLIRQNRSLSRQIKTDKESNSRSPSISSQEHK O94489 EF3_SCHPO BINDING 467..474; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 707..714; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P16521}; MOD_RES 714; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 768; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 783; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1043; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC417.08; CHAIN 1..1047; /note="Elongation factor 3"; /id="PRO_0000093457" MSAKSENKQSVKALEELLKHLTVCDAAEEADAAKALASFVNGPIEEQDAPSQVFSAISKQLNDKNATARERVLKGLEAVANHGSVAADVEPYLVELLPAVIAKVADKQNAVRDAAIAASKAIVRCTTPYAVKAIVPSVLESIHTTGKWNEKMNSLQLLDVLVEVAPSQLSYSLPQIIPVVSESMWDTKAEVKKQSKETMTKVCTLIANADIDRFIPELINCIAHPEEVPETIHSLGATTFVTEVQAPTLSIMVPLLARGLNERSTPIKRKTAVIIDNMSKLVEDPQVVAPFLPKLLPGLYHIKDTIGDPECRSVVQRAITTLERVGNVVDGKIPEVSTAANPEVCLETLKAVLGEIKVPTNEEVIAKYVANIAAQLVEEKDNENESWVLNITPYLTAFIDEAHIHKIVEQLRTRSIAKIPGGASHAEEEEEGEDLCNCEFSLAYGAKILLNRTRLRLKRGRRYGLCGPNGSGKSTLMRAIVNGQVEGFPTHLRTVYVEHDIDESEADTPSVDFILQDPAVPIKDRDEIVKALKENSFTDELINMPIGSLSGGWKMKLALTRAMFKNPDILLLDEPTNHLDVVNVAWLENFLVNQKDVSSIIVSHDSGFLDHVVQAIIHYERFKLRKYLGNMSEFVKKVPSAKSYYELGASEMEFKFPEPGFLEGVKTKQRAIIKVQHMSFQYPGTSKPQLNDISFQVSLSSRIAVIGPNGAGKSTLIKVLTGELLPTVGEIYQHENCRIAYVAQAAFTHLGHHPDKTPSEYIQWRFQSGEDLEAMDKASRVISEADEEAMKNKIFKIEGTQRKILGIHSRRKLKNSYEYECSFLVGENIGMKSERWVPMMSSDNAWLPRGELMETHAKMVAEVDRAEALKSGQFRPLVRKEIEEHCSLLGLDAELVSHSRIKGLSGGQKVKLVLAACTWLRPHVIVLDEPTNYLDRDSLGALSKGLKNFGGGVVLVTHSREFTEGLTEEVWAVNNGHMTPSGHNWVSGQGSGPRIQEKEEGDTFDAFGNKIEKAKKAKKLTGAELRKKKKERMARRKAGLEVSDDEL O94504 TRX2_SCHPO ACT_SITE 59; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 62; /note="Nucleophile"; /evidence="ECO:0000250" TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC12D12.07c; CHAIN 30..133; /note="Thioredoxin-2, mitochondrial"; /id="PRO_0000337144" DISULFID 59..62; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" MRGFIANSLKPHMRSFALRRSFTSSRILRKVNAVESFGDYNTRISADKVTVVDFYADWCGPCKYLKPFLEKLSEQNQKASFIAVNADKFSDIAQKNGVYALPTMVLFRKGQELDRIVGADVKTLSSLLAKYQE O94505 DPNP_SCHPO ACT_SITE 50; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P32179"; ACT_SITE 141; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P32179" BINDING 73; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 73; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 136; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 136; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 138; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 139; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 141; /ligand="adenosine 3',5'-bisphosphate"; /ligand_id="ChEBI:CHEBI:58343"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 232; /ligand="adenosine 3',5'-bisphosphate"; /ligand_id="ChEBI:CHEBI:58343"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 232; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 256; /ligand="adenosine 3',5'-bisphosphate"; /ligand_id="ChEBI:CHEBI:58343"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 256; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 259; /ligand="adenosine 3',5'-bisphosphate"; /ligand_id="ChEBI:CHEBI:58343"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 259; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 273; /ligand="adenosine 3',5'-bisphosphate"; /ligand_id="ChEBI:CHEBI:58343"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 273; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 286; /ligand="adenosine 3',5'-bisphosphate"; /ligand_id="ChEBI:CHEBI:58343"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 286; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P32179"; BINDING 286; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P32179" CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=adenosine 2',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:77643, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:194156, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77644; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol 3,4-bisphosphate + phosphate; Xref=Rhea:RHEA:70319, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414, ChEBI:CHEBI:83241; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70320; Evidence={ECO:0000305|PubMed:10850973}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10850973}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P32179}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77 uM for 1D-myo-inositol 1,4-bisphosphate {ECO:0000269|PubMed:10850973}; Note=KM for adenosine 3',5'-bisphosphate is below 10 uM. {ECO:0000269|PubMed:10850973}; SPCC1753.04; CHAIN 1..353; /note="3'(2'),5'-bisphosphate nucleotidase"; /id="PRO_0000142536" MSFDAEKQLAIAAVRRASYLTEKVFNQLIKEKSAAGALTKDDKSPVTIGDFGAQAIVISMLKDAFPNDPIVGEEDSDFLRENTQTCSRVWELVQETIQHATEYKELGQIKSAEEMMSIIDQGSYHGGRNGRMWTLDPIDGTKGFLRGAQYAICLALIENGKPVVSAIGCPNLPYDFNQPETSPKGIIMSAVRNHGCFQYSLHNEKLEPVQVHMQDVQNTKDSKFCEGVEAGHSMQGTQEEIAKYLGITRGPTKMDSQAKYASLARGDGDIYLRLPTKMTFEEKIWDHAGGSLLVEEAGGVVSDMFGKPLDFGVGRTLKNNNGVIAAYKGIFEKVIEATAAVTSKDPHFQKVAQ O94510 AGN2_SCHPO CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59; SPBC646.06c; CHAIN 1..433; /note="Ascus wall endo-1,3-alpha-glucanase"; /id="PRO_0000119035" MASLTTALPNKAVVAHFMMGLTYNYAQSDFQNDIQNAISLGLDGFVLNFGNDSWMMSKLTLMYNAADALNLQFLLYLNLDMSEMSTVPASTLVTYVQTFANRGHQARINNNVVVGTFLGQDINFGQSSVNQGWQVAFKNALASAGINIFFMPTWPLDASTIYQTYPVADGFCKWNCWPYYTSSPTSDAEDLVYIQNSKATNKKYMATVSPIFYTHFTSKNYSFFSEGLWFTRWMQLIKDQPNYVQVLTWNDYGESTYIGPTNYAADFPVIGSNSHEWVDSFTHAPLSYSLPLFIQMYKQNTTGLPSNFSGISQLYVTYRVHSKNATASSDSIPRPDNYQNSSDVISVISFAKSSYTLRVSVNGTVLGTTNVNAGVQSANVSFIVNNTAAAGLPLFQILNGTTVIAQGYGPLNILGNNSVVLYNFNFCTTRISW O94513 EIF3E_SCHPO MOD_RES 477; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 479; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC646.09c; CHAIN 1..501; /note="Eukaryotic translation initiation factor 3 subunit E"; /id="PRO_0000123519" MGSELKSTSPLAVKYDLSQKIMQHLDRHLIFPLLEFLSLRQTHDPKELLQAKYDLLKDTNMTDYVANLWTNLHGGHTDEDMANAFAEKRRSVLQELSELEEEVQGILGVLENPDLIAALRQDKGQNLQHLQEHYNITPERIAVLYKFAQFQYNCGNYGGASDLLYHFRAFSKDPELNASATWGKFASEILTVDWDGAMEELGKLREMVDSKSFKDSAVQLRNRTWLLHWSLFPLFNHANGCDTLCDLFFYTPYLNTIQTSCPWLLRYLTVAVVTNQNNANQKPRNPRQSYQRRMRDLVRIISQENYEYSDPVTSFISALYTEVDFEKAQHCLRECEEVLKTDFFLVSLCDHFLEGARKLLAEAYCRIHSVISVDVLANKLEMDSAQLIQLVENRNNPSVAAASNVAADQSTEDESIESTSTNVVADDLITEAETATEAEEPEPEVQFGFKAKLDGESIIIEHPTYSAFQQIIDRTKSLSFESQNLEQSLAKSISELKHATV O94529 POB3_SCHPO SPBC609.05; CHAIN 1..512; /note="FACT complex subunit pob3"; /id="PRO_0000245210" MAAKTVQYDNIYLNLSEKPGKLRIAPSGLGWKSPSLAEPFTLPISEIRRFCWSRFARGYELKIILKSKDPVSLDGFSQEDLDDLINVIKQNFDMGIEQKEFSIKGWNWGEANFLGSELVFDVNSRPAFEIPISAVTNTNLSGKNEVALEFSTTDDKQIPSAQVDELVEMRLYVPGTTAKEDAADGEEVEQNAANLFYESLKERADIGQAAGDAIVSFSEILLLTPRGRYDIDMYETCMRLRGKTYDYKVEYSSINSLFLLPKPDEQHVVFVIGLEPPLRQGQTRYPFLVTQFVRDEDMEVDLNIEETVLKEKYADKVKASYDQPAFEVVSQIFRGLTGRKVTTPAEFLSHEGHAAVKCSYKANEGQLYCLDKSFLFIPKPTLLMNTSDITRVTLSRVGMSVSAARTFDLTFTLRSGTSYQFSNINRVEQSALVAFLESKQIKIHNDLADETQQTLLTSALDDEDEEGDEEMEEALSEDEDFQAESESDVAEEYDENAESSDEEGASGAEGSE O94532 FOR3_SCHPO SPCC895.05; CHAIN 1..1461; /note="Formin-3"; /id="PRO_0000194904" MASKMPEGSPPTSRSIQSRNSSYSTSSNERIGTPSTISLSENSDLSKLQSTNDFESREDLSLTSDDNNDPEYVMCYNTVYHQKTKINDKLLSETEQLRKIYPLESRVFPKPTIVKEITNERTKRYTFYDDDAPLTNQHTVLDEATYNRILKRIDFFIEKVVEVPPTYHFLSLLNVQLRIQPIWWMDEFAERNGIESLLSALRNLGHYPERASKTPLESQIIQSLFHCLNSENCRRRYQSSAKCSVPGFNALGTIAETVLSKSLNSARMATFLLKFLCNKKGLSYFKAVIRAFEWLVEQKLSKTRFSAWMHSFNDVITGVRVCADSSPQAIVHMDEFEDTDCLIDYLVATLALIRDLCAAPPDLQLRCALRHELLSAGLQKAIDSLLKWRNRHVRDALQLLIKEHNADARRFRSGSDVNNVDRKCVKKQMNYREESHTPHGNTTRKTSTPVSNNRPTTPEQQAVWDVFQRIYTRFTGSEGSKESFIKLLEYFVTEPDNGKIQKSMQLLTHTLEALEGFKTAKADTNVGLTILSQRLLDKLGTAEEIAEYKTKYNGAMLENKHLKEQVESMLSQLNVGPRDPMQFLKKQLDELKAELNLRDNLLASMQREFETRYRAQIQAYNKLQSQMEHVQNSNEQHLQPGLLNKVSKSFDSVHRRNLSQDSLDAMTEQFSYHVEPNILSGSGIPVRVHTPSKTEDLDESFSGSEISSSPSPLLPDVSDTVEEQQKLLLKSPPPPPPAVIVPTPAPAPIPVPPPAPIMGGPPPPPPPPGVAGAGPPPPPPPPPAVSAGGSRYYAPAPQAEPEPKIDETSLTEEQKIQLEEARKQRKAADDAARAAIEKYTSIPSLRDLHKPTRPLKRVHWQRVDPLPGPNVFTKFCLNFDITAKVFIDNGLLDFLDEKFDNTPREDFVAVEISDQRSSLLPDTVEQNMAIILRSVSNMPVEDLVQKFLVEPDFLPASILYFDRASLASTNAYTDPFIPYSTDYTKKNPKEPTADVNSLSYFEKFFVLFVVNLRHYFQERMKALKFRSTLFGDLEILEVRMKEVIDTSDSIMEDKNFAEFFQVLLIIGNYFNEPYDRASAFSLYMIYRLETLRDSSSALTLMHYFDEIIRTRFPELLQAESTFKKIQSVSGYNIDAMVAGVDGAYDEFCDFQTSLKDGALSKCDQHHPDDKAYDILSEWLPEAKERIRNIKKLKTDMLTKLENTVKYLCEYDSIDKVRNSFFKNLNSFYEMYSIAKAENEERFEKEKRRIMSEDRDKLIRGRQKTSIVAKYRNKRELPEDSDDKQDTASKDKNSLETIDEKMEDASKIEGDAKTGDDNEMEDLDKMEDLEKPDYAEEKDPYITVMSELRSRIQNVPKRTVTVYSDEGVATLEPGAQGDDVVDKAKMILEKMEGHSQLLTSSANPDEEVLRAKLKAAERLQKPAIPRTRRKGHTEPKSAKSLLAELTNGSNASNLVENDRQKQ O94534 ALP14_SCHPO MOD_RES 543; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 548; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 697; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 720; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC895.07; CHAIN 1..809; /note="Spindle pole body component alp14"; /id="PRO_0000064566" MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIKDNDFFNLVAILTKSVSKDANIMVVINAAHCIQAMAKGLRSNFSKYASTSINALLERSKEKKANVIESLSSAMDAVLATSSLDDLAELIASFAGNKNPQIKSSCFSLFSRSFSNMTSLPSKFTVDTCAKACVPGVSDTFEPVRSAAAEALGVLMKLVGERAINQYLSPLDDIRKSKIRSFYETATVKAKAPTKKSKVKPSKQEESKVVVPSNAKAVKKSVVPSSPVVPSPRKATNKSLSMDVSKGNAFENGPLLPRPTTRPVSRGLSRGTSSSLQQKVKASTPLNSGALNETVQNLKNMELDDPAPQPAKHSRVDRYEHPKVLEDNDSTISSLESLKRENEELREQLKVEHEENISMQKQLSELKGELNTLRSARKASPIGDRKPAFMRRANTDFLELSTSPSFQRSVREFEPTRPKLYSSIDVNQRSPLASAKTNGNFTFHAELPRSPFSSRANNINPDWTKAIDLAAKLKQKITEMKQTDQRHQGLIH O94537 IRE1_SCHPO ACT_SITE 774; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 660..668; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 682; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:15821139}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:15821139}; SIGNAL 1..30; /evidence="ECO:0000255" SPAC167.01; CHAIN 31..1072; /note="Sensor for unfolded proteins in the ER ire1"; /id="PRO_0000256815" MKSLKGRLLFLRKFVFFSLLILLFAHGASSSSSSFNYFDKRTNGKANNELALFSPTADSPSSVDGVLELPSAENVFAESSLYNAFIVATVDGSLHSYDRITGQELWSLFTNANPGLSYTKDENSLLSSKFLSQSNFKSYNSTHGEFYSDSTLNISYLSDDDTVWFVEPIDGGILYAFNLQTGLVRLPHSIKDLVHASPIRLLNNNVFVGSKNTTLFTIDVSNGDIVSQYPSGHRYETHHSVHNLGTKRDSVPSGADSDLSFKDPSGKKLSESLDLLDDFNYQVTVSNKSFVDIARTEYFITIYSDSNVILDLVYIDWTPTKNEIMYESFHSSSFDSKLALSSYDSSLHIVDTHSKFIKQNIPLMSPAATVFDIVTLPHNKKIDKSQTPAKFPTSVLLRQPIDTYLETMFPQIARNKTEHVYINHIGNAWFAMSERHYPLVSLAPEASFLYYNGFYIPLNSIFGLHSLMATPKPFFALPGLPGYDIPSYVESEGSTKTLPSIGKKPIPLLDPNPISSTPISITFWVIMFLSVSFTIVTFFSILRIRSSEVRPLKSQKNTVSINNKIDTSKRRRKGKRRKRVSDEHSASSNFNEIESQASFEQNQTLDILSENIVEIQDKSTDPLQKSLDSSLKSHLPEATVIQNTDGSVTVNSLTVYPEVIGYGSHGTIVYRGVYEDREVAVKRVLMEFYDLASREITLLQQSDNHPNIVRYYCKQKSDQFLYIVIELCKCNLSDLIEKPIAYDDLFKSIDLVSLLYQIAFGVSHLHSLDLVHRDLKPQNILLVVNNSPNLSKTRVRALISDFGLSKKLDFNQSSLRNTTFEAAGSYGWRSPEILSGSLSQQSKEIQVKTREGRIRQASHATDIFALGCIFYYTLTGGMHPFGSHYDCEGNILKGNYCLVHLQSLGECGVLAADLIEDMIAFEPSKRPTIEVVLNHPLFWDYAKKLDFLIDVSDRFEVEERDPPSPLLQMLENNSKSVIGENWTTCLHSSLVDNLGKYRKYDGSKILDILRVLRNKRHHYQDLPESVRRVLGDLPDGFTSYFVEKFPMLLLHCYHLVKDVLYEESQFKRYLEY O94544 LKHA4_SCHPO ACT_SITE 295; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 382; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 136..138; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 265..270; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 294; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 298; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 317; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:Q10740}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q10740}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q10740}; SPCC1322.05c; CHAIN 1..612; /note="Leucine aminopeptidase 2"; /id="PRO_0000095128" MKLRLDPSTQSNYHDVSISKLDWHARIDFDQELLHGKVSFVIQSARVSQALSHIILDTSYLEIKNVTINDIPTPFRVDKRRGFLGSALHIVPADEIPSSKSCILTILYSTTKDCTALQFLKPEQTIGGKFPYVFSECQAIHARSFIPCQDTPSVKVPCTFKIRSKLPVIASGIPCGTANFCNGSLEYLFEQKNPIPSYLFCILSGDLASTNIGPRSSVYTEPGNLLACKYEFEHDMENFMEAAEQLTLPYCWTRYDFVILPPSFPYGGMENPNATFATPTLIAGDRSNVNVIAHELAHSWSGNLVTNESWQCFWLNEGMTVFLERKILGRLYGEPTRQFEAIIGWGELEESVKLLGEDSEYTKLIQNLEGRDPDDAFSTVPYEKGSNFLYEIERVIGGPSVFEPFLPFYFRKFAKSTVNEVKFKHALYEYFSPLGLASKLDSIDWDTWYHAPGMPPVKPHFDTTLADPCYKLAESWTNSAKNSDDPSKFSSKDIENWSAGQKSLFLDVVYEAVSFPHNYIKRMGDVYSFAESKNAELSFRFFKLALKSKYKPLYNTIAERVGSVGRMKFVRPIFRLLNEADRAFAIETFEKYKHFYHKICASQVEKDLGLSE O94547 SRK1_SCHPO ACT_SITE 257; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 130..138; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 153; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15629716}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15629716}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15629716}; PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:12589433}. SPCC1322.08; CHAIN 1..580; /note="Serine/threonine-protein kinase srk1"; /id="PRO_0000086680" MRFKSIQQNIEDEGKVNVREVNPDSYAERDHGYTAGIFSDAEENFGITQQVADSTQNPTSKPKSRHAHFHETVHENPSEYSRSKCKQPTNEKEYDKAIEALVAKAIVEEHSGQQFPVYKGLEQYTLLQKMGDGAFSNVYKAIHNRTGEKVAIKVVQRAQPNTDPRDPRKRQGVESHNILKEVQIMRRVKHPNIIQLLEFIQTPEYYYLVLELADGGELFHQIVRLTYFSEDLSRHVITQVAHAIRYLHEDCGVVHRDIKPENLLFDSIDFVPSRVRKYRAGDDPDKVDEGEFIPGVGAGTIGRIRLADFGLSKVVWDSHTQTPCGTMGYTAPEIVRDERYSKGVDMWALGCVLYTILCGFPPFYDESISLLTKKVSRGEYSFLSPWWDDISKSAKDLISHLLTVDPESRYDIHQFLAHPWISGSREPTFPATDAPNTAQRENPFTYDFLEPEDVAAAGSAARTPGVNSLREVFNISYAAHRMEQEKIRKRGQRGNQGIMNFMGDMDDLMEENDDYDDGTKSVEHSMKRVNLSGENDPSLASRQPAQSQQQSSQRSRNKFKGFQLNLSKATLYNRRHRQKV O94561 PRX_SCHPO ACT_SITE 89; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000250|UniProtKB:P40553" CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:P40553}; PTM: The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin. {ECO:0000250|UniProtKB:P40553}. SPBC1773.02c; CHAIN 1..195; /note="Peroxiredoxin bcp1"; /id="PRO_0000314635" DISULFID 89..94; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:P40553" MDAPRRSSRLAAKIANVLDSKGTIIPEAAPVMLKKPAKDESVDSTIQVGDVIPDITLPDEDGTSIRLRDITANKGLVIFAYPKASTPGCTKQGCGFRDNYPKIQASDYEVLGLSFDTSKAQKAFKDKQNFPYHLLSDPKGELIKKLGAEKPGGGKLFRSHWIFEKGTGKCIVKEIDISPLVSVDKAFAVITDSEP O94580 WSS2_SCHPO ACT_SITE 203; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 202; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:27871365, ECO:0007744|PDB:5JIG, ECO:0007744|PDB:5LN5"; BINDING 206; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:27871365, ECO:0007744|PDB:5JIG, ECO:0007744|PDB:5LN5"; BINDING 212; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:27871365, ECO:0007744|PDB:5JIG, ECO:0007744|PDB:5LN5" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:27871365}; SPCC1442.07c; STRAND 108..115; /evidence="ECO:0007829|PDB:5JIG"; STRAND 149..155; /evidence="ECO:0007829|PDB:5JIG"; STRAND 169..172; /evidence="ECO:0007829|PDB:5JIG"; STRAND 177..181; /evidence="ECO:0007829|PDB:5JIG"; STRAND 183..188; /evidence="ECO:0007829|PDB:5JIG"; STRAND 210..213; /evidence="ECO:0007829|PDB:5JIG" HELIX 122..134; /evidence="ECO:0007829|PDB:5JIG"; HELIX 136..145; /evidence="ECO:0007829|PDB:5JIG"; HELIX 193..205; /evidence="ECO:0007829|PDB:5JIG"; HELIX 214..227; /evidence="ECO:0007829|PDB:5JIG" TURN 173..176; /evidence="ECO:0007829|PDB:5JIG"; TURN 206..208; /evidence="ECO:0007829|PDB:5JIG" CHAIN 1..282; /note="DNA-dependent metalloprotease WSS1 homolog 2"; /id="PRO_0000350746" MELKFSCRGNVIALSFNENDTVLDAKEKLGQEIDVSPSLIKLLYKGNLSDDSHLQDVVKNESKIMCLIRQDKDIVNQAISQLKVPDYSTNTYSLKPKKPHTTPKPASIYTFNELVVLDYPHKDRALRYLERLRDDTGIKKIMDSHRWTVPLLSEMDPAEHTRHDSKTLGLNHNQGAHIELRLRTDRYDGFRDYKTVKSTLIHELTHNVHGEHDSSFWELFRQLTKEADAADLLGKPGSYVSDRASYTPQQDNDDEDQKNHRRDLLLAAAERRKQSGSKVQKE O94584 PSS_SCHPO CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8; Evidence={ECO:0000269|PubMed:17905925}; SPCC1442.12; CHAIN 1..240; /note="CDP-diacylglycerol--serine O-phosphatidyltransferase"; /id="PRO_0000318107" MVRSRVSPGLKLQSDASNQSNDKENKLLAYVNDNRHFSLIRALHLADLITLMNGFCGVMSIFSSLRYCLSGQQSAFHLWNAMYFMPFALFFDFLDGKVARWRGKSSLMGQELDSLADLISFGVSPAVFAFCCGFQTFLDTVILSLFVLCGLTRLARFNVSVNSIPKDGSGKSQFFEGTPIPTTLSLVTVCGVCILKGKTHENLPWGEWCGNTPFAFHPLVVLFVLSGIAMTSKKLKVPKI O94603 JHD1_SCHPO BINDING 294; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 297; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"; BINDING 299; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"; BINDING 314; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61976; EC=1.14.11.27; Evidence={ECO:0000250|UniProtKB:P40034}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; SPCC622.16c; CHAIN 1..948; /note="Putative JmjC domain-containing histone demethylation protein 1"; /id="PRO_0000086985" MDSWLEYDDIINQDIDIPSNDLSGSGTLCVGVHSSLLENSLNSIDSFISSKEEISWCGNQSTPIATKSHLSCINPQYVNPFDTSPVSVDTEFQDTYLLDAPSFAQPHFSERQSVDKTRSRCLSRNRRRKRHPNLHKNHQRLLGMSFPQDGFRRMPAESVNFSYFRDTGFNEPTIFPSSDTQNTRQLNLSKIATLIGYDCPLALVDVVTQKQIPNKMDMESWVKYMSLEPSKRGRIYDVLSLEVSTTKLAYYVRKPNIVRDLDLVNTVWPPGSFALGEYPHVDTYCLMSAENSYTEFHIEFGGSSAYYNILDGCKIFYLIPGTSKNWEAYTAWLTSSNDSDKKFLPNMVDVCYCVEVHSQQTILVPSGWIYAVVTPCDTISIAGNFLTFLHIYPQLSIYNLELQLGIEKEYQYPYFESIMWYTAIHFYLAFPDNSSRDGIDDIIAEYETGRLFDINAFTEQELDGFEELLNYLYIRAQILRDCDIIIDIYNEPVKISKNNGYNSAYTMVPPDLDEICVDFVQKFGAWITYHHRRSAKHPSCNCFSHLQTKLIDSGPKPANNSYQHQSNFIGVVISTNHNIIKKCQESQIQTGKNNCSFQLVKKRIKSTKKAPSWRSIIKAFKKRENTRCNFLSSLHATTFREDIVVRPKIKSFVLEQLIFQALFSFAINWTPSFFLNHSNFENIALSKETFNFGGEANCENTDTTLFTTWGDQGFRPSDSICYNDFNLLETANSDAEASIHELELQPLNAVNEREVDISQTDMTPSTALDTRVDTRVDSLPEFSNLILSPSSNDDSFQLDDLLSPSSSNLKQQIQKVVPQNSLEFSVGEKEKKAAEYSLLHTFSYKRLSMENEKPDTTKVPLKYNIQHEEMKAYRRKNDLEYIDQHFASSKSGISNGRNNNKEVNLTKAENVGIKKRRIMKNENNIYDFEDHSPVREKWGHRLRSRGAS O94609 UBA1_SCHPO ACT_SITE 593; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10132" BINDING 22; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"; BINDING 437; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"; BINDING 463; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"; BINDING 474; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2"; BINDING 487; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"; BINDING 513; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"; BINDING 537..538; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:23416107, ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3" CATALYTIC ACTIVITY: Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000269|PubMed:23416107}; SPBC1604.21c; STRAND 39..43; /evidence="ECO:0007829|PDB:4II2"; STRAND 62..67; /evidence="ECO:0007829|PDB:4II2"; STRAND 105..107; /evidence="ECO:0007829|PDB:6O83"; STRAND 109..111; /evidence="ECO:0007829|PDB:4II2"; STRAND 124..128; /evidence="ECO:0007829|PDB:4II2"; STRAND 149..156; /evidence="ECO:0007829|PDB:4II2"; STRAND 159..165; /evidence="ECO:0007829|PDB:4II2"; STRAND 170..176; /evidence="ECO:0007829|PDB:4II2"; STRAND 182..189; /evidence="ECO:0007829|PDB:4II2"; STRAND 193..197; /evidence="ECO:0007829|PDB:4II2"; STRAND 209..214; /evidence="ECO:0007829|PDB:4II2"; STRAND 233..238; /evidence="ECO:0007829|PDB:4II2"; STRAND 247..251; /evidence="ECO:0007829|PDB:4II2"; STRAND 253..257; /evidence="ECO:0007829|PDB:4II2"; STRAND 261..263; /evidence="ECO:0007829|PDB:4II2"; STRAND 272..274; /evidence="ECO:0007829|PDB:4II2"; STRAND 382..387; /evidence="ECO:0007829|PDB:4II2"; STRAND 394..396; /evidence="ECO:0007829|PDB:4II2"; STRAND 429..433; /evidence="ECO:0007829|PDB:4II2"; STRAND 454..456; /evidence="ECO:0007829|PDB:4II3"; STRAND 458..462; /evidence="ECO:0007829|PDB:4II2"; STRAND 505..509; /evidence="ECO:0007829|PDB:4II2"; STRAND 530..534; /evidence="ECO:0007829|PDB:4II2"; STRAND 556..562; /evidence="ECO:0007829|PDB:4II2"; STRAND 565..571; /evidence="ECO:0007829|PDB:4II2"; STRAND 698..702; /evidence="ECO:0007829|PDB:4II2"; STRAND 704..706; /evidence="ECO:0007829|PDB:6O83"; STRAND 815..818; /evidence="ECO:0007829|PDB:6O83"; STRAND 851..853; /evidence="ECO:0007829|PDB:6O83"; STRAND 885..889; /evidence="ECO:0007829|PDB:4II2"; STRAND 894..898; /evidence="ECO:0007829|PDB:4II2"; STRAND 905..908; /evidence="ECO:0007829|PDB:4II2"; STRAND 911..914; /evidence="ECO:0007829|PDB:4II2"; STRAND 919..924; /evidence="ECO:0007829|PDB:4II2"; STRAND 941..947; /evidence="ECO:0007829|PDB:4II2"; STRAND 950..954; /evidence="ECO:0007829|PDB:4II2"; STRAND 988..996; /evidence="ECO:0007829|PDB:4II2"; STRAND 1000..1004; /evidence="ECO:0007829|PDB:5KNL"; STRAND 1007..1011; /evidence="ECO:0007829|PDB:4II2" HELIX 17..27; /evidence="ECO:0007829|PDB:4II2"; HELIX 29..36; /evidence="ECO:0007829|PDB:4II2"; HELIX 47..59; /evidence="ECO:0007829|PDB:4II2"; HELIX 74..78; /evidence="ECO:0007829|PDB:4II2"; HELIX 85..87; /evidence="ECO:0007829|PDB:4II2"; HELIX 92..101; /evidence="ECO:0007829|PDB:4II2"; HELIX 118..122; /evidence="ECO:0007829|PDB:4II2"; HELIX 133..145; /evidence="ECO:0007829|PDB:4II2"; HELIX 221..223; /evidence="ECO:0007829|PDB:4II2"; HELIX 243..245; /evidence="ECO:0007829|PDB:6O82"; HELIX 268..271; /evidence="ECO:0007829|PDB:4II2"; HELIX 282..284; /evidence="ECO:0007829|PDB:4II2"; HELIX 287..304; /evidence="ECO:0007829|PDB:4II2"; HELIX 315..331; /evidence="ECO:0007829|PDB:4II2"; HELIX 340..348; /evidence="ECO:0007829|PDB:4II2"; HELIX 355..372; /evidence="ECO:0007829|PDB:4II2"; HELIX 389..391; /evidence="ECO:0007829|PDB:4II2"; HELIX 400..403; /evidence="ECO:0007829|PDB:4II2"; HELIX 411..417; /evidence="ECO:0007829|PDB:4II2"; HELIX 419..426; /evidence="ECO:0007829|PDB:4II2"; HELIX 437..449; /evidence="ECO:0007829|PDB:4II2"; HELIX 469..471; /evidence="ECO:0007829|PDB:4II2"; HELIX 480..482; /evidence="ECO:0007829|PDB:4II2"; HELIX 487..498; /evidence="ECO:0007829|PDB:4II2"; HELIX 500..502; /evidence="ECO:0007829|PDB:4II2"; HELIX 515..517; /evidence="ECO:0007829|PDB:4II2"; HELIX 523..527; /evidence="ECO:0007829|PDB:4II2"; HELIX 539..552; /evidence="ECO:0007829|PDB:4II2"; HELIX 579..581; /evidence="ECO:0007829|PDB:4II2"; HELIX 592..597; /evidence="ECO:0007829|PDB:4II2"; HELIX 602..617; /evidence="ECO:0007829|PDB:4II2"; HELIX 619..627; /evidence="ECO:0007829|PDB:4II2"; HELIX 633..637; /evidence="ECO:0007829|PDB:4II2"; HELIX 644..655; /evidence="ECO:0007829|PDB:4II2"; HELIX 663..678; /evidence="ECO:0007829|PDB:4II2"; HELIX 680..688; /evidence="ECO:0007829|PDB:4II2"; HELIX 719..735; /evidence="ECO:0007829|PDB:4II2"; HELIX 744..752; /evidence="ECO:0007829|PDB:4II2"; HELIX 788..792; /evidence="ECO:0007829|PDB:4II2"; HELIX 797..799; /evidence="ECO:0007829|PDB:4II2"; HELIX 819..833; /evidence="ECO:0007829|PDB:4II2"; HELIX 841..848; /evidence="ECO:0007829|PDB:4II2"; HELIX 856..874; /evidence="ECO:0007829|PDB:4II2"; HELIX 880..882; /evidence="ECO:0007829|PDB:4II2"; HELIX 890..892; /evidence="ECO:0007829|PDB:4II2"; HELIX 927..936; /evidence="ECO:0007829|PDB:4II2"; HELIX 959..963; /evidence="ECO:0007829|PDB:4II2"; HELIX 970..977; /evidence="ECO:0007829|PDB:4II2" TURN 305..307; /evidence="ECO:0007829|PDB:4II2"; TURN 349..351; /evidence="ECO:0007829|PDB:4II2"; TURN 450..452; /evidence="ECO:0007829|PDB:4II2"; TURN 472..474; /evidence="ECO:0007829|PDB:4II2"; TURN 518..520; /evidence="ECO:0007829|PDB:4II2"; TURN 573..575; /evidence="ECO:0007829|PDB:4II2"; TURN 638..640; /evidence="ECO:0007829|PDB:4II2"; TURN 656..658; /evidence="ECO:0007829|PDB:4II2"; TURN 780..782; /evidence="ECO:0007829|PDB:4II3"; TURN 915..917; /evidence="ECO:0007829|PDB:4II2"; TURN 964..967; /evidence="ECO:0007829|PDB:4II2" CHAIN 1..1012; /note="Ubiquitin-activating enzyme E1 1"; /id="PRO_0000194976" MSNNMNIDQTDQNTIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKSVTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVDELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIFCDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFTEVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKISFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPRNDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGGAVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQIAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTDMDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERVGPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLGTKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLFEGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSFEECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLSFDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKSGIKIQVNENEEAPETAANKDKQELKSIADSLPPPSSLVGFRLTPAEFEKDDDSNHHIDFITAASNLRAMNYDITPADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKNGFFNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQKEEGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPFRKHLVLEICCDDANGEDVEVPFICIKL O94614 CHR4_SCHPO MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1289.01c; CHAIN 1..633; /note="Chitin synthase regulatory factor 4"; /id="PRO_0000076207" MDSASSMRNRSPLGVPEFSYSSQSVNNIRGIKSRNRSSIGHSITDPQVASRINAFYLSNVQSSIPFETDAIGPAYGIGDMIAPEMNDTQSLSASVTNMKKENFYSRPNVSSSSILLTIKRATSSQETKRDRPLPNIRNSAPSATRSHSTPCVAPGYLRTSNEAADVVFPHEEAHFSNHNPKPNNGSPLQKQVVADLPFPLPVSDEEQLDWIRANEDLVHSQDIDEALEWAEYVLRFTQSHLPYLQTYESENLHEINYLESMCENALYKIREFSELENAKAMYFDAYVYETGAFDVESDIQRAWDLYSSSANLGYTRSLYRLGVLLEDQGNLEEAVEYFEKGVSENDSACCWRLSLLILEGMLDGVGEYAHRHASGLELLERSADTADADVPSGLYSHALVNLHEHPGLVDLGSENIRVPIDEATALKSFAKAAFLGHSSAQLRMGAVYEFGKYGCPVVPRYSLFYYSAAAKRGETEADLAVAKWYLNGSDGIPVDEDLAFMHAERASMAGNANAQFLMGYLFDTRGNTEQATYWYNEAAKAGHSEAIERLALLENQIQEPEPENITSSQYPNQDVIKEIPVTASETSPPHAPAVSSTPVTSAPPVSQTKVTKVSVPKKTSKKFLIKHNKCIIS O94623 REV1_SCHPO BINDING 240; /ligand="dCTP"; /ligand_id="ChEBI:CHEBI:61481"; /evidence="ECO:0000250"; BINDING 283..287; /ligand="dCTP"; /ligand_id="ChEBI:CHEBI:61481"; /evidence="ECO:0000250"; BINDING 283; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"; BINDING 283; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"; BINDING 284; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"; BINDING 317..323; /ligand="dCTP"; /ligand_id="ChEBI:CHEBI:61481"; /evidence="ECO:0000250"; BINDING 329; /ligand="dCTP"; /ligand_id="ChEBI:CHEBI:61481"; /evidence="ECO:0000250"; BINDING 378; /ligand="dCTP"; /ligand_id="ChEBI:CHEBI:61481"; /evidence="ECO:0000250"; BINDING 378; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"; BINDING 379; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00216" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions. {ECO:0000250}; SPBC1347.01c; CHAIN 1..935; /note="DNA repair protein rev1"; /id="PRO_0000361684" MAFNQRKRRRPVGIADFDEANDEAYESVGFHDYADYFSRKQRKLQNQNAALYKSIDEDSKSDLFHGLAIAINGYTKPSYTELRQMIVSNGGTFIQYVDGKTSISYLVCSFLTPSKARQWKHQKVVKPEWIVDCIKQKKILPWINYRTFQASSAQATLSFVASKPSQPEGNLEDIQTSSQEEEHDNEKDKTKESKAKGFLDDLSGLSASSLHNYQLLKNPNVRNSTTQNQDFLENFFSSSRLHHLSTWKADFKNEIQAMTTASEPVRPIMKDKSKKSRFLLHVDFDCFFASVSTRFSHELRLKPVAVAHGIKNSEIASCNYEARKFGIKNGMYVGTAKNLCPSLRVVDYDFGAYESVSREFYTILVNTLHDYIKVISIDEALLDITSSVSSFQDCFEIAESIRSQVREKTNCEVSVGIGPNVLLARLALRKAKPHNVYSLSIENVFDVLSPLSVQDLPGVGSSQAQKLFNLYGVRTIGQLQRIEKFNLQETFGVNYGLHLYNISRGIDTDIINNETPRRSISVDVNWGVRFVFQEDGIDFLKRLLHELLSRMGKCQVLLHQIQLRILKRADGAPFSPPKYLGAGEVTSFTKSSTFTSATNSFDLIWKKVTSMYKTINVDPGDVRGIGLQALKIIKDNSKIRKDYRSIQSITSRNKVSLKGASVDISSKDKEIISQKKQLSPKLIPSTPYDLPSSSQISSSALAQLPPSMQSDIQQQLRLQKRSITEYPSQLDPLFMVELPTPIRNEVNDNHEIAMNKRLSLKSHADNKIDERGKKKIRQENAFDKLLQISKKSKTINKPNVDYLTLKELPKDLQKQILKESNLQKSDLISEVKLEKPHIVTFQHVQSLEDLRGLLTKWYSKASKGPNIHDVNYFANYVCRVIREEKNLGKAQMMLKWLYQLNRKECNKPWEKAIDKIIETVQGECLQRNIPPLMIF O94632 EGT1_SCHPO BINDING 51; /ligand="L-histidine"; /ligand_id="ChEBI:CHEBI:57595"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 85; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 91; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 112; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 142..143; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 172; /ligand="L-histidine"; /ligand_id="ChEBI:CHEBI:57595"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 212; /ligand="L-histidine"; /ligand_id="ChEBI:CHEBI:57595"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 287..289; /ligand="L-histidine"; /ligand_id="ChEBI:CHEBI:57595"; /evidence="ECO:0000250|UniProtKB:A0R5M8"; BINDING 382; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:G7CFI3"; BINDING 476; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:G7CFI3"; BINDING 480; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:G7CFI3" CATALYTIC ACTIVITY: Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, ChEBI:CHEBI:15378, ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.44; Evidence={ECO:0000250|UniProtKB:Q7RX33}; CATALYTIC ACTIVITY: Reaction=hercynine + L-cysteine + O2 = H2O + S-(hercyn-2-yl)-L-cysteine S-oxide; Xref=Rhea:RHEA:42704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:15781, ChEBI:CHEBI:35235, ChEBI:CHEBI:82706; EC=1.21.3.10; Evidence={ECO:0000250|UniProtKB:Q7RX33}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q7RX33}; Note=Binds 1 Fe(2+) ion per monomer. {ECO:0000250|UniProtKB:Q7RX33}; SPBC1604.01; CHAIN 1..773; /note="Ergothioneine biosynthesis protein 1"; /id="PRO_0000278511" MTEIENIGALEVLFSPESIEQSLKRCQLPSTLLYDEKGLRLFDEITNLKEYYLYESELDILKKFSDSIANQLLSPDLPNTVIELGCGNMRKTKLLLDAFEKKGCDVHFYALDLNEAELQKGLQELRQTTNYQHVKVSGICGCFERLLQCLDRFRSEPNSRISMLYLGASIGNFDRKSAASFLRSFASRLNIHDNLLISFDHRNKAELVQLAYDDPYRITEKFEKNILASVNAVFGENLFDENDWEYKSVYDEDLGVHRAYLQAKNEVTVIKGPMFFQFKPSHLILIEESWKNSDQECRQIIEKGDFKLVSKYESTIADYSTYVITKQFPAMLQLPLQPCPSLAEWDALRKVWLFITNKLLNKDNMYTAWIPLRHPPIFYIGHVPVFNDIYLTKIVKNKATANKKHFWEWFQRGIDPDIEDPSKCHWHSEVPESWPSPDQLREYEKESWEYHIVKLCKAMDELSTSEKRILWLCYEHVAMHVETTLYIYVQSFQNANQTVSICGSLPEPAEKLTKAPLWVNVPETEIAVGMPLTTQYTSVGSNLQSSDLSAHENTDELFYFAWDNEKPMRKKLVSSFSIANRPISNGEYLDFINKKSKTERVYPKQWAEIDGTLYIRTMYGLLPLDDYLGWPVMTSYDDLNNYASSQGCRLPTEDELNCFYDRVLERTDEPYVSTEGKATGFQQLHPLALSDNSSNQIFTGAWEWTSTVLEKHEDFEPEELYPDYTRDFFDGKHNVVLGGSFATATRISNRRSFRNFYQAGYKYAWIGARLVKN O94640 SIR2_SCHPO ACT_SITE 266; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" BINDING 164..183; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 246..249; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 274; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 277; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 298; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 301; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 373..375; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 398..400; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 416; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; MOD_RES 55; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16D10.07c; CHAIN 1..475; /note="NAD-dependent histone deacetylase sir2"; /id="PRO_0000110279" MASNPLDNNMPTTPVEEKIPVASYSPSSSGSSSGASLLVDIMCGSKETEDEEVDSDEWDKPETENISDLDERSEMVRYLRASGYAKFLEKYLIEEELPVRSILKKLGINLPSALEEFEDIDLLPLLKEVLKREVARRIKLPHFNTFEDVVNLLKKAKNVVVLVGAGISTSLGILDFRSDNGFYARLARHGLSEPSEMFDIHTFRENPEIFYTFARDLLPETNHYSPSHAFIRLLEKKNKLSTLFTQNIDNLEKKTGLSDNKIIQCHGSFATATCIKCKHKVDGSELYEDIRNQRVSYCNECGKPPLKLRRVGQNKKEKHYFSDGDSESSEDDLAQPGIMKPDITFFGEALPDSFFNKVGSGELEETDLLICIGTSLKVAPVSELISVIPPTTPQIYISRTPVRHTQFDVNFLSPYCDWVIVEICKRAGWLNELQALCDLPECHSGSKTRAFETDLDIKFEEPSTYHITSTTNGSC O94641 HS104_SCHPO BINDING 209..216; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 621..628; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255" SPBC16D10.08c; CHAIN 1..905; /note="Heat shock protein 104"; /id="PRO_0000372308" MADYPFTDKAAKTLSDAYSIAQSYGHSQLTPIHIAAALLSDSDSNGTTLLRTIVDKAGGDGQKFERSVTSRLVRLPAQDPPPEQVTLSPESAKLLRNAHELQKTQKDSYIAQDHFIAVFTKDDTLKSLLAEAGVTPKAFEFAVNNVRGNKRIDSKNAEEGFDALNKFTVDLTELARNGQLDPVIGREDEIRRTIRVLSRRTKNNPVLIGEPGVGKTSIAEGLARRIIDDDVPANLSNCKLLSLDVGSLVAGSKFRGEFEERIKSVLKEVEESETPIILFVDEMHLLMGAGSGGEGGMDAANLLKPMLARGKLHCIGATTLAEYKKYIEKDAAFERRFQIILVKEPSIEDTISILRGLKEKYEVHHGVTISDRALVTAAHLASRYLTSRRLPDSAIDLVDEAAAAVRVTRESQPEVLDNLERKLRQLRVEIRALEREKDEASKERLKAARKEAEQVEEETRPIREKYELEKSRGSELQDAKRRLDELKAKAEDAERRNDFTLAADLKYYGIPDLQKRIEYLEQQKRKADAEAIANAQPGSEPLLIDVVGPDQINEIVARWTGIPVTRLKTTEKERLLNMEKVLSKQVIGQNEAVTAVANAIRLSRAGLSDPNQPIASFLFCGPSGTGKTLLTKALASFMFDDENAMIRIDMSEYMEKHSVSRLIGAPPGYVGHEAGGQLTEQLRRRPYSVILFDEIEKAAPEVLTVLLQVLDDGRITSGQGQVVDAKNAVIIMTSNLGAEYLTTDNESDDGKIDSTTREMVMNSIRGFFRPEFLNRISSIVIFNRLRRVDIRNIVENRILEVQKRLQSNHRSIKIEVSDEAKDLLGSAGYSPAYGARPLNRVIQNQVLNPMAVLILNGQLRDKETAHVVVQNGKIFVKPNHEANANGSADIDMDGIDDDVNDEELE O94649 ATG2_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:30911189}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:30911189}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:30911189}; SPBC31E1.01c; STRAND 40..42; /evidence="ECO:0007829|PDB:6A9J"; STRAND 55..62; /evidence="ECO:0007829|PDB:6A9J"; STRAND 80..93; /evidence="ECO:0007829|PDB:6A9J"; STRAND 98..100; /evidence="ECO:0007829|PDB:6A9J"; STRAND 103..115; /evidence="ECO:0007829|PDB:6A9J"; STRAND 185..196; /evidence="ECO:0007829|PDB:6A9J"; STRAND 205..216; /evidence="ECO:0007829|PDB:6A9J"; STRAND 224..229; /evidence="ECO:0007829|PDB:6A9J"; STRAND 232..234; /evidence="ECO:0007829|PDB:6A9J" HELIX 21..39; /evidence="ECO:0007829|PDB:6A9J"; HELIX 46..54; /evidence="ECO:0007829|PDB:6A9J"; HELIX 67..73; /evidence="ECO:0007829|PDB:6A9J"; HELIX 95..97; /evidence="ECO:0007829|PDB:6A9J"; HELIX 139..148; /evidence="ECO:0007829|PDB:6A9J"; HELIX 150..160; /evidence="ECO:0007829|PDB:6A9J"; HELIX 174..184; /evidence="ECO:0007829|PDB:6A9J" CHAIN 1..1646; /note="Autophagy-related protein 2"; /id="PRO_0000297691" MRLPSWLKNSSSWLWTAALSRTVQRRLLAFALRKLIGSILLENVQPEDIDILFSKGVLMLSNLQLNCSFLNAVVSLPMINFTKGTLRRLILRLNVTDIVNLNVELEVNGLSLEIELVPPDESLSSTTYEDAPSQLDILDNVVEYMNKTASQDFEDEVINEGLESEIDGSSHNLLDSILQKCLASTSVLMQDALVYIGTANMSTRLEAKLDFMSFSSVKSNSTSRLLNINGITVSMVRPISKSNAGSSSPPRSEESFVSMDSSSSIVEGFENDLSPSQVTLNESSIISSNREEESFYSVHDSVTQKKTRTSWLIFQCSGEFRLVFSIESSNLLVIESHVPSCVLNINSQVIAFLLYLYGYFLPAPSTPGFSSNKPPLTMLQLDIHISSVQILTHCKLPESQDFSMHNDVDELLHTIPSNGAVFEMKINQIQIFNDNNDIDELTMTFSDLDIFMDSVTLVSFGKSLQSPCSLIFKKLERIVSLFIHIPGGEISLPLGKALLLQESFVEFTNDISNLQNFLSNSDPFKRSIQETFEAPKPFEVEMNQPSFEIIALFDELQLQILNELSTQSLYKLTLRVSHLQFTRKSTGSLSSVLIFVKKIGCQSELFNCENSDWTKVSSSTAFHLSNSLFETHDTTGTSNFAVSIQQEKHYYPVFQPAPTEFSYPEKHFYFAVDNFNVFISKEVVRLFKTLYETIASSLVTPVTPNKLVTSDYKNVLKIRTRTFSLSLLNDDGSSFALKCIRIKHYMCWAGAQLISLSLRLYNVSAEYLSESLEILPVVSFIRNLRNDEKYLLNADFSYALKRSSGSNDNTIFVKITDLGYEHYPTCPWISDLLKTYFPQDPEVPFLAFPDFPFNIKLDLRESIIGLNPRTLEAKLLLYLKSLDVEIDALVASNPLNIRIMAAETVVYIIDKLNQSVLEGKTSVLKREILNSSLHFPGLSIKDTIEFVVKSLGYVEISQLKNLTLSLVVNAEEGVFSTLITVDNLDAQVQSCADSTELLIKVLSDLGSTEDEEISDCYLALPIEDYAKSLTEVDYNFFENRGIDYKSNPTEQSTVLVSSDNDISSQEIKIVDDYYISSNEHSTHASDLASVSSEEFVIDDGSSSIIDISDELQDESSSRDSLKKGIELIEDYYLSQSTSKLESSVEGKNYLLKVKFKDINVNWDLHDGYDWEATRATISSAIEKLCDSSSQNDKISPEAKTLLFQSIVIKSFSKVGRLNINHVSEPIDSDEFADYLSKSISYHLRLGKSKSKKIGIEIKDLQGSFTVYADSNEPNAVLNDLDIGLKDLIIYDHLSTSTWNKFFGRDSRSPSSKNRNQHMNAQIVTVRPLPELNNRELRLEFSVLPCKMYIDQDTLDFLIRFLTFQTPSSSETLNTEPDLPFFQSICINATHVTIDFKFKSADKVGLRSGKLPDLGSLIVMQGSEVFLRQLQIYGLSGAEEFLNALLNVWLQDIRNNQLSKVLNGVVPIRTMFTVGRGIKDIFVSPVRGLQGNHSVGSFRHGIIKFTEKYVNDFLSLNAQGATGTHSLLRQAESYLERGSNASASASRARSYYAEQPETIEQGLRQGYSGLKQGLLGAKSTLMGLPRETRSHKSLGGVAQTVGRKVPLIVLQPMIGATEAVSKTLLGLSNSLQPQRRQDMREKYKRPG O94652 GLE1_SCHPO SPBC31E1.05; CHAIN 1..480; /note="mRNA export factor gle1"; /id="PRO_0000363391" MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWAKKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKHKENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFARLQKNCPWVIPFWYDHGTENGKKKMGFKKLSDGHWEQNTTYNERQCGIFAVYAAILSLDDSLAPESWRTFSRLLNLPSPSQLMKSDLELGQTLCSIVSTYLDIAGQSLLRIYGRQAKKLIVCSFSEAYLGANGGGSQYGRLRIVGEDWMKGQGGLKFSFEP O94655 YPT7_SCHPO BINDING 17..23; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 33..40; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 66; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 125..128; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 157..159; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939" MOD_RES 205; /note="Cysteine methyl ester"; /evidence="ECO:0000250|UniProtKB:P36586" SPBC405.04c; CHAIN 1..205; /note="Ypt/Rab-type GTPase ypt7"; /id="PRO_0000121313" LIPID 203; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P36586"; LIPID 205; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P36586" MAGKKKHLLKVIILGESGVGKTSIMNQYVNRKFSKDYKATIGADFLTKEVLVDDKVVTLQLWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFETLDSWRDEFLIQASPSNPETFPFILLGNKVDVEEQKRMVSKSKALAFCQARGEIPYFETSAKEAINVQEAFETVAKLALENMDSDDIAADFTDPIHLDMESQKTSCYC O94679 CND1_SCHPO SPBC776.13; CHAIN 1..1158; /note="Condensin complex subunit 1"; /id="PRO_0000095043" MSLDLLSRLKKYIHDEENSDLDSIYAECENAGLTAVVNDVIDTLLLGTSSCFDEDCLEKLFAICSHFADLSSSVRNKVYDLLTSNISSESAILEDMISANATDFTVPQTNLETTGIAFQLTVNSLSSSNQLSVIRSSTNTVKGRKKNPTTNSNWNGISHVNALLDAIITLFQKKLSRVWTTSSERDMFLSLFLKPIYTLMESEINIKNASFRSRLFNIIGLAVQFHNHTTAAETNIIQNLQYFEHLSEYAADLVHIVTVQFNSVTLAEGIIRTLCSLEFNDNDVKGPKQVALFLVRLSSLIPNLCLKQLTQLVKLLDSESYTLRCAIIEVLANVVIDQIHDEAQNEMSESVPATVQSLMDLLSERLLDISPYCRTKVLHVFIKIFDLPIKYPRKRQEIAELVIRCLQDRSSHVRRNAIKLFSKLLTTHPFSVMHNGLLTRNIWEKGLSIIEEQLNSLQPKQQEKVVDSELEVDENLLEDATMIQDDESHEGESHLENSLSEYVDSVPAEEIVKVNLTKRFYLEALQYIDIVEAGAKIISQLLFAKNKSEVIESMDFFVFCNSFGISSSKLYIKKMIHLIWVKGTSDEGNNIQNHVLSCYKTLFFEPPPNSGTNEAANYIARNLISLTYDASLAELTSLEQMLCILMKDGYFSHLVITKLWQVYSYQKKDISRTQRRGSIIVIGMLALGNTDVVMQGLDHLIQIGLGPPGLEDLVLARYTCIAIKRIGKDASGSSNINFPNSHTLCQKLCMLLLRPSFSEEWFGLEEQAIEAIYAVAKHPDELCTNIILLLTKQLFKPSNHENTTSNDDHAMDEDLDDSPEEETLKDEEEIGIRLAHLIFLVGHVAIKQLVYIEYCEAEFKRRKADAERLAVQNSNNPINGQETSEYDLITGTSEDDFSEAMTFIRERELLYGENSLLSRFAPLVVELCSNHKSHNNQSLLLAASLTLSKFMCLSNNFCMEHLPLLITILEKCDNPIIRNNLVIGLADLTVCFNHFIDEISEYLYRRLMDEESSVKKTCFMTLAFLILAGQIKVKGQLGIMARSLEDEDARISDLARMFFTDFAAKDNSVYNNFIDIFSVLSRSAEEQDEDDAKFKRIIRFLTSFIEKERHTKQLAERLAARLDRCKTQRQWDHVVYALSLLPHKADNIQKLIDDGYHE O94680 PDAT_SCHPO ACT_SITE 293; /note="Acyl-ester intermediate"; /evidence="ECO:0000250|UniProtKB:Q8NCC3"; ACT_SITE 535; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q8NCC3"; ACT_SITE 586; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q8NCC3" BINDING 136; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q8NCC3"; BINDING 294; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q8NCC3" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a monoacylglycerophospholipid + a triacyl-sn-glycerol; Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615, ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158; Evidence={ECO:0000269|PubMed:12963726}; SPBC776.14; CHAIN 1..632; /note="Phospholipid:diacylglycerol acyltransferase"; /id="PRO_0000058267" MASSKKSKTHKKKKEVKSPIDLPNSKKPTRALSEQPSASETQSVSNKSRKSKFGKRLNFILGAILGICGAFFFAVGDDNAVFDPATLDKFGNMLGSSDLFDDIKGYLSYNVFKDAPFTTDKPSQSPSGNEVQVGLDMYNEGYRSDHPVIMVPGVISSGLESWSFNNCSIPYFRKRLWGSWSMLKAMFLDKQCWLEHLMLDKKTGLDPKGIKLRAAQGFEAADFFITGYWIWSKVIENLAAIGYEPNNMLSASYDWRLSYANLEERDKYFSKLKMFIEYSNIVHKKKVVLISHSMGSQVTYYFFKWVEAEGYGNGGPTWVNDHIEAFINISGSLIGAPKTVAALLSGEMKDTAQLNQFSVYGLEKFFSRSERAMMVRTMGGVSSMLPKGGDVVWGNASWAPDDLNQTNFSNGAIIRYREDIDKDHDEFDIDDALQFLKNVTDDDFKVMLAKNYSHGLAWTEKEVLKNNEMPSKWINPLETSLPYAPDMKIYCVHGVGKPTERGYYYTNNPEGQPVIDSSVNDGTKVENGIVMDDGDGTLPILALGLVCNKVWQTKRFNPANTSITNYEIKHEPAAFDLRGGPRSAEHVDILGHSELNEIILKVSSGHGDSVPNRYISDIQEIINEINLDKPRN O94684 TFB3_SCHPO SPBC776.18c; CHAIN 1..318; /note="RNA polymerase II transcription factor B subunit 3"; /id="PRO_0000055940" MDDEGARKVDEKCPLCQADRYLNPNMKLLINPECYHKMCESCVDRIFTTGPAQCPTPGCNKILRKAKFREQTFEDAQIEREVDVRKRISRIFNKGQQEFDSLQAYNDYLEEVEILTFNLIYKIDVEETEEKVKQYEKQNRDSIAANSARAAAEARILAQNEILLKRQKQEAREAAIREHQKEKERREQVEQQIIFDLATSGKDPNKIIQLSDSLKKQQENIASSVSNISRSSSILLSDVQQVAEDTTPFSPLAGEKDGSKYFSYSKNTYQDLYLEKVSHEPGRKCGFRIEDCHLRCLYEAFSGIDYDLESLKKLEVAS O94687 TAS3_SCHPO SPBC83.03c; HELIX 9..11; /evidence="ECO:0007829|PDB:3TIX"; HELIX 12..17; /evidence="ECO:0007829|PDB:3TIX"; HELIX 29..49; /evidence="ECO:0007829|PDB:3TIX"; HELIX 50..53; /evidence="ECO:0007829|PDB:3TIX"; HELIX 58..79; /evidence="ECO:0007829|PDB:3TIX"; HELIX 435..444; /evidence="ECO:0007829|PDB:3D1B"; HELIX 447..450; /evidence="ECO:0007829|PDB:3D1B"; HELIX 453..467; /evidence="ECO:0007829|PDB:3D1B"; HELIX 473..481; /evidence="ECO:0007829|PDB:3D1B"; HELIX 495..505; /evidence="ECO:0007829|PDB:3D1B"; HELIX 510..526; /evidence="ECO:0007829|PDB:3D1B"; HELIX 530..543; /evidence="ECO:0007829|PDB:3D1B" CHAIN 1..549; /note="RNA-induced transcriptional silencing complex protein tas3"; /id="PRO_0000256153" MEKGIKKYLPSLPFLACISDFPENHGTSRRSATVSLERVHELFTEHWLSNLKNRREKRQELAEEAVYCRSEMLSQRKLLAAVDFPQQLKNSPAKAKATHTSSGVTKEVRASKKYTSSNVEFPLVTDGKEKPVKSKQLRKNSVTEFEKPIETKKSKHRKSRNKFLDKSSGSMEIESWDNSTSDSIIESSSRLHESISLRENDIRSSDSKSVGWDDNSTGFRESSKSLDHTDTSMFMELDSNSDPQFRPKYQAKSSWFAPDDPEASWGNLDDGWGETNGSWSSTDDTKHYKNEWAESINLDNFNRPSQQEDYDKPKNTQVSRSSNHHRRYDSYHPDSRSDSYRSKREHYDNRDTGPRSKHLEKSSYVYNQNFEDRTHLSDHGAHFHLGNANDFNMQGSSRKRKASDRQRESRENELPTKKLNASDSHNPLASLTTDKNDLYINWLKSLSFFQTNSSCAEALVKVIPHYHNKLIDFSQVLQLVFSASEKFPIQENQPLPEQLMFLSNLEKQTPFAKAVGSSIYKLVTGKNLSLDFASQILKEASILEHKNEK O94701 INN1_SCHPO SPBC83.18c; CHAIN 1..272; /note="Ingression protein fic1"; /id="PRO_0000303953" MSKNPLGTLVVRIWKAKNLPNKALVGKQSPYCVCRVGEVVKRTQTDKRSGQEPSWNAVLEFNIPSESYHIMKITVFHEGFRKHPHLIGDTVLSFEKAMKEELQSEWYELKNEFQFAGELSVQFKFIPTDPLYFDRASSKPVLQFPYSSVAALTPVPKKPSKPSKPRKKVPVSHPLPPTPPSREEHVSVPRESSLFTYEDDPLPSFPSPYMVDDYYTQDVFVSDNVNDYSYGVQNPTNPRLSVEDYDANHSSLPPVPPPHLILPTASSSQIFH O94720 FIL1_SCHPO SPCC1393.08; CHAIN 1..557; /note="Transcription factor fil1"; /id="PRO_0000310832" MNYNDTTEFCFPFGQPSFPTSAMTEGSFDGQFSEFDPTFTSPADTALSDIANLPIDLHKDALFANAPGKGDVDFDSVSMLQLLSDYPLAFNSTENNQKLQTNPSARWSLLDSMDFDNQRQCSDLESAQLGDSGLLKSTILSNSHIDIAALSSSKTSEPTPPFSYVQTPCIPTPSSALIDTPFPGALDSEFGFDESQAPLFPASDGDCQRAFASISYPTNYGCKLSNLGFMSPQSPVKRELNDSTSPSKLSESSSSLTGSSSALLSQSEFLGSVPSLSDSIATVDPFFSFESFETDEKARSLLMDASLKLPQFSTPNLSSNSSSLSLKSTLAEGMKGSTPLAAVKTEKASKAARVMKQKKHREHVCFNCGVTETPLWRRTSDKLNFLCNACGLYNKQYGVMRPLSPRNKGSSKALENLVCANCSSTKTSLWRKDRHGQTVCNACGLYARLHGHNRPIGLKKNKITRRRRGKGPGGEDGMSDEVKSEFPVLSKSVTMAEILSSKGLESPQLTNSVSVSKMPNTDADVSLEHAKISFDSLDNSVIVKKEEEIENKFSVSC O94740 CDC37_SCHPO MOD_RES 238; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC9B6.10; CHAIN 1..466; /note="Hsp90 co-chaperone Cdc37"; /id="PRO_0000195066" MAIDYSKWDKLELSDDSDIEVHPNVDKKSFIRWRQRDIHEKRAVRKQKMEDIKGAMAMNRRLLSRISEMETVLEKESPSDPYVLLGSFLEAKKSEDMDSAIPGGMSYHHMLMSLLKVIKDAEDTTEEKSMDDSDKCLRRLKSHKERLLKLLEDAQKEYDTLEAESKNYITSEDLHLGFDSTYVQKKEPEKPKKTKTKKETIQVIESLNNPTPPTDFPGAKEQASTGNAPKNPVNENESEDEEGLSLSEDGKKFANIDFGDYSSSEEFLKEHLNILADEEESDAILLEAFNAELEGKPSLAKQYVHQALLISYCRQLGPNGLSIFFQKIKDPNHQSQRLFLEDVHNTYVRIHERSAAISKEQAESGEGVEQIQLCAVDPNTKLSITIPEAGSTDPETQKARAAFESFPPNLQKALMTNDLDKINVVLGKMAVENAEEVVEKLSSTGMLSIEEGIIDTTKGETIPQLS O94751 BUB1_SCHPO ACT_SITE 861; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" BINDING 724..732; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 762; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. {ECO:0000250}. MOD_RES 550; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1322.12c; CHAIN 1..1044; /note="Checkpoint serine/threonine-protein kinase bub1"; /id="PRO_0000085675" MSDWRLTENVLDQNIPETKPRESKTRLEEIQRLALFQEELDIIEELDDPVDVWYRCIEWLLETRFLGMETVNKMLDDAIQYLERCRFALNDVRHLLIQLAKIKQSYETPDELQQAAKQFYQLASKGIGLELALFYEEYGSLLIRMQRWKEASEVFHAAVSREARPLVRLLRNAAEFSRAYDLHNAHPSIHDAPYSSPFPPPRIVLGSKPVSSSTLPSKPKSFQVFSDASSSRDSQNASDLPQAKSLESEANTPNLPLLYDKSSGKRVEYSAFNFLALYENGEERSMEECRAQRYLSSIQPNTAASFPKVVPKNEISVHHDSSSSNVSPIYKNPVAEQSDTPTRSLPKNYAYVAKSTSPELKVFDTVMPVALSPKPAQKPPSPTIHTKAALADILDIFNQPLRSESLEKSSKSPISAQSSYLGTPLKNDENSSNSGATSLTGRSQEEHLDFIPSLTPSKNYPSKIYSPNKNLDFSHTASKAETYKNSNELENVKREQPFSELLPSTLQEETATGTTSTTFANAKRRPEDSNISPTNPKKLHTLPRSPQYSTVDSNSVLSPAMPKGYMFVNENQSMKHESSVSNPVATIPHENGKHDFGQLSPIEHKPFFPKNDDELPGPSGYLTMPYEEAMASLSNLPTLINPLDQSLRDLLFQVLRPSLLRDKDYHEHETSFALVEHIESFVSKIKPKAGGPGRRRSSNRHSLDGPEFHLFYPPNTNLSVISKLGQGAFAPVYLVKSKIETENGDVSQGGAENNESKLFALKIETPPSCFEFYLTRQAMTRLKGLRETNSILPVHQLHMFHDTSHLLMDYRPQGSILDLVNSMHNSTFSSSGMDEILVVFFSIEFLRIIEALHTHKIIHGDLKADNALLRLETVADSEWSPIYSPEGLYGWSFKGIYLIDFGRGIDLSLFEEKVKFIADWDTDLQDCIEMREGRPWTYQIDYHGLAAIIYTMLFGQYIETRIEVINGQRRQVLTQRMKRYWNQDLWHRLFDLLLNPTLHVSEENLPMTEELSKIRIEMEEWLVNHSTGGSGLKGLLKSIEKRKI P01129 CDC10_SCHPO MOD_RES 252; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC336.12c; CHAIN 1..767; /note="Start control protein cdc10"; /id="PRO_0000067060" MASANFIRQFELGNDSFSYQKRPEDEPSQPLSNRNINKLNDSSTLKDSSSRIFINSQVLRDGRPVELYAVECSGMKYMELSCGDNVALRRCPDSYFNISQILRLAGTSSSENAKELDDIIESGDYENVDSKHPQIDGVWVPYDRAISIAKRYGVYEILQPLISFNLDLFPKFSKQQQIESSSISKNLNTSSFNTRSPLRNHNFSNPSKSSKNGVHTINNMQSSPSPSSSFLLPLTQIDSQNVKRSNNYLSTSPPILEQRLKRHRIDVSDEDLHPSSQLNDNEASSLFPDTPRLNHSLSFVSLVSSLPPLDQNIMQDYHTSKDILTSIFLDVNFADSSALEAKLSDSLDLDVPIDELGHAALHWAAAVAKMPLLQALIHKGANPLRGNLTGETALMRSVLVTNHLNQNSFGDLLDLLYASLPCTDRAGRTVVHHICLTAGIKGRGSASRYYLETLLNWAKKHASGNNGYMLKDFINYLNHQDKNGDTALNIAARIGNKNIVEVLMQAGASAYIPNRAGLSVANFGIFVENALKQPEDSKQTKVSLMSENLSSKEKTAVPPRQKSRDIIASVTDVISSLDKDFQDEMAAKQSMIDSAYTQLRESTKKLSDLREQLHVSETQRTLFLELRQRCKNLMTSIEEQKSELSNLYESFDPNGIHDSLSLDADAPFTVNENNNKNLSIAELKFQVAAYERNEARLNELANKLWQRNSNIKSKCRRVVSLCTGVDESRVDSLLESLLQAVESDGQQGEVDMGRVAGFLRVVKEHQA P04551 CDK1_SCHPO ACT_SITE 134; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 10..18; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 33; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:11486016}; MOD_RES 14; /note="Phosphothreonine"; /evidence="ECO:0000250"; MOD_RES 15; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:2682257"; MOD_RES 167; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC11B10.09; CHAIN 1..297; /note="Cyclin-dependent kinase 1"; /id="PRO_0000085720" MENYQKVEKIGEGTYGVVYKARHKLSGRIVAMKKIRLEDESEGVPSTAIREISLLKEVNDENNRSNCVRLLDILHAESKLYLVFEFLDMDLKKYMDRISETGATSLDPRLVQKFTYQLVNGVNFCHSRRIIHRDLKPQNLLIDKEGNLKLADFGLARSFGVPLRNYTHEIVTLWYRAPEVLLGSRHYSTGVDIWSVGCIFAEMIRRSPLFPGDSEIDEIFKIFQVLGTPNEEVWPGVTLLQDYKSTFPRWKRMDLHKVVPNGEEDAIELLSAMLVYDPAHRISAKRALQQNYLRDFH P04688 TBA1_SCHPO ACT_SITE 258; /evidence="ECO:0000250|UniProtKB:P68363" BINDING 11; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 75; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 75; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 144; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 148; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 149; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 183; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 210; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 232; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; SPBC16A3.15c; CHAIN 1..455; /note="Tubulin alpha-1 chain"; /id="PRO_0000048225" MREVISVHVGQAGVQIGNACWELYCLEHGIGPDGFPTENSEVHKNNSYLNDGFGTFFSETGQGKFVPRSIYVDLEPNVIDQVRTGPYKDLFHPEQMVTGKEDASNNYARGHYTVGKEMIDSVLERIRRMADNCSGLQGFLVFHSFGGGTGSGLGALLLERLNMEYGKKSNLQFSVYPAPQVSTSVVEPYNSVLTTHATLDNSDCTFMVDNEACYDICRRNLDIERPTYENLNRLIAQVVSSITASLRFAGSLNVDLNEFQTNLVPYPRIHFPLVTYSPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRTGRYMATCLLYRGDVIPRDVQAAVTSIKSRRTIQFVDWCPTGFKIGICYEPPQHVPGSGIAKVNRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVGQDSMDNEMYEADEEY P04689 TBA2_SCHPO ACT_SITE 254; /evidence="ECO:0000250|UniProtKB:P68363" BINDING 11; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 71; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 71; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 140; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 144; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 145; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 179; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 206; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 228; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; SPBC800.05c; CHAIN 1..449; /note="Tubulin alpha-2 chain"; /id="PRO_0000048226" MREIISIHVGQAGTQIGNACWELYCLEHGIQPNGYMNPETASQNSDGGFSTFFSETGQGKYVPRSIYVDLEPNVIDQVRTGPYRDLFHPEQLITGKEDASNNYARGHYTVGKELVDEVTDKIRRIADNCSGLQGFLVFHSFGGGTGSGFGALLLERLAMEYTKKSKLQFSVYPAPQVSTSVVEPYNSVLTTHATLDLADCTFMVDNESCYDICRRNLDIERPSYENLNRLIAQVVSSITASLRFEGSLNVDLAEFQTNLVPYPRIHFPLVTYAPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRAGRYMATCLLYRGDVIPRDVQAAVTTIKAKRTIQFVDWCPTGFKIGICDRPPQHIEGSEIAKVDRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVGQDSMEVDYMEEEY P04909 H2A1_SCHPO PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. {ECO:0000269|PubMed:15226425}.; PTM: Acetylated by esa1 to form H2AK4ac and H2AK7ac. {ECO:0000250}. MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250"; MOD_RES 5; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 9; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 106; /note="N5-methylglutamine"; /evidence="ECO:0000269|PubMed:24352239"; MOD_RES 129; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15226425, ECO:0000269|PubMed:24806815" SPCC622.08c; CHAIN 2..132; /note="Histone H2A-alpha"; /id="PRO_0000055324" MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKTSGRTGKPSQEL P04910 H2A2_SCHPO PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. {ECO:0000269|PubMed:15226425}.; PTM: Acetylated by esa1 to form H2AK4ac and H2AK7ac. {ECO:0000250}. MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250"; MOD_RES 5; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 9; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 106; /note="N5-methylglutamine"; /evidence="ECO:0000269|PubMed:24352239"; MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15226425" SPAC19G12.06c; CHAIN 2..131; /note="Histone H2A-beta"; /id="PRO_0000055325" MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKQSGKGKPSQEL P04913 H2B1_SCHPO PTM: Monoubiquitinated by the rhp6/ubc2-bre1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation (By similarity). {ECO:0000250}.; PTM: Phosphorylated by shk1 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation (By similarity). {ECO:0000250}.; PTM: Acetylation of N-terminal lysines and particularly formation of H2BK11ac has a positive effect on transcription. {ECO:0000250}.; PTM: Sumoylation to form H2BK6su or H2BK7su occurs preferentially near the telomeres and represses gene transcription. {ECO:0000250}. MOD_RES 6; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 7; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 11; /note="N6-acetyllysine"; /evidence="ECO:0000250" SPCC622.09; CHAIN 2..126; /note="Histone H2B-alpha"; /id="PRO_0000071937" MSAAEKKPASKAPAGKAPRDTMKSADKKRGKNRKETYSSYIYKVLKQVHPDTGISNQAMRILNSFVNDIFERIATEASKLAAYNKKSTISSREIQTAVRLILPGELAKHAVTEGTKSVTKYSSSAQ P05219 TBB_SCHPO BINDING 11; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509"; BINDING 69; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 69; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P68363"; BINDING 138; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509"; BINDING 142; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509"; BINDING 143; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509"; BINDING 144; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509"; BINDING 204; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509"; BINDING 226; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q13509" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; SPBC26H8.07c; CHAIN 1..448; /note="Tubulin beta chain"; /id="PRO_0000048430" MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYVPRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVVRREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVVEPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSFRFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMMVAADPRHGRYLTVAALFRGKVSMKEVDEQIRSVQTKNSAYFVEWIPDNVLKAVCSVPPKDLKMSATFIGNSTSIQEIFRRLGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEAGIDEGDEDYEIEEEKEPLEY P05764 RS21_SCHPO MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000269|PubMed:3910104" SPBC18E5.06; CHAIN 1..87; /note="Small ribosomal subunit protein eS21"; /id="PRO_0000194760" MENEAGQLVDLYVPRKCSATNRIIQAKDHASVQINVCAVDAEGRQIPGEKTTYAISGFVRSKGESDDCINRLTTQDGLLEGVWSYQR P05933 CALM_SCHPO BINDING 22; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 24; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 26; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 28; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 33; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 58; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 60; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 62; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 64; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 69; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 95; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 97; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 99; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 101; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 106; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 131; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 133; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 135; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 142; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SPAC3A12.14; CHAIN 1..150; /note="Calmodulin"; /id="PRO_0000198327" MTTRNLTDEQIAEFREAFSLFDRDQDGNITSNELGVVMRSLGQSPTAAELQDMINEVDADGNGTIDFTEFLTMMARKMKDTDNEEEVREAFKVFDKDGNGYITVEELTHVLTSLGERLSQEEVADMIREADTDGDGVINYEEFSRVISSK P06652 MPIP_SCHPO ACT_SITE 480; /note="Phosphocysteine intermediate"; /evidence="ECO:0000250|UniProtKB:Q16828" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:P30303}; PTM: Phosphorylated by srk1 in the N-terminus; phosphorylation promotes nuclear exclusion. {ECO:0000269|PubMed:15629716}. MOD_RES 99; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 178; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24H6.05; CHAIN 1..596; /note="M-phase inducer phosphatase"; /id="PRO_0000198661" MDSPLSSLSFTNTLSGKRNVLRPAARELKLMSDRNANQELDFFFPKSKHIASTLVDPFGKTCSTASPASSLAADMSMNMHIDESPALPTPRRTLFRSLSCTVETPLANKTIVSPLPESPSNDALTESYFFRQPASKYSITQDSPRVSSTIAYSFKPKASIALNTTKSEATRSSLSSSSFDSYLRPNVSRSRSSGNAPPFLRSRSSSSYSINKKKGTSGGQATRHLTYALSRTCSQSSNTTSLLESCLTDDTDDFELMSDHEDTFTMGKVADLPESSVELVEDAASIQRPNSDFGACNDNSLDDLFQASPIKPIDMLPKINKDIAFPSLKVRSPSPMAFAMQEDAEYDEQDTPVLRRTQSMFLNSTRLGLFKSQDLVCVTPKQSTKESERFISSHVEDLSLPCFAVKEDSLKRITQETLLGLLDGKFKDIFDKCIIIDCRFEYEYLGGHISTAVNLNTKQAIVDAFLSKPLTHRVALVFHCEHSAHRAPHLALHFRNTDRRMNSHRYPFLYYPEVYILHGGYKSFYENHKNRCDPINYVPMNDASHVMTCTKAMNNFKRNATFMRTKSYTFGQSVLASPDVNDSPTAMHSLSTLRRF P07334 CDR1_SCHPO ACT_SITE 128; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 18..26; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 41; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 550; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC644.06c; CHAIN 1..593; /note="Mitosis inducer protein kinase cdr1"; /id="PRO_0000085844" MVKRHKNTIGVWRLGKTLGTGSTSCVRLAKHAKTGDLAAIKIIPIRYASIGMEILMMRLLRHPNILRLYDVWTDHQHMYLALEYVPDGELFHYIRKHGPLSEREAAHYLSQILDAVAHCHRFRFRHRDLKLENILIKVNEQQIKIADFGMATVEPNDSCLENYCGSLHYLAPEIVSHKPYRGAPADVWSCGVILYSLLSNKLPFGGQNTDVIYNKIRHGAYDLPSSISSAAQDLLHRMLDVNPSTRITIPEVFSHPFLMGCTSLSSMDSTTPPTPSLSIDEIDPLVVDCMCVLWKKSSSKKVVRRLQQRDDNDEKYVYKVLSEILRDDMLKKQRFDENKYLSLYDLIHDNNLFTKASISTTSLVKSNVSTNSRKSSNFEDELARRVSSPLSALNQMSQSPIPIRVSSDKDYDSYACHEVVSNPSTLDDDYNYMFVCPPEEYTYSTDNVRTDSLDLQSLPTPTLEQLESVPFNRYGYVRIFPSTTLSSTASGYYTPDSLSTPEPSIDGLTNLDDVQVGGFVQGSGNQNRRPISFPVISNMQPNITNVRSASAPLCSSPVPSRRYSQYATNARYTPRKVSSGSVLRKISSFFRKD P07527 WEE1_SCHPO ACT_SITE 693; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 572..580; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 596; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 698; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 711; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; PTM: Phosphorylated in the C-terminal by NIM1/CDR1. SPCC18B5.03; CHAIN 1..877; /note="Mitosis inhibitor protein kinase wee1"; /id="PRO_0000086815" MSSSSNTSSHRSYGLRRSQRSMNLNRATLLAPPTPSSLYDANNSTSSTSSQKPNTSFTSLFGPRKQTTSSPSFSHAAPLHPLSPPSFTHSQPQIQAQPVPRRPSLFDRPNLVSRSSSRLGDSPSLSPVAQVANPIHHTAPSPSDVRAFPIHKNASTGVKRSFFSSSMSNGAMSPPSHSPSPFLQSSQHIPPSTPAQKLRKKNNFDSFRISNSHISPFASGSFSPFATSSPNFLSTSTPAPPNSNNANPSTLFSSIPSSRHTTSNHFPSNSAQSSLFSPTARPLTARKLGFASSQTKSAVSNNHSRNSSKDASFMMKSFIPSNRSHPQTQQNESSLFSDNSMVNSSSNSFSLFPNATLPNPPSSELLTTPFQQIKPPSQVFMSTGLLSKQHRPRKNINFTPLPPSTPSKPSTFVRPHSSSTDSPPSPSTPSNTQTDSYFIQRENTPTNHNSIPTIQLEKSSMDFLRFDPPPSAVKTSHNYGLPFLSNQRCPATPTRNPFAFENTVSIHMDGRQPSPIKSRNNNQMSFAMEEEADVSQPSSSSFTLSFPSALTSSKVSSSTSHLLTRFRNVTLLGSGEFSEVFQVEDPVEKTLKYAVKKLKVKFSGPKERNRLLQEVSIQRALKGHDHIVELMDSWEHGGFLYMQVELCENGSLDRFLEEQGQLSRLDEFRVWKILVEVALGLQFIHHKNYVHLDLKPANVMITFEGTLKIGDFGMASVWPVPRGMEREGDCEYIAPEVLANHLYDKPADIFSLGITVFEAAANIVLPDNGQSWQKLRSGDLSDAPRLSSTDNGSSLTSSSRETPANSIIGQGGLDRVVEWMLSPEPRNRPTIDQILATDEVCWVEMRRKAGAIIYEGIHGSSSNPQGDQMMEDWQVNV P07669 TPIS_SCHPO ACT_SITE 95; /note="Electrophile"; /evidence="ECO:0000250"; ACT_SITE 165; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 10; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 12; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000305|PubMed:3912263}; MOD_RES 105; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC24B10.21; STRAND 5..10; /evidence="ECO:0007829|PDB:7PEK"; STRAND 37..42; /evidence="ECO:0007829|PDB:7PEK"; STRAND 59..64; /evidence="ECO:0007829|PDB:7PEK"; STRAND 68..73; /evidence="ECO:0007829|PDB:7PEK"; STRAND 90..94; /evidence="ECO:0007829|PDB:7PEK"; STRAND 122..127; /evidence="ECO:0007829|PDB:7PEK"; STRAND 160..164; /evidence="ECO:0007829|PDB:7PEK"; STRAND 170..173; /evidence="ECO:0007829|PDB:7PEK"; STRAND 205..211; /evidence="ECO:0007829|PDB:7PEK"; STRAND 228..231; /evidence="ECO:0007829|PDB:7PEK" HELIX 17..28; /evidence="ECO:0007829|PDB:7PEK"; HELIX 45..47; /evidence="ECO:0007829|PDB:7PEK"; HELIX 48..54; /evidence="ECO:0007829|PDB:7PEK"; HELIX 80..85; /evidence="ECO:0007829|PDB:7PEK"; HELIX 96..101; /evidence="ECO:0007829|PDB:7PEK"; HELIX 106..119; /evidence="ECO:0007829|PDB:7PEK"; HELIX 133..135; /evidence="ECO:0007829|PDB:7PEK"; HELIX 139..153; /evidence="ECO:0007829|PDB:7PEK"; HELIX 167..169; /evidence="ECO:0007829|PDB:7PEK"; HELIX 178..196; /evidence="ECO:0007829|PDB:7PEK"; HELIX 198..203; /evidence="ECO:0007829|PDB:7PEK"; HELIX 217..220; /evidence="ECO:0007829|PDB:7PEK"; HELIX 233..236; /evidence="ECO:0007829|PDB:7PEK"; HELIX 240..245; /evidence="ECO:0007829|PDB:7PEK"; HELIX 246..248; /evidence="ECO:0007829|PDB:7PEK" TURN 34..36; /evidence="ECO:0007829|PDB:7PEK"; TURN 214..216; /evidence="ECO:0007829|PDB:7PEK" CHAIN 2..249; /note="Triosephosphate isomerase"; /id="PRO_0000090167" MARKFFVGGNFKMNGSLESMKTIIEGLNTTKLNVGDVETVIFPQNMYLITTRQQVKKDIGVGAQNVFDKKNGAYTGENSAQSLIDAGITYTLTGHSERRTIFKESDEFVADKTKFALEQGLTVVACIGETLAEREANETINVVVRQLNAIADKVQNWSKIVIAYEPVWAIGTGKTATPEQAQEVHAEIRKWATNKLGASVAEGLRVIYGGSVNGGNCKEFLKFHDIDGFLVGGASLKPEFHNIVNVHSL P07799 TOP1_SCHPO ACT_SITE 773; /note="O-(3'-phospho-DNA)-tyrosine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01382, ECO:0000255|PROSITE-ProRule:PRU10130, ECO:0000269|PubMed:2547758" CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130}; MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 54; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 136; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 138; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1703.14c; CHAIN 1..814; /note="DNA topoisomerase 1"; /id="PRO_0000145209" MSSSDSDSVSLSIRRRQRRGSSKRISMKESDEESDSSENHPLSESLNKKSKSESDEDDIPIRKRRASSKKNMSNSSSKKRAKVMGNGGLKNGKKTAVVKEEEDFNEIAKPSPKHKRVSKANGSKNGAKSAVKKEESDTDDSVPLRAVSTVSLTPYKSELPSGASTTQNRSPNDEEDEDEDYKWWTSENIDDTQKWTTLEHNGVIFAPPYEPLPKNVKLIYDGNPVNLPPEAEEVAGFYAAMLETDHAKNPVFQDNFFRDFLKVCDECNFNHNIKEFSKCDFTQMFHHFEQKREEKKSMPKEQKKAIKQKKDEEEEKYKWCILDGRKEKVGNFRIEPPGLFRGRGSHPKTGSLKRRVYPEQITINIGEGVPVPEPLPGHQWAEVKHDNTVTWLATWHENINNNVKYVFLAAGSSLKGQSDLKKYEKSRKLKDYIDDIRKGYRKDLKSELTVERQRGTAMYLIDVFALRAGNEKGEDEADTVGCCSLRYEHVTLKPPRTVVFDFLGKDSIRYYNEVEVDPQVFKNLKIFKRPPKKEGDLIFDRLSTNSLNKYLTSLMDGLSAKVFRTYNASYTMAEELKKMPKNLTLADKILFYNRANRTVAILCNHQRSVTKNHDVQMERFAERIKALQYQRMRLRKMMLNLEPKLAKSKPELLAKEEGITDSWIVKHHETLYELEKEKIKKKFDRENEKLAAEDPKSVLPESELEVRLKAADELKKALDAELKSKKVDPGRSSMEQLEKRLNKLNERINVMRTQMIDKDENKTTALGTSKINYIDPRLTYSFSKREDVPIEKLFSKTIRDKFNWAADTPPDWKW P08092 RAN1_SCHPO ACT_SITE 143; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 24..32; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 47; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 469; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19C2.05; CHAIN 1..470; /note="Negative regulator of sexual conjugation and meiosis"; /id="PRO_0000086602" MMRENPELLLGQVLGDSLRFVSIIGAGAYGVVYKAEDIYDGTLYAVKALCKDGLNEKQKKLQARELALHARVSSHPYIITLHRVLETEDAIYVVLQYCPNGDLFTYITEKKVYQGNSHLIKTVFLQLISAVEHCHSVGIYHRDLKPENIMVGNDVNTVYLADFGLATTEPYSSDFGCGSLFYMSPECQREVKKLSSLSDMLPVTPEPIESQSSSFATAPNDVWALGIILINLCCKRNPWKRACSQTDGTYRSYVHNPSTLLSILPISRELNSLLNRIFDRNPKTRITLPELSTLVSNCKNLTRRLRPAPLVSSRYLAYQQQQQQQQMNLQQGIQGYPHQGYMPTQNIGFPWPPTPQFVSNWNHCATPTIPVSLQVLTPNSSLKVDPTTPLTAPIHATESFWPSAAAAAAAVHNNANSYMPITPTPYPNNAKIFGYPNQPPLTPIPFTGFVLHPAPVGRAADAVDPSRKSL P08096 TOP2_SCHPO ACT_SITE 835; /note="O-(5'-phospho-DNA)-tyrosine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01384" BINDING 136; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P06786"; BINDING 165; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P06786"; BINDING 193..195; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P06786"; BINDING 206..213; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P06786"; BINDING 421..423; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P06786"; BINDING 505; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"; BINDING 582; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"; BINDING 582; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"; BINDING 584; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00995" CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-ProRule:PRU00995}; PTM: Phosphorylated at multiple sites at both extremities of the protein. {ECO:0000269|PubMed:1332977, ECO:0000269|PubMed:18257517}. MOD_RES 1310; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1345; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1433; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1A4.03c; CHAIN 1..1485; /note="DNA topoisomerase 2"; /id="PRO_0000145386" MSIDADFSDYEDEASGDENVLPNTTTKRKASTTSSKSRAKKASTPDLRQTSLTSMTASEQIPLVTNNGNGNSNVSTQYQRLTPREHVLRRPDTYIGSIEPTTSEMWVFDSEKNKLDYKAVTYVPGLYKIFDEIIVNAADNKVRDPNMNTLKVTLDPEANVISIYNNGKGIPIEIHDKEKIYIPELIFGNLLTSSNYDDNQKKVTGGRNGYGAKLCNIFSTEFVVETADKERMKKYKQTWYDNMSRKSEPVITSLKKPDEYTKITFKPDLAKFGMDKIDDDMVSIIKRRIYDMAGTVRETKVYLNNERISISGFKKYVEMYLASDTKPDEEPPRVIYEHVNDRWDVAFAVSDGQFKQVSFVNNISTIRGGTHVNYVANKIVDAIDEVVKKENKKAPVKAFQIKNYVQVFVNCQIENPSFDSQTKETLTTKVSAFGSQCTLSDKFLKAIKKSSVVEEVLKFATAKADQQLSKGDGGLRSRITGLTKLEDANKAGTKESHKCVLILTEGDSAKSLAVSGLSVVGRDYYGVFPLRGKLLNVREASHSQILNNKEIQAIKKIMGFTHKKTYTDVKGLRYGHLMIMTDQDHDGSHIKGLIINYLESSYPSLLQIPGFLIQFITPIIKCTRGNQVQAFYTLPEYEYWKEANNNGRGWKIKYYKGLGTSDHDDMKSYFSDLDRHMKYFHAMQEKDAELIEMAFAKKKADVRKEWLRTYRPGIYMDYTQPQIPIDDFINRELIQFSMADNIRSIPSVVDGLKPGQRKVVYYCFKRNLVHETKVSRLAGYVASETAYHHGEVSMEQTIVNLAQNFVGSNNINLLMPNGQFGTRSEGGKNASASRYLNTALSPLARVLFNSNDDQLLNYQNDEGQWIEPEYYVPILPMVLVNGAEGIGTGWSTFIPNYNPKDITANLRHMLNGEPLEIMTPWYRGFRGSITKVAPDRYKISGIINQIGENKVEITELPIRFWTQDMKEYLEAGLVGTEKIRKFIVDYESHHGEGNVHFNVTLTEAGMKEALNESLEVKFKLSRTQATSNMIAFDASGRIKKYDSVEDILTEFYEVRLRTYQRRKEHMVNELEKRFDRFSNQARFIHMIIEGELVVSKKKKKDLIVELKEKKFQPISKPKKGHLVDLEVENALAEEEQSGDVSQDEDSDAYNYLLSMPLWSLTYERYVELLKKKDEVMAELDALIKKTPKELWLHDLDAFEHAWNKVMDDIQREMLEEEQSSRDFVNRTKKKPRGKSTGTRKPRAIAGSSSSTAVKKEASSESKPSTTNRKQQTLLEFAASKEPEKSSDINIVKTEDNSHGLSVEENRISKSPGLDSSDSGKSRKRSQSVDSEDAGSKKPVKKIAASASGRGRKTNKPVATTIFSSDDEDDLLPSSLKPSTITSTKASAKNKGKKASSVKKQSPEDDDDDFIIPGSSSTPKASSTNAEPPEDSDSPIRKRPTRRAAATVKTPIYVDPSFDSMDEPSMQDDSFIVDNDEDVDDYDESD P08463 CKS1_SCHPO SPBC1734.14c; STRAND 34..42; /evidence="ECO:0007829|PDB:1SCE"; STRAND 61..63; /evidence="ECO:0007829|PDB:1PUC"; STRAND 83..85; /evidence="ECO:0007829|PDB:1SCE"; STRAND 94..100; /evidence="ECO:0007829|PDB:1SCE" HELIX 12..16; /evidence="ECO:0007829|PDB:1PUC"; HELIX 22..24; /evidence="ECO:0007829|PDB:1PUC"; HELIX 45..48; /evidence="ECO:0007829|PDB:1PUC"; HELIX 53..55; /evidence="ECO:0007829|PDB:1PUC"; HELIX 68..73; /evidence="ECO:0007829|PDB:1PUC" TURN 17..21; /evidence="ECO:0007829|PDB:1PUC"; TURN 58..60; /evidence="ECO:0007829|PDB:1PUC" CHAIN 2..113; /note="Cyclin-dependent kinases regulatory subunit"; /id="PRO_0000206246" MSKSGVPRLLTASERERLEPFIDQIHYSPRYADDEYEYRHVMLPKAMLKAIPTDYFNPETGTLRILQEEEWRGLGITQSLGWEMYEVHVPEPHILLFKREKDYQMKFSQQRGG P08647 RAS_SCHPO BINDING 15..22; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 62..66; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 121..124; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112}; PTM: Palmitoylated by the erf2-erf4 complex. {ECO:0000269|PubMed:23843742}. MOD_RES 216; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC17H9.09c; PROPEP 217..219; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281333" CHAIN 1..216; /note="Ras-like protein 1"; /id="PRO_0000082678" LIPID 216; /note="S-farnesyl cysteine"; /evidence="ECO:0000250" MRSTYLREYKLVVVGDGGVGKSALTIQLIQSHFVDEYDPTIEDSYRKKCEIDGEGALLDVLDTAGQEEYSAMREQYMRTGEGFLLVYNITSRSSFDEISTFYQQILRVKDKDTFPVVLVANKCDLEAERVVSRAEGEQLAKSMHCLYVETSAKLRLNVEEAFYSLVRTIRRYNKSEEKGFQNKQAVQTAQVPASTAKRASAVNNSKTEDEVSTKCCVIC P08965 MEI2_SCHPO PTM: Inactivated by phosphorylation by ran1/pat1. SPAC27D7.03c; STRAND 598..602; /evidence="ECO:0007829|PDB:6YYL"; STRAND 624..633; /evidence="ECO:0007829|PDB:6YYL"; STRAND 638..649; /evidence="ECO:0007829|PDB:6YYL"; STRAND 663..666; /evidence="ECO:0007829|PDB:7EIU"; STRAND 669..673; /evidence="ECO:0007829|PDB:7EIU"; STRAND 675..678; /evidence="ECO:0007829|PDB:6YYL"; STRAND 706..708; /evidence="ECO:0007829|PDB:6YYL"; STRAND 717..719; /evidence="ECO:0007829|PDB:7EIU" HELIX 586..590; /evidence="ECO:0007829|PDB:6YYL"; HELIX 610..621; /evidence="ECO:0007829|PDB:6YYL"; HELIX 651..660; /evidence="ECO:0007829|PDB:6YYL"; HELIX 684..691; /evidence="ECO:0007829|PDB:6YYL"; HELIX 695..698; /evidence="ECO:0007829|PDB:6YYL"; HELIX 701..703; /evidence="ECO:0007829|PDB:6YYL" TURN 634..637; /evidence="ECO:0007829|PDB:6YYL"; TURN 713..716; /evidence="ECO:0007829|PDB:6YYL" CHAIN 1..750; /note="Meiosis protein mei2"; /id="PRO_0000081626" MIMETESPLSITSPSPSDSTFQVDMEKTMHALPSSLLDSPLLSTNEHYPPKSTLLLSGPSPIRNIQLSATKSSESNSIDYLTDTQNIFPNFVNNENNYQFSTAPLNPIDACRVGERKVFTTGNVLLSADRQPLSTWQQNISVLSESPPQNGIQSYISSSEQAAQALTRKPSVTGFRSSSLNSNSDDIDIFSHASRYLFVTNLPRIVPYATLLELFSKLGDVKGIDTSSLSTDGICIVAFFDIRQAIQAAKSLRSQRFFNDRLLYFQFCQRSSIQKMINQGATIQFLDDNEGQLLLNMQGGSVLSILQLQSILQTFGPLLIMKPLRSQNVSQIICEFYDTRDASFALDELDGRIIHNCCLQVAYYDAMADSVSTSSASSLSVPRGFSGMLNNNSEWNNSMTMSSNQETPTAASCAVSRIGSSYGMSNNFGSVPLGRTESSPAWGTSGYYDVSSTSPVAPSDRNPSRQYNSIRYGLDVNPIAPPNSSRLKQRNSDLLNGINPQWSPFSSNTGKVFDSPTGSLGMRRSLTVGANASCSNPTNLSFASLTLHDSKADSTLSASSLNPDLNLQRYTPTVEKHASDRNSVDYAQIASGIDTRTTVMIKNIPNKFTQQMLRDYIDVTNKGTYDFLYLRIDFVNKCNVGYAFINFIEPQSIITFGKARVGTQWNVFHSEKICDISYANIQGKDRLIEKFRNSCVMDENPAYRPKIFVSHGPNRGMEEPFPAPNNARRKLRSIASAQQIGLFPPTASKC P09627 PMA1_SCHPO ACT_SITE 376; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250" BINDING 632; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 636; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate; Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1; Evidence={ECO:0000305|PubMed:2891694}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20853; Evidence={ECO:0000305|PubMed:2891694}; MOD_RES 89; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 494; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 899; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1071.10c; CHAIN 1..919; /note="Plasma membrane ATPase 1"; /id="PRO_0000046269" MADNAGEYHDAEKHAPEQQAPPPQQPAHAAAPAQDDEPDDDIDALIEELFSEDVQEEQEDNDDAPAAGEAKAVPEELLQTDMNTGLTMSEVEERRKKYGLNQMKEELENPFLKFIMFFVGPIQFVMEMAAALAAGLRDWVDFGVICALLMLNAVVGFVQEYQAGSIVDELKKSLALKAVVIREGQVHELEANEVVPGDILKLDEGTIICADGRVVTPDVHLQVDQSAITGESLAVDKHYGDPTFASSGVKRGEGLMVVTATGDSTFVGRAASLVNAAAGGTGHFTEVLNGIGTILLVLVLLTLFCIYTAAFYRSVRLARLLEYTLAITIIGVPVGLPAVVTTTMAVGAAYLAEKQAIVQKLSAIESLAGVEVLCSDKTGTLTKNKLSLGEPFTVSGVSGDDLVLTACLAASRKRKGLDAIDKAFLKALKNYPGPRSMLTKYKVIEFQPFDPVSKKVTAYVQAPDGTRITCVKGAPLWVLKTVEEDHPIPEDVLSAYKDKVGDLASRGYRSLGVARKIEGQHWEIMGIMPCSDPPRHDTARTISEAKRLGLRVKMLTGDAVDIAKETARQLGMGTNIYNAERLGLTGGGNMPGSEVYDFVEAADGFGEVFPQHKYAVVDILQQRGYLVAMTGDGVNDAPSLKKADTGIAVEGATDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYSYVVYRIALSLHLEIFLGLWLIIRNQLLNLELVVFIAIFADVATLAIAYDNAPYSMKPVKWNLPRLWGLSTVIGIVLAIGTWITNTTMIAQGQNRGIVQNFGVQDEVLFLEISLTENWLIFVTRCNGPFWSSIPSWQLSGAVLAVDILATMFCIFGWFKGGHQTSIVAVLRIWMYSFGIFCIMAGTYYILSESAGFDRMMNGKPKESRNQRSIEDLVVALQRTSTRHEKGDA P09988 H31_SCHPO PTM: Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by ssp2, promotes subsequent H3K14ac formation by gcn5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by sds21.; PTM: Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1 (By similarity). Methylated by clr4 to form H3K9me1. H3K9me1 represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones. Targeting to histone probably involves clr3 and rik1. Essential for silencing of centromeres and directional switching of the mating type. Methylated by set2 to form H3K36me. H3K36me represses gene expression. Methylated by dot1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the dot1-mediated formation of H3K79me require H2BK123ub1 (By similarity). {ECO:0000250}.; PTM: Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by gcn5 is promoted by H3S10ph. H3K14ac can also be formed by esa1. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair (By similarity). {ECO:0000250}. MOD_RES 5; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 5; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 5; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 10; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 10; /note="N6-methyllysine; alternate"; /evidence="ECO:0000269|PubMed:11283354"; MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 15; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 15; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 19; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 19; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 24; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 24; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 37; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 37; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:16087749"; MOD_RES 37; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 37; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 57; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 65; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 80; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 80; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 80; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250" SPAC1834.04;SPBC8D2.04; STRAND 7..9; /evidence="ECO:0007829|PDB:3G7L"; STRAND 128..131; /evidence="ECO:0007829|PDB:2DZE" CHAIN 2..136; /note="Histone H3.1/H3.2"; /id="PRO_0000221366" MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS P0CF96 MZT1_SCHPO SPAC9G1.15c; HELIX 5..18; /evidence="ECO:0007829|PDB:6L80"; HELIX 25..36; /evidence="ECO:0007829|PDB:6L80"; HELIX 41..53; /evidence="ECO:0007829|PDB:6L80" CHAIN 1..64; /note="Mitotic-spindle organizing protein 1"; /id="PRO_0000394216" MSESTKETIEVLYEIGTLLGTELDKTTLSLCISLCENNVHPEAIAQIIREIRMAQEQTVDTEPS P0CT33 TLH1_SCHPO BINDING 1213..1220; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 1240..1247; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:15591066}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; SPAC212.11; CHAIN 1..1887; /note="ATP-dependent DNA helicase tlh1"; /id="PRO_0000255584" MVVASEIAKVASKTARDIAGCFTCQCGTQFDNVERIVQHFKECRYRDETCKDDDIVVYEPSSFVQDEKKDKPIIVEAASEATSEEACNSSKERQLPALSALSALSTLTTSANDDLWTARLIWQSTNDTKLDNSPSSNYTDLNHKLANYGLSILSIHALMCVECECLLNVIHTAQHMQIVHKLELNEDLLWFQELRTLKLKSPTNVLQTHSSQTHVYPYIRGLPVLLNGYECVPCTKNGTGFVHAIMDTFRHHVRRTHGKVIKLENCIRRTALQTVKNKYAQRCQFFKVDYVPLNGGEEEEEEEGEEKEDAQNIKERMVDFCFSKFMEKNQQRREQQDKGENKKRQDDVDQATDNNTNTILEDDEKDNDEEEEEEIVNAREKNLLNQQFNWTAIVKKLGENWDQLVRFEYTNGIVTLDTIVNQLIRYYYRGFRHLSGMTMGMRRMFTQGGSYSAQERGLCRLEQKDTVVRYAQSAALYLIFLLRRPSADSGIRRHLEAMCGATVERKEGGSNSSSNISNVANFDSAEDDNDNDNDNDRDSNNNNNNNNTNTDDDDKLAYLELHEALKLAFLQQYDFSKNVQDLEIMEFLACMSLHKDGTSKYAYEISACFAPLIYTCRLVAACELQRLIDEKQIDLLSIPSFQTAGSIAYAHVFCFITLGQRNLYDVLYETQKVVRDIIRTEGYANTLQGLSPSTVLFQPRSNSMYPCIGDAFNNMVRLDLSELTALYEGMFAKVQDLLKELCFDMNVEKLLPISLLRSIGDDINNSKLGYSFFKESIEIRSSHSVLLRTILKNSELCHRFFPSMSKKDLTKLFGGVSDQQRNECDNYSNHYNDNSNDNDNDVFLKLHWSKSAIKKYETKASIFNELLFCLVYISAGQPARAQEMVYWTLRNGKYKTRELYLMFGRLMIYSRYDKTRNMKFAEKPIPRFLSEPLSILALRYYVLVRPLEALMKYVTTADRSKVAVYLDFMFVIAGERLQRDLPYRIFPKATYQCIQKPLGFRNYRHIAHYFKEKNIEEEMTRESYFDLQAGHTRNTALYIYGRTMDNLHYLPSDYFANFFRASYKWQELLQIRDNPTHGLLVETKHPFIKRVDQLEEALNEKLARLVGEQMVEGDKEKDKTNEEKNKDEVKAEMTQPVVNQDSHDLQDQLATTPTAPTAFHYRPGLLQPSQTSVQHCCWALSQYYGLEAKFRSLKQFQSVYFSLLNRMNLITVLPTGGGKSLSFLIPALIEKKRQTPGKVMNMVTLVLVPMMSLRQDMMLRVNEKGLLVCSGNWTAFKDVRLTLETQLPDLFILTYESALTNSGLRFFESLATLGRLARVVIDEAHLLLTSGAWRTALSRASRLSGLYAPLHLLSATFPRQLEMVARQTFCTNFYVLRETSTARENIFYFLHPYDNTEFLLDLRTLMKRTKVFEGDGRAIIFCRTKKDVEYIHRRLHQSDLFAHTHVTIYTGDVSDEERQMNFDAFRNANGKTRIMIATKAFGLGINYMGVRLVVHYGLPASSMDYVQETGRAGRDGKYAIAALFYEKYDSTWSSYVEDSMKNFLNDNTMCVRSFLASEMDGECVCCASFANCVYCSRCSDSLLGEESTVSTMYGVKPTLPETPKPAIATHSRYNASFSSSPPPQPGNSSGMSAMNTNTTSTTPVSLSELSEITLFPSSVSPTWKKSFGNANTNLKYGLEDMSLSHRRGHKRTYDEHLNNVQQGVNHDMNRVHGSVGGMSGIVGIGIGIGDGDGDGDVDSRTIHFAEYKSRVQAVKKQWVDSTDISAQLERFFRVYKDECLSCTLGNPDTEIRAHTGKACPVRLSTCYKCGKADHNLRECKLRIRFQGLCLFCGLTKFEHADSDMAYTSDCRSWARKANLISLVYYAWNNVQYRRTIADKFLQGDVRD P0CY17 MATMC_SCHPO SPBC23G7.09; CHAIN 1..181; /note="Mating-type M-specific polypeptide Mc"; /id="PRO_0000410974" MDSHQELSAGSPISYDFLDPDWCFKRYLTKDALHSIETGKGAAYFVPDGFTPILIPNSQSYLLDGNSAQLPRPQPISFTLDQCKVPGYILKSLRKDTTSTERTPRPPNAFILYRKEKHATLLKSNPSINNSQVSKLVGEMWRNESKEVRMRYFKMSEFYKAQHQKMYPGYKYQPRKNKVKR P10505 APC3_SCHPO SPAC17C9.01c; CHAIN 1..665; /note="Anaphase-promoting complex subunit 3"; /id="PRO_0000106304" MTDRLKCLIWYCIDNQNYDNSIFYSERLHAIEDSNESLYLLAYSHFLNLDYNIVYDLLDRVISHVPCTYLFARTSLILGRYKQGISAVEACRSNWRSIQPNINDSISSRGHPDASCMLDVLGTMYKKAGFLKKATDCFVEAVSINPYNFSAFQNLTAIGVPLDANNVFVIPPYLTAMKGFEKSQTNATASVPEPSFLKKSKESSSSSNKFSVSESIANSYSNSSISAFTKWFDRVDASELPGSEKERHQSLKLQSQSQTSKNLLAFNDAQKADSNNRDTSLKSHFVEPRTQALRPGARLTYKLREARSSKRGESTPQSFREEDNNLMELLKLFGKGVYLLAQYKLREALNCFQSLPIEQQNTPFVLAKLGITYFELVDYEKSEEVFQKLRDLSPSRVKDMEVFSTALWHLQKSVPLSYLAHETLETNPYSPESWCILANCFSLQREHSQALKCINRAIQLDPTFEYAYTLQGHEHSANEEYEKSKTSFRKAIRVNVRHYNAWYGLGMVYLKTGRNDQADFHFQRAAEINPNNSVLITCIGMIYERCKDYKKALDFYDRACKLDEKSSLARFKKAKVLILLHDHDKALVELEQLKAIAPDEANVHFLLGKIFKQMRKKNLALKHFTIAWNLDGKATHIIKESIENLDIPEENLLTETGEIYRNLET P10506 BYR1_SCHPO ACT_SITE 186; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 72..80; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 93; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; MOD_RES 214; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 218; /note="Phosphothreonine"; /evidence="ECO:0000250" SPAC1D4.13; CHAIN 1..340; /note="Protein kinase byr1"; /id="PRO_0000085688" MFKRRRNPKGLVLNPNASVKSSDNDHKEELINNQKSFESNVEAFMEQCAHMNRRPAWISDLDNSSLEVVRHLGEGNGGAVSLVKHRNIFMARKTVYVGSDSKLQKQILRELGVLHHCRSPYIVGFYGAFQYKNNISLCMEYMDCGSLDAILREGGPIPLDILGKIINSMVKGLIYLYNVLHIIHRDLKPSNVVVNSRGEIKLCDFGVSGELVNSVAQTFVGTSTYMSPERIRGGKYTVKSDIWSLGISIIELATQELPWSFSNIDDSIGILDLLHCIVQEEPPRLPSSFPEDLRLFVDACLHKDPTLRASPQQLCAMPYFQQALMINVDLASWASNFRSS P10651 H33_SCHPO PTM: Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by ssp2, promotes subsequent H3K14ac formation by gcn5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by sds21.; PTM: Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1 (By similarity). Methylated by clr4 to form H3K9me1. H3K9me1 represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones. Targeting to histone probably involves clr3 and rik1. Essential for silencing of centromeres and directional switching of the mating type. Methylated by set2 to form H3K36me. H3K36me represses gene expression. Methylated by dot1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the dot1-mediated formation of H3K79me require H2BK123ub1 (By similarity). {ECO:0000250}.; PTM: Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by gcn5 is promoted by H3S10ph. H3K14ac can also be formed by esa1. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair (By similarity). Acetylation at Lys-123 (H3K122ac) plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. {ECO:0000250, ECO:0000269|PubMed:23415232}. MOD_RES 5; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 5; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 5; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 10; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 10; /note="N6-methyllysine; alternate"; /evidence="ECO:0000269|PubMed:11283354"; MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 15; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 15; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 19; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 19; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 24; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 24; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 28; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 37; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:16087749"; MOD_RES 37; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:16087749"; MOD_RES 37; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 37; /note="N6-methyllysine; alternate"; /evidence="ECO:0000269|PubMed:16087749"; MOD_RES 57; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 65; /note="N6-acetyllysine"; /evidence="ECO:0000250"; MOD_RES 80; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 80; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 80; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250"; MOD_RES 123; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:23415232" SPBC1105.11c; CHAIN 2..136; /note="Histone H3.3"; /id="PRO_0000221367" MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPPTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS P10815 CG23_SCHPO SPBC582.03; CHAIN 1..482; /note="G2/mitotic-specific cyclin cdc13"; /id="PRO_0000080402" MTTRRLTRQHLLANTLGNNDENHPSNHIARAKSSLHSSENSLVNGKKATVSSTNVPKKRHALDDVSNFHNKEGVPLASKNTNVRHTTASVSTRRALEEKSIIPATDDEPASKKRRQPSVFNSSVPSLPQHLSTKSHSVSTHGVDAFHKDQATIPKKLKKDVDERVVSKDIPKLHRDSVESPESQDWDDLDAEDWADPLMVSEYVVDIFEYLNELEIETMPSPTYMDRQKELAWKMRGILTDWLIEVHSRFRLLPETLFLAVNIIDRFLSLRVCSLNKLQLVGIAALFIASKYEEVMCPSVQNFVYMADGGYDEEEILQAERYILRVLEFNLAYPNPMNFLRRISKADFYDIQTRTVAKYLVEIGLLDHKLLPYPPSQQCAAAMYLAREMLGRGPWNRNLVHYSGYEEYQLISVVKKMINYLQKPVQHEAFFKKYASKKFMKASLFVRDWIKKNSIPLGDDADEDYTFHKQKRIQHDMKDEEW P10989 ACT_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P60010}; MOD_RES 202; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 324; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32H8.12c; CHAIN 1..375; /note="Actin"; /id="PRO_0000089007" MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPCLLTEAPLNPKSNREKMTQIIFETFNAPAFYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAIMRLDLAGRDLTDYLMKILMERGYTFSTTAEREIVRDIKEKLCYVALDFEQELQTAAQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSALGLENAGIHEATYNSIMKCDVDIRKDLYGNVVMSGGTTMYPGIADRMQKEIQALAPSSMKVKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVYRKCF P11620 YPT1_SCHPO BINDING 15..23; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62820"; BINDING 33..40; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62820"; BINDING 63..67; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62820"; BINDING 121..124; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62820"; BINDING 151..153; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62820" MOD_RES 164; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1703.10; CHAIN 1..203; /note="GTP-binding protein ypt1"; /id="PRO_0000121308" LIPID 202; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:1597466"; LIPID 203; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:1597466" MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTFELEGKTVKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDVTDQDSFNNVKQWLQEIDRYAVEGVNRLLVGNKSDMVDKKVVEYSVAKEFADSLNIPFLETSAKDSTNVEQAFLTMSRQIKERMGNNTFASSNAKSSVKVGQGTNVSQSSSNCC P12000 DNLI1_SCHPO ACT_SITE 416; /note="N6-AMP-lysine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" BINDING 414; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 421; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 437; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 469; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 568; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 573; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 587; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 593; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC20G8.01; CHAIN 1..768; /note="DNA ligase 1"; /id="PRO_0000059585" MRTVFSQIPRFKQVNQYIRMSTRQSDISNFFISSASHKSEHVEVSQSSSDSKNVDGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSEAKKQKTLGSSSSSSDAVSSNNDSGASTPIPLPIKEPPLESNARNDKLKGHATFAEMVKAFTKIENTSKRLEIIDIMGTYFFGILRDHPSDLLACVYLSINKLGPDYSGLELGIGESIIMKAIGESTGQTLQQIKLSFHKVGDLGLVAQTSRQNQPTMFKPAALTIPFLFDSLKKIAQMSGNQSQNRKIGVIKRLLSSCEGAEPKYLIRALEGKLRLQLAEKTILVALANATAQYHADKNGEKLSQQDRIEGEQILRDVYCQLPSYDLIVPHLIEHGLGTLRETCKLTPGIPTKPMLAKPTKQISEVLNTFDQAAFTCEYKYDGERAQVHFTEDGKFYVFSRNSENMSVRYPDISVSVSKWKKPDARSFILDCEAVGWDRDENKILPFQKLATRKRKDVKIGDIKVRACLFAFDILYLNGQPLLETPLNERRKLLYSMFQPSTGDFTFAKHSDQKSIESIEEFLEESVKDSCEGLMVKMLEGPDSHYEPSKRSRHWLKVKKDYLSGVGDSLDLIVIGAYYGKGKRTSVYGAFLLGCYDPDTETVQSICKLGTGFSEEHLETFYNQLKDIVISKKKDFYAHSDVPAHQPDVWFEPKYLWEVLAADLSLSPVYKAAIGYVQEDKGISLRFPRFIRIREDKSWEDATTSEQVSEFYRSQVAYSQKEKEGSPAAEDY P13681 PP11_SCHPO ACT_SITE 124; /note="Proton donor"; /evidence="ECO:0000250" BINDING 63; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 65; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 91; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 91; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 123; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 172; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 247; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; MOD_RES 316; /note="Phosphothreonine; by CDC2"; /evidence="ECO:0000269|PubMed:7957097" SPBC776.02c; CHAIN 1..327; /note="Serine/threonine-protein phosphatase PP1-1"; /id="PRO_0000058818" MSNPDVDLDSIIDRLLEVRGSRPGRQVQLSEDEIRFLCNKAREIFISQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLEVICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFTMHGGLSPDLNSMDQIQRIMRPTDVPDTGLLCDLLWSDPDKDLTGWGDNDRGVSFTFGPDVVSRFLHKHDMDLVCRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAEKKQRYGYQGSSQNWHMTPPRKNKTGNSK P14068 XPO1_SCHPO SPAC1805.17; CHAIN 1..1078; /note="Exportin-1"; /id="PRO_0000204709" MEGILAFDRELDVALLDRVVQTFYQGVGAEQQQAQQVLTQFQAHPDAWSQAYSILEKSEYPQTKYIALSVLDKLITTRWKMLPKEQRLGIRNYIVAVMIKNSSDETVLQQQKTFLNKLDLTLVQILKQEWPHNWPNFIPEIVQASKTNLSLCENNMIVLRLLSEEIFDYSAEQMTQLKTKNLKNQMCGEFAEIFQLCSQILERAQKPSLIKATLGTLLRFLNWIPLGYIFETNIVELITNRFLNVPDFRNVTIECLTEIASLTSQPQYNDKFVTMFNLVMTSVNSMLPLQTDFREAYEESSTNEQDFIQNLALFLCAFFSSHLRPLENPENQEVLLNAHSYLLNISRINEREIFKICLEYWSKLVAQLYEEMQQIPMSEMNPLLNLSSPTSLISSNPNMLANLPLRKHIYKDILSTLRLVMIENMVKPEEVLIVENDEGEIVREFVKETDTITLYKSMREVLVYLTHLDVVDTEIVMTEKLARIVVGTEWSWQNLNTLCWAIGSISGAMNEEMEKRFLVNVIKDLLGLCEMKRGKDNKAVVASNIMYVVGQYPRFLKAHWKFLKTVVNKLFEFMHEYHEGVQDMACDTFIKIAQKCRRHFVAQQLGETEPFINEIIRNLAKTTEDLTPQQTHTFYEACGYMISAQPQKHLQERLIFDLMALPNQAWENIVAQAAQNAQVLGDPQTVKILANVLKTNVAACTSIGSGFYPQIAKNYVDMLGLYKAVSGLISEVVAAQGNIATKTPHVRGLRTIKKEILKLVDAYISRAEDLELVGNTLIPALFEAVLLDYLQNVPDARDAEVLNLITTIVNQLSELLTDKIPLVLDAVFGCTLEMISKDFSEYPEHRAAFFQLLRAINLNCFPALLNIPAPQFKLVINSIVWSFKHVSRDIQETGLNILLELINNMASMGPDVSNAFFQTYYISLLQDILYVLTDSDHKSGFKLQSLILARLFYLVESNQITVPLYDPSQFPQEMNNQLFLRQYIMNLLVTAFPHLQPIQIQEFVQTVLALNQDSIKFKLALRDFLIQLKEFGGDNAELYLEEKEQELAAQQKAQLEKAMTVPGMIKPVDMPTMEEEEL P14605 CYAA_SCHPO BINDING 1337; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1380; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; SPBC19C7.03; CHAIN 1..1692; /note="Adenylate cyclase"; /id="PRO_0000195733" MDQSKRLLKSAVPNPPEHFKTGISWLDDLDEKDDDSATSVNYDIPEITEANLCNDSHEALSPCTQPVGNSGRPVEAFKTYPSTPAVPSKSVLFHFYEPDENFSLSDTGRTKSDTALAARESSEKSEVPRDTRSAGIKPYKENNSSNCAISKEAGLRRLIDKDRESFDKNLNQSFTNLTFPEPISDDSDSVEFQRDSLNNNWPASLEGSIHELPRNSDDDGIPASAAHILDLDYHRDSYDSPWKKFLPYPSILSDDSWKAPESWGTSLPTEAIPKQVFTTRFFARPSLGNRKKEFFLRVYRDDRTSVSFICPIGIQTHEVIKLLARLFFLPSSANFYLLLIQFNTERILLPHEQPCIIFERLLSLFGCKVTSDEEINEEDNYSVARLVFTTMDIGADVLRKFSEKKITANLDISRSNLEVIPVKIYPYAHELISLNVSHNLSLDLPLDFMERCVKLKRLDISNNLRSPRGKPITALRQLEVLNMSRNDIYELDPLIFSGLSRNSLKELNIANNKLFFLPHSTRYLVNLTYLDLSYNNFVTFPLIITELSQLETLNFSHNLLSQISSKIGSLVKLKHLYLQFNDLSNRLPQEIGLLKNLETIDLSYNAITNIASLSECPKLNSINVACNLLSFYEYSNPSATFIDFSFCPLTTIDPAFSYSNLVYFDISHAKLIGLKDSVIETLVNVETVKVNYNHFTSISDAISAMQNLKYLSCTNCEMSYVSPNLGKLKHLVHLDLHANNIKIFPEEVWQVSSLKVVNLSSNILEKIKLPVATSKKLTRTISQLKIMRTLSGNPVSSLSSQEFVMPTVEELYLVDNRLGNDCFTALEYFKCLKVLNLSYNYLTEIPSKFFQNFSDLKHLFVSGNELANLSISSTAQVLLETLYANGNRLSSFPKNEALSKSLRFLDISTNNLQNLAVEKAEKKSLTKLPQLEYLNLSGNTWFRFSEHEDTNFTKSYLKNLKFLSIMDLNTKFSNAPSDVLNHFIQRNSPQPNILRYGVCGYLSRSIPVISACELVVNNFLHPQSSLYCVLDSDISAGKNNRVLKFVYDNLASCLAHEINAADSSSEQICNALRRGFLRLNKKLGNVIHYDLRKSSEGDVDSNYVTTMNISEKGYSMDSSCLDIGVSIILVYVRDTRAFVANVGTSMAIMSTRNDSEPTTLSVMHDVYNRDEIRRIVDSCGFISGEIKSTTTRAIGRLSQFPGVQAVPYVNVQYLSELNEFIILANQEFWSVLSKRTVIDVVRANRHSPLLASTKLRDYAIAYGAEKNVLVVIVELNGLFEENSLNFNQLRGDEKTLAISEKNDNMSFVQDLPDDSSLARMNREVSPPKGCIAMVFTDIKNSTLLWERHPIAMRSAIKTHNTIMRRQLRATGGYEVKTEGDAFMVCFQTVPAALLWCFSVQLQLLSADWPNEIVESVQGRLVLGSKNEVLYRGLSVRIGVNYGVTVSELDPITRRMDYYGPVVNRTSRVVSVADGGQIAVSAEVVSVLNQLDSETMSSEKTNVNEMEVRALKQIGYIIHNLGEFKLKGLDTTEMISLVYPVQLQGRLERLIKSRSLGTPTALPETQTYTPVRSRSNSLRPMLARLSDSKSVHGEEGGSGKRSVSSLRNVSPSESTGGYEGCIFDDQQYQLLYELCERLEDHAAILHGFPEPPPCDTGLAAPVNQAEEYSLFYRLTLRIENTIYCVSQMLGHTG P17608 RYH1_SCHPO BINDING 18..25; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 66..70; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 124..127; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 201; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC4C5.02c; CHAIN 1..201; /note="GTP-binding protein ryh1"; /id="PRO_0000121307" LIPID 199; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"; LIPID 201; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MSENYSFSLRKFKLVFLGEQSVGKTSLITRFMYDQFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAIIVYDITNHNSFVNTEKWIEDVRAERGDDVIIVLVGNKTDLADKRQVTQEEGEKKAKELKIMHMETSAKAGHNVKLLFRKIAQMLPGMENVETQSTQMIDVSIQPNENESSCNC P17610 YPT3_SCHPO BINDING 17..24; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 65..69; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 123..126; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 42; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC18G6.03; CHAIN 1..214; /note="GTP-binding protein ypt3"; /id="PRO_0000121310" LIPID 213; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:1597466"; LIPID 214; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:1597466" MCQEDEYDYLFKTVLIGDSGVGKSNLLMRFTRNEFNIESKSTIGVEFATRNIVLDNKKIKAQIWDTAGQERYRAITSAYYRGAVGALIVYDITKQSSFDNVGRWLKELREHADSNIVIMLVGNKTDLLHLRAVSTEEAQAFAAENNLSFIETSAMDASNVEEAFQTVLTEIFRIVSNRSLEAGDDGVHPTAGQTLNIAPTMNDLNKKKSSSQCC P17871 TBP_SCHPO SPAC29E6.08; CHAIN 1..231; /note="TATA-box-binding protein"; /id="PRO_0000153989" MDFALPTTASQASAFMNNSSLTFPVLPNANNEATNETADSGDAEVSKNEGVSGIVPTLQNIVATVNLDCRLDLKTIALHARNAEYNPKRFAAVIMRIREPKSTALIFASGKMVVLGGKSEDDSKLASRKYARIIQKLGFNAKFTDFKIQNIVGSCDVKFPIRLEGLAYSHGTFSSYEPELFPGLIYRMVKPKVVLLIFVSGKIVLTGAKVREEIYQAFEAIYPVLSEFRKH P18296 CUT1_SCHPO ACT_SITE 1730 CATALYTIC ACTIVITY: Reaction=All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.; EC=3.4.22.49; SPCC5E4.04; CHAIN 1..1828; /note="Separin"; /id="PRO_0000205903" MSTRSIVTSKVSWTPEKFISALSYPEHCSITLVKRLKASVKLKDLKQNISRDAPSWTFEHLFVAFKCAVSNLAKQWAELSTTDKEKTRRMFCTPSRLNTAHRPEVFYLLECCTYILEQMQVVTKNTSHLYDCIRSGVSICNRLLDMEIFEPAISLLMKTHKNLIILLTYRDHDAIPTATLLNPTLDVSEIQLESCLFVPMVPASYFLNIGTIVVTFQLNVLRCLSLSQINGLSLNTINNLQSEDGPFQWIERSFPSQVQLANSRREILARLLTRFSMIQNNALQSFKLLILSIALWLNILSSQRADDKEFDVNQLETRILQLFSKVVQLCKSEDIEGSILNKDMTQLHHLLENLSKESRLHILLQLSQLYYKYNDFQLSAAYVIRGYSLSFEDISFKLKFLLFSFRLSIHDNSICFPFNLIQELSSLQQLFVENALPYSEALHLLDSIERSFRLFNDSTVFDDTVFALNISEILSWILSSVVRDILVEDELLNLQLKIRKFLMFTFHIIRSFSELTKFQSSLEGCLNLAAYYEDAEFPQKLSNHLYNLCVKSSNVNYARECISLSIKIAVSHKLTNDETYLLKILKNFQLRYHDSLQLQEKCDVLHTTFNQLDLYVGTTSVGKSSVLDNILKRIFNSLTSINDSNIEKLLESISYSLLKLFFKCANEGSRYNASAALSFKLSLMLHEKEEVLLLKTNVSCVLANHGYNDIKFEEMVLCVIKGDQNLLEHNSNNNAKLALNESLLCSWENLLCYRRAEDDSRILTIIESWTIFISRFSSVISRCSFTDFEINSILNFFFCFLHTVEPSGKLTFELAFLEIFYELFNCLLHLQFSKYLVIIGTLLSDKYMTLGFSGKAHLFYTKCYSYLRQCKSSPFINFWNVSYGKYLILTGNTDKGILQLKKYSLSSEEDFNSNGLSRTVSLNLLLYERIQLSDALFQLGYTTVSLGFIMQNLKVIKGLFSKSSKEHFNGGKYITWRLFAVSAHSNVCAARIYEHMGQAREAEFFYRQACSISEKMPFSCFSATFQLRLCSLLTRAGKLEKGEKILFDLTEAMKSTDTYHKLLWNYGAAEVCATKSELDGAICHYSECVKLLEIIKSEYYLFFNRNREKSLTKGIKRLSLSSQPTFVTESNTTEFDDWSILQNTAANLLRLISMFELKRGNLEIAKALMTDSTKCSIASFFNIVSANILKSKLIVCEADSTLFGDPVLRTLPDSVISLPGISHKFQKNQSKTKALGENTGFRKGSKRLDYLRERLKINLQNVRLSCEIIFSNAYERSSVCVCREVNELISYSTIMQSALTTIGETTDVDSSSASFFLEIPKALGFHRRREAQKFRNQHKELHFSSLEQILNSRLSIPDVRTFQDNFIDSLPSIWNVVSITINNSGEDLFISKIRKGHSPLIFRLPLQRHNSRDADEEILVFTKAQTELFRIISKSNQMAQNGKHYTRREDKETWWKERRHLDQCLQQLLENIEISWLGGFKGIFNPHKIDTSLFAKFSSQFQNIIAKNFNMDKKTPVPTLSPEILELFITLGKPGYEGYEQLLEDLIYFILDIFQFRGLHFAYDEIDTDQLSMDLQDALNAYFNNYVSEENRSHTVLVLDKSVHQFPWESLPCLNRQSVSRVPSLSILRDILSQSFVVNGEYVEVRKEAGSYILNPSLDLKHTQEMFEHKLVEGGWKGLIASQPSNRDFIKMLSGNDFFLYFGHGGGEQYTTSYDLATLKRCAVTILMGCSSGALYECGSFEPWGTPLDYLSAGCPTLVANLWDVTDKDIDRFSLKMLESWGLFENKAPFVNSTSICTAVSESRSCCHLRYLNGAAPVIYGIPAYIIP P20772 PUR2_SCHPO BINDING 141..202; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 291; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 293; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evidence={ECO:0000269|PubMed:967158}; CATALYTIC ACTIVITY: Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000269|PubMed:967158}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305}; SPBC405.01; CHAIN 1..788; /note="Bifunctional purine biosynthetic protein ADE1"; /id="PRO_0000454642" MEPIIALLIGNGGREHTIAWKLCESPLISKVYVAPGNGGTASNGAESKMENVNIGVCDFEQLVKFALDKDVNLVIPGPELPLVEGIEGHFRRVGIPCFGPSALAARMEGSKVFSKDFMHRNNIPTAVYKSFSNYDHAKSFLDTCTFDVVIKADGLAAGKGVIIPKTKKEAFEALESIMLNEEFGSAGKNVVIEELLEGEELSILTFSDGYTCRSLPPAQDHKRAFDGDKGPNTGGMGCYAPTPVASPKLLETVQSTIIQPTIDGMRHEGYPLVGILFTGLMLTPSGPRVLEYNVRFGDPETQAVLPLLESDLAEIILACVNHRLDAIDIVISRKFSCAVVCVAGGYPGPYNKGDIITFDALKDKNTRIFHAGTSIRDGNVVTNGGRVLAVEATGDSVEAAVRLAYEGVKTVHFDKMFYRKDIAHHALNPKRKTREILTYENSGVSVDNGNEFVQRIKDLVKSTRRPGADADIGGFGGIFDLKQAGWNDPLLVSATDGVGSKLLIALSLNKHDTVGIDLVAMNVNDLVVQGAEPLIFLDYFATGSLDLKVSTSFVEGVVKGCKQAGCALVGGETSEMPGLYHDGHYDANGTSVGAVSRDDILPKPESFSKGDILLGLASDGVHSNGYSLVRKIVEYSDLEYTSVCPWDKNVRLGDSLLIPTRIYVKPLLHVIRKNIVKGMAHITGGGLVENVPRMLPSHLNAIIDVDTWEVPEVFKWLKDAGNVPISDMARTFNMGIGMVVAVASEDAEETMKELTSVGETVYRIGQLVDKESSSERCHLVNLNKWETF P21135 SECU_SCHPO PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. {ECO:0000269|PubMed:9312055}. SPBC14C8.01c; CHAIN 1..301; /note="Securin"; /id="PRO_0000206365" MLPRTMFSYGKENAFPVTPISNRNGTKGAGSKRAPLGSTKQSNAPSSVTVPRTVLGGKSTNISKFISAPSTKKMSPMDISMDSPTILEPNSQGISRSAVQERSKRLSASPRRSSLTDTPLPNELEEDIEYMPPPVHLDPIQSLGFDDVAIDCETLDPWPSMQNKATSVTIRNTPASDFHVYKEFSDDDPIQFPLLSVDGDSPLTEKDTNLTTPATLKASDQQRKVLEKPSVSKQSSSRTRLSTVYRTKLASGKSIPRPLSHKLTRPRVTASGNSRRRPLSRSIHSLSSSRIDFSSLDTGLL P21565 SRP54_SCHPO BINDING 108..115; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 190..194; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 248..251; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4; Evidence={ECO:0000250|UniProtKB:P61011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P61011}; SPCC188.06c; CHAIN 1..522; /note="Signal recognition particle subunit SRP54"; /id="PRO_0000101201" MVFADLGRRLNSALGDFSKATSVNEELVDTLLKNICTALLETDVNVRLVQELRSNIKKKINVSTLPQGINGKRIVQKAVFDELCSLVDPKVDAFTPKKGRPSVIMMVGLQGSGKTTTCSKLALHYQRRGLKSCLVAADTFRAGAFDQLKQNAIKARVPYFGSYTETDPVVIAKEGVDKFKNDRFDVIIVDTSGRHQQEQELFAEMVEISDAIRPDQTIMILDASIGQAAESQSKAFKETADFGAVIITKLDGHAKGGGALSAVAATKTPIVFIGTGEHINDLERFSPRSFISKLLGLGDLEGLMEHVQSLDFDKKNMVKNLEQGKFTVRDFRDQLGNIMKLGPLSKMASMIPGMSNMMNGMNDEEGSLRMKRMLYIVDSMTEQELDSDGLLFVEQPSRVLRVARGSGTSVLEVEETISQVRVFAQMAKKIGGKDGILGKLGGNPAAALKKDPRQLAAMQKRMQAMGMGGGMPGLNPGSMNFGDISKMANMLMGGGGPGGAGGMDFSGMLNQFQNMQKPPRRR P22068 ATPB_SCHPO BINDING 203..210; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; TRANSIT 1..44; /note="Mitochondrion"; /evidence="ECO:0000269|PubMed:1831760" SPAC222.12c; CHAIN 45..525; /note="ATP synthase subunit beta, mitochondrial"; /id="PRO_0000002453" MLKKQALSGIRRFSLATKQSFVKTSYKLPRKSWLNTAKFNTIRYASTEAAKHNKGSIKQVIGAVVDCQFEDADSLPSILNALEVKLPDNKRLVLEVAQHVGENTVRTIAMDGTEGLVRGTAVIDTGSPISIPVGPGTLGRIMNVIGEPVDERGPIKAVKYSPIHADAPSFEEQSTTPEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGYSVFTGVGERTREGNDLYREMQETGVIKLEGESKAALVFGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGAMQERITTTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSISELGIYPAVDPLDSKSRMMDPRILGEEHYNLAGSVQQMLQEYKSLQDIIAILGMDELSEADKLTVERARKVQRFLSQPFAVAEVFTGIEGRLVSLKDTIRSFKEILEGKHDSLPESAFYMVGSIDDAVKKAEKIAQELAA P22189 ATN_SCHPO ACT_SITE 368; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:P04191" BINDING 368; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 370; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 370; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 468; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 520; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 559; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 620; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 621; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 622; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 678; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 684; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 703; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 706; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191" CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000250|UniProtKB:P13587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634; Evidence={ECO:0000250|UniProtKB:P13587}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate; Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:11932440}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; PTM: The active site is phosphorylated in presence of sodium or potassium and in conditions of higher pH. Not phosphorylated in presence of calcium ions. {ECO:0000250|UniProtKB:P13587}. MOD_RES 1012; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC839.06; CHAIN 1..1037; /note="Sodium/potassium exporting P-type ATPase cta3"; /id="PRO_0000046238" CARBOHYD 869; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MVTINISNPVYFSDIKDVESEFLTSIPNGLTHEEAQNRLSEYGENRLEADSGVSAWKVLLRQVLNAMCVVLILAAALSFGTTDWIEGGVISAIIVLNITVGFIQEYKAEKTMDSLRTLASPMAHVTRSSKTDAIDSHLLVPGDVVVLKTGDVVPADLRLVETVNFETDEALLTGESLPVIKDAHATFQMNEDVPIGDRINLAYSSSIVTKGRAKGICYATGMQTQIGAIAAGLRQKGKLFQRPEKDEPNYRRKLNKYYLKVTSYYVQRVLGLNVGTPLQRKLTVLAYILFCIAIILAIIVMAAHSFHVTNEVSIYAISLGISIIPESLIAVLSITMAMGQKNMSKRRVIVRKLEALEALGGVTDICSDKTGTITQGKMITRRVWIPSYGYLSVDTSDANNPTIGTVSGLEAAMQDVLKEKKQEMKNIDPSNQPSDQFIPLLKTCALCNLSTVNQTETGEWVVKGEPTEIALHVFSKRFNYGKEDLLKTNTFVREYPFDSEIKRMAVIYEDQQGQYTVYAKGAVERILERCSTSNGSTLEEPDRELIIAQMETLAAEGLRVLALATKVIDKADNWETLPRDVAESSLEFVSLVGIYDPPRTESKGAVELCHRAGIRVHMLTGDHPETAKAIAREVGIIPPFISDRDPNMSWMVMTGSQFDALSDEEVDSLKALCLVIARCAPQTKVKMIEALHRRKAFVAMTGDGVNDSPSLKQANVGIAMGQNGSDVAKDASDIVLTDDNFSSIVNAIEEGRRMFDNIMRFVLHLLVSNVGEVILLVVGLAFRDEVHLSVFPMSPVEILWCNMITSSFPSMGLGMELAQPDVMERLPHDNKVGIFQKSLIVDMMVYGFFLGVVSLMTWVVIMYGFGTGNLSYDCNAHYHAGCNDVFKARSAVFAVVTFCILIMAVEVKNFDNSLFNLHGIPWGEWNFRYFLHTLVENKFLAWAIALAAVSVFPTIYIPVINRDVFKHTYIGWEWGVVAVAVMFYFFYVEIWKSIRRSLTNPQKKGKFRRTLSNTITTESKLSEKDLEHRLFLQSRRA P22192 PAC1_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8710510}; MOD_RES 122; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC119.11c; CHAIN 1..363; /note="Double-strand-specific pac1 ribonuclease"; /id="PRO_0000180467" MGRFKRHHEGDSDSSSSASDSLSRGRRSLGHKRSSHIKNRQYYILEKKIRKLMFAMKALLEETKHSTKDDVNLVIPGSTWSHIEGVYEMLKSRHDRQNEPVIEEPSSHPKNQKNQENNEPTSEEFEEGEYPPPLPPLRSEKLKEQVFMHISRAYEIYPNQSNPNELLDIHNERLEFLGDSFFNLFTTRIIFSKFPQMDEGSLSKLRAKFVGNESADKFARLYGFDKTLVLSYSAEKDQLRKSQKVIADTFEAYLGALILDGQEETAFQWVSRLLQPKIANITVQRPIDKLAKSKLFHKYSTLGHIEYRWVDGAGGSAEGYVIACIFNGKEVARAWGANQKDAGSRAAMQALEVLAKDYSKFAR P22193 RAD1_SCHPO SPAC1952.07; CHAIN 1..323; /note="DNA damage checkpoint control protein rad1"; /id="PRO_0000097151" MFQAETVCLKQIQSTLRCIDFSKECTIEITSRGLRFAVEESQSLQAHAFLDKSLFQTFNFQGDSDGDTYMFQTMISPLLQSLSIYTDGKERISTSAWDQPTVNIMHKRGVICKVQYNGPGCPFIWEVEEMAGYATACELLTMECEDDVDINRLASTLCTKIIMKSNWLYDALVELDNNMGENLIIHTSSQKSTFLLRCVGALSTTEIEYPNEKSVLESFETDSENTYSYRFSLIRHALKALQVGSKVNLRIDENGTLSIQIMLVGQEGLCTFVDFCIVPLDLVSEDEEEDEEEEPAESNQSDNNVLRNDPNYRGDAETEDEDS P22194 SDS22_SCHPO PTM: Phosphorylated. SPAC4A8.12c; CHAIN 1..332; /note="Protein phosphatase 1 regulatory subunit SDS22"; /id="PRO_0000071446" MSNVSSEDGIAPETQLIIDDPDVQQIDADEDLLDDVPDDVDCVELIQSRIQSMASLGLERFKNLQSLCLRQNQIKKIESVPETLTELDLYDNLIVRIENLDNVKNLTYLDLSFNNIKTIRNINHLKGLENLFFVQNRIRRIENLEGLDRLTNLELGGNKIRVIENLDTLVNLEKLWVGKNKITKFENFEKLQKLSLLSIQSNRITQFENLACLSHCLRELYVSHNGLTSFSGIEVLENLEILDVSNNMIKHLSYLAGLKNLVELWASNNELSSFQEIEDELSGLKKLETVYFEGNPLQKTNPAVYRNKVRLCLPQLRQIDATIIPKTSKQFP P22774 HSP7M_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000269|PubMed:26545917}; TRANSIT 1..43; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC664.11; CHAIN 44..674; /note="Iron-sulfur cluster biogenesis chaperone, mitochondrial"; /id="PRO_0000013551" MISSRFTNVVRSGLRFQSKGASFKIGASLHGSRMTARWNSNASGNEKVKGPVIGIDLGTTTSCLAIMEGQTPKVIANAEGTRTTPSVVAFTKDGERLVGVSAKRQAVINPENTFFATKRLIGRRFKEPEVQRDIKEVPYKIVEHSNGDAWLEARGKTYSPSQIGGFILSKMRETASTYLGKDVKNAVVTVPAYFNDSQRQATKAAGAIAGLNVLRVVNEPTAAALAYGLDKKNDAIVAVFDLGGGTFDISILELNNGVFEVRSTNGDTHLGGEDFDVALVRHIVETFKKNEGLDLSKDRLAVQRIREAAEKAKCELSSLSKTDISLPFITADATGPKHINMEISRAQFEKLVDPLVRRTIDPCKRALKDANLQTSEINEVILVGGMTRMPRVVETVKSIFKREPAKSVNPDEAVAIGAAIQGGVLSGHVKDLVLLDVTPLSLGIETLGGVFTRLINRNTTIPTRKSQVFSTAADGQTAVEIRVFQGERELVRDNKLIGNFQLTGIAPAPKGQPQIEVSFDVDADGIINVSARDKATNKDSSITVAGSSGLTDSEIEAMVADAEKYRASDMARKEAIENGNRAESVCTDIESNLDIHKDKLDQQAVEDLRSKITDLRETVAKVNAGDEGITSEDMKKKIDEIQQLSLKVFESVYKNQNQGNESSGDNSAPEGDKK P22987 KIN1_SCHPO ACT_SITE 266; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 131..139; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 154; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 528; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 535; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 536; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4F6.06; CHAIN 1..891; /note="Protein kinase kin1"; /id="PRO_0000086130" MEYRTNNVPVGNETKSAALNALPKIKISDSPNRHHNLVDAFMQSPSYSTQPKSAVEPLGLSFSPGYISPSSQSPHHGPVRSPSSRKPLPASPSRTRDHSLRVPVSGHSYSADEKPRERRKVIGNYVLGKTIGAGSMGKVKVAHHLKTGEQFAIKIVTRLHPDITKAKAAASAEATKAAQSEKNKEIRTVREAALSTLLRHPYICEARDVYITNSHYYMVFEFVDGGQMLDYIISHGKLKEKQARKFVRQIGSALSYLHQNSVVHRDLKIENILISKTGDIKIIDFGLSNLYRRQSRLRTFCGSLYFAAPELLNAQPYIGPEVDVWSFGIVLYVLVCGKVPFDDQNMSALHAKIKKGTVEYPSYLSSDCKGLLSRMLVTDPLKRATLEEVLNHPWMIRNYEGPPASFAPERSPITLPLDPEIIREMNGFDFGPPEKIVRELTKVISSEAYQSLAKTGFYSGPNSADKKKSFFEFRIRHAAHDIENPILPSLSMNTDIYDAFHPLISIYYLVSERRVYEKGGNWNRIAKTPVSSVPSSPVQPTSYNRTLPPMPEVVAYKGDEESPRVSRNTSLARRKPLPDTESHSPSPSATSSIKKNPSSIFRRFSSRRKQNKSSTSTLQISAPLETSQSPPTPRTKPSHKPPVSYKNKLVTQSAIGRSTSVREGRYAGISSQMDSLNMDSTGPSASNMANAPPSVRNNRVLNPRGASLGHGRMSTSTTNRQKQILNETMGNPVDKNSTSPSKSTDKLDPIKPVFLKGLFSVSTTSTKSTESIQRDLIRVMGMLDIEYKEIKGGYACLYKPQGIRTPTKSTSVHTRRKPSYGSNSTTDSYGSVPDTVPLDDNGESPASNLAFEIYIVKVPILSLRGVSFHRISGNSWQYKTLASRILNELKL P23566 UBC2_SCHPO ACT_SITE 88; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPAC18B11.07c; CHAIN 1..151; /note="Ubiquitin-conjugating enzyme E2 2"; /id="PRO_0000082536" MSTTARRRLMRDFKRMQQDPPAGVSASPVSDNVMLWNAVIIGPADTPFEDGTFKLVLSFDEQYPNKPPLVKFVSTMFHPNVYANGELCLDILQNRWSPTYDVAAILTSIQSLLNDPNNASPANAEAAQLHRENKKEYVRRVRKTVEDSWES P23636 PP2A2_SCHPO ACT_SITE 131; /note="Proton donor"; /evidence="ECO:0000250" BINDING 70; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 72; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 98; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 98; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 130; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 180; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 254; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; MOD_RES 322; /note="Leucine methyl ester"; /evidence="ECO:0000250" SPBC16H5.07c; CHAIN 1..322; /note="Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit"; /id="PRO_0000058872" MSIDPANDSKLAPEANDATLGDVDRWIEQLKKCEPLSEADVEMLCDKAREVLCQENNVQPVRNPVTVCGDIHGQFHDLMELFKIGGDVPDMNYLFMGDYVDRGYHSVETVSLLVAMKLRYPNRITILRGNHESRQITQVYGFYDECLRKYGSANVWKHFTNLFDYFPLTALIEDRIFCLHGGLSPSIDSLDHVRTLDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISETFNHANGLSLTARAHQLVMEGFNWAHDGDVVTIFSAPNYCYRCGNQAAILEVDDTMNQVFLQFDPAPREGEPVIARRTPDYFL P23880 PP12_SCHPO ACT_SITE 121; /note="Proton donor"; /evidence="ECO:0000250" BINDING 60; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 62; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 88; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 88; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 120; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 169; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 244; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; SPCC31H12.05c; CHAIN 1..322; /note="Serine/threonine-protein phosphatase PP1-2"; /id="PRO_0000058819" MDYDIDAIIEKLVKARNGKPSKQVQLSDAEIRYLCTTSRSIFLSQPMLLELEAPLKICGDIHGQYSDLLRLFEYGGYPPDANYLFLGDYVDRGKQSLEVICLLFAYKIKYPENFFLLRGNHEFASINRIYGFYDECKRRYSIKLWKTFTDCFNCMPVAAVIDEKIFCMHGGLSPDLNSLDQIQRIIRPTDIPDTGLLCDLVWSDPEKDLTGWGENDRGVSYTFGADVVSRFLQKHDLDLICRAHQVVEDGYEFFGKRQLVTIFSAPNYCGEFDNVGAMMSVNEDLLCSFQILKPAEKRQRVSQSSIKESKSATNSLKKSKNN P24339 CUT7_SCHPO BINDING 159..166; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" MOD_RES 1011; /note="Phosphothreonine; by CDC2"; /evidence="ECO:0000250" SPAC25G10.07c; CHAIN 1..1085; /note="Kinesin-like protein cut7"; /id="PRO_0000125370" MAPRVAPGGSQQFLGKQGLKAKNPVSTPNSHFRSASNPRKRREPPTIDTGYPDRSDTNSPTDHALHDENETNINVVVRVRGRTDQEVRDNSSLAVSTSGAMGAELAIQSDPSSMLVTKTYAFDKVFGPEADQLMLFENSVAPMLEQVLNGYNCTIFAYGQTGTGKTYTMSGDLSDSDGILSEGAGLIPRALYQLFSSLDNSNQEYAVKCSYYELYNEEIRDLLVSEELRKPARVFEDTSRRGNVVITGIEESYIKNAGDGLRLLREGSHRRQVAATKCNDLSSRSHSIFTITLHRKVSSGMTDETNSLTINNNSDDLLRASKLHMVDLAGSENIGRSGAENKRARETGMINQSLLTLGRVINALVEKAHHIPYRESKLTRLLQDSLGGKTKTSMIVTVSSTNTNLEETISTLEYAARAKSIRNKPQNNQLVFRKVLIKDLVLDIERLKNDLNATRKKNGVYLAESTYKELMDRVQNKDLLCQEQARKLEVLDLNVKSSREQLQYVSKSNQEHKKEVEALQLQLVNSSTELESVKSENEKLKNELVLEIEKRKKYETNEAKITTVATDLSQYYRESKEYIASLYEKLDRTERNNKENENNFWNLKFNLLTMLRSFHGSFTDETNGYFTLLNDFNASMEELLNTHSNQLLISMTKITEHFQSLDEALQSARSSCAVPNSSLDLIVSELKDSKNSLLDALEHSLQDISMSSQKLGNGISSELIELQKDMKESYRQLVQELRSLYNLQHTHEESQKELMYGVRNDIDALVKTCTTSLNDADIILSDYISDQKSKFESKQQDLIANIGKIVSNFLQEQNESLYTKADILHSHLNDTNSNIRKANEIMNNRSEEFLRNAASQAEIVGANKERIQKTVENGSQLLDSKSKAIHSNSRSMYDHCLALAESQKQGVNLEVQTLDRLLQKVKEHSEDNTKEKHQQLLDLLESLVGNNDNLIDSIKTPHTELQKITDHVLKGTTSLANHTNELLGLGDESLCNLETTIEDTSLVKLETTGDTPSKRELPATPSWTRDSSLIKETTNLNLDSDKKFVRETYTSSNQTNEPDVYDKPSNSSRTSLLRSSRSAYSKMKR P24488 HAP2_SCHPO SPBC725.11c; CHAIN 1..334; /note="Transcriptional activator hap2"; /id="PRO_0000198783" MNPYEPVEGLYVNAKQYHRILKRREARAKLEERLRGVQTTKKPYLHESRHKHAMRRPRGPGGRFLTADKVSKLRAQEAAEAAANGGSTGDDVNATNANDATVPATVSSEVTHTSEGYADSNDSRPSSISNSSESPAPINSATASMSPANNTSGNNITSPNVRGELDMSGNIAMSGGPTNTASTSGPVPHDMTVLPQTDSNTSNLMSSGSQLGSFATASTNGNNSTTTTTSSAAHPGSFHKGTNDYSSTLAGNEHSAFPGLDVYHDDSVSAGAAFIPHNPMDSIDHLDVNDPTATGLPVLPASDIDPLNLTGNTQDSMIIGQQTYPSHGSSGTMK P25295 TBG_SCHPO BINDING 142..148; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" SPBC32F12.04; CHAIN 1..446; /note="Tubulin gamma chain"; /id="PRO_0000048480" MGREIITLQAGQCGNQIGSQFWQQLCLEHGIGPDGTLESFATEGVDRKDVFFYQSDDTRYIPRAILIDLEPRVVNNILSDTYGSLYNPENILITKNGGGAGNNWANGYSHAERIFEDIMDMIDREADGSDSLEGFSLLHSIAGGTGSGLGSFLLERLNDRYPKKIIQTYSVFPNSQSVSDVVVQPYNSLLALKRLTLNADSVVVLDNAALAHIAADRLHTQNPTFHQQNQLVSTVMSASTTTLRYPGYMNNDLVSIIASLIPSPRCHFLLTSYTPFTNQQVEEAKAIRKTTVLDVMRRLLLPKNQMVSVNPSKKSCFISILDIIQGEADPADVHKSLLRIRERRYASFIPWGPASIQVALSKKSPYIKTNHRVSGLMLANHTSIASLFKRTLDQYDRLRKRNAFLEQYKKEAIFEDDLNEFDSSRDVVADLINEYEACEDPNYLSL P26306 RAD9_SCHPO SPAC664.07c; CHAIN 1..426; /note="DNA repair protein rad9"; /id="PRO_0000097157" MEFTVSNVNLRDLARIFTNLSRIDDAVNWEINKNQIEITCLNSSRSGFSMVTLKKAFFDKYIFQPDSVLLTGLMTPTIRIRTQVKPILSVFRNKIFDFIPTVVTTNSKNGYGSESASRKDVIVENVQISISTGSECRIIFKFLCKHGVIKTYKISYEQTQTLHAVFDKSLSHNNFQINSKILKDLTEHFGQRTEELTIQPLQERVLLTSFTEEVVHNRDILKQPTQTTVSIDGKEFERVALNEGVSVTLSLREFRAAVILAEALGSSICAYYGVPGKPILLTFAKGKNSEIEAQFILATVVGSDEQEVSSMMGNRWQHSSTPASLFNSVERNNSLTAVAHNPPGSIGWQTDQSDSSRMFNSALDRSDETNGIKEPSTTNDAGQSLFLDGIPNESELAAFNNDVNDDAEFGPTQAEQSYHGIFSQED P26359 MSH3_SCHPO BINDING 759..766; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC8F11.03; CHAIN 1..993; /note="DNA mismatch repair protein msh3"; /id="PRO_0000115196" MRGMSYNITHECDAINILSDNLHEGAISEDMVALSGPAIELLENNVGSSKNSYQEDEGSSSIDENAPLISIKRKRRIRTVKSTSNKELVQRKASKPTKQKSVFTPLEQQYLELKKNYQETILAIEVGYKFRFFGKDAKIASEVLGISCYFEHNFLNASVPSYRIDYHLERLINFGLKVAVVRQTETAALKSTSSSRNTLFDRRVARVLTKGTTLDDSFFRFEQTQHGTLQASQFILCVADNVDKSKAKSGRVQVGLIAIQLSSGTTVYDHFQDDFLRSELQTRLSHFQPCELIYSNKLSSESVALLNHYVSTEKTCGRVVRVQHAVQQDVKLALENLQDFFSSKCIMSGSKIIELHMEKVKSLHSLSIICLDMAISYLMEFSLEDLFVASNFYQPFDSISSMVLSKQALEGLELFVNQTDHTPVGSLFWVLDRTYTRFGQRMLQRWLQKPLVDKENIIERLDAVEELAFNSNSQVQAIRKMLYRLPDLEKGLSRIYYQRGFYKAASAFSKNSYSCFKSALLRRLIQQLPSISSIIDHFLGMFDQKEAENNNKVDMFKDIDNFDLSEEPNDVDYELAQEIRELKMSILMVRTEMDFHLQELRDYLEYPNLEFSIWGNVKFCIEVSKGCKKIPPDWIKLSSTRSLFRFHTPKIQSLLIELSSHEENLTISSEKIYRSFLSRISEHYNELRNVTTVLGTLDCLISFARISSQSGYTRPEFSDKELLIHESRHPMIELLSDKSFVPNHIHLSSDGVRCLLITGPNMGGKSSFVKQLALSAIMAQSGCFVPAKSALLPIFDSILIRMGSSDNLSVNMSTFMVEMLETKEVLSKATEKSMVIIDELGRGTSTIDGEAISYAVLHYLNQYIKSYLLFVTHFPSLGILERRFEGQLRCFHMGYLKSKEDFETSVSQSISFLYKLVPGVASKSYGLNVARMAGIPFSILSRATEISENYEKKHRNARKNVFIRKVAKLLMILNAEEIDFKRLFYDLTAFEEI P26659 RAD15_SCHPO BINDING 42..49; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 115; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074"; BINDING 133; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074"; BINDING 154; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074"; BINDING 189; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P18074" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.; EC=5.6.2.3; Evidence={ECO:0000250|UniProtKB:P06839}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.3; Evidence={ECO:0000250|UniProtKB:P06839}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P06839}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P06839}; SPAC1D4.12; CHAIN 1..772; /note="General transcription and DNA repair factor IIH helicase subunit XPD"; /id="PRO_0000101984" MKFYIDDLPILFPYPRIYPEQYQYMCDLKHSLDAGGIALLEMPSGTGKTISLLSLIVSYQQHYPEHRKLIYCSRTMSEIDKALAELKRLMAYRTSQLGYEEPFLGLGLTSRKNLCLHPSVRREKNGNVVDARCRSLTAGFVREQRLAGMDVPTCEFHDNLEDLEPHSLISNGVWTLDDITEYGEKTTRCPYFTVRRMLPFCNVIIYSYHYLLDPKIAERVSRELSKDCIVVFDEAHNIDNVCIESLSIDLTESSLRKASKSILSLEQKVNEVKQSDSKKLQDEYQKLVRGLQDANAANDEDQFMANPVLPEDVLKEAVPGNIRRAEHFIAFLKRFVEYLKTRMKVLHVIAETPTSFLQHVKDITFIDKKPLRFCAERLTSLVRALQISLVEDFHSLQQVVAFATLVATYERGFILILEPFETENATVPNPILRFSCLDASIAIKPVFERFRSVIITSGTLSPLDMYPKMLQFNTVMQESYGMSLARNCFLPMVVTRGSDQVAISSKFEARNDPSVVRNYGNILVEFSKITPDGLVAFFPSYLYLESIVSSWQSMGILDEVWKYKLILVETPDPHETTLALETYRAACSNGRGAVLLSVARGKVSEGVDFDHHYGRAVIMFGIPYQYTESRVLKARLEFLRDTYQIREADFLTFDAMRHAAQCLGRVLRGKDDHGIMVLADKRYGRSDKRTKLPKWIQQYITEGATNLSTDMSLALAKKFLRTMAQPFTASDQEGISWWSLDDLLIHQKKALKSAAIEQSKHEDEMDIDVVET P27574 PYP1_SCHPO ACT_SITE 470; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 320; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26F1.10c; CHAIN 1..550; /note="Tyrosine-protein phosphatase 1"; /id="PRO_0000094858" MNFSNGSKSSTFTIAPSGSCIALPPQRGVATSKYAVHASCLQEYLDKEAWKDDTLIIDLRPVSEFSKSRIKGSVNLSLPATLIKRPAFSVARIISNLHDVDDKRDFQNWQEFSSILVCVPAWIANYVTNAEVIGEKFRKESYSGDFGILDLDYSKVSGKYPSVIDNSPVKSKLGALPSARPRLSYSAAQTAPISLSSEGSDYFSRPPPTPNVAGLSLNNFFCPLPENKDNKSSPFGSATVQTPCLHSVPDAFTNPDVATLYQKFLRLQSLEHQRLVSCSDRNSQWSTVDSLSNTSYKKNRYTDIVPYNCTRVHLKRTSPSELDYINASFIKTETSNYIACQGSISRSISDFWHMVWDNVENIGTIVMLGSLFEAGREMCTAYWPSNGIGDKQVYGDYCVKQISEENVDNSRFILRKFEIQNANFPSVKKVHHYQYPNWSDCNSPENVKSMVEFLKYVNNSHGSGNTIVHCSAGVGRTGTFIVLDTILRFPESKLSGFNPSVADSSDVVFQLVDHIRKQRMKMVQTFTQFKYVYDLIDSLQKSQVHFPVLT P27584 GPA1_SCHPO BINDING 81..88; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 215..221; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 221; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 240..244; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 309..312; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 380; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPBC24C6.06; CHAIN 2..407; /note="Guanine nucleotide-binding protein alpha-1 subunit"; /id="PRO_0000203608" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000250"; LIPID 3; /note="S-palmitoyl cysteine"; /evidence="ECO:0000250" MGCMSSKYADTSGGEVIQKKLSDTQTSNSSTTGSQNARVPVLENWLNIVLRGKPQNVESSGVRVKGNSTSGGNDIKVLLLGAGDSGKTTIMKQMRLLYSPGFSQVVRKQYRVMIFENIISSLCLLLEAMDNSNVSLLPENEKYRAVILRKHTSQPNEPFSPEIYEAVHALTLDTKLRTVQSCGTNLSLLDNFYYYQDHIDRIFDPQYIPSDQDILHCRIKTTGISEETFLLNRHHYRFFDVGGQRSERRKWIHCFENVTALLFLVSLAGYDQCLVEDNSGNQMQEALLLWDSICNSSWFSESAMILFLNKLDLFKRKVHISPIQKHFPDYQEVGSTPTFVQTQCPLADNAVRSGMYYFYLKFESLNRIASRSCYCHFTTATDTSLLQRVMVSVQDTIMSNNLQSLMF P27638 SPK1_SCHPO ACT_SITE 163; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 45..53; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 68; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; PTM: Dually phosphorylated on Thr-199 and Tyr-201, which activates the enzyme. {ECO:0000250}. MOD_RES 199; /note="Phosphothreonine"; /evidence="ECO:0000250"; MOD_RES 201; /note="Phosphotyrosine"; /evidence="ECO:0000250" SPAC31G5.09c; CHAIN 1..372; /note="Mitogen-activated protein kinase spk1"; /id="PRO_0000186340" MASATSTPTIADGNSNKESVATSRSPHTHDLNFELPEEYEMINLIGQGAYGVVCAALHKPSGLKVAVKKIHPFNHPVFCLRTLREIKLLRHFRHENIISILDILPPPSYQELEDVYIVQELMETDLYRVIRSQPLSDDHCQYFTYQILRALKAMHSAGVVHRDLKPSNLLLNANCDLKVADFGLARSTTAQGGNPGFMTEYVATRWYRAPEIMLSFREYSKAIDLWSTGCILAEMLSARPLFPGKDYHSQITLILNILGTPTMDDFSRIKSARARKYIKSLPFTPKVSFKALFPQASPDAIDLLEKLLTFNPDKRITAEEALKHPYVAAYHDASDEPTASPMPPNLVDLYCNKEDLEIPVLKALIFREVNFR P28040 DPOLA_SCHPO BINDING 1256; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1259; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1283; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1285; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1316; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1321; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1335; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13382"; BINDING 1340; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13382" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P09884}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22509; Evidence={ECO:0000250|UniProtKB:P09884}; SPAC3H5.06c; CHAIN 1..1405; /note="DNA polymerase alpha catalytic subunit"; /id="PRO_0000046439" MRKRNAGIKPSQRFAELRALRQAGKTRASTYESKENEELYDNVSEEEYRKIVRQRLDEDDFVVDDNGAGYVDNGYDEWDQSHYSDEDDENEKGSSGRKRKKSKNVLAEPNQQIGAFFKANAIQPASRIANRKNNEKEDEFMAEILGSIDQDIPERLSTKKGNRSHTTSNAKRRSQKAASSISTTNVVSSDPKKYIPETVPSTPQPASSLPIPSSPPAALETEENVDSQPMELDEPELPVGSDAPIIDVEESIAMKPLMSHDQVDDTASLSKATISQQPLSPMTPLSSELDVSAFSEINSKIKNVDVPASSYSSPISKVSPSDVTEEDGSLFFFWMDYTEMYGSLCLFGKVYDKATKQYVSCFLKVDGIMRSLYFLPRPSSSSVSEDSIAAQTKDVYDEVANLLSKRGVKEWKSRVSKYKYAFELEDVPRTADYLEVIYSYSYPALPTDLTGSSFSHVFGTNTALFEQFVLSRRVMGPCWLKIQQPNFDAVKNASWCRVEIGCSSPQNISVSFEKNEITSKTPPMTVMSLAFRTLINKEQNKQEVVMISARIFENVDIEKGLPANDMPSYSFSLIRPLKQIFPNGFEKLARQHKSSIFCERSEVSLLNNFLNKVRTYDPDVYFGHDFEMCYSVLLSRLKERKIHNWSSIGRLRRSEWPRSFNRSSQQFVEKQIIAGRLMCDLSNDFGRSMIKAQSWSLSEIVLKELDIKRQDINQEKALQSWTDTAHGLLDYLVHCEIDTFFIAAVAFKIQMLQLSKNLTNIAGNSWARTLTGTRAERNEYILLHEFKKNGYIVPDKQQSIRRHAEAFGAEDGLQEESLGKKKDKYKGGLVFEPQKGLYETCILVMDFNSLYPSIIQEYNICFTTVDRSPSNSDSDDQIPDTPSASANQGIFPRLIANLVERRRQIKGLLKDNSATPTQRLQWDIQQQALKLTANSMYGCLGYTKSRFYARPLAVLITYKGREALMNTKELADQMGLQVIYGDTDSVMLNTNVTDKNHALRIGNEFKEKVNERYSKLEIDIDNVYQRMLLHAKKKYAALQLDSQGKPNLDVKGLDMKRREFCTLAKEASKFCLDQILSGELTETVIENIHSYLMDFSEKMRNGKFPANKFIIFNRLGKNPEDYPNGKTMPFVQVALKKKARGENVRVGDVIPFIIAGSDADGHPADRAYSPQEIMNTNSTLVIDYNYYLSHQILPPIERVIAPIEGTNRARLAECLGLDARKYYSHETSESSAFQRYESTLTDDQCFINVSPLLLKCPSCNATSFSLRSVKSLKETLYANTVECDCGYEYSDFTIILQFSSQLRDFINLYYEGILVCDDSSCGNRTRQMSVYGKRCCNKSCRGSVHFEYNDEQLYNQIKFLLKAVQTTTGATRNGIIRCNAINKNISRIMNKNAREFVDMGLIFSS P28745 RCC1_SCHPO SPBC557.03c; CHAIN 1..539; /note="Protein pim1"; /id="PRO_0000206636" MTSNRSTRSSTKREEVSKNGVEKRELDESDVMKNGKKPVKRAKVSSLPKPVRVPGSAKRINKIPELPTERLNVYVFGSGSMNELGMGEEEMDVVYRPRLNPILSTDKVGVVDLAVGGMHSAALSHDGRVYTWGVNDDYALGRLTKDQKDENGDKVDNDLLEGTPSKVEGALSHLRVTKVICSDNLTAAITDNGCCFTWGTFRCSDGVLGYSDSQKRTAEPTQMRLPEICQLATGTDHIIALTTTGKVYTWGNGQQFQLGRRMLERRRLQGLTPQPLALKNIISVGAGSYHSFAIDNKGRVYAWGLNITRQCGIEVEDEEEGAVITKPTLVDALEGYNVKSITGGEHHTLALLEDGRVLAWGRDDRHQLGIPDNALPETVVKDEKGNNYYLSTPTIIPGLTNVIQVVCGTHHNLAVTSDGKVYSWGSAENYEVGQGDNDEDVAVPTLVRSKAIKEVAIRVAGAGGQFSIIAGIPNASEEPVANGIKSEPENEKKLKTEETSKTDDSPVTDAKPDVTSNGEPSTATSESKDSVLEPSSTTA P28829 BYR2_SCHPO ACT_SITE 522; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 400..408; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 423; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O94547}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O94547}; SPBC1D7.05; STRAND 72..76; /evidence="ECO:0007829|PDB:1K8R"; STRAND 82..86; /evidence="ECO:0007829|PDB:1K8R"; STRAND 109..115; /evidence="ECO:0007829|PDB:1K8R"; STRAND 117..122; /evidence="ECO:0007829|PDB:1K8R"; STRAND 138..140; /evidence="ECO:0007829|PDB:1I35"; STRAND 143..150; /evidence="ECO:0007829|PDB:1K8R" HELIX 91..102; /evidence="ECO:0007829|PDB:1K8R"; HELIX 127..133; /evidence="ECO:0007829|PDB:1I35"; HELIX 155..160; /evidence="ECO:0007829|PDB:1K8R" TURN 78..80; /evidence="ECO:0007829|PDB:1I35" CHAIN 1..659; /note="Protein kinase byr2"; /id="PRO_0000085689" MEYYTSKEVAEWLKSIGLEKYIEQFSQNNIEGRHLNHLTLPLLKDLGIENTAKGKQFLKQRDYLREFPRPCILRFIACNGQTRAVQSRGDYQKTLAIALKKFSLEDASKFIVCVSQSSRIKLITEEEFKQICFNSSSPERDRLIIVPKEKPCPSFEDLRRSWEIELAQPAALSSQSSLSPKLSSVLPTSTQKRSVRSNNAKPFESYQRPPSELINSRISDFFPDHQPKLLEKTISNSLRRNLSIRTSQGHNLGNFGQEILPRSSRRARPSELVCPLSSLRISVAEDVNRLPRIDRGFDPPLTVSSTQRISRPPSLQKSITMVGVEPLYQSNGNEKSSKYNVFSESAHGNHQVLSFSPGSSPSFIEQPSPISPTSTTSEDTNTLEEDTDDQSIKWIRGALIGSGSFGQVYLGMNASSGELMAVKQVILDSVSESKDRHAKLLDALAGEIALLQELSHEHIVQYLGSNLNSDHLNIFLEYVPGGSVAGLLTMYGSFEETLVKNFIKQTLKGLEYLHSRGIVHRDIKGANILVDNKGKIKISDFGISKKLELNSTSTKTGGARPSFQGSSFWMAPEVVKQTMHTEKTDIWSLGCLVIEMLTSKHPYPNCDQMQAIFRIGENILPEFPSNISSSAIDFLEKTFAIDCNLRPTASELLSHPFVS P29458 MCM4_SCHPO BINDING 545..552; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 38; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 41; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 92; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16A11.17; CHAIN 1..911; /note="DNA replication licensing factor mcm4"; /id="PRO_0000194106" MSSSQQSGRANELRTPGRANSSSREAVDSSPLFFPASSPGSTRLTTPRTTARTPLASSPLLFESSSPGPNIPQSSRSHLLSQRNDLFLDSSSQRTPRSTRRGDIHSSVQMSTPSRRREVDPQRPGVSTPSSLLFSGSDALTFSQAHPSSEVADDTVRVIWGTNVSIQESIASFRGFLRGFKKKYRPEYRNELMPPPDAEQLVYIEALRNMRIMGLEILNLDVQDLKHYPPTKKLYHQLYSYPQEIIPIMDQTIKDVMLDLLGTNPPEDVLNDIELKIYKIRPFNLEKCINMRDLNPGDIDKLISIKGLVLRCTPVIPDMKQAFFRCSVCGHCVTVEIDRGRIAEPIKCPREVCGATNAMQLIHNRSEFADKQVIKLQETPDVVPDGQTPHSVSLCVYDELVDSARAGDRIEVTGIFRCVPVRLNPRMRTVKSLFKTYVDVVHIKKQDKRRLGTDPSTLESDIAEDAALQIDEVRKISDEEVEKIQQVSKRDDIYDILSRSLAPSIYEMDDVKKGLLLQLFGGTNKSFHKGASPRYRGDINILMCGDPSTSKSQILKYVHKIAPRGVYTSGKGSSAVGLTAYITRDQDTKQLVLESGALVLSDGGICCIDEFDKMSDATRSILHEVMEQQTVTVAKAGIITTLNARTSILASANPIGSKYNPDLPVTKNIDLPPTLLSRFDLVYLILDRVDETLDRKLANHIVSMYMEDTPEHATDMEVFSVEFLTSYITYARNNINPVISEEAAKELVNAYVGMRKLGEDVRASEKRITATTRQLESMIRLSEAHAKMHLRNVVEVGDVLEAARLIKTAIKDYATDPATGKISLDLIYVNERETLVPEDMVKELANLISNLTVGGKTMLVSQLLTRFREQSSTRLDASDFEACLGALERRGRIKVITSAGHRIVRSIAQTD P30261 DPOD3_SCHPO MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1734.02c; CHAIN 1..372; /note="DNA polymerase delta subunit 3"; /id="PRO_0000186049" MEEWRNFLDIKVINESSLVTVDNLSLQLDISSEKAQEYLNMFYQGNDFLYPIYLIHGQPIDDEINLEIDEESQPISNFPVLQYILCDKSSLQEKQSRLKSGYKTVIFALSSAPLSDFDELLPAVYEIREKDVLYKKEDADKYGFIFNENSVPRVLKKAPSTHSPQLSVPSKTSTIDKTDTRSTEKTKGKDIFSNARNQKGNSSRKNKKAPLENHKEKEPLLPKEEKLSEQAKRERDDLKNIMQLEDESVSTTSVHDSEDDNLDSNNFQLEIGTEAKSAAPDEPQEIIKSVSGGKRRGKRKVKKYATTKDEEGFLVTKEEEVWESFSEDENISTGTSNVVRNKPTTVNIATKKKNTAQSKPQQKSIMSFFGKK P30290 MIK1_SCHPO ACT_SITE 417; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 295..303; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 320; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 422; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 435; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC660.14; CHAIN 1..581; /note="Mitosis inhibitor protein kinase mik1"; /id="PRO_0000086327" MDSSTTIPITPTRTPCFFNISSSFNEHSPLNFYDEPIYNFSSGHEENQSHKSSKLTFFKPSNTKRSPHTPMQNNAKAIRLSTTVRHGIFKNSDLDGCSKPFAFSSGLKLSKKIVDASTPIDLKRKRAVTSLSTGLLSKREKWSLWEGNLTNPRSEQPHTPCKKGTKIKLKPPQSPLSPTTSLLARKCKHIDLDTFSRLDHPNSDSSDETFEMEELPSLSYGSEDLLEFCETPCKSQPIFLSSSHVNNWDEKDVPSSLSWTPTSPIFLNINSADDYEEEEDWTSDLRIRFQQVKPIHESDFSFVYHVSSINPPTETVYVVKMLKKNAAKFTGKERHLQEVSILQRLQACPFVVNLVNVWSYNDNIFLQLDYCENGDLSLFLSELGLLQVMDPFRVWKMLFQLTQALNFIHLLEFVHLDVKPSNVLITRDGNLKLGDFGLATSLPVSSMVDLEGDRVYIAPEILASHNYGKPADVYSLGLSMIEAATNVVLPENGVEWQRLRSGDYSNLPNLKDLLLSKEKVQINKVRCAESLQCLLQRMTHPYVDCRPTTQDLLAMPEMIFISEHSQKAAIIYEDHNSWLET P30316 DPOD_SCHPO BINDING 993; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 996; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 1008; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 1011; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 1040; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 1043; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 1053; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 1058; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P15436}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P15436}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436}; SPBC336.04; CHAIN 1..1086; /note="DNA polymerase delta catalytic subunit"; /id="PRO_0000046453" MTDRSSNEGVVLNKENYPFPRRNGSIHGEITDVKRRRLSERNGYGDKKGSSSKEKTSSFEDELAEYASQLDQDEIKSSKDQQWQRPALPAINPEKDDIYFQQIDSEEFTEGSVPSIRLFGVTDNGNSILVHVVGFLPYFYVKAPVGFRPEMLERFTQDLDATCNGGVIDHCIIEMKENLYGFQGNEKSPFIKIFTTNPRILSRARNVFERGEFNFEELFPVGVGVTTFESNTQYLLRFMIDCDVVGMNWIHLPASKYQFRYQNRVSNCQIEAWINYKDLISLPAEGQWSKMAPLRIMSFDIECAGRKGVFPDPSIDPVIQIASIVTQYGDSTPFVRNVFCVDTCSQIVGTQVYEFQNQAEMLSSWSKFVRDVDPDVLIGYNICNFDIPYLLDRAKSLRIHNFPLLGRIHNFFSVAKETTFSSKAYGTRESKTTSIPGRLQLDMLQVMQRDFKLRSYSLNAVCSQFLGEQKEDVHYSIITDLQNGTADSRRRLAIYCLKDAYLPQRLMDKLMCFVNYTEMARVTGVPFNFLLARGQQIKVISQLFRKALQHDLVVPNIRVNGTDEQYEGATVIEPIKGYYDTPIATLDFSSLYPSIMQAHNLCYTTLLDSNTAELLKLKQDVDYSVTPNGDYFVKPHVRKGLLPIILADLLNARKKAKADLKKETDPFKKAVLDGRQLALKVSANSVYGFTGATNGRLPCLAISSSVTSYGRQMIEKTKDVVEKRYRIENGYSHDAVVIYGDTDSVMVKFGVKTLPEAMKLGEEAANYVSDQFPNPIKLEFEKVYFPYLLISKKRYAGLFWTRTDTYDKMDSKGIETVRRDNCPLVSYVIDTALRKMLIDQDVEGAQLFTKKVISDLLQNKIDMSQLVITKALSKTDYAAKMAHVELAERMRKRDAGSAPAIGDRVAYVIIKGAQGDQFYMRSEDPIYVLENNIPIDAKYYLENQLSKPLLRIFEPILGEKASSLLHGDHTRTISMAAPSVGGIMKFAVKVETCLGCKAPIKKGKTALCENCLNRSAELYQRQVAQVNDLEVRFARLWTQCQRCQGSMHQDVICTSRDCPIFYMRIAEHKKLQQSVDLLKRFDEMSW P30666 MCM3_SCHPO BINDING 356..363; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPCC1682.02c; CHAIN 1..879; /note="DNA replication licensing factor mcm3"; /id="PRO_0000194100" MTELLADEVFKDRVRIFQEYLEHDTDDANVTLYQEAILRMLNMGQRRLIVNIDELRDYNRELADGVLLKPLEYVEPFDEALRNVVSTLIDPVVHKDLKDKLFYVGFRGSFGDHHVNPRTLRAMHLNKMISLEGIVTRCSFVRPKVIKSVHYCEATKRHHFKQYADATMNGGLSFQSTVYPTQDENGNPLSIEFGFSTFRDHQSISLQEMPERAPPGQLPRSIDILLDDDLVDTVKPGDRVNIVGQYRSMGSKTSGNTSATFRTVLLANNVVLLGNKPGLGNVGGGALDITDADIRNINKLARKKNVFELLSTSLAPSIYGYEYVKQAILLLLLGGTEKNLTNGTHIRGDINILMVGDPSTAKSQLLRFVLNTAPLAIATTGRGSSGVGLTAAVTTDKETGERRLEAGAMVLADRGVVCIDEFDKMSDIDRVAIHEVMEQQTVTIAKAGIHTSLNARCSVIAAANPIYGQYDIRKDPHQNIALPDSMLSRFDLLFIVTDDIDDKKDRALSEHVLRMHRYLPPGVEPGTPVRDSLNSVLNVGATNAAGVSTENVEQEVETPVWETFSSLLHANARTKKKELLNINFVRKYIQYAKSRIHPILNQATAEYITNIYCGLRNDDLQGNQRRTSPLTARTLETLIRLSTAHAKARLSSVVEVKDAKAAEKILRYALFREVVKPKRKKHKKQRLEAGEEFDSEDDNSDDMDIEESEEEMDTNMVIDSGSRRVTRSQNATSQSQESGSEIGSSIAGTAGSYNVGTSNTQLSWPSTHSTLPATSRELASSDRNINTGTSVASEVSASVSEQSTVSLPREKMSVFMARLASLTKSELFSEECASLEDVLESINNIEDDVGFSREEAIVALKEMDAQNKIMFSDNVVYRI P30776 RAD21_SCHPO PTM: Hyperphosphorylated during S and G2 phases.; PTM: Proteolytic cleavage of a fraction of hyperphosphorylated form at the onset of anaphase may be essential for the proper progression of anaphase and sister chromatid separation. MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 547; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 553; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC338.17c; CHAIN 1..628; /note="Cohesin subunit rad21"; /id="PRO_0000097871" MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAIIDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNESPEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLFDAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVISVKQDVAIQNEITLTAKRGMLLSSL P31209 PABP_SCHPO MOD_RES 167; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A7.04c; CHAIN 1..653; /note="Polyadenylate-binding protein, cytoplasmic and nuclear"; /id="PRO_0000081718" MPSTDLKKQADAAVESDVNTNNEAVESSTKEESSNTPSTETQPEKKAEEPEAAAEPSESTSTPTNASSVATPSGTAPTSASLYVGELDPSVTEAMLFELFNSIGPVASIRVCRDAVTRRSLGYAYVNFHNMEDGEKALDELNYTLIKGRPCRIMWSQRDPSLRKMGTGNVFIKNLDPAIDNKALHDTFSAFGKILSCKVAVDELGNAKGYGFVHFDSVESANAAIEHVNGMLLNDKKVYVGHHVSRRERQSKVEALKANFTNVYIKNLDTEITEQEFSDLFGQFGEITSLSLVKDQNDKPRGFGFVNYANHECAQKAVDELNDKEYKGKKLYVGRAQKKHEREEELRKRYEQMKLEKMNKYQGVNLFIKNLQDEVDDERLKAEFSAFGTITSAKIMTDEQGKSKGFGFVCYTTPEEANKAVTEMNQRMLAGKPLYVALAQRKEVRRSQLEAQIQARNQFRLQQQVAAAAGIPAVQYGATGPLIYGPGGYPIPAAVNGRGMPMVPGHNGPMPMYPGMPTQFPAGGPAPGYPGMNARGPVPAQGRPMMMPGSVPSAGPAEAEAVPAVPGMPERFTAADLAAVPEESRKQVLGELLYPKVFVREEKLSGKITGMLLEMPNSELLELLEDDSALNERVNEAIGVLQEFVDQEPGFTE P31317 OTC_SCHPO ACT_SITE 276; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P00480" BINDING 63..66; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 114; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 141; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 144; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 172; /ligand="L-ornithine"; /ligand_id="ChEBI:CHEBI:46911"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 236; /ligand="L-ornithine"; /ligand_id="ChEBI:CHEBI:46911"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 240; /ligand="L-ornithine"; /ligand_id="ChEBI:CHEBI:46911"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 241; /ligand="L-ornithine"; /ligand_id="ChEBI:CHEBI:46911"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 276..277; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P00480"; BINDING 303; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P00480" CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000269|PubMed:1313366, ECO:0000269|PubMed:18849471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19514; Evidence={ECO:0000305|PubMed:1313366, ECO:0000305|PubMed:18849471}; TRANSIT 1..?; /note="Mitochondrion" SPAC4G9.10; CHAIN ?..327; /note="Ornithine carbamoyltransferase, mitochondrial"; /id="PRO_0000020346" MSFKKFPRHLLSIRDLSRGEIVKLIDRSSEIKQAYKQNFQNRRSVQMSGLSSQNVAMIFSKRSTRTRVSVESAVSCLGGNAMFLGKDDIQLGVNESLYDTSKVISSMVSGIVARVNKYSDVATLAKHASCPVINGLCDTFHPLQALADLLTIKETFKSFDGLKVAWVGDANNVLHDLMIANAKVGIHTSVAKPKDVNVRDDILSIVNEAANENGSTFEIVNDPKVAVKNADIVVTDTWISMGQEAEKEQRLKQFTGFQVTGEIMKLAKPSCKFMHCLPRHPEEVSDEVFYGENSLVFQEAENRKWTTVAVLEALLVNRGEILPPASA P31318 ARG56_SCHPO ACT_SITE 703; /evidence="ECO:0000255|PROSITE-ProRule:PRU10010" CATALYTIC ACTIVITY: Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000269|PubMed:1313366}; CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000269|PubMed:1313366}; TRANSIT 1..59; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: The protein precursor is probably cleaved into the two biologically active enzymes, the kinase and the reductase. {ECO:0000305|PubMed:1313366}. SPAC4G9.09c; CHAIN 60..550; /note="Acetylglutamate kinase"; /evidence="ECO:0000255"; /id="PRO_0000002071"; CHAIN 551..885; /note="N-acetyl-gamma-glutamyl-phosphate reductase"; /evidence="ECO:0000255"; /id="PRO_0000002072" MLIELQQIVKSGLVRNGAKHCTKRSLLCSNASVIASKRFQGSFAPGQQQPLNPLAKPIEQDRDAIIRILSSIGSRREVEQYLRYFTSFEAQRFAIIKVGGAIITDELDTLAQSLAFLNHVGLYPIVVHGAGPQLNKILASRNVEPEYSDGIRITDAETLSVARKVFLEENAKLVDALEKLGTRARPITGGVFQAEYLDKEKYKYVGKIVKVNKAPIEHSIRAGTLPILTSMAETASGQLLNVNADITAGELARVLKPLKVVYLNEKGGLINGETKKKISSIYLDREYDGLMKQPWVKYGTKLKIKEIKELLDTLPRTSSVAIISTKDLQKELFTESGAGTLISRGFVINKHDSLDSIPDAALENLIIQKNSLAAPSESLKQFKDTLKDRKLRIYSDSFNESVAIVDTTDSSLPVLLAFGAADNNWLNNVVDSILTTLKADFPSLLWRLQPSAKNLEWFFSKSEGTLFANNFYYFWYGVKDLNKISKFIQSDKPFADAIIQTQSTKPPTASSTTNNPSSSQINQKRSYSTSSLFSKNKKMNRSLFLKGGKRFFSAEAQKTQKPLKAVSSKPAKVVLLGARGYTGKNLIGLINTHPYLELSHVSSRELEGTKLPGYTKKEIQYVNLSTDDVKKLEEEGAVDAWVMALPNGVCKPYVDALTSANGKSVIVDLSADYRFEPSWQYGLPELNDREALRNSKRISNPGCYATGSQVGLTPILSLIDGQPSIFGVSGYSGAGTKPSPKNDLNVLTNNLIPYSLTDHIHEREISYRLKQPVAFIPHVAQWFQGITLTINVPLKKSITSRELRNLYQDRYNGEPLIHVQGDVPLVKDNAHKHHVSVGGFGVHSSGKRAVIVVTIDNLLKGAATQALQNLNLSCGYDEYAGIHLD P32372 RAD4_SCHPO MOD_RES 592; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C4.18c; STRAND 11..16; /evidence="ECO:0007829|PDB:4BU0"; STRAND 38..41; /evidence="ECO:0007829|PDB:4BU0"; STRAND 46..50; /evidence="ECO:0007829|PDB:4BU0"; STRAND 52..54; /evidence="ECO:0007829|PDB:4BU0"; STRAND 67..70; /evidence="ECO:0007829|PDB:4BU0"; STRAND 106..111; /evidence="ECO:0007829|PDB:4BU0"; STRAND 133..135; /evidence="ECO:0007829|PDB:4BU0"; STRAND 141..147; /evidence="ECO:0007829|PDB:4BU0"; STRAND 161..163; /evidence="ECO:0007829|PDB:4BU0"; STRAND 307..310; /evidence="ECO:0007829|PDB:4BMD"; STRAND 342..345; /evidence="ECO:0007829|PDB:4BMD"; STRAND 361..363; /evidence="ECO:0007829|PDB:4BMD"; STRAND 401..406; /evidence="ECO:0007829|PDB:4BMD"; STRAND 425..429; /evidence="ECO:0007829|PDB:4BMD"; STRAND 435..439; /evidence="ECO:0007829|PDB:4BMD"; STRAND 462..465; /evidence="ECO:0007829|PDB:4BMD" HELIX 19..31; /evidence="ECO:0007829|PDB:4BU0"; HELIX 55..63; /evidence="ECO:0007829|PDB:4BU0"; HELIX 74..83; /evidence="ECO:0007829|PDB:4BU0"; HELIX 116..126; /evidence="ECO:0007829|PDB:4BU0"; HELIX 150..157; /evidence="ECO:0007829|PDB:4BU0"; HELIX 166..174; /evidence="ECO:0007829|PDB:4BU0"; HELIX 180..183; /evidence="ECO:0007829|PDB:4BU0"; HELIX 315..326; /evidence="ECO:0007829|PDB:4BMD"; HELIX 351..353; /evidence="ECO:0007829|PDB:4BMD"; HELIX 364..372; /evidence="ECO:0007829|PDB:4BMD"; HELIX 383..385; /evidence="ECO:0007829|PDB:4BMD"; HELIX 391..393; /evidence="ECO:0007829|PDB:4BMD"; HELIX 394..397; /evidence="ECO:0007829|PDB:4BMD"; HELIX 409..421; /evidence="ECO:0007829|PDB:4BMD"; HELIX 447..458; /evidence="ECO:0007829|PDB:4BMD"; HELIX 467..475; /evidence="ECO:0007829|PDB:4BMD"; HELIX 483..485; /evidence="ECO:0007829|PDB:4BMD" TURN 6..9; /evidence="ECO:0007829|PDB:4BU0"; TURN 90..96; /evidence="ECO:0007829|PDB:4BU0"; TURN 101..104; /evidence="ECO:0007829|PDB:4BU0"; TURN 302..305; /evidence="ECO:0007829|PDB:4BMD"; TURN 327..329; /evidence="ECO:0007829|PDB:4BMD" CHAIN 1..648; /note="S-M checkpoint control protein rad4"; /id="PRO_0000097153" MGSSKPLKGFVICCTSIDLKQRTEISTKATKLGAAYRSDFTKDVTHLIAGDFDTPKYKFAAKSRPDIKIMSSEWIPVLYESWVQGEDLDDGLLVDKHFLPTLFKCRVCLTNIGQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQRNAVLEPQYFQLDMPAEKIGLGAYVRLDPNTTEAKSYSENQKISKNKEKSGQSLAALAEEADLEPVIMKRGKKRDRSILWEELNNGKFEFSSRSEENSVLLDDFTPETVQPLEENELDTELNIENEAKLFKNLTFYLYEFPNTKVSRLHKCLSDNGGQISEFLSSTIDFVVIPHYFPVDELPIFSFPTVNEWWIERCLYYKKIFGIDEHALAKPFFRPSLVPYFNGLSIHLTGFKGEELSHLKKALTILGAVVHEFLGVQRSILLVNTNEPFSMKTRFKIQHATEWNVRVVGVAWLWNIIQSGKFIDQVSPWAIDKKENQEIKKFTNQNNMVFPTSDRDTRLQNSLAQQPIGHSTPHNSPSLLSVKKRQNNHIRSNTLIQLNSNSKDSTIFPRRSVTVPGDKIDTVWKSSVTKPETPTSPQEHVSYIDPDAQREKHKLYAQLTSNVDAIPPANDLQNQENGLLLITESHRKLRRR P32390 ARP3_SCHPO SPAC630.03; STRAND 8..12; /evidence="ECO:0007829|PDB:8UXW"; STRAND 14..21; /evidence="ECO:0007829|PDB:8UXW"; STRAND 28..33; /evidence="ECO:0007829|PDB:8UXW"; STRAND 35..38; /evidence="ECO:0007829|PDB:8UXW"; STRAND 88..91; /evidence="ECO:0007829|PDB:8UXW"; STRAND 93..95; /evidence="ECO:0007829|PDB:8UXW"; STRAND 125..130; /evidence="ECO:0007829|PDB:8UXW"; STRAND 153..159; /evidence="ECO:0007829|PDB:8UXW"; STRAND 169..173; /evidence="ECO:0007829|PDB:8UXW"; STRAND 181..186; /evidence="ECO:0007829|PDB:8UXW"; STRAND 191..197; /evidence="ECO:0007829|PDB:8UXW"; STRAND 207..210; /evidence="ECO:0007829|PDB:8UXW"; STRAND 265..271; /evidence="ECO:0007829|PDB:8UXW"; STRAND 277..282; /evidence="ECO:0007829|PDB:8UXW"; STRAND 330..334; /evidence="ECO:0007829|PDB:8UXW"; STRAND 403..405; /evidence="ECO:0007829|PDB:8UXW"; STRAND 421..423; /evidence="ECO:0007829|PDB:8UXW" HELIX 78..81; /evidence="ECO:0007829|PDB:8UXW"; HELIX 82..86; /evidence="ECO:0007829|PDB:8UXW"; HELIX 102..114; /evidence="ECO:0007829|PDB:8UXW"; HELIX 121..123; /evidence="ECO:0007829|PDB:8UXW"; HELIX 136..148; /evidence="ECO:0007829|PDB:8UXW"; HELIX 160..167; /evidence="ECO:0007829|PDB:8UXW"; HELIX 174..176; /evidence="ECO:0007829|PDB:8UXW"; HELIX 203..205; /evidence="ECO:0007829|PDB:8UXW"; HELIX 213..226; /evidence="ECO:0007829|PDB:8UXW"; HELIX 234..244; /evidence="ECO:0007829|PDB:8UXW"; HELIX 251..260; /evidence="ECO:0007829|PDB:8UXW"; HELIX 262..264; /evidence="ECO:0007829|PDB:8UXW"; HELIX 285..288; /evidence="ECO:0007829|PDB:8UXW"; HELIX 290..293; /evidence="ECO:0007829|PDB:8UXW"; HELIX 296..298; /evidence="ECO:0007829|PDB:8UXW"; HELIX 307..317; /evidence="ECO:0007829|PDB:8UXW"; HELIX 320..322; /evidence="ECO:0007829|PDB:8UXW"; HELIX 323..328; /evidence="ECO:0007829|PDB:8UXW"; HELIX 335..337; /evidence="ECO:0007829|PDB:8UXW"; HELIX 342..365; /evidence="ECO:0007829|PDB:8UXW"; HELIX 382..384; /evidence="ECO:0007829|PDB:8UXW"; HELIX 385..394; /evidence="ECO:0007829|PDB:8UXW"; HELIX 399..401; /evidence="ECO:0007829|PDB:8UXW"; HELIX 406..412; /evidence="ECO:0007829|PDB:8UXW"; HELIX 413..417; /evidence="ECO:0007829|PDB:8UXW" TURN 70..72; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..427; /note="Actin-related protein 3"; /id="PRO_0000089088" MASFNVPIIMDNGTGYSKLGYAGNDAPSYVFPTVIATRSAGASSGPAVSSKPSYMASKGSGHLSSKRATEDLDFFIGNDALKKASAGYSLDYPIRHGQIENWDHMERFWQQSLFKYLRCEPEDHYFLLTEPPLNPPENRENTAEIMFESFNCAGLYIAVQAVLALAASWTSSKVTDRSLTGTVVDSGDGVTHIIPVAEGYVIGSSIKTMPLAGRDVTYFVQSLLRDRNEPDSSLKTAERIKEECCYVCPDIVKEFSRFDREPDRYLKYASESITGHSTTIDVGFERFLAPEIFFNPEIASSDFLTPLPELVDNVVQSSPIDVRKGLYKNIVLSGGSTLFKNFGNRLQRDLKRIVDERIHRSEMLSGAKSGGVDVNVISHKRQRNAVWFGGSLLAQTPEFGSYCHTKADYEEYGASIARRYQIFGNSL P32747 PYRD_SCHPO ACT_SITE 267; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 122..126; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 126; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 146; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 171..175; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 234; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 264..269; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 264; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 306; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 335..336; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 358; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 387; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 408..409; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Note=Binds 1 FMN per subunit.; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=257 uM for (S)-dihydroorotate {ECO:0000269|PubMed:15196933}; KM=109 uM for decylubiquinone {ECO:0000269|PubMed:15196933}; Vmax=2 umol/min/mg enzyme {ECO:0000269|PubMed:15196933}; TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 168; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A10.12c; CHAIN 22..443; /note="Dihydroorotate dehydrogenase (quinone), mitochondrial"; /id="PRO_0000029896" MYQRSLFRGVAQGLKRSSVRFQSTSSGSSNGNFFLRHWKLLSVIGSFTAGVAIYDMSDVRSFIHGRIEMPLFHAFTTPEFSHRVAILAASWGITPKDRVADDPSLAVEVWGKKFCNPIGLAAGFDKQADAISGLLNFGFSYLEIGSVTPKPQPGNPKPRYFRLKPDLSVINRYGFNSIGHDAILAKIQKRVRKYIAKTSPQLLKQFDANPASCTDPAVLGVPRSLIPNKFLGINLGKNKNGNEIEDYVEGVRTFGNFADILVINVSSPNTPGLRNLQKKSALSTLLTAVVSERNKLNSPHPPVLVKIAPDLNEEELTDIADVLKKCKIDGVIVGNTTVQRPKTLKSTSHVEETGGLSGPPLKPIALNTLRTLRKHLSSDIPIIGCGGISSGKDAIEYARAGATMVQVYTALGYDGPVIAHKIKQEILAELKGKRWVDIIGKEE P32825 SXA2_SCHPO ACT_SITE 200; /evidence="ECO:0000250"; ACT_SITE 434; /evidence="ECO:0000250"; ACT_SITE 487; /evidence="ECO:0000250" SIGNAL 1..22; /evidence="ECO:0000255" SPAC1296.03c; CHAIN 23..507; /note="Carboxypeptidase sxa2"; /id="PRO_0000004288" CARBOHYD 38; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 45; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 259; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 260; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 300; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 448; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLSLFLKSLFAIIIIELTIIHALPTYTVHWKCSIQQANTSSASSNQTVQPRQHAAPSSDRIKSLPEFKGSLPELYSGYLEANSDKSLFYTYAPAVVDSETFIVWLQGGPGCAGTLGFFSENGPIEISQSSPSPSLNPESWTNFANMLWLDQPFGTGYSQGQAAYTTTIEEASSDFVNALKSFYQKFPHLMKKKLYLVGESYGSIWSANFAEALLSEPSLNINFMGVGIVSGLTADYETQEQITASIWVEHISKLGYYFNNTSSTISEEFKKRNKECQYDSVLNRLTFPTEQYPIWRPEYNFSTSTSLRKREALDGEDIGNVFNSISGCDLYSLSNFLLYLENSCVITYDVSLDCSFNEYNDPLITYLNREDVRSSLHATKASTALTSGEGVFADGCNFDLYKKIVSNNVESVLVEIIPRLTEKYKVSFLAGALDLQILWTGTLLALQNTTWNGWQGFTQSPGSLETTNGFTLDERNLAFTLSNSVGHMAPSKDPQMVREWLENTLLY P33075 KAD2_SCHPO BINDING 13..18; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 34; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 39; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 60..62; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 89..92; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 96; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 131; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 140..141; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 164; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 175; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168"; BINDING 203; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03168" CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:8496185}; SPAC4G9.03; CHAIN 1..220; /note="Adenylate kinase"; /id="PRO_0000158906" MAGMRLILVGPPGAGKGTQAPNIQKKYGIAHLATGDMLRSQVARQTELGKEAKKIMDQGGLVSDDIVTGMIKDEILNNPECKNGFILDGFPRTVVQAEKLTALLDELKLDLNTVLELQVDDELLVRRITGRLVHPGSGRSYHLEFNPPKVPMKDDVTGEPLIQRSDDNADALRKRLVTYHEQTTPVVEFYKKKGKWAAVDAAQKPEQVWEQIVAILEKAE P33277 GAP1_SCHPO SPBC646.12c; CHAIN 1..766; /note="GTPase-activating protein"; /id="PRO_0000056660" MTKRHSGTLSSSVLPQTNRLSLLRNRESTSVLYTIDLDMESDVEDAFFHLDRELHDLKQQISSQSKQNFVLERDVRYLDSKIALLIQNRMAQEEQHEFAKRLNDNYNAVKGSFPDDRKLQLYGALFFLLQSEPAYIASLVRRVKLFNMDALLQIVMFNIYGNQYESREEHLLLSLFQMVLTTEFEATSDVLSLLRANTPVSRMLTTYTRRGPGQAYLRSILYQCINDVAIHPDLQLDIHPLSVYRYLVNTGQLSPSEDDNLLTNEEVSEFPAVKNAIQERSAQLLLLTKRFLDAVLNSIDEIPYGIRWVCKLIRNLTNRLFPSISDSTICSLIGGFFFLRFVNPAIISPQTSMLLDSCPSDNVRKTLATIAKIIQSVANGTSSTKTHLDVSFQPMLKEYEEKVHNLLRKLGNVGDFFEALELDQYIALSKKSLALEMTVNEIYLTHEIILENLDNLYDPDSHVHLILQELGEPCKSVPQEDNCLVTLPLYNRWDSSIPDLKQNLKVTREDILYVDAKTLFIQLLRLLPSGHPATRVPLDLPLIADSVSSLKSMSLMKKGIRAIELLDELSTLRLVDKENRYEPLTSEVEKEFIDLDALYERIRAERDALQDVHRAICDHNEYLQTQLQIYGSYLNNARSQIKPSHSDSKGFSRGVGVVGIKPKNIKSSNTVKLSSQQLKKESVLLNCTIPEFNVSNTYFTFSSPSTDNFVIAVYQRGHSKVLVEVCICLDDVLQRRYASNPVVDLGFLTFEANKLYHLFEQLFLRK P33520 RES1_SCHPO SPBC725.16; CHAIN 1..637; /note="Cell division cycle-related protein res1/sct1"; /id="PRO_0000067072" MYNDQIHKITYSGVEVFEYTINGFPLMKRCHDNWLNATQILKIAELDKPRRTRILEKFAQKGLHEKIQGGCGKYQGTWVPSERAVELAHEYNVFDLIQPLIEYSGSAFMPMSTFTPQSNRKPTEAYRRNSPVKKSFSRPSHSLLYPYTSSNNMTSTSRMSGIHDALSLQSDFTRSPDMPSDSFTGSLHDIKASPFSSNNYAQSLLDYFLLPNTTQPPDFVYDRPSDWDVNAGIDEDGHTALHWAAAMGNLEMMHALLQAGANVVAVNYLQQTSLMRCVMFTMNYDLQTFEVVSELLQSAICMNDSFGQTVFHHIALLASSKSKMEAARYYMDILLQNLTATQSVDVAAQIINLQDDHGDTALLICARNGAKKCARLLLSFYASSSIPNNQGQYPTDFLSSKDMSFPENDDSPLNSKIEDNLIDNLKYPQSLDDHLSSKKPISYFSNKLTHQTLPNVFTQLSELSKCHEASLAEKQLTYNLAMEALEQTVRETETCQRLWNERTNNDENYLVNQREDLIHQCKKFLHTLKTARYYLETVQLHQLKKYVTYFSQIWSTDELADISETKNLVGHDTKTNRSSLSSKHEVDLFTAENEAAREKLVEQLCSLQAQRKQKINEILNLLSMGMYNTINTDQSGS P33532 BSU1_SCHPO SPAC17A2.01; CHAIN 1..526; /note="Vitamin B6 transporter bsu1"; /id="PRO_0000173433" MASKIASLFSPSETASKDQHENVAEDLELGTASSQSDGIHETNSEYDEKKREESPEVIDISNLISSDHPAHPQNWHWAKRWSIVFMFCLMQIYVIWTSNGFGSIEYSVMAQFNVSAQVATLCLSMNILGSGLGPMFLGPLSDIGGRKPVYFCSIFVYTVFNISCALPRNIVQMIISHFIIGVAGSTALTNVAGGIPDLFPEDTAGVPMSLFVWACAGGAIGAPMATGVDINAKYGWRWLYYINIIVGGFFLIVILIIPETLPIKVITRYENAKGRIVEGIPKNNLKEVLKKCKFVTTMGFRMMLTEPIILSMGLYNFYAYGISYFFLTAIWPVFYDTYKMSEMGASCTYLSGFVASTLLFLYQPIQDWIFRRDKAKNNGVARPEARFTSALFITLLFPAGMFLFAFTCHPPFPWMSPIVGNSMVTVANGHNWMCILNYLTDSYPLLSGSAVAAFTLPSFIGATVFAHVSQIMFNNMSVKWAVATMAFISISIPFIIYTFYFFGQRIRALSSLTGNKALKYLPLENN P33886 WIS1_SCHPO ACT_SITE 441; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 326..334; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 349; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; PTM: Dephosphorylated by pyp1 and pyp2. MOD_RES 168; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 469; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 473; /note="Phosphothreonine"; /evidence="ECO:0000250" SPBC409.07c; CHAIN 1..605; /note="Protein kinase wis1"; /id="PRO_0000086817" MSSPNNQPLSCSLRQLSISPTAPPGDVGTPGSLLSLSSSSSSNTDSSGSSLGSLSLNSNSSGSDNDSKVSSPSREIPSDPPLPRAVPTVRLGRSTSSRSRNSLNLDMKDPSEKPRRSLPTAAGQNNIGSPPTPPGPFPGGLSTDIQEKLKAFHASRSKSMPEVVNKISSPTTPIVGMGQRGSYPLPNSQLAGRLSNSPVKSPNMPESGLAKSLAAARNPLLNRPTSFNRQTRIRRAPPGKLDLSNSNPTSPVSPSSMASRRGLNIPPTLKQAVSETPFSTFSDILDAKSGTLNFKNKAVLNSEGVNFSSGSSFRINMSEIIKLEELGKGNYGVVYKALHQPTGVTMALKEIRLSLEEATFNQIIMELDILHKAVSPYIVDFYGAFFVEGSVFICMEYMDAGSMDKLYAGGIKDEGVLARTAYAVVQGLKTLKEEHNIIHRDVKPTNVLVNSNGQVKLCDFGVSGNLVASISKTNIGCQSYMAPERIRVGGPTNGVLTYTVQADVWSLGLTILEMALGAYPYPPESYTSIFAQLSAICDGDPPSLPDSFSPEARDFVNKCLNKNPSLRPDYHELANHPWLLKYQNADVDMASWAKGALKEKGEKRS P34208 CHK1_SCHPO ACT_SITE 137; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 16..24; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 38; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Phosphorylated. SPCC1259.13; CHAIN 1..496; /note="Serine/threonine-protein kinase chk1"; /id="PRO_0000085856" MAQKLDNFPYHIGREIGTGAFASVRLCYDDNAKIYAVKFVNKKHATSCMNAGVWARRMASEIQLHKLCNGHKNIIHFYNTAENPQWRWVVLEFAQGGDLFDKIEPDVGIDEDVAQFYFAQLMEGISFMHSKGVAHRDLKPENILLDYNGNLKISDFGFASLFSYKGKSRLLNSPVGSPPYAAPEITQQYDGSKVDVWSCGIILFALLLGNTPWDEAISNTGDYLLYKKQCERPSYHPWNLLSPGAYSIITGMLRSDPFKRYSVKHVVQHPWLTSSTPFRTKNGNCADPVALASRLMLKLRIDLDKPRLASSRASQNDSGFSMTQPAFKKNDQKELDRVEVYGALSQPVQLNKNIDVTEILEKDPSLSQFCENEGFIKRLAKKAKNFYEICPPERLTRFYSRASRETIIDHLYDSLRLLAISVTMKYVRNQTILYVNLHDKRKCLLQGVIELTNLGHNLELINFIKRNGDPLEWRKFFKNVVSSIGKPIVLTDVSQN P35551 FBRL_SCHPO BINDING 160..161; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 179..180; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 204..205; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 224..227; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; PTM: By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). MOD_RES 111; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 114; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2D10.10c; CHAIN 1..305; /note="rRNA 2'-O-methyltransferase fibrillarin"; /id="PRO_0000148526" MAYTPGSRGGRGGSRGGRGGFNGGRGGFGGGRGGARGGGRGGARGGRGGRGGARGGRGGSSGGRGGAKGGAKVIIEPHRHAGVFIARGKEDLLVTRNLVPGESVYNEKRISVDSPDGTKVEYRVWNPFRSKLAAGILGGLDNIYIKPGARVLYLGAANGTSVSHVADVVGPEGLVYAVEFSHRSGRDLLNMAKKRTNVIPIVEDARHVQKYRMLVGMVDVVFADVAQPDQARIVALNAAAFLKNEGGVVISVKASCIDSTADAAVVFAREVKKMQEEKIKPQEQLTLEPYERDHCIIVGKYLRHQ P35669 GSHB_SCHPO BINDING 128; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 146; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 146; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 148; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 150..153; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 233..235; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 239; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 291..294; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 330; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 387..396; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 391; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 398; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 420..423; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 446; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 473; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 475; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 481; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 484..485; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.3; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; MOD_RES 356; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3F10.04; CHAIN 1..498; /note="Glutathione synthetase large chain"; /id="PRO_0000211265" MEIEKYTPEQIEELGKGARDFAFAHGVVFTELSVSKEGRNIATQIPITLFPSVIPHGAFVEAVSVQKAYNKLYAKIANDYEFLRLHLQSITKYDEFMNKLWNLYQKHREAVAHLKENQFQPLSLGVFRSDYMVHQDDSFIGCKQVEFNTISVSFGGVSKAVSNLHAYCSQSGLYRKPLTTNYLTVNTSVSGICTGISNAVDAYRDYVKNITSKMNIASDNTKPIVLFVVKGGERNITDQRTLEYELLNRFHVISKRIDIAELNSLIHDKSSNKLYMKTSFTTYEVAVVYYRVGYALDDYPSQEAWDMRLTIENTLAIKCPSISTHLAGSKKIQQVLAESNALERFLEGDELQAVRSTFADMYPLDDTPRGKEGIKLAFEKPEDFVLKPQREGGGNNTYGKDIPGLLSKMPQEEWDSYILMRYINAVPSQNYILKGERPEKFDVVDEIGILGTIVWNIKTDEVVQNGQSGFICRTKPKKTNEGGVATGYASLSSIELSE P36581 CALX_SCHPO BINDING 136; /ligand="an alpha-D-glucoside"; /ligand_id="ChEBI:CHEBI:22390"; /evidence="ECO:0000250|UniProtKB:P14211"; BINDING 138; /ligand="an alpha-D-glucoside"; /ligand_id="ChEBI:CHEBI:22390"; /evidence="ECO:0000250|UniProtKB:P14211"; BINDING 154; /ligand="an alpha-D-glucoside"; /ligand_id="ChEBI:CHEBI:22390"; /evidence="ECO:0000250|UniProtKB:P14211"; BINDING 161; /ligand="an alpha-D-glucoside"; /ligand_id="ChEBI:CHEBI:22390"; /evidence="ECO:0000250|UniProtKB:P14211"; BINDING 391; /ligand="an alpha-D-glucoside"; /ligand_id="ChEBI:CHEBI:22390"; /evidence="ECO:0000250|UniProtKB:P14211" SIGNAL 1..22; /evidence="ECO:0000255" MOD_RES 551; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 553; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 555; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3C7.11c; CHAIN 23..560; /note="Calnexin homolog"; /id="PRO_0000004209" CARBOHYD 418; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 132..163; /evidence="ECO:0000250"; DISULFID 326..332; /evidence="ECO:0000250" MKYGKVSFLALLCSLYVRGSLADPESEQEPLVFNPTEVKAPLVEQFQGAWSERWIPSHAKRFVNGIEEMSYVGEWTVEESSGPGALKGEAGLVMKDEAAHHAISYEFDEPINEPEKDLVVQYEVNPEEGLNCGGAYLKLLAEPTHGEMSNSIDYRIMFGPDKCGVNDRVHFIFKHKNPLTGEYSEKHLDSRPASLLKPGITNLYTLIVKPDQTFEVRINGDVVRQGSLFYDFIPPVLPPVEIYDPEDIKPADWVDEPEIPDPNAVKPDDWDEDAPRMIPDPDAVKPEDWLEDEPLYIPDPEAQKPEDWDDEEDGDWIPSEIINPKCIEGAGCGEWKPPMIRNPNYRGPWSPPMIPNPEFIGEWYPRKIPNPDYFDDDHPSHFGPLYGVGFELWTMQPNIRFSNIYVGHSIEDAERLGNETFLPKLKAERELLSKQESMEKQSMHVDEESNQILEKFLDVYDIIKAKLPPNVAEKVDYYVETIIETPEIGIAIVAVLGSLTAVILTCYFYFFASSSPASLSTGTTEAEKEQQEKFKQETETEKIDVSYAPETESPTAKNED P36582 PCK1_SCHPO ACT_SITE 789; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 670..678; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 693; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; SPAC17G8.14c; CHAIN 1..988; /note="Protein kinase C-like 1"; /id="PRO_0000055740" MVQLDDALQDAYKKVEREESLILGAKAMVASTKNPEVKRRLESNIAVSENNIKYLRERIDALKVESGSERESQSDKDSSKKYSDSAKSTNSDDHLLSYNRSAFDLFNSEKPLSPEKISTMLQHLQMRLSIEQQCVSGIEKIMSLYSKEQKDKTDVIIKLKEGKQKVNLLKRSLKRYNELHIPFDISTPSSEEKQQASGLNFRGLAKPISGTLKVTIHSLRNIEHTSFLQTHSFTMPSYAVLYVDDAQVAKSRISQTDTWDETFIFDVHRAKEFQIIIYEKKKDFDIPIALILIPTTIIAEELRRKRNIQEMSETSWKPSIAESASRSDEKGSKSDPINAPNSSSSISTNSPLAPTAYYKLLSKSWLSLEPVGQICISLSFSKRTTKRQFPETGLGRQGAIRQKKEDVVASQVGHQFVQRQFYQIMRCAVCAELFSYSPGLQCENCSFVCHKKCVTKVLASCIAQSNSEKSDFGGLRYRIPHRFEPFNSLGAQWCAHCGFFLPLRRKDCFKCVECGITCHGQCAHLIPDYCGMSNDLKHQLLTELEVSKRPKKPELPNQENKTTNEKVYRKPLSSQNTFDTLPTISQGLLAATQPVTSVLNTSPLPKTPEKDRSLNVTPSSSTPTPASVLAPPSSASLSSSKDANRSVPESPRREKKNRVTLDDFTFLAVLGKGNFGKVMLAEYKVNKKFYAIKVLKKEAILKNEELESLKTEKHVFEVANKEKHPFLLNLFASFQTSTRVYFVMEYILGGDLMVHIQRQQFSVKRARFYGAEVCLALKYFHENGIAYRDLKLDNILLCPDGHIRIADYGLCKENMLLGNTTSTFCGTPEFMAPEILLEQQYSKDVDWWAFGVLMYQMLLGQSPFKGEDEEEIFDAILSDEPLFPINMPADAVSLLRGLLTRDPNQRLGSGPKDANEVMAHPFFASIVWDDLYNKLYEPSYKPLINDPRDLNNFDEEFTSACPTLTPVNTVLTRQQQECFRGFSSFATE P36583 PCK2_SCHPO ACT_SITE 808; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 689..697; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 712; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; MOD_RES 984; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC12D12.04c; CHAIN 1..1016; /note="Protein kinase C-like 2"; /id="PRO_0000055741" MDMIDEAITEVVRKIERERSVIHGALSMKRLTQNQTVHQQLHSNIEESKKSIIYLEERLEKLKLRKNGVRKSNSEKPSVGIEKNPSFSTTKSAKSFSSTSSNIDSNLDLLNYDTPLTISKISFLLQQLEFKLSVEEQYRKGIEKMAKLYEREHDRRSIAEAEKKYVESAQKITLLKQALKRYHDLHIEIDEEDVPSTESRGNLNARRPQSGLLKITVGSLRNVTHSAGISKQTEMIVAIRAEDLERARTRPSRTDRFNETFEIDLEKTNEVEIVVYEKKNEKLLLPVGLLWIRLSDLVEKQRRKKVEQEVSDKGWVSADKMINQRLSIFLPSALNNISKPESTDRPNTASGNQSVSAWFSLEPMGQINLTMNFTKHNTRKRPMDAGLGRQGAIRQRKESVHEVYGHKFLQHQFYQIMRCALCGEFLKNAAGMQCIDCHYTCHKKCYPKVVTKCISKSSDSASSEYEKINHRIPHHFESHTNIGANWCCHCGYILPLGRKTARKCTECGITAHAQCVHLVPDFCGMSMEMANRVISEIRTTKIYKAQQHKQKSSHHKHHHHKKSKSSSSKHKENDKASVSITTTTTPSITPADPVPTSPKPLAIEPVKRKPVHAGNLEVTSVSDNKLGATVQVVEQKVDDKADALTKPPSLDAVKEPIPVPSVETSVVAQDLTHKAKRIGLEDFTFLSVLGKGNFGKVMLAELKSEKQLYAIKVLKKEFILENDEVESTKSEKRVFLVANRERHPFLVNLHSCFQTETRIYFVMDFVSGGDLMLHIQQEQFSRRRAQFYAAEVCLALKYFHDNGIIYRDLKLDNILLSPDGHVKVADYGLCKEDMWHDNTTATFCGTPEFMAPEILLEQQYTRSVDWWAFGVLIYQMLLGQSPFRGEDEEEIFDAILSDEPLYPIHMPRDSVSILQQLLTRDPKKRLGSGPNDAEDVMTHPFFSNINWDDIYHKRTQPPYIPSLNSPTDTKYFDEEFTRELPVLTPVNSILTKEMQQHFEGFSYSCEDDKPSTTDNA P36592 RAD22_SCHPO MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 319; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC30D11.10; CHAIN 1..469; /note="DNA repair and recombination protein rad22"; /id="PRO_0000173891" MSFEQKQHVASEDQGHFNTAYSHEEFNFLQSSLTRKLGPEYVSRRSGPGGFSVSYIESWKAIELANEIFGFNGWSSSIRSINVDFMDENKENGRISLGLSVIVRVTIKDGAYHEDIGYGSIDNCRGKASAFEKCKKEGTTDALKRALRNFGNSLGNCMYDKYYLREVGKMKPPTYHFDSGDLFRKTDPAARESFIKKQKTLNSTRTVNNQPLVNKGEQLAPRRAAELNDEQTREIEMYADEELDNIFVEDDIIAHLAVAEDTAHPAANNHHSEKAGTQINNKDKGSHNSAKPVQRSHTYPVAVPQNTSDSVGNAVTDTSPKTLFDPLKPNTGTPSPKFISARAAAAAEGVVSAPFTNNFNPRLDSPSIRKTSIIDHSKSLPVQRASVLPIIKQSSQTSPVSNNSMIRDSESIINERKENIGLIGVKRSLHDSTTSHNKSDLMRTNSDPQSAMRSRENYDATVDKKAKKG P36594 RPB1_SCHPO BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 72; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 109; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 112; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 150; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 175; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 487; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 487; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="ligand shared with RPB2"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 489; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 489; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="ligand shared with RPB2"; /evidence="ECO:0000250|UniProtKB:P04050"; BINDING 491; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P04050" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. {ECO:0000269|PubMed:18257517}.; PTM: Following transcription stress, the elongating form of RNA polymerase II (RNA pol IIo) is polyubiquitinated via 'Lys-63'-linkages on Lys-1252 at DNA damage sites without leading to degradation: ubiquitination promotes RNA pol IIo backtracking to allow access by the transcription-coupled nucleotide excision repair (TC-NER) machinery. Subsequent def1-dependent polyubiquitination by the elongin complex via 'Lys-48'-linkages may lead to proteasome-mediated degradation; presumably at stalled RNA pol II where TC-NER has failed, to halt global transcription and enable 'last resort' DNA repair pathways. {ECO:0000250|UniProtKB:P04050}. MOD_RES 1489; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1499; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1506; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1529; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1531; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC28F2.12; CHAIN 1..1752; /note="DNA-directed RNA polymerase II subunit rpb1"; /id="PRO_0000073945" MSGIQFSPSSVPLRRVEEVQFGILSPEEIRSMSVAKIEFPETMDESGQRPRVGGLLDPRLGTIDRQFKCQTCGETMADCPGHFGHIELAKPVFHIGFLSKIKKILECVCWNCGKLKIDSSNPKFNDTQRYRDPKNRLNAVWNVCKTKMVCDTGLSAGSDNFDLSNPSANMGHGGCGAAQPTIRKDGLRLWGSWKRGKDESDLPEKRLLSPLEVHTIFTHISSEDLAHLGLNEQYARPDWMIITVLPVPPPSVRPSISVDGTSRGEDDLTHKLSDIIKANANVRRCEQEGAPAHIVSEYEQLLQFHVATYMDNEIAGQPQALQKSGRPLKSIRARLKGKEGRLRGNLMGKRVDFSARTVITGDPNLSLDELGVPRSIAKTLTYPETVTPYNIYQLQELVRNGPDEHPGAKYIIRDTGERIDLRYHKRAGDIPLRYGWRVERHIRDGDVVIFNRQPSLHKMSMMGHRIRVMPYSTFRLNLSVTSPYNADFDGDEMNMHVPQSEETRAEIQEITMVPKQIVSPQSNKPVMGIVQDTLAGVRKFSLRDNFLTRNAVMNIMLWVPDWDGILPPPVILKPKVLWTGKQILSLIIPKGINLIRDDDKQSLSNPTDSGMLIENGEIIYGVVDKKTVGASQGGLVHTIWKEKGPEICKGFFNGIQRVVNYWLLHNGFSIGIGDTIADADTMKEVTRTVKEARRQVAECIQDAQHNRLKPEPGMTLRESFEAKVSRILNQARDNAGRSAEHSLKDSNNVKQMVAAGSKGSFINISQMSACVGQQIVEGKRIPFGFKYRTLPHFPKDDDSPESRGFIENSYLRGLTPQEFFFHAMAGREGLIDTAVKTAETGYIQRRLVKAMEDVMVRYDGTVRNAMGDIIQFAYGEDGLDATLVEYQVFDSLRLSTKQFEKKYRIDLMEDRSLSLYMENSIENDSSVQDLLDEEYTQLVADRELLCKFIFPKGDARWPLPVNVQRIIQNALQIFHLEAKKPTDLLPSDIINGLNELIAKLTIFRGSDRITRDVQNNATLLFQILLRSKFAVKRVIMEYRLNKVAFEWIMGEVEARFQQAVVSPGEMVGTLAAQSIGEPATQMTLNTFHYAGVSSKNVTLGVPRLKEILNVAKNIKTPSLTIYLMPWIAANMDLAKNVQTQIEHTTLSTVTSATEIHYDPDPQDTVIEEDKDFVEAFFAIPDEEVEENLYKQSPWLLRLELDRAKMLDKKLSMSDVAGKIAESFERDLFTIWSEDNADKLIIRCRIIRDDDRKAEDDDNMIEEDVFLKTIEGHMLESISLRGVPNITRVYMMEHKIVRQIEDGTFERADEWVLETDGINLTEAMTVEGVDATRTYSNSFVEILQILGIEATRSALLKELRNVIEFDGSYVNYRHLALLCDVMTSRGHLMAITRHGINRAETGALMRCSFEETVEILMDAAASGEKDDCKGISENIMLGQLAPMGTGAFDIYLDQDMLMNYSLGTAVPTLAGSGMGTSQLPEGAGTPYERSPMVDSGFVGSPDAAAFSPLVQGGSEGREGFGDYGLLGAASPYKGVQSPGYTSPFSSAMSPGYGLTSPSYSPSSPGYSTSPAYMPSSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSATSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS P36596 ERG9_SCHPO CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000305|PubMed:8474436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32296; Evidence={ECO:0000305|PubMed:8474436}; CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000305|PubMed:8474436}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32300; Evidence={ECO:0000305|PubMed:8474436}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29704}; SPBC646.05c; CHAIN 1..460; /note="Squalene synthase"; /id="PRO_0000067451" MSLANRIEEIRCLCQYKLWNDLPSYGEDENVPQNIRRCYQLLDMTSRSFAVVIKELPNGIREAVMIFYLVLRGLDTVEDDMTLPLDKKLPILRDFYKTIEVEGWTFNESGPNEKDRQLLVEFDVVIKEYLNLSEGYRNVISNITKEMGDGMAYYASLAEKNDGFSVETIEDFNKYCHYVAGLVGIGLSRLFAQSKLEDPDLAHSQAISNSLGLFLQKVNIIRDYREDFDDNRHFWPREIWSKYTSSFGDLCLPDNSEKALECLSDMTANALTHATDALVYLSQLKTQEIFNFCAIPQVMAIATLAAVFRNPDVFQTNVKIRKGQAVQIILHSVNLKNVCDLFLRYTRDIHYKNTPKDPNFLKISIECGKIEQVSESLFPRRFREMYEKAYVSKLSEQKKGNGTQKAILNDEQKELYRKDLQKLGISILFVFFIILVCLAVIFYVFNIRIHWSDFKELNLF P36597 NMT1_SCHPO ACT_SITE 66; /evidence="ECO:0000250|UniProtKB:P43534" BINDING 114..117; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P43534" CATALYTIC ACTIVITY: Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]; Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893, Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190, ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692; Evidence={ECO:0000250|UniProtKB:P43534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757; Evidence={ECO:0000250|UniProtKB:P43534}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P43534}; MOD_RES 62; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P43534" SPCC1223.02; CHAIN 1..346; /note="4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase"; /id="PRO_0000211624" MSTNKITFLTNWEATPYHLPIFLAQTRGYYEREGIEVAILEPTNPSDVTALIGSGKVDMGLKAMIHTLAAKARGYPVTSFGSLLNEPFTGLITLKGNGINDFKDIKGKRIGYVGEFGKIQLDDLCSKFGLSPSDYTAIRCGMNIAPAIINGEIDGGIGIECMQQVELERWCVSQGRPRSDVQMLRIDRLANLGCCCFCTILYIAHDEFIAKHPDKIKAFLRAIHSATLDMLKDPVQTYKEYIHFKREMGSELHREQFERCFAYFSHDISNVPRDWNKVTNYSKRLGIIPQDFEPNCTNGYLTWELDPDEKDPMGKQEAIAEIQDEIKQKGGVFSGNSLRYVEPANL P36600 KAPR_SCHPO BINDING 143..277; /ligand="3',5'-cyclic AMP"; /ligand_id="ChEBI:CHEBI:58165"; /ligand_label="1"; /ligand_note="high affinity"; BINDING 224; /ligand="3',5'-cyclic AMP"; /ligand_id="ChEBI:CHEBI:58165"; /ligand_label="1"; /ligand_note="high affinity"; BINDING 233; /ligand="3',5'-cyclic AMP"; /ligand_id="ChEBI:CHEBI:58165"; /ligand_label="1"; /ligand_note="high affinity"; BINDING 278..412; /ligand="3',5'-cyclic AMP"; /ligand_id="ChEBI:CHEBI:58165"; /ligand_label="2"; /ligand_note="low affinity"; BINDING 344; /ligand="3',5'-cyclic AMP"; /ligand_id="ChEBI:CHEBI:58165"; /ligand_label="2"; /ligand_note="low affinity"; BINDING 353; /ligand="3',5'-cyclic AMP"; /ligand_id="ChEBI:CHEBI:58165"; /ligand_label="2"; /ligand_note="low affinity" MOD_RES 104; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC8C9.03; CHAIN 1..412; /note="cAMP-dependent protein kinase regulatory subunit"; /id="PRO_0000205414" MSFEEVYEELKALVDEQNPSDVLQFCYDFFGEKLKAERSVFRRGDTITESFSDGDESDFLSELNDMVAGPEAIGPDAKYVPELGGLKEMNVSYPQNYNLLRRQSVSTESMNPSAFALETKRTFPPKDPEDLKRLKRSVAGNFLFKNLDEEHYNEVLNAMTEKRIGEAGVAVIVQGAVGDYFYIVEQGEFDVYKRPELNITPEEVLSSGYGNYITTISPGEYFGELALMYNAPRAASVVSKTPNNVIYALDRTSFRRIVFENAYRQRMLYESLLEEVPILSSLDKYQRQKIADALQTVVYQAGSIVIRQGDIGNQFYLIEDGEAEVVKNGKGVVVTLTKGDYFGELALIHETVRNATVQAKTRLKLATFDKPTFNRLLGNAIDLMRNQPRARMGMDNEYGDQSLHRSPPSTKA P36601 RAD51_SCHPO BINDING 149..156; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC644.14c; CHAIN 1..365; /note="DNA repair protein rhp51"; /id="PRO_0000122924" MADTEVEMQVSAADTNNNENGQAQSNYEYDVNVQDEEDEAAAGPMPLQMLEGNGITASDIKKIHEAGYYTVESIAYTPKRQLLLIKGISEAKADKLLGEASKLVPMGFTTATEYHIRRSELITITTGSKQLDTLLQGGVETGSITELFGEFRTGKSQICHTLAVTCQLPIDMGGGEGKCLYIDTEGTFRPVRLLAVADRYGLNGEEVLDNVAYARAYNADHQLELLQQAANMMSESRFSLLVVDSCTALYRTDFSGRGELSARQMHLARFMRTLQRLADEFGIAVVITNQVVAQVDGISFNPDPKKPIGGNILAHSSTTRLSLRKGRGEQRICKIYDSPCLPESEAIFAINSDGVGDPKEIIAPV P36602 RIR1_SCHPO ACT_SITE 427; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 429; /note="Cysteine radical intermediate"; /evidence="ECO:0000250"; ACT_SITE 431; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 5..6; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="allosteric activator"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 11..17; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="allosteric activator"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 53; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="allosteric activator"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 57; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="allosteric activator"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 202; /ligand="GDP"; /ligand_id="ChEBI:CHEBI:58189"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 217; /ligand="GDP"; /ligand_id="ChEBI:CHEBI:58189"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 226..228; /ligand="dTTP"; /ligand_id="ChEBI:CHEBI:37568"; /ligand_note="allosteric effector that controls substrate specificity"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 243; /ligand="dTTP"; /ligand_id="ChEBI:CHEBI:37568"; /ligand_note="allosteric effector that controls substrate specificity"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 256; /ligand="dTTP"; /ligand_id="ChEBI:CHEBI:37568"; /ligand_note="allosteric effector that controls substrate specificity"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 263..264; /ligand="dTTP"; /ligand_id="ChEBI:CHEBI:37568"; /ligand_note="allosteric effector that controls substrate specificity"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 427; /ligand="GDP"; /ligand_id="ChEBI:CHEBI:58189"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 431; /ligand="GDP"; /ligand_id="ChEBI:CHEBI:58189"; /evidence="ECO:0000250|UniProtKB:P23921"; BINDING 603..606; /ligand="GDP"; /ligand_id="ChEBI:CHEBI:58189"; /evidence="ECO:0000250|UniProtKB:P23921" CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; SPAC1F7.05; CHAIN 1..811; /note="Ribonucleoside-diphosphate reductase large chain"; /id="PRO_0000187201" DISULFID 218..444; /note="Redox-active"; /evidence="ECO:0000250" MFVYKRDGRQEKVAFDKITARVSRLCYGLDSDHVDPVEITQKVISGVYPGVTTIELDNLAAETAATMTTKHPDYAILAARIAVSNLHKQTEKVFSTVVQQLHDYVNPKTDKPAPMISDKIYDIVMKHKDELDSAIIYDRDFTYNFFGFKTLERSYLLRIDGKVAERPQHMIMRVAVGIHGEDIEAAIETYNLMSQRYFTHASPTLFNAGTPRPQLSSCFLVTMKDDSIEGIYDTLKMCAMISKTAGGIGINIHNIRATGSYIAGTNGTSNGIVPMIRVYNNTARYVDQGGNKRPGAFAAYLEPWHADVMDFLELRKTHGNEDFRAREMFYALWIPDLFMQRVERNEQWTFFCPNEAPGLADVWGDEFVALYEKYEKENRGRRSLPAQKVWYAILQSQVETGNPFMLYKDSCNRKSNQKNVGTIRCSNLCTEIVEYSSPDEVAVCNLASVALPTFIKDGKYNFQKLHDVVKVVTRNLNKIIDVNYYPVPEARRSNMRHRPVGLGVQGLADAFFALRLPFESAGAKKLNIQIFETIYHAALEASCEIAQVEGTYESYEGSPASQGILQYDMWNVNPTDLWDWAELKEKIAKHGIRNSLLVAPMPTASTSQILGFNECFEPYTSNMYQRRVLSGEFQIVNPWLLKDLVERDLWNEDMKNKLVMLDGSIQAIPEIPQDLKDLYKTVWEISQKTVIDYAADRGPFIDQSQSLNIHLKDPSYGKITSMHFYGWKKGLKTGMYYLRTMAASAAIKFTVDPVALRARNEESNEENKKPVIKNGKAEISAEPTKEEIDIYNEKVLACSIKNPEACEMCSA P36603 RIR2_SCHPO ACT_SITE 173; /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" BINDING 135; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"; BINDING 166; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"; BINDING 166; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 169; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"; BINDING 229; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 263; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 266; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10014}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; Note=Binds 2 iron ions per subunit. {ECO:0000250}; SPBC25D12.04; CHAIN 1..391; /note="Ribonucleoside-diphosphate reductase small chain"; /id="PRO_0000190463" MGLEHLEEFSYPKEHGEEVEYDSEQGVRKIYVKSIKETFNFDNVSEEEKQEGGDYYLGKKEDELDEVVLRPNPHRFVLFPIKYHEIWQFYKKAEASFWTAEEIDLSKDLVDWDNKLNADERYFISTVLAYFAASDGIVNENLLERFSSEVQIPEARCVYGFQIMIENIHSETYSLLLDTYIREPKEKQRHFDAILTMGSIKAKAKWALRWINDEDSTYAIRLVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELICRDEGLHTDFACLMFSHLKHRPGRKVVEAIIVEAVDIEKEYFTDALPVSLLGMNKDLMCQYIEFVADRLLVALGNDKYYNVTNPFDFMENISLAGKTNFFEKKVSDYQIAGVMSGTKRAEKDDHTFTIDEDF P36604 BIP_SCHPO BINDING 43..46; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P11021"; BINDING 102; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P11021"; BINDING 232..234; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P11021"; BINDING 298..305; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P11021"; BINDING 369..372; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P11021" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P11021}; SIGNAL 1..24; /evidence="ECO:0000255" PTM: Partially N-glycosylated. SPAC22A12.15c; CHAIN 25..663; /note="Endoplasmic reticulum chaperone BiP"; /id="PRO_0000013585" CARBOHYD 29; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKKFQLFSILSYFVALFLLPMAFASGDDNSTESYGTVIGIDLGTTYSCVAVMKNGRVEIIANDQGNRITPSYVAFTEDERLVGEAAKNQAPSNPENTIFDIKRLIGRKFDEKTMAKDIKSFPFHIVNDKNRPLVEVNVGGKKKKFTPEEISAMILSKMKQTAEAYLGKPVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVIRIVNEPTAAAIAYGLDKTDTEKHIVVYDLGGGTFDVSLLSIDNGVFEVLATSGDTHLGGEDFDNRVINYLARTYNRKNNVDVTKDLKAMGKLKREVEKAKRTLSSQKSVRIEIESFFNGQDFSETLSRAKFEEINMDLFKKTLKPVEQVLKDSNLKKSEIDDIVLVGGSTRIPKVQELLESFFGKKASKGINPDEAVAYGAAVQAGVLSGEEGSDNIVLLDVIPLTLGIETTGGVMTKLIGRNTPIPTRKSQIFSTAVDNQNTVLIQVYEGERTLTKDNNLLGKFDLRGIPPAPRGVPQIEVTFEVDANGVLTVSAVDKSGKGKPEKLVIKNDKGRLSEEDIERMVKEAEEFAEEDKILKERIEARNTLENYAYSLKGQFDDDEQLGGKVDPEDKQAVLDAVEDVAEWLEIHGEDASKEEFEDQRQKLDAVVHPITQKLYSEGAGDADEEDDDYFDDEADEL P36606 NAH_SCHPO MOD_RES 449; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 451; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC977.10; HELIX 130..142; /evidence="ECO:0007829|PDB:2M7X"; HELIX 147..152; /evidence="ECO:0007829|PDB:2M7X" CHAIN 1..468; /note="Na(+)/H(+) antiporter"; /id="PRO_0000052405" CARBOHYD 287; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 319; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGWRQLDIDKVHLALIVAGGFITFFCYFSEVFRKKLLVGEAVLGSITGLIFGPHAAKLVDPFSWGDHGDYLTVEICRIVLDVRVFASAIELPGAYFQHNFRSIIVMLLPVMAYGWLVTAGFAYALFPQINFLGSLLIAGCITSTDPVLSALIVGEGPLAKKTPERIRSLLIAESGCNDGMAVPFFYFAIKLLTVKPSRNAGRDWVLLVVLYECAFGIFFGCVIGYLLSFILKHAQKYRLIDAISYYSLPLAIPLLCSGIGTIIGVDDLLMSFFAGILFNWNDLFSKNISACSVPAFIDQTFSLLFFTYYGTIIPWNNFNWSVEGLPVWRLIVFSILTLVCRRLPVVFSVKPLVPDIKTWKEALFVGHFGPIGVCAVYMAFLAKLLLSPDEIEKSIYESTTVFSTLNEIIWPIISFVILSSIIVHGFSIHVLVIWGKLKSLYLNRKVTKSDSDLELQVIGVDKSQEDYV P36607 RAD5_SCHPO BINDING 529..536; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" MOD_RES 18; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13G6.01c; CHAIN 1..1133; /note="DNA repair protein rad8"; /id="PRO_0000056127" MKRKVQKIIDEAPLEENSPPRFFDSDVEADSKPNDLTAANSIVDLKTNSQHENANAAGKEYGDSGVSESWVLDFLSVTGEKTISEFLAQKIWKTSNGDLNVAVDMYFDESFNIKNSNPDSESQKDTDASLTQMDQLSNTVSVKDLSINRNTNKKALNAVSPSLNLSSNSSVQDVSIDKEEMMKKQSRNALTPLDFIMKKNELMKYIGCFGVEAYSTASGTRTLQAGERIYLERQKLSIKSQSRNSRKKSKLLSINSSCYSNIVRFCNSDHHEIGKLPTEVASVISTLMEQGFWSFEAICIYSDNIIRFGSNVTLQVYCFINVNHPSLNRSPFTLATNSMQEEEEHLKASFAQNKRDHLLRLFTWIALEPDLEDCNTKESIHIDDILKTSSLPEARDESNSDLTPSSTEDEEDVVSDQLAILYDKVKTSGAELPSAPKPSTFALDLREYQKQALYWMCCKEEGVQSDGSAPKLHPLWSRFRFPKDSEFPEFFKCSSDDDNTHFYVNLYTGETTMLFPNSMPYHRGGILADEMGLGKTIEVLSLIHSRPCFSTDEIPEAFRHSKPSLPVASRTTLVVAPMSLLDQWHSEACKVSQGTKFRSMIYYGSEKPLDLKSCVIDTSTAPLIIITSYGVLLSEFSQQSHSSGLFSVHWFRVVLDEGHNIRNRESKTAKACHSISSQNRWVITGTPIVNKLDDLYSLIKFMRYEPWCNYTYWQTFVSLPYQSKDVLKALNVVQSILEFLVLRRTKETKDRNGNSIVTLPPKTVKIEYLDFSDSERKIYDSLYTKAKSTVNANIVAGTLFRNYTTILGLLLRLRQACCDPVLLSNMTINSETFDDFEFSVEQFNSLINQFVVTGKPIPSDILKIDTLKSFEALITECPICCNEPIQNPLLLNCKHACCGDCLSEHIQYQKRRNIIPPLCHTCRQPFNEQDVYKPFFVKNNGTQSTLLVGEEVKWKYWNRLQSVKLNGLLGQLRQLTHSSEPEKVVIFSQFTTFLDIIADVLESEKMGYARFDGTMSQQMRSTALETFRNDPDVNVLIISLKAGGVGLNLTCANHVFIMDPWWSWSVEAQAIDRIHRLGQEKPVFVTRYIVRDTVEERMLKIQERKNFITGTLGMSEGKQQVQSIEDIKMLFEY P36613 CGM2_SCHPO MOD_RES 310; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP16F5.02; CHAIN 1..322; /note="Cyclin mcs2"; /id="PRO_0000080505" MSADKFRDSTHYRDWIFTEEDLSKTRAKVNEKFTNIVRERMLEELSLQNKEASLEVLPPTLTVEEELELVNYYSFQLNALSSALSLPTHIRSTAILFFKRFYLINSVMEYSPKIISFTSLFLATKCNDHYISIEQFCKNMPKTTPEEVLEYEFNVCQSLKWDLYVWLPFRPLQGFLLDCQTVLPKVAVEKFYECHDLSKKFLIETLHSDIYFLHSPSIIALGAIYHTNPTICLQYIEAKKIPELQPLIISISANLKATKKFKIEKKKAQDYGRKLYFCMNPLRNKSSALYLKRKAEEESTNNNKWAKKFSTSSNVLDKNPFE P36614 PPE1_SCHPO ACT_SITE 112; /note="Proton donor"; /evidence="ECO:0000250" BINDING 51; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 53; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 79; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 79; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 111; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 161; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 235; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; SPCC1739.12; CHAIN 1..305; /note="Serine/threonine-protein phosphatase ppe1"; /id="PRO_0000058882" MFDLDEWIATVRKCKYLPEHQLKRLCEMVKVILMEESNIQPVRTPVTVCGDIHGQFYDLLELFRVGGELPSTNYIFMGDFVDRGYFSLETFTLFMLLKARYPDKITLLRGNHESRQITQVYGFYDECQTKYGNANVWKYCCQVFDFLTLAAVIDNKILCVHGGLSPEVRTLDQIRILARAQEIPHEGSFCDLMWSDPEDIESWTVSPRGAGWLFGSKVTTEFSQINDLTLIARAHQLVQEGYKYHFADKNLVTVWSAPNYCYRCGNVASVMKVDESLEPEFRIFSAVADEDRTVPPSRKRSEYFI P36615 CSK1_SCHPO ACT_SITE 129; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" BINDING 17..25; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 40; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; SPAC1D4.06c; CHAIN 1..306; /note="Serine/threonine-protein kinase csk1"; /id="PRO_0000085881" MKSVGHFVPWLTDIRHLTDGTISEVFVGERKNSKKLYVIKVQGLVFKRPPHDAMRGKLILESIGHPHIERIVDSFIDNEAGSVYLITSFKSFVLSDVMDEISIDTKCKIVLQISSALEYLEKHGILHRDIHPNNILLDSMNGPAYLSDFSIAWSKQHPGEEVQELIPQIGTGHYRAIETLFGCHSYGHEVDRWTFGILIAELFSNQALFDDGSSEGWPSELRLTSSIIQTLGTPNPSMWPELSTFPDWNKFIFHEYPPKPWSEILPSVDTSIQYIVSHLVTYSNRASPSFVIESFPKVSARLSQYA P36616 DSK1_SCHPO ACT_SITE 214; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 87..95; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 110; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Phosphorylated on Ser residue(s). SPBC530.14c; CHAIN 1..544; /note="Protein kinase dsk1"; /id="PRO_0000085927" MGSDGSSLSPKVSQPGHTEIVDHVSEKVITNGKNVNKKVNAEVDGKSMVEKVKTHEENAEDYHYGGYHPVYIGEEFHHRRYVVERKLGWGHFSTVWLAYDRAAKRRVALKVVRSAEHYRETSIDEIRILQKIREGDEKHLGKKHIISLLDYFVHRGPNGAHVCMVFEVLGENLLSLIQSYGHRGVPVGIVKQIAYQLLIALDYLHRECGIIHTDLKPENVLICIDQDALQHIEAPATTSSPTSNTSSSKTRNNTGYTAKAPIIKRGQSVDNSAQERKTFAKNPTKNSKPAGQVIPSSPFTSTLSRFPSLEGAVSEISLRDSQKHNSHPNSPFSSGDNSLILDGVNGSQEPVPKITVKIADLGNACWTRKHFTNDVQTRQYRSPEVILGCRWGASADCWSFACIIFELLTGDYLFDPRNGNSYSKEDDHIAQIIELLVNYPKQMALSGKHSRDLFNRRGELRNIHKLKFWPLKDVLEQKYHFSAELAQQISDFLSPMLCFDPAKRTNAGYMSNSPWLREVADPTFKIETTGATGEDVPGWATEIR P36617 RAD16_SCHPO MOD_RES 71; /note="Phosphoserine; by CK2"; /evidence="ECO:0000255" SPCC970.01; CHAIN 1..877; /note="DNA repair protein rad16"; /id="PRO_0000198856" METKVHLPLAYQQQVFNELIEEDGLCVIAPGLSLLQIAANVLSYFAVPGSLLLLVGANVDDIELIQHEMESHLEKKLITVNTETMSVDKREKSYLEGGIFAITSRILVMDLLTKIIPTEKITGIVLLHADRVVSTGTVAFIMRLYRETNKTGFIKAFSDDPEQFLMGINALSHCLRCLFLRHVFIYPRFHVVVAESLEKSPANVVELNVNLSDSQKTIQSCLLTCIESTMRELRRLNSAYLDMEDWNIESALHRSFDVIVRRQLDSVWHRVSPKTKQLVGDLSTLKFLLSALVCYDCVSFLKLLDTLVLSVNVSSYPSNAQPSPWLMLDAANKMIRVARDRVYKESEGPNMDAIPILEEQPKWSVLQDVLNEVCHETMLADTDAETSNNSIMIMCADERTCLQLRDYLSTVTYDNKDSLKNMNSKLVDYFQWREQYRKMSKSIKKPEPSKEREASNTTSRKGVPPSKRRRVRGGNNATSRTTSDNTDANDSFSRDLRLEKILLSHLSKRYEPEVGNDAFEVIDDFNSIYIYSYNGERDELVLNNLRPRYVIMFDSDPNFIRRVEVYKATYPKRSLRVYFMYYGGSIEEQKYLFSVRREKDSFSRLIKERSNMAIVLTADSERFESQESKFLRNVNTRIAGGGQLSITNEKPRVIVDLREFRSSLPSILHGNNFSVIPCQLLVGDYILSPKICVERKSIRDLIQSLSNGRLYSQCEAMTEYYEIPVLLIEFEQHQSFTSPPFSDLSSEIGKNDVQSKLVLLTLSFPNLRIVWSSSAYVTSIIFQDLKAMEQEPDPASAASIGLEAGQDSTNTYNQAPLDLLMGLPYITMKNYRNVFYGGVKDIQEASETSERKWSELIGPEAGRRLYSFFRKQLKDYE P36621 CAP_SCHPO MOD_RES 92; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 96; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC306.09c; CHAIN 1..551; /note="Adenylyl cyclase-associated protein"; /id="PRO_0000205705" MSDMINIRETGYNFTTILKRLEAATSRLEDLVESGHKPLPNMHRPSRDSNSQTHNISFNIGTPTAPTVSTGSPAVASLHDQVAAAISPRNRSLTSTSAVEAVPASISAYDEFCSKYLSKYMELSKKIGGLIAEQSEHVEKAFNLLRQVLSVALKAQKPDMDSPELLEFLKPIQSELLTITNIRDEHRTAPEFNQLSTVMSGISILGWVTVEPTPLSFMSEMKDSSQFYANRVMKEFKGKDDLQIEWVRSYLTLLTELITYVKTHFKTGLTWSTKQDAVPLKTALANLSASKTQAPSSGDSANGGLPPPPPPPPPSNDFWKDSNEPAPADNKGDMGAVFAEINKGEGITSGLRKVDKSEMTHKNPNLRKTGPTPGPKPKIKSSAPSKPAETAPVKPPRIELENTKWFVENQVDNHSIVLDSVELNHSVQIFGCSNCTIIIKGKLNTVSMSNCKRTSVVVDTLVAAFDIAKCSNFGCQVMNHVPMIVIDQCDGGSIYLSKSSLSSEVVTSKSTSLNINVPNEEGDYAERAVPEQIKHKVNEKGELVSEIVRHE P36623 PMGY_SCHPO ACT_SITE 15; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250|UniProtKB:P00950"; ACT_SITE 93; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P00950" BINDING 14..21; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950"; BINDING 27..28; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950"; BINDING 66; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950"; BINDING 93..96; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950"; BINDING 104; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950"; BINDING 120..121; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950"; BINDING 164..165; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00950" CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; PTM: The N-terminus is blocked. MOD_RES 37; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 96; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 166; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26F1.06; STRAND 9..12; /evidence="ECO:0007829|PDB:1FZT"; STRAND 28..30; /evidence="ECO:0007829|PDB:1FZT"; STRAND 57..64; /evidence="ECO:0007829|PDB:1FZT"; STRAND 83..89; /evidence="ECO:0007829|PDB:1FZT"; STRAND 121..124; /evidence="ECO:0007829|PDB:1FZT"; STRAND 158..162; /evidence="ECO:0007829|PDB:1FZT"; STRAND 182..184; /evidence="ECO:0007829|PDB:1FZT"; STRAND 189..191; /evidence="ECO:0007829|PDB:1FZT"; STRAND 193..197; /evidence="ECO:0007829|PDB:1FZT"; STRAND 199..201; /evidence="ECO:0007829|PDB:1FZT"; STRAND 203..205; /evidence="ECO:0007829|PDB:1FZT" HELIX 19..23; /evidence="ECO:0007829|PDB:1FZT"; HELIX 36..52; /evidence="ECO:0007829|PDB:1FZT"; HELIX 65..78; /evidence="ECO:0007829|PDB:1FZT"; HELIX 97..99; /evidence="ECO:0007829|PDB:1FZT"; HELIX 104..120; /evidence="ECO:0007829|PDB:1FZT"; HELIX 133..148; /evidence="ECO:0007829|PDB:1FZT"; HELIX 151..154; /evidence="ECO:0007829|PDB:1FZT"; HELIX 164..175; /evidence="ECO:0007829|PDB:1FZT" TURN 179..181; /evidence="ECO:0007829|PDB:1FZT" CHAIN 1..211; /note="Phosphoglycerate mutase"; /id="PRO_0000179838" MTTEAAPNLLVLTRHGESEWNKLNLFTGWKDPALSETGIKEAKLGGERLKSRGYKFDIAFTSALQRAQKTCQIILEEVGEPNLETIKSEKLNERYYGDLQGLNKDDARKKWGAEQVQIWRRSYDIAPPNGESLKDTAERVLPYYKSTIVPHILKGEKVLIAAHGNSLRALIMDLEGLTGDQIVKRELATGVPIVYHLDKDGKYVSKELIDN P36626 REC8_SCHPO PTM: Phosphorylated during prophase until after meiosis I. {ECO:0000269|PubMed:10207075, ECO:0000269|PubMed:10440376}. SPBC29A10.14; CHAIN 1..561; /note="Meiotic recombination protein rec8"; /id="PRO_0000097880" MFYNQDVLTKEKGGMGVIWLAATLGSKHSLRKLHKKDIMSVDIDEACDFVAFSPEPLALRLSSNLMIGVTRVWAHQYSFFHSQVSTLHLRVRKELDHFTSKPFKNIDIQNEQTNPKQLLLAEDPAFIPEVSLYDAFNLPSVDLHVDMSSFTQPKENPNISVLETLPDSTSYLINTSQNYSLRNNVSSFVYEDSRAFSTEEPLDFEFDENGDIQELTKGTINSDPSLQAASQHSNLGSVQREYNSEEQESRIHMFEIDEDVLPLPVPLQSVMDSEHNENEPRALKRRKVQKLLEPDENIELSTRTLSQWRKNYVERMIALEATKYVRRRGASSAKKKELNKFFDWESFHPLLKPWIEKLKPSNNTPSEIDDVLRNIDTSEVEVGRDVQGELGLNIPWNTSSRSNSAINSKSHSQTGSEHSTPLLDTKYRKRLPHSPSMPSRVEFLPALESSQFHETLNSELSLQLSDDFVLYKNTQEENAHLMLSMEKECANFYEYAKTAIYENNGRITFSSLLPNDLKRPVVAQAFSHLLSLATKSAFLVKQDKPYSEISVSLNLKSTDAI P36629 U2AF2_SCHPO SPBC146.07; STRAND 154..156; /evidence="ECO:0007829|PDB:7C08" HELIX 108..118; /evidence="ECO:0007829|PDB:4YH8"; HELIX 125..127; /evidence="ECO:0007829|PDB:4YH8"; HELIX 147..152; /evidence="ECO:0007829|PDB:4YH8" TURN 119..121; /evidence="ECO:0007829|PDB:4YH8"; TURN 140..143; /evidence="ECO:0007829|PDB:7C07" CHAIN 1..517; /note="Splicing factor U2AF 59 kDa subunit"; /id="PRO_0000081993" MDLSSRLSSGSSRIPKRHRDYRDEEPRRERGSGGIGREDPRGHYGSERPRRRRRDESDFRRHRESRERSYREDERPRRERRYDDYEPRSLRYSSVGRSRSPPPSRERSVRSIEQELEQLRDVTPINQWKRKRSLWDIKPPGYELVTADQAKMSGVFPLPGAPRAAVTDPEKLLEFARSAEGSIIAPPPPLQPGASRQARRLVVTGIPNEFVEDAFVSFIEDLFISTTYHKPETKHFSSVNVCKEENFAILEVATPEDATFLWGLQSESYSNDVFLKFQRIQNYIVPQITPEVSQKRSDDYAKNDVLDSKDKIYISNLPLNLGEDQVVELLKPFGDLLSFQLIKNIADGSSKGFCFCEFKNPSDAEVAISGLDGKDTYGNKLHAQFACVGLNQAMIDKSNGMAILTELAKASSQSIPTRVLQLHNLITGDEIMDVQEYEDIYESVKTQFSNYGPLIDIKIPRSIGTRNSGLGTGKVFVRYSDIRSAEVAMEEMKGCKFNDRTIVIAFYGEDCYKANAW P36630 CG22_SCHPO PTM: Phosphorylated. {ECO:0000269|PubMed:11163211}. SPAPB2B4.03; CHAIN 1..411; /note="G2/mitotic-specific cyclin cig2"; /id="PRO_0000080401" MALYSISKPVGSKINKHSYQDENTLVGKQALSKGTEKTKLSTNFEINLPRRTVLSDVSNVGKNNADEKDTKKAKRSFDESNLSTNEEADKPVESKFVKKLKVYSKNADPSVETLQKDRVSNVDDHLSSNPLMAEEYAPEIFEYIRKLDLKCLPNPKYMDQQKELTWKMREILNEWLVEIHSNFCLMPETLYLAVNIIDRFLSRRSCSLSKFQLTGITALLIASKYEEVMCPSIQNFVYMTDGAFTVEDVCVAERYMLNVLNFDLSYPSPLNFLRKISQAEGYDAQTRTLGKYLTEIYLFDHDLLRYPMSKIAAAAMYLSRRLLRRGPWTPKLVESSGGYEEHELKEIAYIMLHYHNKPLEHKAFFQKYSSKRFLKASIFVHQLVRQRYSVNRTDDDDLQSEPSSSLTNDGH P36631 STE11_SCHPO PTM: Phosphorylation results in inactivation. {ECO:0000269|PubMed:12697825, ECO:0000269|PubMed:18257517}. MOD_RES 173; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:12697825"; MOD_RES 209; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:12697825" SPBC32C12.02; CHAIN 1..468; /note="Transcription factor ste11"; /id="PRO_0000048579" MSASLTAEQKDQKSSVKRPLNSFMLYRRDRQAEIPTSNHQSISRIIGQLWRNESAQVKKYYSDLSALERQKHMLENPEYKYTPKKRSTVRRRHKKVSPSSGSFVASDYVVLQQIAQSSKTLKQTEPEKPVNEEETLAALLAPALSYPKSGKSNLIETSELSCLSSSPMIRSHTIPSLSFTDQVSTTISTLDKSEQAPSSLGIYYRSPSSGSPIGRTKSVCLANKARIVPKRSMSSDGCVDKSYQMSKTPSLEANLPQNSSNCSARRVPKFDSKGTVSEQSNSDSPELSADKVLSHCSPIDARPSTPSCPNASISPKTPNTGDHYGFDGAEYLGTPLSVGSTTAYLYGQETELLSTPYCHTSYPAMSRLNSSSGYTCVSSSSVTNSGHTENNTWRSDEQSKGFVDINSFSQSLFSNGNYEFAAHSQELDDLFSQITDFTSTDPIASSLKDANSLGPSLLEPWLPNSNLF P37202 DIS3_SCHPO COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPBC26H8.10; CHAIN 1..970; /note="Exosome complex exonuclease dis3"; /id="PRO_0000166421" MSTVSGLKRPQSSEKNHRDRVFVRATRGKVQKVVREQYLRNDIPCQSRACPLCRSKLPKDSRGNVLEPILSEKPMFLEKFGHHYLIPDSNIFYHCIDALEHPNNFFDVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDESANDRNDRAIRNAASWFASHLASLGIKIVLLTDDRENARLAAEQGIQVSTLKDYVQYLPDSEILLDMVSAIADAIASKEQVESGTKNVYELHWSMSRLLACIKNGEVHKGLINISTYNYLEGSVVVPGYNKPVLVSGRENLNRAVQGDIVCIQILPQDQWKTEAEEIADDDEDVVVSTAAEPDSARINDLELITKRNAHPTAKVVGILKRNWRPYVGHVDNATIAQSKGGSQQTVLLTPMDRRVPKIRFRTRQAPRLVGRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRPFPKAVLDCLPEEGHNWKVPADKTHPLWKNRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGTDLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQKMQDPLTQGMRVLLKLSKILKQKRMDEGALNLASPEVRIQTDNETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAFPQTAVLRRHAAPPLTNFDSLQDILRVCKGMHLKCDTSKSLAKSLDECVDPKEPYFNTLLRILTTRCMLSAEYFCSGTFAPPDFRHYGLASPIYTHFTSPIRRYADVLAHRQLAAAIDYETINPSLSDKSRLIEICNGINYRHRMAQMAGRASIEYYVGQALKGGVAEEDAYVIKVFKNGFVVFIARFGLEGIVYTKSLSSVLEPNVEYVEDEYKLNIEIRDQPKPQTVQIQMFQQVRVRVTTVRDEHSGKQKVQITLVY P38937 CUT8_SCHPO PTM: The N-terminal part (residues 1 to 72) is polyubiquitinated by rhp6, which is required for the interaction with the proteasome. {ECO:0000269|PubMed:16096059}. SPAC17C9.13c; STRAND 94..96; /evidence="ECO:0007829|PDB:3Q5W"; STRAND 154..156; /evidence="ECO:0007829|PDB:3Q5W"; STRAND 181..185; /evidence="ECO:0007829|PDB:3Q5W" HELIX 35..38; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 44..57; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 60..66; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 74..90; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 101..121; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 122..125; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 133..148; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 157..159; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 160..178; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 191..200; /evidence="ECO:0007829|PDB:3Q5W"; HELIX 206..215; /evidence="ECO:0007829|PDB:3Q5W" TURN 127..129; /evidence="ECO:0007829|PDB:3Q5X"; TURN 201..205; /evidence="ECO:0007829|PDB:3Q5W" CHAIN 1..262; /note="Tethering factor for nuclear proteasome cut8"; /id="PRO_0000079568" METLSYSQIKKRKADFDEDISKRARQLPVGEQLPLSRLLQYSDKQQLFTILLQCVEKHPDLARDIRGILPAPSMDTCVETLRKLLINLNDSFPYGGDKRGDYAFNRIREKYMAVLHALNDMVPCYLPPYSTCFEKNITFLDAATNVVHELPEFHNPNHNVYKSQAYYELTGAWLVVLRQLEDRPVVPLLPLEELEEHNKTSQNRMEEALNYLKQLQKNEPLVHERSHTFQQTNPQNNFHRHTNSMNIGNDNGMGWHSMHQYI P39750 FEN1_SCHPO BINDING 34; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 47; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 71; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 87; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 159; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 159; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 161; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 180; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 182; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 232; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 234; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140"; BINDING 234; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03140" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03140}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000255|HAMAP-Rule:MF_03140}; PTM: Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. {ECO:0000255|HAMAP-Rule:MF_03140}. MOD_RES 350; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 351; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G6.06c; CHAIN 1..380; /note="Flap endonuclease 1"; /id="PRO_0000154037" MGIKGLAQVLSEHAPASVKHNDIKNYFGRKVAIDASMSLYQFLIQVRSQDGQQLMNEQGETTSHLMGMFYRTLRIVDNGIKPCFVFDGKPPTLKSGELAKRVARHQKAREDQEETKEVGTAEMVDRFAKRTVKVTRQHNDEAKRLLELMGIPFVNAPCEAEAQCAALARSGKVYAAASEDMDTLCFQAPVLLRHLTFSEQRKEPISEYNIEKALNGLDMSVEQFVDLCILLGCDYCEPIRGVGPARAVELIRQYGTLDRFVKEADRSKYPIPEDWPYEDARRLFLDAEVLPGEEIELKWKSPDADGIIQFLVKEKGFNEDRVKLGINRLEKASKTIPQGRLDSFFKPVPSSPKKPVDTKSKGSAKRKRDSNKGGESKKKR P39825 PROF_SCHPO SPAC4A8.15c; STRAND 19..24; /evidence="ECO:0007829|PDB:3D9Y"; STRAND 30..33; /evidence="ECO:0007829|PDB:3D9Y"; STRAND 62..64; /evidence="ECO:0007829|PDB:3D9Y"; STRAND 67..74; /evidence="ECO:0007829|PDB:3D9Y"; STRAND 76..83; /evidence="ECO:0007829|PDB:3D9Y"; STRAND 86..92; /evidence="ECO:0007829|PDB:3D9Y"; STRAND 94..102; /evidence="ECO:0007829|PDB:3D9Y" HELIX 3..8; /evidence="ECO:0007829|PDB:3D9Y"; HELIX 12..14; /evidence="ECO:0007829|PDB:3D9Y"; HELIX 41..52; /evidence="ECO:0007829|PDB:3D9Y"; HELIX 56..60; /evidence="ECO:0007829|PDB:3D9Y"; HELIX 108..125; /evidence="ECO:0007829|PDB:3D9Y" TURN 9..11; /evidence="ECO:0007829|PDB:3D9Y" CHAIN 1..127; /note="Profilin"; /id="PRO_0000199607" MSWQAYVDTSLLGTGKIDRAAIVSRAGDSVWAASAGFNLSPQEIQGLAAGFQDPPSMFGTGIILAGQKYITIRAEGRSIYGKLQKEGIICVATKLCILVSHYPETTLPGEAAKITEALADYLVGVGY P39964 CEF1_SCHPO SPAC644.12; CHAIN 1..757; /note="Pre-mRNA-splicing factor cdc5"; /id="PRO_0000197104" MVVLKGGAWKNTEDEILKAAVSKYGKNQWARISSLLVRKTPKQCKARWYEWIDPSIKKTEWSREEDEKLLHLAKLLPTQWRTIAPIVGRTATQCLERYQKLLDDLEAKENEQLGLISGEGAEAAAPVNDPNSRLRFGEAEPNLETLPALPDAIDMDEDEKEMLSEARARLANTQGKKAKRKDREKQLELTRRLSHLQKRRELKAAGINIKLFRRKKNEMDYNASIPFEKKPAIGFYDTSEEDRQNFREKREADQKIIENGIRNNEMESEGRKFGHFEKPKPIDRVKKPNKDAQEEKMRRLAEAEQMSKRRKLNLPSPTVSQDELDKVVKLGFAGDRARAMTDTTPDANYSTNLLGKYTQIERATPLRTPISGELEGREDSVTIEVRNQLMRNREQSSLLGQESIPLQPGGTGYTGVTPSHAANGSALAAPQATPFRTPRDTFSINAAAERAGRLASERENKIRLKALRELLAKLPKPKNDYELMEPRFADETDVEATVGVLEEDATDRERRIQERIAEKERLAKARRSQVIQRDLIRPSVTQPEKWKRSLENEDPTANVLLKEMIALISSDAINYPFGNSKVKGTANKVPDLSNEEIERCRLLLKKEIGQLESDDYIQFEKEFLETYSALHNTSSLLPGLVIYEEDDEDVEAAEKFYTNDIQRDLAKKALECNKLENRVYDLVRSSYEQRNFLIKKISHAWKALQTERKNLTCYEFLYNQERLALPNRLEAAEIELSKMQQIEAYAQQDYARVTGQN P40231 CSK2A_SCHPO ACT_SITE 160; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 49..57; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 72; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P68400}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P68400}; SPAC23C11.11; CHAIN 1..332; /note="Casein kinase II subunit alpha"; /id="PRO_0000085903" MNQTEAAPVVSVSRVYAHVNEEMPREYWDYENMQEVFGYQDNYEIIRKVGRGKYSEVFEGLNVLNNSKCIIKVLKPVKYKKIKREIKILQNLAGGPNIISLLDIVRDPESKTPSLIFEFVDNIDFRTLYPTLSDYDIRYYSYELLKALDFCHSRGIMHRDVKPHNVMIDHKKRKLRLIDWGLAEFYHAGMEYNVRVASRYFKGPELLVDFREYDYSLDIWSFGVMFAALIFKKDTFFRGRDNYDQLVKIAKVLGTDELFAYVQKYQIVLDRQYDNILGQYPKRDWYSFVNRDNRSLANDEAIDLLNRLLRYDHQERLTCQEAMAHPYFQVLK P40233 CKI1_SCHPO ACT_SITE 131; /note="Proton acceptor" BINDING 18..26; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; BINDING 41; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 329; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1347.06c; STRAND 12..20; /evidence="ECO:0007829|PDB:1CSN"; STRAND 25..31; /evidence="ECO:0007829|PDB:1CSN"; STRAND 36..44; /evidence="ECO:0007829|PDB:1CSN"; STRAND 65..67; /evidence="ECO:0007829|PDB:1EH4"; STRAND 71..77; /evidence="ECO:0007829|PDB:1CSN"; STRAND 80..86; /evidence="ECO:0007829|PDB:1CSN"; STRAND 137..139; /evidence="ECO:0007829|PDB:1CSN"; STRAND 142..144; /evidence="ECO:0007829|PDB:1CSN"; STRAND 150..152; /evidence="ECO:0007829|PDB:1CSN"; STRAND 159..162; /evidence="ECO:0007829|PDB:1CSN" HELIX 52..61; /evidence="ECO:0007829|PDB:1CSN"; HELIX 92..98; /evidence="ECO:0007829|PDB:1CSN"; HELIX 105..123; /evidence="ECO:0007829|PDB:1CSN"; HELIX 134..136; /evidence="ECO:0007829|PDB:1CSN"; HELIX 187..190; /evidence="ECO:0007829|PDB:1CSN"; HELIX 197..213; /evidence="ECO:0007829|PDB:1CSN"; HELIX 226..239; /evidence="ECO:0007829|PDB:1CSN"; HELIX 242..245; /evidence="ECO:0007829|PDB:1CSN"; HELIX 251..262; /evidence="ECO:0007829|PDB:1CSN"; HELIX 271..284; /evidence="ECO:0007829|PDB:1CSN"; HELIX 294..296; /evidence="ECO:0007829|PDB:1CSN" TURN 9..11; /evidence="ECO:0007829|PDB:1CSN"; TURN 32..35; /evidence="ECO:0007829|PDB:1CSN"; TURN 62..64; /evidence="ECO:0007829|PDB:1CSN"; TURN 99..101; /evidence="ECO:0007829|PDB:1CSN"; TURN 124..126; /evidence="ECO:0007829|PDB:1CSN"; TURN 145..148; /evidence="ECO:0007829|PDB:1CSN"; TURN 164..166; /evidence="ECO:0007829|PDB:1CSN"; TURN 182..184; /evidence="ECO:0007829|PDB:1CSN"; TURN 246..248; /evidence="ECO:0007829|PDB:1CSN" CHAIN 1..446; /note="Casein kinase I homolog 1"; /id="PRO_0000192861" MSGQNNVVGVHYKVGRRIGEGSFGVIFEGTNLLNNQQVAIKFEPRRSDAPQLRDEYRTYKLLAGCTGIPNVYYFGQEGLHNILVIDLLGPSLEDLLDLCGRKFSVKTVAMAAKQMLARVQSIHEKSLVYRDIKPDNFLIGRPNSKNANMIYVVDFGMVKFYRDPVTKQHIPYREKKNLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYERIGEKKQSTPLRELCAGFPEEFYKYMHYARNLAFDATPDYDYLQGLFSKVLERLNTTEDENFDWNLLNNGKGWQSLKSRNAETENQRSSKPPAPKLESKSPALQNHASTQNVVSKRSDYEKPFAEPHLNSASDSAEPNQNSLPNPPTETKATTTVPDRSGLATNQPAPVDVHDSSEERVTREQVQNATKETEAPKKKKSFWASILSCCSGSNEDT P40234 CKI2_SCHPO ACT_SITE 131; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 18..26; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 41; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 361; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP35G2.05c; CHAIN 1..435; /note="Casein kinase I homolog 2"; /id="PRO_0000192862" MNSQTSVVGVHYRVGRKIGEGSFGVIFDGMNLLNNQLIAIKFEPKKSEAPQLRDEYRTYKLLVGNAGIPNVYYFGQEGLHNILVIDLLGPSLEDLFEWCGRRFSVKTVAMTAKQMLSRVQTIHEKNLVYRDIKPDNFLIGRPSSRNANMVYMVDFGMAKYYRDPKTKQHIPYSERKSLSGTARYMSINTHLGREQSRRDDLESLGHVFMYFLRGSLPWQGLKAANNKHKYEKISEKKQSTSISELCAGFPNEFSKYMTYVRSLEFDEEPDYAFLQELFDDVLRANGDTNDGVYDWMLLNDGKGWESSSSHFSVVAMKRRKNYLGLNVVQNDDSRKKNSTLQTQNMRFKSSYGVRGPRNYSSFDALPSKNAPLVRQEQSASKKTIYAHSSRGYDRVRPMYVSQPSNNAVGVNHPNDNSDSEAKGGFFDMICCRCFS P40235 HHP1_SCHPO ACT_SITE 130; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 17..25; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 40; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC3H7.15; CHAIN 1..365; /note="Casein kinase I homolog hhp1"; /id="PRO_0000192864" MALDLRIGNKYRIGRKIGSGSFGDIYLGTNVVSGEEVAIKLESTRAKHPQLEYEYRVYRILSGGVGIPFVRWFGVECDYNAMVMDLLGPSLEDLFNFCNRKFSLKTVLLLADQLISRIEFIHSKSFLHRDIKPDNFLMGIGKRGNQVNIIDFGLAKKYRDHKTHLHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLVYFCRGSLPWQGLKATTKKQKYEKIMEKKISTPTEVLCRGFPQEFSIYLNYTRSLRFDDKPDYAYLRKLFRDLFCRQSYEFDYMFDWTLKRKTQQDQQHQQQLQQQLSATPQAINPPPERSSFRNYQKQNFDEKGGDINTTVPVINDPSATGAQYINRPN P40236 HHP2_SCHPO ACT_SITE 131; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 18..26; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 41; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC23C4.12; CHAIN 1..400; /note="Casein kinase I homolog hhp2"; /id="PRO_0000192865" MTVVDIKIGNKYRIGRKIGSGSFGQIYLGLNTVNGEQVAVKLEPLKARHHQLEYEFRVYNILKGNIGIPTIRWFGVTNSYNAMVMDLLGPSLEDLFCYCGRKFTLKTVLLLADQLISRIEYVHSKSFLHRDIKPDNFLMKKHSNVVTMIDFGLAKKYRDFKTHVHIPYRDNKNLTGTARYASINTHIGIEQSRRDDLESLGYVLLYFCRGSLPWQGLQADTKEQKYQRIRDTKIGTPLEVLCKGLPEEFITYMCYTRQLSFTEKPNYAYLRKLFRDLLIRKGYQYDYVFDWMILKYQKRAAAAAAASATAPPQVTSPMVSQTQPVNPITPNYSSIPLPAERNPKTPQSFSTNIVQCASPSPLPLSFRSPVPNKDYEYIPSSLQPQYSAQLRRVLDEEPAP P40371 PP2C1_SCHPO BINDING 109; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 109; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 110; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 275; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 314; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; SPCC4F11.02; CHAIN 1..347; /note="Protein phosphatase 2C homolog 1"; /id="PRO_0000057770" MKGSHPNAGSLLEPLHKLNPFSENSTSGHRKNASDHSADGETRPIAIEMKDSKGNTVPVGNSRPSKASNWLAGLMEDKNQRWRRSMEDTHICLYDFGGNQDDGFVAVYDGHAGIQASDYCQKNLHKVLLEKVRNEPDRLVTDLMDETFVEVNSKIAKATHNDICGCTAAVAFFRYEKNRTRRVLYTANAGDARIVLCRDGKAIRLSYDHKGSDANESRRVTQLGGLMVQNRINGVLAVTRALGDTYLKELVSAHPFTTETRIWNGHDEFFIIACDGLWDVVSDQEAVDFVRNFVSPREAAVRLVEFALKRLSTDNITCIVVNLTRNPGDLDDSGLTADNDSYSNDYY P40376 KAPB_SCHPO ACT_SITE 324; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 207..215; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 230; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11; MOD_RES 356; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC106.10; CHAIN 1..512; /note="cAMP-dependent protein kinase catalytic subunit"; /id="PRO_0000086047" MDTTAVASKGSTNVGSSTDTLSTSASLHPSMNAGSVNEYSEQQRHGTNSFNGKPSVHDSVGSDASVSNGHNNHNESSLWTSGIPKALEEATKSKKPDSLVSTSTSGCASAHSVGYQNIDNLIPSPLPESASRSSSQSSHQRHSRDGRGELGSEHGERRSAMDGLRDRHIRKVRVSQLLDLQRRRIRPADHTTKDRYGIQDFNFLQTLGTGSFGRVHLVQSNHNRLYYAIKVLEKKKIVDMKQIEHTCDERYILSRVQHPFITILWGTFQDAKNLFMVMDFAEGGELFSLLRKCHRFPEKVAKFYAAEVILALDYLHHNQIVYRDLKPENLLLDRFGHLKIVDFGFAKRVSTSNCCTLCGTPDYLAPEIISLKPYNKAADWWSLGILIFEMLAGYPPFYSENPMKLYENILEGKVNYPSYFSPASIDLLSHLLQRDITCRYGNLKDGSMDIIMHPWFRDISWDKILTRKIEVPYVPPIQAGMGDSSQFDAYADVATDYGTSEDPEFTSIFKDF P40377 MCM2_SCHPO BINDING 534..541; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPBC4.04c; CHAIN 1..830; /note="DNA replication licensing factor mcm2"; /id="PRO_0000194092" MDSFRKRGRRDSESLPFESENSSLGATPLSLPPSSPPPEFSDEAAEALVEEDIEDLDGEALDVEDEEGEDLFGEGMERDYQQNLELDRYDIEELDDDNDLEELDIGARRAVDARLRRRDIELDAAAGRTKPAAFLQDEDDDLDSNLGTGFTRHRHRIYDEYSPNVGALDESGELPLESIADVKADSIAEWVTLDPVRRTIAREFKNFLLEYTDENGTSVYGNRIRTLGEVNAESLMVNYAHLGESKPILAYFLANAPAPIFRIFDRVALEATLLHYPDYERIHSDIHVRITNLPTCFTLRDLRQSHLNCLVRVSGVVTRRTGLFPQLKYIRFTCTKCGATLGPFFQDSSVEVKISFCHNCSSRGPFVINSERTVYNNYQRITLQESPGTVPSGRLPRHREVILLADLVDVAKPGEEIDVTGIYRNNFDASLNTKNGFPVFATIIEANHISQLDGSGNTDDDFSLSRLTDDEEREIRALAKSPDIHNRIIASMAPSIYGHRSIKTAIAAALFGGVPKNINGKHKIRGDINVLLLGDPGTAKSQFLKYVEKTAHRAVFATGQGASAVGLTASVRKDPITNEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCTIIAAANPIGGRYNTTIPFNQNVELTEPILSRFDILQVVKDTVNPEIDEQLANFVVSSHIRSHPAFDPNMDVLKKVPTETGIDAKPIPQDLLRKYIHFAREKVFPRLQQMDEEKISRLYSDMRRESLATGSYPITVRHLESAIRLSEAFAKMQLSEFVRPSHIDKAIQVIIDSFVNAQKMSVKRSLSRTFAKYLI P40380 RUM1_SCHPO PTM: Phosphorylated by cig1-associated cdc2 which leads to increased stability. Phosphorylation by MAPK reduces cdc2 kinase inhibitor ability. {ECO:0000269|PubMed:12135491, ECO:0000269|PubMed:9303310, ECO:0000269|PubMed:9430640}. MOD_RES 13; /note="Phosphothreonine; by MAPK"; /evidence="ECO:0000269|PubMed:12135491"; MOD_RES 19; /note="Phosphoserine; by MAPK"; /evidence="ECO:0000269|PubMed:12135491"; MOD_RES 58; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:9430640"; MOD_RES 62; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:9430640" SPBC32F12.09; CHAIN 1..230; /note="Cyclin-dependent kinase inhibitor rum1"; /id="PRO_0000097531" MEPSTPPMRGLCTPSTPESPGSFKGVIDASLEGNSSIMIDEIPESDLPAPQVSTFPPTPAKTPKKQLLPNLMLQDRSNSLERCMEEDREHNPFLSSSDNQLLSRKKRKPTPPPSDGLYYVFRGKRIKKSFRPGTDLSTFKPKLLFADSAPSSSSDNPTSSVDLNDYSQIGILPPNLNSIGNKMFSLKSRVPSSSSGSFVAPPPQMRLPAYSSPQKSRSNTKDENRHNLLR P40381 SWI6_SCHPO MOD_RES 24; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 220; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 227; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 240; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 246; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC664.01c; STRAND 83..91; /evidence="ECO:0007829|PDB:2RSO"; STRAND 98..104; /evidence="ECO:0007829|PDB:2RSO"; STRAND 113..116; /evidence="ECO:0007829|PDB:2RSO"; STRAND 273..281; /evidence="ECO:0007829|PDB:1E0B"; STRAND 287..293; /evidence="ECO:0007829|PDB:1E0B"; STRAND 298..302; /evidence="ECO:0007829|PDB:1E0B" HELIX 118..122; /evidence="ECO:0007829|PDB:2RSO"; HELIX 125..135; /evidence="ECO:0007829|PDB:2RSO"; HELIX 303..309; /evidence="ECO:0007829|PDB:1E0B"; HELIX 311..319; /evidence="ECO:0007829|PDB:1E0B" TURN 268..272; /evidence="ECO:0007829|PDB:1E0B" CHAIN 1..328; /note="Chromatin-associated protein swi6"; /id="PRO_0000080217" MKKGGVRSYRRSSTSKRSVIDDDSEPELPSMTKEAIASHKADSGSSDNEVESDHESKSSSKKLKENAKEEEGGEEEEEDEYVVEKVLKHRMARKGGGYEYLLKWEGYDDPSDNTWSSEADCSGCKQLIEAYWNEHGGRPEPSKRKRTARPKKPEAKEPSPKSRKTDEDKHDKDSNEKIEDVNEKTIKFADKSQEEFNENGPPSGQPNGHIESDNESKSPSQKESNESEDIQIAETPSNVTPKKKPSPEVPKLPDNRELTVKQVENYDSWEDLVSSIDTIERKDDGTLEIYLTWKNGAISHHPSTITNKKCPQKMLQFYESHLTFRENE P40383 XRN1_SCHPO COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1637812}; SPAC17A5.14; CHAIN 1..1328; /note="5'-3' exoribonuclease 1"; /id="PRO_0000071394" MGIPKFFRWMSERYPLCSQLIENDRIPEFDNLYLDMNGILHNCTHKNDDHSSPPLPEEEMYIAIFNYIEHLFEKIKPKKLLYMAVDGCAPRAKMNQQRSRRFRTAKDAHDARLKAERNGEDFPEEQFDSNCITPGTTFMERVSRQLYYFIHKKVTNDSQWQNIEVIFSGHDCPGEGEHKIMEYIRTQKAQPSYNPNTRHCLYGLDADLIMLGLLSHDPHFCLLREEVTFGPASRNRSKELAHQKFYLLHLSLLREYLEFEFQECRSTFTFKYDLEKILDDFILLAFFVGNDFLPHLPGLHINEGALALMFSIYKKVMPSAGGYINEKGVINMARLELILLELENFEKEIFKAEVSETKNNGNSDKPSFDFLKYITESTNDIKAMTGEQKNYFLQIKKFLSSREPFIDFSANISSVDQRFLRRLCNDLHLSFSKIIKVDGTHLLRITFRDLEFNDEDEDEIEQDEIERVLQKYDNIPLLNEEQALKEKNVEKDFIQWKDDYYRSKVGFSYYDEEALKAMAERYVEGLQWVLFYYYRGCQSWGWYYNYHFAPKISDVLKGLDVKIDFKMGTPFRPFEQLMAVLPARSQALVPPCFRDLMVNSESPIIDFYPENFALDQNGKTASWEAVVIIPFIDETRLIDALASKDKFLTEEERKRNSFNAPTVFSLAEDYTSFYPSSLPSLFPDLVTRCIQKPYSLPSMEGKEYLVGLCPGVFLGAFGMVGFPSFHTLKHKAELVYHGINVFGNESRNPSVIVNVEDVKSALTSEQIAMQYVGKRIFVDWPYLREAYVESAMDESYMYLASNSTIEKRDLAEIEKSQWGRKCSHKIREYSKRFGVLFGDISLLLQVRPIKGLEYTREGALVKIFNESVLEDYPAQLVVEKIAIDDPRFTEREAPPVEVEYPPGTKAFHLGEYNYGRPAQITGCKDNKLIIWLSTAPGLDAQWGRVLVNDSKSKEKYYPSYIVAKLLNIHPLLLSKITSSFLISNGTKRENIGLNLKFDARNQKVLGFSRKSTKGWEFSNKTVALVKEYINTFPQLFNILTTHATKDNLTVKDCFPKDDTQQLAAVKHWIKEKGINSLTRVSLDEDALDSDIIKLIEEKASTIDSTYQVPKKVFGVPRYALLKPSQTRGILHSQEFALGDRVVYVQDSGKVPIAAYGTVVGIMLHHLDVVFDLPFMSGTTLDGRCSPYHGMQVEVSMVLNVTNPQFVVNTRAGKNRKTNVSANNVSQGTDSRLVTKPTSTFPSPPSPPSSSVWNKREHHPKPFSLHQVPPPESLIHKSKSKFSKGNHHSTNGTQSIRGRGGKRGKPLRSKELNRKHDHIVQPMGKLQIN P40384 SPO11_SCHPO ACT_SITE 98; /note="O-(5'-phospho-DNA)-tyrosine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01385, ECO:0000269|PubMed:12437782" BINDING 179; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q57815"; BINDING 229; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q57815" CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU01385, ECO:0000269|PubMed:12437782}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q57815}; SPAC17A5.11; CHAIN 1..345; /note="Meiotic recombination protein rec12"; /id="PRO_0000145477" MNSNDKKKVVRSWIEQFVHDFVEQLSKPTKDSVNVALKRRKHNSWNGSLDSKANERQKVKVFSFPRNETTIAQLFRVLDCVHEAVISDTVITKRDIYYRDVDLFKRQTVVDELLGDISNTIGCSRSDLNVEASAKGLVFGSIHIALENGTVITATKPLLISHHRISSITSTAKWVLVIEKEAVFQTLTEEALADTIIVTAKGFPDLMTRKFLVKLAKALPDAKFFGIFDWDPHGLCIYSCFKYGSNAYSHEPHSQLRNLQLLGPLYEDIFNKNQEFSLKLNKRDIKMITTLLQFEGFQKEPVVREQLQRMLFIQKKAEIQAILEFPSWIKGKLADADKSGKHSVR P40387 TPS1_SCHPO BINDING 104; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 158; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 294; /ligand="UDP"; /ligand_id="ChEBI:CHEBI:58223"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 294; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 299; /ligand="UDP"; /ligand_id="ChEBI:CHEBI:58223"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 299; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 332; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 393..401; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /evidence="ECO:0000250|UniProtKB:Q92410"; BINDING 397..401; /ligand="UDP"; /ligand_id="ChEBI:CHEBI:58223"; /evidence="ECO:0000250|UniProtKB:Q92410" CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; Evidence={ECO:0000250|UniProtKB:Q00764}; MOD_RES 40; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC328.03; CHAIN 1..513; /note="Alpha,alpha-trehalose-phosphate synthase [UDP-forming]"; /id="PRO_0000122500" MSDAHDTIKSLTGDASNSRRLIVVSNRLPITIKRKDNGTYDFSMSSGGLVSALSGLKKLMTFQWLGWCGQEIPEDEKPMIIQRLQDECSAIPVFLDDETADRHYNGFSNSILWPLFHYHPGEINFDEENWEAYRAANYAFAEAIVKNLQDGDLIWVQDYHLMVLPQMLRELIGDKFKDIKIGFFLHTPFPSSEIYRVLPVRNEILEGVLNCDLVGFHTYDYARHFLSACSRILNLSTLPNGVEYNGQMVSVGTFPIGIDPEKFSDALKSDVVKDRIASIERRLQGVKVIVGVDRLDYIKGVPQKFHAFEVFLEQYPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGRFGTVEYTPIHFLHKSVRFEELVALYNVSDVCLITSTRDGMNLVSYEYICTQQERHGALILSEFAGAAQSLNGSIVINPWNTEELANSIHDALTMPEKQREANENKLFRYVNKYTSQFWGQSFVGELQRIQHYSHPHPRRTNPILRTKSAQVLSMNSSS P40847 SAP1_SCHPO MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 19; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1672.02c; HELIX 34..46; /evidence="ECO:0007829|PDB:5JDK"; HELIX 48..50; /evidence="ECO:0007829|PDB:5JDK"; HELIX 56..71; /evidence="ECO:0007829|PDB:5JDK"; HELIX 78..98; /evidence="ECO:0007829|PDB:5JDK"; HELIX 107..131; /evidence="ECO:0007829|PDB:5JDK" CHAIN 1..254; /note="Switch-activating protein 1"; /id="PRO_0000097581" MEAPKMELKSYKRKNASLSPSSSPAKAQRTHLSLEEKIKLMRLVVRHKHELVDRKTSEFYAKIARIGYEDEGLAIHTESACRNQIISIMRVYEQRLAHRQPGMKTTPEEDELDQLCDEWKARLSELQQYREKFLVGKRKCDCNDEINERLKKLTEEQQNVDMLVAKVNFLSKHLHDNEEKLMQVNAKMDEVLAENKRLQQLLDHNDLLSKLEPPSAYAPHGVNMGTNMGANMGANMNAIRGGLHSSISPNLGDH P40848 XRN2_SCHPO SPAC26A3.12c; STRAND 18..20; /evidence="ECO:0007829|PDB:3FQD"; STRAND 49..55; /evidence="ECO:0007829|PDB:3FQD"; STRAND 67..69; /evidence="ECO:0007829|PDB:3FQD"; STRAND 95..102; /evidence="ECO:0007829|PDB:3FQD"; STRAND 194..198; /evidence="ECO:0007829|PDB:3FQD"; STRAND 229..232; /evidence="ECO:0007829|PDB:3FQD"; STRAND 248..255; /evidence="ECO:0007829|PDB:3FQD"; STRAND 292..296; /evidence="ECO:0007829|PDB:3FQD"; STRAND 336..338; /evidence="ECO:0007829|PDB:3FQD"; STRAND 369..371; /evidence="ECO:0007829|PDB:3FQD"; STRAND 712..715; /evidence="ECO:0007829|PDB:3FQD"; STRAND 719..722; /evidence="ECO:0007829|PDB:3FQD"; STRAND 757..761; /evidence="ECO:0007829|PDB:3FQD"; STRAND 776..778; /evidence="ECO:0007829|PDB:3FQD"; STRAND 780..782; /evidence="ECO:0007829|PDB:3FQD"; STRAND 796..800; /evidence="ECO:0007829|PDB:3FQD"; STRAND 828..830; /evidence="ECO:0007829|PDB:3FQD"; STRAND 833..839; /evidence="ECO:0007829|PDB:3FQD" HELIX 3..13; /evidence="ECO:0007829|PDB:3FQD"; HELIX 15..17; /evidence="ECO:0007829|PDB:3FQD"; HELIX 57..64; /evidence="ECO:0007829|PDB:3FQD"; HELIX 75..93; /evidence="ECO:0007829|PDB:3FQD"; HELIX 109..143; /evidence="ECO:0007829|PDB:3FQD"; HELIX 149..152; /evidence="ECO:0007829|PDB:3FQD"; HELIX 159..161; /evidence="ECO:0007829|PDB:3FQD"; HELIX 167..184; /evidence="ECO:0007829|PDB:3FQD"; HELIX 188..190; /evidence="ECO:0007829|PDB:3FQD"; HELIX 206..218; /evidence="ECO:0007829|PDB:3FQD"; HELIX 238..244; /evidence="ECO:0007829|PDB:3FQD"; HELIX 297..308; /evidence="ECO:0007829|PDB:3FQD"; HELIX 319..329; /evidence="ECO:0007829|PDB:3FQD"; HELIX 330..333; /evidence="ECO:0007829|PDB:3FQD"; HELIX 346..348; /evidence="ECO:0007829|PDB:3FQD"; HELIX 350..365; /evidence="ECO:0007829|PDB:3FQD"; HELIX 377..388; /evidence="ECO:0007829|PDB:3FQD"; HELIX 391..402; /evidence="ECO:0007829|PDB:3FQD"; HELIX 591..598; /evidence="ECO:0007829|PDB:3FQD"; HELIX 608..629; /evidence="ECO:0007829|PDB:3FQD"; HELIX 647..649; /evidence="ECO:0007829|PDB:3FQD"; HELIX 668..675; /evidence="ECO:0007829|PDB:3FQD"; HELIX 678..683; /evidence="ECO:0007829|PDB:3FQD"; HELIX 686..693; /evidence="ECO:0007829|PDB:3FQD"; HELIX 700..702; /evidence="ECO:0007829|PDB:3FQD"; HELIX 729..737; /evidence="ECO:0007829|PDB:3FQD"; HELIX 740..742; /evidence="ECO:0007829|PDB:3FQD"; HELIX 745..749; /evidence="ECO:0007829|PDB:3FQD"; HELIX 767..774; /evidence="ECO:0007829|PDB:3FQD"; HELIX 788..791; /evidence="ECO:0007829|PDB:3FQD"; HELIX 819..824; /evidence="ECO:0007829|PDB:3FQD"; HELIX 864..873; /evidence="ECO:0007829|PDB:3FQD" TURN 269..273; /evidence="ECO:0007829|PDB:3FQD"; TURN 403..405; /evidence="ECO:0007829|PDB:3FQD" CHAIN 1..991; /note="5'-3' exoribonuclease 2"; /id="PRO_0000071398" MGVPALFRLLSRKFAKVITPVIEAPTEKLPDGTEIEPDLSLPNPNGVECDNLYLDMNGIVHPCSHPEDRPAPETEDEMMVAVFEYTDRILAMVRPRQLLFIAIDGVAPRAKMNQQRSRRFRSSREAALKEEELQAFIEEAKQQGIPIDENATKKKSWDSNCITPGTPFMDTLAKSLRYYIINKLNSDPCWRNVRFILSDASVPGEGEHKIMEFIRSQRVKPEYDPNTHHVVYGLDADLIMLGLATHEPHFRVLREDVFFQQGSTKKTKEERLGIKRLDDVSETNKVPVKKPFIWLNVSILREYLEVELYVPNLPFPFDLERAIDDWVFFIFFVGNDFLPHLPSLDIRDGAVERLTEIWRASLPHMGGYLTLDGSVNLARAEVILSAVGNQEDDIFKRLKQQEDRRNENYRRRQQRESNQESESYVDNVVIQRSVETQSTEVVTSSKSTSVDTKPPKKTQKIDAPAPVDLVNLSEKTSNRSLGATNRELINNRAANRLGLSREAAAVSSVNKLAASALKAQLVSNETLQNVPLEDSIASSSAYEDTDSIESSTPVVHPIDTKVSNVGQKRKAPDSTEENENTDTVRLYEPGYRERYYEQKFHISPDEPEKIREAVKHYVHGLCWVLLYYYQGCPSWTWYYPYHYAPFAADFKDLASIDVKFELNQPFKPYEQLLGVLPAASKNNLPEKLQTLMTDENSEIIDFYPENFTIDLNGKKFEWQGVALLPFIDENRLLNAVSKIYPQLTEEESKRNEDGSTLLFISEHHPMFSELVKQLYSKKRQGKPLKLSGKMAHGLFGKVNTNDSVIPNVSVQCPIDVTSADALQKYGSIDDNQSISLVFEVPKSHFVHKSMLLRGVKMPNRVLTPEDINQVRAERSFSSRRNNGNSYRGGHQSYGVRRSYQSQSYSSRQSYTGVTNGFANGGVQPPWSGNGNFPRSNASYNSRGGHEGYGGRSRGGGYSNGPPAGNHYSSNRGKGYGYQRESYNNNNRNGYY P40984 UBC9_SCHPO ACT_SITE 93; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" SPAC30D11.13; STRAND 25..30; /evidence="ECO:0007829|PDB:3RCZ"; STRAND 34..46; /evidence="ECO:0007829|PDB:3RCZ"; STRAND 57..63; /evidence="ECO:0007829|PDB:3RCZ"; STRAND 74..79; /evidence="ECO:0007829|PDB:3RCZ"; STRAND 90..92; /evidence="ECO:0007829|PDB:3RCZ" HELIX 4..18; /evidence="ECO:0007829|PDB:3RCZ"; HELIX 95..97; /evidence="ECO:0007829|PDB:3RCZ"; HELIX 109..120; /evidence="ECO:0007829|PDB:3RCZ"; HELIX 131..139; /evidence="ECO:0007829|PDB:3RCZ"; HELIX 141..154; /evidence="ECO:0007829|PDB:3RCZ" TURN 52..55; /evidence="ECO:0007829|PDB:3RCZ"; TURN 66..70; /evidence="ECO:0007829|PDB:3RCZ"; TURN 99..102; /evidence="ECO:0007829|PDB:3RCZ" CHAIN 1..157; /note="SUMO-conjugating enzyme ubc9"; /id="PRO_0000082568" MSSLCKTRLQEERKQWRRDHPFGFYAKPCKSSDGGLDLMNWKVGIPGKPKTSWEGGLYKLTMAFPEEYPTRPPKCRFTPPLFHPNVYPSGTVCLSILNEEEGWKPAITIKQILLGIQDLLDDPNIASPAQTEAYTMFKKDKVEYEKRVRAQARENAP P40995 SCD1_SCHPO MOD_RES 583; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16E8.09; CHAIN 1..872; /note="Rho guanine nucleotide exchange factor scd1"; /id="PRO_0000080973" MAYFQDRKTSSRSLPSYINHSTQNLVGPRKDETNLSEYMKLRLLQSPSQVIYNLENTVSLYRRCLNLRKRLMDISELAAFFDSIHREALNSSFKILEFKDIEFDDPVTEIWLFCRLGYPLCALFNCLPVKQKLEVNSSVSLENTNVCKASLYRFMLMCKNELGLTDAALFSISEIYKPSTAPLVRALQTIELLLKKYEVSNTTKSSSTPSPSTDDNVPTGTLNSLIASGRRVTAELYETELKYIQDLEYLSNYMVILQQKQILSQDTILSIFTNLNEILDFQRRFLVGLEMNLSLPVEEQRLGALFIALEEGFSVYQVFCTNFPNAQQLIIDNQNQLLKVANLLEPSYELPALLIKPIQRICKYPLLLNQLLKGTPSGYQYEEELKQGMACVVRVANQVNETRRIHENRNAIIELEQRVIDWKGYSLQYFGQLLVWDVVNVCKADIEREYHVYLFEKILLCCKEMSTLKRQARSISMNKKTKRLDSLQLKGRILTSNITTVVPNHHMGSYAIQIFWRGDPQHESFILKLRNEESHKLWMSVLNRLLWKNEHGSPKDIRSAASTPANPVYNRSSSQTSKGYNSSDYDLLRTHSLDENVNSPTSISSPSSKSSPFTKTTSKDTKSATTTDERPSDFIRLNSEESVGTSSLRTSQTTSTIVSNDSSSTASIPSQISRISQVNSLLNDYNYNRQSHITRVYSGTDDGSSVSIFEDTSSSTKQKIFDQPTTNDCDVMRPRQYSYSAGMKSDGSLLPSTKHTSLSSSSTSTSLSVRNTTNVKIRLRLHEVSLVLVVAHDITFDELLAKVEHKIKLCGILKQAVPFRVRLKYVDEDGDFITITSDEDVLMAFETCTFELMDPVHNKGMDTVSLHVVVYF P40996 SCD2_SCHPO SPAC22H10.07; CHAIN 1..536; /note="Protein scd2/ral3"; /id="PRO_0000097620" MLKIKRTWKTHSRILDKDPFSIEPPRKVIRALYDYTARKATEVSFAKGDFFHVIGRENDKAWYEVCNPAAGTRGFVPVSHFEEIGKTVKSERDSDGSGQISFTDLTTNSSTTRSSISELHSGSQPLFGIVQFDFAAERPDELEAKAGEAIIIIARSNHEWLVAKPIGRLGGPGLIPLSFIQLRDLKTGAVIKDVSEAVLRISCIPRVEDWKRAAADYKKSSIPLGKFSDGETQTMPSLSPSTENLQINNDVTYQAATDNSSTFPGSVANELTPLQTLESRTASIASKNKKDMSSEPTVVAAMVENYMIRDDQYWYLVRAVMSDGKHRNLCRYYEDFFNFQTKFLELFPNEAGRGDERRVIPYMPGPVDDVNELISSQRAMDLDVYLKEMCRLPARLLENELVKLFFLPLDGDVESPHPTSTMPEALPREPLSFSLPEKAPEKATNISIPESAPTTAGSTCKVKVRLGDETFALRVPSDISFEDFCERLTNKLGECEHLSYRDTNANKVLPLNNVDDLRKACSQESGVLLFAERRRF P40999 PMT1M_SCHPO ACT_SITE 81; /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" CATALYTIC ACTIVITY: Reaction=cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42956, Rhea:RHEA-COMP:10299, Rhea:RHEA-COMP:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.204; SPBC19C2.02; STRAND 7..13; /evidence="ECO:0007829|PDB:6FDF"; STRAND 30..38; /evidence="ECO:0007829|PDB:6FDF"; STRAND 54..56; /evidence="ECO:0007829|PDB:6FDF"; STRAND 73..77; /evidence="ECO:0007829|PDB:6FDF"; STRAND 83..85; /evidence="ECO:0007829|PDB:6FDF"; STRAND 111..113; /evidence="ECO:0007829|PDB:6FDF"; STRAND 116..123; /evidence="ECO:0007829|PDB:6FDF"; STRAND 144..151; /evidence="ECO:0007829|PDB:6FDF"; STRAND 164..171; /evidence="ECO:0007829|PDB:6FDF"; STRAND 192..195; /evidence="ECO:0007829|PDB:6FDF"; STRAND 252..254; /evidence="ECO:0007829|PDB:6FDF" HELIX 18..25; /evidence="ECO:0007829|PDB:6FDF"; HELIX 40..50; /evidence="ECO:0007829|PDB:6FDF"; HELIX 59..61; /evidence="ECO:0007829|PDB:6FDF"; HELIX 64..70; /evidence="ECO:0007829|PDB:6FDF"; HELIX 99..107; /evidence="ECO:0007829|PDB:6FDF"; HELIX 108..110; /evidence="ECO:0007829|PDB:6FDF"; HELIX 126..128; /evidence="ECO:0007829|PDB:6FDF"; HELIX 130..141; /evidence="ECO:0007829|PDB:6FDF"; HELIX 153..155; /evidence="ECO:0007829|PDB:6FDF"; HELIX 179..185; /evidence="ECO:0007829|PDB:6FDF"; HELIX 198..200; /evidence="ECO:0007829|PDB:6FDF"; HELIX 209..211; /evidence="ECO:0007829|PDB:6FDF"; HELIX 215..221; /evidence="ECO:0007829|PDB:6FDF"; HELIX 222..224; /evidence="ECO:0007829|PDB:6FDF"; HELIX 261..268; /evidence="ECO:0007829|PDB:6FDF"; HELIX 269..272; /evidence="ECO:0007829|PDB:6FDF"; HELIX 279..285; /evidence="ECO:0007829|PDB:6FDF"; HELIX 301..309; /evidence="ECO:0007829|PDB:6FDF"; HELIX 314..324; /evidence="ECO:0007829|PDB:6FDF"; HELIX 326..328; /evidence="ECO:0007829|PDB:6FDF" TURN 15..17; /evidence="ECO:0007829|PDB:6FDF"; TURN 240..244; /evidence="ECO:0007829|PDB:6FDF" CHAIN 1..330; /note="tRNA (cytosine(38)-C(5))-methyltransferase"; /id="PRO_0000088042" MLSTKRLRVLELYSGIGGMHYALNLANIPADIVCAIDINPQANEIYNLNHGKLAKHMDISTLTAKDFDAFDCKLWTMSPSCQPFTRIGNRKDILDPRSQAFLNILNVLPHVNNLPEYILIENVQGFEESKAAEECRKVLRNCGYNLIEGILSPNQFNIPNSRSRWYGLARLNFKGEWSIDDVFQFSEVAQKEGEVKRIRDYLEIERDWSSYMVLESVLNKWGHQFDIVKPDSSSCCCFTRGYTHLVQGAGSILQMSDHENTHEQFERNRMALQLRYFTAREVARLMGFPESLEWSKSNVTEKCMYRLLGNSINVKVVSYLISLLLEPLNF P41003 SMC2_SCHPO BINDING 32..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBP4H10.06c; CHAIN 1..1172; /note="Structural maintenance of chromosomes protein 2"; /id="PRO_0000119012" MKIEELIIDGFKSYAVRTVISNWDDQFNAITGLNGSGKSNILDAICFVLGITNMSTVRAQNLQDLIYKRGQAGITRASVTIVFNNRDPASSPIGFENHPQVSVTRQIIMGGTSKYLINGHRALQQNVQNLFQSVQLNINNPNFLIMQGRITKVLNMKATEILSMIEEASGTRMFEERKEKAFRTMQRKEAKVEEINTLLREEIEPRLTKLRTEKKTFLEYQHIYNDLERLSHLCTAYDYYKLSLKVEELTVQASQKHSHIAEMESSLQTSKQEVLILKEKIKKIEDERMRQMSVSSDRTLDSQLQTVNENITRISTSIELKNTALEEEHGDLQQIRGKAKELETLLRGKRKRLDEVLSVYEKRKDEHQSISKDFKSQEELISSLTTGLSTTEGHETGYSRKLHEARDTLNDFKAEKETNRLKLEGLNKQISLTKPKKAEATKRCDQLNREIDILQNHVEKLKMSLKNTNSDITGEDVLQQKLKQLAKDRGNLLNELDALKSKLAYMEFTYTDPTPNFDRSKVKGLVAQLLTLNEENYDKQTALEITAGGRLYNLIVETEKIGAQLLQKGNLKRRVTIIPLNKITSFVASAERVGAAKKISNNKAQLALELIGYDDELLPAMQYVFGSTLVCDTPESAKKVTFHPSVKLKSVTLDGDVYDPSGTLTGGSVNKSAGPLLQIQKLNSLQLKLQVVTSEYEKLETQLKDLKTQNANFHRLEQEIQLKQHELTLLIEQRETDSSFRLLSDYQQYKDDVKDLKQRLPELDRLILQSDQAIKKIERDMQEWKHNKGSKMAELEKEFNQYKHKLDEFTPILEKSENDYNGVKLECEQLEGELQNHQQSLVQGESTTSLIKTEIAELELSLVNEEHNRKKLTELIEIESAKFSGLNKEIDSLSTSMKTFESEINNGELTIQKLNHEFDRLEREKSVAITAINHLEKENDWIDGQKQHFGKQGTIFDFHSQNMRQCREQLHNLKPRFASMRKAINPKVMDMIDGVEKKEAKLRSMIKTIHRDKKKIQDTVKSIDRFKRSALEKTWREVNSSFGEIFDELLPGNSAELQPPENKEFTDGLEIHVKIGSIWKDSLAELSGGQRSLVALALIMSLLKYKPAPMYILDEIDAALDLSHTQNIGRLIKTKFKGSQFIIVSLKEGMFTNANRLFHVRFMDGSSVVQAR P41004 SMC4_SCHPO BINDING 155..162; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" PTM: Phosphorylated by CDC2 on Thr-19 at metaphase. {ECO:0000269|PubMed:10485849}. MOD_RES 19; /note="Phosphothreonine; by CDC2"; /evidence="ECO:0000269|PubMed:10485849" SPBC146.03c; CHAIN 1..1324; /note="Structural maintenance of chromosomes protein 4"; /id="PRO_0000119017" MSDKGIFRTSSTPSIVDVTPDRGERPRKLVRSVLESPSQKDVASIVKIEQTPSRPFFNDFLKKRITDSLNERPNLLNKFMSAQDGTPSKSTGFNERSSQLVSEFTTTEDIENCEETTQVLPPRLVVYELRLTNFKSYAGTQIVGPFHPSFSSIVGPNGSGKSNVIDALLFVFGFRASKLRQSKASALIHKSATHPSLDSCDVEITFKEVNSDFTYVDGSELTVRRTAYKNNTSKYFVNGVESSFSAVSNLLKEKGIDLNHKRFLILQGEVESIAQMKPRAISEGDDGLLEYLEDIIGTSKYKPIIEENMQELSNSDDICAEKESRLKLVLSEKAKLEDSKNSVLSFLKDENELFMKQNQLYRTILYETRNKKTLVQNLLNSLEGKLQAHLEKFEQTERDISEKNEEVKSLREKAAKVKNDCTSEKKTRQSYEQQTVKIEEQLKFLLNKEKKLKKSIEALSFEKSEAENSLSSHDIDSQKLNSEIADLSLRLQQEELSLDDIRKSLQGKTEGISNAIEEKQKAMAPALEKINQLTSEKQILQVELDMLLNKENDLINDVESSQSSLDKLRNDAEENRNILSSKLKVLSDLKGEKKDVSKNIERKKETVHNTYRNLMSNRTKLEEMKASLSSSRSRGNVLESLQRLHESDNLNGFFGRLGDLATIDEAYDVAISTACPALNHIVVDNIETGQKCVAFLRSNNLGRASFIILKELAQKNLARIQTPENVPRLFDLLRFNDQKFAPAFYNVLQNTLVAKNLEQANRIAYGKTRWRVVTLSGQLIDKSGTMTGGGTRVKKGGMSSAITSDVSPASVETCDKQVQLEDTRYRQHLSELESLNQRFTEISERIPSAELEISKLQLDVSACDRLVAGEERRILQLKSDLKSIRNNNERKRNLQNKISNMDKEVEAININNEGLVTEIKTLQDKIMEIGGIRYRIQKSKVDDLHEQLKFVKDKLNKMSFKKKKNEQRSQSFQVELSNLTSEYDTTTESIATLKTELQSLNKYVDEHKSRLREFENALWDINSSIDELVKFIEFESKQMNSVKAERIELENQIQEQRTALSEVGNNENKYLKLMSNLKLHNLTEFCDQTTMDSTFPEYSEDELSSVDKSELVSNISVLKKKTEDREVDINVLSEYRRCNKEAEKRDSDYQSELQKRTDLKKVVTDLQSQRLDEFMYGFGIISMKLKEMYQIITMGGNAELELVDSLDPFSEGVLFSVMPPKKSWKNISNLSGGEKTLSSLALVFALHNYKPTPLYVMDEIDAALDFKNVSIVANYIKERTKNAQFIVISLRSNMFELSSRLVGIYKTANMTKSVTINNKEILTD P41389 MCM5_SCHPO BINDING 372..379; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; MOD_RES 350; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 352; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B2.05; CHAIN 1..720; /note="DNA replication licensing factor mcm5"; /id="PRO_0000194112" MAAATGWERSAVYYTPVLPGEQELDSNVSHEKNFIQFIEEFVIDNDFIYRTQLRDNLVVKQYMLNIDLRHLISYNEDLAHLLLSQPTDILPLFESAVTTVAKRLLYRSQENASTNIPTCQVTLRYDANILPIRNLTASHISKLVRVPGIIIGASTLSCRATALHLVCRNCRATRILQISGGFSGVQLPRVCEAPVLDGEKKDCPMDPFIIDHSKSTFIDQQVLKLQEAPDMVPVGELPRHILLNADRYLTNQITPGTRCVITGIFSIFQNKSVKASGAVAIRNPYIRVVGIQMDSNDGSKSTPLFSEEEEEEFLEISRTPNLYDIISNSISPAIYGNVDIKKAIACLLFSGSKKILPDGMRLRGDINVLLLGDPGTAKSQFLKFVERLAPIAVYTSGKGSSAAGLTASIQRDSVTREFYLEGGAMVLADGGIVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTILNSRTSVLAAANPIFGRYDDMKTPGENIDFQSTILSRFDMIFIVKDEHDETKDRNIARHVINLHTNLQESSETLAIGEIPFDKFRRYINYCRHKCAPNLDAEAAEKLSSQFVAIRKRVHQSEQDSNSRSTIPITVRQLEAIIRITESLAKMSLSPIASEAHATEAIRLFLTSTLAAATQSSPEVTEEVKKIEASLRKRLPIGFQASYRMLIREYVNGHGYSQHALEMALQILSSKETIQLRNGGQTVYRSGV P41391 RNA1_SCHPO SPAC22E12.07; STRAND 3..5; /evidence="ECO:0007829|PDB:2CA6"; STRAND 12..15; /evidence="ECO:0007829|PDB:2CA6"; STRAND 36..38; /evidence="ECO:0007829|PDB:2CA6"; STRAND 42..44; /evidence="ECO:0007829|PDB:2CA6"; STRAND 64..66; /evidence="ECO:0007829|PDB:2CA6"; STRAND 98..100; /evidence="ECO:0007829|PDB:2CA6"; STRAND 126..128; /evidence="ECO:0007829|PDB:2CA6"; STRAND 163..165; /evidence="ECO:0007829|PDB:2CA6"; STRAND 191..193; /evidence="ECO:0007829|PDB:2CA6"; STRAND 220..222; /evidence="ECO:0007829|PDB:2CA6"; STRAND 248..250; /evidence="ECO:0007829|PDB:2CA6"; STRAND 278..280; /evidence="ECO:0007829|PDB:2CA6"; STRAND 307..309; /evidence="ECO:0007829|PDB:2CA6"; STRAND 313..315; /evidence="ECO:0007829|PDB:2CA6" HELIX 19..22; /evidence="ECO:0007829|PDB:2CA6"; HELIX 23..25; /evidence="ECO:0007829|PDB:1K5D"; HELIX 26..30; /evidence="ECO:0007829|PDB:2CA6"; HELIX 46..54; /evidence="ECO:0007829|PDB:2CA6"; HELIX 76..78; /evidence="ECO:0007829|PDB:2CA6"; HELIX 80..90; /evidence="ECO:0007829|PDB:2CA6"; HELIX 111..120; /evidence="ECO:0007829|PDB:2CA6"; HELIX 135..156; /evidence="ECO:0007829|PDB:2CA6"; HELIX 173..175; /evidence="ECO:0007829|PDB:2CA6"; HELIX 176..185; /evidence="ECO:0007829|PDB:2CA6"; HELIX 201..209; /evidence="ECO:0007829|PDB:2CA6"; HELIX 212..214; /evidence="ECO:0007829|PDB:2CA6"; HELIX 229..239; /evidence="ECO:0007829|PDB:2CA6"; HELIX 240..242; /evidence="ECO:0007829|PDB:2CA6"; HELIX 258..269; /evidence="ECO:0007829|PDB:2CA6"; HELIX 288..301; /evidence="ECO:0007829|PDB:2CA6"; HELIX 320..332; /evidence="ECO:0007829|PDB:2CA6" TURN 55..58; /evidence="ECO:0007829|PDB:2CA6"; TURN 108..110; /evidence="ECO:0007829|PDB:2CA6" CHAIN 1..386; /note="Ran GTPase-activating protein 1"; /id="PRO_0000056741" MSRFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKKDLEIAEFSDIFTGRVKDEIPEALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSKHTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPPLRSIICGRNRLENGSMKEWAKTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIALKSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDEKMPDLLFLELNGNRFSEEDDVVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAESQSPEPETSEEEKEDKELADELSKAHI P41410 RAD54_SCHPO BINDING 294..301; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P32863}; SPAC15A10.03c; CHAIN 1..852; /note="DNA repair protein rhp54"; /id="PRO_0000074343" MIQQPTTAKPRISTSSKLNTVLSKNKENVPGKLFKKFKCPSLVISEKRKELPLRKKPRVNYSEYGSVDGKYDSAYVSENVSGLATIKEANRLILNHERRDPSTVIKKQFSVPKPIKGHEDISKLCAHRPPPTLGMKRKVDFIPRPLYDPADEFAIVLYDPTTDADEIIPDIKEVLAEKRKKDELLKNRKGKKEISDSEPESDHDSCVSTDTVASCSTEQSLITSNTSKHRRPNKSLKDLLGIQKEKPPPPPVAVVIDPKLARILRPHQIEGVKFLYKCVTGRIDRCANGCIMADEMGLGKTLQCIALLWTLLKQSPQAGKPTIEKAIITCPSSLVKNWANELVKWLGKDAITPFILDGKSSKQELIMALQQWASVHGRQVTRPVLIASYETLRSYVEHLNNAEIGMLLCDEGHRLKNSDSLTFTALDKLNVQRRVILSGTPIQNDLSEYFSLLNFANPGLLGSRQEFRKNYEIPILKGRDADGTEKDKENGDAKLAELAKIVNRFIIRRTNDILSKYLPVKYEHVVFCNLSEFQLSLYKHFITSPEINKILRGTGSQPLKAIGLLKKICNHPDLLNLTEDLEGCEALFPPGFIPRELRGRDRNIDSSLSGKMLVLERMLYQIKQETDDKIVLISNYTSTLDLFEQLCRARGYKALRLDGTMNVNKRQRLVDTFNDPEKDAFVFLLSSKAGGCGINLIGANRLILFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATGTIEEKIFQRQSHKQSLSSCVVDEAQDVERHFSLDNLRQLFQLNDHTVCETHETYKCKRCRDGKQFIRAPAMLYGDTSTWNHFTNPTLDRIEDHLLKREAGKQQVSTVFQYKSH P41411 CDC18_SCHPO BINDING 199..206; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" PTM: Ubiquitinated by pop1 and pop2 and targeted to the 26S proteasome for degradation. SPBC14C8.07c; CHAIN 1..577; /note="Cell division control protein 18"; /id="PRO_0000150978" MCETPIGCHTPRRCNRFIDSAALIDCTNKTNQREHSPSFSIEIPTTPSRKRTLASSHFQTPTKRIKYELGELQEEKTDLYPNFPAQLKENKKPKLPTTPQTPKTPKRTIQIVTPKSLNRTCNPVPFATRLLQSTPHRQLFPPTPSTPSTPSYNSTAKLSLRKSYRSAGVVGRENEKSIVESFFRQHLDANAGGALYVSGAPGTGKTVLLHNVLDHVVSDYPKVNVCYINCMTINEPKAIFEKIHSKIVKEEILENEDHHINFQCELESHFTQSANELYNPVIIVLDEMDHLIAREQQVLYTLFEWPSRPTSRLILVGIANALDMTDRFLPRLRTKHITPKLLSFTPYTAQEISTIIKARLKTAATTSEKNNPFTPIKSISEVSDDSINVVSQHADETPFIHPAAIELCARKVAASSGDLRKALDICRHAIELAEREWKAQHDNTLSSVDIPRASIAHVVRATSAMSQSASARLKNLGLQQKAILCTLVVCEKTSLSVADVFEKYSSLCLRDRLIYPLTSSEFCDVANSLETLAIIRLRTKQRNGKPQDRIISLLVPEMDVITAVGDIGTLKRFFDRR P41412 RES2_SCHPO SPAC22F3.09c; CHAIN 1..657; /note="Cell division cycle-related protein res2/pct1"; /id="PRO_0000067073" MAPRSSAVHVAVYSGVEVYECFIKGVSVMRRRRDSWLNATQILKVADFDKPQRTRVLERQVQIGAHEKVQGGYGKYQGTWVPFQRGVDLATKYKVDGIMSPILSLDIDEGKAIAPKKKQTKQKKPSVRGRRGRKPSSLSSSTLHSVNEKQPNSSISPTIESSMNKVNLPGAEEQVSATPLPASPNALLSPNDNTIKPVEELGMLEAPLDKYEESLLDFFLHPEEGRIPSFLYSPPPDFQVNSVIDDDGHTSLHWACSMGHIEMIKLLLRANADIGVCNRLSQTPLMRSVIFTNNYDCQTFGQVLELLQSTIYAVDTNGQSIFHHIVQSTSTPSKVAAAKYYLDCILEKLISIQPFENVVRLVNLQDSNGDTSLLIAARNGAMDCVNSLLSYNANPSIPNRQRRTASEYLLEADKKPHSLLQSNSNASHSAFSFSGISPAIISPSCSSHAFVKAIPSISSKFSQLAEEYESQLREKEEDLIRANRLKQDTLNEISRTYQELTFLQKNNPTYSQSMENLIREAQETYQQLSKRLLIWLEARQIFDLERSLKPHTSLSISFPSDFLKKEDGLSLNNDFKKPACNNVTNSDEYEQLINKLTSLQASRKKDTLYIRKLYEELGIDDTVNSYRRLIAMSCGINPEDLSLEILDAVEEALTREK P41878 RPN11_SCHPO BINDING 112; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 114; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 125; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182" SPAC31G5.13; CHAIN 1..308; /note="26S proteasome regulatory subunit rpn11"; /id="PRO_0000213959" MESLQRLLQGARMGTGMMGDQPLVDNSECVYISSLALLKMLRHGRHGTPMEVMGLMLGEFVDDFTVRVVDVFAMPQSGTGVSVEAVDPVFQKNMMDMLKQTGRPEMVVGWYHSHPGFGCWLSSVDINTQQSFEQLTPRAVAVVVDPIQSVKGKVVIDAFRLINPSTLMMGQEPRQTTSNLGHINKPSIQALIHGLGRHYYSLRINYKKTELEEIMLLNLHKQPWAHGLLLENFNSAAEKNHASIDKMKSLSEQYTERVQNEVTLSPEQLRIQYVGKQDPKKHLDAEVQKCIDNNISSMLACMLDSVAF P41887 HSP90_SCHPO BINDING 38; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 80; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 99; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 125; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 375; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" MOD_RES 245; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 277; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC926.04c; CHAIN 1..704; /note="Heat shock protein 90 homolog"; /id="PRO_0000062963" MSNTETFKFEAEISQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQSLSDPHALDAEKDLFIRITPDKENKILSIRDTGIGMTKNDLINNLGVIAKSGTKQFMEAAASGADISMIGQFGVGFYSAYLVADKVQVVSKHNDDEQYIWESSAGGSFTVTLDTDGPRLLRGTEIRLFMKEDQLQYLEEKTIKDTVKKHSEFISYPIQLVVTREVEKEVPEEEETEEVKNEEDDKAPKIEEVDDESEKKEKKTKKVKETTTETEELNKTKPIWTRNPSEVTKEEYASFYKSLTNDWEDHLAVKHFSVEGQLEFRAILFVPRRAPMDLFEAKRKKNNIKLYVRRVFITDDCEELIPEWLGFIKGVVDSEDLPLNLSREMLQQNKIMKVIRKNLVRRCLDMFNEIAEDKENFKTFYDAFSKNLKLGIHEDAANRPALAKLLRYNSLNSPDDLISLEDYITKMPEHQKNIYFITGESKQAVENSPFLEIFRAKKFDVLFMVDPIDEYAVTQLKEFEGKKLVNITKDGLELEETDEEKAAREKLEKEYEEFAKQLKTILGDKVEKVVVSNKIVGSPCLLTTGQYGWSANMERIMKAQALRDTSMSAYMSSRKTFEINPKSPIIAELKKKVEENGAEDRSVKDLATILYETALLSSGFTLDDPSAYAQRINRLISLGLSIDEEEEAPIEEISTESVAAENNAESKMEEVD P41889 CUT9_SCHPO PTM: Phosphorylated. {ECO:0000269|PubMed:9264466}. SPAC6F12.15c; HELIX 50..53; /evidence="ECO:0007829|PDB:2XPI"; HELIX 55..59; /evidence="ECO:0007829|PDB:2XPI"; HELIX 83..96; /evidence="ECO:0007829|PDB:2XPI"; HELIX 100..114; /evidence="ECO:0007829|PDB:2XPI"; HELIX 117..129; /evidence="ECO:0007829|PDB:2XPI"; HELIX 133..142; /evidence="ECO:0007829|PDB:2XPI"; HELIX 145..147; /evidence="ECO:0007829|PDB:2XPI"; HELIX 150..162; /evidence="ECO:0007829|PDB:2XPI"; HELIX 166..173; /evidence="ECO:0007829|PDB:2XPI"; HELIX 198..212; /evidence="ECO:0007829|PDB:2XPI"; HELIX 216..229; /evidence="ECO:0007829|PDB:2XPI"; HELIX 234..242; /evidence="ECO:0007829|PDB:2XPI"; HELIX 248..257; /evidence="ECO:0007829|PDB:2XPI"; HELIX 261..264; /evidence="ECO:0007829|PDB:2XPI"; HELIX 265..267; /evidence="ECO:0007829|PDB:2XPI"; HELIX 268..276; /evidence="ECO:0007829|PDB:2XPI"; HELIX 285..296; /evidence="ECO:0007829|PDB:2XPI"; HELIX 301..303; /evidence="ECO:0007829|PDB:2XPI"; HELIX 305..317; /evidence="ECO:0007829|PDB:2XPI"; HELIX 321..334; /evidence="ECO:0007829|PDB:2XPI"; HELIX 342..352; /evidence="ECO:0007829|PDB:2XPI"; HELIX 355..368; /evidence="ECO:0007829|PDB:2XPI"; HELIX 373..385; /evidence="ECO:0007829|PDB:2XPI"; HELIX 389..402; /evidence="ECO:0007829|PDB:2XPI"; HELIX 407..420; /evidence="ECO:0007829|PDB:2XPI"; HELIX 423..435; /evidence="ECO:0007829|PDB:2XPI"; HELIX 442..454; /evidence="ECO:0007829|PDB:2XPI"; HELIX 457..470; /evidence="ECO:0007829|PDB:2XPI"; HELIX 475..487; /evidence="ECO:0007829|PDB:2XPI"; HELIX 491..507; /evidence="ECO:0007829|PDB:2XPI"; HELIX 513..515; /evidence="ECO:0007829|PDB:2XPI"; HELIX 516..528; /evidence="ECO:0007829|PDB:2XPI"; HELIX 532..545; /evidence="ECO:0007829|PDB:2XPI"; HELIX 550..562; /evidence="ECO:0007829|PDB:2XPI"; HELIX 566..579; /evidence="ECO:0007829|PDB:2XPI"; HELIX 584..592; /evidence="ECO:0007829|PDB:2XPI" TURN 281..284; /evidence="ECO:0007829|PDB:2XPI"; TURN 436..439; /evidence="ECO:0007829|PDB:2XPI" CHAIN 1..671; /note="Anaphase-promoting complex subunit cut9"; /id="PRO_0000106281" MVVKRTQTDSRMQSTPGNHNHPDAHANAAYMTPPSMGALNANNSNSQLSTLTISPMTYLANNTSTDGSFLKERNAQNTDSLSREDYLRLWRHDALMQQQYKCAAFVGEKVLDITGNPNDAFWLAQVYCCTGDYARAKCLLTKEDLYNRSSACRYLAAFCLVKLYDWQGALNLLGETNPFRKDEKNANKLLMQDGGIKLEASMCYLRGQVYTNLSNFDRAKECYKEALMVDAKCYEAFDQLVSNHLLTADEEWDLVLKLNYSTYSKEDAAFLRSLYMLKLNKTSHEDELRRAEDYLSSINGLEKSSDLLLCKADTLFVRSRFIDVLAITTKILEIDPYNLDVYPLHLASLHESGEKNKLYLISNDLVDRHPEKAVTWLAVGIYYLCVNKISEARRYFSKSSTMDPQFGPAWIGFAHSFAIEGEHDQAISAYTTAARLFQGTHLPYLFLGMQHMQLGNILLANEYLQSSYALFQYDPLLLNELGVVAFNKSDMQTAINHFQNALLLVKKTQSNEKPWAATWANLGHAYRKLKMYDAAIDALNQGLLLSTNDANVHTAIALVYLHKKIPGLAITHLHESLAISPNEIMASDLLKRALEENSLTSGFLNSKYVFEDEVSEYMQQSNLNTSDKSMSMEDQSGKVTESVNDRTQVLYADSRSEMMMDDIEGNVSEQR P41892 CDC7_SCHPO ACT_SITE 131; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 15..23; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 38; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; SPBC21.06c; CHAIN 1..1062; /note="Cell division control protein 7"; /id="PRO_0000085765" MHNIQASSITLGDCLGKGAFGAVYRGLNIKNGETVAVKKVKLSKMLKSDLSVIKMEIDLLKNLDHPNIVKYRGSYQTNDSLCIILEYCENGSLRSICKNFGKIPENLVALYTFQVLQGLLYLHNQGVIHRDIKGANILTTKDGTIKLADFGVATKINALEDHSVVGSPYWMAPEVIELVGATTASDIWSVGCTVIELLDGNPPYYDLDPTSALFRMVKDEHPPLPSNISSAAKSFLMQCFQKDPNLRIKTRKLLKHPWVIMNQTSSKFSDAIDEVQKYNERVKESTLTAIIEPTSNRINPTLHSGRQSSYHMPESPKTPIAESPDHDNWDNEFQGTLKISDDVLKKSEHFMDFCSNFKGKNNSSSITSSPSKSRHAFNSDQISESNNFNASPLSTPLKAQFDPSKPALNRSIDHQKTPQHKRYLSTEFKENIPDGIEKFVETPRDSEFTDIFPTSSIKVQGLRKETGLGTLVLNKCYGSWNNEENEDGEESDIFDSIETNLENLDIENNIALDKRTHLASLLSSLLGSLRDKNIGSKDTTVSQIASILSEDLSLKREIIQAHGILPLLETLREIKTPDVQLLLLKLINTVAFDDHTTLQKVCFAGGLPLMLSFSNREHSFEFRYESAIFIQQMYRTSALTLQMFLSSNGLNSLLLFIKEDYGTNRDFVFVGVEGIWKLLRQQDYIPKNDICTMVVNDSLEPLTKAMLKALATDDDSSRMSLTRICEILLALSQADNYVKESLLCESALRRILRILLYLPHSDMAITLQFFKQLSMVPSSLSLLRKVHIIPLLTHILGDSKIEKGRKEIRSEALAALFNVCKLDKKSQEEAVISGAIPLLQEVIIKDRLFKEFALPILLALPQAGPVSRIYLWQNKCLDFFLSLLSDLNWQSAVFDTIASWLQFELREVQRVLAEKRNVQLVLKVFCISQSASSNRMLDTLGRVCQISPRLAASYGQPIIFQKFKEKLTHKGTKPIVVLNIFQIMKSMCEASSQSVAYIAHCGLPDVVANLNQTSDSVLVKELAKDLLKYLKVPQGPINEHKSPISKPHMPPPRWQPKQPLTQ P42656 RAD24_SCHPO MOD_RES 34; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 66; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC8E11.02c; CHAIN 1..270; /note="Checkpoint signal transducer rad24"; /id="PRO_0000058717" MSTTSREDAVYLAKLAEQAERYEGMVENMKSVASTDQELTVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKGNTAQVELIKEYRQKIEQELDTICQDILTVLEKHLIPNAASAESKVFYYKMKGDYYRYLAEFAVGEKRQHSADQSLEGYKAASEIATAELAPTHPIRLGLALNFSVFYYEILNSPDRACYLAKQAFDEAISELDSLSEESYKDSTLIMQLLRDNLTLWTSDAEYSAAAAGGNTEGAQENAPSNAPEGEAEPKADA P42881 GPT_SCHPO BINDING 59..61; /ligand="UDP-N-acetyl-alpha-D-glucosamine"; /ligand_id="ChEBI:CHEBI:57705"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 71; /ligand="UDP-N-acetyl-alpha-D-glucosamine"; /ligand_id="ChEBI:CHEBI:57705"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 154; /ligand="dolichyl phosphate"; /ligand_id="ChEBI:CHEBI:57683"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 208..216; /ligand="dolichyl phosphate"; /ligand_id="ChEBI:CHEBI:57683"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 215; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 221; /ligand="UDP-N-acetyl-alpha-D-glucosamine"; /ligand_id="ChEBI:CHEBI:57705"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 286; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9H3H5"; BINDING 335..337; /ligand="UDP-N-acetyl-alpha-D-glucosamine"; /ligand_id="ChEBI:CHEBI:57705"; /evidence="ECO:0000250|UniProtKB:Q9H3H5" CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-alpha-D-glucosaminyl-diphospho-di-trans,poly-cis-dolichol + UMP; Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19507, ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:58427; EC=2.7.8.15; Evidence={ECO:0000269|PubMed:7893167}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13290; Evidence={ECO:0000305|PubMed:7893167}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H3H5}; SPBC15D4.04; CHAIN 1..446; /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase"; /id="PRO_0000108764" CARBOHYD 395; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIESCFNVGIWATGLALLMNQGQSPLLSNVGLSVLAYKATAMFIPRVGPSFIKRGFSGKDMNKVEKYVIPETMGAVSALVYFMCMIIFIPVLFYKYLVPNHNPNLPSDGSVAEVAKSQFPHDLLGAYLSALLSILSVSLLGILDDLFDIRWRHKFFLPAIAAIPLLVVYYVDYGVTYVSVPSIVRPFLKRSLINLGFLYYFYMAAVAIFCPNSINIIAGVNGVEAGQSLVLALVIACNDLFYVLSPKNKDALRAHLLSLYLVLPLIGVTAGLLKYNWWPSRVFVGDTFCYFAGMVMAVVGILGHFSKTLMLFFIPQIFNFALSVPQLFGLVECPRHRLPKLNVKTGLLENSYTEFSLNEHPLPKKTLLTISIFEKLRLIRVEYDPSTGRPLRCTNFTIINFVLYHLGPMREDHLTICIMGLQLLTGIFGLIIRHFVAPLVYPEDNI P46595 UBC4_SCHPO ACT_SITE 85; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPBC119.02; STRAND 20..26; /evidence="ECO:0007829|PDB:4II2"; STRAND 29..38; /evidence="ECO:0007829|PDB:4II2"; STRAND 49..55; /evidence="ECO:0007829|PDB:4II2"; STRAND 66..69; /evidence="ECO:0007829|PDB:4II2" HELIX 2..14; /evidence="ECO:0007829|PDB:4II2"; HELIX 87..89; /evidence="ECO:0007829|PDB:4II2"; HELIX 99..111; /evidence="ECO:0007829|PDB:4II2"; HELIX 121..129; /evidence="ECO:0007829|PDB:4II2"; HELIX 131..145; /evidence="ECO:0007829|PDB:4II2" TURN 44..47; /evidence="ECO:0007829|PDB:4II2"; TURN 58..62; /evidence="ECO:0007829|PDB:4II2"; TURN 90..92; /evidence="ECO:0007829|PDB:4II2" CHAIN 1..147; /note="Ubiquitin-conjugating enzyme E2 4"; /id="PRO_0000082569" MALKRINRELADLGKDPPSSCSAGPVGDDLFHWQATIMGPADSPYAGGVFFLSIHFPTDYPFKPPKVNFTTRIYHPNINSNGSICLDILRDQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHVYKTDRSRYELSAREWTRKYAI P47979 ZFS1_SCHPO SPBC1718.07c; CHAIN 1..404; /note="Zinc finger protein zfs1"; /id="PRO_0000089175" MVYSPMSRPQVPLAFRQWPPYNYKSDPLVNSKLSQSTTSVNAGPSLISPSFLDSYANSSSLLHKPSTNLGSLKTSSLLASDEVFPSSVMPQLRPLDSSLSVSPEMDGWPWHHNSSSNPQGYAWTPSLLSSNATSYLHSGSSPHGNTSNHPSPISSLESLPSRSSTGSGSLDFSGLANLHDDSKSLAMSLNMAGVPVSVDENSQTSFPFVHGQPESTMSRKPKLCVQSKSMTNIRNSVAKPSLVRQSHSAGVIPIKPTASNASIRNAPSNLSKQFSPSGNSPLTEASKPFVPQPSAAGDFRQAKGSASHPHGSGSSNGVAPNGKRALYKTEPCKNWQISGTCRYGSKCQFAHGNQELKEPPRHPKYKSERCRSFMMYGYCPYGLRCCFLHDESNAQKSATIKQSP P48003 H2AZ_SCHPO PTM: Acetylated at the N-terminus. N-terminal acetylation is essential for function. {ECO:0000269|PubMed:19915592}. SPBC11B10.10c; CHAIN 1..139; /note="Histone H2A.Z"; /id="PRO_0000055337" MSGGGKGKHVGGKGGSKIGERGQMSHSARAGLQFPVGRVRRFLKAKTQNNMRVGAKSAVYSAAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDTLIRATIAGGGVLPHINKQLLIRTKEKYPEEEEII P48008 SPN3_SCHPO BINDING 59..66; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 201..209; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 274; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 342; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16A3.01; CHAIN 1..412; /note="Septin homolog spn3"; /id="PRO_0000173505" MWYTYNEDFGVVQLLFLHSNDTLTARTHITKGQIDIELTMRTTKKSSKKGIPLNLMVVGDVGLGRTAFINTLCEKPLIRHNNNFDPAEASSVSPVEIVPYQTDIILEDGTKINLTVLDTPHFGEAIDNENNFDIILQYIESQYDNVLEEESRIKRNARFCDDRVHALIYFISPTGHGLRELDIELMRRLAPRVNIIPAIAKADSLTAQELQTTKEMINADIEYYKIPVYDFPYDIEEDEEAIINLSQQLRATIPFAIVSSDRLIEMNGQTVRGRAYPWGVVEVDNPRHSDFLALRSALFATHIEDLHNITSNQLYETYRTEKLSTSQLLLDSTVGLDGKNLSQHDQVLREDRLRAIELSVQKEIEEKRRQLLAREEALRALEEKLAASTAAMANASVSTLPSSVSSTNHSQS P48009 SPN4_SCHPO BINDING 35..42; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 70; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 96; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 175..183; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 231; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 247; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC9G1.11c; CHAIN 1..380; /note="Septin homolog spn4"; /id="PRO_0000173506" MNEEETNFVGIADLPNQRHKIVSRNGVAFTLMLCGESGLGKTTFCNTLFSTTIKSHMGPEKVRAKHAEKTVEIEITKAELEEKNFHLRLTVIDTPGFGDFINNSGCWESVVEFIEDQHESYMRQDQQPDRRKIIDMRIHACLYFLRPVRNGVRPMDLEAMKHISKRVNLIPVIAKADMYTRRDLALYKTRISQVLEYHQVNVYKPNMDEGDPVFHRQIQGIINCMPFAIVGSEDDIRTPDGRVVKGREYPWGIVEIENEEHCDFKQLRNILIRSCMLDLIQTTEEKLYEQYRQEQMKVRQYGEPKLRTIDNAKFKEEEENLRKRFTEQVRVEETRFRQWEQRLIAERDSLNKDLEAQHVQIKQIELEIERLKAATSSRKR P48010 SPN5_SCHPO BINDING 125..132; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 151; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 177; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 257..265; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 304; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 319; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC24C9.15c; CHAIN 1..464; /note="Septin homolog spn5"; /id="PRO_0000173507" MDSSNLSSSMPQEGQLKLTEEAIITIKQVDESSAKRSVSNESRKSKDVTRKEQIASDQQGDDQCPQSDTAKDKKTEFKQDEVPNSNGKSIPTFHPCNNIGINDFNHQHYSRVCRNGIDINLIVVGESSLGKTTFVNSFLQSNDTNFRPKKTMDFVEHKATLSDGDQKFNLTIVDTPGFGDKSDNSNCWRPIATNLLHRLNAYFQNEVKMDRETSEIDSRIHGCLFFINPNGHRLQPLEIYIMKKIDQFVNIIPVIGKADTMTSDELNHFKKRVIADMVREKIRYFREPHNEKKAKIPIPFAIVGAGAPIEHDGKCIRGRAYPWGLVDIDDPKQSDFCQLRNFLLYTHIEGLKHKTHKLIYDTFRTEKLVALNATPGSQFISAEEMNQKYISEQTQLVEEALTKVMKEKYREKENNLELLETNLKTHHKDYKHALKKRITALEEEKNRLIKEIGPEKVKKAGILA P48011 RPAB4_SCHPO BINDING 24; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 41; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" SPBC19C2.03; CHAIN 1..63; /note="DNA-directed RNA polymerases I, II, and III subunit RPABC4"; /id="PRO_0000159752" MNHPTSTGGTAFNPPRPATMIYLCADCGARNTIQAKEVIRCRECGHRVMYKMRTKRMVQFEAR P49731 MCM6_SCHPO BINDING 476..483; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; MOD_RES 96; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 98; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC211.04c; CHAIN 1..892; /note="DNA replication licensing factor mcm6"; /id="PRO_0000194118" MSSLASQGNNASTPAYRYGFQTSEVGDRPTVSMPSQPESSAMLEDDGMVKRKPFAAIGEAIPKVIDTTGESVREAFEEFLLSFSDDRVAGGDALPSASQEKYYVQQIHGLAMYEIHTVYVDYKHLTSYNDVLALAIVEQYYRFSPFLLRALQKLIEKFEPEYYRSSLSRENASLSPNFKASDKTFALAFYNLPFRSTIRDLRTDRIGRLTTITGTVTRTSEVRPELAQGTFICEECHTVVSNVEQAFRYTEPTQCPNELCANKRSWRLNISQSSFQDWQKVRIQENSNEIPTGSMPRTLDVILRGDIVERAKAGDKCAFTGILIAVPDVSQLGIPGVKPEAYRDSRNFGGRDADGVTGLKSLGVRDLTYKLSFLACMVQPDDANDKSGADVRGDGSQGIEEQDEFLQSLSQEEIDDLRAMVHSDHIYSRLTNSLAPSVYGHEIIKKGILLQLMGGVHKLTPEGINLRGDLNICIVGDPSTSKSQFLKYVCNFLPRAIYTSGKASSAAGLTAAVVKDEETGDFTIEAGALMLADNGICAIDEFDKMDLSDQVAIHEAMEQQTISIAKAGIQATLNARTSILAAANPIGGRYNRKTTLRNNINMSAPIMSRFDLFFVVLDECNESVDRHLAKHIVDIHRLRDDAMQPEFSTEQLQRYIRYARTFKPKLNTESCAEIVKKYKQLRMDDAQGAGKNSYRITVRQLESMIRLSEAIARANCVDDITPAFVNEAYSLLRQSIIHVERDDIEVEEDDAEAQELENDNTNTTNGNDNVSSEEALQKPKVKITYDKYVSIMNGILQVLRQRSTEGVDGVPAGDLVQSYLELREDQFHTEEDIIYEVGLVRKVLTRLVHESIIMEIQNLTDSAVRLPFEERVFSIHPNCDIDALLSNGDVPN P49777 ABP1_SCHPO MOD_RES 460; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1105.04c; STRAND 5..7; /evidence="ECO:0007829|PDB:1IUF"; STRAND 23..26; /evidence="ECO:0007829|PDB:1IUF"; STRAND 46..49; /evidence="ECO:0007829|PDB:1IUF"; STRAND 66..72; /evidence="ECO:0007829|PDB:1IUF"; STRAND 116..119; /evidence="ECO:0007829|PDB:1IUF" HELIX 12..22; /evidence="ECO:0007829|PDB:1IUF"; HELIX 30..41; /evidence="ECO:0007829|PDB:1IUF"; HELIX 52..60; /evidence="ECO:0007829|PDB:1IUF"; HELIX 80..92; /evidence="ECO:0007829|PDB:1IUF"; HELIX 102..114; /evidence="ECO:0007829|PDB:1IUF"; HELIX 129..137; /evidence="ECO:0007829|PDB:1IUF" TURN 61..63; /evidence="ECO:0007829|PDB:1IUF" CHAIN 1..522; /note="ARS-binding protein 1"; /id="PRO_0000126133" MGKIKRRAITEHEKRALRHYFFQLQNRSGQQDLIEWFREKFGKDISQPSVSQILSSKYSYLDNTVEKPWDVKRNRPPKYPLLEAALFEWQVQQGDDATLSGETIKRAAAILWHKIPEYQDQPVPNFSNGWLEGFRKRHILHAINEQPTESVVLNNTEPPNDPLSRVYDVTRLTNINDIFTMQETGLFWKLVPNGTPEVEDIKGITRFKARITLTVCCNASGTERLPLWVIGYSQSPRVFRAANVKPEVMNFKWRSNGKASMTTAIMEEWLRWFDACMEGRKVILLIDSYTPHLRAVENIRNSGNDLRNTTVITLPSTSASISQPCSEGVIYALKACYRKHWVQYILEQNELGRNPYNTTNVLRAILWLVKAWTTDISPEIIENAFNLSGVLGLFNESAVTSRALDEMIHPLRELVSEFSVQAAMRIEDFISPSEENIVDSSEDIINQIASQYMDDRAFETDEEESTEFQITTKDAMKAIELLLNYEAQQPDGNPAITISLLNYQKLLEARGGNVNLSRLRST P50520 VPS34_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:7772832, ECO:0000269|PubMed:8719881}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000269|PubMed:7772832}; SPAC458.05; CHAIN 1..801; /note="Phosphatidylinositol 3-kinase vps34"; /id="PRO_0000088817" MDRLVFSYCPSSKVTARFLVKFCFIEYQDSQEPCICTIQLFSGNESGSLMQKCFVSKIPNKSLLPTELSKISTHEWLDFGVTVSELSLNAKFVVSAWKPSFNDEEVYEFVGCTTYRLFDENNLLRQGLQKIPLQTSKEIKKYSPTSLELEQVKEINRLDGLLLKLQLGDVPSVNWLDDISFGKIKDFRSKHMSLVTIPILYLDFLQFSFPVVFQRSYYPKSENRVYYSSFDLELNLDSPAELKHRRLVRSQRNGPLDKDLKPNSKIRKELESILSYPPSEELSLEEKDLIWKFRFYLTRNKKAMTKFLKSVVWTDSSEVNQALSLLDSWTEIDIDDALELLSPSFVHPKVRAYAVSRLETASNEELLLYLLQLVQALRYDNPISSDERFQPSPLALFLVNRAISSPSIGNDLYWYLVVEIEDEPVSKLFSSVMFLFQKELSKSVEGRLIRETLSAQAKFVEKLLRISKSVQSFRGTRLKKIEYLKVLLEDHKYHLLDFHALPLPLDPSVNIVGIIPDACTVFKSTMQPLRLLFKCQDGSKYPIIFKNGDDLRQDQLVIQILTLMDKLLKKEKLDLHLKPYRILATGPTHGAVQFVPSKTLATILAEYHGSVLAYLRENNPDDGLNSANYGIDPVAMDNYVRSCAGYCVITYLLGVGDRHLDNLLITKDGHFFHADFGYILGRDPKLFSPAMKLSKEMVEGMGGYNSPFYQQFKSYCYTTFTALRKSSNLILNLFSLMVDANIPDIKFDKEKVVYKVKERFCLQMSESDAIKYFEQLINDSVSALFPQIIDRMHNLAQYMRS P50521 HXK2_SCHPO BINDING 68..73; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P19367"; BINDING 144..145; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 161..162; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 196..197; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 222; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 225; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 252; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 283; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 288..289; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 325..329; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 400..404; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557" CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; CATALYTIC ACTIVITY: Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for D-glucose {ECO:0000269|PubMed:9790975}; SPAC4F8.07c; CHAIN 1..455; /note="Hexokinase-2"; /id="PRO_0000197610" MEANFQQAVKKLVNDFEYPTESLREAVKEFDELRQKGLQKNGEVLAMAPAFISTLPTGAETGDFLALDFGGTNLRVCWIQLLGDGKYEMKHSKSVLPRECVRNESVKPIIDFMSDHVELFIKEHFPSKFGCPEEEYLPMGFTFSYPANQVSITESYLLRWTKGLNIPEAINKDFAQFLTEGFKARNLPIRIEAVINDTVGTLVTRAYTSKESDTFMGIIFGTGTNGAYVEQMNQIPKLAGKCTGDHMLINMEWGATDFSCLHSTRYDLLLDHDTPNAGRQIFEKRVGGMYLGELFRRALFHLIKVYNFNEGIFPPSITDAWSLETSVLSRMMVERSAENVRNVLSTFKFRFRSDEEALYLWDAAHAIGRRAARMSAVPIASLYLSTGRAGKKSDVGVDGSLVEHYPHFVDMLREALRELIGDNEKLISIGIAKDGSGIGAALCALQAVKEKKGLA P50526 SSP1_SCHPO ACT_SITE 267; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 141..149; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 164; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 58; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 59; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 63; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPCC297.03; CHAIN 1..652; /note="Serine/threonine-protein kinase ssp1"; /id="PRO_0000086683" MGSVNNEEKTLIEPQRLLRKNTWHPEVDDSEVPPSVFPEYPVHKAIQKTSDSFRKRNYSAGDYVIAPLGGEREGSSLTHSWTFQPGKHNQRLYSDNFQEAQRQWKRLQEWGEVKETKKIRKRFDRFSGRKYINHYEIIKELGRGMHGKVKLGRDTVTRELLAIKIIPKTERRPKLGRANASSQKEKVRREIAILKKCVHPNVVRLREVIDDPSSTKVYLVLEYMSGGEVPWTDCDSPVLSISEARQYFRDVVLGLEYLHYQGIIHRDIKPANLLLNSSNCVKISDFGVSYIANAGLNEDNDVELAKTVGTPAFFAPELCWTDLDRPRPKISEAIDVWALGVTLFCLLFGRCPFNASMEYELFDKIVNERLNIPSTPDIGEEGRDLLKRLLCKDPEQRITLVEVKLHPWTLDGLKDPEKWLQNTDPSTVSRVEVSTDEVASAISLVGRLRRKLGKLFRFRRPKARVFDSSSSVPSDSSICRPESSGNSSIGLSASELSDSFNRLAVNESQKDRERKQVHPVEMGRNSSEKKPRCDFGWDYEAFPNDNQDADDACSYNTGDSIPQVSKSINGHFETYSRTSMDTDDVASFESPNAKHEESGMPVVTFRNYENYDANPSNFHPVVPGFVSSPNLHLAGGSDTPIYCIEHSFTPTN P50527 STE20_SCHPO ACT_SITE 505; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 392..400; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 415; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated on serine residues. {ECO:0000269|PubMed:18257517}. MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1604.14c; CHAIN 1..658; /note="Serine/threonine-protein kinase shk1/pak1"; /id="PRO_0000086651" MERGTLQPRKKAPNGYGITPIVAHKTGEPVRYEVEDDLRKLKPSRTAPKPPAINTNLAEDTFSGFPLSQSRTTVSRVSLGSRQHSSSSIRKLQTNVSDVRSYDERNQKKSAFENFVSSMSSFLTGGGSSPTSSYGSGSASPRKSTVISSPFDPKHVTHVGFNYDTGEFTGMPTEWQALLKVSGITKSEQVQHPQAVLDAMAFYSQSKKYLEEGAKPPFPRESTEKPLLSVSALSSSSHLQPTSATSSSSRLYPSRPAPTPPASSSSSPLLSSQTVKTTTSNASRQPSPLVSSKSTDNIIRSHSPVLLTPQTLSTSETKHIRPNNSTPYQRRAETSTKPKAVATPQKVEAPSAPRLQKRAPRQQSNDSAVLAKLQSICNPKNPTLLYRNFVKIGQGASGDVYSARQVGTNLSVAIKKMNINQQPKKEFIVNEILVMKSHHHKNIVNFIDTFFYKSELWMVMEYMRGGSLTEVVTNNTLSEGQIAAICKETLEGLQHLHENGIVHRDIKSDNILLSLQGDIKLTDFGFCAQIDSNMTKRTTMVGTPYWMAPEVVTRKEYGFKVDVWSLGIMAIEMVEGEPPYLNENPLRALYLIATIGTPKISRPELLSSVFHDFLSKSLTVNPKQRPSSGELLRHPFLKQAVPVSSLIPLIKSIHHSGK P50528 PLO1_SCHPO ACT_SITE 163; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 47..55; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 69; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; Evidence={ECO:0000250|UniProtKB:P32562}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21; Evidence={ECO:0000250|UniProtKB:P32562}; MOD_RES 442; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 585; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C11.16; CHAIN 1..683; /note="Serine/threonine-protein kinase plo1"; /id="PRO_0000086572" MASVAIKEPKTAITPKKKSKASRLCFTPPTNLHNNKKNIFYTRYDCIGEGGFARCFRVKDNYGNIYAAKVIAKRSLQNDKTKLKLFGEIKVHQSMSHPNIVGFIDCFEDSTNIYLILELCEHKSLMELLRKRKQLTEPEVRYLMMQILGALKYMHKKRVIHRDLKLGNIMLDESNNVKIGDFGLAALLMDDEERKMTICGTPNYIAPEILFNSKEGHSFEVDLWSAGVVMYALLIGKPPFQDKEVKTIYRKIKANSYSFPSNVDISAEAKDLISSLLTHDPSIRPSIDDIVDHEFFHTGYMASTLPDEILHSMPIWPSSQSKSSFQRNLDFVASASGVGFGNSAGVEKNKPYALRTDEVDNDRILPSVLSPRDRVNPVMKIGPETKPVPSKLSTALHAARKSTDGSLGSRVKVLREESQSFVPTKSAVTEQVEPIQLIRSLSANTVSRLSKVGNMKSDIWISVKKTALKIGMALEAHTHALTSEDADSEPVLFITKWVDYSNKYGLGYQLSDESVGVHFNDDTSLLFSADEEVVEYALHPKDTEIKPYIYPASKVPESIRSKLQLLKHFKSYMGQNLSKAVQDESFEKPKNSTSNTMLFMQHYLRTRQAIMFRLSNGIFQFNFLDHRKVVISSTARKIIVLDKERERVELPLQEASAFSEDLRSRLKYIRETLESWASKMEVS P50530 SCK1_SCHPO ACT_SITE 428; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 308..316; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 331; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 632; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 665; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B9.02c; CHAIN 1..696; /note="Serine/threonine-protein kinase sck1"; /id="PRO_0000086639" MTEIFGKLHRSSNSENTNQASPSTIQSHSTQPVLSNDHSTKVNDYEGKEGASSNGYDPVFMSDRMKMRYNEITAQLHKEQSLKEDKESGSNSSESNGITPMGTYSEKPKLLQSRTPPSSCYIRHDTVVPKDKNGQHAFGRLYVRLHQGRDLNVKSVNAQPYAVITFEKTQVMVPPPFKDIDGGIPISIPSKNRPLAGSASGSSSGLHSELMLADVRCPHWDFETVFDVTKMKSQMVVSVYDKYEDDKFLGSVKITPIFLHEYVQEAWYKLEPLDLTKSLEGEIKVETIYEHIEHVRYGPEDFTALRLIGKGTFGQVYLVRKNDTNRIYAMKKISKKLIVRKKEVTHTLGERNILVRTSLDESPFIVGLKFSFQTASDLYLITDYMSGGELFWHLQHEGRFPEQRAKFYIAELVLALEHLHKHDIIYRDLKPENILLDADGHIALCDFGLSKANLSANATTNTFCGTTEYLAPEVLLEDKGYTKQVDFWSLGVLVFEMCCGWSPFYAPDVQQMYRNIAFGKVRFPKGVLSSEGRSFVRGLLNRNPNHRLGAVADTTELKEHPFFADINWDLLSKKKVQPPFKPNVQNDLDVSNFDKEFTNTNVKNINIVSNVDPANASTPLSNTIQDRFRGFTFVNKSIDEQFQNLGLQENEETDNLHACRTTTHSSVNSINSHGNPRTVDANDPVADTVFGETFEA P50531 RAD17_SCHPO BINDING 112..119; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC14C4.13; CHAIN 1..606; /note="Checkpoint protein rad17"; /id="PRO_0000209952" MRRQLSFHESTKRSLKKKKIRKIEKPSLVSKTSRDKNASITDIHEEDIEAFSDEENKIVHLNNLKEDRFQLWFEKYIPQKAADLAVHKSKISAIKQWMLTDSLESRLLLICGPSGCGKSTAVQVLAKELGYSLIEWLNPMNLKEPSNQESDTLSLTEKFSRFMSLCETYPELELMDSNNIQKRGKNAQGKKKFIFLDEIPHLSKFNGSLDAFRNVIRTALTSRGAFSIIMVLTEIQLNNLEGINSQDRNSFNSVQIMGNDLLQDPRVTVLQFNPIAPTYMKKCLGSILRKEGVPKSPKLLSLVENICSASEGDLRSAINSLQLSISQSFEKKGTKNIREVKEGKGKGNDFSLEAAQVLERLSKSDSEAYARFKNYKSAYIPKSDKNENSFFKKDVGLGMMHAIGKVVWNKREGDDEVLKASSQQTGNSERIKGVKVSKSQENKNCISLKSDQRERMLNVDQCFTSKRRSLVDIESTINQSGLSGSVFRYGLFENYVDSCVTTDEAFNVCDLLSISDCLSHDFPYSYTGDEISTWFSVQGTLFYLPSPVPRKWRQLRFQQWNNEGIVRGIFDDYMVIYGKRSVSDPVIEAHEDQVLEDIDDPIEDED P50537 MAE1_SCHPO MOD_RES 413; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 423; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 428; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 432; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 433; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 437; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB8E5.03; CHAIN 1..438; /note="Malic acid transport protein"; /id="PRO_0000084550" MGELKEILKQRYHELLDWNVKAPHVPLSQRLKHFTWSWFACTMATGGVGLIIGSFPFRFYGLNTIGKIVYILQIFLFSLFGSCMLFRFIKYPSTIKDSWNHHLEKLFIATCLLSISTFIDMLAIYAYPDTGEWMVWVIRILYYIYVAVSFIYCVMAFFTIFNNHVYTIETASPAWILPIFPPMICGVIAGAVNSTQPAHQLKNMVIFGILFQGLGFWVYLLLFAVNVLRFFTVGLAKPQDRPGMFMFVGPPAFSGLALINIARGAMGSRPYIFVGANSSEYLGFVSTFMAIFIWGLAAWCYCLAMVSFLAGFFTRAPLKFACGWFAFIFPNVGFVNCTIEIGKMIDSKAFQMFGHIIGVILCIQWILLMYLMVRAFLVNDLCYPGKDEDAHPPPKPNTGVLNPTFPPEKAPASLEKVDTHVTSTGGESDPPSSEHESV P50582 HSK1_SCHPO ACT_SITE 216; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 74..82; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 129; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. Phosphorylated by cds1 in vitro. {ECO:0000269|PubMed:11027263, ECO:0000269|PubMed:18257517}. MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 291; /note="Phosphothreonine"; /evidence="ECO:0000250"; MOD_RES 493; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC776.12c; CHAIN 1..507; /note="Cell cycle serine/threonine-protein kinase hsk1"; /id="PRO_0000086003" MAEAHITLSPKVTHEQQTDIDSECEITEVDDENVNENKSQEMIQDIPARDREEIENITRTFVELQENYRLIEKIGEGTFSSVYKAEDLHYGRYINDWDIQSEVLKESSFGKEKIPVNEDSRKPKYVAIKKIYATSSPARIYNELEILYLLRGSSVIAPLITALRNEDQVLVVLPYYEHTDFRQYYSTFSYRDMSIYFRCLFQAMQQTQTLGIIHRDIKPSNFLFDVRTKHGVLVDFGLAERYDGRQQSHSCRCTNSNAAELAHDFSIAQETSLGYIKNDTRPSKRANRAGTRGFRAPEVLFKCSSQSPKVDIWSAGVILLSFLTKRFPMFNSKDDVDALMEIACIFGKSEMRQCAALHGCTFETNVSTLTEKRVNFRKLILWASCGSASIYKEKLRHKPSQEERLCLDFLEKCLELDCNKRISAEEALDHDFLYLDNLAYEKKDDDTAFDNSFGETSFEKDEDLTAKHLSHILDFKEQEETDEPTSLSKRKRSIDEILPNDALQDGA P50998 AMPD_SCHPO ACT_SITE 609; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10104" BINDING 319; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 321; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 321; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 390..395; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 587; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 590; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 664; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 665..668; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; Evidence={ECO:0000269|PubMed:8440738}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; MOD_RES 79; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 84; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 758; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 776; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 780; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 782; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC106.04; CHAIN 1..831; /note="AMP deaminase"; /id="PRO_0000194413" MNMEQEDDQVPAVAAETVPLKRYVTNPGANRDEEVAAAPSSQDTPYFDYAYERSLRHQDAKFLAMNGTQNGRDGLPSKSPRRPSVSASTVRNSDDVNHSKAGPGSGKLLNDTLQSKISSIHMPHVQQGDNAVVSSVGGPETDPGNMETTDPLFSDELAEIYLSIHKCMDMRHKYIRVSLQGELDNPIDDDSWIIYPDCKEGEDDTGLFNFADCKIPGIENEMEYHMDHQGIFQVYENDSAYIAGTPSFHIPTIRDYYIDLEFLLSASSDGPSKSFSFRRLQYLEGRWNMYMLLNEYQELADTKKVPHRDFYNVRKVDTHVHHSALANQKHLLRFIKAKLRKCPNEKVIWRDGKFLTLQEVFDSLKLTSYDLSIDTLDMHAHTDTFHRFDKFNLKYNPIGESRLRTIFLKTDNDINGRYLAELTKEVFTDLRTQKYQMAEYRISIYGRNREEWDKLAAWIIDNELFSPNVRWLIQVPRLYDVYKKSGIVETFEEVVRNVFEPLFEVTKDPRTHPKLHVFLQRVIGFDSVDDESKPERRTFRKFPYPKHWDINLNPPYSYWLYYMYANMTSLNSWRKIRGFNTFVLRPHCGEAGDTDHLASAFLLSHGINHGILLRKVPFLQYLWYLDQIPIAMSPLSNNALFLAYDKNPFLTYFKRGLNVSLSTDDPLQFAFTREPLIEEYAVAAQIYKLSAVDMCELARNSVLQSGFERQLKERWLGVDFQDIDRTNVPIIRLAYRALTLTQEIALVNKHVQPSKHPSNHDLEELIHKYDAMTGTSDPLSASPRTNDATISSRLSLHDGHDHGAFFPGLSVISERRRRKDSMASSSQDLKD P52890 ATF1_SCHPO PTM: Phosphorylated by sty1/spc1. {ECO:0000269|PubMed:8824587}. SPBC29B5.01; CHAIN 1..566; /note="Transcription factor atf1"; /id="PRO_0000076533" MSPSPVNTSTEPASVAAVSNGNATASSTQVPENNQSDSFAPPSNNSQQNQQSSTIAPNGGAGSVANANPADQSDGVTPSFVGSLKLDYEPNPFEHSFGSTASVGQGNPSLNRNPSLSNIPSGVPPAFARTLLPPVSSIASPDILSGAPGIASPLGYPAWSAFTRGTMHNPLSPAIYDATLRPDYLNNPSDASAAARFSSGTGFTPGVNEPFRSLLTPTGAGFPAPSPGTANLLGFHTFDSQFPDQYRFTPRDGKPPVVNGTNGDQSDYFGANAAVHGLCLLSQVPDQQQKLQQPISSENDQAASTTANNLLKQTQQQTFPDSIRPSFTQNTNPQAVTGTMNPQASRTQQQPMYFMGSQQFNGMPSVYGDTVNPADPSLTLRQTTDFSGQNAENGSTNLPQKTSNSDMPTANSMPVKLENGTDYSTSQEPSSNANNQSSPTSSINGKASSESANGTSYSKGSSRRNSKNETDEEKRKSFLERNRQAALKCRQRKKQWLSNLQAKVEFYGNENEILSAQVSALREEIVSLKTLLIAHKDCPVAKSNSAAVATSVIGSGDLAQRINLGY P53692 SMC6_SCHPO BINDING 124..131; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" PTM: Sumoylated by nse2. {ECO:0000269|PubMed:15601841}. SPCC5E4.06; STRAND 557..560; /evidence="ECO:0007829|PDB:5MG8"; STRAND 578..583; /evidence="ECO:0007829|PDB:5MG8"; STRAND 603..605; /evidence="ECO:0007829|PDB:5MG8"; STRAND 629..632; /evidence="ECO:0007829|PDB:5MG8"; STRAND 649..651; /evidence="ECO:0007829|PDB:5MG8"; STRAND 671..675; /evidence="ECO:0007829|PDB:5MG8"; STRAND 677..679; /evidence="ECO:0007829|PDB:5MG8"; STRAND 683..686; /evidence="ECO:0007829|PDB:5MG8"; STRAND 693..698; /evidence="ECO:0007829|PDB:5MG8"; STRAND 707..709; /evidence="ECO:0007829|PDB:5MG8" HELIX 450..491; /evidence="ECO:0007829|PDB:5MG8"; HELIX 502..511; /evidence="ECO:0007829|PDB:5MG8"; HELIX 512..514; /evidence="ECO:0007829|PDB:5MG8"; HELIX 524..528; /evidence="ECO:0007829|PDB:5MG8"; HELIX 532..539; /evidence="ECO:0007829|PDB:5MG8"; HELIX 553..556; /evidence="ECO:0007829|PDB:5MG8"; HELIX 562..564; /evidence="ECO:0007829|PDB:5MG8"; HELIX 565..571; /evidence="ECO:0007829|PDB:5MG8"; HELIX 575..577; /evidence="ECO:0007829|PDB:5MG8"; HELIX 584..597; /evidence="ECO:0007829|PDB:5MG8"; HELIX 614..616; /evidence="ECO:0007829|PDB:5MG8"; HELIX 626..628; /evidence="ECO:0007829|PDB:5MG8"; HELIX 634..644; /evidence="ECO:0007829|PDB:5MG8"; HELIX 646..648; /evidence="ECO:0007829|PDB:5MG8"; HELIX 655..663; /evidence="ECO:0007829|PDB:5MG8" TURN 492..498; /evidence="ECO:0007829|PDB:5MG8"; TURN 515..522; /evidence="ECO:0007829|PDB:5MG8" CHAIN 1..1140; /note="Structural maintenance of chromosomes protein 6"; /id="PRO_0000119021" MTTELTNVSLEEAITEKTSENRRKRDSDVLQTEEVDLSNVKRIRASRNQDNRPERQSRLQRSSSLIEQVRGNEDGENDVLNQTRETNSNFDNRVGVIECIHLVNFMCHDSLKINFGPRINFVIGHNGSGKSAILTGLTICLGAKASNTNRAPNMKSLVKQGKNYARISVTISNRGFEAYQPEIYGKSITIERTIRREGSSEYRLRSFNGTVISTKRDELDNICDHMGLQIDNPMNILTQDTARQFLGNSSPKEKYQLFMKGIQLKQLEENYSLIEQSLINTKNVLGNKKTGVSYLAKKEEEYKLLWEQSRETENLHNLLEQKKGEMVWAQVVEVEKELLLAEKEFQHAEVKLSEAKENLESIVTNQSDIDGKISSKEEVIGRAKGETDTTKSKFEDIVKTFDGYRSEMNDVDIQKRDIQNSINAAKSCLDVYREQLNTERARENNLGGSQIEKRANESNNLQREIADLSEQIVELESKRNDLHSALLEMGGNLTSLLTKKDSIANKISDQSEHLKVLEDVQRDKVSAFGKNMPQLLKLITRETRFQHPPKGPMGKYMTVKEQKWHLIIERILGNVINGFIVRSHHDQLILKELMRQSNCHATVVVGKYDPFDYSSGEPDSQYPTVLKIIKFDDDEVLHTLINHLGIEKMLLIEDRREAEAYMKRGIANVTQCYALDPRNRGYGFRIVSTQRSSGISKVTPWNRPPRIGFSSSTSIEAEKKILDDLKKQYNFASNQLNEAKIEQAKFKRDEQLLVEKIEGIKKRILLKRREVNSLESQELSVLDTEKIQTLERRISETEKELESYAGQLQDAKNEEHRIRDNQRPVIEEIRIYREKIQTETQRLSSLQTELSRLRDEKRNSEVDIERHRQTVESCTNILREKEAKKVQCAQVVADYTAKANTRCERVPVQLSPAELDNEIERLQMQIAEWRNRTGVSVEQAAEDYLNAKEKHDQAKVLVARLTQLLQALEETLRRRNEMWTKFRKLITLRTKELFELYLSQRNFTGKLVIKHQEEFLEPRVYPANRNLATAHNRHEKSKVSVQGLSGGEKSFATICMLLSIWEAMSCPLRCLDEFDVFMDAVNRLVSIKMMVDSAKDSSDKQFIFITPQDMGQIGLDKDVVVFRLSDPVVSSSALPPSTAP P53695 EXO1_SCHPO BINDING 30; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 78; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 150; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 152; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 171; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 173; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 225; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000250}; SPBC29A10.05; CHAIN 1..571; /note="Exodeoxyribonuclease 1"; /id="PRO_0000154044" MGIKGLLGLLKPMQKSSHVEEFSGKTLGVDGYVWLHKAVFTCAHELAFNKETDKYLKYAIHQALMLQYYGVKPLIVFDGGPLPCKASTEQKRKERRQEAFELGKKLWDEGKKSQAIMQFSRCVDVTPEMAWKLIIALREHGIESIVAPYEADAQLVYLEKENIIDGIITEDSDMLVFGAQTVLFKMDGFGNCITIRRNDIANAQDLNLRLPIEKLRHMAIFSGCDYTDGVAGMGLKTALRYLQKYPEPRAAIRAMRLDKSLKVPVSFEKEFALADLAFRHQRVYCPKDKTLVHLSPPERELSVHEDAFIGSFFDNQLAIDIAEGRSNPITKCAFDIKDSSMQSFTKTTITISKRKGISKTDISNFFMKSIPPSKRPTKSTSLIDVTNVKVQRTHLANDISSEKQSIKSANEKAYVTPKSNSLKPGFGKSLSDISNSATKNENVPFLPPRTGVSKYFKLQKNTEKEIDEQVPSQSNNTTPTSAKSDSASPQNWFSSFSYQTPNSASPPFSSLSHTLPISALAKIGHDALNRKNHASLPSRRIVYKPPSSPSTPISMNPRPKGILSLQQYKFR P54789 ORC1_SCHPO BINDING 334; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q13415"; BINDING 368..376; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q13415"; BINDING 454; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q13415"; BINDING 455; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q13415"; BINDING 455; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q13415"; BINDING 488; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q13415"; BINDING 557; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q13415" MOD_RES 291; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 292; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 320; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC29A10.15; CHAIN 1..707; /note="Origin recognition complex subunit 1"; /id="PRO_0000127073" MPRRKSLRSQLLINGIDKSLLSDDSADSSDIDEEEVYGVWTEEPFQKEAGRSYYRSLKKNDVIYRVGDDITVHDGDSSFYLGVICKLYEKAIDKHSGKKYVEAIWYSRAYAKRMEIKPEYLLPDRHINEVYVSCGRDENLTSCIIEHCNVYSEAEFFSKFPAGIPTKRKDLFPCNFFIRRGVHLKVNKYTEPLDWSYYAHNLERIEDLLVEMEENLRPTKKKSGSRGRGRPRKYPLPNVESKESSSKVNSKDENFDLQDDSESSEDNLTIQPQTPRRRHKRSRHNSSNLASTPKRNGYKQPLQITPLPIRMLSLEEFQGSPHRKARAMLHVASVPSTLQCRDNEFSTIFSNLESAIEEETGACLYISGTPGTGKTATVHEVIWNLQELSREGQLPEFSFCEINGMRVTSANQAYSILWESLTGERVTPIHAMDLLDNRFTHASPNRSSCVVLMDELDQLVTHNQKVLYNFFNWPSLPHSRLIVVAVANTMDLPERILSNRISSRLGLSRVPFEPYTHTQLEIIIAARLEAVRDDDVFSSDAIRFAARKVAAVSGDARRALDICRRASELAENKNGKVTPGLIHQAISEMTASPLQKVLRNLSFMQKVFLCAIVNRMRRSGFAESYVYEVLEEAERLLRVMTTPDAEAKFGELILRRPEFGYVLSSLSENGVLYLENKSSRNARVRLAIADDEIKLAFRGDSELAGIA P54874 ERG13_SCHPO ACT_SITE 86; /note="Proton donor/acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"; ACT_SITE 118; /note="Acyl-thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"; ACT_SITE 250; /note="Proton donor/acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10116" CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10; Evidence={ECO:0000255|PROSITE-ProRule:PRU10116, ECO:0000305|PubMed:8750242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189; Evidence={ECO:0000305|PubMed:8750242}; MOD_RES 398; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4F8.14c; CHAIN 1..447; /note="Hydroxymethylglutaryl-CoA synthase"; /id="PRO_0000213757" MSFDRKDIGIKGLVLYTPNQYVEQAALEAHDGVSTGKYTIGLGLTKMAFVDDREDIYSFGLTALSQLIKRYQIDISKIGRLEVGTETIIDKSKSVKSVLMQLFGDNHNVEGIDCVNACYGGVNALFNTIDWIESSAWDGRDGIVVAGDIALYAKGNARPTGGAGCVALLVGPNAPIVFEPGLRGTYMQHAYDFYKPDLTSEYPYVDGHFSLECYVKALDGAYANYNVRDVAKNGKSQGLGLDRFDYCIFHAPTCKQVQKAYARLLYTDSAAEPSNPELEGVRELLSTLDAKKSLTDKALEKGLMAITKERFNKRVSPSVYAPTNCGNMYTASIFSCLTALLSRVPADELKGKRVGAYSYGSGLAASFFSFVVKGDVSEIAKKTNLVNDLDNRHCLTPTQYEEAIELRHQAHLKKNFTPKGSIERLRSGTYYLTGIDDMFRRSYSVKP P56523 CLR3_SCHPO ACT_SITE 195; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:17289569}; SPBC800.03; STRAND 57..61; /evidence="ECO:0007829|PDB:5IKK"; STRAND 106..110; /evidence="ECO:0007829|PDB:5IKK"; STRAND 181..188; /evidence="ECO:0007829|PDB:5IKK"; STRAND 228..232; /evidence="ECO:0007829|PDB:5IKK"; STRAND 234..236; /evidence="ECO:0007829|PDB:5IKK"; STRAND 249..258; /evidence="ECO:0007829|PDB:5IKK"; STRAND 285..293; /evidence="ECO:0007829|PDB:5IKK"; STRAND 318..324; /evidence="ECO:0007829|PDB:5IKK"; STRAND 359..363; /evidence="ECO:0007829|PDB:5IKK"; STRAND 470..473; /evidence="ECO:0007829|PDB:5IKK"; STRAND 481..488; /evidence="ECO:0007829|PDB:5IKK"; STRAND 492..494; /evidence="ECO:0007829|PDB:5IKK"; STRAND 510..512; /evidence="ECO:0007829|PDB:5IKK"; STRAND 528..533; /evidence="ECO:0007829|PDB:5IKK"; STRAND 570..577; /evidence="ECO:0007829|PDB:5IKK"; STRAND 597..603; /evidence="ECO:0007829|PDB:5IKK"; STRAND 628..632; /evidence="ECO:0007829|PDB:5IKK"; STRAND 652..654; /evidence="ECO:0007829|PDB:5IKK" HELIX 65..68; /evidence="ECO:0007829|PDB:5IKK"; HELIX 82..93; /evidence="ECO:0007829|PDB:5IKK"; HELIX 117..129; /evidence="ECO:0007829|PDB:5IKK"; HELIX 140..142; /evidence="ECO:0007829|PDB:5IKK"; HELIX 146..151; /evidence="ECO:0007829|PDB:5IKK"; HELIX 160..178; /evidence="ECO:0007829|PDB:5IKK"; HELIX 209..220; /evidence="ECO:0007829|PDB:5IKK"; HELIX 239..245; /evidence="ECO:0007829|PDB:5IKK"; HELIX 269..271; /evidence="ECO:0007829|PDB:5IKK"; HELIX 279..281; /evidence="ECO:0007829|PDB:5IKK"; HELIX 297..306; /evidence="ECO:0007829|PDB:5IKK"; HELIX 308..315; /evidence="ECO:0007829|PDB:5IKK"; HELIX 341..351; /evidence="ECO:0007829|PDB:5IKK"; HELIX 355..357; /evidence="ECO:0007829|PDB:5IKK"; HELIX 369..383; /evidence="ECO:0007829|PDB:5IKK"; HELIX 398..411; /evidence="ECO:0007829|PDB:5IKK"; HELIX 435..451; /evidence="ECO:0007829|PDB:5IKK"; HELIX 477..479; /evidence="ECO:0007829|PDB:5IKK"; HELIX 515..524; /evidence="ECO:0007829|PDB:5IKK"; HELIX 548..562; /evidence="ECO:0007829|PDB:5IKK"; HELIX 580..590; /evidence="ECO:0007829|PDB:5IKK"; HELIX 619..626; /evidence="ECO:0007829|PDB:5IKK"; HELIX 637..639; /evidence="ECO:0007829|PDB:5IKK"; HELIX 647..649; /evidence="ECO:0007829|PDB:5IKK"; HELIX 660..666; /evidence="ECO:0007829|PDB:5IKK"; HELIX 668..678; /evidence="ECO:0007829|PDB:5IKK" TURN 222..224; /evidence="ECO:0007829|PDB:5IKK"; TURN 260..263; /evidence="ECO:0007829|PDB:5IKK"; TURN 333..335; /evidence="ECO:0007829|PDB:5IKK"; TURN 412..414; /evidence="ECO:0007829|PDB:5IKK"; TURN 506..508; /evidence="ECO:0007829|PDB:5IKK"; TURN 563..566; /evidence="ECO:0007829|PDB:5IKK"; TURN 594..596; /evidence="ECO:0007829|PDB:5IKK" CHAIN 1..687; /note="Histone deacetylase clr3"; /id="PRO_0000114739" MLASNSDGASTSVKPSDDAVNTVTPWSILLTNNKPMSGSENTLNNESHEMSQILKKSGLCYDPRMRFHATLSEVDDHPEDPRRVLRVFEAIKKAGYVSNVPSPSDVFLRIPAREATLEELLQVHSQEMYDRVTNTEKMSHEDLANLEKISDSLYYNNESAFCARLACGSAIETCTAVVTGQVKNAFAVVRPPGHHAEPHKPGGFCLFNNVSVTARSMLQRFPDKIKRVLIVDWDIHHGNGTQMAFYDDPNVLYVSLHRYENGRFYPGTNYGCAENCGEGPGLGRTVNIPWSCAGMGDGDYIYAFQRVVMPVAYEFDPDLVIVSCGFDAAAGDHIGQFLLTPAAYAHMTQMLMGLADGKVFISLEGGYNLDSISTSALAVAQSLLGIPPGRLHTTYACPQAVATINHVTKIQSQYWRCMRPKHFDANPKDAHVDRLHDVIRTYQAKKLFEDWKITNMPILRDSVSNVFNNQVLCSSNFFQKDNLLVIVHESPRVLGNGTSETNVLNLNDSLLVDPVSLYVEWAMQQDWGLIDINIPEVVTDGENAPVDILSEVKELCLYVWDNYVELSISKNIFFIGGGKAVHGLVNLASSRNVSDRVKCMVNFLGTEPLVGLKTASEEDLPTWYYRHSLVFVSSSNECWKKAKRAKRRYGRLMQSEHTETSDMMEQHYRAVTQYLLHLLQKARPTSQ P78753 ASNS_SCHPO ACT_SITE 2; /note="For GATase activity"; /evidence="ECO:0000250" BINDING 50..54; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250"; BINDING 75..77; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250"; BINDING 99; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250"; BINDING 235; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 280; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 354..355; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4; MOD_RES 391; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 489; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC119.10; CHAIN 2..557; /note="Probable asparagine synthetase [glutamine-hydrolyzing]"; /id="PRO_0000056916" MCGILAVHHVAEDIEAFKPKALHLSKQLRHRGPDWSGKAIRNQTILCHERLAIVGVESGAQPLVSDDGKLVLTVNGEIYNHLKLRENLKGNYKFKTYSDCEVILYLYREHGPACANMLDGMFSWVLYDQDKDKVVAARDPIGITTLYQGFSSDSPDTAYFASELKALHPVCDKIIAFPPGHYYDSETKQTVRYFKPSWWDENKIPSNPVDYKLLRETLEASVRKRLMAEVPYGVLLSGGLDSSLIASIAARETEKLANSTSQSEEARTITAWPKLHSFAIGLPGSPDLLAARKVADFLHTFHHEHTFTIDEGLDALRDVIYHLETYDVTTIRASTPMYLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFGNAPSREAFHSECVRRVKNLHLSDCLRANKSTMAWGLEARVPFLDKDFLEVALNIDPEEKMYINGRKEKYILRKAFDTTHDSSLQPYLPQDILWRQKEQFSDGVGYSWIDALKDTAELCISDDEFALPRREWGDDIPTTKEAFWYRKLFDEIFPRQCADTVMRWVPKAEWGCPEDPSGRYQAGHVAALK P78774 ARPC1_SCHPO SPBC14C8.06; STRAND 3..9; /evidence="ECO:0007829|PDB:8UXW"; STRAND 15..19; /evidence="ECO:0007829|PDB:8UXW"; STRAND 23..29; /evidence="ECO:0007829|PDB:8UXW"; STRAND 31..33; /evidence="ECO:0007829|PDB:8UXW"; STRAND 35..41; /evidence="ECO:0007829|PDB:8UXW"; STRAND 44..51; /evidence="ECO:0007829|PDB:8UXW"; STRAND 58..63; /evidence="ECO:0007829|PDB:8UXW"; STRAND 69..74; /evidence="ECO:0007829|PDB:8UXW"; STRAND 79..84; /evidence="ECO:0007829|PDB:8UXW"; STRAND 90..95; /evidence="ECO:0007829|PDB:8UXW"; STRAND 103..108; /evidence="ECO:0007829|PDB:8UXW"; STRAND 112..122; /evidence="ECO:0007829|PDB:8UXW"; STRAND 124..129; /evidence="ECO:0007829|PDB:8UXW"; STRAND 136..141; /evidence="ECO:0007829|PDB:8UXW"; STRAND 149..154; /evidence="ECO:0007829|PDB:8UXW"; STRAND 160..165; /evidence="ECO:0007829|PDB:8UXW"; STRAND 168..174; /evidence="ECO:0007829|PDB:8UXW"; STRAND 190..192; /evidence="ECO:0007829|PDB:8UXW"; STRAND 198..203; /evidence="ECO:0007829|PDB:8UXW"; STRAND 208..213; /evidence="ECO:0007829|PDB:8UXW"; STRAND 220..224; /evidence="ECO:0007829|PDB:8UXW"; STRAND 228..233; /evidence="ECO:0007829|PDB:8UXW"; STRAND 242..248; /evidence="ECO:0007829|PDB:8UXW"; STRAND 250..252; /evidence="ECO:0007829|PDB:8UXW"; STRAND 254..261; /evidence="ECO:0007829|PDB:8UXW"; STRAND 264..269; /evidence="ECO:0007829|PDB:8UXW"; STRAND 275..280; /evidence="ECO:0007829|PDB:8UXW"; STRAND 283..290; /evidence="ECO:0007829|PDB:8UXW"; STRAND 330..333; /evidence="ECO:0007829|PDB:8UXW"; STRAND 340..342; /evidence="ECO:0007829|PDB:8UXW"; STRAND 347..355; /evidence="ECO:0007829|PDB:8UXW"; STRAND 362..367; /evidence="ECO:0007829|PDB:8UXW"; STRAND 371..376; /evidence="ECO:0007829|PDB:8UXW" HELIX 292..295; /evidence="ECO:0007829|PDB:8UXW"; HELIX 317..329; /evidence="ECO:0007829|PDB:8UXW" TURN 65..67; /evidence="ECO:0007829|PDB:8UXW"; TURN 131..133; /evidence="ECO:0007829|PDB:8UXW"; TURN 178..180; /evidence="ECO:0007829|PDB:8UXW"; TURN 225..227; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..377; /note="Actin-related protein 2/3 complex subunit 1"; /id="PRO_0000050858" MATSQVLHILPKPSYEHAFNSQRTEFVTTTATNQVELYEQDGNGWKHARTFSDHDKIVTCVDWAPKSNRIVTCSQDRNAYVYEKRPDGTWKQTLVLLRLNRAATFVRWSPNEDKFAVGSGARVISVCYFEQENDWWVSKHLKRPLRSTILSLDWHPNNVLLAAGCADRKAYVLSAYVRDVDAKPEASVWGSRLPFNTVCAEYPSGGWVHAVGFSPSGNALAYAGHDSSVTIAYPSAPEQPPRALITVKLSQLPLRSLLWANESAIVAAGYNYSPILLQGNESGWAHTRDLDAGTSKTSFTHTGNTGEGREEEGPVSFTALRSTFRNMDLKGSSQSISSLPTVHQNMIATLRPYAGTPGNITAFTSSGTDGRVVLWTL P78795 EIF3G_SCHPO MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:18257517"; MOD_RES 164; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:18257517" SPBC18H10.03; CHAIN 1..282; /note="Eukaryotic translation initiation factor 3 subunit G"; /id="PRO_0000123513" MSSSKSLDWADDEDYGTGLPSIQTFDNPDGTKTMIEFRIDDNGKKVKVTRVIRKTVITERVQHAVAERKKWKKFGKEAGKNSGVDARTTSVGENVQLRLQLGWTTTKEEEQDEAALAAAKVKAKGSSVVRCRACKGNHFTAQCPYKSIIGPVDEPPLDASPVSSRASGALGEKGRYIAPHLRAGSGRESGDSMFKRERDDSATLRVTNLSDDTREEELRDLFRRFGGIQRVYLAKDKETGRAKGFAFVSYYDRDCAIKARDRLDGYGWNNLILRCEFSKPRD P78810 VTC4_SCHPO ACT_SITE 453; /evidence="ECO:0000250|UniProtKB:P47075" BINDING 198; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 262; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 264; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 279; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 292; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 357; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 359; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P47075"; BINDING 421; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:P47075" CATALYTIC ACTIVITY: Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP; Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1; Evidence={ECO:0000250|UniProtKB:P47075}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19574; Evidence={ECO:0000250|UniProtKB:P47075}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P47075}; MOD_RES 495; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 497; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 501; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 534; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 546; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1322.14c; CHAIN 1..721; /note="Vacuolar transporter chaperone complex subunit 4"; /id="PRO_0000363396" MKFGQLLKETLMYEYKYSYVNYDKLKKEIKRRNDQGGWSEEDESDFVELLEKELDKVYSFQKNKSAEVMERIRFCEEQTDEVVRRLDSDNPPNENDFAILETELTDIMATVHDLAKFSELNYTAFYKIIKKHDKHTGWILKPVFAARLNAKPFFKEQYDLLVVKLSKLYDFVRTRGSPIKGDSAAGGTQQNFVRQTTKYWVHPNNVTELKIYILKHLPVLVFNPNKEFAREDAAITSIYYDNDDLDFYLGRLEKREGAEAIRLRWYGNMDNNNIFVERKTHREDWTGEKSVKARFPLKEKYVNAFLRGDYTVEEAFAKMRKDGKKSLKEIESLERLAKEVQYTVLSRGMKPYVRSFYERTAFQLPGDARVRISLDTNLSLIREDGPSRAGNNWRRMDIGIDYPFDQLPDEDIVRFPYAILEVKLQTQFGQDPPEWVNNLVNSHLVEAVPKFSKFIHGVSTLFYDRVTLLPYWFPQMDIDIRKPATHTFIQGRSQSGTHSSSVSANVLTDSENTPIHADGDNYVDEESRIGSSSTRNDNSTFQTSDSFQELDERTNLLDISKRKGRDSFVAALNSRLKDIKDSFFLETVPKFEEPTEPTVIYEQKYVSPPGKRIYVPVRVEPKTYFALERTYLDYLRYSILMGSIGITLFSFAKTRSGILGAASFTLVALFAIFYSTFLYLWRAVNIAKHNAVRYDDRFGPTAICVITFAAISANVILNFNA P78820 ACAC_SCHPO ACT_SITE 393; /evidence="ECO:0000250" BINDING 266..271; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 375; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 389; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 389; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 391; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 1772; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250"; BINDING 2074; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250"; BINDING 2076; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000250|UniProtKB:Q00955}; CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14; Evidence={ECO:0000250|UniProtKB:Q5SWU9}; COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250|UniProtKB:O00763}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; MOD_RES 745; /note="N6-biotinyllysine"; /evidence="ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU01066"; MOD_RES 1179; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1181; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC56E4.04c; CHAIN 1..2280; /note="Acetyl-CoA carboxylase"; /id="PRO_0000146769" MRQSVTSSSSCSKLYAIKATISLPRLFYRRLRTMAPRVASHFLGGNSLDKAPAGKVKDYIASHGGHTVITSILIANNGIAAVKEIRSIRKWAYETFNNERAIKFTVMATPDDLKVNADYIRMADQYVEVPGGSNNNNYANVELIVDIAERMNVHAVWAGWGHASENPKLPEMLSASSKKIVFIGPPGSAMRSLGDKISSTIVAQSARVPCMSWSGNELDQVRIDEETNIVTVDDDVYQKACIRSAEEGIAVAEKIGYPVMIKASEGGGGKGIRQVTSTEKFAQAFQQVLDELPGSPVFVMKLAGQARHLEVQILADQYGNNISLFGRDCSVQRRHQKIIEEAPVTIAPAATFHEMERAAVRLGELVGYASAGTIEYLYEPENDRFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQVAMGLPLSRIPHIRELYGLPRDGDSEIDFFFQNPESFKVQKVPTPKGHCVACRITSEDPGEGFKPSSGMIKDLNFRSSSNVWGYFSVGTAGGIHEFADSQFGHIFSFAESRESSRKSMVVALKELSIRGDFRTTVEYLVRLLETKEFSENEFTTGWLDRLIAQKVTSARPDKMLAVVCGALVRAHATADTQYRAFKSYLERGQVPSREFLKNVYDIEFIYDNTRYRFTASRSSPGSYHLFLNGSRCTAGVRSLTDGGLLVLLNGHSYTVYYRDEVTGTRISIDNLSCMLEQENDPTQLRTPSPGKLVRFLVETGEHIKAGEAYAEVEVMKMIMPLVATEDGVVQLIKQPGASLDAGDILGILTLDDPSRVTHALPFDGQLPNWGEPQIAGNKPCQRYHALLCILLDILKGYDNQIILNSTYNEFVEVLRNHELPYSEWSAHYSALVNRISPVLDKLFVSIIEKARSRKAEFPAKQLEVAIQTYCDGQNLATTQQLKVQIAPLLKIISDYKDGLKVHEYNVIKGLLEEYYNVEKLFSGINKREEDVILRLRDENKDDVDKVIALALSHSRIGSKNNLLITILDLMKSEPSTFVSLYFNDILRKLTDLDSRVTSKVSLKARELLITCAMPSLNERFSQMEHILKSSVVESHYGDAKFSHRTPSLDILKELIDSKYTVFDVLPAFFCHTDPWVSLAALEVYVRRAYRAYSVLEINYHTEAGTPYVLTWRFQLHSSGAPGLGANSTNGSNFPASTTPSYENSNRRLQSVSDLSWYVNKTDSEPFRFGTMIAAETFDELENNLALAIDRLPLSRNYFNAGLTLDGNSSSANDNTQELTNVVNVALTSTGDLDDSAIVSKLNQILSDFRDDLLEHNVRRVTIVGGRINKSAYPSYYTYRVSAEQKDGNLVHYNEDERIRHIEPALAFQLELGRLSNFNIEPVFTDNHNIHVYRATAKNMDTDKRFFTRALVRPGRLRDEIPTAEYLISETHRLINDILDALEVIGHEQTDLNHIFINFTPAFGLAPKQVEAALGGFLERFGRRLWRLRVTAAEIRIICTDPSTNTLFPLRVIISNVSGFVVNVEIYAEVKTENNSWIFKSIGQPGSMHLRPISTPYPTKEWLQPRRYKAQLMGTTFVYDFPELFRRAFTDSWKKVPNGRSKVTIPQNMFECKELVADEHGVLQEVNREPGTNSCGMVAWCITVKTPEYPNGRKIIVVANDITFQIGSFGPQEDEYFYKVTQLARQRGIPRIYLAANSGARIGVADEIVPLFNIAWVDPDSPEKGFDYIYLTPEAYERLQKENPNILTTEEVVTETGELRHKITTIIGSSEGLGVECLRGSGLIAGVTSRAYNDIFTCTLVTCRAVGIGAYLVRLGQRAVQIEGQPIILTGAPALNKVLGREVYTSNLQLGGTQVMHRNGISHLTSQDDFDGISKIVNWISYIPDKRNNPVPISPSSDTWDRDVEFYPSQNGYDPRWLIAGKEDEDSFLYGLFDKGSFQETLNGWAKTVVVGRARMGGIPTGVIAVETRTIENTVPADPANPDSTEQVLMEAGQVWYPNSAFKTAQAINDFNHGEQLPLFILANWRGFSGGQRDMFNEVLKYGSYIVDALASYKQPVFVYIPPFSELRGGSWVVVDPTINEDQMEMYADEESRAGVLEPEGMVSIKFRREKLLSLMRRCDHKYASLCNELKRDDLSADDLSTIKVKLMEREQKLMPIYQQISIHFADLHDRVGRMVAKKVVRKPLKWTEARRFFYWRLRRRLNEHYALQKITQLIPSLTIRESREYLQKWYEEWCGKQDWDESDKSVVCWIEEHNDDLSKRTQELKSTYYSERLSKLLRSDRKGMIDSLAQVLTELDENEKKELAGKLASVN P78831 GHT5_SCHPO MOD_RES 528; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 537; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1235.14; CHAIN 1..546; /note="High-affinity glucose transporter ght5"; /id="PRO_0000050413" CARBOHYD 357; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGKNLTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRFADRYNPVTDSYSYSSARQGLITGMVNVGSFFGCFLSSPLMDRIGKRTSIMFWTIVYLIGIILQVTAVPSWVQIMVAKIWTGLSIGALSVLAPGFQSEVAPADLRGTIVTTYQLAVTGGIFIAACINMGTHKLHKTAQWRVSMGINLLWGIITFIGISFLPESPRYLISVGRDEEALQIMAKNNDLPIEHEVIQTEYHVIKSDCEAELAGGPATWPEIFGPDIRYRTFLGLGVMSLQQLTGDNYYFYYGFEVFEGTGMNSPYLSALILDAVNFGCTFGGLFVLEFFGRRMPLIIGALWQSITFFIYAAVGNRALTRKNGTSNHRAGAVMIVFSCLFIFSFAQTWGPAAYVIVGESYPIRYRSKCAAVATTGNWLWGFLISFFTPFITNSIGFKYGYIFAACNLCAACIIFLFAHETKGLTLEEINELYISGAKPWMPRPKNLGNFTKQQEEVREKSRGVQGESAAHLENVDGEEGIEDSSNDISSTTSSDGRAKPESSYHDQEEQFA P78871 RST2_SCHPO SPAC6F12.02; CHAIN 1..567; /note="Zinc finger protein rst2"; /id="PRO_0000046883" MTRESLAPIASKANTLSESKVSENLMSINSDSGTSNANTPSSVTSNSKPVASSTAAKKDPNAPPQKVKQYVCETCTRAFARLEHLKRHIRSHTNEKPFTCSEIDGLPTGCGRQFSRRDLLLRHQQKIHRNPQPRRRRRSTTALPNPSLSNVSVSTTNLASKPVISLPQADSIDKFRYPKLHAALQAQLANNSGSFSASWLQAQQQRLVSAGNGRETVNASASGAVNPTSSQWSDQRLGVPYGPDSPLYYRRATIASDLRPSVYQHPQLYDFNRPESLSGQLDDESLARMPYSPNAVSRNYAMNMTLPESIPEGYEIDKLDWMSFSESLNLPTFNQPSGPSDVSASFLNLQAMPSPHASPKDSLINKSNSYFFQNPPKSNSVDYTRLDNLEHMRQSCISPSGTNFSPSCYSPESLMQQPLTLSPSSIPSGLPTYAHVNSPLGTEQYPSEAYPPKGYVDMEGRISEGIKEEGISLSEEITDKDQAFASMGYFDSYNFEGVENSNSLNNEGDQMETNFQSEKLDNSNSIPFFNFNSFNNNGANWSSDFNYPVSETSGLLTDNNRNQPPSF P78875 TPP1_SCHPO CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12; Evidence={ECO:0000305|PubMed:11004189}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P31688}; SPAC19G12.15c; CHAIN 1..817; /note="Trehalose-phosphatase"; /id="PRO_0000122508" MSVYGKIPSTSFEHENTFELSGDLLDPEELKSLGVSGRIIYVLRHLPFKSSINEETREWDLSGRRGATTMYSSMNWLANSTYWQTTLVGWTGVIPTVSEKEENKDAVTRLDSQDVKRFEETYSQWNSGERSTEYVPVWLPGPEKGSETIINETRSQQSRWLAYAENVIRPLIHYKYWPSSEVDENEEQWWRDYVKMNHAFADKICEIYKPGDFIIVQDYSLFLVPQLIRNKIDDAVIGFYHHHPFPSSEIARCFPRRRAILRSVLGADFIGFEDYSYARHFISCCSRVLDLEIGHDWVNLNGNKVTVRAITVGIDVPRIIRSSGNVSVSEKLEELNKRYENMKVILGRDRLDELYGVPQKLRSFQRFLRTYPEWRKKVVLIQITISSAFKHPKLLSSIKKLVQAINQEFGTDDYTPVHHVEEQLEPADYFALLTRADALFINSIREGVSNLALEYVVCQRDRYGMVLLSEFTATSAMLHDVPLINPWDYNECAEIISNALSTPLERRKMIERESYKQVTTHTMQSWTSSLIRSLANKLAATKTDQRIPTLTPEHALSVYSKASKRLFMMDYDGTLTPIVRDPNAAVPSKKLLDNLATLAADPKNQVWIISGRDQQFLRNWMDDIKGLGLSAEHGSFVRKPHSTTWINLAELLDMSWKKEVRRIFQYYTDRTQGSSIEEKRCAMTWHYRKADPENGAFQALECEALLEELVCSKYDVEIMRGKANLEVRPSSINKGGIVKQILSSYPEDSLPSFIFCAGDDRTDEDMFRSLHKNTRINKETSFAVTIGSDKKLSIADWCIADPANVIDILADLANFTN P78929 COFI_SCHPO SPAC20G4.06c; STRAND 26..32; /evidence="ECO:0007829|PDB:2I2Q"; STRAND 36..45; /evidence="ECO:0007829|PDB:2I2Q"; STRAND 59..61; /evidence="ECO:0007829|PDB:2I2Q"; STRAND 63..71; /evidence="ECO:0007829|PDB:2I2Q"; STRAND 73..76; /evidence="ECO:0007829|PDB:2I2Q"; STRAND 78..86; /evidence="ECO:0007829|PDB:2I2Q"; STRAND 115..119; /evidence="ECO:0007829|PDB:2I2Q" HELIX 10..21; /evidence="ECO:0007829|PDB:2I2Q"; HELIX 50..55; /evidence="ECO:0007829|PDB:2I2Q"; HELIX 93..107; /evidence="ECO:0007829|PDB:2I2Q" CHAIN 1..137; /note="Cofilin"; /id="PRO_0000214914" MSFSGVKVSPECLEAFQELKLGKSLRYVVFKMNDTKTEIVVEKKSTDKDFDTFLGDLPEKDCRYAIYDFEFNLGEGVRNKIIFISWSPDVAPIKSKMVYSSSKDTLRRAFTGIGTDIQATDFSEVAYETVLEKVTRK P78937 MET3_SCHPO ACT_SITE 194; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; ACT_SITE 195; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; ACT_SITE 196; /evidence="ECO:0000255|HAMAP-Rule:MF_03106" BINDING 193..196; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; BINDING 193; /ligand="sulfate"; /ligand_id="ChEBI:CHEBI:16189"; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; BINDING 195; /ligand="sulfate"; /ligand_id="ChEBI:CHEBI:16189"; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; BINDING 287..290; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; BINDING 291; /ligand="sulfate"; /ligand_id="ChEBI:CHEBI:16189"; /evidence="ECO:0000255|HAMAP-Rule:MF_03106"; BINDING 329; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03106" CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03106}; MOD_RES 356; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27.08c; CHAIN 1..490; /note="Sulfate adenylyltransferase"; /id="PRO_0000105953" MTKALLKDLNARDAPLREQLEQEATSLPKIVLSERQFCDVELILNGGFSPLDGFMNQKDYLNVVENLRLSTGEVFPIPITLDLNESQADSLKAGDRVALLDPRDGQTVIAILTVEDKYTPDKANEAEKVFGANDRAHPAVDYLFGRAGNVYVGGKLQAVTPIRHFDFVEYRYSPAQLRSDFQRNNWNRVVAFQTRNPMHRAHRELTVRAAKQHGARVLIHPVVGMTKPGDIDHFTRVRVYEAILQRYPKGSAKLSLLPLAMRMAGPREALWHAIIRKNYGASHFIIGRDHAGPGKNSQGEDFYGPYDAQYLVEQYAQEIGITIVPFQMMTYLPDEDIYKPVDKVEPGTRTLNISGTELRRRLRVGANIPEWFSYPEVVAILRQSYPPKYSQGFVLAVPATSDKLLPSALVSALNEDGRRHVTLLPRLDAISVFYAQELQRAGAAVVVSLADADASVKVPAEWTTVNIKPKDSVSEVTFAVLSQLSDEGYL P78953 MID1_SCHPO PTM: Phosphorylated (PubMed:18257517, PubMed:8946912). At the onset of mitosis, becomes hyperphosphorylated, leaves the nucleus, and forms a medial ring (PubMed:8946912). Phosphorylation by plo1 and other kinases may contribute to solubilizing mid1 for export from the nucleus (Probable) (PubMed:21376600). Phosphorylation by sid2 drives removal from the cortex at the actomyosin contractile ring constriction onset (PubMed:28605916). {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:21376600, ECO:0000269|PubMed:28605916, ECO:0000269|PubMed:8946912, ECO:0000305|PubMed:31243991}. MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:21376600"; MOD_RES 24; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:21376600"; MOD_RES 34; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:21376600"; MOD_RES 46; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:21376600"; MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:21376600"; MOD_RES 95; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:21376600"; MOD_RES 531; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4B3.15; STRAND 583..595; /evidence="ECO:0007829|PDB:4XOH"; STRAND 605..611; /evidence="ECO:0007829|PDB:4XOH"; STRAND 614..620; /evidence="ECO:0007829|PDB:4XOH"; STRAND 628..638; /evidence="ECO:0007829|PDB:4XOH"; STRAND 642..652; /evidence="ECO:0007829|PDB:4XOH"; STRAND 714..723; /evidence="ECO:0007829|PDB:4XOH"; STRAND 736..744; /evidence="ECO:0007829|PDB:4XOH"; STRAND 762..774; /evidence="ECO:0007829|PDB:4XOH"; STRAND 797..799; /evidence="ECO:0007829|PDB:4XOH"; STRAND 803..810; /evidence="ECO:0007829|PDB:4XOH"; STRAND 818..824; /evidence="ECO:0007829|PDB:4XOH"; STRAND 827..832; /evidence="ECO:0007829|PDB:4XOH"; STRAND 837..844; /evidence="ECO:0007829|PDB:4XOH"; STRAND 846..848; /evidence="ECO:0007829|PDB:4XOH"; STRAND 867..873; /evidence="ECO:0007829|PDB:4XOH"; STRAND 878..884; /evidence="ECO:0007829|PDB:4XOH"; STRAND 901..903; /evidence="ECO:0007829|PDB:4XOH" HELIX 724..726; /evidence="ECO:0007829|PDB:4XOH"; HELIX 728..731; /evidence="ECO:0007829|PDB:4XOH"; HELIX 780..782; /evidence="ECO:0007829|PDB:4XOH"; HELIX 787..794; /evidence="ECO:0007829|PDB:4XOH"; HELIX 860..863; /evidence="ECO:0007829|PDB:4XOH"; HELIX 886..896; /evidence="ECO:0007829|PDB:4XOH"; HELIX 910..918; /evidence="ECO:0007829|PDB:4XOH" TURN 833..836; /evidence="ECO:0007829|PDB:4XOH" CHAIN 1..920; /note="Anillin-related medial ring protein mid1"; /id="PRO_0000079937" MKEQEFSYREAKDVSLDSKGLENSFLSSPNREKTPLFFEGNSNETSGYDQTKNFTHGDGDMSLGNLSELNVATDLLESLDLRSMYMHGYGHLDSSFSSQHSPDNRKRMSSTSVFKRINSEEEGRIPSLTYSAGTMNSTSSSTASLKGADIVADYETFNPDQNLAELSFDRSKSSRKRAVEVAEFSRAKTMSPLEYTVQHPYQSHNELSTNPARARAGSVPNLARIPSDVKPVPPAHLSASSTVGPRILPSLPKDTTEDNPALERVETTASLDMDYKPLEPLAPIQEAPVEDTSEPFSSVPEATLDDSDISTESLRKKVLAKMEAKRISSGSSYASTLRKVYDFSELSLPTNGKDYDELYLQSSRNSEPEISTIINDSLQQENMDEDISATSIPKSQAAYGHGSVTYHEVPRYNLTSASVGYSISSQRGRIKSSSTIDNLSAILSSEDLRHPSMQPVPGTKRTYSNYCENEPNKSSQSLVSSESHNVEGWNYSETGTVGFYDPSAEISASIDELRQSTPVARDSELLSRAHSFDLNRLDLPSQDKSTSYEVPNGTENQSPRPVTSLGFVNETFFEEKPKAPLPLGRFYIHLNSILNISISEVHSPIKIIVNTPTQNMQLPWQAVNGNNRLDHDFAFHVDDNFKVSFMFLDIPIEDKSNGSKGVSATKDVSNGKPAETKSKARKFFDKLFNRRKKRKLNKAAAVENSKAKKSVVIKKVSGTATLNLGNVKDSCFGKAFNVEIPIISRGFLEAIPVKINSIGKRTLGNLTLTCLYIPELSVPEQELPFTLEQATMDLRHVRSNYLYNEGYLYRLEDSSIRRRFVVLRSKQLNFYAEKGGQYLDTFQLSKTVVSIPMVNFSEAVSNLGLVAGILATSVDRRHVQLFADSKKVCQKWLQVMNSRSFALDRGTEKLWLQEYVNFMA P78955 HUS1_SCHPO MOD_RES 210; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC20G4.04c; CHAIN 1..287; /note="Checkpoint protein hus1"; /id="PRO_0000084096" MRFKTRISNLYTLTRLVQALDKIGRFCWLRLMPETVNFVIVPDFRMTQVWSVLEVETIFEDYVVQSNADNVINLEVPIDNFYKALRSAANASDSTVRLSKKNNQPLLSLSTTWSGRAFGSNIVTHNIPVRVLSQSYVSVIKEPTAPEPDCHIFLPQLNFLRHVVDKYKSLSDRIIMSANMSGELQLSVNIPSARVSTKWKGLENPELDPSQVEDISRHPSQTRAPEEFVHMRLDSKDLVNMLKISSVAKRVIACFCEGHALVLYVYITDPEDEHTAVLTYYISTYVD P78958 G3P1_SCHPO ACT_SITE 152; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10009" BINDING 13..14; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 35; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 80; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 151..153; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 182; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 211..212; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 234; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 316; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PRU10009}; MOD_RES 59; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32F12.11; CHAIN 1..336; /note="Glyceraldehyde-3-phosphate dehydrogenase 1"; /id="PRO_0000145580" MAIPKVGINGFGRIGRIVLRNALVAKTIQVVAINDPFIDLEYMAYMFKYDSTHGRFDGSVEIKDGKLVIDGNAIDVHNERDPADIKWSTSGADYVIESTGVFTTQETASAHLKGGAKRVIISAPSKDAPMYVVGVNEEKFNPSEKVISNASCTTNCLAPLAKVINDTFGIEEGLMTTVHATTATQKTVDGPSKKDWRGGRGASANIIPSSTGAAKAVGKVIPALNGKLTGMAFRVPTPDVSVVDLTVKLAKPTNYEDIKAAIKAASEGPMKGVLGYTEDAVVSTDFCGDNHSSIFDASAGIQLSPQFVKLVSWYDNEWGYSRRVVDLVAYTAAKDN P78963 SKB1_SCHPO ACT_SITE 422; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:O14744"; ACT_SITE 431; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:O14744" BINDING 316; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O14744"; BINDING 325..326; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O14744"; BINDING 379; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O14744"; BINDING 406..407; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O14744" SPBC16H5.11c; CHAIN 1..645; /note="Protein arginine N-methyltransferase skb1"; /id="PRO_0000212346" MLLRDGRIPQYSIYPLPVPPMNSKTPTLGIVCSEGTISLSLEEGFEFVGVPLSGEGLKLRVEALAPSERLQEFLDDEVAYHPEENVHKVVGLSSAWLELDSEDTLIADRSEEVLLKEASYASYCGLSSIILNGPTSPMNVMRYARAVSSALNSTMNLKFLVQLAIESGHEDYFETWKMWDTIRSACGYHPRLKVALELPPACSPPIELVNRWYAEPIEMITMSCMAFVPNPNGYPVLGRKLRAIYALYLRLNPRILLWDNDAPEKIGDSPDYSIYMKHLFDSQPPAPLVEDLADSYKDYLQVPLQPLSYNLENITYEIFERDPVKYAQYEQAIFSALMDRDESSVTRIAVVGAGRGPLVDCALRAAISSSRTVDMIALEKNPNAFSMLLMRNRQDWAGKVTLVFGDMRTWNPDYKIDILVSELLGSMGDNELSPECLDGVQHVLDEETGICIPSSYISYVTPIMSPKLWSEARNMNDPNAFERQYVVLMNSFDFLAADDEFRFQSLWSFHHPNKDSEVYTKNLHNKRFASVRFQASSPGILHGFAGYFEATLYKDISLSIMPATMEAKSPDMFSWFPIYMPIKKPMYVPENSQLEFHMWRLTDGMRVWFEWCANAYLVLRNGSQIKLSSTEVHNISGKAFSCNMY P78965 GSHR_SCHPO ACT_SITE 453; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 37..46; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7; Evidence={ECO:0000269|PubMed:9287302}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11742; Evidence={ECO:0000269|PubMed:9287302}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; SPBC17A3.07; CHAIN 1..464; /note="Glutathione reductase"; /id="PRO_0000067970" DISULFID 46..51; /note="Redox-active"; /evidence="ECO:0000250" MAPISKVFDYLVIGGGSGGLASARRAAKHGAKVALIEASGRLGGTCVNYGCVPKKIMWNIADLVAKMKTAKQNGFPNSQLGSFDWGMIKRKRDAYIGRLNGIYERNVNKDGVAYISGHASFVSPTEVAVDMNDGSGTQVFSAKYILIAVGGHPIWPSHIPGAEYGIDSDGFFELESQPKRVAIVGAGYIAVELAGVFAALGTETHMFIRQSKFLRKFDPIISDGIMDHFQHIGINVHTNSLEFKKVEKLPSGELCIHQQDGSTFNVDTLLWAIGRAPKIQGLRLEKAGVKTLPNGIIIADTYQRTNVPTVLSLGDVCGKLELTPVAIAAGRRLSDRLFGGIKDAHLDYEEVPSVVFAHPEAGTIGLTEQEAIDKYGESQIKVYNTKFNGLNYSMVEQEDKVPTTYKLVCAGPLQKVVGLHLVGDFSAEILQGFGVAIKMGATKSDFDSCVAIHPTSAEELVTLV P78966 MAM1_SCHPO BINDING 469..476; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 1135..1142; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPBC25B2.02c; CHAIN 1..1336; /note="Mating factor M secretion protein mam1"; /id="PRO_0000093369" CARBOHYD 437; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 454; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 536; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 664; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 697; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1011; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1063; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1120; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1235; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1280; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MHIHSDLSLPQFEHASIDPPSYSPQKSSFEEKKHNFSITNKSLETLRSQESPCSTTFPVSDRKDALLNIPTVVDDEFQHTEELAGVSSWSDFFYLFHFSDIPLIFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGKRARSLCFHVLSSKSSTFYSLTESKSGLVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFIKTLCESHDPIEAAKRSAAKIKSISFERGFRFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVLFEDFENNVSIDEKVLKEEADNPFILPNEESLLEKYWINYNESFSQLSRESLFTSLESPFTDIESPTIVSRRKIVEQRKLRMEKESFQETNVDQTFHLFDDKEHACSLTLIFKSIWKVKKLRWFFLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSISAKIWCDHYRLLAVKVLFTQDQAWFDQIENYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATFTLLMASTCIMSLPNVSASRIATSRVLKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHRGEWIE P78968 PPZ_SCHPO ACT_SITE 309; /note="Proton donor"; /evidence="ECO:0000250" BINDING 248; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 250; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 276; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 276; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 308; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 357; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 432; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; MOD_RES 18; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 505; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 514; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A7.08; CHAIN 1..515; /note="Serine/threonine-protein phosphatase PP-Z"; /id="PRO_0000058890" MGQGSSKHADSKLDSYPSFSRSDTQGSIKSLKSLKTVLGKGKDSNHDRRTSTDTTHSRHRYPETPPSLPPPPSPGILATSPAVLQKHQQEDSGNSSQSPTSPHPSNQPAMLSPSTAASQHHHHHSSSSSYAVSPTSPTSPTSSGPIGSNFDSASEHNGPVYPQDQQGPVIIPNSAISSTDPDDPETVVSLNVDEMIQRLIHVGYSRKSSKSVCLKNAEITSICMAVREIFLSQPTLLELTPPVKIVGDVHGQYSDLIRLFEMCGFPPSSNYLFLGDYVDRGKQSLETILLLFLYKIRYPENFFLLRGNHECANITRVYGFYDECKRRCNIKIWKTFINTFNCLPIASVVAGKIFCVHGGLSPSLSHMDDIREIPRPTDVPDYGLLNDLLWSDPADTENDWEDNERGVSFVFNKNVIRQFLAKHDFDLICRAHMVVEDGYEFFNDRTLCTVFSAPNYCGEFDNWGAVMSVNSELLCSFELIKPLDQAAIRRELKKSKRSGMAIYQSPPAEQVTQSV P78972 SLP1_SCHPO SPAC821.08c; STRAND 127..132; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 169..173; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 186..188; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 192..198; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 201..206; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 212..217; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 224..229; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 233..240; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 245..249; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 255..259; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 266..272; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 275..280; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 283..289; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 292..294; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 296..301; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 307..312; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 316..323; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 328..332; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 336..342; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 351..354; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 361..365; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 372..377; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 383..388; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 393..398; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 400..409; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 415..422; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 425..433; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 441..444; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 448..454; /evidence="ECO:0007829|PDB:4AEZ"; STRAND 458..464; /evidence="ECO:0007829|PDB:4AEZ" TURN 207..209; /evidence="ECO:0007829|PDB:4AEZ"; TURN 250..252; /evidence="ECO:0007829|PDB:4AEZ"; TURN 368..370; /evidence="ECO:0007829|PDB:4AEZ"; TURN 378..380; /evidence="ECO:0007829|PDB:4AEZ"; TURN 411..413; /evidence="ECO:0007829|PDB:4AEZ" CHAIN 1..488; /note="WD repeat-containing protein slp1"; /id="PRO_0000051220" MEIAGNSSTISPTFSTPTKKRNLVFPNSPITPLHQQALLGRNGRSSKRCSPKSSFIRNSPKIDVVNTDWSIPLCGSPRNKSRPASRSDRFIPSRPNTANAFVNSISSDVPFDYSESVAEACGFDLNTRVLAFKLDAPEAKKPVDLRTQHNRPQRPVVTPAKRRFNTTPERVLDAPGIIDDYYLNLLDWSNLNVVAVALERNVYVWNADSGSVSALAETDESTYVASVKWSHDGSFLSVGLGNGLVDIYDVESQTKLRTMAGHQARVGCLSWNRHVLSSGSRSGAIHHHDVRIANHQIGTLQGHSSEVCGLAWRSDGLQLASGGNDNVVQIWDARSSIPKFTKTNHNAAVKAVAWCPWQSNLLATGGGTMDKQIHFWNAATGARVNTVDAGSQVTSLIWSPHSKEIMSTHGFPDNNLSIWSYSSSGLTKQVDIPAHDTRVLYSALSPDGRILSTAASDENLKFWRVYDGDHVKRPIPITKTPSSSITIR P79005 TAZ1_SCHPO MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16A10.07c; HELIX 131..161; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 169..176; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 178..194; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 204..209; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 211..217; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 221..233; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 234..237; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 244..256; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 263..280; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 289..294; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 302..308; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 311..315; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 318..329; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 340..355; /evidence="ECO:0007829|PDB:4ZMI"; HELIX 376..389; /evidence="ECO:0007829|PDB:2L3N"; HELIX 410..414; /evidence="ECO:0007829|PDB:4ZMK"; HELIX 427..447; /evidence="ECO:0007829|PDB:4ZMK"; HELIX 451..477; /evidence="ECO:0007829|PDB:4ZMK" TURN 163..165; /evidence="ECO:0007829|PDB:4ZMI"; TURN 418..421; /evidence="ECO:0007829|PDB:4ZMK" CHAIN 1..663; /note="Telomere length regulator taz1"; /id="PRO_0000197124" MISVQSTETIQKVLENEGDQQFDKEVVQNSDSNIETGQISDSLTKAVEERAETESSSNLSNFTTSESESSKPAYCFNSHSQNMAEGSISIPVISHSMNVENEVSTAEGQDSRTGESENDQNAMIVRSIWDIEKASLLVNDCQNIANMAEQKVMMVSAIFSESSKDIVNPESFSERLGKETVKDLYEFNEQLTTKYGLEFRTIFFSYIRKYDAYWCLFEDLEKPLKSIQFFTGLIDLLDNTNKHLTLRSIVLDALLSADEEDSFYGDALVLFEELVIRYFGTDSNPSIDASEFILSCLPYTSLDALNVVCGQVWKSQKICDFLKSTIGNTSNSPLQLRASFPAFVNAVIHFLLEFKNVRRLERKDLSVKGMLYDSDSQQILNRLRERVSGSTAQSADEASGHESDASEDTFSERTLGLNSIDNTEISEVVSLGLVSSALDKITGLLSADNLSETVSQARDFSHTLSKSLKSRAKSLSQKEAANRSKLIAKRGDNLRREASLSSEQDDLSEDFPPVRESDEQESRSGGRSSAMRVSIERSAARSGTRRSQGNPYEGYRTRRKWTDEEENELYEMISQHGCCWSKIIHIQKLENGPLKTFGPTQIKDKARLIKARFMKQNRLQELYSKSLNWKNVTVGQAYCELHKIPYIEATPPLLREELVNYQS P79051 RHP16_SCHPO BINDING 281..288; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPCC330.01c; CHAIN 1..861; /note="ATP-dependent helicase rhp16"; /id="PRO_0000056131" MGTSCNKINSNSNKGKENMHFVLDDNGDSKGNASNQQVERDDKLDMETTRWNGKEFEEPLSTNKKLIIQSNNTSSQHSTPPLSISDTSTHTGSSTDNVEANPNTGFSSARKRSLRSSNLKKKFVPLSSPEESNESEFIDDDESDEVASIIDIKEDETFDSKVEIPEAAPSSSTESDEESIPLSYQSKRRRVSARASSSASSSSRTQAKSIPSHERTHYRLIRQHPELEHVWEKLEEEAPREVKQIEQPKELVLNLLPFQREGVYWLKRQEDSSFGGGILADEMGMGKTIQTIALLLSEPRGKPTLVVAPVVAIMQWKEEIDTHTNKALSTYLYYGQARDISGEELSSYDVVLTSYNVIESVYRKERSGFRRKNGVVKEKSLLHQMEFYRIILDEAHGIKSRTCNTARAVCGLRTTRKICLSGTPLQNRIGELFSLLRFLRADPFAYYYCLQCECKSLHWRFSDRSNCDECGHKPMSHTCYFNAEMLKPIQKFGYEGPGKLAFKKVHSLLKHIMLRRTKLERADDLGLPPRVVEVRKDLFNEEEEDVYQSLYMDSKRKFNTYLAEGVVLNNYANIFQLITRMRQMADHPDLVLASKRKTVDIENQENIVCKICDEVAQDAIESRCHHTFCRLCVTEYINAAGDGENVNCPSCFIPLSIDLSAPALEDFSEEKFKNASILNRIDMNSWRSSTKIEALVEELYLLRKKDRTLKSIVFSQFTSMLDLIHWRLRKAGFNCVKLDGGMTPKARAATIEAFSNDINITIFLVSLKAGGVALNLTEASQVFMMDPWWNGAVQWQAMDRIHRIGQKRPIKVITLCIENSIESKIIELQEKKAQMIHATIDQDEKALNQLSVEDMQFLFSN P79063 ERF1_SCHPO MOD_RES 182; /note="N5-methylglutamine"; /evidence="ECO:0000250"; MOD_RES 425; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1834.01; STRAND 27..29; /evidence="ECO:0007829|PDB:3E20"; STRAND 31..35; /evidence="ECO:0007829|PDB:3E20"; STRAND 91..97; /evidence="ECO:0007829|PDB:3E20"; STRAND 105..111; /evidence="ECO:0007829|PDB:3E20"; STRAND 121..127; /evidence="ECO:0007829|PDB:3E20"; STRAND 315..320; /evidence="ECO:0007829|PDB:3E20"; STRAND 388..391; /evidence="ECO:0007829|PDB:3E20"; STRAND 408..411; /evidence="ECO:0007829|PDB:3E20" HELIX 5..21; /evidence="ECO:0007829|PDB:3E20"; HELIX 42..55; /evidence="ECO:0007829|PDB:3E20"; HELIX 62..79; /evidence="ECO:0007829|PDB:3E20"; HELIX 100..102; /evidence="ECO:0007829|PDB:3E20"; HELIX 133..136; /evidence="ECO:0007829|PDB:3E20"; HELIX 275..292; /evidence="ECO:0007829|PDB:3E20"; HELIX 302..310; /evidence="ECO:0007829|PDB:3E20"; HELIX 373..380; /evidence="ECO:0007829|PDB:3E20"; HELIX 381..384; /evidence="ECO:0007829|PDB:3E20"; HELIX 396..403; /evidence="ECO:0007829|PDB:3E20" TURN 346..348; /evidence="ECO:0007829|PDB:3E20" CHAIN 1..433; /note="Eukaryotic peptide chain release factor subunit 1"; /id="PRO_0000143166" MSETAEKAIEIWKIRRLVKQLINCHGNGTSMITLIIPPGEQISRYSNMLAEEYGTASNIKSRVNRLSVLSAITSTRERLKLYNKVPDNGLVIYCGEVIMEGNKTRKLNIDFEPFKPINTSQYLCDNKFHTEALAELLESDQRFGFIVMDGHQTLYGVVSGSAREVLQRFTVDLPKKHGRGGQSALRFARLRDEKRHNYVRKVAEGAVQHFITDDKPNVAGIVLAGSADFKTELGQSDLFDQRLQSRIIKTVDVSYGGDAGFNQAIELAADTLSNVKYVQEKKLIQRFFDEISLDSGKYCFGVVDTMNALQEGAVETLLCFADLDMIRYEFKNSEGNPVITYMTKEQEEKDSTNSFLLDKDTGAEMELVSSMLLSEWLAEHYKDYGANLEFVSDRSQEGMQFVKGFGGIGAVMRYQLDLSMLDPESDEFYSDSD P79065 TIP1_SCHPO MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 84; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 289; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 294; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 305; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 367; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3C7.12; CHAIN 1..461; /note="Tip elongation protein 1"; /id="PRO_0000083544" MFPLGSVVEVITGERGFVRYAGEVENRKGVYVGLELLPEFAEFGKNRGVVDGREYFKTKNNEKTGIFVPFDKCKLASSISSSPSPKIDGTAASIGMGFPPMSPNLQSSIPRLTNVSSSSNLSMNTISSTALTPTEKILQKRIEDLLYERQNHQQQLEEVLATVDQLQSLVTNFNDQQDEVDELRERITLKEERIQQMRNEASQRRFEFKTTIECLEESSNRAIETYENRIAELEAQLEMYMSGKSEDDLLFSLQQERDYALNQVEILQERVDTLMKQKANSSTANEKLSHMESSSPTLTNASFESPKRGKGSNDLPENHPQRRQTLEFYEIEIEVLREKVEKLQALSDEKDFYISKLEKSLDRNDTTPVPSDEKLSNYAAEKENLVSRISELEHTIEQLTINNERDNERMSPAEFELETTQEVEENDSDSHDDEETWCEVCETNNHSLQECPTVFGSTDEA P79083 EIF3I_SCHPO SPAC4D7.05; CHAIN 1..328; /note="Eukaryotic translation initiation factor 3 subunit I"; /id="PRO_0000051040" MRPIILQGHERPLTQIKYNHDGDLLFSCAKDKVINVWFSHNGERLGTYEGHTGAIWTCDINKSSTLMVSGAADNTMRLWDVKTGKQLYKWEFPTAVKRVEFNEDDTRILAVTEERMGYAGTVTVFRVPISESDAAAETPLYVITTRESKATVAGWSYLSKFLFTGHEDGSVSRYDAITGEFVESKQVHNSGSTITDLQFYPDRTYFITSCKDTTAKAIDVDSFEVIKTYLTDTPLNTSSFTPVQDFVILGGGQEARDVTTTAARQGKFEARFYHAILEEELGRVKGHFGPINTIAVHPKGTGYASGGEDGYVRVHFFDKNYFDFKYTL P87027 SPG1_SCHPO BINDING 17..24; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 65..69; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 122..125; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC1565.06c; CHAIN 1..198; /note="Septum-promoting GTP-binding protein 1"; /id="PRO_0000122465" MADARKNNVTIKVGMIGDSSIGKTSLMVTYVQGSFDEESTQTLGVNFMEKTISIRNTEITFSIWDLGGQREFVNMLPMVCNDAVAILFMFDLSRKSTLNSIKEWYRQARGFNKTAVPILIGTKYDHFMTFPREDQEEITKQARRYAKAMKASLVFCSTSHSINVQKIFKIVLAKVFDLKCTIPEIKNVGDPILEYIDR P87048 RPN1_SCHPO MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP19A11.03c; CHAIN 1..891; /note="26S proteasome regulatory subunit rpn1"; /id="PRO_0000173814" MSSKDISSKSPSGNDALNDKKGTKTSETNDRNSTNNTKERDELEDLSEEDLQLKNDLELLVQAVQDATPELVGSSLTQLKEIIRTSTSSMTAVPKPLKFLRPHYFTLVKIYDSWPQSPQKTQLADILSVLGMSYSNTSKHESLKYRLQGVTTDPSLWGHEYVRHLASEIEEEFASRQEEEAPTDDLMELALTIVPFFLTHNAEADAIDLLQELGAIEKVVPFVELDNASRVCLYITSCVNLLPFPEDVAMLRTAHAIYRKFDQLTQALNVAIRLDDMSLIKEDCEAATDPLLKKQMSYMLARQQIPMDMGDEELNDALNNTHLSDHFHYLGKELNLMDPKVPEDIFKTHLEVARTGLGASGVYSAKQNLANTFVNALVNAGYSNDRLILVDDEKTSWIYKNKESGLISATASIGLLQLWNVDMGLSLLDKYLYSSEENTKAGALLGIGVTNVAVRNEADPAMAILSEYLETGSVKLRASAILGLGLAYSGANREDLLDMLSPIVTDTDCPMQLSCLAALSLGLIFVGTCNGDVASTILQTLMEREESAQNDQWGRFMALGLALLFNGKQDLADATVETLKAIEGKIARQAEILVDICSYAGTGNVLHIQKLLHICSEPPSDDAKESETTIQTFAALGVATIAMGEDIGAEMVLRHFDHMMHYGEPSIRKAIPLALGLLSASNPQMRIFDTLSRYSHDNDLDVAYNAIFAMGLVGAGTSNARLAQLLRQLASYYHKESNALFMVRIAQGLLYLGKGTMTLNPYHTERQILGQTAFAGLMTVVLAMLDANTFVLDTSHWLLYAITLAIRPRMLITLGEDGQYLPVSVRVGQAVDVVGQAGRPKVITGWVTHTTPVLLHHNERAELATEAYTPLTSLEGIVILKKNTEDIEMTA P87050 CDR2_SCHPO ACT_SITE 133; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 16..24; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. {ECO:0000269|PubMed:18257517}. MOD_RES 309; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 311; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 476; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 587; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 632; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A10.02; CHAIN 1..775; /note="Mitosis inducer protein kinase cdr2"; /id="PRO_0000085845" MSTISEVGPWELGLSLGSGGPNSSRLAKHRETGQLAVVKPIVGWSELTSSQQARIEGELVLLRLIEHPNVLQLIDVISAQEQLFVVVEYMPGGELFDCMLRKGSFTEQDTAKFLWQILCGLEYCHKLHICHRDLKPENLYLDAHGSIKIGEFGMASIQQPGKLLQTSCGSPHYASPEIIMGRSYDGCASDIWSCGIIFFALLTGKLPFDDDNIRSLLLKVCQGQFEMPSNISPQAQHLLYRMLDVDSSTRITMEQIREHPFLSCFVHPNISIPIISAPIQPIDPLIVQHLSLVFRCSDDPMPLYEKLASQSPLVEKTLYTLLSRHLHPPSSAAVDRNRAVVDDLLGTAASNGQQMDEEEIEQAINIPTLAPYPISYAAESVPRPATSASPFLTPVTTSGTFNYSFNATNPQSILQRPATTSSAVPQLPKSVTPGLAYPHDSSMLSSNYRPPSALSPRNFNVSINDPEVQLSRRATSLDMSNDFRMNENDPSIVGNLAASNFPTGMGPPRKRVTSRMSEHTGNRVVSFPRGSAFNPRVTRFNVGNEQFSNNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDSLNVPKHRRRQSLFSPSSTKKKLSGSPFQPKRSFLRRLFSSEPSCKCVYASLVASELEHEILEVLRRWQLLGIGIADIIYDSVSASISARIKRQNSLNLKPVRFRISVLAEFFGSQAVFVLESGSSTTFDHLATEFQLIFEDKGFLDNLELSYFQASASRPVSRMSVSSSPFAVFRQRQSVQS P87053 POF1_SCHPO MOD_RES 229; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 232; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A10.05c; CHAIN 1..605; /note="F-box/WD repeat-containing protein pof1"; /id="PRO_0000051136" MTTGYESVPTSEPSDNLAPRAELWQRHLLEKKEGDQSISVSAFNISSMHNELSGLSEKSRQRVEAVWAAFSEASCSERKLALQGILNNCSSSLLSFASSTLDSLVRLDFLSLLPVEISFRILSFLDARSLCQAAQVSKHWKELADDDVIWHRMCEQHINRKCEKCGWGLPLLERNTLYAAKASIQKRYERLTKRGVDQAHESSPVKKAKLDDYPTSSNEETISSVKPPSPNSDSKFFLPFKTRPWKEVYAERCRVECNWRHGRCRQVVLSGHSDGVMCLQLVRNILASGSYDATIRLWNLATFQQVALLEGHSSGVTCLQFDQCKLISGSMDKTIRIWNYRTSECISILHGHTDSVLCLTFDSTLLVSGSADCTVKLWHFSGGKRITLRGHTGPVNSVRIIRDRGLVLSGSDDSTIKIWSLETNTCLHTFSAHIGPVQSLALADSRLFSCSLDGTIKQWDIEKKKCVHTLFGHIEGVWEIAADHLRLISGAHDGVVKVWEACECVHTLKNHSEPVTSVALGDCEVVSGSEDGKIYLWLFNNAPNESPVSTQSVPISSLNGQRSNSSVQRALSSVPNYSSSLSNISTRNLNIPPSNANNDDVSIQS P87058 LAH1_SCHPO MOD_RES 61; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 124; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A10.10c; CHAIN 1..298; /note="La protein homolog"; /id="PRO_0000207607" MSTEEQKEEIKDISSKQENSSEVPKAEEAGKVVESQKDTTSEEKKEETTEKKEDDGKKDLSFDEAEVLKQVEFYFSDTNLPHDKFLWTTSQKNDGWVPIQTIANFKRMRRFQPLEAIVNALRKSPELLEVDEAGEKVRRMIPLVRVDNKSVMERSVYCKGFGDEKDDTQIALEKFFEENAGPISAVRMRRDDDKKFKGSVFVEFKEPDVANKFLEKVKTAPLKWGEDELTIMSKKEYVDMKAELHKNDPPKFSSKRRRFDAFKEMDRQRPGKYSNRGRKFKKQRSSNASEEKPSAASE P87060 POP1_SCHPO SPBC1718.01; CHAIN 1..775; /note="WD repeat-containing protein pop1"; /id="PRO_0000051139" MNEKKKDSLSVLDSNEFFGETTMVSPSIDVSSSPRPNVERFSPCSTKKDLLEGNNIMTRIPEELSRVSLQFDSKGSQQSMIFTNNRCLSDKENLENLQNLLYLHCDLNRPHLSCELPSEHREKCLKRRNSSLSSNLHANKRFLFNSQSDGNKKNETFPSTNYSNVFYPNNCDSKEVASETTFSLDAPNNSVNYSYFSPNLLGNDSKTRQSFPPHSSSSSHNSLHEPVIYDFSSENPSIHPSNHLSSQKNAVLKLAQLISSFEKLPESVRQYLLFHLLSRCGKHAVQNIHKILLPIFQKNFLTGFPAEITNLVLTHLDAPSLCAVSQVSHHWYKLVSSNEELWKSLFLKDGFFWDSIDSKIRTMCLEQSLSACAIMKRVYFRHFNLRERWLHAPEKIKRCSFPIHGVRLITKLQFDDDKIIVSTCSPRINIYDTKTGVLIRSLEEHEGDVWTFEYVGDTLVTGSTDRTVRVWDLRTGECKQVFYGHTSTIRCIKIVQGNQSTTDTDDVEKENRPASNDANSMPPYIISSSRDCTIRLWSLPCLDDPPFVNVNENPDQNNDFTSATTNPFYIRTLRGHTDSVREVACLGDLIVSASYDGTLRVWKASTGVCLHVLRGHVGRVYSVTINPSRQQCISAGTDAKIRIWNLESGELLQTLHGHSNLVSQVTFNQNILVSASAPPDTSLRVWDLNTGSCRDILKCPLGHIFFQHDESKVVSGSHSTLQLWDIRSGKLVRDLLTDLDIIWQVAYNENVCVAAVLRNNRFWIEVLEFGSTKSS P87061 TEA1_SCHPO MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1223.06; CHAIN 1..1147; /note="Tip elongation aberrant protein 1"; /id="PRO_0000119146" MSFLFKRNKGSAHKPTKPNFSKTSTTPSTSQLKHSHESNVKMSTSTVTEHRKKPTGSGSHITASPWSKLTVRGSSNVLPRYSHASHLYAEGGQEIYIFGGVASDSQPKNDLWVLNLATSQFTSLRSLGETPSPRLGHASILIGNAFIVFGGLTNHDVADRQDNSLYLLNTSSLVWQKANASGARPSGRYGHTISCLGSKICLFGGRLLDYYFNDLVCFDLNNLNTSDSRWELASVVNDPPPARAGHVAFTFSDKLYIFGGTDGANFFNDLWCYHPKQSAWSKVETFGVAPNPRAGHAASVVEGILYVFGGRASDGTFLNDLYAFRLSSKHWYKLSDLPFTPSPRSSHTLSCSGLTLVLIGGKQGKGASDSNVYMLDTSRFRLGSVPTTSGRQRNTSFFSNSTGNTNPSAFNGLLTSSRIPSYNGSKVRSTSHPSRQQYIGSSNSRFNTRHQTISTPVSGRASNDLPSPVVPTRSNSSSILQPSYNLNSHSSDRRNTNDDDQSSLNSQQLSNQAKAQGEVSPTLSFVPSSHSMEQGNGSVASANNAQSEAATRSINSISEVSEVRFPEQSSVKTVDERKSLDGRITSVTLETLVEKYSELSKQQIVEWFKSKLYEILRDSASKIDSLTEKLKVANAEKNAALCEAALEKVPLAKHNKLSDGTFSTPDKENVQSTNDAHIMQENFSLHKALEVMRETSSDLDKQLKDATASQKELIVQTSSFQKELVEERERHNAISKRLQEIESLYRDRELLVTNLEDQLVDQTVTINKFAFERDQFRERSMGFENTIKDLTRKMEATDMLNVSLHESLRSVQTENSELVTEMALLKAELVKKQAIIDANANIYDKLTADHTNYETVSADINQNLKETLDKLLNGSSDFKNNEIELLHDQIRITNAKLEKREKLINASKYIEDTLRSEIQEAAEKVSNLEFSNFNLKEENSNMQLQLMKALEQRNTGAKQLVNLRMQLSTATSELDMLKLKLRTTALALEESPDDYSDILSILRADMSPFHDLHKQCGVLIDTLNGVKRGFGIFEKKFTDYHKFLENISDKLKSEEDTSLETPIHENQSIQSDQIKEVGEVLSAIKSLSDSVMLLKNQIDDLAKEKLPLSSSDDEKVNIKEKTDFMKLLVKSGLSNPPAKEPVHDNEN P87074 RHP9_SCHPO PTM: Phosphorylation of Thr-73 and Ser-80 by rad3/ATM promotes interaction with chk1 (PubMed:22792081). Phosphorylation at Thr-187 is dependent on phosphorylation at Thr-215 and Thr-235. Phosphorylation at Thr-215 and Thr-235 may prime the non-canonical Thr-187 site for cdc2/CDK phosphorylation (PubMed:24074952). {ECO:0000305|PubMed:22792081, ECO:0000305|PubMed:24074952}. MOD_RES 73; /note="Phosphothreonine; by ATM"; /evidence="ECO:0000305|PubMed:22792081"; MOD_RES 80; /note="Phosphoserine; by ATM"; /evidence="ECO:0000269|PubMed:22792081"; MOD_RES 187; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:24074952"; MOD_RES 215; /note="Phosphothreonine; by cdc2"; /evidence="ECO:0000269|PubMed:10488332, ECO:0000269|PubMed:16314498, ECO:0000269|PubMed:24074952"; MOD_RES 235; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:24074952" SPBC342.05; STRAND 182..184; /evidence="ECO:0007829|PDB:4BU0"; STRAND 365..369; /evidence="ECO:0007829|PDB:2FHD"; STRAND 372..374; /evidence="ECO:0007829|PDB:2FHD"; STRAND 377..386; /evidence="ECO:0007829|PDB:2FHD"; STRAND 395..400; /evidence="ECO:0007829|PDB:2FHD"; STRAND 405..409; /evidence="ECO:0007829|PDB:2FHD"; STRAND 412..416; /evidence="ECO:0007829|PDB:2FHD"; STRAND 423..426; /evidence="ECO:0007829|PDB:2FHD"; STRAND 434..440; /evidence="ECO:0007829|PDB:2FHD"; STRAND 459..464; /evidence="ECO:0007829|PDB:2FHD"; STRAND 467..472; /evidence="ECO:0007829|PDB:2FHD"; STRAND 476..478; /evidence="ECO:0007829|PDB:2FHD"; STRAND 543..547; /evidence="ECO:0007829|PDB:2VXB"; STRAND 605..610; /evidence="ECO:0007829|PDB:2VXB"; STRAND 652..658; /evidence="ECO:0007829|PDB:2VXB"; STRAND 663..666; /evidence="ECO:0007829|PDB:2VXB"; STRAND 693..696; /evidence="ECO:0007829|PDB:2VXB"; STRAND 730..732; /evidence="ECO:0007829|PDB:2VXB"; STRAND 743..746; /evidence="ECO:0007829|PDB:2VXB"; STRAND 748..750; /evidence="ECO:0007829|PDB:2VXB" HELIX 237..239; /evidence="ECO:0007829|PDB:4BU1"; HELIX 362..364; /evidence="ECO:0007829|PDB:2FHD"; HELIX 449..451; /evidence="ECO:0007829|PDB:2FHD"; HELIX 473..475; /evidence="ECO:0007829|PDB:2FHD"; HELIX 480..483; /evidence="ECO:0007829|PDB:2FHD"; HELIX 558..567; /evidence="ECO:0007829|PDB:2VXB"; HELIX 578..580; /evidence="ECO:0007829|PDB:2VXB"; HELIX 599..603; /evidence="ECO:0007829|PDB:2VXB"; HELIX 618..626; /evidence="ECO:0007829|PDB:2VXB"; HELIX 634..642; /evidence="ECO:0007829|PDB:2VXB"; HELIX 649..651; /evidence="ECO:0007829|PDB:2VXB"; HELIX 678..684; /evidence="ECO:0007829|PDB:2VXB"; HELIX 714..726; /evidence="ECO:0007829|PDB:2VXB"; HELIX 763..772; /evidence="ECO:0007829|PDB:2VXB" TURN 539..542; /evidence="ECO:0007829|PDB:2VXB"; TURN 584..587; /evidence="ECO:0007829|PDB:2VXC"; TURN 659..662; /evidence="ECO:0007829|PDB:2VXB"; TURN 688..691; /evidence="ECO:0007829|PDB:2VXB" CHAIN 1..778; /note="DNA repair protein crb2"; /id="PRO_0000097328" MEVNDTSLHKGFGLDINSQRVFGAQAAISRNNYSKVNASINPSPPRSNDNSNKEFSYSKDVNNNGAVEELSLTQLFEVPSQAAFAKQSSQDISDDELIQHDSRKVISSPYSPKQTHTVLKRLYDRQSVISDHEKLLTPQNVSNSSQILSPFTSLLPSTLSTLKDTPLSVSQNEKNLETVGEVLVPETVAQHRTKFYDYTLDEMENETESGQVETTPTRLATSLGSPVLYGRVESTPPAFLPETSEKQYKRKFSFTEPSSEKVDNTETKFSKKTKNINDENFPNPFNVISSYETSASPSTVIDQSSQVSSIFVNKRLRKSVNNQAISRSDSLSLDTPKIDSLFTRASIKPLKPSQSPNSRRSFKNRVLAFFKGYPSFYYPATLVAPVHSAVTSSIMYKVQFDDATMSTVNSNQIKRFFLKKGDVVQSTRLGKIKHTVVKTFRSTNEQLSLIAVDALNNDMVILAHGEIEVTVPISTIYVAPVNIRRFQGRDLSFSTLKDMKFEETSFLPSHDSQRNRSSLKERDSSFVKKNLDSESNQLIFDDCVFAFSGPVHEDAYDRSALETVVQDHGGLVLDTGLRPLFNDPFKSKQKKLRHLKPQKRSKSWNQAFVVSDTFSRKVKYLEALAFNIPCVHPQFIKQCLKMNRVVDFSPYLLASGYSHRLDCTLSQRIEPFDTTDSLYDRLLARKGPLFGKKILFIIPEAKSWQKKIENTEQGQKALAHVYHALALGADVEIRPNVAHLECDLILTMDGNIVDETNCPVVDPEWIVECLISQSDIST P87115 NAT10_SCHPO BINDING 285..294; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03211"; BINDING 465; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03211"; BINDING 626..628; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000255|HAMAP-Rule:MF_03211"; BINDING 633..639; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000255|HAMAP-Rule:MF_03211"; BINDING 727; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000255|HAMAP-Rule:MF_03211" CATALYTIC ACTIVITY: Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate; Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA-COMP:13576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:25402480}; CATALYTIC ACTIVITY: Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-acetylcytidine in tRNA + CoA + H(+) + phosphate; Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:13671, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_03211}; SPAC20G8.09c; CHAIN 1..1033; /note="RNA cytidine acetyltransferase"; /id="PRO_0000215889" MPKKALDSRIPTLIKNGCQEKQRSFFVVVGDRARDQVVNLHWLLSQSKVAARPNVLWMYKKDLLGFTSHRKKRENKIKKEIKRGIRDPNSEDPFELFCSITNIRYCYYKESEKILGQTYGMLVLQDFEALTPNLLARTIETVEGGGIVVLLLHKLNSLKQLYTMSMDIHSRYRTEAHSDVTARFNERFILSLGNCENCLVIDDELNVLPISGGKNVKALPPTLEEDNSTQNSIKELQESLGEDHPAGALVGVTKTLDQARAVLTFVESIVEKSLKGTVSLTAGRGRGKSAALGLAIAAAIAHGYSNIFITSPSPENLKTLFEFIFKGFDALNYEEHVDYDIIQSTNPAYHNAIVRVNIFRDHRQTIQYISPEDSNVLGQAELVVIDEAAAIPLPLVRKLIGPYLVFMASTINGYEGTGRSLSLKLLQQLREQSRIYSGSGNNKSDSQSHISGRTLKEISLDEPIRYAMGDRIELWLNKLLCLDAASYVSRMATQGFPHPSECSLYRVSRDTLFSYHPISEAFLQRMMSLYVASHYKNSPNDLQLMSDAPAHQLFVLLPPVDLKNPKLPDPICVIQLALEGSISRESIMNSLSRGQRAGGDLIPWLISQQFQDENFAALGGARIVRIAVSPEHVKMGYGTRAMQLLHEYFEGKFISASEEFKAVKHSLKRIGDEEIENTALQTEKIHVRDAKTMPPLLLKLSELQPEPLHYVGVSYGLTPSLQKFWKREGYCPLYLRQTANDLTGEHTCVMLRVLEGRDSEWLGAFAQNFYRRFLSLLGYQFREFAAITALSVLDACNNGTKYVVNSTSKLTNEEINNVFESYDLKRLESYSNNLLDYHVIVDLLPKLAHLYFSGKFPDSVKLSPVQQSVLLALGLQYKTIDTLEKEFNLPSNQLLAMLVKLSKKIMKCIDEIETKDIEEELGSNKKTESSNSKLPEFTPLQQSLEEELQEGADEAMLALREKQRELINAIDLEKYAIRGNEEDWKAAENQIQKTNGKGARVVSIKGEKRKNNSLDASDKKTKEKPSSKKKFRK P87117 BECN1_SCHPO SPAC20G8.10c; CHAIN 1..464; /note="Vacuolar protein sorting-associated protein atg6"; /id="PRO_0000218560" MQYLCQRCHSLINFKDVYDDDLLKLKNLPKSRFVQASSLTEMNESGESDDQMNSSSEDYPAQRLQLYKKTISEGDYNFDNVPPPELRTPTLDSFVVLPAAKDGYEEEKNSPEEVNDLFSWKIEIYNRIFDLLSSKTKVDHPLCVECAELLTEEMSKTLRALKEEKKMYFNYDNFLSSQTVHEENTAALDSEIDELMKQINEKEEKIEEISDETDKLQKLLRELDEEKEKVYAEEQEFYNNLNQFQIKKLSLERQYDCANLEFEHNSRKLEKLQKMNVFSDIFYISHYSEPNGEGSIATINGLRLGRLPSQKVNWAEINAAWGMTVLLLDVLTEKLDFHSSSYQLKPFGSQSFIIRFDRDPNGNQVKPTKLDLFSSGELKIFMNRRFDQGMVAFLDYLHQFGDFCAAKTPSAVLPYAIENDRIGGKCIRLAFNQDENWTRALKFVLTDIKFLEAYVSSQDKQSNF P87126 CWC2_SCHPO SPAC3A12.11c; CHAIN 1..388; /note="Pre-mRNA-splicing factor cwf2"; /id="PRO_0000081549" MSENGLEQEVTVEEKNNDVTEKILVEGEKSKEYEETPRKVKIVKRKKQPARKQIETRPEYEMEPEQPGQVYNLWYNKWSGGMRQDPLKSQVKSETRCVISRDSGYTKADKNPGSFFCLYFARGMCSEGSKCEYLHRLPKDTDFFNANVDCFGREKHADYRDDMGGVGSFLRQNYTLYVGGITPTDDIEEIVSRHFAEWGDIERIRVLNSRGIAFITYLNEANAQFAKEAMAHQSLDHDECLNVRWATTDPNPASQARNQRRLEERAANAVKKLLPKQFLLDLEETKNGKSGNRKRKLELEFGLKGYVPSDDLLYADGANSVHNQLAANEFPNKSQSEEGSNDDHKSVTTTESQNKFVNSQILSDLQVAKQAVHTNQSALVSYYDSDED P87141 MIP1_SCHPO MOD_RES 834; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 837; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000305|PubMed:18076573"; MOD_RES 882; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573" SPAC57A7.11; CHAIN 1..1313; /note="Target of rapamycin complex 1 subunit mip1"; /id="PRO_0000051078" MNDRISEVSGSSRARRSVLSYGTTETGSDRYTENSNIATENGVDTASSMIDGIQSGFPQPRHGFEEEYNNAEYINMLEQVFYMYYTDKRHRGVISKKNAEPTETIHDWRMRERLKTVSAALLVCLNIGVDPPDVIKPNPAAKYECWIDPFSLPASKALEAIGKNLQQQYETLSMRTRYRHYLDPAIEEVKKLCIGQRRNAKEERILFHYNGHGVPMPTASGEIWVFNKNYTQYIPVSLYDLQSWLGAPCIYVYDCSAAGNIIVNFNRFAEQRDKEALRIAKQNPNVLAMPSHTSCIQLAACGPKETLPMNPDLPADLFTSCLTSPIEISVRWYVLQNPFPNKLNLNMLLKIPGRLQDRRTPLGELNWIFTAITDTIAWNVFPKHLFRRLFRQDLMVAALFRNFLLAERIMLVHSCHPQSSPELPPTHDHPMWNSWDLAIDNCLSQLPDMLDAESKGIAYEYKHSTFFSEQLTAFEVWLSQGLISRKPPDQLPLVLQVLLSQVHRLRALILLSKFLDLGVWAVDLALSIGIFPYVLKLLQSPAIELKPVLVFIWARILAVDDSCQADLLKDNGYGYFVQILNPNSSIFPSSNISEHRAMCAFILSVFCRGFPQGQLACLNPQVLSHCLSHLNSPDSLLRQWACLCISQLWENYSEAKWSGTRDNAHVKLAEIIVDSVPEVRASVLTAFTTFLGFPEKTEEVVAVETYIAIAALAALSDASPLVRHELVIFLSHFVVNYKKQLMVVAYESSLADILEKKNHNSISASTIYETVWQAVLVLAADPSIEISLAAEAIINYVYQSMLNSELRESFLAFLLQHLPALHKASLSKDTDTNSVTSDPKPHPFVPSVSENKILNRSFSLTRSLKGLALSLAGSDRASELLSLNGENKPAESNLNHLTSAKVPGPPAFNELEYQSELDMPLTSYLFDWSRKYFTEPQMRPNEDDEPGSICYNQRLWRRNRNEKLIYRTRPLAEYSTNGRWNQQLMTFNNTIAPRKLMFHQFEDQLITLGDKDIIQVWDWRRNRCLNSFKTSASATTNVTDMQLLNEDDVALLMTGSSDGTIKLYRDYENEKVELVTSWNSLSDLVFGDRNASLLMSWQQNCGHLLVAGDVRVIRIWDASKEICYANLPVRSSNSITSLTSDLVGCNIIVAGFSDGVLRVYDKRLPARDSLTDVWKEHSSEIVNVEMQSSGMRELISASSDGEVKLWDIRMNHSLQTFSTDNSGLTSLTVHSHAPVYATGSSNQSIKIWDTLGQNINTFRENPRFLNQPKPSSLMCLKFHPHHLLLACGDNTDSRVNLYSCTKNEIHTDSPNEF P87154 DPOE_SCHPO BINDING 2069; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2072; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2104; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2107; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2138; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2141; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2153; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436"; BINDING 2155; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P15436" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P15436}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P15436}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436}; SPBC25H2.13c; CHAIN 1..2199; /note="DNA polymerase epsilon catalytic subunit A"; /id="PRO_0000046464" MPLKTARGASKYQFRKFNGNYNGKSKSNGRTFAKSTEEVGFNDPMKIVYKKNEIDRMMGFDSYEGGQPREAWLLNVHPTVIESTKGNSTLSAVDFYFIQDDGDTFRCTIPYSPYFYIAAREGKEALVDDYLKKKFVGLIKSTTRIFKEDLQLKNHIVGYQKLYIKLVFDNLNDLQAVRKSLMSAVKANSSQQDAVDAYTNLSSENLNGIIENAFEDPLNHVLDIREYDVPYHSRTLIDLNIRVGQWYTVSYHEGHVQISLLASRIERAEPTIMAFDIETTKLPLKFPDSSFDKIMMISYMIDGQGFLITNREIISQNIEDFHYTPREEFEGPFIIFNEPDEVGLLHRFFKHIRSAKPSVIVTYNGDFFDWPFVDARAAFHGLNLTEETGFFRDAEDEYKSSYCSHMDAFRWVKRDSYLPQGSQGLKAVTVSKLGYNPIELDPELMTPYASEKPQVLAQYSVSDAVATYFLYMKYVHPFIFSLCNIIPLNPDEVLRKGTGTLCETLLTVEACTKNIILPNKHVDASQKFFDGHLLASETYVGGHVESLESGVFRSDLPTNFNMDPKVYEELILQLDKALDFSLTVENNVNVDEIENYEEVRDSILKKLSDLRDRPKRSEKPRIYHLDVASMYPNIMITNRLQPDSVKDESFCATCDLNVPNKTCDRRMVWAWRGEYYPAKKGEYHMIYSALQSERFPGPTPFSPFRSFQELSPSEQAAMVQKRIADYSRKVYHRLYDNTVIERETIICQKENSFYIDTVKSFRDRRYDFKGLQKKWVKQLAAIKEKGGLAEIEEAKKMVVLYDSLQLAHKVILNSFYGYVMRKGSRWYSIEMAGITCLTGATIIQMARQIVERAGRPLELDTDGIWCILPESFPENFEFKKKSGGKVFISYPCVMLNHLVHEKFTNHQYSALKDPEKLVYETTSENSIFFEVDGPYRAMILPASTEEGKNLKKRYAVFNFDGSLAELKGFEVKRRGELKLIKDFQSQIFKVFLKGDSLEECYQEVAYVADTWLEILFTKGSNLTDDELIELISENRSMSKALSEYGSQKSTSITTARRLADFLGDQMTKDKGLACRFIISASPKGRPVAERAVPVAIFFAEESVKRHFLRLWLKDNGLYDVDIRDIIDWDYYLKRLGSVVQKLISIPAALQRISNPVTRFPLPDWLQKRVAVLNSKYQQKKIDSIFSLAPTNPSTINNTKVTDIEDLGSVTHKDKRIVARVTKRKLLQQSGNSEAPVSFEVKPVSFMDGYSNWLKYAKKKWKYQKQVKLRRRHLIGFQSRQFTNVLQSSAEVMFENLWHILQIRETDVPGILHAWVIIRNRLTSIRFIVNRKFFVCFKDETLPNVEIEGCLIEKSNAILPHGSTSDKLFLLEIPEKSYLTEKVSISMIFAHPSVSGIYETRIEPIERLILEMGSRKRFNNSVPGALGKGFEFGFESKMFTDPSDNDVSYLDGVEMNYLYAFHFSISNRFVFSLFMPHLKKVEAIIYDKLPGSDMSFPSISKIYEELRSKFDNLIKESSIEYPDTLSCNVIFSGNERKAYKLIDEKLLQYFSTKTKNSLLIIESSLPHILKANVKQIEELPYIMIPRLESNIQSLSWKQHIATKMIQHFLAIGSWLFHRIQLSRFSDIPLCNFESDDIQYSIDVVYSRKLKEHNIILWWNKGPTPDLGGIEKDSILQIASPKDPLEVNNPGAYSNACVDISLSNLALCSILNSALINDIEGIGDMAALNDNYMTAINDDLEEKLGIHDNIGLTHSLPVLKALVKTWWNEAASGNNLADLIIQHLARWISSSKSYLYSPLLSSHVEVIMRKTFLQLLSEIKRLGAHIIHASANKILIKTSKLIVQNAVTYSNYLLKSIKTLPLFHFLDLNVTEYWDYLLWMDSVNYGGKMVAANFSATNEEPQTVVSWHIKSHLPPIIQPEFQSWIVEFIEEVYKQKLEKSNTKVGFVRVKNNNADEDSEIVGSGILKSKLIHPLKRKVAQVRRCFQELQLDENTREDLKFPKLPGSFLNYTDGALELVKSICAVFELSHDLNLEVRFLKKSLLSLLQIQEFSTQAVFRYPSRRLSLDQIPCKQCGVHQDFDLCLHEHLWPTRDDMGTLVFSDGWSCSSCNLVYDRWVFEETLVDNLYHQLTLYQLQDLICSKCKTVKQWSLKERCSCSGEWVLQLSPTKFREMLNVYQSVADFYEFSILQNSVQSILSVLN P87174 DPB4_SCHPO SPBC3D6.09; STRAND 69..71; /evidence="ECO:0007829|PDB:5Y27" HELIX 10..15; /evidence="ECO:0007829|PDB:5Y27"; HELIX 19..28; /evidence="ECO:0007829|PDB:5Y27"; HELIX 38..65; /evidence="ECO:0007829|PDB:5Y27"; HELIX 73..82; /evidence="ECO:0007829|PDB:5Y27"; HELIX 86..88; /evidence="ECO:0007829|PDB:5Y27"; HELIX 89..105; /evidence="ECO:0007829|PDB:5Y27" CHAIN 1..210; /note="DNA polymerase epsilon subunit D"; /id="PRO_0000191752" MNQDKSKETSELDDLALPRSIIMRLVKGVLPEKSLVQKEALKAMINSATLFVSFLTSASGEIATNNNRKILMPQDVLNALDEIEYPEFSKTLKKHLEAYELALKEKRLKLPNVSDVDNRKKAKIDAHDTTPLDEEKDELEEERIAEDIAQNEVEQNIDDVEDLEEVNDTLDANAESPQIETIHLTDATGNPIEDSSESDSEESLQLNDSS P87175 APN2_SCHPO ACT_SITE 151; /evidence="ECO:0000250"; ACT_SITE 191; /note="Proton donor/acceptor"; /evidence="ECO:0000250" BINDING 42; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 191; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 193; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 294; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 458; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"; BINDING 461; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"; BINDING 484; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"; BINDING 508; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01343" CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000269|PubMed:14704348}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250}; SPBC3D6.10; CHAIN 1..523; /note="DNA-(apurinic or apyrimidinic site) endonuclease 2"; /id="PRO_0000200019" MRILSWNVNGIQNPFNYFPWNKKNSYKEIFQELQADVICVQELKMQKDSFPQQYAVVEGFDSYFTFPKIRKGYSGVGFYVKKDVAIPVKAEEGITGILPVRGQKYSYSEAPEHEKIGFFPKDIDRKTANWIDSEGRCILLDFQMFILIGVYCPVNSGENRLEYRRAFYKALRERIERLIKEGNRKIILVGDVNILCNPIDTADQKDIIRESLIPSIMESRQWIRDLLLPSRLGLLLDIGRIQHPTRKGMFTCWNTRLNTRPTNYGTRIDYTLATPDLLPWVQDADIMAEVMGSDHCPVYLDLKEEYEGKKLSNFLSHSKEPPLLSTAHHSAYRPSKNIHSMFQHFNSMKKNKNNSPTQSENVSASASSGSSPTVSRANSVIDVDAYPPEKRRRKEQSKLLSFFAKQKEEKEETNKTEDVSIEVLDNNNESDIGLTVKKKVENGNAWKQIFSERAPPLCEGHKEPCKYLTVRKPGINYGRKFWICARPVGELIKNSNAVSEEDTQPFQCRFFIWDSDWRANSKD P87176 SLX8_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; SPBC3D6.11c; CHAIN 1..269; /note="E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8"; /id="PRO_0000056331" MPPAHKRDTNVRNLSAPYNIPSQSARVAAGNAAINRRRSSPVENSPGNGFPVSEDATDYPSGTTSENESLPLNRAPRSLREVASELAQEETLPVETSDLNIDVESEVFDLEDINFQNDADDINQRFTYNNHPASVENSLTNVNSIHAQPTTISDMIDLTDETSYDPRKQKFEQGKNPSTTNAEIEKEEPSKKQVVPSSQRLADYKCVICLDSPENLSCTPCGHIFCNFCILSALGTTAATQKCPVCRRKVHPNKVICLEMMLGSQKKKS P87227 CENPI_SCHPO SPAC1687.20c; CHAIN 1..672; /note="Inner kinetochore subunit mis6"; /id="PRO_0000096493" MESFENKGFLDIEEGIQWIKKNSENLSSSKKTILARLQQFHKLCSEVGLNQHSISSLLDVILSKKTHFDKNHVQLLIKCLYPNELISQTIAIRIISSLDPHGLRCSYAIQAKLLNWLIHVYEFLDGNNLLCRYYGVLFHFLDFLTLRPYISNLLVLLTKHYHVKSFRIHQLLALYQKPGNTADPYLLALILTYKQHFPDVIVGSYTYRKHGSVRLDSEWIAATKAILNRQSEDVPLETWSSEKRKRQSSLIPDLITMKNTSSSYSLEELTSVQQMGLVYEKIVFPSRIAAVLKSKLFLIFLFLKNKNVYYSRLDEWLHITLNYGLALRSGSNNQEEEVLHLLYKYLLFSPKFPKSLLQYVITFFSKPNITEENYNLLTLLVTHIPITTDSSYFNSLLKEFEQFILQKNAEFCSKHLNILWLWLFRMLNLRIASMGNNHTLLEKCLLITNHATFLVSHFSWDVSLAYQLSRLFQLYYKILTKIRKQIEPNIPPKELIYVLFFQPSAFYINSMVGLLLLTKNYQERLMDSRIDAISKFTHSYLKSLSEIILLKEKRAILSFLQLWEPFKSDYSQFLPIATRIANDHPYAQRVFSLTCAPQFFSYINGYQIYLQQTNPATGSIPLKPIQEETFGAFQSNLHLSDSWEDFQKNFIIYLKKKGYLAISDFLLSTLNR P87231 MUS81_SCHPO COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11719193}; PTM: Phosphorylated in a cds1-dependent manner in response to hydroxyurea (HU) treatment. This phosphorylation promotes dissociation of mus81 from chromatin which may prevent cleavage of intact stalled replication forks. {ECO:0000269|PubMed:11073977, ECO:0000269|PubMed:15805465}. SPCC4G3.05c; CHAIN 1..608; /note="Crossover junction endonuclease mus81"; /id="PRO_0000198860" MDCGNPLFLQWIQEWMEESTRRFPKSYQTWRKAYDSMKSCPITFHRPSQALALKGIGPTICAKLEKKWNAYCLENNIPISTHNEQNDSHVNANKSSSETSSEKPRSVKKPTTRKRKVYVPSYRSGAYSILCALYMLNKHEFATKPQIVTMAQPYCDSSFGSATDRNMRYTAWSAMKTLITKNLVYQTGHPSKYCLTDDGEEVCIRLAKVDDSFQRKHTVSNFSVSKSDDHDSSLCQPPNFVTSINKAGSSSDHGGELHVTYCPVDHNEVSDGVETDIDVDQVDSLTGIHDHHIINNEQLIDLTEQEKKQPNESNLSNLKIETVLFSNCTVFLLIDTREIRSPLDRNLIIDKLTNDFGVNCQVRSLELGDALWVARDMESGQEVVLDFVVERKRYDDLVASIKDGRFHEQKARLKKSGIRSVTYILEESSYDESFTESIRTAVSNTQVDQLFHVRHTRSLEHSVSLLAEMTKQINLFYEKRKTLAVIPDLSIEAKTYESLREQLLKIDPSTPYHISYHAFSSVLSKSSTLTVGDIFIRMLMTIKGISASKAIEIQKKYPTFMHLFEAYEKSSSSQERNLLLNKTCQGYGFQTIGPALSAKVASVFFPES P87245 KMS1_SCHPO SPAC3A11.05c; CHAIN 1..607; /note="Karyogamy meiotic segregation protein 1"; /id="PRO_0000084310" MLNERDFDLIFDSYDFKHEGKVHLSNFLPIINDLQLLHPASAPPLLSEFQKQCTLEFVRQNADLSITKDNFRDVYKKLTENEDDSFANQAEKPSMEQQNSKNSIKEDANEHSVNSAHSKSSSNASPESLNPSQMMSKRLSLPPMSQFTDSDFVNILRTPFAQSTPLNRNTSSRNTEMPLVRKDKPDFSNGHHDLIKQITELQDMLDKARDQARKKSRTVDILEGKVNELTHQLNMADSKYNESKVANNSQNNQIKTLKAQNLNIHKNFQKIQSELIQTNSGLYSTKKELSALQVRYATLLRKFTDQTKKIEELSLAASRSSENENTIRRLALENHELKNSNNQLNNHIDDLTREKHLIALSNNPKGDEFLSPSNLDEMVYSKEVGLSFTQPSVCISIPAVGMRESEELRELEFKCKQQKKTIEECKHISQSLQSSLTAESSRNKELVAGFLMLSEEIGIQKWIIQSLSKMSPTLNDFCRRYDSSMPTYEESSHECTVLSSFSDDETGLMATNTTMNNSSKDFMASQDTVNADNPHFLATKGQPLLLLSVMKSNILRLFYVLFLFACFYGLDYILCAELLQAFLRVVFTFCEHIIILLYGRYELVQPS P87297 DAD1_SCHPO SPAC16A10.05c; CHAIN 1..90; /note="DASH complex subunit dad1"; /id="PRO_0000127611" MSSENMDITENIQNEQNKDFDDIDFERRRRLLTLQISKSMNEVVNLMSALNKNLESINGVGKEFENVASLWKEFQNSVLQKKDREMLDAP P87314 HIR1_SCHPO SPBC31F10.13c; STRAND 477..479; /evidence="ECO:0007829|PDB:2Z34"; STRAND 485..487; /evidence="ECO:0007829|PDB:2Z34"; STRAND 490..493; /evidence="ECO:0007829|PDB:2Z34" CHAIN 1..932; /note="Protein hir1"; /id="PRO_0000051023" MKIKKIPWLGHFDDRGHRLSIFSIHIHPDGSRIATGGLDGTIRIWSTEAINRENENENENEDLPKQLCCMSTHTGTVTSVRFSPNGQYLASGSDDRVVIIWHKEEAIPGLGSTFGSGEKHTENWRSYRRLLGHDNDIQDLCWSYDSQLVVSVGLDSSIIVWNGTTFERLKRIEAHQSHVKGITFDPAGKYFATESDDRTIKVWRVSDFSIEKTITGPFNNSPLSTYFRRPSWSPDGKHIAAPNAMNGPVSCVSIIERGTWTSEINLIGHEGPVEVTAFNPKLFRDKNDKLVCILACGGQDRSLSIWSSALPRPLLSCQNVFQKSIGDVCWSPDGLSLFLCSYDGNVLVCTFEKEEFGDMVSDEEISKALAKYGHGRHGIVLPESAKQLELEETAYAILKKPSSLSTTDPTLVPQSSSTPKSAQKTPQKLPAFLPNRLTAETVDTNKLTASKEQIASPKRPGPSDNGNEIPTKFVQKVTITKEGKKRVAPQLLTTLSATPSTSRLASTQLQHTGSSQLPPQQFSQPINSLPKGGVPILIVGNKTKVNHENDESDQALQEEKIEEGLLKNYYSSLIDSSTSISNINFEAPRYKTNIVHSLNNEQKYVLEVKNGTSEKNPTRIVALENGNTKWMDYLPRPVILVTGSIHFWSIACDDGSLHLYSLTGSRLLPPIMIESKASFLHCNNAYLLCISSSGMVYAWNVVNKTALFTANSLAPILSRVSNNVTIENNSTDIPHVVIASISKEGVPSVTLSTGETYVYSSTMLCWQRITEPWWAIGSREWDSSGLLQSNTQTESQPLKIYEHRTNNVLMDSGRGKLLQKMVADAITEEGYDDFETIVTINHLENKIASARLLKLDDEFLVTSEVYVRLLMHHGLWQKLEEFLGELRTQTKCSIKLSGREVVAKMLVVLRQAVQTDNEFDRANKLIEKYAST P87320 MSP1_SCHPO BINDING 273; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 274; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 275; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 276; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 277; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 277; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:O60313"; BINDING 278; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 292; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:O60313"; BINDING 297; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:O60313"; BINDING 370; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:O60313"; BINDING 439; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 441; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266"; BINDING 468; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32266" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000305|PubMed:27664110}; TRANSIT 1..78; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of msp1 (l-msp1) (By similarity). Further processing by a rhomboid protease after the transmembrane regions produces a short peripheral membrane form of msp1 (s-msp1) (By similarity). Both isoforms are required for full activity (By similarity). {ECO:0000250|UniProtKB:P32266}. SPBC1718.06; CHAIN 79..903; /note="Dynamin-like GTPase msp1, long form"; /evidence="ECO:0000305|PubMed:19567474"; /id="PRO_0000007402"; CHAIN ?..903; /note="Dynamin-like GTPase msp1, small form"; /evidence="ECO:0000305|PubMed:19567474"; /id="PRO_0000460454" DISULFID 802..811; /evidence="ECO:0000250|UniProtKB:P32266" MGISWFLSRFRIRTVAPSSFLKPRGLVYRPSQIRRRVSLLSLSGFHPYRAYSILGPKTPTAFNSANTVRFFSFSSISRLVFRSLRLPVAGFSLVAGGAAYIGAQVQRASDYTKDIFDKTFGILDSTWEKTRETVASVTNVQLPEISMPLWLEKILRLDEESAERRRVLQAERAKEHRSNSNDKQKSSDNDEDPNDTTVGIGAALAASILSVDSVDGEDTLTADEKRKLAQESKEDRMMLFTKKMIEIRNILQDIQDNNSAVTLPSIVVIGSQSSGKSSVLEAIVGHEFLPKGSNMVTRRPIELTLVHSADTAIPYGEFSGVQLGKITDFSKIQHILTDLNMAVPSSQGVDDNPIRLTIYASHIPNLSLIDLPGYIQIHSEDQPADLDMKISKLCEKYIREPNIILAVCAADVDLANSAALRASRRVDPLGLRTIGVVTKMDLVPPSKAISILHNNNYPLHYGYIGVISRIVPTGRFSAGQNLTDLVSTQENSYFSTHQQFADARIGNYLGIQSLRKCLINVLEYTMSKNLQHTADSIRTELEECNYQYKVQYNDRVLTADSYIAEGLDIFKAAFKEFTQKFGKSEVRDLLKSSLNEKVMDLLAERYWTDDDISNWSKHTNALDEHWKYKLDSCVSTLTRMGLGRVSTLLVTDSISKCIDEITKASPFADHPAAMQYIMNAAQDILRRRFHATSEQVENCVKPYKYDVEVNDDEWKSSRGQAEKLLQRELGLCQSALEKIKNAVGSRRMNQVLQYLEEQKTSSEPLPASYSTALLEQGRMLQYLKMREDILKLRISVLKSRACKHKEAKYTCPEIFLNAVSDKLVNTAVLFINIELLSEFYYQFPRELDQRLIHSLSSEQLNAFVNENPRLKSQLQLQHKRQCLELALQKINSLVILEQQADSD P87324 DPOD2_SCHPO CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; SPAC27E2.05; CHAIN 1..462; /note="DNA polymerase subunit delta-2"; /id="PRO_0000096173" MVEVRHSIPCEETKRLELSLSQQTYSQQYASIYFARLTALRPRITEAASKKWPDKQRLERVLDVKSDEDCWVVATAYMTTALKPNVMNDVTQLHTIVTTTEESPYVSPEDAASGDIEYALEDDYGRIDCSGSFLYDAGVVTGVVLAVLGHEDEQGRFVVVDVCFPGIFSHSIPMTTDESQAQPEYIAAVSGLGLSNDGIEGIQVHQLVDFLRGTLPHVSSFSPSSIKRLIILGNCLAPSIEIADSASASVPIGKKKVKRYGYDTSAYNPNPTFQLDNFLDQVCSSIDVTLMPGPYDYSSTILPQQPLHPALLTKSKVWLGSSLQTVTNPTWLSLGNHFVLATSGQNINDLRKYHPKKSSLQCMENTLLWNHITPTSPDTLWCYPFTDKDTFVMEEMPDLYLCGNQPKFGCKTVINEGNRIQLVSVPEFRKTGVLVLINMHTLNVEIIQFRPMSVKAETPITS Q00619 MAM2_SCHPO SPAC11H11.04; CHAIN 1..348; /note="Pheromone P-factor receptor"; /id="PRO_0000195074" MRQPWWKDFTIPDASAIIHQNITIVSIVGEIEVPVSTIDAYERDRLLTGMTLSAQLALGVLTILMVCLLSSSEKRKHPVFVFNSASIVAMCLRAILNIVTICSNSYSILVNYGFILNMVHMYVHVFNILILLLAPVIIFTAEMSMMIQVRIICAHDRKTQRIMTVISACLTVLVLAFWITNMCQQIQYLLWLTPLSSKTIVGYSWPYFIAKILFAFSIIFHSGVFSYKLFRAILIRKKIGQFPFGPMQCILVISCQCLIVPATFTIIDSFIHTYDGFSSMTQCLLIISLPLSSLWASSTALKLQSMKTSSAQGETTEVSIRVDRTFDIKHTPSDDYSISDESETKKWT Q01112 CDC42_SCHPO BINDING 10..17; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 57..61; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 115..118; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 189; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC110.03; PROPEP 190..192; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281284" CHAIN 1..189; /note="Cell division control protein 42 homolog"; /id="PRO_0000198954" LIPID 189; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MPTIKCVVVGDGAVGKTCLLISYTTNKFPSDYVPTVFDNYAVTVMIGDEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVTSPASFENVKEKWFPEVHHHCPGVPCLIVGTQIDLRDDPSVQQKLARQHQHPLTHEQGERLARELGAVKYVECSALTQKGLKNVFDEAIVAALDPPVPHKKKSKCLVL Q01475 SAR1_SCHPO BINDING 27..34; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 70..73; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 129..132; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; MOD_RES 138; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC31F10.06c; CHAIN 1..190; /note="Small COPII coat GTPase sar1"; /id="PRO_0000206273" MFIINWFYDALAMLGLVNKHAKMLFLGLDNAGKTTLLHMLKNDRLAVMQPTLHPTSEELAIGNVRFTTFDLGGHQQARRLWRDYFPEVNGIVYLVDCCDFERLSESKAELDALLAMEELARVPFLILGNKIDAPGAISEDELKAALGLYQTTGKGVSKPVPGIRPIEVFMCSVVLRQGYGEGFKWLAQYV Q01663 AP1_SCHPO PTM: Depending on the oxidative stress inducing agent, pap1 can undergo two distinct conformational changes, both masking the nuclear export signal, thus abolishing nuclear export by crm1/exportin 1. The glutathione-depleting agent diethylmaleate (DEM) leads to the non-reversible modification of at least 2 cysteine residues in the c-CRD. Peroxide stress induces the formation of a tpx1-dependent interdomain disulfide bond between Cys-278 and Cys-501. {ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244, ECO:0000269|PubMed:15824112}. SPAC1783.07c; HELIX 80..125; /evidence="ECO:0007829|PDB:1GD2"; HELIX 128..138; /evidence="ECO:0007829|PDB:1GD2" CHAIN 1..552; /note="AP-1-like transcription factor"; /id="PRO_0000076532" DISULFID 278..501; /note="In nuclear retained form"; /evidence="ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244"; DISULFID 285..532; /note="In nuclear retained form"; /evidence="ECO:0000250|UniProtKB:P19880" MSGQTETLSSTSNIPIAKAEPEQSADFSASHKKRGPVSDRSSRRTSSEEVDLMPNVDDEVDGDVKPKKIGRKNSDQEPSSKRKAQNRAAQRAFRKRKEDHLKALETQVVTLKELHSSTTLENDQLRQKVRQLEEELRILKDGSFTFEMSLPHRNPSLSSLPTTGFSSNFAHMKDGISPQSNLHLSPNSIEKPNMHQNVLHNDRSADNLNHRYQVPPTLVDSNSAQGTLSPETPSSSDSPSNLYLNYPKRKSITHLHHDCSALSNGENGEDVADGKQFCQKLSTACGSIACSMLTKTTPHRASVDILSNLHESTVSPPMADESVQRSSEVSKSIPNVELSLNVNQQFVSPFGGTDSFPLPTDTGLDSLFEPDSAIENSHLKNVVMEPELFQAWREPAESLDKEFFNDEGEIDDVFHNYFHNSNENGDLITNSLHGLDFLENANESFPEQMYPFIKHNKDYISNHPDEVPPDGLPQKGKHDTSSQMPSENEIVPAKERAYLSCPKVWSKIINHPRFESFDIDDLCSKLKNKAKCSSSGVLLDERDVEAALNQFN Q02061 RPB2_SCHPO BINDING 826; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="ligand shared with RPB1"; /evidence="ECO:0000250"; BINDING 1152; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1155; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1170; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; SPAC23G3.01; CHAIN 1..1210; /note="DNA-directed RNA polymerase II subunit RPB2"; /id="PRO_0000048090" MSYEDYQYNETLTQEDCWTVISSFFEETSLARQQLFSFDEFVQNTMQEIVDDDSTLTLDQYAQHTGAQGDVTRRYEINFGQIYLSRPTMTEADGSTTTMFPQEARLRNLTYSSPLYVDMRKKVMVAADSNVPIGEEEWLVEEEDEEPSKVFIGKIPIMLRSTFCILNGVSDSELYDLNECPYDQGGYFIINGSEKVIIAQERSAANIVQVFKKAAPSPIAYVAEIRSALERGSRLISSMQIKLMARNTENSGQTIRATLPYIRSDIPIVIVFRALGVVPDRDILEHICYDPNDFQMLEMMKPCIEEAFVIQDKDIALDYIGKRGSTTGVTREKRLRYAHDILQKELLPHITTMEGFETRKAFFLGYMIHRMLLCALERREPDDRDHFGKKRLDLAGPLLASLFRMLFRKMTRDVYKYMQKCVETNREFNLTLAVKSNIITNGLRYSLATGNWGDQKRSMVNRVGVSQVLNRYTFASTLSHLRRTNTPIGRDGKLAKPRQLHNTHWGMVCPAETPEGQACGLVKNLSLMSYVSVGSPSAPIIEFLEEWGLETLEDYNPSASPNATKVFVNGVWLGVHRDPAHLTETLRSLRRRLDISAEVSIVRDIREKELRLFTDAGRICRPLFIVDNNPNSERRGELCIRKEHIQQLIEDKDRYDIDPEQRFGWTALVSSGLIEYLDAEEEETVMIAMSPEDLEASRQMQAGYEVKEELDPAQRVKPAPNPHVHAWTHCEIHPAMILGILASIIPFPDHNQSPRNTYQSAMGKQAMGVYLTNYQVRMDTMANILYYPQKPLATTRSMEYLKFRELPAGQNAIVAILCYSGYNQEDSIIMNQASIDRGLFRSIFYRTYTDQEKKIGMTVMEEFERPVRSTTLRMKHGTYDKLEDDGLIAPGTRVSGEDIIIGKTAPIPLDHEELGQRTQLHAKRDVSTPLRSTESGIVDQVMVTTNQEGLKFVKVRMRSTRIPQIGDKFASRHGQKGTIGMTYRHEDMPFSAQGIVPDIIINPHAIPSRMTVAHLVECQLSKVSALSGFEGDATPFTDVTVEAVSKLLRSHGFQSRGFEVMYHGHTGRKLVAQVFLGPTYYQRLKHLVDDKIHARARGPVQILTRQPVEGRSRDGGLRFGEMERDCQISHGCSSVLRERLFDCSDAYRVIVCDICGLIAIASYKKDSYECRSCQNRTRFSQVYLPYAAKLLFQELMSMNIAPRLFTKNHK Q02088 TPM_SCHPO SPAC27F1.02c; CHAIN 1..161; /note="Tropomyosin"; /id="PRO_0000205694" MDKLREKINAARAETDEAVARAEAAEAKLKEVELQLSLKEQEYESLSRKSEAAESQLEELEEETKQLRLKADNEDIQKTEAEQLSRKVELLEEELETNDKLLRETTEKMRQTDVKAEHFERRVQSLERERDDMEQKLEEMTDKYTKVKAELDEVHQALEDL Q02099 RAD3_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC216.05; CHAIN 1..2386; /note="Protein kinase rad3"; /id="PRO_0000088837" MSQHAKRKAGSLDLSPRGLDDRQAFGQLLKEVLALDKEHELGRSNSLPSMTSELVEVLIEVGLLAFKHDDSKSEFISPKMLKEAHLSLQALMLILKRSPTVLREIKSSVTLLDWILPRTISLFADIRFIKLFDSLKEFHKLIYQLISEKSFLWDLYASFMRYWKYYITNVSSIVLQITNATFPYKMPSPNSQPLQSITPNYPTHREDKFDLLIINIEEACTFFFESAHFFAQCSYLKKSNFPSPPLFTAWTWIKPCFFNFVILLKRISIGDSQLFLHLHSRIVQTLCCFSLNFIYHGLPICEKSKHILMSSINLTLGSLKKTYTVANTAISLFFLSLFVLPKTVAGLFYPFGVSLLSDFKVLEQLEPDSDLKKAIILFKCRYQSSEIDQTTLRAFGEICTGKLENTLFSNSELNLFLLHYLSLDNDLSNILKVDFQNGHNICTFAKWCINNNLDEPSNLKHFREMLDYYSSHNVTISEDDLKNFSLVLCTHVAKVNEKTNSIFRTYEVHGCEVCNSFCLLFDERSLFKIPYHELFCALLKNPDIISSSVKQSLLLDGFFRWSQHCSNFNKESMLSLREFIMKALASTSRCLRVVAAKVLPIFIKGPNNLDIVEFHKESKALIFNTLKILAVENTAILETVILSWISLSRVVEEEELHFVLLEVISSVINSGIFYQGIGLSALQQIASTRHISVWQLLSPYWPTVSVAIVQGMGKKPNIASLFAQLMNISEGDFLIRTQAYTLPFLVLTKNKALIVRIAELSQSDVATLCLTNMHKILASLLTTDHPNLEESVMLLLSLATSDFEKVDLTSLLRSDPISITVELLQLYQNDVPHEKIENALRKVAMIVSQVVNDEDLSNKELLYDFFNNHILGILAEFSNILNDLKGKTSINEKIKTIVGIEKMLSLCGGAVKLGLPQILSNLQSAFQNEHLRFYAIKAWFSLILATKEPEYSSIAGLSLVILPPLFPYLEPQEAELVIQIFDFISSDTHKCLQGLKWAIPTSLDSACFSLKAKEIFCSLQNEDFYSELQSIIKCLTNENEPVCYLGLQKLELFFQAKVDELHDTLNLDISNEVLDQLLRCLLDCCVKYASTNMQISYLAAKNLGELGAIDPSRAKAQHIIKETVVLDNFENGEESLKFILDFMQSQLIPAFLVTTDTKAQGFLAYALQEFLKLGGFKSAVINKKKGLTVVTEHWMSLPDLSKRVLIPFLTSKYHLTPIPKIDIRYPIYKENVTIHTWMQLFSLKLMEYAHSQNAEKIFGICSKVVKDQEVNIPCFLLPFLVLNVILTESELEVNKVIEEFQLVINQPGPDGLNSVGQQRYTSFVDVFFKIVDYLNKWLRMRKKRNWDRRSAIARKENRYMSVEDATSRESSISKVESFLSRFPSKTLGIVSLNCGFHARALFYWEQHIRNATAPYAALESDYRVLQEIYAGIDDPDEIEAVSLNFHDYSFDQQLLLHENSGTWDSALSCYEIIIQKDPENKKAKIGLLNSMLQSGHYESLVLSLDSFIINDNHEYSKMLNLGIEASWRSLSIDSLKKCLSKSNLESFEAKLGSIFYQYLRKDSFAELTERLQPLYVDAATAIANTGAHSAYDCYDILSKLHAINDFSRIAETDGIVSDNLDIVLRRRLSQVAPYGKFKHQILSTHLVGYEKFENTKKTAEIYLEIARISRKNGQFQRAFNAILKAMDLDKPLATIEHAQWWWHQGQHRKAISELNFSLNNNMFDLVDEHEERPKNRKETLGNPLKGKVFLKLTKWLGKAGQLGLKDLETYYHKAVEIYSECENTHYYLGHHRVLMYEEEQKLPVNEQSERFLSGELVTRIINEFGRSLYYGTNHIYESMPKLLTLWLDFGAEELRLSKDDGEKYFREHIISSRKKSLELMNSNVCRLSMKIPQYFFLVALSQMISRVCHPNNKVYKILEHIIANVVASYPGETLWQLMATIKSTSQKRSLRGKSILNVLHSRKLSMSSKVDIKALSQSAILITEKLINLCNTRINSKSVKMSLKDHFRLSFDDPVDLVIPAKSFLDITLPAKDANRASHYPFPKTQPTLLKFEDEVDIMNSLQKPRKVYVRGTDGNLYPFLCKPKDDLRKDARLMEFNNLICKILRKDQEANRRNLCIRTYVVIPLNEECGFIEWVNHTRPFREILLKSYRQKNIPISYQEIKVDLDFALRSPNPGDIFEKKILPKFPPVFYEWFVESFPEPNNWVTSRQNYCRTLAVMSIVGYVLGLGDRHGENILFDEFTGEAIHVDFNCLFDKGLTFEKPEKVPFRLTHNMVDAMGPTGYEGGFRKASEITMRLLRSNQDTLMSVLESFLHDPLVEWNRKKSSSKYPNNEANEVLDIIRKKFQGFMPGETIPLSIEGQIQELIKSAVNPKNLVEMYIGWAAYF Q02592 HMT1_SCHPO BINDING 429..433; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250"; BINDING 492..495; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250"; BINDING 542; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250"; BINDING 593; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 617..628; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SIGNAL 1..27 SPCC737.09c; CHAIN 28..830; /note="Heavy metal tolerance protein"; /id="PRO_0000000259" CARBOHYD 150; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 350; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVLRYNSPRLNILELVLLYVGFFSIGSLNLLQKRKATSDPYRRKNRFGKEPIGIISWWILGIALTYVVDISNLVIYALRVPNWWPCKTTVVCLILFLLFWIIVLISCADSKALPKNADSILKAYRLSVLYVWAIDIVFETIFIVYSPHPNETFQGIVLADHVARLVLCVFATAIYLTYRRKRHTHDPLDFEERQLTEESNVNENAISQNPSTVQLGVSASTSNFGTLKSTSKKPSDKSWAEYFRSFSTLLPYLWPTKDYRLQFQIFICIVLLFLGRAVNILAPRQLGVLTEKLTKHSEKIPWSDVILFVIYRFLQGNMGVIGSLRSFLWVPVSQYAYRAISTKALRHVLNLSYDFHLNKRAGEVLTALTKGSSLNTFAEQVVFQIGPVLLDLGVAMVYFFIKFDIYFTLIVLIMTLCYCYVTVKITSWRTEARRKMVNSWRESYAVQNDAIMNFETVKNFDADDFENERYGHAVDIYLKQERKVLFSLNFLNIVQGGIFTFSLAIACLLSAYRVTFGFNTVGDFVILLTYMIQLQQPLNFFGTLYRSLQNSIIDTERLLEIFEEKPTVVEKPNAPDLKVTQGKVIFSHVSFAYDPRKPVLSDINFVAQPGKVIALVGESGGGKSTIMRILLRFFDVNSGSITIDDQDIRNVTLSSLRSSIGVVPQDSTLFNDTILYNIKYAKPSATNEEIYAAAKAAQIHDRILQFPDGYNSRVGERGLKLSGGEKQRVAVARAILKDPSIILLDEATSALDTNTERQIQAALNRLASGRTAIVIAHRLSTITNADLILCISNGRIVETGTHEELIKRDGGAYKKMWFQQAMGKTSAETH Q02787 PURA_SCHPO ACT_SITE 26; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; ACT_SITE 54; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125" BINDING 25..31; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 26..29; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 26; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 51..54; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 53..55; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 53; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 142; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 156; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 233; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 248; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 308..314; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 312; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 314; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 340..342; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125"; BINDING 422..424; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03125" CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03125}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03125}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03125}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1500 uM for L-aspartate {ECO:0000269|PubMed:4708672}; KM=200 uM for IMP {ECO:0000269|PubMed:4708672}; KM=20 uM for GTP {ECO:0000269|PubMed:4708672}; SPAC144.03; CHAIN 1..434; /note="Adenylosuccinate synthetase"; /id="PRO_0000095137" MASVRETGVNVSNDGITVVLGSQWGDEGKGKLVDILCDNVDVCARCQGGNNAGHTIVANGVTYDFHILPSGLVNPKCQNLIGSGVVVYLPAFFSELEKLEQKGLKCRDRIFISDRAHLVFDYHQRADALNEAELGKQSIGTTGKGIGPAYSTKATRSGIRVHHLYHWAEFEARYRKNVADLQKRYGAFEYDVEAELIRYKELAQRLKPFVIDAVAFMYEALQSKKRILVEGANALMLDLDFGTYPFVTSSNTTVGGVCTGLGVPPQRIANSIGVVKAYTTRVGAGPFPTEQLNEIGDHLQSVGREVGVTTGRKRRCGWLDLVVVKYSTMINGYTSLNLTKLDILDALDEIKVAVAYIINGKRIETFPADLDSLEEAEIVYETFPGWKVPTTGITHWDQMPENAKKYIEFIEKFVGVPITFIGVGPGRDEMLVKE Q02953 HSF_SCHPO MOD_RES 350; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2E12.02; CHAIN 1..609; /note="Heat shock factor protein"; /id="PRO_0000124580" MIQTASTISSNGGTNQGMESSSANSPEMNGTQNSMSVGMSGSGSSQNRKITQFSNKLYNMVNDSSTDSLIRWSDRGDSFLVIGHEDFAKLVLPRYFKHNNFSSFVRQLNMYGFHKVPHIQQGVLQSDSPNELLEFANPNFQRDQPELLCLVTRKKAGSQPVEESNTSLDMSTISSELQNIRIQQMNLSNELSRIQVDNAALWQENMENRERQRRHQETIDKILRFLASVYLDGKQKPPSKVMPKSRRLLLEAKYPTVSPTNEPSAHSRPSPQGTTANSSSASISSLHNTTPDGEGKYRSVQNGRALNYVSSFNSDSHSPKDYISQSYTNEPGLKKESADSFNNSIDSYISPNQSPNTDVPSLNRDDTTDPKVVNTGDIINMLDDANSIEGSNMNSLSPLLFDYPNSLYPVNNTSSEQHHNSYRGSVSNSQPSGNLSESTNLQPVQPVDYMSNSNPSYGSYNAEDQLTNFHPGYAMDQKRISKLSDGITKQDQNIQALADILGIPLGDGKIDDAGFSANSPTNLNLPVSSDLDSVLNIPPNEDVFPDSNPVFDEFTNISNLTSPIEASNGNTFGSNPVSLPNQQKSVNPSLMTVSSPRQVRKKRKSSIGA Q03392 PCNA_SCHPO PTM: Monoubiquitinated on Lys-164 by the rhp6/rhp18 complex upon DNA damage, and then polyubiquitinated through 'Lys-63'-linkage by ubc13/mms2 (PubMed:16641370). Ubiquitination contributes to efficient DNA replication in the absence of DNA damage (PubMed:28481910). {ECO:0000269|PubMed:16641370, ECO:0000269|PubMed:28481910}. SPBC16D10.09; STRAND 2..5; /evidence="ECO:0007829|PDB:6QH1"; STRAND 24..30; /evidence="ECO:0007829|PDB:6QH1"; STRAND 32..40; /evidence="ECO:0007829|PDB:6QH1"; STRAND 44..53; /evidence="ECO:0007829|PDB:6QH1"; STRAND 58..64; /evidence="ECO:0007829|PDB:6QH1"; STRAND 66..71; /evidence="ECO:0007829|PDB:6QH1"; STRAND 87..92; /evidence="ECO:0007829|PDB:6QH1"; STRAND 97..105; /evidence="ECO:0007829|PDB:6QH1"; STRAND 110..117; /evidence="ECO:0007829|PDB:6QH1"; STRAND 134..140; /evidence="ECO:0007829|PDB:6QH1"; STRAND 156..163; /evidence="ECO:0007829|PDB:6QH1"; STRAND 166..170; /evidence="ECO:0007829|PDB:6QH1"; STRAND 174..182; /evidence="ECO:0007829|PDB:6QH1"; STRAND 196..201; /evidence="ECO:0007829|PDB:6QH1"; STRAND 203..208; /evidence="ECO:0007829|PDB:6QH1"; STRAND 223..230; /evidence="ECO:0007829|PDB:6QH1"; STRAND 233..241; /evidence="ECO:0007829|PDB:6QH1"; STRAND 244..250; /evidence="ECO:0007829|PDB:6QH1" HELIX 10..20; /evidence="ECO:0007829|PDB:6QH1"; HELIX 54..56; /evidence="ECO:0007829|PDB:6QH1"; HELIX 72..79; /evidence="ECO:0007829|PDB:6QH1"; HELIX 141..154; /evidence="ECO:0007829|PDB:6QH1"; HELIX 209..215; /evidence="ECO:0007829|PDB:6QH1"; HELIX 216..221; /evidence="ECO:0007829|PDB:6QH1" CHAIN 1..260; /note="Proliferating cell nuclear antigen"; /id="PRO_0000149175" MLEARFQQAALLKKLLDAIKELVTDANFDCNDNGISLQAMDSSHVALVSMLIKSDGFEPYRCDRNIALGINLNALSKVLRCAQNEDLVTLKAEDTPEVLNLVFESEKNDRISDYDVKLMDIDQEHLGIPDIEYDATITMPAAEFQRITRDLLTLSDSVTINASKEGVRFSCKGDIGNGSTTLKQHTDLSDQDQSIEISLTQAVTLTFSLKYLAQFTKATPLATRVTLSMSNDVPLLVEYKMESGFLRFYLAPKIGEEDEE Q04665 GPA2_SCHPO BINDING 41..48; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 48; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 173..179; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 179; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 198..202; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 269..272; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 326; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC23H3.13c; CHAIN 1..354; /note="Guanine nucleotide-binding protein alpha-2 subunit"; /id="PRO_0000203609" MTIFNGLSESGESKKLNSKIEKQIENASKKDKKIYKVLLLGASDSGKSTISKQIKILNKNGFSQEEIMTFIPVIRRNLLESAKTLVKIIVQKGINLDPLGTHNCEIIEKFNPTPGELINANIGQAITSLWSANSVRSCTYGNDSVLIDSAPYFFSRADEICSRHYVPTIDDILRSRNSTLGISEISFTLDHLQIRMFDVGGQRTERRKWIYCFENVNSIIFCVSLNDYDKKLYERAAPERNRLVESISLFDSIINSQWFMHSSIILFLNKFDLFRKKLEHVPFQDYFPQYEGKNSVKSITRYILWLFVNPSINRAKHNIYPHITTAVDTSNIKVVFSAVKETILQHSLKEAGMF Q06182 SWI10_SCHPO SPBC4F6.15c; CHAIN 1..252; /note="Mating-type switching protein swi10"; /id="PRO_0000072347" MSDIDDEEFEQLAVSALEEVEKKAGFAQQPTPQKVSRVTAHSILVNPRQKGNPLLPHVRNVPWEYTDIVPDFVMGTGICSLFLSLKYHHLHPEYIYSRISKLGKSYNLRILLILVDVENHQASIQELVKTSIVNQYTLILAWSSEEAARYLETYKAYENMSPALIMEKPSTDYLSQVQSFLTSIRGINKSDSLSLLSKFGSLERALVASRDELEQLEGWGPTKVNRFLEAVQQPFMSHSTIKRPEAINLKQT Q07538 PRP4_SCHPO ACT_SITE 286; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 165..173; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 188; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 92; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 320; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPCC777.14; CHAIN 1..477; /note="Serine/threonine-protein kinase prp4"; /id="PRO_0000086585" MSDDRFAEDEIIQQRRKRRLEILKKYQQTGNGHSDLSIPEKKLKEDVDQVSTTKPIEAVPKMKTNASKIEINKEGSNSNTKLDVTNSTTSDSPSIKSSVQIEDTEDDMFADSPSPSVKRQNTGKGISTLTRSFADMQDNWDDIEGYYKVVLMEELDSRYIVQSNLGKGMFSTVVSALDRNRNQTFAIKIIRNNEVMYKEGLKEVSILERLQAADREGKQHIIHYERHFMHKNHLCMVFEMLSLNLRDILKKFGRNVGLSIKAVRLYAYQMFMALDLLKQCNVIHSDIKPDNMLVNEKRNILKICDLGSASDASENEITPYLVSRFYRAPEIILGFPYSCPIDTWSVGCSLYELYTGQILFPGRTNNQMLRYMMECKGKFSHKMLKRSQFLNDHFDADFNFIQIDHDPITNQETRKPVKFSKPTKDIRSRLKEVPTSTDEEFIIRQELMDLLEKCLELNPEKRVPPEVALKHPFFIKK Q08I43 ERI1_SCHPO ACT_SITE 88; /note="Proton acceptor"; /evidence="ECO:0000255"; ACT_SITE 264; /note="Proton acceptor"; /evidence="ECO:0000255" BINDING 86; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 86; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 88; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250"; BINDING 88; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 89; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250"; BINDING 206; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 264; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250"; BINDING 269; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; SPBC30B4.08; CHAIN 1..313; /note="3'-5' exonuclease eri1"; /id="PRO_0000362146" MESPVQILVWPFPCDEMNQKTPSTVEEIRIALQELGLSTNGNKEKLKRRWKFREKRLEEKRKQERYQKFSTSNENKTCLRYLLIVDVEATCEEGCGFSFENEIIELPCLLFDLIEKSIIDEFHSYVRPSMNPTLSDYCKSLTGIQQCTVDKAPIFSDVLEELFIFLRKHSNILVPSVDEIEIIEPLKSVPRTQPKNWAWACDGPWDMASFLAKQFKYDKMPIPDWIKGPFVDIRSFYKDVYRVPRTNINGMLEHWGLQFEGSEHRGIDDARNLSRIVKKMCSENVEFECNRWWMEYEKNGWIPNRSYPPYFAS Q09116 SPN2_SCHPO BINDING 39..46; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 73; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 99; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 179..187; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 235; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 250; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC821.06; CHAIN 1..331; /note="Septin homolog spn2"; /id="PRO_0000173504" MEVPSAVTLNNYVGFDSITSQINRKLIRRGFQFNVMVVGPSGSGKSTLINTLFSAHLMDSKGRLDYQAPYRQTTEIHVTSQVVRENRVQLQLNLIDTPGYGDQINNDKCWEPIIKYIRDQHSSYLRRELNSHREKRLQDTRVHCCLFFIRPTGHSLRPIDIAVLKRLTEVVNVVPVIAKSDSLTLEERAAFKQQIREEFVKHDINLYPYDSDDADEEEINLNAAVRNLIPFAVVGSEKAIIVDGRPIRGRQNRWGVVNVDDENHCEFVFLRNFLMRTHLQDLIETTSYYHYEKFRFKQLSSLKEQSSLATRMGSPAPVYPSEPHLHTATAQ Q09140 UGGG_SCHPO COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8631292}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:8631292}; SIGNAL 1..18; /evidence="ECO:0000269|PubMed:7982990, ECO:0000269|PubMed:8631292" PTM: Glycosylated. {ECO:0000269|PubMed:8631292}. SPBPJ4664.06; CHAIN 19..1448; /note="UDP-glucose:glycoprotein glucosyltransferase"; /id="PRO_0000012275" CARBOHYD 66; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 749; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 880; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1046; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1441; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRWGFWFAIATLITICYAAKPLDVKIAATFNAPSFSALIAESLYQEKKEGFIWYLNHLSDLLDAENTTEKELYINVVNSLKREYVLSDEELSSLQFSLGLFSGAPKLQAFSSIVQSRSCDCDTWLQLDEESQVCFSDLPKDSPLFSKLYSKNPLDYEVVKTSATGIPYAVVVTSFERDLIPFHELYYKLALEGKCNYVIRYSPPSSSKLNSKLYVKGFGTHVSLKRTDYLVVDDREFPREKGDNPASFTSSRNKRSNERLFGMTSDSLQTVTPDKIAILDLLATQSIASSTDMLTAFRELTQDFPIYAHYLSIQPDVSNDLIEELNQFQSQYVPEGINTIWLNGLSLDLEETDAFSILSLIKKEKDMFDRFEALGIKSSKVLDIVTNEAFANEDSDFKFVKFHCQDDIEDWKAIHWVNEIESNPKYDNWPKSIQILLKPIYPGQLHMLGKQLHTVIYPIFPSSPSSLPLLSELIQFSRRPSPVQTGMVCAANDDDEFAQTVCKSFFYISKESGTDSALKFLYKCLNSDSSADLYSLLEEHLPLSEHDDDTLANLKKDLSSSFFDHYMSKSNSWVNRLGIDSSASEVIVNGRIISHDENYDRSMYGIFLEDIPEVQIAVAEGKISEDDNLLDFILRDASLTRNPLVYPSAKSSIKSIDIKRVLENVGSLNHEDILLIGSSNAKYSFWLVADFNEKEGLEILSLLADLLSENKDANLMLIQEGKNHVVPPLFAKLLSSPKRSSKHLQEILNSSLDPSSGVVNDMDKALKFLKKSKAVVKELGLTGECKSALLLNGRMICSFSVDSLNTADLKMLMQMEYDNYLSKLSNIAGSSRRLKNSRAISFLSSYLKTLESTPMSTSSPTKEEKLFPRDFIYNKLGVGNATFETDDFSKAYYQFVAVLDPLSKDSQKWSAILEAVSKLNGVGVRIHFNPKQTLSELPLTRFYRYSISAEPEFDALGHLEESYVEFDNLPADTLLTMDIEARDAWTVMQKDVDIDLFNIKLEHTSEAEALDSHTAIYELKNILVQGYSQEEFRKSPPRGMQLKLGNLTNSHVTDTIVLSNLGYFQLKANPGVWTLEPMDGRSSQFYEILSLNKKNSYKDPQVIVDSFEGVTLNPVMRRKPGFESADIMDEDLSSHKFFDKIKKSLSFFNFKRKEASINIFSVASGHLYERFLYIMTKSVIEHTDKKVKFWFIENFLSPSFKSSIPAIAKKYNFEYEYITYNWPHWLRKQEEKQREIWGYKILFLDVLFPLELHKVIYVDADQIVRADLQELMDMDLHGAPYGYTPMCDSREEMEGFRFWKKGYWKKFLRGLKYHISALYVVDLDRFRKMGAGDLLRRQYQLLSADPNSLSNLDQDLPNHLQHLIPIYSLPQDWLWCETWCSDESLKTAKTIDLCQNPLTKEKKLDRARRQVSEWTSYDNEIASVLQTASSQSDKEFEEKDNNSSPDEL Q09142 ORC2_SCHPO PTM: Phosphorylated by cdc2 and cdc13 (in vitro) (PubMed:11486016). Phosphorylation appears first in S phase and becomes maximal in G2 and M when cdc2 kinase activity is required to prevent reinitiation of DNA replication (PubMed:11486016). {ECO:0000269|PubMed:11486016}. MOD_RES 44; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:11486016"; MOD_RES 57; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:11486016"; MOD_RES 62; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:11486016"; MOD_RES 65; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:11486016" SPBC685.09; CHAIN 1..535; /note="Origin recognition complex subunit 2"; /id="PRO_0000127081" MLINEHVRERYHFLRVSLTRVAHLVFANSHESNDLKMVENVSSTPKKGVLEDPSTLTPEVVTPRTPGHRIIKAKGAYTKDRSAKRRRGRIEIERHLLGEFDDNVGSNSLLDVPLYSLEAEPLSPSVMLEDESMEGINQSPQGISVEKLGKEDNRSRSSTPASPSLESHEFSESREAGLSQSNGFEARSHGTGFDEYFDKFSQRKTSSNTLSQLPVLDNQVYLDTVKEICTETEQHTQTLVHFQSRNFHQWYFELVNNFNLLFYGFGSKEHFLSSFVEKKLPCFPIFVVKGYFPQLQLKNVLSSFLEFLEVTPAASVSDMLIQSLSIINSPSFSLGKIVFLVHNIDGESLIDERFQSALAAIASSKNVYFIASVDHVNFALLWDTSLESSFNFVMHDATTFARYYNETTYENSLGIGRANVSNKEKAIKHVLYSLPANSRGIFKFLLIHQLERMMDTQDFDARQGEKVGIEYRSFFQKCSAEFLCSNEPNFRSQLTEFFDHNIIESKRDVSNSEILWVPYPKNLLEILLEDMMEDV Q09154 UCRI_SCHPO BINDING 172; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"; BINDING 174; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"; BINDING 191; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"; BINDING 194; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P08067}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628}; TRANSIT 1..26; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC16H5.06; CHAIN 27..228; /note="Cytochrome b-c1 complex subunit Rieske, mitochondrial"; /id="PRO_0000030682" DISULFID 177..193; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" MLAKQFISKSLASSLRRLLPVSSTASSLKGSMMTIPKFTSIRTYTDSPEMPDFSEYQTKSTGDRSRVISYAMVGTMGALTAAGAQATVHDFLASWSASADVLAMSKAEVDLSKIPEGKNLVVKWQGKPVFIRHRTPEEIQEANSVDISTLRDPQADSDRVQKPEWLVMIGVCTHLGCVPIGEAGDYGGWFCPCHGSHYDISGRIRRGPAPLNLAIPAYTFEGSKIIIG Q09170 CDS1_SCHPO ACT_SITE 294; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 173..181; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 196; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9450932}. MOD_RES 443; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC18B5.11c; CHAIN 1..460; /note="Serine/threonine-protein kinase cds1"; /id="PRO_0000085846" MEEPEEATQATQEAPLHVSQNIAKQVVNNENVFMKLVMTRMLDGKTEVIPLTTDVHNGFWRFGRHKSCEVVLNGPRVSNFHFEIYQGHRNDSDESENVVFLHDHSSNGTFLNFERLAKNSRTILSNGDEIRIGLGVPKDEISFLCQVPVKHSRDSQKNMIKSENSHYEIIRTLGSGTFAVVKLAVEVNSGKWYAIKIINKRKILLTSSEKRATEMFQREIDILKSLHHPGVVQCHEIFENDDELFIVMEYVEGGDLMDFLIANGSIDEQDCKPLLKQLLETLLHLHKQGVTHRDIKPENILITNDFHLKISDFGLAKVIHGTGTFLETFCGTMGYLAPEVLKSKNVNLDGGYDDKVDIWSLGCVLYVMLTASIPFASSSQAKCIELISKGAYPIEPLLENEISEEGIDLINRMLEINPEKRISESEALQHPWFYTVSTHEHRTPPSSSEHEATEQLNSSS Q09173 PP2C3_SCHPO BINDING 62; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 62; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 63; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 230; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 279; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; SPAC2G11.07c; CHAIN 1..414; /note="Protein phosphatase 2C homolog 3"; /id="PRO_0000057772" MGQTLSEPVTEKHSVNGSNEFVLYGLSSMQGWRISMEDAHSAILSMECSAVKDPVDFFAVYDGHGGDKVAKWCGSNLPQILEKNPDFQKGDFVNALKSSFLNADKAILDDDQFHTDPSGCTATVVLRVGNKLYCANAGDSRTVLGSKGIAKPLSADHKPSNEAEKARICAAGGFVDFGRVNGNLALSRAIGDFEFKNSNLEPEKQIVTALPDVVVHEITDDDEFVVLACDGIWDCKTSQQVIEFVRRGIVAGTSLEKIAENLMDNCIASDTETTGLGCDNMTVCIVALLQENDKSAWYKKIADRVAANDGPCAPPEYAENHGPGWRSGDNNKKVIVPPNFHQVKLNGSDGYDKDANENSKEDDSTNGSLAAGFRWKEHFFPHKAEEENSSSETDIVNSNKDVADDHKEAVSAAD Q09175 KRP1_SCHPO ACT_SITE 162; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 200; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 371; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240" COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; SIGNAL 1..22; /evidence="ECO:0000255" PTM: N-glycosylated. SPAC22E12.09c; PROPEP 23..82; /evidence="ECO:0000255"; /id="PRO_0000027046"; PROPEP 83..102; /evidence="ECO:0000255"; /id="PRO_0000027047" CHAIN 103..709; /note="Dibasic-processing endoprotease"; /id="PRO_0000027048" CARBOHYD 155; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 463; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 471; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 620; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 216..363; /evidence="ECO:0000250"; DISULFID 308..338; /evidence="ECO:0000250" MHPALLCGPILAIFLQFLVSSCSPLENDDLFLVQVEPEVDPVVAAEAIGAKYVRPLLNLKYHHLIKLHKGSDDSVQSSIRKRGIDAGILELERQTPRWRYKRDASESDELLNEFSNHFGISDPLFYGQWHIFNSNNPGHDLNLREVWDAGYFGENVTVAFVDDGIDFKHPDLQAAYTSLGSWDFNDNIADPLPKLSDDQHGTRCAGEVAAAWNDVCGVGIAPRAKVAGLRILSAPITDAVESEALNYGFQTNHIYSCSWGPADDGRAMDAPNTATRRALMNGVLNGRNGLGSIFVFASGNGGHYHDNCNFDGYTNSIFSATIGAVDAEHKIPFYSEVCAAQLVSAYSSGSHLSILTTNPEGTCTRSHGGTSAAAPLASAVYALALSIRPDLSWRDIQHITVYSASPFDSPSQNAEWQKTPAGFQFSHHFGFGKLDASKFVEVAKDWQVVNPQTWLIAPEINVNKSFGSVNNETITEMVSEFTVTKDMIEKSNFKRLEHVTVRVCIPFNRRGALEILLESPSGIRSILASERPYDENSKGFLDWTFMTVQHWAEPPEGVWKLLVNDRSGGKHEGTFENWQLALWGESENPSNTAPLPYDTLELPKEMVLGIYSEPNSDLTNSSTLLSPTSTSFTSYTVSATATPTSTSHIPIPTVLPPTQPVLEPSYREIVAFITFFLLFAFIFVAVIWTWISAFWKAKAPPPLSQQEIA Q09176 U2AF1_SCHPO SPAP8A3.06; STRAND 15..17; /evidence="ECO:0007829|PDB:7C06"; STRAND 34..36; /evidence="ECO:0007829|PDB:4YH8"; STRAND 44..48; /evidence="ECO:0007829|PDB:4YH8"; STRAND 58..60; /evidence="ECO:0007829|PDB:7C08"; STRAND 90..96; /evidence="ECO:0007829|PDB:4YH8"; STRAND 107..113; /evidence="ECO:0007829|PDB:4YH8"; STRAND 128..133; /evidence="ECO:0007829|PDB:7C06"; STRAND 137..139; /evidence="ECO:0007829|PDB:4YH8"; STRAND 164..166; /evidence="ECO:0007829|PDB:7C06" HELIX 19..24; /evidence="ECO:0007829|PDB:4YH8"; HELIX 30..32; /evidence="ECO:0007829|PDB:4YH8"; HELIX 55..57; /evidence="ECO:0007829|PDB:4YH8"; HELIX 61..63; /evidence="ECO:0007829|PDB:4YH8"; HELIX 66..84; /evidence="ECO:0007829|PDB:4YH8"; HELIX 85..87; /evidence="ECO:0007829|PDB:4YH8"; HELIX 114..124; /evidence="ECO:0007829|PDB:4YH8"; HELIX 144..147; /evidence="ECO:0007829|PDB:4YH8"; HELIX 150..154; /evidence="ECO:0007829|PDB:4YH8"; HELIX 160..162; /evidence="ECO:0007829|PDB:4YH8"; HELIX 173..191; /evidence="ECO:0007829|PDB:4YH8" TURN 101..105; /evidence="ECO:0007829|PDB:4YH8" CHAIN 1..216; /note="Splicing factor U2AF 23 kDa subunit"; /id="PRO_0000081998" MASHLASIYGTEQDKVNCSFYYKIGACRHGERCSRKHVKPNFSQTILCPNMYKNPIHEPNGKKFTQRELAEQFDAFYEDMFCEFSKYGEVEQLVVCDNVGDHLVGNVYVRFKYEESAQNAIDDLNSRWYSQRPVYAELSPVTDFREACCRQHETSECQRGGLCNFMHAKKPSPQLLRDLVLAQRKYLALNAAEEMKKEPNSDSTNRWVSVTAERKN Q09180 MATP2_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" PTM: Proteolytically cleaved by kpr, probably at the C-terminal side of dibasic Lys-Arg residues. {ECO:0000269|PubMed:7813430}.; PTM: Glycosylated. Most of the precursor molecules are glycosylated on at least one site, but only a small proportion are glycosylated on both sites. {ECO:0000269|PubMed:7813430}. SPCC1795.06; PROPEP 21..31; /id="PRO_0000021642"; PROPEP 58..65; /evidence="ECO:0000269|PubMed:8314086"; /id="PRO_0000021644"; PROPEP 92..99; /id="PRO_0000021646"; PROPEP 126..133; /id="PRO_0000021648"; PROPEP 160..201; /id="PRO_0000021650" CARBOHYD 187; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 194; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKITAVIALLFSLAAASPIPVADPGVVSVSKSYADFLRVYQSWNTFANPDRPNLKKREFEAAPAKTYADFLRAYQSWNTFVNPDRPNLKKREFEAAPEKSYADFLRAYHSWNTFVNPDRPNLKKREFEAAPAKTYADFLRAYQSWNTFVNPDRPNLKKRTEEDEENEEEDEEYYRFLQFYIMTVPENSTITDVNITAKFES Q09191 RPAB1_SCHPO MOD_RES 152; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C4.15; CHAIN 1..210; /note="DNA-directed RNA polymerases I, II, and III subunit RPABC1"; /id="PRO_0000146084" MSAEEKNIVRVFRAWKTAHQLVHDRGYGVSQAELDLTLDQFKAMHCGMGRNLDRTTLSFYAKPSNDSNKGTIYIEFAKEPSVGIKEMRTFVHTLGDHNHKTGILIYANSMTPSAAKIIATVTGQFTIETFQESDLIVNITHHELVPKHILLSPDEKKELLDRYKLRETQLPRIQLADPVARYLGLKRGEVVKIVRRSETSGRYNSYRICA Q09196 MLR4_SCHPO BINDING 87; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 89; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 91; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 93; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 98; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" PTM: Phosphorylated on either Ser-2 or Ser-6 but not both. Phosphorylation is not essential for the function of the protein. {ECO:0000269|PubMed:10364209}. MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:10364209"; MOD_RES 6; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:10364209" SPAP8A3.08; STRAND 17..23; /evidence="ECO:0007829|PDB:1GGW"; STRAND 53..56; /evidence="ECO:0007829|PDB:1GGW"; STRAND 68..73; /evidence="ECO:0007829|PDB:1GGW" HELIX 9..14; /evidence="ECO:0007829|PDB:1GGW"; HELIX 25..34; /evidence="ECO:0007829|PDB:1GGW"; HELIX 41..48; /evidence="ECO:0007829|PDB:1GGW"; HELIX 57..64; /evidence="ECO:0007829|PDB:1GGW"; HELIX 76..84; /evidence="ECO:0007829|PDB:1GGW"; HELIX 96..107; /evidence="ECO:0007829|PDB:1GGW"; HELIX 112..121; /evidence="ECO:0007829|PDB:1GGW"; HELIX 133..139; /evidence="ECO:0007829|PDB:1GGW" TURN 6..8; /evidence="ECO:0007829|PDB:1GGW"; TURN 130..132; /evidence="ECO:0007829|PDB:1GGW" CHAIN 1..141; /note="Myosin regulatory light chain cdc4"; /id="PRO_0000198763" MSTDDSPYKQAFSLFDRHGTGRIPKTSIGDLLRACGQNPTLAEITEIESTLPAEVDMEQFLQVLNRPNGFDMPGDPEEFVKGFQVFDKDATGMIGVGELRYVLTSLGEKLSNEEMDELLKGVPVKDGMVNYHDFVQMILAN Q09683 RAD32_SCHPO ACT_SITE 134; /note="Proton donor"; /evidence="ECO:0000255|PIRSR:PIRSR000882-1" BINDING 25; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 27; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 65; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 65; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 133; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 222; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 250; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX"; BINDING 252; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:22705791, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX" COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22705791}; SPAC13C5.07; STRAND 18..23; /evidence="ECO:0007829|PDB:4FBW"; STRAND 58..62; /evidence="ECO:0007829|PDB:4FBW"; STRAND 67..71; /evidence="ECO:0007829|PDB:4FBW"; STRAND 89..91; /evidence="ECO:0007829|PDB:4FBW"; STRAND 97..100; /evidence="ECO:0007829|PDB:4FBW"; STRAND 123..125; /evidence="ECO:0007829|PDB:4FBW"; STRAND 127..129; /evidence="ECO:0007829|PDB:4FBW"; STRAND 154..157; /evidence="ECO:0007829|PDB:4FCX"; STRAND 167..169; /evidence="ECO:0007829|PDB:4FBW"; STRAND 172..176; /evidence="ECO:0007829|PDB:4FBW"; STRAND 179..186; /evidence="ECO:0007829|PDB:4FBW"; STRAND 203..209; /evidence="ECO:0007829|PDB:4FBW"; STRAND 215..223; /evidence="ECO:0007829|PDB:4FBW"; STRAND 228..233; /evidence="ECO:0007829|PDB:4FBW"; STRAND 244..250; /evidence="ECO:0007829|PDB:4FBW"; STRAND 255..261; /evidence="ECO:0007829|PDB:4FBW"; STRAND 266..270; /evidence="ECO:0007829|PDB:4FBW"; STRAND 288..295; /evidence="ECO:0007829|PDB:4FBW"; STRAND 298..305; /evidence="ECO:0007829|PDB:4FBW"; STRAND 307..309; /evidence="ECO:0007829|PDB:4FBW"; STRAND 312..318; /evidence="ECO:0007829|PDB:4FBW"; STRAND 327..329; /evidence="ECO:0007829|PDB:4FBW"; STRAND 373..379; /evidence="ECO:0007829|PDB:4FBW"; STRAND 406..410; /evidence="ECO:0007829|PDB:4FBW" HELIX 40..54; /evidence="ECO:0007829|PDB:4FBW"; HELIX 74..88; /evidence="ECO:0007829|PDB:4FBW"; HELIX 115..117; /evidence="ECO:0007829|PDB:4FBW"; HELIX 133..135; /evidence="ECO:0007829|PDB:4FBW"; HELIX 145..151; /evidence="ECO:0007829|PDB:4FBW"; HELIX 191..199; /evidence="ECO:0007829|PDB:4FBW"; HELIX 236..238; /evidence="ECO:0007829|PDB:4FBW"; HELIX 281..284; /evidence="ECO:0007829|PDB:4FBW"; HELIX 319..321; /evidence="ECO:0007829|PDB:4FBW"; HELIX 332..358; /evidence="ECO:0007829|PDB:4FBW"; HELIX 389..394; /evidence="ECO:0007829|PDB:4FBW" TURN 29..33; /evidence="ECO:0007829|PDB:4FBW"; TURN 35..39; /evidence="ECO:0007829|PDB:4FBW"; TURN 210..214; /evidence="ECO:0007829|PDB:4FBW"; TURN 262..265; /evidence="ECO:0007829|PDB:4FBW"; TURN 381..383; /evidence="ECO:0007829|PDB:4FBW"; TURN 395..399; /evidence="ECO:0007829|PDB:4FBW" CHAIN 1..649; /note="Double-strand break repair protein rad32"; /id="PRO_0000138683" MPNDPSDMNNELHNENTIRILISSDPHVGYGEKDPVRGNDSFVSFNEILEIARERDVDMILLGGDIFHDNKPSRKALYQALRSLRLNCLGDKPCELELLSDTSLTTGDTAVCNINYLDPNINVAIPVFSIHGNHDDPSGDGRYSALDILQVTGLVNYFGRVPENDNIVVSPILLQKGFTKLALYGISNVRDERLYHSFRENKVKFLRPDLYRDEWFNLLTVHQNHSAHTPTSYLPESFIQDFYDFVLWGHEHECLIDGSYNPTQKFTVVQPGSTIATSLSPGETAPKHCGILNITGKDFHLEKIRLRTVRPFIMKDIILSEVSSIPPMVENKKEVLTYLISKVEEAITEANAQWYEAQGTVPVVENEKPPLPLIRLRVDYTGGYQTENPQRFSNRFVGRVANATDVVQFYLKKKYTRSKRNDGLYTSAVEDIKINSLRVESLVNEYLKTNRLECLPEDSLGEAVVNFVEKDDRDAIKECVETQLNKQINLLVKKRVTEENLEQEISSIINDLPKISTTKRKDYEELPEEVSETSINIAEHTPVLKHTSSLLDHHSPLATSSSEHEMEATPSPALLKKTNKRRELPSSLTKKNTRTPQRSKEVKKVPARKLSQSTKKSDKNTQSTLLFYDPSSTTEAQYLDNEDDEILDD Q09684 KAR5_SCHPO SIGNAL 1..29; /evidence="ECO:0000255" PTM: N-glycosylated. {ECO:0000269|PubMed:9442101}. SPAC13C5.03; CHAIN 30..577; /note="Nuclear fusion protein tht1"; /id="PRO_0000072529" CARBOHYD 163; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 372; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKFHPTRPFGLYFEFFIIISFFFTSESTGDVESFMKYSNVAFSEGLAGFDSLAHVYQALLKKSTCYQEVAATLISKCSLLNTELTIDNRIHSAIQMTLCDFERSQILAPSECVRGSQSECVSKLESTSTWWLSFTSHFHDVNHLCRLANLEMQKELSIEVNMNVTLVQKQFLEMVILHLRNFESVTDKMNQRIDKFDGKFNSVIENSFKDINFRVNQEIMGLVELQNHQQEGMVQQKEILSTIKQLKSEIFDINSFFANFIEESAGYSNSLIEKLNEKFTSENAIALSAIGKYTSEFSAFMEKRIKNLITTTEDSLQQSVQSNIDFVNSGFQPLYDLTIQLKEELQSLKRLSSEQQNLQHEQILQWKSDFLNVSKDHLKVLQQLRPLIDIVEKFMNVYFKGLSNIISSFAFIGFTLFATLSSLFFKVLKIHRRPIIVFGSLSIIFIHIYCFKITSWVNLYGWITCTIARTLSFIKLNIRTFYLTAFLCALLNFLRYLKYRNSKKDTELSLFLPAPEECNIYHNEHIQVQEDNYLCPIENSLIDLFGSENNKEKLGKQENVRFAFLNSESLEQSPWWD Q09685 DRE4_SCHPO SPAC13C5.02; CHAIN 1..411; /note="Pre-mRNA-splicing factor dre4"; /id="PRO_0000076095" MSQPLPPGWTEHKAPSGIPYYWNAELKKSTYQRPSFIEKNHSSSVTASQASLAFNTSEKLFVNENAEERKNSRDLRKQLPDRPKFKKRIPNNDSWVVVFTKKNRYFFHNLKSHESYWEPPLEISKDLKILRLPIRKQISKDSSQSQNVDSGKTNHEEIHESRHLQTEIEEPSGLEESSEESVLYSEEFYEKSDEEEDEEKSHSAEELEFGEEDIMYQLQQLDDETVSYDIQEQATNLSTDDARRVFTELLKDKNIGAYQPWELVYPKLLDDDRFYVLDSGERRKEVFEEYCKSVVSTKKITRRKNTLSDFWTLLHSLPSTLLWPQFKRKYRKSSTLQIPGYSERDFEKLFREFQILRKQPMQDKLLNFKKLCKSKTVDPKNPDEFTESILNDTRYAVLTREELDSLACSSN Q09690 POM1_SCHPO ACT_SITE 825; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 705..713; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 728; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772}; PTM: Autophosphorylates at the cell cortex to lower lipid affinity and promote membrane release (PubMed:21703453, PubMed:26150232). Dephosphorylation by dis2, regulated by tea4, triggers membrane association (PubMed:21703453). {ECO:0000269|PubMed:21703453, ECO:0000269|PubMed:26150232}. MOD_RES 513; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F7.03c; CHAIN 1..1087; /note="DYRK-family kinase pom1"; /id="PRO_0000086579" MGYLQSQKAVSLGDENTDALFKLHTSNRKSANMFGIKSELLNPSELSAVGSYSNDICPNRQSSSSTAADTSPSTNASNTNISFPEQEHKDELFMNVEPKGVGSSMDNHAITIHHSTGNGLLRSSFDHDYRQKNSPRNSIHRLSNISIGNNPIDFESSQQNNPSSLNTSSHHRTSSISNSKSFGTSLSYYNRSSKPSDWNQQNNGGHLSGVISITQDVSSVPLQSSVFSSGNHAYHASMAPKRSGSWRHTNFHSTSHPRAASIGNKSGIPPVPTIPPNIGHSTDHQHPKANISGSLTKSSSESKNLSTIQSPLKTSNSFFKELSPHSQITLSNVKNNHSHVGSQTKSHSFATPSVFDNNKPVSSDNHNNTTTSSQVHPDSRNPDPKAAPKAVSQKTNVDGHRNHEAKHGNTVQNESKSQKSSNKEGRSSRGGFFSRLSFSRSSSRMKKGSKAKHEDAPDVPAIPHAYIADSSTKSSYRNGKKTPTRTKSRMQQFINWFKPSKERSSNGNSDSASPPPVPRLSITRSQVSREPEKPEEIPSVPPLPSNFKDKGHVPQQRSVSYTPKRSSDTSESLQPSLSFASSNVLSEPFDRKVADLAMKAINSKRINKLLDDAKVMQSLLDRACIITPVRNTEVQLINTAPLTEYEQDEINNYDNIYFTGLRNVDKRRSADENTSSNFGFDDERGDYKVVLGDHIAYRYEVVDFLGKGSFGQVLRCIDYETGKLVALKIIRNKKRFHMQALVETKILQKIREWDPLDEYCMVQYTDHFYFRDHLCVATELLGKNLYELIKSNGFKGLPIVVIKSITRQLIQCLTLLNEKHVIHCDLKPENILLCHPFKSQVKVIDFGSSCFEGECVYTYIQSRFYRSPEVILGMGYGTPIDVWSLGCIIAEMYTGFPLFPGENEQEQLACIMEIFGPPDHSLIDKCSRKKVFFDSSGKPRPFVSSKGVSRRPFSKSLHQVLQCKDVSFLSFISDCLKWDPDERMTPQQAAQHDFLTGKQDVRRPNTAPARQKFARPPNIETAPIPRPLPNLPMEYNDHTLPSPKEPSNQASNLVRSSDKFPNLLTNLDYSIISDNGFLRKPVEKSRP Q09693 DPO4_SCHPO BINDING 355; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 357; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 419; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC2F7.06c; CHAIN 1..506; /note="DNA polymerase type-X family protein pol4"; /id="PRO_0000218800" MKILASSTNYVLHNRLSNSQYEDARSKIVNFGGEFTNDAAKADYIFVNYSQINRVRRELRTIGTPLETCVSCKLIVKIDWLNEPKESLTPGNPYVIWHRKPEMKVGSPYTPSTRPASHTEAPNDFENHETPNTENNNEVKSIDNVDQEGSVYPTTKEYPYVLEIPRYACQRKTPLKCVNQAFVNALSVLKTCREVNGESVRTRAYGMAIATIKAFPLPIDSAEQLEKMPGCGPKIVHLWKEFASTGTLKEAEEFQKDPASKILLLFYNIFGVGASHAAEWYQKGWRTIEQVRKHKDSFTKQIKVGLEFYEDFCKTVTIEEATEIYETIVSRMPDGIKIQSCLVGGFRRGKPVGADVDMVLSPSHTHSTKHLVDVLLRILDEEFQFRLISVQEHSCGGKKGYVMLAVILSNSSKINRRVDIIVVPPAYIGSAVLGWSGGIFFLRDLKLYANSHLGLSYDSFEIINLKTGKDICPDEFNEWKDPVEAEKDIFRYFSLEYIEPKFRNTG Q09697 RGA8_SCHPO PTM: Phosphorylated by pak1/shk1. {ECO:0000269|PubMed:14506270, ECO:0000269|PubMed:18257517}. MOD_RES 676; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 680; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 682; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 686; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 694; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 698; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13A11.01c; CHAIN 1..777; /note="Rho-GTPase-activating protein 8"; /id="PRO_0000097316" MISSFSNGFWSKDYATGVKKLFDCLDNGVEENEQVKNLLKLYKEANEEFGEKLQEITKECLKGKKPENTEDGATSNKAFEGLRSEIANQGKQHIRIAKDLETLIIAPFSKMSIDHSQKLQTSQQVLTNQIKSYEKKYYTLKKTKSAYYNKCRNLEDYEEESKESNETTSEAITDLTTVSSPQQQSLLENDDDLIQLGFMEFRPEELKEVLAQVLQEIPLQDYRVPILGTYPNTCSGNIIVSWLQENLPVPTLVAAEAFGQDLIAQGFLRHMGVGGSFVNSTNFHYQWKDKAFQFAGLNSVDSLVENAKALPLVGEYLSDYISHRKLYSSETQSQRLKREVLDANKIYSESVVDLDKCRTLVEETIADHLQFLQKCETDRVLYYKDFFMDLSTIISNFLPSMKLLADQIVVYQEIIQPESDIRYILESAATGPFLPRVEIYEDYYNDIKDQIFGVDVEFLSHRDKKRVPIIVSTILSYLDLLYPTLASDEVRQNIWLVNSPLSSVHQLREALNHSSSVTKEVLSQYTPSVVIGVLKLYFLELPDSIVPSSAFELIRSIYMNHSNDTPYRLRLLQNLLSQLRRVNLATLSAIITHLNRLITLTPNKETFTINLANSLSLCISRPATWNLGIQHDKHPTKFMEDLLTYGPSIFEELRKLNSSKRVSDRVLYQSSATPRSTDVSPTRPDSISSVRSHTAVESPRSSFEELQPSEIPAESEFTLENVPTSLIRSSYALNTRKTRRNFSHSSASNESAAIFIDQDAKIVNEAVASRDSSLSGS Q09702 NRD1_SCHPO MOD_RES 93; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F7.11; STRAND 208..211; /evidence="ECO:0007829|PDB:2RT3"; STRAND 233..238; /evidence="ECO:0007829|PDB:2RT3"; STRAND 243..247; /evidence="ECO:0007829|PDB:2RT3"; STRAND 272..274; /evidence="ECO:0007829|PDB:2RT3" HELIX 196..199; /evidence="ECO:0007829|PDB:2RT3"; HELIX 219..226; /evidence="ECO:0007829|PDB:2RT3"; HELIX 251..260; /evidence="ECO:0007829|PDB:2RT3"; HELIX 261..263; /evidence="ECO:0007829|PDB:2RT3"; HELIX 267..269; /evidence="ECO:0007829|PDB:2RT3" TURN 227..229; /evidence="ECO:0007829|PDB:2RT3"; TURN 239..242; /evidence="ECO:0007829|PDB:2RT3" CHAIN 1..529; /note="Negative regulator of differentiation 1"; /id="PRO_0000081687" MSSSSPSSQSRLSVPGRTPHLPPLTIPHTVSAEGLATPNTPHALLPTGLLMGSPFVQSPTSYTSMHGLPFSTTQMAAAPAHPTTGYNVSRVTSPNVANFAPGYFPLPNNTTQPVKTVYVGNLPPNTPIDEILSCVRTGPIESAWILPEKNCAFISFLDPSHATAFFQDAALKRLTIRGTEVKVGWGKNSASNSSVLLAVQQSGACRNVFLGNLPNGITEDEIREDLEPFGPIDQIKIVTERNIAFVHFLNIAAAIKAVQELPLNPKWSKRRIYYGRDRCAVGLKQPAYFSKGQVGVVGGYPVMGYPPPSPVLQKPDLIMTGNRTVYIGNIHADTTIEEICNAVRGGLLHNIRYLQEKHICFVTFVDPVSAFRFFEMSNIHGLVIRNRRLKIGWGKHSGPLPSNIALAVAGGASRNIYIGNADDSLTIERLKEDFEEFGEIEYVNFFREKNCAFVNFTSLASAINAIDRIKQKKGYENYRISYGKDRCGNPPRTNSKSDVLSVSSDMSMPVDLVVPQQGISGFMPTNSNI Q09704 RRP4_SCHPO SPAC2F7.14c; CHAIN 1..329; /note="Exosome complex component rrp4"; /id="PRO_0000097454" MVTILKPEEFYVSSEADIVNDVSMTEMEDEIMEDEQMGLVDGEDVLEEFDKSIHQNLVTPGQLVTDDPQFMRGHGTYFEDGGIYASVAGSVQRVNKLISVKPLRSKYVPEIGDLIIGKIAEVQPKRWKVDIGAKQNAVLMLSSINLPGGIQRRKLETDELQMRSFFQEGDLLVAEVQQYFSDGSVSIHTRSLKYGKLRNGVFLKVPPALVVRSKSHAYALAGGVDIILSVNGYVWVSKHNENQHSSVSITRLEEEASESIYSNENDEIDGYTRLNISRVSICIKGLASRSLPLTQASITNFYESSLVFSNLQDLTVPKNMDQIAMEAMQ Q09706 PLD1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; Evidence={ECO:0000269|PubMed:20579106}; SPAC2F7.16c; CHAIN 1..1369; /note="Phospholipase D1"; /id="PRO_0000218826" MTIHQGGNSVIDNVPYSLNTNVNDSIYSEKGTGRKDAEDHTPSKITDLEKNVDHSIPSFPENDPKNYSEFVNLNPPKRPDLEHTRGSSWHTASENVNDLAANDSTRVQTPEFITQTMEDENVEVPPLERDERDAAAAHTSKANRNSARQMWAQLMASVRKFKREDEKPILKENLPAINLFEAGIPASLPIAKHFIRDKSGQPVLPIITDLIKVSVLDVEPKHNRIHSTFTIQVEYGTGPHAIRWLIYRQLRDFINLHSHFLFFEFQHRFSGRRMKLPKFPKEVLPYLVKLRGYQKILYSNPSDQLIDETHSISDISWESHSQDGDRTTGQPRHANNGRKKHGNFWTIQGNTLGVYLQEMIHNLQFFPEVNVLYSFLEFSSLGLYLAGAGTFHGKEGFATLKRNYSPTQYMLCCNTTMMKTRSQPFWIIVSESCIILCDNMLSMQPADVFIWDVDFEITRKNFRKAHSKDTNEKIRLSHHSFKIKNRQKVMKLSVRSGRWLQQFINSVQVAQGLTAWCEIHRFDSFAPVRTNVAVQWMVDARDHMWNVSRAIKNAKRCIMIHGWWLSPELQMRRPYSMAHKWRIDRILNEKAHEGVMVYIMIYRNIDATIPIDSFHTKEHLQSLHPNIYVIRSPSHFRQNALFWAHHEKLVVVDDAITFIGGIDLCFGRYDTPQHILYDDKPVADKTGLCEQTWRGKDYSNARVHDFFDLTEPYKDMYDRLAVPRMGWHDVSMCIIGQPARDAARHFVQRWNYLIQCKKPARKTPLLIPPPDFTTDQLTDSQLTGTCEVQVLRSAGLWSLGLVDTVEQSIQNAYVTCIEKSEHFIYIENQFFVTSTTCEGTTIENRVGDALVERIIRAHKNNEKWRGVIMIPLLPGFEGQIDLQEGGSLRLIVECQYRSICHGEHSIFGRLNAKGIDGSKYLRFYGLRGWAHLGENHELVTEMIYVHAKILIADDRVAVIGSANINERSLLGNRDSEIAAVIRDTLTIDSKMDGKPYKVGKFAHTLRKRLMREHLGLETDVLEQREYNMDGLDRDTEWKRVEVWTPDEGNAINGSAYTAEELKMKYRSQSQFTTTPDILRKAEKSMKKLDQRVSLIPSSIEFNIKTQKDKVEFEKNYEKSKKGPDVIANALVGGIPLSLKTKEDSLYELSKFSQCGEDQRPMVLKDPDHLVPEPSRPHCGNGLVFYDDIPLLEVNPISGETIPKFDASSFEDPVCDEFFEDIWSKVASNNTTIYRHIFRCVPDDEMLTWESYNEWKKYGKRFKEEQARWRQEELSNLHETHEKSENDPKNPKAGSQGSGNTSASEDSKTEKPKTRTNNGLQVPDKRVVYDLLRGIRGQLVELPLKWMSTESNARNWLSSIDKIPPLEIYD Q09711 NCS1_SCHPO BINDING 73; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 75; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 77; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 79; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 84; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 109; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 111; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 113; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 120; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 157; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 159; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 161; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 163; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 168; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SPAC18B11.04; STRAND 74..76; /evidence="ECO:0007829|PDB:2L2E" HELIX 10..20; /evidence="ECO:0007829|PDB:2L2E"; HELIX 25..37; /evidence="ECO:0007829|PDB:2L2E"; HELIX 45..55; /evidence="ECO:0007829|PDB:2L2E"; HELIX 61..72; /evidence="ECO:0007829|PDB:2L2E"; HELIX 82..89; /evidence="ECO:0007829|PDB:2L2E"; HELIX 98..108; /evidence="ECO:0007829|PDB:2L2E"; HELIX 118..135; /evidence="ECO:0007829|PDB:2L2E"; HELIX 146..156; /evidence="ECO:0007829|PDB:2L2E"; HELIX 166..174; /evidence="ECO:0007829|PDB:2L2E"; HELIX 178..184; /evidence="ECO:0007829|PDB:2L2E" CHAIN 2..190; /note="Calcium-binding protein NCS-1"; /id="PRO_0000073794" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000269|PubMed:14722091" MGKSQSKLSQDQLQDLVRSTRFDKKELQQWYKGFFKDCPSGHLNKSEFQKIYKQFFPFGDPSAFAEYVFNVFDADKNGYIDFKEFICALSVTSRGELNDKLIWAFQLYDLDNNGLISYDEMLRIVDAIYKMVGSMVKLPEDEDTPEKRVNKIFNMMDKNKDGQLTLEEFCEGSKRDPTIVSALSLYDGLV Q09725 MIS4_SCHPO MOD_RES 183; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31A2.05c; CHAIN 1..1587; /note="Sister chromatid cohesion protein mis4"; /id="PRO_0000218601" MLFEMTPETFKKVNSSNRIIKGLQYTPLASSIPLENGLQNVLYPSSKFQNEPLQLNSEESSIMQRYVDMLNPGATFVNDSETFNFYKNALSAMITEPAMPAMRVNASPVLDQKVCNSDSLSELNDFTKSLIQPSMLMCEPKEKPDASSINTNRSSSDNGFLTPSSSPRSPSCSRVFNAVQLCSPKKSKDDITTPKKRLMEDTYSPRESPSKIQRLQDVLLKQLQDTRLLISQVIEAENSEDFSSNSLFIKREDDDGKHISSHAIEKLYMALTKLSRLGACDKLLEEGSIILVKQILEKELKELPVACYSIINLHDSLTQFPNLDFILKTTALVLFIIFLVPSFKKLQNEESILHLLNILHSIFEYTVPEAIDNIVQSKTSDARTSEIQHLSVLLQKVANVLNILSKVAHEIPLSEAVVIRIVYLFPKVSTLDNSFKTKLPNCNSSSFDFLKAPLFQTLQYLFRLYPYQRDFIIEESLTNFSHLPTARSVSRTYRLSNGKSIQYYSTLFVRLIQSCSIQNLFDSEIVQSESKSTEALHSGNLTEHLKTVESILSKSRHEEYRIANHIVAYLLSRSLKQNKTESDNSFAILTKILLEDLLNMLSLPEWCGTETIIRQFAMNLVMTVTNDKQAVSSKNAALDLISLIVNKVLALFDLSLFEKHNIPAPTNFNDIISFIPSITRLNELSQVSFNHFYFLCKGDISLENILPYNYNKWFSFLLQLRKVCNDSEALKIIDNCIDKNMQKSQEGFQGPSPFKADENDEDIFIISLYHSSLFLNLKFFVSLIIGFLDSPQASLRTKCLRIINQMKTIPSILRTHPEVLAQIISKSNDQSAIVRDTVLDLLGTYIMAYRETIPQIYGCIISGISDPSTIVRKRAIKQLCEVYEATEDLNIRVDIASKLLTRSNDEEETISELSLEVLEKLWFSPASNELDCQKGYEQLTFLEKQKLRVQYFPILKLCAEPSTERHVLLVTSLKTMLTSKEEINLSTLHTQIRLLLSCLFNQLIEVVTEDQVDESTKGILYEIMSTLFVFSRAFPFLFDLSYLHLLKPYLRSASTIEEQRFLYYVVAIFRQVLPFQKEISESFLRSLESVLLQRLTKAGTATLMEIVPCLCSLFTRLNDYERLKKIVVSCLKSLEEARHSENNFQKMVRLIDLIGLFSRYGDLNRINDDWKHSLDFISPECDDAYVILLGYFQKLLKDAKGQLRIHIIDNMSRICLRETSLFISPLMLSTLDMIIAENNVNEVSVLFKSFLELLAADEDLIFEADQKLSLKGKQNVQSNKSVDRDMLKGTKDKQWIEGVSASLMQHFLPCILDSCFSKNLRYSMLGIEILKCIIHQGLVNPRMCFSTIIALESNAIKETREVAILLHTELHRRHESLIDGLYAQSADLIFSLQKTEEYQTFKLGEFSPFQSAYTIVSADKSSKSRKKLIMQILKPLKLDGIDLPSFTEEKVSFVSFCCVCLAGIPYVSIEEPLMIISTVDSVLATIGPTITGWMKKLDHERFKILAGINLCNLIYLKRYIKYAFSISDSSRPIREKKPLTLLNRGYVDLITSDAKPDIVSKLVIKLFEEENILSGEDQVEGEQLTVV Q09728 CUF1_SCHPO BINDING 11; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"; BINDING 14; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"; BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055" SPAC31A2.11c; CHAIN 1..411; /note="Metal-binding regulatory protein cuf1"; /id="PRO_0000194930" MVVINNVKMACMKCIRGHRSSTCKHNDRELFPIRPKGRPISQCEKCRIARITRHLHVKCTCNSRKKGSKCSTSSTTDLDSSSASNSSCSIPSSISEKLLPRDNVKTHCPKRSASCCGKKPDVMPLKINLESQTDFMGMPLQSQRPHSESYRMLPEPEKFKSEYGYPSQFLPIEKLTSNVAYPPNYNNYLKSPYQQPTNFPPEIQYNYSHSPQHSIQEAEEAAVYGPPVYRSGYQILYNNNTDSIAAAAATHDLYPQPDVPLTFAMLADGNYVPLPSSTNTYGPSNSYGYEININESTNHVDSSYLPHPIQLSNYFTLPSSCAQADAACQCGDNCECLGCLTHPNNATTLAALNHISALEKETISHTDLHHTFKHEVNSSNNYELTNDELAASSPLYTSSSVPPSHITTGST Q09736 CP51_SCHPO BINDING 442; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000305|PubMed:27585850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000305|PubMed:27585850}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10613}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000250|UniProtKB:P10613}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P10614}; SPAC13A11.02c; CHAIN 1..495; /note="Lanosterol 14-alpha demethylase erg11"; /id="PRO_0000052009" MAFSLVSILLSIALAWYVGYIINQLTSRNSKRPPIVFHWIPFVGSAVAYGMDPYVFFRECRAKYGDVFTFVCMGRKMTAFLGVQGNDFLFNGKLADLNAEEAYSHLTTPVFGKDVVYDIPNHVFMEHKKFIKSGLGFSQFRSYVPLILNEMDAFLSTSPDFGPGKEGVADLLKTMPVMTIYTASRTLQGAEVRKGFDAGFADLYHDLDQGFSPVNFVFPWLPLPRNRRRDRAHKIMQKTYLKIIKDRRSSTENPGTDMIWTLMSCKYRDGRPLKEHEIAGMMIALLMAGQHTSAATIVWVLALLGSKPEIIEMLWEEQKRVVGENLELKFDQYKDMPLLNYVIQETLRLHPPIHSHMRKVKRDLPVPGSKIVIPANNYLLAAPGLTATEEEYFTHATDFDPKRWNDRVNEDENAEQIDYGYGLVTKGAASPYLPFGAGRHRCIGEQFAYMHLSTIISKFVHDYTWTLIGKVPNVDYSSMVALPLGPVKIAWKRRN Q09743 RICTR_SCHPO PTM: Either Ser-203 or Ser-204 are phosphorylated as well. {ECO:0000269|PubMed:18076573}. MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 1203; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18076573" SPBC12C2.02c; CHAIN 1..1309; /note="Target of rapamycin complex 2 subunit ste20"; /id="PRO_0000072263" MKPVRRGQTDTALDISSHAKTNGDFIKKMNTTDSKRLKLLEDLKGKLEVECKIRDGAETLLQVFDTNFKKETKERKEMLKKKCTDELESSKKKIEELVSSIESFQGENGEAKTGSTSLTRSASATVSRKSSLQEKYSTRFSYKAGCSDSCSVTVSGTGELIGPTRNAHSNLTPTVIQRIDFENVNEKNNSSSEDTQPNGKRPSSLQSNFSQFPLNPWLDNIYKACLEGSMKDVIDSSNNLCEYLHEHSDPAYAKNFSLITPTILSMLELNVSEVTASVYRLLRHLFLDATAFSCCQMLNLPWILSKSLLSGTDAYQIEREQAFRLIRTLYFLSSTEGHEDYLSGITRTIISICEHVSDVSRGIAVETLIELMIIRPKILFKANGLRVLMISLIDGSISENLAASAALALVYLLDDPESACYVNLPYDIGILLSPFTSSSSRDTFNSSEEQSEQAAKAMKSSAKVASVLLNSWSGLLALSTNDFQALRSIVDTLRVPSFAPRSDVIDLFFLIFQVEYSSWSESFLAGKRLTVVKNQAVSNDDNINMVNIPDGSNKKYMSLRQHFTAVLLFIFLELGLVESIVCMIRASDDPSASRKATYLLGEVLRLSDELLPIHLGAKIQSLPSLFNMASQFTAEDRFVATSVLQSIESLNRVKFHSATQPFSQTTSLLFKEQKTDGSFRGQRQVEHVKLKMGMQIDDSHFRSMLAETNVLATKNYQKWRWDTLVQIMEGPLLSPKRIDETLRTTKFMRRLLAFYKPFSNRFSSIQNTKPNQKFIKVGCLVFRTLLANPEGVKYLSESKVIKQIAESLSQIDGYSEQVSEPIFSNSRLQKTLTHGYFPMLKVLSSQKEGHAIMERWRIFTTLYHLTELRNRDDLIIIFLTNLDYRLEGHTRIIFSKALNTGQQAVRLTATKHLAALINSESANDNLNHWAISLLIFQLYDPCLEVCKTAVKVLNEVCARNENLLAQVVQLQPSLAHLGEIGSPLLLRFLATTVGFHYLSEINFIEHELDNWYHHRNIDYVDLLEQNFFLSFVSNLKIIDKKNNEPDENILPLHFYGELVKSPQGCEVLESSGHFESFMGTLVEFYDKPLGNEAIRQLKSALWAIGNIGKTDQGITFLINHDTIPLIVKYAENSLIPTVRGTAYFVLGLISRTSKGVEILESLHWYSLMSLMGTSQGICIPRHAGQVLSTPRRNVEFVNERVPTPEFSSLLSSLTNSEREVIRLVSNLSNHVLTNESARQLTKIRSKNAKVFSSKRLVKACMTILGKFHYRVQIQQFVFELFPYSVLLSSSTSQDLNESPSRPNNLSISA Q09748 DNM1_SCHPO BINDING 33..40; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 170..174; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 239..242; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; SPBC12C2.08; CHAIN 1..781; /note="Dynamin-related protein dnm1"; /id="PRO_0000206589" MEQLIPLVNQLQDLVYNTIGSDFLDLPSIVVVGSQSCGKSSVLENIVGKDFLPRGTGIVTRRPLILQLINLKRKTKNNHDEESTSDNNSEETSAAGETGSLEGIEEDSDEIEDYAEFLHIPDTKFTDMNKVRAEIENETLRVAGANKGINKLPINLKIYSTRVLNLTLIDLPGLTKIPVGDQPTDIEAQTRSLIMEYISRPNSIILAVSPANFDIVNSEGLKLARSVDPKGKRTIGVLTKLDLMDQGTNAMDILSGRVYPLKLGFVATVNRSQSDIVSHKSMRDALQSERSFFEHHPAYRTIKDRCGTPYLAKTLSNLLVSHIRERLPDIKARLSTLISQTQQQLNNYGDFKLSDQSQRGIILLQAMNRFANTFIASIDGNSSNIPTKELSGGARLYSIFNNVFTTALNSIDPLQNLSTVDIRTAILNSTGSRATLFLSEMAFDILVKPQLNLLAAPCHQCVELVYEELMKICHYSGDSDISHFPKLQTALVETVSDLLRENLTPTYSFVESLIAIQSAYINTNHPDFLGVQGAMAVVLSRKEQNRLMLSQENDEPISSALDTVKPDGIELYSSDPDTSVKSITNKATNEITTLKSDDSAKMQPLDVLASKRYNNAFSTETAERKTFLSYVFGANNATRKAMSIDKSSSYPLNDSLSGGDTNHKNNHPLKMTDLSNEVETMALEDMSEREEVEVDLIKELITSYFNLTRKIIIDQVPKVIMHLLVNASKDAIQNRLVSKLYREDFFDTLLIEDENVKSEREKCERLLSVYNQANKIISTVF Q09751 LGUL_SCHPO ACT_SITE 149; /note="Proton donor/acceptor"; /evidence="ECO:0000250" BINDING 14; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 18; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 75; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 79; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 99; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 103; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 103; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 149; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000269|PubMed:11859360}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19071; Evidence={ECO:0000305|PubMed:15042280}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15042280}; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:15042280}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:15042280}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15042280}; Note=Binds 1 zinc ion per subunit. Cobalt, nickel and manganese ions can also function as cofactors. {ECO:0000269|PubMed:15042280}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 mM for methylglyoxal (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:15042280}; KM=0.8 mM for glutathione (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:15042280}; KM=0.24 mM for phenylglyoxal (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:15042280}; Vmax=2 mmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:15042280}; Vmax=197 umol/min/mg enzyme with phenylglyoxal as substrate (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:15042280}; SPBC12C2.12c; CHAIN 1..302; /note="Lactoylglutathione lyase"; /id="PRO_0000168086" MASTTDMSTYKLNHTMIRVKDLDKSLKFYTEVFGMKLIDQWVFEENEFSLSFLAFDGPGALNHGVERSKREGILELTYNFGTEKKEGPVYINGNTEPKRGFGHICFTVDNIESACAYLESKGVSFKKKLSDGKMKHIAFALDPDNYWIELVSQSETKPKANISNFRFNHTMVRVKDPEPSIAFYEKLGMKVIDKADHPNGKFTNYFLAYPSDLPRHDREGLLELTHNWGTEKESGPVYHNGNDGDEKGYGHVCISVDNINAACSKFEAEGLPFKKKLTDGRMKDIAFLLDPDNYWVEVIEQK Q09756 HXK1_SCHPO BINDING 90..95; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P19367"; BINDING 160..161; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 177..178; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 213..214; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 237; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 240; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 269; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 302; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 307..308; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 344..348; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557"; BINDING 419..423; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P35557" CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; CATALYTIC ACTIVITY: Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for D-fructose {ECO:0000269|PubMed:9790975}; KM=9.4 mM for D-glucose {ECO:0000269|PubMed:9790975}; KM=0.2 mM for D-mannose {ECO:0000269|PubMed:9790975}; SPAC24H6.04; CHAIN 1..484; /note="Hexokinase-1"; /id="PRO_0000197609" MSLHDAYHWPSRTPSRKGSNIKLNKTLQDHLDELEEQFTIPTELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLPQELKVGTREALFDYIADCIKKFVEEVHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKYDFPEDMNMIINCEWCDFDNQHVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFENLDETQTLFEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPSMIVGTDGSVYNLYPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSALEAKGKALTSDILAEHLKN Q09763 GEF1_SCHPO SPAC24H6.09; CHAIN 1..753; /note="Rho guanine nucleotide exchange factor gef1"; /id="PRO_0000080988" METLKADLSDMSDSPEYFETLANRDLPRLPGTSKLHRAACIKRKSINLSLPSNSYSLSYRQSDDTDGDVSESQSEYRLSSGRRSRASFARALQDPQTPNTPPVSSQHRRFFSEGSFNLPNSNMSHSLNGDSTASNSSTLTPNRIYGDRNRQDYAQSSRYTLPSLPSSPSYNCPTTLRKIHTNTSSNGTSRRVSGLGSFMAQNSSETSSNRTSAYLPGSSTDEQEKRSSVTLASMPSSHSSTASLLSPLDTTSFSTKLDSTILALETDESLSRTISYATTSLPSTPGKRLSKESLAMSEASSINPEYKRIKKRANLIKELVTTEAAYLNDLIAIQQSYGLRVKECSALNPVDAQTVFGDIESLLTFTVEFHSRLYQAGEGSWRVNLDTQLIDPLPCNLGLIFLESLSEIGQIYTGYCNRQDSVFKIITKWREKPATASWIMEGDKIVQKYTNAWDLGSLIIKPLQRLLKYPLLLQKIIDVTPESSSERPDLVLSYQLLQELISGINQKQKPSHKRGSLSASHKRDAAWSLLYKATSNKSRPTTTSTELKTDARLNFQRQVLQDFRQRFAILKALHATLETWYVTVHRGFSVFEKVLAELEGLSALEPEDKPVDTWRKYHLLAHMMTANLPSQIQTSLNSSILNPITNILRVIQKVIQFIISAEFVIPAQKLEAISTLVEKEFHSVVYHFIGIQRSLYENYAQGFLFLIPQDMRDSILEETQDYAELVRAFEPMHYDDEVLLEELMKSVSLAARV Q09772 RDH54_SCHPO BINDING 235..242; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPAC22F3.03c; CHAIN 1..811; /note="Meiotic recombination protein rdh54"; /id="PRO_0000074345" MKRRATFQCPLIESTIKHQSTNYTKTETATTSHEVSENANEHKGKSNIDINKIAYYNVVWRKITMKKHKTWEGDGFLVREDSNLTLYNSDFTRLGSCHSRVPQIKEGELLRISGKEISIEKEISAESYEAGTHIDDSLRDVHMPEMKRKFKPPLRPNTMYQTISALPKPRHDPTVLGALVMSRPKTWDPRTHVDVVIDPFLSKHLYSHQREGVSFLYDCLLGMEGKCGYSAILADEMGLGKTLQTITVVWTLLKQSYYANRSSTINNAMVVAPVTLLKNWENEFYNWLGHERIHVYIARCAEDFQEFTSNKTYSIIITGYETVCTYLRNYGCGIDIDLLICDEAHRLKSMSSQTWITLNKLKTRKRLLLTGTPLQNDLSEYFSMVNFIIPGSLGTPNSFKAQYERPILRSRSMNASSRDISLGAARLQRLFEFTSNFTLRRKANILAKHLPPRTDIVLFIKPTHQQENVYGHVLDGFKSSVDQKGYYLKILTRLSKICNSTILLRNEKENFLSTELQDKHVFEQENMLLSSSKLQILAALLKSFQRGCQKAVIVSQYKETLELIELFLSILHVRFCKLLGSTPFSERDLIVHNFNTSSFKEFSVLLLSSKAGGCGLNLTGSTRLIIYEPSWNPAQDLQALSRIYRSGQKRPVCIYTFLSSGMLDERIFIRQNTKQGLSSSFIDSDASQKKNFFTGEDIKTLFSYSKTETCLTYELAFDSDEIDSLTKKKDPLTKIDHTIDSPNTKEKDKEISSWKKASEYMDTNLGKKCPENAFQGWTWQFPNDLSIMNGVEDYIPLEPLPINCLMHKKFE Q09790 DDP1_SCHPO BINDING 42; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 42; /ligand="5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate"; /ligand_id="ChEBI:CHEBI:58628"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 42; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 62; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 62; /ligand="5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate"; /ligand_id="ChEBI:CHEBI:58628"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 62; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 73; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 73; /ligand="5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate"; /ligand_id="ChEBI:CHEBI:58628"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 73; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 73; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 89; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:O95989, ECO:0000250|UniProtKB:Q99321"; BINDING 89; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 93; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 109; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 111; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 111; /ligand="5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate"; /ligand_id="ChEBI:CHEBI:58628"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 153; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 176; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 176; /ligand="5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate"; /ligand_id="ChEBI:CHEBI:58628"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 176; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 193; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 193; /ligand="5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate"; /ligand_id="ChEBI:CHEBI:58628"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 193; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321"; BINDING 195; /ligand="P(1),P(5)-bis(5'-adenosyl) pentaphosphate"; /ligand_id="ChEBI:CHEBI:62041"; /evidence="ECO:0000250|UniProtKB:Q99321" CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:10419486}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-tetraphosphate + ADP + 2 H(+); Xref=Rhea:RHEA:51724, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58450, ChEBI:CHEBI:63740, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10090752}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP + 2 H(+); Xref=Rhea:RHEA:30527, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:62041, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10090752}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q99321}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 nM for PP-InsP5 {ECO:0000269|PubMed:10419486}; KM=19 uM for Ap6A {ECO:0000269|PubMed:10090752}; KM=22 uM for Ap5A {ECO:0000269|PubMed:10090752}; Note=kcat is 2 sec(-1) for Ap6A. kcat is 1.7 sec(-1) for Ap5A.; SPAC13G6.14; CHAIN 1..210; /note="Diphosphoinositol polyphosphate phosphohydrolase aps1"; /id="PRO_0000057068" MLENNGSVILMEPDHLRTAVNRSMTSREGRTKNRFNPITGARLAAGVVALSADKRKVLLVSSAKKHPSWVVPKGGWEADESVQQAALREGWEEGGLVGHITRSLGSFKDKRPTDTIDRRKKYLKQLMSKSSGNDVSTNTELGAEAEKLLLPPRAECEFFEVIVERLEDNYPEMRKRRRKWMSYQEAKEALTSRKDILAALEKSSIIKEEN Q09794 PYR1_SCHPO ACT_SITE 338; /note="Nucleophile; for GATase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 422; /note="For GATase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 424; /note="For GATase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" BINDING 101; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 309; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 311; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 342; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 380; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 382; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 383; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P0A6F1"; BINDING 594; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 634; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 640; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 641; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 671; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 673; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 678; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 704; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 705; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 706; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 747; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 747; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 747; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 761; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 761; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 761; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 761; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 761; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 763; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 763; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1169; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1208; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1210; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1215; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1240; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1241; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1242; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1243; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1283; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1283; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1283; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1295; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00968"; BINDING 1295; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1295; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1295; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1295; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1297; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1297; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"; BINDING 1988; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 1989; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2016; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2037; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2065; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2068; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2098; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2160; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2199; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786"; BINDING 2200; /ligand="carbamoyl phosphate"; /ligand_id="ChEBI:CHEBI:58228"; /evidence="ECO:0000250|UniProtKB:P0A786" CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000305|PubMed:8590465}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000305|PubMed:8590465}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000305|PubMed:8590465}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000269|PubMed:8590465}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; MOD_RES 1119; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1881; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1885; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22G7.06c; CHAIN 1..2244; /note="Multifunctional protein ura1"; /id="PRO_0000199510" MSGLLPSLSSSFPLVQSEALGMPRTHGPKPSENDPKEPTCSPSPAFYSVNGEMKDYKLMALELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDRRILDEISGLPKYFESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLIQKDESPINPSSITGLGKDWSTAFEDIPWKNPNTENLTSQVSIKEPKLYEPHPTTAIKKADGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVLESKTVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVKRSADAKSLQPFKLPGGTIEENRSRHPLVDAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDSIYVTFGGQTALNVGIELKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATSPQVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKLGLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNTGFNVKDALMSIDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLLKTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDKGVMVLGSGVYRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANNIALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVAREGKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPIQPYPDVDLPRDYVAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKNILISIGSYKEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANNEYSLSAHLANNMIDMYINLPSNNRYRRPANYISSGYKSRRLAIDYSVPLVTNVKCAKLMIEAICRNLDFSLSTVDFQSSFQTANLPGLINISAFLPEFTSEAVSDYTKECIASGFTMARFLPFSTSSTLADKDSLSAVKKLALDHAHCDYNFSVIASSTNEVTISELTSESGCLFFHFEKDDSGIDHVTAVASHFNVWPDTQTVMTDAKSTTLASLLLLASLHNRRIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQNDYPGATFLPTADDQVEIWNKLSYIDCFSIGSIPSRLAKFVGNTAFTGFGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRLHDQDDSGVQLEVDRSVSWSSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGELNFEHTYGRDYSSASLADKSKATRKVSALMSPGLPHAAPSLAEAFGQAPENKAHPDISLNMTPNFKPSHELVQLINSSPFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFIGDLKYGRTVHSLARLLAFWHVELHLVSPEQLALPDDVKDDIRANGLNFIEHRELTKEVVAQSDVLYCTRVQKERFASVDEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNREISEEVDFDQRRAAYFRQMRYGLYIRMALLACVMGATEVAN Q09803 VPS4_SCHPO BINDING 169..176; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; SPAC2G11.06; CHAIN 1..432; /note="Suppressor protein of bem1/bed5 double mutants"; /id="PRO_0000084769" MSNPDCLSKAISLVKTAIDNDNAEQYPDAYKYYQSALDYFMMALKYEKNEKSKEIIRSKVIEYLDRAEKLKVYLQEKNNQISSKSRVSNGNVEGSNSPTANEALDSDAKKLRSALTSAILVEKPNVRWDDIAGLENAKEALKETVLLPIKLPQLFSHGRKPWSGILLYGPPGTGKSYLAKAVATEAGSTFFSISSSDLVSKWMGESERLVRQLFEMAREQKPSIIFIDEIDSLCGSRSEGESESSRRIKTEFLVQMNGVGKDESGVLVLGATNIPWTLDSAIRRRFEKRIYIPLPNAHARARMFELNVGKIPSELTSQDFKELAKMTDGYSGSDISIVVRDAIMEPVRRIHTATHFKEVYDNKSNRTLVTPCSPGDPDAFESSWLEVNPEDIMEPKLTVRDFYSAVRKVKPTLNAGDIEKHTQFTKDFGAEG Q09808 SMN_SCHPO SPAC2G11.08c; HELIX 11..35; /evidence="ECO:0007829|PDB:7BB3"; HELIX 122..124; /evidence="ECO:0007829|PDB:4RG5"; HELIX 125..149; /evidence="ECO:0007829|PDB:4RG5" CHAIN 1..152; /note="SMN complex subunit smn1"; /id="PRO_0000218907" MDQSQKEVWDDSELRNAFETALHEFKKYHSIEAKGGVSDPDSRLDGEKLISAARTEESISKLEEGEQMINQQTETTLEGDTHIQQFADNKGLSDEKPETRAAETHQEFMEVPPPIRGLTYDETYKKLIMSWYYAGYYTGLAEGLAKSEQRKD Q09811 HUS2_SCHPO BINDING 555..562; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:12724426}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; SPAC2G11.12; CHAIN 1..1328; /note="ATP-dependent DNA helicase hus2/rqh1"; /id="PRO_0000205058" MTVTKTNLNRHLDWFFRESPQKIENVTSPIKTLDFVKVKVSSSDIVVKDSIPHKSKNVFDDFDDGYAIDLTEEHQSSSLNNLKWKDVEGPNILKPIKKIAVPASESEEDFDDVDEEMLRAAEMEVFQSCQPLAVNTADTTVSHSTSSSNVPRSLNKIHDPSRFIKDNDVENRIHVSSASKVASISNTSKPNPIVSENPISATSVSIEIPIKPKELSNNLPFPRLNNNNTNNNNDNNAIEKRDSASPTPSSVSSQISIDFSTWPHQNLLQYLDILRDEKSEISDRIIEVMERYPFSSRFKEWIPKRDILSQKISSVLEVLSNNNNSNNNNGNNGTVPNAKTFFTPPSSITQQVPFPSTIIPESTVKENSTRPYVNSHLVANDKITATPFHSEAVVSPLQSNIRNSDIAEFDEFDIDDADFTFNTTDPINDESGASSDVVVIDDEEDDIENRPLNQALKASKAAVSNASLLQSSSLDRPLLGEMKDKNHKVLMPSLDDPMLSYPWSKEVLGCLKHKFHLKGFRKNQLEAINGTLSGKDVFILMPTGGGKSLCYQLPAVIEGGASRGVTLVISPLLSLMQDQLDHLRKLNIPSLPLSGEQPADERRQVISFLMAKNVLVKLLYVTPEGLASNGAITRVLKSLYERKLLARIVIDEAHCVSHWGHDFRPDYKQLGLLRDRYQGIPFMALTATANEIVKKDIINTLRMENCLELKSSFNRPNLFYEIKPKKDLYTELYRFISNGHLHESGIIYCLSRTSCEQVAAKLRNDYGLKAWHYHAGLEKVERQRIQNEWQSGSYKIIVATIAFGMGVDKGDVRFVIHHSFPKSLEGYYQETGRAGRDGKPAHCIMFYSYKDHVTFQKLIMSGDGDAETKERQRQMLRQVIQFCENKTDCRRKQVLAYFGENFDKVHCRKGCDICCEEATYIKQDMTEFSLQAIKLLKSISGKATLLQLMDIFRGSKSAKIVENGWDRLEGAGVGKLLNRGDSERLFHHLVSEGVFVEKVEANRRGFVSAYVVPGRQTIINSVLAGKRRIILDVKESSSKPDTSSRSLSRSKTLPALREYQLKSTTASVDCSIGTREVDEIYDSQMPPVKPSLIHSRNKIDLEELSGQKFMSEYEIDVMTRCLKDLKLLRSNLMAIDDSRVSSYFTDSVLLSMAKKLPRNVKELKEIHGVSNEKAVNLGPKFLQVIQKFIDEKEQNLEGTELDPSLQSLDTDYPIDTNALSLDHEQGFSDDSDSVYEPSSPIEEGDEEVDGQRKDILNFMNSQSLTQTGSVPKRKSTSYTRPSKSYRHKRGSTSYSRKRKYSTSQKDSRKTSKSANTSFIHPMVKQNYR Q09814 TGS1_SCHPO CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in snRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-ribonucleoside in snRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:78471, Rhea:RHEA-COMP:19085, Rhea:RHEA-COMP:19087, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:172880; Evidence={ECO:0000269|PubMed:15590684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78472; Evidence={ECO:0000269|PubMed:15590684}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in snoRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-ribonucleoside in snoRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:78475, Rhea:RHEA-COMP:19086, Rhea:RHEA-COMP:19088, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:172880; Evidence={ECO:0000269|PubMed:15590684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78476; Evidence={ECO:0000269|PubMed:15590684}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-ribonucleoside in snRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-ribonucleoside in snRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:78479, Rhea:RHEA-COMP:19087, Rhea:RHEA-COMP:19089, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623, ChEBI:CHEBI:172880; Evidence={ECO:0000269|PubMed:15590684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78480; Evidence={ECO:0000269|PubMed:15590684}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-ribonucleoside in snoRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-ribonucleoside in snoRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:78507, Rhea:RHEA-COMP:19088, Rhea:RHEA-COMP:19090, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623, ChEBI:CHEBI:172880; Evidence={ECO:0000269|PubMed:15590684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78508; Evidence={ECO:0000269|PubMed:15590684}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.57 mM for m(7)GDP {ECO:0000269|PubMed:15590684}; KM=8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15590684}; SPAC2G11.15c; CHAIN 1..239; /note="Trimethylguanosine synthase"; /id="PRO_0000116412" MNKNEELDEDELLKKCIICPPVPKALKKYWNNRYNLFSRFDEGIWLDYQSWYSVTPEKVAVAIAKSVVDFIQPELIIDAFSGCGGNTIQFAKYCPVISIEIDPIKIAMAKHNLEIYGIPSSRVTFIQGDVLDTFKSLQFAKDYRSLVFMSPPWGGPSYSGKTVYSLNDLNPYAFDVLFKEATRISPYVAAFLPRNTDVKELAAYGSIHNKPYITNFLFEGYAKAICCYFNMKGAIARKI Q09815 PPK5_SCHPO ACT_SITE 644; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 524..532; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 547; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 678; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16C9.07; CHAIN 1..836; /note="Serine/threonine-protein kinase ppk5"; /id="PRO_0000086041" MVGLISTSETLPKQESKSSSAPVSNFLSPNNLTEQTCSPLRAHSTFKEPVFLLSQRQYSHNSKILTELINSVKRPNKPDQNEEKSAVGIEEKSFKDEHLAQKKGLHHFADLKEIFLNKNLSTLDGLQDASLHDNIQSGKLDNPVISQNRRIVLEKLANPNSSKEYETIPTVENRHPLNKLSKTKTLAYEETINQLDETPGGTNYPMNKKKTLSSETNKYEYPQQSKFHECSQFASPRSSIVNGPRTLGKNSKRADDTARMASRMKPSNFNNNIQSSSYGHASQSTKLTSQRDNDHQKDLNFSPYKSIPLNNRPYSPMSEIVGFSGSTTPLDTYGNRPSGKKFNKNSKFRPPGSTISSYSSASTLRRLPRAPGSKVHAERQNSTFNSGISLRALRKEMGNTAPVSSNQLLKDADLVMENLSTRNTEKVLREVNILKRLRESCVAITAKSYDTLDERKIRSLTTFEYLEIKNFQKIYFTGSENCQKLSKQIPLDECNEALFDDDNGDYKAIQGDHLLYRYEIIDTVGKGSFGQVLKCIDHKRGQVVAIKVIKNRQKFHGQTLVEVGILKRLCEADPADKNNVIRYLSHFDFRGHLCIVTELLGSNLFDVIRENNYKGLPLIVVKSFALQGLQALRLLQGQNIIHCDLKPENLLLSHPLKARIKLIDFGSSCFYNEKVYTYLQSRFYRAPEIILGLEYGKEIDIWSFGCILAELFTGVPLFPGGNETEQLGYIMEVLGPPPMALIRNSTRSKAYFDSEGKPHPITDSHNRLLVPSTRTFSQLLNTKQASFLDFLSKCLKWDPKDRITVDSALQHEFILGKTSQKPMVSKGSHPLPDLPV Q09820 RENT1_SCHPO BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 47; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 58; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 61; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 80; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 86; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 104; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 107; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 130; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 134; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"; BINDING 397; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q92900"; BINDING 417..421; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q92900"; BINDING 593; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q92900"; BINDING 630; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q92900"; BINDING 761; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q92900" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P30771}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P30771}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q92900}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q92900}; SPAC16C9.06c; CHAIN 1..925; /note="ATP-dependent helicase upf1"; /id="PRO_0000080715" MSLGLQPNNDISSLVSSKNMTSENGLEHQFEELLVEKQYSEEHCAYCHIKNPNSILKCLHCNKWFCNVRGKSGASHIISHLVRARHKQVALHSHSSLSDTVLECYNCGTRNVFLLGFIPAKAKTVVVLLCRQPCARASIAKDMNWDLTQWQPIISDRQFLPWLITPPSEEEQKLAIPITSQQMVRLEELWRKDPNANLEDLDKPIEDDSLPSVELRYKDAHAYQAVLSPLIQAEADYDKRLKESQTQKDVVVRWDQAINKRYTAWFLLPKLESGEIRLAIGDEMKLTYEGELRAPWSSTGYVIKIPNNVSDEVGLELKRSDKVPIECTHNFSVDYVWKSTSFDRMQTALRLFATDGSRLSSFLYHKLLGHDIPPSFLKPKLPSDLSVPNLPKLNASQSEAVRAVLSKPLSLIQGPPGTGKTVTSASVVYHLATMQSRKRKSHSPVLVCAPSNVAVDQLAEKIHRTGLRVVRVAAKSREDIESSVSFLSLHEQIKNYKFNPELQRLLKLRSENNELSIQDEKKLRILVAAAEKELLRAAHVICCTCVGAGDRRISKYKFRSVLIDEATQASEPECMIPLVLGAKQVVLVGDHQQLGPVVMNKKVALASLSQSLFERLIILGNSPFRLVVQYRMHPCLSEFPSNTFYEGTLQNGVTTSERIARHVDFPWIQPDSPLMFYANFGQEELSASGTSFLNRTEASTCEKIVTTFLRSNVLPEQIGIVTPYDGQRSYIVQYMQNNGSMQKDLYKAVEVASVDAFQGREKDFIILSCVRSSEHQGIGFVNDPRRLNVALTRAKYGVIVLGNPKVLAKHALWYHFVLHCKEKGYLVEGTLNSLQKFSLTLTPPQKPQKFKRDLNVQRSLSPIQNAGSAMLPSFSNLPNLYSSSYLEEWNVFAQYKRRESNATDFEDFRSQVGDDESKFDEPTRF Q09822 CDC15_SCHPO MOD_RES 331; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 529; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 636; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 639; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 700; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 774; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC20G8.05c; CHAIN 1..927; /note="Cell division control protein 15"; /id="PRO_0000089443" MEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV Q09823 REC10_SCHPO SPAC25G10.04c; CHAIN 1..791; /note="Linear element protein rec10"; /id="PRO_0000097220" MDIFSEFLNCLSSDGTLNESSIYKTYQILESLNPKDVDTKENYIKLSNTFSTLGSGVGFQDNLLIEMFKILTVLFFKTRSTDLGDLLIESFTSLEIEKLMRVKKTIGSIVLTKGIQELQEIELPKVGFNCMTYDESIFQGISLERLILQLMSIFIAKCEENKLWLVNNRKDLDLRVIGQRLLHRDFACRFLSGLFISRFSVSGDTDESKHQNGIRLQLFIDFSKFETRLTMQILKADRIFSTCVANTVHAYEGLFSSGSNIDSTIATLVLEPRDLIVYRKGFALLQIPWTSVTTIDKIKKVKSLKIITEVSSLDEFVFQCKDGDKFDELFSTSEEIMNKLLPAIIVSPKLTLRNRSIIQIKEGESKLPNTSKQASQNLPHLDDELAYQRFEDQVIDKSVCDDECTNTENTPSSNIPADVKDSLSADDYAYDTKRKTQIEDLEEDQNKSKIASKDGTNLKEINSVPEFSDENVINQTGPAKKTPVQRRKDGKFAKSTKRKKQKSLKPDTENQESSVKNKKAKSNVNLQYSPKTPICKINDETLKPPTIANIAGHKQMNHLTSENIETPVPVPNGNWYNGVKHETATDIFTTCHDGNNSLKSSVWKELLKEKHWKQESKPQLTGNSRQIDLSTFVKQANTPNITSLLDGTCSSPPNNECFNDKEPDSSSSTLISDRQELEYRNPNAETVKLEEIPYNKFFKTVEKNEAYNPSSKSATIDGLQRYTSMIGNQIYEGILQNEKELRSKLEAYHINCNKVIKEFSKRQTARYKIIEKELAQIEVNLVSQIDSLMFK Q09825 SAD1_SCHPO MOD_RES 236; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000255" SPBC12D12.01; HELIX 90..99; /evidence="ECO:0007829|PDB:6A6W" CHAIN 1..514; /note="Spindle pole body-associated protein sad1"; /id="PRO_0000218915" MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSNIRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRKSQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKVGGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLSTGAEVLPALTSKRYVRRPSAFIPRFTSYFFDSLVVRGHEPSIALTPNNAVAMCWSFQGSEGQLGISLSRPVYVTNVTIEHVQHKIAHDLSSAPKDFELWVQGMSSKMFVLLGKARYSLTEDSIQTFSFESSNYIVAEPIQNVILKIKSNWGNPNYTCLYQVRVHGTVPNADEQPIPSLGEKAESTAENTGQDSS Q09826 SDS23_SCHPO PTM: Phosphorylated during the stationary phase of the cell cycle. {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9242669}. MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 329; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 333; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9242669"; MOD_RES 341; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC646.13; CHAIN 1..408; /note="Protein sds23/moc1"; /id="PRO_0000097651" MPLSTQSSDSLSSAGRQSFGVNSVSDFLAQFPIPTNLPSNKWQDIPVTFLHDNEIALIDPETSMEEASSILIDRDLSALPIVAAKGSNEIATTFDYADLNSFLLMVVGFDDFNDGRFKKVAEDIRAGKVITAYEVAKLGKNKDDFITIPHTTSLGRLAEILSSGIRRVAVTNEQGELSFMASQRSIIRFLWNNIRAFPDLEPLMSRTIHSLDIGSTDITCISGDQKVAAALRQMNQTGIGSLAVVDAQFRLLGNISLVDVKYVTRSSSVYLLNKSCAHFLSVIKSEQGIRAGKDSAPAFNIYESSTFAFTLAKLVATQCHRLWLVQSPSCPPSPKNNAHLSPGSMGGVKVNQLLGVVSLTDIISVLYAHMKGTLPPAPHSAPSLRHGRRGSTSSHRSHSKASVDTQRR Q09838 PRZ1_SCHPO PTM: Phosphorylated. Dephosphorylated by calcineurin which leads to rapid translocation from the cytoplasm to the nucleus. {ECO:0000269|PubMed:12637524, ECO:0000269|PubMed:18257517}. MOD_RES 543; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 546; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4G8.13c; CHAIN 1..681; /note="Transcriptional regulator prz1"; /id="PRO_0000046814" MERQRSEEANRRFKDLNPSSLYDNLSKPDLGGSSELHTYMNDTSLADIPLFEDTLASEVSSSLISNPSKNNIQHLHPNTSEPFKTSSKSDEYDSYPRTGNVPTFSFTELNDTSVSGFGSQAVFENSVSPLSNPSNSPQAFDLTQGSSSTHNANDFTVNNVGSRRQSIYEFNIGIPSSNIDSSQFLPVSRAIAASEISPSSSPQLLTSFLPSGSVSNPSSPYLQGSVGALYEADAFNFVDVMSQASGTEVDSERFPSVDFEDPSLLMENQQNITGTGSFADYLQPPSSGSLGAFTNASPGESNTGIDFDTDNTNLNPSVDLLSNHSTPSFIFENSPSAEFSHQSSPYLVPNSGRTLNSENARESTIRSVNSPFSEDHADASLTTHVFDPISPTALSNSVLNYDSNNFSGTPQINVVPSSPSKSQSGPSLPANPLLQTDISITYSQSASPVSGQPAMNENSYDLQNANLCAPEMSPTYTARHRSNSAGSRFDAYEPIPQLYTHFSHSSECLSVNQDTELLGKIENDNSKSNDYLSVRNTRPRSRSLNSLVGNKSENSSSSKAKSESKSQGNYVCTFAGCNKRFTRAYNLKSHMNTHTNYRPFQCSICKKSFARQHDKRRHEQLHTGIKAFACVTCNQRFARMDALNRHYKSEVGQNCLRTATERGIQVPPSRKTAVASTSKQK Q09843 RFC2_SCHPO BINDING 59..66; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC23D3.02; CHAIN 1..340; /note="Replication factor C subunit 2"; /id="PRO_0000121759" MSFFAPRNKKTEQEAKKSIPWVELYRPKTLDQVSSQESTVQVLKKTLLSNNLPHMLFYGSPGTGKTSTILALSRELFGPQLMKSRVLELNASDERGISIIREKVKSFAKTTVTNKVDGYPCPPFKIIILDEADSMTQDAQAALRRTMESYARITRFCLICNYMTRIIDPLSSRCSKYRFKPLDNENMVKRLEFIAADQAVSMEPGVVNALVECSGGDMRKAITFLQSAANLHQGTPITISSVEELAGAVPYNIIRSLLDTAYTKNVSNIETLSRDVAAEGYSTGIILSQLHDVLLKEETLSSPVKYKIFMKLSEVDKRLNDGADETLQLLDLLSSISVVC Q09849 ARP42_SCHPO SPAC23D3.09; CHAIN 1..424; /note="SWI/SNF and RSC complexes subunit arp42"; /id="PRO_0000089146" MEEIPSLVIDPGSCWTRFGYAGEESPMTILPSYYGVRSDVTGRNKYVVDELQIHAPIPGMEVKNGKSNGIIQDWESTLYTWERGLKEKLQVNPTEYAMMITEPSWNPQSVRQQIMEAAFEQLHVPAFYLTKQAVCVAFANSKSTALIVDIGSDNASVTPVVDGLIIRKGIFKQSLAGDFLNANIEQLFNTMNIEFPPHYRIARKSVAIQQSGNMANGSADAVKPAVLYPPIQDLTSSYEIFQKRRVIEEWKESVLDVLDTPFDEAKASSRNPKPFEFPDGVTHKFGQERFRISEILFNPSFSASRSAETTPPQGSVGLHELVYQSILACDSELRSPLLNNIVVTGGTSLIPGLSERLQAEVQRLATGSRINVHTAETASATSNAVWFGGSILASLDNFQHLWVSKQEYDEVGVDRALFVEKRCK Q09850 ENG2_SCHPO ACT_SITE 457; /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"; ACT_SITE 533; /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"; ACT_SITE 537; /evidence="ECO:0000255|PROSITE-ProRule:PRU01352" BINDING 461; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 531; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 533; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 537; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 614; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1" CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:17933563, ECO:0000269|PubMed:19542306}; SPAC23D3.10c; CHAIN 1..706; /note="Ascus wall glucan endo-1,3-beta-D-glucosidase"; /id="PRO_0000215818" MDVLVPIYTGPINPVFPSRAHPSPPLGLTSNLFPIQTNKFYGNLYIGTRHNPSWSHPYSVTWLNGSSYYGLAISHIDDSQRVFGPDPESVPCQYYFNPAGLYSIIISAREFASGNLLSLDQSRHFSIQATLSATTSGSGTIILPIVAGMGFVSGYYTNLTPVFNSSILFSSITKINFSRGYKYRIQLTDGKIWFLYAFPTSSSSTFNLTLASNSQLTTSTKFTGLIQICKVPNESVNNSYPDTIYDASAGVYTTSISLSAQVSGTTGEYWFRFATAGYTNLNPLMFALPHHMQSFGSDTQAYKTGLGLASTTMGIMFAYATKTWHLIEKNLPTQVGFLPIPWNGGSNTYSPTALAAIRAACATDINFDVVNASNLDSMYTSGKIVAMYAQVCLVASRILGDSTLTNTGLTKLKQAMARFTTNTQMYPLVYDTTYKGIISTAGYSSPLADYGNTYYNDHHFHWGYHIYACAVIGLLDPSWLVNDNIRYVNALLRDSANPSESDTYFAMFRNFDWFVGHSWATGIFESGDGKDEESTSEDFNFLYATKLWGMVRNDTVLINRANLMLAVLKNSLNTYIYMTPTTSVQPSQILGNYVTGITFMNKVDYATYFSAEEYCKQGIHMIPTTPISGYLRSPSYVQQDWNAKIAPIINTFSNNWTGILWSNYAIYDPKTAYNTFAASTFTADKIDNGASKTWYLAMAAGMGGSP Q09851 AYR1_SCHPO ACT_SITE 148; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 152; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 9; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 35; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 41; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 56; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 84; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 117; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 148; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 152; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 181; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 183; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-hexadecanoylglycerone 3-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:17341, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57783, ChEBI:CHEBI:58303, ChEBI:CHEBI:58349; EC=1.1.1.101; Evidence={ECO:0000250|UniProtKB:P40471}; CATALYTIC ACTIVITY: Reaction=a 1-acylglycerone 3-phosphate + H(+) + NADPH = a 1-acyl-sn-glycero-3-phosphate + NADP(+); Xref=Rhea:RHEA:33375, ChEBI:CHEBI:15378, ChEBI:CHEBI:57534, ChEBI:CHEBI:57783, ChEBI:CHEBI:57970, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P40471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33376; Evidence={ECO:0000250|UniProtKB:P40471}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P40471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P40471}; SPAC23D3.11; CHAIN 1..296; /note="NADPH-dependent 1-acyldihydroxyacetone phosphate reductase"; /id="PRO_0000054874" MEAEKFVLITGCSEGGIGNALALKFHQEGFQVLATARQVERMDNLTKAGLQTLKLDVTDEDSVREVEQEVRKFTNGSLHYLINNAGAPCSAPAIDLDIEDVSKVMDVNFYGVIRMNKAFQHQLIRAKGTIVNVNSLVSYVPFAFNAAYNASKAALLAYSNTLRIELAPFGVQVTSIMTGGVQTKIQSKPLGTMTEAAIPENSIYYPYRKLILENRNPVEKFVTIEEFADAAYPQLVGRGRWYQLFKPGVRPAQIWAGYMSSAGRVGSMLPVEVFSMSVRLIVKLPSTAVWRDHTVD Q09864 HSP60_SCHPO TRANSIT 1..35; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 92; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12G12.04; CHAIN 36..582; /note="Heat shock protein 60, mitochondrial"; /id="PRO_0000005043" MVSFLSSSVSRLPLRIAGRRIPGRFAVPQVRTYAKDLKFGVDARASLLTGVDTLARAVSVTLGPKGRNVLIDQPFGSPKITKDGVTVARSVSLKDKFENLGARLVQDVASKTNEVAGDGTTTATVLTRAIFSETVRNVAAGCNPMDLRRGIQLAVDNVVEFLQANKRDITTSEEISQVATISANGDTHIGELLAKAMERVGKEGVITVKEGRTISDELEVTEGMKFDRGYISPYFITDVKSQKVEFENPLILLSEKKVSAVQDILPSLELAAQQRRPLVIIAEDVDGEALAACILNKLRGQLQVVAIKAPGFGDNRRNMLGDLAVLTDSAVFNDEIDVSIEKAQPHHLGSCGSVTVTKEDTIIMKGAGDHVKVNDRCEQIRGVMADPNLTEYEKEKLQERLAKLSGGIAVIKVGGSSEVEVNEKKDRIVDALNAVKAAVSEGVLPGAGTSFVKASLRLGDIPTNNFDQKLGVEIVRKAITRPAQTILENAGLEGNLIVGKLKELYGKEFNIGYDIAKDRFVDLNEIGVLDPLKVVRTGLVDASGVASLMGTTECAIVDAPEESKAPAGPPGMGGMGGMPGMM Q09879 UBP72_SCHPO ACT_SITE 120; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q96AP4"; ACT_SITE 222; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 464; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:28947618}; SPCC188.08c; CHAIN 1..1108; /note="Ubiquitin carboxyl-terminal hydrolase 5"; /id="PRO_0000080606" MVTGETLVDSQKSLINNDTLLNEKLKEDFEENVSIDVKIHEELRRALPDYEESGFQRFTWHIKSWHELDRRAVSPQFAVGSRQFKITYFPQGTLQSAGFTSIFLEYIPSEEEKLSNKYGCCCQFAFVISNPRKPSLSVANSAHCRFSPEIVDWGFTQFAELKKLLCRQAPDVPPIVEDGALLLTAYVRILKDPTGVLWHSFNDYDSKIATGYVGLKNQGATCYMNSLLQSLYIIHAFRRIVYQIPTDSPQGKDSIAYALQRCFYNLQFMNEPVSTTELTKSFGWDSLDSFMQHDVQEFNRVLQDNLERSMRDTKVENALTNLFVGKMKSYIACVNVNFESARSEDYWDIQLNVKGMKNLEDSFRSYIQVETLEGDNCYFADTYGFQEAKKGVIFESFPPILHLQLKRFEYDFERDMMIKINDRYEFPLEFDAKAFLSPEADQSQNCEYVLYGVLVHSGDLHNGHYYALLKTEKDGPWYKYDDTRVTRATLREVLEENYGGDYIMHPPFRSPVKLKRFMSAYMLLYLRKDKLDELMNPVSADEIPEHLKEALNPSIQLAELRRKERLESHLYTKVQLITPEFYSEHHEFDIADFGNAYKEETIPQFRIKKEAKFSEFIPIVAEKLGYPQECMRFWYVVKRHNCTVRVESPVNELNSTMEEVKNVWNSQGEILRLYLEITPENELSSSLTHQNTGEWNAFIFVKYFDRKSQEISGCGTLHVNKSDEIRSICPLLCERANLPKNTPLNIYEEIKPGMVDFLRLEKTFTQSELSTGDIICFEPCRPSALEDDIVNSGFDSALKLYDFLSNKVLVLFRPRFIDQDSIIEFEMLLDRRIKYDDLCIELGQKLGIGADHIRLTTCNPLTYSAGMVVPNDSNITLYEILYSSEEEMPSNVIFYETMDVSLSDLDRKRLVRLRWLVDGLANIELVEAYINKSGDINDLFGAVCERFPDSDLRKKKVRVYEVFESRYHRDLSLRTLIRTINPAATLVGEVVPLDQLQLYPEEKIVQVHHFHKDIARIHGIPFSFVIKPQEKFIDTKLRLAARTQYPESIFSVIKFCVVDFDNNRVVYLNDEDITYDVVEKLNGTLALDRAKKDSKKPNILDRAIQMKN Q09882 PRP45_SCHPO MOD_RES 228; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 236; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 376; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC188.11; CHAIN 1..557; /note="Pre-mRNA-processing protein 45"; /id="PRO_0000084822" MALLSEELSSILPNPDFDDEEEDYVERETSHADERQIGVKFHIPPYGQRKGWFPSSPEDFGDGGAFPEIHVAQYPLDMGRKRSAKSAGNTLALQVTSSGAVDYNAIARQGHEHGELVQASFRDLIPLRARLGVGEISLEKPSDEQKQEVANKTKLALQKILSKQIAQSQPKSAVVQQRDDPVYIRYTPSNQMGQALSKQRIIKMVTAEQDPMEPPKFRHKKVPRGPPSPPPPVLHSPPRKVSAQEQQDWQIPPSISNWKNPKGYTIPLDKRLAADGRGLNDVEINDGFAKFSEALYTVERQAREEVRYRAIMRQKMAEKEKQEKEQRLFMLAQKAREDRMGRNAASSGPSHAKPRSTSVSSEERSRSRAGSFSHHSESENEDEDSEAFRRRQELRRERRRQAEKDLRLSRMGAEKRAKLAEKDRPRDVAERVALGLSKPSMSSDTMIDSRLFNQASGLGSGFQDEDSYNVYDKPWRAAPSSTLYRPGATLSRQVDASAELERITSESRYDVLGNAHKKFKGSDEVVESRAGPVTFEKDIADPFGVDTFLNNVSSKKT Q09883 SPN6_SCHPO BINDING 37..44; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 72; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 98; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 177..185; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 246; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPCC188.12; CHAIN 1..380; /note="Septin homolog spn6"; /id="PRO_0000173508" MSLTENLQLLLNLDSLPSKRENLIKRKECGLTIMLCGASGTGKTTFFNTLFATSLQPEKSYETAKETIAKKTLEVKKNKAVIEEDGFHINLTVLDTPGFGDFIDNTSCWNTVAEYLDEQHERYLIHDQNSLRVPRKDTRVHVCLYFITPVSFGMLPLDVLAMKELSTHVNLVPVIAKADTFTTPELTQIKQKIRRILEAQSIDVFHPSTEYSDYETAELLDSSLPYAIISSVNEVCKDDGEKSQGRRYPWGTSEIYEETHCDFLKLKKLLINRHMLELINTTETNIYERYRREQLTNRKSGIPKLKKEHYERLNNEKRAIQQKITQMTNETESFFQAKEEKMIETRDALNSELSEYHERIRALETQIESLKSYKGRGHKK Q09884 DCR1_SCHPO BINDING 32..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 1123; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1219; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1222; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1275; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21847092, ECO:0007744|PDB:2L6M"; BINDING 1312; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21847092, ECO:0007744|PDB:2L6M"; BINDING 1350; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21847092, ECO:0007744|PDB:2L6M"; BINDING 1352; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:21847092, ECO:0007744|PDB:2L6M" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; SPCC188.13c; STRAND 1278..1286; /evidence="ECO:0007829|PDB:2L6M"; STRAND 1294..1297; /evidence="ECO:0007829|PDB:2L6M"; STRAND 1303..1311; /evidence="ECO:0007829|PDB:2L6M"; STRAND 1314..1323; /evidence="ECO:0007829|PDB:2L6M" HELIX 1262..1270; /evidence="ECO:0007829|PDB:2L6M"; HELIX 1324..1341; /evidence="ECO:0007829|PDB:2L6M"; HELIX 1344..1347; /evidence="ECO:0007829|PDB:2L6M" TURN 1271..1274; /evidence="ECO:0007829|PDB:2L6M"; TURN 1351..1353; /evidence="ECO:0007829|PDB:2L6M" CHAIN 1..1374; /note="Protein Dicer"; /id="PRO_0000102194" MDISSFLLPQLLRKYQQDVYNIASKQNTLLVMRTGAGKTLLAVKLIKQKLEEQILIQESNLEHKKISVFLVNKVPLVFQQAEYIRSQLPAKVGMFYGELSIEMSEQLLTNIILKYNVIVITADLFYLFLARGFLSINDLNLIIFDECHHAIGNDAYARIMNDFYHRAKAVLSKKHFTLPRIFGMTASPFTGKKGNLYHRLYQWEQLFDSKAHVVSENELADYFCLPEESYVMYSNKLVVPPSDSIIKKCEETLQGCKLISRAVKTALAETIDMGLWFGEQVWLYLVDFVETKRLKKKALGKQLSDDEELAIDRLKIFVEDWKNNKYSDNGPRIPVFDSTDVTDKVFKLLELLKATYRKSDSVRTVIFVERKATAFTLSLFMKTLNLPNIRAHSFIGHGPSDQGEFSMTFRRQKDTLHKFKTGKYNVLIATAVAEEGIDVPSCNLVIRFNICRTVTQYVQSRGRARAMASKFLIFLNTEELLIHERILHEEKNLKFALSELSNSNIFDSLVCEERERVTDDIVYEVGETGALLTGLYAVSLLYNFCNTLSRDVYTRYYPTFTAQPCLSGWYCFEVELPKACKVPAAQGSPAKSIRKAKQNAAFIMCLDLIRMGLIDKHLKPLDFRRKIADLETLEEDELKDEGYIETYERYVPKSWMKVPEDITRCFVSLLYTDANEGDNHIFHPLVFVQAHSFPKIDSFILNSTVGPRVKIVLETIEDSFKIDSHLLELLKKSTRYLLQFGLSTSLEQQIPTPYWLAPLNLSCTDYRFLENLIDVDTIQNFFKLPEPVQNVTDLQSDTVLLVNPQSIYEQYAFEGFVNSEFMIPAKKKDKAPSALCKKLPLRLNYSLWGNRAKSIPKSQQVRSFYINDLYILPVSRHLKNSALLIPSILYHIENLLVASSFIEHFRLDCKIDTACQALTSAESQLNFDYDRLEFYGDCFLKLGASITVFLKFPDTQEYQLHFNRKKIISNCNLYKVAIDCELPKYALSTPLEIRHWCPYGFQKSTSDKCRYAVLQKLSVKRIADMVEASIGACLLDSGLDSALKICKSLSVGLLDISNWDEWNNYFDLNTYADSLRNVQFPYSSYIEETIGYSFKNKKLLHLAFIHPSMMSQQGIYENYQQLEFLGDAVLDYIIVQYLYKKYPNATSGELTDYKSFYVCNKSLSYIGFVLNLHKYIQHESAAMCDAIFEYQELIEAFRETASENPWFWFEIDSPKFISDTLEAMICAIFLDSGFSLQSLQFVLPLFLNSLGDATHTKAKGDIEHKVYQLLKDQGCEDFGTKCVIEEVKSSHKTLLNTELHLTKYYGFSFFRHGNIVAYGKSRKVANAKYIMKQRLLKLLEDKSNLLLYSCNCKFSKKKPSDEQIKGDGKVKSLT Q09891 ATCX_SCHPO ACT_SITE 569; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0" BINDING 569; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 569; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 570; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 571; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 571; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 700; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 741; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 743; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P32660"; BINDING 746; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 764; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 799; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 800; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 879; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 880; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 881; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 986; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 992; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1012; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 1015; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 1016; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1016; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q8NB49"; BINDING 1275; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"; /ligand_id="ChEBI:CHEBI:57262"; /evidence="ECO:0000250|UniProtKB:G0S196" CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:P32660}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; SPAC24B11.12c; CHAIN 1..1402; /note="Phospholipid-transporting ATPase dnf2"; /id="PRO_0000046239" MESVEEKSKQRRWLPNFKALRLKVYRLADRLNIPLADAARVELEEYDGSDPQSLRGLQKLPRTLYFGLPLPDSELDDTGEAKRWFPRNKIRTAKYTPIDFIPKNIFLQFQNVANLFFLFLVILQSISIFGEQVNPGLAAVPLIVVVGITAVKDAIEDFRRTMLDIHLNNTPTLRLSHYQNPNIRTEYISYFRRFKKRISALFRVFLAKQEEKKRAKRLNDAVPLEDMAGSESRPSYDSIFRESFEAKRSFEDSKGKVPLSALDGTATILQSRPMDIIDYEAEATGECHFKKTYWKDVRVGDFVKVMDNDEIPADIVIINSSDPEGICYIETKNLDGETNLKMRHALTCGKNVVDEASCERCRFWIESEPPHANLYEYNGACKSFVHSEAGGSDTSQTVSEPISLDSMLLRGCVLRNTKWVIGVVVFTGDDTKIMLNSGAPPLKRSRITRNLNWNVYLNFIILFSMCFVCAVVEGIAWRGHSRSSYYFEFGSIGGSPAKDGVVTFFTGVILFQNLVPISLYISIEIVKTIQAIFIYFDKDMYYKKLKYACTPKSWNISDDLGQVEYIFSDKTGTLTQNVMEFKKCTINGVAYGEAFTEAMAGMAKREGKDTEELTLQKQSFIERDRMQMISQMRNMHDNKYLVDDNLTFISSQFVHDLAGKAGEEQSLACYEFFLALALCHSVVADRVGDRIVYKAQSPDEAALVGTARDVGFVFLDQRRDIMVTRALGETQRFKLMDTIEFSSARKRMSVIVKGPDNRYVLICKGADSIIFERLEPNEQVELRKTTSEHLRIFALEGLRTLCIAKRELTEEEYYEWKEKYDIAASAIENREEQIEEVADLIESHLTLLGGTAIEDRLQEGVPDSIALLAQAGIKLWVLTGDKMETAINIGFSCNLLDAGMDMIKFDVDQEVSTPELEVILADYLYRYFGLSGSVEELEAAKKDHDTPSGSHALVIDGSVLKRVLDGPMRTKFLLLCKRCKAVLCCRVSPAQKADVVQLVRESLEVMTLAIGDGANDVAMIQKADIGVGIVGEEGRAAAMSADYAIGQFRFLSKLVLVHGRWDYNRVAEMVNNFFYKSVVWTFTLFWYQIYNNFDANYLFDYTYVMLFNLIFSSLPVIVMGVYDQDVNADLSLRIPQLYKRGILQLNSARKIFIGYMLDGFYQSVICFFFSFLVINNVTTAAQNGRDTMAVQDLGVYVAAPTIMVVDTYVILNQSNWDVFSIGLWALSCLTFWFWTGVYSQSLYTYEFYKSASRIFRTPNFWAVLCGTIVSCLFPKFLFMTTQKLFWPYDVDIIRESYRTKRLHELDEEEEIENAEQSPDWASSTLQVPFNASSSSLATPKKEPLRLDTNSLTLTSSMPRSFTPSYTPSFLEGSPVFSDEILNRGEYMPHRGSISSSEQPLRP Q09892 HOG1_SCHPO ACT_SITE 141; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 26..34; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 49; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:P32485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:P32485}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:P32485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:P32485}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q16539}; PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme (By similarity). Phosphorylated by wis1 in response to osmotic stress, nutrient limitation, hydrogen peroxide and arsenite. Dephosphorylated by pyp1 and pyp2. {ECO:0000250, ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:16087744, ECO:0000269|PubMed:16141205, ECO:0000269|PubMed:16464860, ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:7501024, ECO:0000269|PubMed:8649397, ECO:0000269|PubMed:9188094, ECO:0000269|PubMed:9443913}. MOD_RES 171; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 173; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 176; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24B11.06c; CHAIN 1..349; /note="Mitogen-activated protein kinase sty1"; /id="PRO_0000186342" MAEFIRTQIFGTCFEITTRYSDLQPIGMGAFGLVCSAKDQLTGMNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPFEDIYFVTELLGTDLHRLLTSRPLETQFIQYFLYQILRGLKFVHSAGVIHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYNVEVDIWSAGCIFAEMIEGKPLFPGRDHVNQFSIITELLGTPPMEVIETICSKNTLRFVQSLPQKEKVPFAEKFKNADPDAIDLLEKMLVFDPRKRISAADALAHNYLAPYHDPTDEPVADEVFDWSFQDNDLPVETWKVMMYSEVLSFHNMDNELQS Q09898 SID2_SCHPO ACT_SITE 331; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 214..222; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 237; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 56; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 219; /note="Phosphotyrosine"; /evidence="ECO:0000250"; MOD_RES 402; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24B11.11c; CHAIN 1..607; /note="Serine/threonine-protein kinase sid2"; /id="PRO_0000086654" MNRVNDMSPVEGDLGLQLSSEADKKFDAYMKRHGLFEPGNLSNNDKERNLEDQFNSMKLSPVASSKENYPDNHMHSKHISKLPIASPIPRGLDRSGELSYKDNNHWSDRSSTGSPRWENGSMNLSVEEMEKVVQPKVKRMATICQMFFLDHYFEQLHYLYTRKQRARLFEEQLLKEPDSRRDELVKRYNGRERVYLRKRRTRISHGDFQTITQVGQGGYGSVWLARKRDTKEIVALKIMNKSVLHKMDEIRHVLTERDILTTANSEWLVRLLYAFQDTSNIYLAMEFVPGGDFRTLLSNSGVLRDHHAKFYATEMFLAIDALHQLGYIHRDLKPENFLVGASGHIKLTDFGLSSGIISKKKIESMKIRLQEVNNVVVPERSMRERRQVFRTLLSQDPVYAHSVVGSPDYMAPEVLRGENYNHSVDYWSLGCIMYECLSGFPPFSGSNVNETWSNLKNWRKCFQRPHYDDPRDLEFNWRDDAWDFVCHCITDPKDRFCSLKQVMQHPYFSKIDWKNVRTAYRPPFVPDLNSEIDAGYFDDFTNENDMSKYKEVHEKQAAIANMVNTFNKPKRNAFIGFTFRHQKNSHPTSSSSALSSPLSAPSFGTLL Q09906 HFL1_SCHPO MOD_RES 364; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC30D11.06c; HELIX 395..401; /evidence="ECO:0007829|PDB:7YO8" TURN 392..394; /evidence="ECO:0007829|PDB:7YO8" CHAIN 1..426; /note="Vacuole membrane protein hfl11"; /id="PRO_0000211557" MDNEIVALCGFFVAIALVLSCISIITHLKNYKKPVLQRSVVRILMMIVIYSSVSFLSVYNEKIGSIFEPFREIYEAFALYCFFCLLIDYLGGERAAVISLHGHLPRPRLWPLNYLQDDIDLSDPYTFLSIKRGILQYTWLKPFLVIAVLLTKVTGVYDREDQPVYASADLWIGLVYNISITLSLYSLTTFWVCLHEELAPFRPFPKFLSVKAIIFASYWQQTVLSITNWLGLLNGTGWIYSLLNQNVLMCLEMPFFALSHWYAFRIEDYDTPTWLSCARLPLLKAFKDVIGLKDVWCDSLQTLHGDRYVYQNFEPGENLIPSRNDGRINRTSHGLRYSQGGQSKYWISRYDQSRVRLINNSQNSPQSNKSYFSIPGMSTSHFENGLQFEIDDEMEPLYNQAKQMRYGDYNYPVLLVNNTHASSSYT Q09907 NTH_SCHPO ACT_SITE 142; /note="Nucleophile; for N-glycosylase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03183" BINDING 210; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03183"; BINDING 217; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03183"; BINDING 220; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03183"; BINDING 228; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03183" CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:9425081}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03183}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand. {ECO:0000255|HAMAP-Rule:MF_03183}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=963 nM for 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity) {ECO:0000269|PubMed:9425081}; KM=173 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-glycosylase activity) {ECO:0000269|PubMed:9425081}; KM=360 nM for 5-hydroxycytosine containing duplex oligonucleotides (N-glycosylase activity) {ECO:0000269|PubMed:9425081}; KM=1741 nM for thymine glycol containing duplex oligonucleotides (N-glycosylase activity) {ECO:0000269|PubMed:9425081}; KM=111 nM for 5,6-dihydroxycytosine containing duplex oligonucleotides (N-glycosylase activity) {ECO:0000269|PubMed:9425081}; SPAC30D11.07; CHAIN 1..355; /note="Endonuclease III homolog"; /id="PRO_0000102226" MSKDYGTPPENWREVYDEICKMKAKVVAPVDVQGCHTLGERNDPKKFRFQTLVALMLSSQTKDIVLGPTMRNLKEKLAGGLCLEDIQNIDEVSLNKLIEKVGFHNRKTIYLKQMARILSEKFQGDIPDTVEDLMTLPGVGPKMGYLCMSIAWNKTVGIGVDVHVHRICNLLHWCNTKTEEQTRAALQSWLPKELWFELNHTLVGFGQTICLPRGRRCDMCTLSSKGLCPSAFKEKSGITITKRKVKTIKRVKKRPASESPPLSPLSLPTDDLYYQSIEDKSLIKLEDLDPVDSISHMNEPLKKEPAADIDVDQKPPVAFHSTTKETRSLRRSKRVAKKSSQYFSQQSLQDIEDLV Q09914 RHO1_SCHPO BINDING 13..20; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 60..64; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 118..121; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 199; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC1F7.04; STRAND 6..14; /evidence="ECO:0007829|PDB:8ETD"; STRAND 43..49; /evidence="ECO:0007829|PDB:8ETD"; STRAND 52..59; /evidence="ECO:0007829|PDB:8ETD"; STRAND 79..86; /evidence="ECO:0007829|PDB:8ETD"; STRAND 109..111; /evidence="ECO:0007829|PDB:8ETD"; STRAND 113..118; /evidence="ECO:0007829|PDB:8ETD"; STRAND 155..159; /evidence="ECO:0007829|PDB:8ETD" HELIX 19..28; /evidence="ECO:0007829|PDB:8ETD"; HELIX 71..74; /evidence="ECO:0007829|PDB:8ETD"; HELIX 90..98; /evidence="ECO:0007829|PDB:8ETD"; HELIX 100..107; /evidence="ECO:0007829|PDB:8ETD"; HELIX 120..122; /evidence="ECO:0007829|PDB:8ETD"; HELIX 126..134; /evidence="ECO:0007829|PDB:8ETD"; HELIX 142..151; /evidence="ECO:0007829|PDB:8ETD"; HELIX 168..179; /evidence="ECO:0007829|PDB:8ETD" TURN 68..70; /evidence="ECO:0007829|PDB:8ETD"; TURN 162..164; /evidence="ECO:0007829|PDB:8ETD" PROPEP 200..202; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281270" CHAIN 1..199; /note="GTP-binding protein rho1"; /id="PRO_0000198940" LIPID 199; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MATELRRKLVIVGDGACGKTCLLIVFSKGTFPEVYVPTVFENYVADVEVDGRHVELALWDTAGQEDYDRLRPLSYPDSHVILICFAVDSPDSLDNVQEKWISEVLHFCSSLPILLVACKADLRNDPKIIEELSKTNQHPVTTEEGQAVAQKIGAYKYLECSAKTNEGVREVFESATRAAMLKHKPKVKPSSGTKKKKRCILL Q09917 PKD2_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" MOD_RES 599; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 632; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F7.03; CHAIN 24..710; /note="TRP-like ion channel pkd2"; /id="PRO_0000045821" MRLWRSPLLLLVVVVELFSWADALTRFISADSLSTCMTDSQLSASKLYASYFPDNQSVAFDISIQSLVSTNVSIDVDISAYGIEIKKVIDPCDMEISGFCPMQTGNIALSGSHTLTGEALSILDSIPSIAYTVPDLDAVVTINIYESDTNTQLACVRTTVQNGRSVYHRAVYWVMCMVIGIPLLIFLLISPVLQTPALWEIVETMITLFQFAQIQALYSMMATSLPAIIYSWGRNFMWSMGIIRIGFMQDVFTWYVKSTGGTPSTLVDLGIHANVALAKRGIDLGSLAKRATTTVTTSTSDSITLRGIKRISYMMGIETTNFFATGFSFFIILLFFSLLVAMASRFIVEMVLLASRNQALKKQRIRLYWKSISKGFFYRVIFVGFTQMSVLSMWEIYTRDSSALAFLSMYVIVDMAVLLCYAFVRTIQIIRKTGPYSHPDVLYNLYSDTQHLMRWGFMYVQLDVRFFYFTFPLLLITLVRSMFIGFGQGSPKVQGCAMFGISVVVFALMVILRPYATKHMNTLHIGVALMNLISGSFILVMCQAFYVEELARQVIGIIFFALNAITMLLLILGIFIRTLIVLFRKSGHGTYYRILDDQSEKATSYNKSIKDMSSSDMAFSDPAYSGTTLRSSVDLNTPEYPFSNRNDSDSTFTNNKYVSPWDAIEEASYANLRGNTDVEQPFMESDYTRISENNNNAERRRKPLPNNAFR Q09926 PCR1_SCHPO SPAC21E11.03c; CHAIN 1..171; /note="Transcription factor pcr1"; /id="PRO_0000076535" MTAKKKEVDDEKRRRILERNRIAASKFRQKKKEWIKELEQTANAAFEQSKRLQLLLSQLQQEAFRLKSQLLAHQGCQCSVKIRSVLTDFQTAHNALHSQHMAYRPVQPPPGDNMLESVVSVSPTQMHPSLQGLPPNQHPQMPPSSQQPNSDDVQQHMFSAAGLPRSLGGPI Q09933 DIS1_SCHPO MOD_RES 279; /note="Phosphothreonine; by CDC2"; /evidence="ECO:0000269|PubMed:7628693"; MOD_RES 293; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:7628693"; MOD_RES 300; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000269|PubMed:7628693"; MOD_RES 551; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:7628693"; MOD_RES 556; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:7628693"; MOD_RES 590; /note="Phosphoserine; by CDC2"; /evidence="ECO:0000269|PubMed:7628693"; MOD_RES 649; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 650; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC736.14; CHAIN 1..882; /note="Phosphoprotein p93"; /id="PRO_0000079913" MELDDFNSRILSQIFDKSWKVRFEAYESLLHALNRALDDSDVCFQPWIHDPALWKQGLCDSNVPTQEHAVKSLRCFLDKSRQKGVNSAKSFVVAPLLEKCLPSPRQSIRDASHQALLILAKSDALDYVLEGLFSAARVKHPKQAVASIKELNSLLENFGIPALSPIPFYKLIPTLFAQSDKNIRQEASNLSITLYAWVGNAFKTHVFPQLKQIQVSDLEASFQNVTSRTTTGGHISNSLNTQEVVLPSFSSNAKPKPHLSSKSSSQGNTLQRSTSSFSTPNRKVSQPSDFSASPSRSIVSPAKNIVGSTPVDVLSKLTPEFHTALSSPKWKDRKEALESMVPVCSNPVYQEGDYSELLRVIAKSLKDANVVVVGVAALLLTHIAKALRKGFLPYTGIVLPSLFDRFKERKSSLVHSLLDAANAIFESCGLNDIMDETLEFLKHKNPQVKTETLRWLNRCLQLTDVCPPRASLETLCSLCVTLINDTFEPVRMATTNVLATLVQIFSQPVLSKYIVGLDPKKLPKILELSKDITVNAHPNQPSRPRLPRVASPLKTSPVKLAVTPQAPSPLPSSNPSQASLTEESLSTRSSPTKPSTTSLRSQSLVNRFASSTLKAPSSSSKGVSNAASSKQSFPSSPSISKKLETSRLSTKKLPGSTMKAASALKEYPQQQSMKSGGEKQDNLVTITMSEKVELDLLREEKAIRQVQEAEDALERERLFREINDLQIQNAEMKEQVYEKESTISQKEVEITSLRNEKDRLSTRLQQVLLELEKQHETNEEAMDIDLKVPESGAIGRVTTRATATTAMDESGNAGMVSSGIHSVSTKPSSYGTRRSLAGSMLQKPTQFSRPSFMFSPEARDNWRESHDLSSHLWEQIQRMKKA Q10055 FAL1_SCHPO BINDING 65..72; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F5.10; CHAIN 1..394; /note="ATP-dependent RNA helicase fal1"; /id="PRO_0000054967" MADEIMENVELTTSEDVNAVSSFEEMNLKEDLLRGIYAYGYETPSAVQSRAIIQICKGRDVIAQAQSGTGKTATFSIGILQSIDLSVRDTQALILSPTRELAVQIQNVVLALGDHMNVQCHACIGGTSVGNDIKKLDYGQHVVSGTPGRVTDMIRRRNLRTRNVKMLILDEADELLNQGFKEQIYDIYRYLPPGTQVVVVSATLPQDVLEMTNKFTTNPVRILVKRDELTLEGLKQYFIAVEKEEWKFDTLCDLYDTLTITQAVIFCNSRRKVDWLTEKMREANFTVTSMHGEMPQKERDAIMQDFRQGNSRVLICTDIWARGIDVQQVSLVINYDLPANRENYIHRIGRSGRFGRKGVAINFVTNEDVRILRDIEQYYSTVIDEMPMNIGDMV Q10059 CDC12_SCHPO MOD_RES 1541; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1544; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F5.04c; CHAIN 1..1841; /note="Cell division control protein 12"; /id="PRO_0000194901" MRNSSKGQDPNFSYDSILSTPTPSARRTIGPRAPKSKTTYHKPPSSIESVSTLIQPNKSQSVTSPYVKQFTFSSKEYNSHNKHALQNSQLPLPKTPEKSTVHRPKANKVEVTDLPSSSSVEHLHTSKHLKGPRLPKNIIKSSEDVQIAPVTPPVHSRSFDPLPKPPVPSVPVSKTKRRTKHKLAPVVEVPEITNEVSPKFTSTNDEQVYRLRSIRAGSPNSVCSFQFEIPSTRPPSLDQLIHLFNDFLRHPVFDFDENAIEMLQSCTPDEKWCFIRSNFAGFDDPSFQIPELAAVHRPVSWFVIQLWNKTISNLQLITLSSLLSTQSDRWISLFLELQGLRALHNLLTYFNSSAVVQPQQAEVPRCMLTLLKKKPTLVTSNSYIFQAITVTLISPNLLPRKVAADLLTWVLSLKEPLVVSILETGFKEINAEYEKEVPLFFGWIKSFKDIILEKELARTPPSSPARNSASSSPSNIAFLEYCTSTMEFINQLIVACEELEQGFDLDILDSLRESGIHEVIQLLRNFPDQQLEKQLNIYESEEERRTISQTTHEDVDSFMSNESSILSSFNEFASNEVGRLLESTIQNILLAKGTEKQKVKLIKVFNSLLQRILLNSKVSNESFEDSLQASLNMLTERFYSDDTARNALKEAKASRAMAEKMVIERDAMAAQVNLGAEDLIAKLNKEVEDQKDVILSQKRTNETLKTEIDALQKSHVTQIQRSEVELRELYLLINSDSFQGSTNSKERIIEYLLDKLDLRKKEIAAESTLWSNDGIDDKLRDLREQMSRQSSQPSTVSTILQIPDKKFHRPFPRHLHRYVGRSASESLTSEKDESIKSMKGIDDFANLEIPGKGIESNVVIKDISNQTHEINSVENKAETVSNNSKITNFDIPNDATSLPTIITHPTPPPPPPLPVKTSLNTFSHPDSVNIVANDTSVAGVMPAFPPPPPPPPPLVSAAGGKFVSPAVSNNISKDDLHKTTGLTRRPTRRLKQMHWEKLNSGLEFTFWTGPSDEANKILETLHTSGVLDELDESFAMKEAKTLVKKTCARTDYMSSELQKLFGIHFHKLSHKNPNEIIRMILHCDDSMNECVEFLSSDKVLNQPKLKADLEPYRIDWANGGDLVNSEKDASELSRWDYLYVRLIVDLGGYWNQRMNALKVKNIIETNYENLVRQTKLIGRAALELRDSKVFKGLLYLILYLGNYMNDYVRQAKGFAIGSLQRLPLIKNANNTKSLLHILDITIRKHFPQFDNFSPELSTVTEAAKLNIEAIEQECSELIRGCQNLQIDCDSGALSDPTVFHPDDKILSVILPWLMEGTKKMDFLKEHLRTMNTTLNNAMRYFGEQPNDPNSKNLFFKRVDSFIIDYSKARSDNLKSEEEEASQHRRLNLVNNHKEHVLERAMSENNKMDNEAMDGFLDKLRNVKLESHHKPRNRSAITMGKEHLIEAPNTSTKSSPAKNELFVPKRSSVKSDLAKVRPRYPKGSESTDGLSDALNITPTKKGEVSSKAKKGYNYEKRRSGRQVSDSYVLNKNSKNKSNKGRSASYTFSDPSSLEDSNRQKPFNGEKFRRFSSKSRRGSQNRDSKKTGKARKDKGINNNQTSPQNKPSKESLKSDTISNEKKVFPQKASKVNLLTPTISNGTRASKHANEKENTFPRGVENNLVAPMIPNNTELNEDTSAVSRNLENATNDLKETFPTTTTISTARAKPGNNDINTILRRNNSRGRRRMLQQMSPLKSNKFSGTNDLNFQQATKPDGSNKSSYMERLEKLKQNSERHLQSVGGKKVYSSEETPVNKILVSPSVSILDHNRILSQSTPIKSPQRAQEMLAGLLSGKLAPKENEK Q10074 AVT3_SCHPO MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 53; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 172; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H1.09c; CHAIN 1..656; /note="Vacuolar amino acid transporter 3"; /id="PRO_0000093833" MSNSQSIKIKKPRSNENFASGSYSSRRSQQIHRLSHSPMAEGFHKPKLNISPSESNLPNNVAENTTDTPVNYGSIRDENHNSRKGKDVTLNSDEAHSENVPSTSEDPDVVRRHLGGQAADDDNFSSLQLQGGDMHRQVYRWQQEVDQNKQIRRGRSRSFSAKVSDPNLHLRSVQDMKQAGGMRRDFLRNRASSISMSSNAHGNPNFLNRNFIEFLSVYGHFAGEELSEEDEDEDTDDFAMPRDVNPSLIHSTVPSEQEPLISRHGRYKLQTPGNASNGKAVLLLLKSFVGTGVLFLPKAFKLGGLVFSSATLLIVGVLSHICFLLLIQTRMKVPGSFGDIGGTLYGPHMRFAILASIVVSQIGFSSAYISFVASTLQACVKVISTTHREYHLAVFIFIQFLVFVPLSLVRKISKLSATALIADVFILLGILYLYFWDVITLATKGIADVAMFNKTDFSLFIGVAIFTYEGICLILPIQEQMAKPKNLPKLLTGVMAAISLLFISIGLLSYAAFGSKVKTVVILNMPESTFTVIIQFLYAIAILLSTPLQLFPAIAIIEQGIFTRSGKRNRKIKWRKNYLRVLIVILAILISWAGSSRLDLFVSMVGSVCCIPLIYMYPPMLHYKACANNWILRTLDIFMFTIGAFAMAFTTYMTFF Q10099 SEH1_SCHPO SPAC15F9.02; CHAIN 1..339; /note="Nucleoporin seh1"; /id="PRO_0000051214" MDDISATTIQTNHQDLVNDVTYDFYGRRMVSCSADQRVKVYDFNDDTETWAITSEWRAGDASLMRVAWAHPSFGQVLAVCSLDRGVRIYEEQKKNFESKTWVEVAKLMDARSAVLDISFCPFQHGCKLAAVSADATLRIYEAMEPGNLTYWTLMNEIALMPSPPSRNEQPAFCVNWCPSRWREQYIAVGCMNDAYIYKQNSHGKWKKVAELPGHTDLIRDICWAPSMGSSYYLIATACKDGNVRIFKVETLCEEVFQEEEDAGNSMTEDSNFNLNSLKVELIGEYDNHKCQVWRCRFNVTGTILSSSGDDGCVRLWKASYANLFKCISVVSLEKKPEKL Q10103 CHP1_SCHPO SPAC18G6.02c; STRAND 21..32; /evidence="ECO:0007829|PDB:3G7L"; STRAND 34..36; /evidence="ECO:0007829|PDB:2RSN"; STRAND 38..44; /evidence="ECO:0007829|PDB:3G7L"; STRAND 53..56; /evidence="ECO:0007829|PDB:3G7L"; STRAND 519..526; /evidence="ECO:0007829|PDB:3TIX"; STRAND 531..539; /evidence="ECO:0007829|PDB:3TIX"; STRAND 561..564; /evidence="ECO:0007829|PDB:3TIX"; STRAND 566..569; /evidence="ECO:0007829|PDB:3TIX"; STRAND 582..587; /evidence="ECO:0007829|PDB:3TIX"; STRAND 589..595; /evidence="ECO:0007829|PDB:3TIX"; STRAND 608..613; /evidence="ECO:0007829|PDB:3TIX"; STRAND 618..623; /evidence="ECO:0007829|PDB:3TIX"; STRAND 641..648; /evidence="ECO:0007829|PDB:3TIX"; STRAND 696..701; /evidence="ECO:0007829|PDB:3TIX"; STRAND 723..727; /evidence="ECO:0007829|PDB:3TIX"; STRAND 736..744; /evidence="ECO:0007829|PDB:3TIX"; STRAND 766..771; /evidence="ECO:0007829|PDB:3TIX"; STRAND 804..808; /evidence="ECO:0007829|PDB:3TIX"; STRAND 812..816; /evidence="ECO:0007829|PDB:3TIX"; STRAND 842..846; /evidence="ECO:0007829|PDB:3TIX"; STRAND 889..891; /evidence="ECO:0007829|PDB:3TIX"; STRAND 923..928; /evidence="ECO:0007829|PDB:3TIX"; STRAND 941..944; /evidence="ECO:0007829|PDB:3TIX" HELIX 18..20; /evidence="ECO:0007829|PDB:2RSN"; HELIX 49..51; /evidence="ECO:0007829|PDB:3G7L"; HELIX 57..60; /evidence="ECO:0007829|PDB:3G7L"; HELIX 64..72; /evidence="ECO:0007829|PDB:3G7L"; HELIX 541..544; /evidence="ECO:0007829|PDB:3TIX"; HELIX 550..558; /evidence="ECO:0007829|PDB:3TIX"; HELIX 570..576; /evidence="ECO:0007829|PDB:3TIX"; HELIX 596..606; /evidence="ECO:0007829|PDB:3TIX"; HELIX 627..632; /evidence="ECO:0007829|PDB:3TIX"; HELIX 653..660; /evidence="ECO:0007829|PDB:3TIX"; HELIX 675..682; /evidence="ECO:0007829|PDB:3TIX"; HELIX 692..694; /evidence="ECO:0007829|PDB:3TIX"; HELIX 707..718; /evidence="ECO:0007829|PDB:3TIX"; HELIX 731..734; /evidence="ECO:0007829|PDB:3TIX"; HELIX 745..747; /evidence="ECO:0007829|PDB:3TIX"; HELIX 751..753; /evidence="ECO:0007829|PDB:3TIX"; HELIX 757..762; /evidence="ECO:0007829|PDB:3TIX"; HELIX 818..823; /evidence="ECO:0007829|PDB:3TIX"; HELIX 827..837; /evidence="ECO:0007829|PDB:3TIX"; HELIX 850..861; /evidence="ECO:0007829|PDB:3TIX"; HELIX 867..882; /evidence="ECO:0007829|PDB:3TIX"; HELIX 894..896; /evidence="ECO:0007829|PDB:3TIX"; HELIX 903..918; /evidence="ECO:0007829|PDB:3TIX"; HELIX 932..934; /evidence="ECO:0007829|PDB:3TIX"; HELIX 946..952; /evidence="ECO:0007829|PDB:3TIX" TURN 61..63; /evidence="ECO:0007829|PDB:2RSN"; TURN 527..530; /evidence="ECO:0007829|PDB:3TIX"; TURN 687..691; /evidence="ECO:0007829|PDB:3TIX"; TURN 748..750; /evidence="ECO:0007829|PDB:3TIX"; TURN 838..841; /evidence="ECO:0007829|PDB:3TIX"; TURN 919..921; /evidence="ECO:0007829|PDB:3TIX" CHAIN 1..960; /note="Chromo domain-containing protein 1"; /id="PRO_0000080238" MVSVKPLPDIDSNEGETDADVYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKKRKKLIAKGLLEPFDAEDNEAKKMKREKEILRQQRQKRKSELTQLSQKVKEKFKKMRKKPARRIVTIANDEEEEDDQTMDEDAFERKSMQGELKERNLTDKTSTLSTSFGETSPDVNPFYLSEWPTVTDSILLSKSLSSDAIPLKNGEIKSTMLMPSDSDNSVPGIQNSNNLENTGAFVENANSPQSNTPLSTFRHSSPLSLSPVITSDNDVANSLFFSNSTPLPSSLKIKKEAPKLETHTILVSDNSGSLTKQDILSYFAFIKGNIEVFFLKSPKKDKVCNMAYIQFDSIEQAKLAYDKGHPSWHVTLVKGKISTDMEECKVSKSILKTTPSKKANARSVSFTQTTTDTLSESEKFASNVDLDENFDFNVNVTNEDAKQLKKSVIGSSWTTVNNDWNSVSKSDQTFENDGASKVVPAGNITLNSDNSLHHSISESEDLSSASTLSDYFRFVLRVGKSLYYAGELSFDISKLKAETEHQQLLRSLVSCKQVDVLRFVTSQYLEVFGTCLTKVLSGSLCIRSDVDMTHFKNILNRGNGAGIVLGSNYTLLLFTEDNNALMNLYDCQGQSNSPFWMVIFEPLESILVEWSAKNLRPKKPYHKSQSYLSYLLQLGHIDLHKIGAFQATQILIVSKQPSPEAEELEDTFREAAIPTFRGLEIPESLFLSQNVFVFLNVSLEDDFDQLQFLTLAKRKSCKFFLFGLSLPLKSPNDSHVGTDFKKNNEPLDKLTYSQYLRPMFPKGGVVSVTLSALIKTPRLLELISPFLEIKKDSWILILPPSIVDMVKSYFVTNNPDKSLLEIQNLLNTLQRYLTNPALKNVTLYQDWDIVIDDSADVSLASTLQLYQKKNYDKYRRFVLIHELKNELTPVNGLDIVDYDEFKETFMRAIGLK Q10109 LEM2_SCHPO MOD_RES 683; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 684; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC18G6.10; HELIX 261..273; /evidence="ECO:0007829|PDB:5YCA" CHAIN 1..688; /note="Lap-Emerin-Man domain protein 2"; /id="PRO_0000116460" MDNWEDPNFELRNLRVIDLKKILHESGVSFPVNARKIEYIRMVDRIRKNKLSSGPQHLLSHLQKEENSNTSKASSSEDEIAPKYLYPSSPSKSTKKPHNETEPLLSPQFIDKPSNIETPVKIESPHVSQNNTFQSYSELSPNVETSLTMKTPPAHASTPKFRSHKSHRVAVPMSFMDSSALHTSPAFSERLKLLSSSNNFSPQLRSPKISHRLQTSATSSPLQHKRPFTNVPERVSRDIEFAPLDSARPSESSSPYSEVDSAEEDDELFQNYVLQQTRKESKLWSFIKKVFHDIKYANYRLLHNLRAFPGISAISSSYLVHIFMILLGVVAAIFLALLREKMFTAGFCDSGASGSSASILGISFPSLCRTCPPNAICPSPNYVECKPGYVLYEPWYSSLGFWPSKYCVSDTSREESVNIFREECLSVLRSWNAILHCSNNSSDLLERNMSYNAHPYVADNLNISSDHISFPSKPFALGLLHDTLLERKSPTLGLEMFEDLFKASLAVLSETNEVVMDSKLICYDSWAGIPLRCRLKQQLIKFVWRNKVFLFGILALSGVIFKLINFFRTRSIVAKYLPSASRFCVESLKRQKANYQMSRSQEPVIPLIEMHDILFHGNGPLEQIHMTKATARTLWEAIVERVEQVGSVRTRESEVDGEWTRVWEWVGTNTLDFQTDRSFINTTSPLRE Q10113 MAL3_SCHPO SPAC18G6.15; HELIX 177..220; /evidence="ECO:0007829|PDB:5M97"; HELIX 227..239; /evidence="ECO:0007829|PDB:5M97" CHAIN 1..308; /note="Microtubule integrity protein mal3"; /id="PRO_0000213431" MSESRQELLAWINQVTSLGLTRIEDCGKGYAMIQIFDSIYQDIPLKKVNFECNNEYQYINNWKVLQQVFLKKGIDKVVDPERLSRCKMQDNLEFVQWAKRFWDQYYPGGDYDALARRGNRGPANTRVMNSSAGATGPSRRRQVSSGSSTPSMTKSSANNNNVSSTANTAAVLRAKQAQQQITSLETQLYEVNETMFGLERERDFYFNKLREIEILVQTHLTTSPMSMENMLERIQAILYSTEDGFELPPDQPADLTTALTDHDTNNVAEEAQMTDLKDSETQRVPSAPDFVHARLQSLEVDDDENITF Q10133 RHO2_SCHPO BINDING 15..22; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 62..66; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 120..123; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 197; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC16.01; PROPEP 198..200; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281271" CHAIN 1..197; /note="GTP-binding protein rho2"; /id="PRO_0000198941" LIPID 197; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MLQSQPIRRKLVVVGDGACGKTSLLSVFTLGYFPTEYVPTVFENYVSDCRVDGKSVQLALWDTAGQEEYERLRPMSYAKAHIILVGFAIDSPDSLENVSTKWIEEINTLCPNVPFILVGMKADLRSDPVAIEEMRRRNQNFVKSQQAELVAQRIGARKYMECSSLTGDGVDDVFEAATRAALTVRDSENDKSSTKCCIIS Q10134 FEP1_SCHPO MOD_RES 109; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23E2.01; CHAIN 1..564; /note="Iron-sensing transcriptional repressor"; /id="PRO_0000083476" MAAKPAPFGQSCSNCHKTTTSLWRRGPDNSLLCNACGLYQKHRKHARPVKSEDLKDISPLIQQVCKNGTCAGDGFCNGTGGSASCTGCPALNNRIRSLNASKSQSGRKSLSPNPSSVPSSTETKASPTPLESKPQIVSDTTTETSNGTSRRRSSHNQHEDSSPPHEPSVTFCQNCATTNTPLWRRDESGNPICNACGLYYKIHGVHRPVTMKKAIIKRRKRLVFNGNANESQHNLKRMSSGDSGSSVKQQSTRDGPFSKSFPNGNGHASGNSGEGLAEHGMNTGVLPPASTFPSYNSNFTGFLPSSFNPSPLMTLSRLAAGEPDNNGKVYYSYGPTQEQSILPLPENKHEGLPPYQNEYVPNGIRANQVVYPGQLVAVGNDSSKQLSESTTSNTDNNGVATANQSNPLGMKFHLPPILPVGESVCLPPRTSAKPRIAEGIASLLNPEEPPSNSDKQPSMSNGPKSEVSPSQSQQAPLIQSSTSPVSLQFPPEVQGSNVDKRNYALNVLSQLRSQHDLMIQELHNLNQHIQQIDEWLRSSDNENMASEHIKSSTPAVVASGALQT Q10135 LSD2_SCHPO BINDING 509..551; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255"; BINDING 517; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 550; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 558; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 572..573; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 1147; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 1156..1157; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; SPAC23E2.02; CHAIN 1..1273; /note="Lysine-specific histone demethylase 2"; /id="PRO_0000116463" MPLGRSSWICCAKYFVNTKSRFNEILPPRFTLIVSFYSMNTSENDPDGHYDFPEMTEHHSDRASSYANANNVNSTQPQLVSSEQALLAILGGGLQSITPNSVNQNAYSRSTYRTDGGLNSQPVSSLNNQWGNYNPAFLPSRYDSSFHPYTISQAANQPFPQHLLGNSNAGVAQQSGMRTIGLPPTVGSSFPQQKSSTYENFFDANSPSSQQFPSTYPSRSQNPLSSSGDGSTAIHAGPIQHQNSNAFSNYPYPLDASHLSSQQLLSMYRDQVSHGVTPSTFRNHESFMPTQLVSATELSKSVDNAVLPIPPTTAPAVVSPPASSFPLMSSAATSGNISSPALFDSELGARPEGSVAIEPSRVLLQWSSQSSSHTIPSAGASIPTSSLKSFFEHAAEAARKCNLDPRALESFEQHMLSDRLHDPVVLFHYFQIRNSICWLWIKNPTHAISRVEAQGVCVDRCLFQLASLAYEFLVRYGYINYGCLSFDSSFTNETNTGTTSSSASKQKTIAVVGAGLTGLICARQLTGLFSQYSSSFLSKNELPPKVIILEAKERTGGRIYSRALPVSHTSATQINHHTSNSNSISSNSTSLNPKDVTDPSHIPSAIDLGFQFLFSPMDDILLNLLNKQLGIEVTEMTGSDLVYDETDTKVLDMVEVKKLNILWEKLLEYVSVCFFINVEESVRISWISQFQLFIDEMFPDHLSKSLSLNASHEFSFKKTMLILIDEVSSYAKLGNSQKKFLIWCFKVAELDDTLYPLNTVDTDFSKDILIPKVARRGLSQLPWALQSYPSPLNIHYEKFVSKVTIENDKCTLDCKDNSSYEVDQVVIACSPSHFSSNIEFSPGLPNFVTENIKSIDFKPGKKVILRYAAAFWRKNIRSFGIIPKSLSQEMNNDENDGKSCFVLRIWNMLPETGVPILVADINPQMTSSSSNETSHLIQELHSLIVDHFQNDSNSSADLLDAWVTNWSRNGVYDGLNSYPNFANDKQQYEKRFRQSQLSYNLGRLHIAGDYIFSCVGCRTLQRSFLSGLSVCTGIIDSLAPISLTIPIIGETSRKELDQFLRNSKVNNFDPNAEAQRHLSYQARYRLKKQERLDEHKEEQEQLVTELLGYLPEPPSKPNANPFLLYQKMQWHVCRALADEDKRRLTGDSTAKATINETRAKLGKTWRQLDDLGKKPWIDEIAAQREAYAGKILRYQRLTKEYEMRAEQIRNDYAAKCQDEPIPDDEARLFMQAQREEEQRKQTQDDNISKSREASDEEYHDDGSSDSGYNGTRY Q10137 SEC14_SCHPO SPAC3H8.10; CHAIN 1..286; /note="Sec14 cytosolic factor"; /id="PRO_0000210742" MSETISDPYPLTNPNAPLGHPGHLNSTQQATLDSMRLELQKLGYTERLDDATLLRFLRARKFNLQQSLEMFIKCEKWRKEFGVDDLIKNFHYDEKEAVSKYYPQFYHKTDIDGRPVYVEQLGNIDLKKLYQITTPERMMQNLVYEYEMLALKRFPACSRKAGGLIETSCTIMDLKGVGITSIHSVYSYIRQASSISQDYYPERMGKFYVINAPWGFSSAFNLIKGFLDEATVKKIHILGSNYKSALLEQIPADNLPAKLGGNCQCPGGCELSDAGPWHEEQWMNKN Q10146 RRP6_SCHPO BINDING 243; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 243; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 245; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 245; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 245; /ligand="UMP"; /ligand_id="ChEBI:CHEBI:57865"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 245; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 246; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 246; /ligand="UMP"; /ligand_id="ChEBI:CHEBI:57865"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 301; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 304; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 304; /ligand="UMP"; /ligand_id="ChEBI:CHEBI:57865"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 347; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 347; /ligand="UMP"; /ligand_id="ChEBI:CHEBI:57865"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 350; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 350; /ligand="UMP"; /ligand_id="ChEBI:CHEBI:57865"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 370; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q12149"; BINDING 370; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q12149" SPAC1F3.01; CHAIN 1..777; /note="Exosome complex exonuclease rrp6"; /id="PRO_0000116595" MDESELFKGLMNSTAYCSELAKVDIPFYKSIDTEFNENIKSVSSRFMRLIELLLSKVDRSRAEDIVDVEDIDNRWAEVSDTLDILFEKADYSIDKAQGLLKKPAIETHASTSDVANKKPKKEKLPYKVIHAAHLTKPQLRFRVQPNNSREFVWSWKLTEKPHSLVPLEKIIAQVKLDPSLKNSLPHPYEPEIQNSVYPPWVSEMSNPIDTGSVDETEPIWVSTESQLSDMLKELQNSKEIAVDLEHHDYRSFRGFVCLMQISNREKDWIVDTLELREELEALNVVFTNPNIIKVFHGATMDIIWLQRDFGLYVVNLFDTYYATKVLGFEGHGLAFLLQKYCDYDADKRYQMADWRIRPLPREMLKYAQSDTHYLLYIWDHLRNELISKSAERKENLMQSVFNSSKQISLRKYELEPYDPIYGLGTDGWRNVLTKFGSSKIIGREALMIYRALHDWRDSVARKEDESVRYVLPNRLLIAIAASKPVEAADVFSISKQLTPIARMYVEDIVKVVQEAEKLYNEQVDREKSQFKEVEKQNQPLAVFSESNTLGDYKVDSSVFEISKQNRSKLKTLLANGSAFWIEGQSQDDLRKARKERLFIVNQNIPFSLTLPCTQGHVESELNVKQSTVTEAANPSLNGEKKQEPIVIRDLGLNKQKRDSSKLNHKEPSNPIEERNEDIEPSEASTSVSKKRKQKKKKKNSGKLTIEAEHVSNDSPIINEAPFDYKNQKNFIADLDSDVGKNKFGKRGFNPLNKVSLPKRNTRELKKRKVSDGKSTSY Q10156 LKH1_SCHPO ACT_SITE 488; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 368..376; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 391; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; PTM: Autophosphorylates on all three types of residues. {ECO:0000305}. SPAC1D4.11c; CHAIN 1..690; /note="Dual specificity protein kinase lkh1"; /id="PRO_0000086236" MHSLKRRRNHAPDWQDFYKNGVPQEVIVIEDSASPRLTPNLPPPFSVHQLQSFVPPQPPSSSSPSTTGTVAVPINGANAVYPSTNSVSLPQSYDPWLDANGVVPLPHDVASHPSYMVQSPTSYHACSNNQSPFPHSHHPPLHNPLPVSCQPVLRPPPVPQVPSHWYPVSLPSPNLPHQPISKPPVIPNLPKLQVHPNRLPHPIHNHPYSSPTSYPPPLCPATYCPSNPPQLAPATAIAPSSQSSQHKSVNYSVTPSSINNHTAVPLSPTLAVWLPMTQPTFQPPSANVYQPASNANQVITPVSISDYRPPKKRKRAAWPPYKKVDRVNVPVVHDTTAFDPSTFDDDDGHYKVVPNSKFANRYTVVRLLGHGTFGKVIQCYDQSTGRHCAIKVTRAIPKYREASLIELRVLQTIAHSDPTNENKCIQLRDYFDYRKHICIVTDLFGWSVFDFLKNNNYIPFPLKHIQMLSQQLFKSVAFLHSLGLVHTDLKPENVLLVSNASRTIRLPYRNYSQKVLNSCEIRLIDFGSATFEDEYHSSVVSTRHYRAPEIILGLGWSYPCDVWSIGCILVELFTGQALFQTHEDSEHLCMMEKILGPFDRNMISRSSRTSQRFFKSDGKVRYPLSNTPKKSINYLQSLQTLEQIFAVSSPEVALLLDLLKKVFVYDPKRRITAKEALWHPFFTQPISSNL Q10159 MYH1_SCHPO ACT_SITE 69; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P83847" BINDING 226; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 233; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 236; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 242; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.; EC=3.2.2.31; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand. {ECO:0000250}; SPAC26A3.02; CHAIN 1..461; /note="Adenine DNA glycosylase"; /id="PRO_0000102242" MSDSNHSLDLHSYTQLEVERFRESLIQFYDKTKRILPWRKKECIPPSEDSPLEDWEQPVQRLYEVLVSEIMLQQTRVETVKRYYTKWMETLPTLKSCAEAEYNTQVMPLWSGMGFYTRCKRLHQACQHLAKLHPSEIPRTGDEWAKGIPGVGPYTAGAVLSIAWKQPTGIVDGNVIRVLSRALAIHSDCSKGKANALIWKLANELVDPVRPGDFNQALMELGAITCTPQSPRCSVCPISEICKAYQEQNVIRDGNTIKYDIEDVPCNICITDIPSKEDLQNWVVARYPVHPAKTKQREERALVVIFQKTDPSTKEKFFLIRKRPSAGLLAGLWDFPTIEFGQESWPKDMDAEFQKSIAQWISNDSRSLIKKYQSRGRYLHIFSHIRKTSHVFYAIASPDIVTNEDFFWISQSDLEHVGMCELGLKNYRAALEIKKRKVTSLSNFKEPKLTSARRIVTKAEC Q10163 RSMB_SCHPO SPAC26A3.08; CHAIN 1..147; /note="Small nuclear ribonucleoprotein-associated protein B"; /id="PRO_0000125528" MGTTKMVSLLNHSLNVTTKDGRTFVGQLLAFDGFMNLVLSDCQEYRHIKKQNVPSNSVYEEKRMLGLVILRGEFIVSLSVQGPPPMDPSMRGSLLSGPGVARPAGRGIPLGQAPVGLAGPVRGVGYTAPPPPAGFGRGAPPPGFRPV Q10168 NSP1_SCHPO MOD_RES 489; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26A3.15c; CHAIN 1..598; /note="Nucleoporin nsp1"; /id="PRO_0000204921" MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNSTNASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTNTTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSNTTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFTKPATSTGDNKPTFSFGNTSKPTENTSTTATSAPPLSNNTKPAEGANQTSSGFSFGKPATDTTTSTSKTGPLFGNKPADPSAKPGATASTTPSEPPPSSIKHKTLQEILNKWSTDLTTQTEVFNKLCDQVSDWDRTLVDNGALISKLYTETVEAEQMSNRIDDGLEYVSSSQQELFKLLDSYETQLETFDGRATSALNVERERAFGVADDILSRLDRLGEDLGTVINQMNDFSKPDDSISEIVKVLNAQLASLGWVENRIFQMEEKLDTIKKKNSDVLF Q10173 NUF2_SCHPO MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC27F1.04c; CHAIN 1..441; /note="Kinetochore protein nuf2"; /id="PRO_0000057994" MARKHTFPSLKRAEILECIDGLGIPFTAKELDQPTSKAVIPLYEEFLDLFMGLTRQNLEEKVNSLQDSVENFEIIHESLRFTVFYQILSQFMQNICFHDFTIQDLLKPDRNRLQLILSAVINFAKLREERLQQFDDDIQKRESLLETYTLLDAQRKDLEEKVLLSQDRKLESEAIIKQNEERNEEMFQSLIEDKRLCSQVRTEYDRIRMEASELKIRYHNVDSLMASTLEEIEKLQSSIVHSPEKLKGKIADTSLRIQNDRSQQVELDKKSKILHTKLNSLQLIEGDLNACLKVLEECLVELDKLEHATVLLSTNQELCDQIEINKKKLEFRKEQLLKQLSNAQEKLEHEQHSRNQKLEAAKQRMDNIREEYKVITQERNKKIQETEKKNAMIEMTEQKIAGMREELESQISSITMEFEKLKSHVELYIAELLRNLRSSNS Q10178 SF3B1_SCHPO SPAC27F1.09c; CHAIN 1..1205; /note="U2 snRNP component prp10"; /id="PRO_0000174326" MSTGTYPYKMFKMDVTNLNKVEDVEIERLRAERELLRRQKEAAKNSSTNGSVNIEGTQDSNDLQYNAHLFKSSNPKEEYDSAIDVRNDISQDEDDYKRTNDVNDSYRLVRQYEAPKELLNEYADESYDPMQERQSKKQIQDRESDYQKQRYDRQLTPTRVDAFQPDGTQSNGRSYAEVMRQVELEKEERRVHMELNQRRREGTLKEVEEEESISDKKRELELNNTEISQKPKRSRWDQAPPSVTQVSTTKRRSRWDKAPENFTISEHVIENGISEDLINKEVNVVEEKLRPPVRLLTEEELNELLPSEGYAILEPPPGYLESIHPELLQKGTTLDTYHVPQEQELPLEKELPAALPTEIPGVGDLAFFKQEDVKYFGKLLKVEDEAKLTIAELRERKILRLLLKVKNGTPPMRKSALRQLTDQARDFGAAALFNQILPLLMERTLEDQERHLLVKVIDRILYKLDDLVRPFTHKILVVIEPLLIDEDYYARAEGREIISNLAKASGLAHMIATMRPDIDHVDEYVRNTTARAFSVVASALGVPALLPFLKAVCRSKKSWQARHTGVRIIQQIALLLGCSILPHLKNLVDCIGHGLEDEQQKVRIMTALSLSALAEAATPYGIEAFDSVLKPLWSGVQRHRGKSLAAFLKATGFIIPLMEPEYASHFTRRIMKILLREFNSPDEEMKKIVLKVVSQCASTDGVTPEYLRTDVLPEFFHCFWSRRMASDRRSYKQVVETTVVLAQQVGSRQIVERVVNNFKDESEPYRKMTAETVDKVIGSLGVSEIDERLEELLLDGVLFAFQEQSVEEKVILTCFSTVVNALGTRCKPYLPQIVSTILYRLNNKSANVREQAADLVSSITIVLKACGEEALMRKLGVVLYEYLGEEYPEVLGSILGAIKAIVSVVGMSSMQPPIRDLLPRLTPILRNRHEKVQENTIDLVGKIADRGSEYVSAREWMRICFELIDMLKAHKKSIRRAAVNTFGYISKAIGPQDVLATLLNNLKVQERQNRVCTTVAIAIVAETCMPFTVVPALMADYRTPEMNVQNGVLKSLAFMFEYIGEQARDYVYAITPLLADALMDRDAVHRQTAASVIKHLSLGCVGLGVEDAMIHLLNILWPNILEESPHVINAVREGIDGIRNCIGVGPIMAYLVQGLFHPSRKVRNTYWTSYNSAYVQSADAMVPYYPHVDDDQFNNYDMKTLHICI Q10179 SYG_SCHPO BINDING 221; /ligand="glycine"; /ligand_id="ChEBI:CHEBI:57305"; /evidence="ECO:0000250|UniProtKB:P41250"; BINDING 253..255; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P41250"; BINDING 264..265; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P41250"; BINDING 272; /ligand="glycine"; /ligand_id="ChEBI:CHEBI:57305"; /evidence="ECO:0000250|UniProtKB:P41250"; BINDING 380..381; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P41250"; BINDING 499..501; /ligand="glycine"; /ligand_id="ChEBI:CHEBI:57305"; /evidence="ECO:0000250|UniProtKB:P41250"; BINDING 506; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P41250" CATALYTIC ACTIVITY: Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000250|UniProtKB:P41250}; CATALYTIC ACTIVITY: Reaction=2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl) tetraphosphate; Xref=Rhea:RHEA:34935, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58141; Evidence={ECO:0000250|UniProtKB:P41250}; SPAC3F10.03; CHAIN 1..652; /note="Putative glycine--tRNA ligase"; /id="PRO_0000073004" MTEVSKAAAFDRTQFEELMKKRFFFSPSFQIYGGISGLYDYGPPGSALQSNLVDIWRKHFVIEESMLEVDCSMLTPHEVLKTSGHVDKFADWMCKDPATGEIFRADHLVEEVLEARLKGDKEARGQNSNDQPEESDDKKKRKKKVKEIRATRLDDKTVEEYEFILAQIDNYDGDQLGELMKKYDIRNPATNGELETPRQFNLMFETQIGPSGGLKGYLRPETAQGQFLNFSRLLEFNNGKVPFASAMVGKAFRNEISPRSGLLRVREFLMAEVEHFVDPKNKEHDRFDEVSHMPLRLLPRGVQLEGKTDILEMPIGDAVKKGIVDNTTLGYFMARISLFLEKIGIDMNRVRFRQHMSNEMAHYACDCWDAEIQCSYGWIECVGCADRSAYDLSVHSKATKTPLVVQEALPEPVVVEQFEVEVNRKKFGPRFKRDAKAVEEAMISWPESEKVEKSAQLVAEGKIIVNVNGVEHTVESDLVTIEKRKHTEHIRTYTPNVIEPSFGLGRILYVLMEHAYWTRPEDVNRGVLSFPASIAPIKALIVPLSRNAEFAPFVKKLSAKLRNLGISNKIDDSNANIGRRYARNDELGTPFGLTVDFETLQNETITLRERDSTKQVRGSQDEVIAALVSMVEGKSSFEDALAKFGEFKSTQE Q10185 ABC2_SCHPO BINDING 631..638; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 1273..1280; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" MOD_RES 839; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 843; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 863; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3F10.11c; CHAIN 1..1478; /note="ATP-binding cassette transporter abc2"; /id="PRO_0000093468" CARBOHYD 86; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 139; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVLEQDLDPFVGGNWMNSAYKGFTFLSATWLAPNIYLLISGCLQYFYEVRKRSHYFHFRRFWTIWLKSLVIMVLLFTHIYDCYKTNESVWNVLSIITYFLALFLHVVEQPTLRIPMASLLMFWLFKFLASALVLLLRPNYTMFPMLNVVPSITFFCSLVCLLAEIYVPPANRVWYPDDAAELEETGLRPSRFTYANIFSRISFGWLSPLMKFGYRNYLTESDAWSLPPAERSSNLTIVFEKNWISHAKKKKSSLYMWGVLFLNHWKLTVVIIVLKLVQDVVAFIQPNLIRKIVIFVSSYSSEHPQPPQVGFSLAIAMFLTNVVQTALLQQYFQLGMVLGMRWRSELITAIYRKSLRLSSAARQSRSVGDIVNYMSVDTQKVCDLTMFLFVIVSGPFQIVLALTNLYHLVGYGALSGAFVTFLLFPCNVVIASIFKRFQNRQMKNKDARSQFMTEIINNIRSIKLYAWENIFLQKLLQLRNTRELRMLKKIGIVNTIGNFTWLFAPILVSAATFGTFIVLYGKTRVLSVDIVFACLSLFNLLQFPLTMLPIVVSSVLEASVAISRIYGFLTAGELDSNAVQRYPANKEPSGVCLEIKKGTFSWSGPGQNAAEPTLRDIDFVARRGELCCIVGKVGMGKSSLLEACLGNMQKHSGSVFRCGSIAYAAQQPWILNATIQENILFGLELDPEFYEKTIRACCLLRDFEILADGDQTEVGEKGISLSGGQKARISLARAVYSRSDIYLLDDILSAVDQHVNRDLVRNLLGSKGLLRSRCVILSTNSLTVLKEASMIYMLRNGKIIESGSFTQLSSSPDSQLFQLLSEFSKKDTASSTGADTPLSRSQSVITSSTDVTSSASRSSDTVSNYPKATIKGTGRIRKRLTDEDNVKATGQAAEKMERGKVKWKVYWTYFKACSLFLIFLYFLFIIGGIGMNVGTNVWLKHWSEVNTQLGYNPKPYFYLGIYTLFGLLSCALISLSSLTITVFCAIKSCRYLHDSMVKAVLRAPMSFFETTPTGRILNRFSSDVYRVDEVISRVFMFFFRNLFQIVFVLAVICYSSPMFMILIVPLFFLYRYNQVYYTQTSRELKRLDSVTRSPLYAHFQESLGGLSTIRAYDMEDTFISENDIRVDTNHRIWFLYFSSNRWQAIRVEAIGALVVFSSAFFGVLSAVRGNPNSGLVGLSLSYAVQITQSLTFVVRQSVDVETNIVSVERMLEYIGLPSEAPSIIPDHRPPEGWPSHGAIKFDHYSVRYRENLPLVLNDISVNIKPQEKIGIVGRTGAGKSTLTLALFRLIEPTSGDIQLDDINITSIGLHDLRSRLAIIPQENQAFEGTIRENLDPNANATDEEIWHALEAASLKQFIQTLDGGLYSRVTEGGANLSSGQRQLMCLTRALLTPTRVLLLDEATAAVDVETDAIVQRTIRERFNDRTILTIAHRINTVMDSNRILVLDHGKVVEFDSTKKLLENKASLFYSLAKESGLI Q10197 ALP1_SCHPO SPBC11C11.04c; CHAIN 1..1105; /note="Tubulin-folding cofactor D"; /id="PRO_0000064568" CARBOHYD 122; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 126; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 373; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 721; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 883; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1083; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MEEEESLEGIISIDESLITSRLSQILDDVLDDRSSSHSVEKLKDVAVKYLQFCQFQPTLLDKLLSKYVPNLASYLLKVKNIGKCNSITVILYQFCKIRGYKAVRVLFPVGVQYIKELYTLLNESSNNTWHFHYIVLLWLSQALNTPFPLNSLDDSLDVKKTIYTIAIKYLENSGIDKEASCLVLSRLFSRDDGLDLLLGFLHHCESSWFKRSIFYKIGCLFSLSSFLKICPRNDCLQTVDVAFQFLNVAREDLVGQENSALRKLLCKCYTRLGIVLLPVNSSPNWKYSISNPDSFFQLPDDSNEEVHIYLEVIVDFLLSSVSDIDSFVRWSAAKGLAKIISRLPWNLAEQVIDAIIELMTENMFLNPIENTVNISITSPLVWHGAILFFAKLAGAGLIKYSKCLHILPLIEVGLSYEVRYGTRVTGQSIRDASCYFVWSFYHCYSKSAIEGLQTNLILCLLQTVLFDNEINVRRAATAALFEVIGRHASIPDGLSLISHINYVSVTDISNCYGDLCMKVAHFPQFRSCVFQRLFTNLQHWDVKVQQLSAFSLRQLSIKYPKELSIYLPPILDYLSVGNADFIFGYTIGLASIIGGFLSISFPFDINRIHDLLSHKNLLSLKKFSRQQQTKIILGILKGIQQIFANDIRVDRAFFSEAFSVIIAAIDLQEETIIKDISDAYSVLVKFDDMEETLEVLLDYIRKCSTSKEARIVYIILQNLPNISFRYQKKICKLLLDIYPQLHSIDYQAPVANALQNIIPFTYEKTESIEEFVKELLQVCSNYLTDTRGDVGSWIRKPAMKAISSLLVKDSSGKKLSEDIVWCCISYIIRQTFDKIDSLRGLAYQALEQIRVHYLIRRCEALTNIINRIRNNPNMDGEVLNELNISLLEIPNLRLQAFYGITVFTADGFGSDLAVKCFEFYLSYVYQLEDSFKKSNSRYGKRDLLQLYIDILSSEDEIARFYFPIMKSFTSLLAYGCFTDFQNVKGMSKAIFIVQRRALTCKSPGGLSAILELYRTLFLSKNELLRHHALKYTANLLLNPIEKVRYQAADTLLYAKSIGLLTFLPNELNQKLLTLDWFVPVSQNATFVKQLRNIIQKQIDKLIADR Q10198 NDC80_SCHPO SPBC11C11.03; CHAIN 1..624; /note="Kinetochore protein ndc80"; /id="PRO_0000116533" MQDSSSYARRYSQAPSSSNLRTTTFGFNGLGTSRTSLAPQRTLVNARQSIDPDGLSSRVLTPTMRPSLAPNTRRSSVRVSNASFISQTPNITSIKDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIFKHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVEQNSLDDHLVDKVLFDYLVRTYHLYLDESPEESEPEKELKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQASIDSLEKKVQKFNSLAYRIGIVPIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNSMLQLDQRIQSINIEADQIAHACMEYKNNIYKEVAFVLGEIIHFKLHVQDSLEDLKMDYQKELDDLSRSEL Q10199 IMP2_SCHPO MOD_RES 397; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 531; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC11C11.02; STRAND 280..284; /evidence="ECO:0007829|PDB:5C1F"; STRAND 304..306; /evidence="ECO:0007829|PDB:5C1F" HELIX 18..21; /evidence="ECO:0007829|PDB:5C1F"; HELIX 28..69; /evidence="ECO:0007829|PDB:5C1F"; HELIX 79..108; /evidence="ECO:0007829|PDB:5C1F"; HELIX 111..165; /evidence="ECO:0007829|PDB:5C1F"; HELIX 166..168; /evidence="ECO:0007829|PDB:5C1F"; HELIX 172..262; /evidence="ECO:0007829|PDB:5C1F"; HELIX 266..277; /evidence="ECO:0007829|PDB:5C1F"; HELIX 292..294; /evidence="ECO:0007829|PDB:5C1F" CHAIN 1..670; /note="Septation protein imp2"; /id="PRO_0000084186" MSQQLSFNASSAKPDKSFSNYFWGANDEGYHALLSRFSDVKHINEELRSFYHERANIEEDYAKRMAKLSRTTFSSLETGCLKESVQVMKAEVDNMAKSHLQISQLLQDDVENAFTRYAASLKDKKKMIVSGIEKVHKDKLSKHQALVKAQDKYHYLCKKVNYYVSQQNMLFGKELEKNNAKLNKTQNAITASSSDYQSAVAAVRDSYARWTNEWRSTCDKLQDIEEERRHFLKSVMWTFTLLISRSCFNDDQACERIRKNLEQCSVSQDVLEFIDAKSTGTGIPQPPKFYDYYKGEVPDDSVELVQANFQRAQTKIENDNMPLNRPYVLSATARNESSFENTLPNTPSAIQSLTTVSSNSSQNGRSSPKKSFLSKFKLTSRPSTPNVGNTAPDALSSPRNDSPLTSAADEQMKHLSLQEEPKQNPTPAAPGAFPNSNTLPPRYNELGSLPSPNSVSFTEDSRPNVNTPSRRQQIQEEFGSVLQMENRAVSPVYDSRKNGSRSSFTLRKSRSPKRPSSSLSQNASRLPRSLTPGNLEPNYDFGVRVDPASGTAPTDDEPYTDRDSSFVDDTINTKATGNTSNRLSLPAYPTDGGDTSIDNPTSTDGQRILGYVSALYDYDAAIPEEISFRKGDTIAVLKLYEDGWWEGFVVGEDDHNRGQFPSNFVREIEV Q10223 POF14_SCHPO SPAC13D6.01; CHAIN 1..431; /note="F-box protein pof14"; /id="PRO_0000116488" MLQFSFQNCKTHTCYMNTSVNEHLDQDESFLRILIDTRKKIRSSYFKPQTFDEFVHCLARVRAMKRLVSICSNFDEEDNWNGVWNTLVVDGDSHASAMIDYEGLLDKCSLSRNLLELINDYAEYTTQVLPFRKIPSSDNLDSSLNLTVASPKSNLYYRYSSESPKYAKILDCPDEILQLIFSYCYDASYIEKLPFAFSYRKQRHTLIHDLPNTCLRFKKILSPRNVSFWKRLLKVHKKNPNSAVTCSESINTSAVAKFTDIPTIIPIFLDPSYQSYAAKTIHSDTSSLASSIIQTGDGTQSCDESTYIELACNLVGRCVLCNRIPKLTKFKDCITSFYRPSVATNICDQCLEAIIDFYEPVSRYKFDVMKDRLGVGYISRPGQKFPSWLSEHVQLARDEEKAFKSIYHSQGEFARSLFRLFRAQLAELCEQ Q10256 MUD1_SCHPO ACT_SITE 127; /evidence="ECO:0000250|UniProtKB:Q5TDH0" SPAC56F8.08; HELIX 296..305; /evidence="ECO:0007829|PDB:1Z96"; HELIX 310..319; /evidence="ECO:0007829|PDB:1Z96"; HELIX 324..331; /evidence="ECO:0007829|PDB:1Z96" TURN 320..322; /evidence="ECO:0007829|PDB:1Z96" CHAIN 1..332; /note="UBA domain-containing protein Mud1"; /id="PRO_0000096643" MNNLTPENIRQTILATPFLLNRIRTEFPQLAAVLNDPNAFATTWQSINASQLLQIPSSTYSMGMPSFSEDDLFDVEVQRRIEEQIRQNAVTENMQSAIENHPEVFGQVYMLFVNVEINGHKVKAFVDSGAQATILSADCAEKCGLTRLLDTRFQGVAKGVGMAKILGCVHSAPLKIGDLYLPCRFTVIEGRDVDMLLGLDMLRRYQACIDLENNVLRIHGKEIPFLGESEIPKLLANVEPSANAHGLGIEPASKASASSPNPQSGTRLGTKESVAPNNEGSSNPPSLVNPPTDPGLNSKIAQLVSMGFDPLEAAQALDAANGDLDVAASFLL Q10258 MTHR1_SCHPO ACT_SITE 21; /note="Proton donor/acceptor"; /evidence="ECO:0000250" BINDING 21..26; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 53..54; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 53..54; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 82; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 112..114; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 114; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 130..131; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 153; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 173; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 184; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 276; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.20; Evidence={ECO:0000269|PubMed:12112238}; CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH; Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.20; Evidence={ECO:0000269|PubMed:12112238}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC56F8.10; CHAIN 1..603; /note="Methylenetetrahydrofolate reductase 1"; /id="PRO_0000190253" MKISDKLLHPDWKEKVTYSYEFFPPKTSTGVQNLYNRIDRMKTWGRPMFVDVTWGAGGTSSELTPGIVNVIQTDFEVDTCMHLTCTNMSTEMIDAALKRAHETGCRNILALRGDPVKDTDWTEGESGFRYASDLVRYIRTHYNDEFCIGVAGYPEGYSPDDDIDESIKHLKLKVDEGADFIVTQMFYDVDNFIAWVDKVRAAGINIPIFPGIMPIQAWDSFIRRAKWSGVKIPQHFMDTLVPVKDDDEGVRERGVELIVEMCRKLIASGITRLHFYTMNLEKAVKMIIERLGLLDENLAPIVDTNNVELTNASSQDRRINEGVRPIFWRTRNESYVSRTDQWDELPHGRWGDSRSPAFGEFDAIRYGLRMSPKEITTSWGSPKSYSEIGDLFARYCEKKISSLPWSDLPISDEADLIRDQLLSMNRNAFLTINSQPALNGEKSSHPVFGWGPPNGYVFQKPYVEFFVHPSLLNELKETVKKLNSVSYFVTNKNGDLDTNSQYEIPNAVTWGVFPNREIIQPTIVESTSFLAWKDEAYSLGMEWANAYSPDSISRKLLVSMMKEWFLCVIVDNDFQNGQSLFDVFNKMRSLKDIHPELYYANAS Q10274 TEB1_SCHPO SPAC13G7.10; CHAIN 1..390; /note="Telobox protein 1"; /id="PRO_0000197147" MRSMKPPGFSSDLMDEHSVDLLNGSILAAENPSKREVAQDVPGFERKPTKVRKPRVKWTEKETNDLLRGCQIHGVGNWKKILLDERFHFTNRSPNDLKDRFRTILPEDYKKFYPNAKTHMGRPQKIPHTVGLSKSTRKERKQFTPEEDERLLEGFFLHGPCWTRISKDANLGLQNRRSTDLRDRFRNAFPERYAAAGFKLKNNPGNRSKYYQNNMVNDATTPNDSSTTEAAAAAVAAVAAVAASNPNASPQQTTEQPASDELLDWPHHNLPSQFFTSQRNPNYSTDSFLLGQSLSDPFNHTLQSFHPYESLFSAGQPPSLPISPSTSQNSVQPFPFSIQQPPLHLEPPLSSNTLNSSTLPQPNSTDFNTFPPLPSTPRISSEDIPWDNRG Q10280 GAF1_SCHPO MOD_RES 150; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 727; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 729; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1902.01; CHAIN 1..855; /note="Transcription factor gaf1"; /id="PRO_0000083475" MDLKFSNFFKEAEHPALVKKFDKSTTDESSSKEDYSTMSDLWKMFSKAKSELSNGRRVENLTWRLMSINLQKNLTPNGDSNTLTPDTFSDPTAPSSAQSVPPTSSAETTADNSDTEMKLNPIPAYSVPADTTGSSLMEFNYIQRRVRKTSFDESTAKSKKRSIADSHFPDPNAMQRPHDLESQPFSYPKIHASNSFNFVKRDIDSSNFSNLDASALPISPPSDFFSVHSHNLPNAPPSIPANSNNSASPNQRIKASPKHADTDVLGLDFDMTPSEPSSFPENGGFPSFVDANTHEQTLFPSSATNSFSFEHGSAGFPIPGSVPSTSYHANTASEDGFSSSYNSQGLFGISSPLSSGVTPNQSFFPDVSGNNIFDVSRNNHEVSSPLIQSPGSYVSMPSINMVSSLPISAPVPNSNSQFPRRPNTFRTNSSKSVGQGSSGVDSNQENAESFNPSISSHNSAEWASGETTGHSSNSPLPGSDMFSPQFMRVGTAMGVAPVRSNSSNNFGQNFFHQTSPQFSAVPHRKVSAQDTNLMGSSPGMYNHMPYLNRATSANSITSPGVLPEGMAASLKKRTTNTAATPQAALPTTLDTKKDRSVSFNINKNAEKPTVSNAAEDKKGDANTRRANATNPTPTCTNCQTRTTPLWRRSPDGQPLCNACGLFMKINGVVRPLSLKTDVIKKRNRGVGTSATPKQSGGRKGSTRKSSSKSSSAKSTAADMKPKADSKSISPGFVGGNQSLSSERIPLDPSMRSPLQQQSSENESKSQSMLSANNLNAGVNDFGLGFSEGLGSAHLDSNDSSMVQGKNDFAPVVDSPLFDAFDTDLGMSSVAESHTMNMDPSDLSRVSKSWDWYSVM Q10281 GBLP_SCHPO MOD_RES 10; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 39; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 52; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 255; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6B12.15; CHAIN 1..314; /note="Small ribosomal subunit protein RACK1"; /id="PRO_0000127757" MPEQLVLRATLEGHSGWVTSLSTAPENPDILLSGSRDKSIILWNLVRDDVNYGVAQRRLTGHSHFVSDCALSFDSHYALSASWDKTIRLWDLEKGECTHQFVGHTSDVLSVSISPDNRQVVSGSRDKTIKIWNIIGNCKYTITDGGHSDWVSCVRFSPNPDNLTFVSAGWDKAVKVWDLETFSLRTSHYGHTGYVSAVTISPDGSLCASGGRDGTLMLWDLNESTHLYSLEAKANINALVFSPNRYWLCAATGSSIRIFDLETQEKVDELTVDFVGVGKKSSEPECISLTWSPDGQTLFSGWTDNLIRVWQVTK Q10282 GBB_SCHPO SPBC32H8.07; CHAIN 1..305; /note="Guanine nucleotide-binding protein subunit beta"; /id="PRO_0000127719" MDSGSRVNVNIQGTRVLKNKLGKIPDIDISTDGKYLLSASTNDVLLVWDLHTSNKVAFFEAPSVWIMTCAFSPSTKSIAAGGLNNFCVVYDTSVPDADPVELVGHAGFVSCCKYVDDGHLLTGSGDKTCMFWDIEQAKAISVLKGHEMDIVSLDFLPSNPNLFVTGGCDKLAKLWDLRAAYCCATFPGNTSDINSISFFPSNADFVTGAEDGIARCFDIRASAEIFQYSSPSSSPINSVLFSKSGKLLFIAKDKTCEVWDSISSKTITSLTGHENRISSLALTSDGTMLATGSWDECVRLWSSSG Q10283 HMDH_SCHPO ACT_SITE 712; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P04035"; ACT_SITE 846; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P04035"; ACT_SITE 922; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P04035"; ACT_SITE 1018; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10003" BINDING 718..724; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:P04035"; BINDING 779..781; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P04035"; BINDING 806..814; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P04035"; BINDING 875..877; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:P04035"; BINDING 1017..1018; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:P04035"; BINDING 1022..1023; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P04035" CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000305|PubMed:8896278}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15991; Evidence={ECO:0000305|PubMed:8896278}; MOD_RES 1024; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1028; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC162.09c; CHAIN 1..1053; /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase"; /id="PRO_0000114455" CARBOHYD 137; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 518; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQIPAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDSSSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVLLSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRHFSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGNDSSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAISSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPEKKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDVTRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTMRGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRFCTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTVEDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPATDALKSVNSRVPGR Q10284 SSB1_SCHPO BINDING 15..17; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SCU5"; BINDING 73; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SCU5"; BINDING 204..206; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SCU5"; BINDING 270..277; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SCU5"; BINDING 341; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SCU5" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P11484}; MOD_RES 40; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 151; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 153; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 155; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 256; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 501; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 514; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 515; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 516; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1709.05; CHAIN 1..613; /note="Ribosome-associated molecular chaperone sks2"; /id="PRO_0000078381" MSEVYEGAIGIDLGTTYSCVAVWETANVEIIPNDQGARTTPSFVAFTETERLVGDAAKNQAAMNPRNTVFDAKRLIGRRYEDPETQKDIKHWPFKVIDNNGIPTIEVNYLGEKKQFTAQEISAMVLTKMKEISEAKLNKRVEKAVITVPAYFSDSQRAATKDAGAIAGLNVLRIINEPTAAAIAYGLDAKSDKPKNVLIFDLGGGTFDVSLLKIQGGVFEVLATAGDTHLGGEDFDNALVEHFIQEFKRKQKIDISDDPRALRRLRSACERAKRALSSVTQTTVEVDSLSNGIDFSSSITRARFEDINATTFKATIDPVAKVLKDSKVPKADVHDIVLVGGSTRIPKVQRLVSDFFDGRALNKSINPDEAVAYGAAVQAAVLTNKADSDKTQDLLLLDVVPLSLGVAMEGNVFGVVCPRNTPIPTIKKRTFTTVADNQTTVTFPVYQGERVNCAENEPLGEFQLTGIPPMPRGQAELEATFELDANGILKVTAVEKTTGRSAHIEITNSVGHLSSTKIQEMIENADKFKQQDKDFAKKLEAKSQLESYISNIETTISEPNVMMKLKRGDKSKIEAQLAECMSQLELEDTNTDALRKAELRLKRTVQKAFASLR Q10287 FKS1_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000250|UniProtKB:P38631}; MOD_RES 23; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 784; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 788; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19G7.05c; CHAIN 1..1729; /note="1,3-beta-glucan synthase component bgs1"; /id="PRO_0000121721" MDQYWREQEGRGLFEDDANSYVSDDDTMSSLTRMIYDKNSSRDALHSDYDSSSFNVDSSSVAYPAWNQAGEEAPVTMEGVQEILLDLTNKLGFQKDNMRNIFDYVMVLLDSRASRMSPSSALLTIHADVIGGEHANFSKWYFASHFNDGHAIGFHDMSSPIVETMTLKEAEQAWRDQMAAFSPHRMMVQVCLYFLCWGEANNVRFVPECLCFIFECAYDYYISSEAKDVDAALPKEFYLDSVITPIYRFIHAQLFEILDGKYVRRERDHSQIIGYDDINQLFWSYKGLQEIMCADKTPLLDLPPFMRYRHLSDVEWKSCFYKSYYEYRSWFHNVTNFSRIWVMHISAYWYYSAYNSPNLYTKNYHIRLNNKPPASCRWTACGLAGAIASFITLAAVVFEYIHVPRRYHSARRLWPSMLLLISTLLLNIAPVVFIFASSTKEQHYASRLVVGIVHFFFSLVCVVYYSITPLRNLVGFTTKRSGKNLANRFFTANFTPTSKTGAFVSWCLWITVLVAKFLESYFFLTLNLADSIRFLGAMRPYDCRDYILGAGLCKAQPKILLSLLYLTDLSLFFLDTYLWYILISTIYSLAYAFCLGISVWTPWRELFYRVPRRIYTKLLYTDDMEIVFKPKVLISQVWNAIIISMYREHLISRTQIQELLYHQVPSEKAGYHTLRAPNFFYSQQVKHYKQDLFPANSEAARRISFFAQSLAESIPKTSSIDAMPTFTVLVPHYSEKILLSLREIIREEDQLSRVTLLEYLKQLYPVEWRNFVDDTKLLADENDSVIGSIDNEKNGVNKAYDLPFYCVGFKSATPEYTLRTRIWASLRTQTLYRTINGFSNYSRAIKLLYRTETPELVEWTNGDPVRLDEELDLMANRKFRFCVSMQRYAKFTKEEAENAEFLLRAYPDLQIAYMDEDPQSRHNDERHLYSVLIDGHCPIMENGKRRPKYRIRLSGNPILGDGKSDNQNMSIPYIRGEYVQMIDANQDNYLEECLKIRSILAEFEQLTPPLHSPYSVNAKAADNHPVAILGAREYIFSENTGMLGDVAAGKEQTFGTLFARILSLIGGKLHYGHPDFINVLFMITRGGVSKAQKGLHVNEDIYAGMIALQRGGRIKHCDYYQCGKGRDLGFGSILNFTTKIGTGMAEQMLSREYFNLGTQLPFDRFLSFFYAHAGFHVNNMVIMFSLQLLMLVIINLGAMYTVVPVCRYRQFDSLTASLYPEGCYQLKPVLEWLKRCILSIFIVFGIAFVPLAVCELGERGAIRMVIRLAKQIFSLSPIFEIFTCQIYAQSLIANLTFGGARYIGTSRGFATVRVPFSLLYSRFSGPSLYFGSRLMYMLLFGSITAWLPHYIYFWITLTALCISPFLYNPHQFAWTDFFVDYREFMRWLFRENSRNQANSWIGNCQLCRTRVTGYKRKIYGKKADKIAMDSPRARITTMFYGEILGPLGTLFFTCIPFLFINSQPGNDDETQSTNAFIRLIIMSVAPLVLSAIIAFFFFCLGIMLRPILGDRSKTYGVYLAGVAHFLFVCVDVVVFEVLGYLEGWSFSKTLLGFVAIISIHRFAHKFFIICFLSREFRHDGANLAWWSGRWNGQGFGYMVLTQPWREFVCKTTELNMFAGDFLLSHLLLFLQAPVILIPYIDKLHSIILFWLVPSRQIRPPIYTIRQNKLRRQIVLRYATLYFSLFIAFFVLLILPFVFGKSAAGTSMDKFNLIQPATKIVYSSTKNSSV Q10289 FAS2_SCHPO ACT_SITE 1262; /note="For beta-ketoacyl synthase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"; ACT_SITE 1501; /note="For beta-ketoacyl synthase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"; ACT_SITE 1542; /note="For beta-ketoacyl synthase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" BINDING 1728..1730; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 1728; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1729; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1730; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1754; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 1764; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 1773..1783; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 1797..1800; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 1827..1829; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 1828; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1829; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).; EC=2.3.1.86; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; MOD_RES 180; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"; MOD_RES 604; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1412; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4A8.11c; CHAIN 1..1842; /note="Fatty acid synthase subunit alpha"; /id="PRO_0000180286" MRPEVEQELAHTLLLELLAYQFASPVRWIETQDVILSPPVSAERIVEIGPSPTLAGMAKRTLKLKYENMDAALSINREVLCYSKDAREIYYNFEDEVADEPAEAPASTSSTPKVETAAAAAPAATPAPAPAQTSAPAAALPDEPPKALEVLHTLVAQKLKKSIEEVSPQKSIKDLVGGKSTLQNEILGDLQKEFGATPEKPEEVPLDELGAIMQSSFNGSLGKQSSSLISRMISSKMPGGFNNSAVRGYLGNRYGLGPGRLESVLLLALTMEPASRLGSEADAKAWLDSVAQKYAARNGVTLSSPTAEGGSSSGSAAVIDEETFKKLTKNNTMLVTQQLELFARYLNKDLRAGQKAQVAEKVISDTLRAQLDLWNEEHGEFYASGIAPIFSPLKARVYDSDWNWARQDALKMFFDIIFGRLKHVDTEIVARCISVMNRSNPTLLEFMQYHIDHCPAEKGETYQLAKTLGQQLIDNCKSVIDAPPVFKNVNHPTAPSTTIDERGNLNYEEIPRPGVRKLTHYVTEMAKGGKLPTESKNKAKVQNDLARIYRIIKSQNKMSRSSKLQIKQLYGQVLHALSLPLPSSNDEQTPVKETIPFLHIRKKSVDGNWEFNKSLTGTYLDVLESGAKNGITYQDKYALVTGAGAGSIGAQIVEGLLAGGAKVVVTTSRFSRKVTEFYQSLYTRHGSRGSCLIVVPFNQGSKTDVEALIDYIYDEKKGLGWNLDYIVPFAAIPENGREIDGIDSRSEFAHRIMLTNILRLLGAVKSQKASRGMDTRPAQVILPLSPNHGTFGNDGLYSESKLGLETLFNRWYSESWANYLTICGAVIGWTRGTGLMAPNNIVSQGIEKYGVRTFSQSEMAFNILGLMSQKVVDLCQSEPIYANLNGGLELLPDLKDLSTRLRTELLETAEIRRAVAAETAFDHSITNGPDSEAVFQKTAIQPRANLKFNFPKLKPYEALSHLSDLRGMVDLEKVPVVTGFSEVGPWGNSRTRWDMECYGEFSLEGCVEIAWIMGLIKNFNGKGKDGKPYSGWVDTKTGEPVDDKDVKAKYEKYILEHCGIRIIEAELFHGYNPEKKELLQEVVIDHDLEPFEASKEAAHEFKLRHGDQVEIFEIPDSTEWSVRFKRGTSMLIPKALRFDRFVAGQIPLGWDPKRYGIPDDIISQVDPTTLYVLVSTVEALVASGITDPYECYKYIHVSELGNTVGSGIGGMSALRGMYKDRWTDKPVQKDILQESFINTANAWINMLLLSASGPIKTPVGACATAVESVDAAVDLITSGKARICISGGYDDFSEEGSYEFANMGATSNAAKETERGRTPQEMSRPATSTRDGFMESQGAGVQIIMQAKLAIEMGVPIHGIVGYVSTAMDKQGRSVPAPGQGILTGAREIATKTPLPIVDLKFRSRQLQRRRSQIGEWAEREYLYLEEELDAMKVQNPDLDLEAYRIERINVIKEEVVRQEKEALNTFGNEFWKRDPTIAPIRGALAVWGLTIDDLGVASFHGTSTKANEKNECDVIDSQLTHLGRSKGNAVYGVFQKYLTGHSKGGAGAWMLNGALQILRSGFVPGNRNADNIDEYLARFDRVMFPSEGIQTDGIKAASVTAFGFGQVGGQVIVIHPDYIYGVIDEATYNAYKAKTAARYKASYRYTHDALVYNNLVRAKDSPPYTKEQEKAVYLNPLARASKSKAGTWTFPATLPAESDISKTNETTRTLQSLTTSLTNSNENVGVDVELVSAISIDNETFIERNFTDTERKYCFAAPNPQASFAGRWSAKEAVFKSLGISGKGAAAPLKDIEIISSESGAPEVVLHGEAAKAATTAGVKSVSVSISHDDNQSVSVALAHK Q10292 MEK1_SCHPO ACT_SITE 281; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 166..174; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 189; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC14C4.03; CHAIN 1..445; /note="Meiosis-specific serine/threonine-protein kinase mek1"; /id="PRO_0000086320" MDFLSHAMLSRSESTQILCELSQIDESTMDPQYTEDDVLARLFVFSSSSPQTVLNVKKYEDVSVGRSNTCNYQLLQFTASYKHFRVYSVLIDDDMDPLVYCEDQSSNGTFLNHRLIGKGNSVLLSDGDILDVRHCASFLFQQKYTTDNDFHHEYAGERFNITQRLLGIGGFSRIYMAMDNNTGGQYACKIIDKKKISTKRFFEDHEMTILRKLDHPNIIKVNMEYNSETQFFIFEEMVTGGDLFSYLTKLGTVPEVTTLFIMFQILQGLKYLHEQNIIHRDLKLENILIASSSDTIFRIILTDFGVARCMQKGKRLSTFVGTPEYTAPEIQRLKGRSQVEKENSSGYGKEVDLWSLGVIMFLLLSGNSPSFADGVKEKQVDFRDPVWKSVSRQAKDLISNLLKTNPPDRFTVKQCLSHPWFARHSSRLTKLYETRILKPLKHSRL Q10295 PAP_SCHPO BINDING 86..88; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 99..101; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 99; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 99; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 101; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 101; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 153; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 153; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 214; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 223; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 232..233; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:8692700}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333; Evidence={ECO:0000305|PubMed:8692700}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250}; SPBC646.04; STRAND 7..9; /evidence="ECO:0007829|PDB:7Q73"; STRAND 82..86; /evidence="ECO:0007829|PDB:7Q73"; STRAND 100..106; /evidence="ECO:0007829|PDB:7Q73"; STRAND 129..135; /evidence="ECO:0007829|PDB:7Q73"; STRAND 138..140; /evidence="ECO:0007829|PDB:7Q73"; STRAND 142..147; /evidence="ECO:0007829|PDB:7Q73"; STRAND 150..158; /evidence="ECO:0007829|PDB:7Q73"; STRAND 160..162; /evidence="ECO:0007829|PDB:7Q73"; STRAND 304..307; /evidence="ECO:0007829|PDB:7Q73"; STRAND 358..369; /evidence="ECO:0007829|PDB:7Q73"; STRAND 397..402; /evidence="ECO:0007829|PDB:7Q73"; STRAND 407..415; /evidence="ECO:0007829|PDB:7Q73"; STRAND 432..435; /evidence="ECO:0007829|PDB:7Q73"; STRAND 468..481; /evidence="ECO:0007829|PDB:7Q73"; STRAND 491..493; /evidence="ECO:0007829|PDB:7Q72"; STRAND 516..524; /evidence="ECO:0007829|PDB:7Q73" HELIX 19..34; /evidence="ECO:0007829|PDB:7Q73"; HELIX 41..68; /evidence="ECO:0007829|PDB:7Q73"; HELIX 73..78; /evidence="ECO:0007829|PDB:7Q73"; HELIX 87..91; /evidence="ECO:0007829|PDB:7Q73"; HELIX 112..117; /evidence="ECO:0007829|PDB:7Q73"; HELIX 119..124; /evidence="ECO:0007829|PDB:7Q73"; HELIX 173..176; /evidence="ECO:0007829|PDB:7Q73"; HELIX 181..199; /evidence="ECO:0007829|PDB:7Q73"; HELIX 203..219; /evidence="ECO:0007829|PDB:7Q73"; HELIX 225..227; /evidence="ECO:0007829|PDB:7Q73"; HELIX 232..245; /evidence="ECO:0007829|PDB:7Q73"; HELIX 251..263; /evidence="ECO:0007829|PDB:7Q73"; HELIX 292..295; /evidence="ECO:0007829|PDB:7Q73"; HELIX 317..338; /evidence="ECO:0007829|PDB:7Q73"; HELIX 344..348; /evidence="ECO:0007829|PDB:7Q73"; HELIX 353..356; /evidence="ECO:0007829|PDB:7Q73"; HELIX 370..382; /evidence="ECO:0007829|PDB:7Q73"; HELIX 384..393; /evidence="ECO:0007829|PDB:7Q73"; HELIX 416..423; /evidence="ECO:0007829|PDB:7Q73"; HELIX 437..446; /evidence="ECO:0007829|PDB:7Q73"; HELIX 495..505; /evidence="ECO:0007829|PDB:7Q73"; HELIX 525..527; /evidence="ECO:0007829|PDB:7Q73"; HELIX 530..532; /evidence="ECO:0007829|PDB:7Q73" TURN 288..290; /evidence="ECO:0007829|PDB:7Q73"; TURN 311..314; /evidence="ECO:0007829|PDB:7Q73"; TURN 513..515; /evidence="ECO:0007829|PDB:7Q73" CHAIN 1..566; /note="Poly(A) polymerase pla1"; /id="PRO_0000051620" MTTKQWGITPPISTAPATEQENALNTALINELKNQNLFESPAESEKRVKVLDELQQITTEFVKKVSLAKHMNEKMANEAGGKIFTYGSYRLGVYGPGSDIDTLVVVPKHVSRDNFFQDLEPMLREREEVTDLAAVPDAYVPIIKFKFLGISIDLIFARLSVPRVPRDLELSDNNLLKGVEERCVLSLNGTRVTDQILQLVPNRAVFKHALRAIKFWAQRRAIYANVVGFPGGVAWAMMVARICQLYPNAVSSVIVAKFFRILHQWNWPQPILLKPIEDGPLQVRIWNPKLYPSDKAHRMPIITPAYPSMCATHNITLSTQTIILREMVRAGEIADQIMVKALPWSALFQKHDFFHRYKHYLTITAAAKTAEAQLKWAGLVESKLRHLVTRLELVDAIALAHPFNKGFDKVYNCSSEEEAQQVASGVTLEVAYESTDHEKLANDTVNEEKADNTESKADGSENGEKQIFPVYTTTCYIGLELEKKKGHPIKRLDISWPTQEFYELCKKWDKYDDTLMNVFIKNTKNTALPDEVFEPGEERPKATKKRSTADTAHSTEQLKRQKVSTA Q10309 ATC7_SCHPO ACT_SITE 408; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0" BINDING 408; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 408; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 409; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 410; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 410; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 491; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 528; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 530; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P32660"; BINDING 533; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 551; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 580; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 581; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 662; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 663; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 664; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 744; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 750; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 770; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 773; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 774; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 774; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q8NB49" CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P40527}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P40527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:P40527}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P40527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P40527}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527}; SPAC6C3.06c; CHAIN 1..1033; /note="Phospholipid-transporting ATPase neo1"; /id="PRO_0000046319" MDSRLNRIQSKMKLWIKDKNLSNPSIPLKVLNKSFRSSRQSSVSNGHGLYSLDRDETESLMSSHEASNAGISLDSSFRVIQVGQPEPQYGNNAVTNTKYDLFTFLPKCLYEQFRYFYNMYFLLVSLSQLIPPLKIGYLSTYIAPLIFVLLITLTKEAVDDLKRRRRDSYANNEIYTVNDSPCAAQNIQAGDVVYIAKDQRIPADMILLETTVGNEAFIRTDQLDGETDWKLRIPCSNQHTEGIVHADAPIKSVHHFYGTFTLNNQKRPISVDHTLWANTVLASDGVYGVVVYTGKDTRQSMNSSKAKTKVGLLEKEINFYSKILCTFVLVLSIGLTFSHGIKTDWYISVFRYLILFSSIIPINLRVNLDLAKIVHSKNTESDPNLPGVVVRSSNIPEELGRIEYVLTDKTGTLTQNEMEMKKLHVGTMGFSAESMDVVQACIQNYSTPIPLSEDSKTLVRNLVLALSLCHNVTPSKGHDGVVSYQAASPDEVAIVKWTSTLGLVLTNRTRDAITLNNNVYKILNIFPFKSETKRMGIIVQSPDEKITFYLKGADSIMQNFVKPSFWLEEECGNLAREGLRTLVVAKKDLSAEEYSAFSLAHSDASLSFSNSRDKKMEEIVSRYLENDMDLLGLTGVEDKLQKDVKITLELLRNAGIHVWMLTGDKVETARCIAISSRLVSRGQYIHTINQLSSREEAHNHLLTLRNKPDSCLIIDGESMEFCIGYLQNEFIDIVSDLSSVVICRCTPTQKANMTRLIQEKKQASVCCIGDGGNDVGMIQVANVGIGIVGKEGQQASLAADYSVKEFSHVSRLLLWHGRISYKQTSKLAMFVIHRGLLISVCQVVYSVISAFEPIALFQGLLLVGYSTMYTMLPVFSIVYDRDVSEKLVFLFPELYKEMREQKCFSYKNFISCVLISVYQGLIIQLFTFYLIGFEEEGKMLAVCFSCLIFNELIMVALQINTWEQTIVMSELLTLMMYILSVPFLTNYFELKFLLGLKFYWVSALILFISLLPVWCGKALKRKLKPSSYAKLQR Q10322 DMA1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P38823}; SPAC17G8.10c; CHAIN 1..267; /note="Probable E3 ubiquitin-protein ligase dma1"; /id="PRO_0000055897" MTKSVEGYLKEQELAAETDSEKDDDKISIRLTNFVGPNAHSFSFDPLVRYWNRKQNNLPIYIGRYTERYNGGDVSAIVFRSKVVSRRHAQIFYENNTWYIQDMGSSSGTFLNHVRLSPPSKTSKPYPISNNDILQLGADYRGGHEVNYRCVRARVELNNSWKIKLSPYNLNEFKRMQELVLCGSSESGPPECCICLMPVLPCQALFVAPCSHSYHYKCIRPTLNESHPYFSCFICRKYHDLEAPVEEGDESLNDLLRNATVKDDASE Q10325 MST2_SCHPO ACT_SITE 274; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q9H7Z6" BINDING 241..243; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q9H7Z6"; BINDING 243; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250"; BINDING 248..254; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q9H7Z6"; BINDING 278; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q9H7Z6"; BINDING 287; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q9H7Z6" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q9H7Z6}; PTM: Autoacetylation at Lys-198 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}. MOD_RES 198; /note="N6-acetyllysine; by autocatalysis"; /evidence="ECO:0000250|UniProtKB:Q9H7Z6" SPAC17G8.13c; CHAIN 1..407; /note="Histone acetyltransferase mst2"; /id="PRO_0000051565" MPATILKSTASSKTLLIIKFDTNSSRYPFYKKHLLELNSESTFLGLLTKGQADTSITRLNQDDVRLFEKAKTVADRTKDVAYSFSDPILSTQLRTPPPQPTSIRYLYFGTYRIKPWYTSPYPEEYSCAKNLYICESCLKYMNSDHVLQRHKMKCSWSYPPGDEIYRDKNISIFEVDGQRQPIYCQNLCLLAKMFLHSKMLYYDVEPFLFYVLTEFDGQECKVIGYFSKEKRSASDYNVSCILTLPIYQRRGYGVFLIDFSYLLTQVEGKLGSPEKPLSDLGLVTYRSYWKMRVAKALLEITTPISINAIAKSTSMVCDDVISTLESLSVFKYDPLKKKYVLQLKRDELENVYKAWNIKHPQRVNPKLLRWTPYLGEEQISNLLLKENILIPLPQKRLLDNSHHLDSV Q10331 NU107_SCHPO SPBC428.01c; CHAIN 1..813; /note="Nucleoporin nup107"; /id="PRO_0000204834" MACCCYSTILTHTRLDFKTMHQNALNNATLNVLGHKKNGSSSIQELIEMDEEEAEMNQNVVCIGPNETAVSVELGDEYEKFNIITSLKKDNLFSKDGLLYAYYELCQEKFEKCLKEDDEEWIELWDLESRTWDLIQRLYSFRLSEQQGHIQSHAFSSRAVLEEEYYSQNPEAFENNIVFNWARDNSSDPPSIEIRGNRWFYTREDIKMKNRGGSRFSSNISGTIVSNLDPDADIRDDKRLDERDDNFERQFFHTAFCLFRSGSFEELLELCRRTGNHWRSASLQGILEYRDNLIDDVLQSETSGNKRKELLRRSCLALTKNKRIDSYERALYGALCGDLNSVLDVCTTWEDAMWAYYNSMTQYNLDVYLSSKAPQTETQLPPVDSGLGLTPELIFNSLSNSSIASIQEEASHPLIKLQTHIICNKISEILSSAHIQLEAIRTGNAPESGDLVTPPLLRILTHIILFLKISGLAVDEYTSDSIIQAYIELLASAKKVNLVPLYIQYLSNQVQYEAYSRFLILVDEESARSEQLQLAKKYSLDINHAALLAVEYVYDEVVSVSPEEVHTVYLKSIEEPVEPSYKKLICTLEWLLITSQTDELLRFANLVYRFFLSIGELNSAYDLYTHIPSDALNTLSSSDGEPENDSKFRDAYELMNYRALCRALKFYQEWEELSKQEVFEDSAVTKASTSYKVWKKKLNFASRKCVKSFTDLLQANWLHPSTLELKPDDDPLLYKTLMTIRNLYVPELILGLHNVYFSLEDYDSCFALANEVASEDLKLYHCLIKSGRLVEYVSYLGKAGECSLSTPNGLFSL Q10336 MCP6_SCHPO SPBC582.06c; CHAIN 1..327; /note="Meiotic coiled-coil protein 6"; /id="PRO_0000096292" MEYQEEASLASAEDSTFIASSPVQSVSEMKSIKQKSFQYFDDYEKNVSDKTIQFQKLQMTAKEIIDAFERDSTQRTLQIESLESKIGEQERDLNNEKLASETLREKTQLLEKENGALKVENGYLYEKSRKLEEEMAHLKKKCNVYKSKFEESSLRCKSLYSSNTKLKDSMETMKRRMETETKEMNKIKPKNDSESDRFKRNSQSLSQQSPLLDVHSPDNSNHRTMLNINNSSPIKPKKIFKPNEVKNRISRLQKTFADLENQHHSFQQICQTLRKRLENDSSTTKQRLSKLEEIIRNRAPPSYSFSLNCSHTYQPVSCVEPVNHDLS Q10341 SST_SCHPO ACT_SITE 221; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P45131"; ACT_SITE 443; /evidence="ECO:0000250|UniProtKB:P45131"; ACT_SITE 480; /evidence="ECO:0000250|UniProtKB:P45131" BINDING 290; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P45131"; BINDING 481; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P45131" CATALYTIC ACTIVITY: Reaction=L-serine + succinyl-CoA = CoA + O-succinyl-L-serine; Xref=Rhea:RHEA:52820, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:136856; Evidence={ECO:0000269|PubMed:28581482}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for L-serine {ECO:0000269|PubMed:28581482}; KM=0.025 mM for succinyl-CoA {ECO:0000269|PubMed:28581482}; KM=0.045 mM for acetyl-CoA {ECO:0000269|PubMed:28581482}; KM=738 mM for L-homoserine {ECO:0000269|PubMed:28581482}; Note=kcat is 7.4 sec(-1) with L-serine and succinyl-CoA as substrates. kcat is 0.2 sec(-1) with acetyl-CoA as substrate (in the presence of L-serine). kcat is 13.8 sec(-1) with L-homoserine as substrate (in the presence of succinyl-CoA). {ECO:0000269|PubMed:28581482}; TRANSIT 1..26; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC106.17c; CHAIN 27..504; /note="Serine O-succinyltransferase"; /evidence="ECO:0000255"; /id="PRO_0000155759" MLRASSKRLQLSWQVFRRFQSSNPQLSFPCVDQAQERSRQFEQSLQKQQACPNSVDPSASITSPSLSSGPEPVYGKIVSGFKKFYHNKPFLCDHGGILPKFEIAYETWGTLNKDHSNAILLHTGLSASSHAHSHPENTAPGWWEQFIGPGKDVDTNKFFVICTNVLGSCYGSTGPSSVDPGDGKHYATRFPIITVNDMIRAQLLLLDHLKIEKLYASVGSSLGGMQSLTLGALAPHRVGRIASISGGARSHPYSIALRFTQRQILMNDPYWNRGFYYDGVPPHTGMKLAREVATISYRSGPEWEQRFGNRRADPSVSPAFCPDFLIETYLDHAGEKFCLQYDPNSLLYISKAMDMHDMSASHQRSLSENRKKNQHKLDKYLSADVSAEEIIKLNEDTSVLPDVPYQEIANEDRAPEPDPETNLIAGLAPLKDTPVMVMGVESDNLMPVECQRETARCLEKAGNKQVVYHELDANESFYGHDTFLIYRKDLDLVGGKLKKFLELS Q10343 AAKG_SCHPO BINDING 35; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 141; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 141; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX"; BINDING 141; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:17289942, ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2OOY"; BINDING 142; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 162..165; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 191; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 191; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX"; BINDING 191; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOY"; BINDING 196; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 196; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX"; BINDING 196; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOY"; BINDING 217..218; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 217..218; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX"; BINDING 217..218; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOY"; BINDING 287..289; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 290; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:17289942, ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2OOY"; BINDING 303..308; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOY"; BINDING 305..308; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1"; BINDING 305..308; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX" SPAC1556.08c; STRAND 30..38; /evidence="ECO:0007829|PDB:2QRD"; STRAND 58..62; /evidence="ECO:0007829|PDB:2QRD"; STRAND 67..72; /evidence="ECO:0007829|PDB:2QRD"; STRAND 141..148; /evidence="ECO:0007829|PDB:2QRD"; STRAND 155..162; /evidence="ECO:0007829|PDB:2QRD"; STRAND 217..222; /evidence="ECO:0007829|PDB:2QRD"; STRAND 227..233; /evidence="ECO:0007829|PDB:2QRD"; STRAND 269..271; /evidence="ECO:0007829|PDB:2OOX"; STRAND 290..294; /evidence="ECO:0007829|PDB:2QRD"; STRAND 299..305; /evidence="ECO:0007829|PDB:2QRD"; STRAND 317..320; /evidence="ECO:0007829|PDB:2OOX"; STRAND 329..331; /evidence="ECO:0007829|PDB:2OOX" HELIX 4..21; /evidence="ECO:0007829|PDB:2QRD"; HELIX 24..27; /evidence="ECO:0007829|PDB:2QRD"; HELIX 43..53; /evidence="ECO:0007829|PDB:2QRD"; HELIX 74..87; /evidence="ECO:0007829|PDB:2QRD"; HELIX 91..98; /evidence="ECO:0007829|PDB:2QRD"; HELIX 102..111; /evidence="ECO:0007829|PDB:2QRD"; HELIX 128..137; /evidence="ECO:0007829|PDB:2QRD"; HELIX 163..173; /evidence="ECO:0007829|PDB:2QRD"; HELIX 175..179; /evidence="ECO:0007829|PDB:2QRD"; HELIX 184..186; /evidence="ECO:0007829|PDB:2QRD"; HELIX 204..214; /evidence="ECO:0007829|PDB:2QRD"; HELIX 235..241; /evidence="ECO:0007829|PDB:2QRD"; HELIX 242..244; /evidence="ECO:0007829|PDB:2OOX"; HELIX 246..250; /evidence="ECO:0007829|PDB:2QRD"; HELIX 253..257; /evidence="ECO:0007829|PDB:2QRD"; HELIX 276..285; /evidence="ECO:0007829|PDB:2QRD"; HELIX 306..314; /evidence="ECO:0007829|PDB:2QRD" TURN 63..66; /evidence="ECO:0007829|PDB:2QRD"; TURN 150..152; /evidence="ECO:0007829|PDB:2QRD" CHAIN 1..334; /note="5'-AMP-activated protein kinase subunit gamma"; /id="PRO_0000204390" MTDVQETQKGALKEIQAFIRSRTSYDVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSFPEAIAEIDKFRLLGLREVERKIGAIPPETIYVHPMHSLMDACLAMSKSRARRIPLIDVDGETGSEMIVSVLTQYRILKFISMNCKETAMLRVPLNQMTIGTWSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRPANFDGVHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYIIYDKTTTPGVPEQTDNFESAV Q10356 DJ1_SCHPO ACT_SITE 16; /evidence="ECO:0000305|PubMed:24758716"; ACT_SITE 111; /evidence="ECO:0000305|PubMed:24758716"; ACT_SITE 130; /evidence="ECO:0000305|PubMed:24758716" CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000269|PubMed:24302734, ECO:0000269|PubMed:24758716}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.8 mM for methylglyoxal {ECO:0000269|PubMed:24758716}; Note=kcat is 85.7 min(-1) with methylglyoxal as substrate. {ECO:0000269|PubMed:24758716}; SPAC22E12.03c; STRAND 4..9; /evidence="ECO:0007829|PDB:4QYT"; STRAND 31..38; /evidence="ECO:0007829|PDB:4QYT"; STRAND 43..45; /evidence="ECO:0007829|PDB:4QYT"; STRAND 51..53; /evidence="ECO:0007829|PDB:4QYT"; STRAND 55..57; /evidence="ECO:0007829|PDB:4QYT"; STRAND 72..76; /evidence="ECO:0007829|PDB:4QYT"; STRAND 106..110; /evidence="ECO:0007829|PDB:4QYT"; STRAND 125..127; /evidence="ECO:0007829|PDB:4QYT"; STRAND 147..152; /evidence="ECO:0007829|PDB:4QYT"; STRAND 155..158; /evidence="ECO:0007829|PDB:4QYT" HELIX 14..26; /evidence="ECO:0007829|PDB:4QYT"; HELIX 58..60; /evidence="ECO:0007829|PDB:4QYT"; HELIX 64..70; /evidence="ECO:0007829|PDB:4QYT"; HELIX 80..87; /evidence="ECO:0007829|PDB:4QYT"; HELIX 90..99; /evidence="ECO:0007829|PDB:4QYT"; HELIX 111..114; /evidence="ECO:0007829|PDB:4QYT"; HELIX 115..119; /evidence="ECO:0007829|PDB:4QYT"; HELIX 131..133; /evidence="ECO:0007829|PDB:4QYT"; HELIX 134..139; /evidence="ECO:0007829|PDB:4QYT"; HELIX 161..163; /evidence="ECO:0007829|PDB:4QYT"; HELIX 164..175; /evidence="ECO:0007829|PDB:4QYT"; HELIX 178..187; /evidence="ECO:0007829|PDB:4QYT" CHAIN 1..191; /note="Glutathione-independent glyoxalase DJ-1"; /id="PRO_0000157857" MVKVCLFVADGTDEIEFSAPWGIFKRAEIPIDSVYVGENKDRLVKMSRDVEMYANRSYKEIPSADDFAKQYDIAIIPGGGLGAKTLSTTPFVQQVVKEFYKKPNKWIGMICAGTLTAKTSGLPNKQITGHPSVRGQLEEGGYKYLDQPVVLEENLITSQGPGTAMLFGLKLLEQVASKDKYNAVYKSLSMP Q10361 ETP1_SCHPO BINDING 181; /ligand="heme o"; /ligand_id="ChEBI:CHEBI:24480"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P12946"; BINDING 256; /ligand="heme o"; /ligand_id="ChEBI:CHEBI:24480"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P12946"; BINDING 383; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P12946"; BINDING 446; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P12946"; BINDING 541; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000269|PubMed:21536008, ECO:0007744|PDB:2WLB"; BINDING 547; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000269|PubMed:21536008, ECO:0007744|PDB:2WLB"; BINDING 550; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000269|PubMed:21536008, ECO:0007744|PDB:2WLB"; BINDING 587; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000269|PubMed:21536008, ECO:0007744|PDB:2WLB" CATALYTIC ACTIVITY: [Heme A synthase etp1(cd)]: Reaction=2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a; Xref=Rhea:RHEA:63388, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:60530, ChEBI:CHEBI:61715; EC=1.17.99.9; Evidence={ECO:0000250|UniProtKB:P40086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389; Evidence={ECO:0000250|UniProtKB:P40086}; COFACTOR: [Heme A synthase etp1(cd)]: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P40086}; COFACTOR: [Mitochondrial ferredoxin etp1(fd)]: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:15219990, ECO:0000269|PubMed:21497579, ECO:0000269|PubMed:21536008}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:21536008}; TRANSIT 1..45; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: The etp1 preprotein is cleaved into 2 chains after imort into mitochondria. The N-terminal chain containing a heme A synthase cox15-like domain etp1(cd) is a subunit of the membrane-embedded cytochrome c oxidase complex and functions in the respiratory chain. The C-terminal chain containing a ferredoxin yah1-like domain etp1(fd) is released and serves in the matrix as electron transfer protein. {ECO:0000269|PubMed:11841224}. SPAC22E12.10c; STRAND 519..524; /evidence="ECO:0007829|PDB:2WLB"; STRAND 530..535; /evidence="ECO:0007829|PDB:2WLB"; STRAND 551..554; /evidence="ECO:0007829|PDB:2WLB"; STRAND 583..585; /evidence="ECO:0007829|PDB:2WLB"; STRAND 598..601; /evidence="ECO:0007829|PDB:2WLB" HELIX 556..561; /evidence="ECO:0007829|PDB:2WLB"; HELIX 567..573; /evidence="ECO:0007829|PDB:2WLB"; HELIX 593..595; /evidence="ECO:0007829|PDB:2WLB" TURN 540..543; /evidence="ECO:0007829|PDB:2WLB"; TURN 586..588; /evidence="ECO:0007829|PDB:2WLB" CHAIN 46..616; /note="Heme A synthase-mitochondrial ferredoxin fusion protein"; /evidence="ECO:0000255"; /id="PRO_0000006079"; CHAIN 46..?; /note="Heme A synthase etp1(cd)"; /id="PRO_0000460045"; CHAIN ?..616; /note="Mitochondrial ferredoxin etp1(fd)"; /id="PRO_0000460046" MNISRSSGLMRQFLLQPLRKGCDISCLGRSSWRMSRSFSGSSVLNEINLSRTKNLFLNDCKFNKNSFEKFFARRLSNSVAPTPGGILQETEKIPSKKVAFWLLGSSALVLAIVVVGGITRLTESGLSITEWKPITGVIPPLTDEQWNQEFELYKKSPEFEKLNSHMTVDEFKNIFFWEWFHRVLGRGIGLTILLPSIYMIVTKRASPWLSKRLIGLTGLVGLQGVIGWWMVKSGLSEELFSDGSHPRVSHYRLATHLAAAVALYIGLVWTGHGILQRHAFLKSMKSGSTSQLTSMVSSVQKMKGFRTSVNSFVGLVLITLLSGAFVAGLDAGMIYCTFPEMGEGRLAPSKSELFDQRFCRKDDKSDLIWRNMIDNPSLVQLEHRILAITTFVAACGLFIFSRAKRNILPKKIKTSINVVTGVVTAQATLGIMTLIYVVPVPLAALHQAGSLVTLTAALSLAQRLHPEYALKNIRSWTKLISSPPKSSISSSILTQQRQFHTFRPSFHSEIKKPLPGTGIKVFFVTPEGREIMIEGNEEGACEGSVACSTCHVIVDPEHYELLDPPEEDEEDMLDLAFGLEETSRLGCQVLLRKDLDGIRVRIPAQTRNIRLERPKA Q10364 SCK2_SCHPO ACT_SITE 392; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 272..280; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 295; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC22E12.14c; CHAIN 1..646; /note="Serine/threonine-protein kinase sck2"; /id="PRO_0000086640" MMNKWAKNWFGLSKKSVSTNSAKGSLPRSPLASIQTNQPVEEGEGGSLPSVSNLGPSSIDHPMEEFASDQSTVGNRNSNDILPEVDHEPSGYLKLQIGSLVLGGPHTDAALAMECSRLNQLFVVVQFGTTEFVSPPLKWESPGRDIGTSSRDSANVSRSSSMMSSHPIPTPAIQRTSSIPNPLTPSYVVFDVAKPVPIDVNIYDHGNNNEFVGRTYIHPSYNYGQFEQFCNSVEVSPAYNRMVDLRLSLNTVFQPLSQHSYGPDDFVPLKLIGKGTFGQVYLVRKKDTERVYAMKVLSKKVIVRRKEVAHTVGERDILVQTSAADSPFIVALRFSFQTPKDLYLVTDYMAGGELFWHLQKSVRFPEERAKFYIAELLLALQALHKRGIVYRDLKPENILLDVQGHIALCDFGLSKANLSVGTTTRTFCGTTDYLAPEVILDEAGYDMMVDFWSLGVLLYEMTCGWSPFYADNTQQLYKNIVFGKVRFPRGLLSVEARDLIKLLLNRNPKHRLGAHGDVEEVMKHPFFDGIDWKKLAAKEISPPFKPIVEGEIDVSNFDVEFTNKAIDRDFSSTDEMSTSAPLSSTVQNGFKGFTYIDASAMDEAFGYHNSNDSASSISSQDDYSKDNSDMDLNRANDEVFMGQIDP Q10407 MKH1_SCHPO ACT_SITE 955; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 831..839; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 854; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; SPAC1F3.02c; CHAIN 1..1116; /note="MAP kinase kinase kinase mkh1"; /id="PRO_0000086331" MAADIGSQSSGSLEERFEQSLHLQNVDKQDWSLNSVLQFLKLYKFNKEWEDVFIKSRIEMDLFINLADQSKAEEFAFKNKLSKESAIQLSSCIRKTLLAPSSTRVPSKNSSYETLTYSAKDSSDDVFTETNSGFRSSNQNSSLKSFQSVPDSNVNVFGGFGGSVVDNNELLSTGKNSHQTTSLNLEGSPINLHAYKGTVTSIINDDSRNINKKTLSKQPVSEHKEKQTSFLRRFRVPGFSRDKDKTKDCPSSNSNPFHLASSNVKTLDASLDQGEWVPRIHRLESQIGLISKKKSFVLATMDDMKFTVVDITNVQNATQLRKLIAKSMYLDISIDQFDLFLTEVGGAQYIEILDDRKLDIARLYSDEFGTIKFFVKPSQNEESGMDSDTYLSFGTKSSSTYKADDDSIYHRKEDFKKQPSYPVLTSDFEITDAGPNLSLSGHQPDNKYYKGFSSAPNLAVVPELPSRRFRGFEKIRGAKGEMATKILDATEAQSEKNKFTVCRPHKKVTLKMPLNSGSSAPQSPSSNTSASVLTRNFVAHRDPPPPPTETSSLRRKNTLTRRPSIRHARSSPYIDTGHNEASKFSHTSFDPKASSKSSNSLKESVEALSEIPFEDAPALDESDLSGDPFWAIQPKQSSSQVPKENHHNIQSKLSINTEAATDLKANELSSPKTPEYCRGDDRSISLSPLSYRLRKSKHIRESPPSSKVINSGNWEVRPSADDLYEDVDRFFPRYDLDKVLVVDQSRMVSSPSKVSIRPKMKSVRLLAREASEARKEIRHNARRNKSGNLLRRSSTKLWGSRIVELKPDTTITSGSVVSQNATFKWMKGELIGNGTYGKVFLAMNINTGELIAVKQVEIPQTINGRHDQLRKDIVDSINAEISMIADLDHLNIVQYLGFEKTETDISIFLEYVSGGSIGRCLRNYGPFEEQLVRFVSRQVLYGLSYLHSKGIIHRDLKADNLLIDFDGVCKISDFGISKHSDNVYDNDANLSMQGSIFWMAPEVIHNDHQGYSAKVDVWSLGCVVLEMLAGRRPWSTDEAIQAMFKLGTEKKAPPIPSELVSQVSPEAIQFLNACFTVNADVRPTAEELLNHPFMKCDEEFNFKDTNLYDMLCKRKS Q10423 CCE1_SCHPO BINDING 46; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; BINDING 230; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420" CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).; EC=3.1.21.10; Evidence={ECO:0000269|PubMed:9343409}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC25G10.02; STRAND 40..47; /evidence="ECO:0007829|PDB:1KCF"; STRAND 52..59; /evidence="ECO:0007829|PDB:1KCF"; STRAND 65..73; /evidence="ECO:0007829|PDB:1KCF"; STRAND 112..118; /evidence="ECO:0007829|PDB:1KCF"; STRAND 162..165; /evidence="ECO:0007829|PDB:1KCF"; STRAND 203..208; /evidence="ECO:0007829|PDB:1KCF" HELIX 6..15; /evidence="ECO:0007829|PDB:1KCF"; HELIX 26..33; /evidence="ECO:0007829|PDB:1KCF"; HELIX 91..109; /evidence="ECO:0007829|PDB:1KCF"; HELIX 128..151; /evidence="ECO:0007829|PDB:1KCF"; HELIX 168..179; /evidence="ECO:0007829|PDB:1KCF"; HELIX 191..200; /evidence="ECO:0007829|PDB:1KCF"; HELIX 209..217; /evidence="ECO:0007829|PDB:1KCF"; HELIX 224..253; /evidence="ECO:0007829|PDB:1KCF" TURN 123..125; /evidence="ECO:0007829|PDB:1KCF"; TURN 221..223; /evidence="ECO:0007829|PDB:1KCF" CHAIN ?..258; /note="Cruciform cutting endonuclease 1, mitochondrial"; /id="PRO_0000020865" MATVKLSFLQHICKLTGLSRSGRKDELLRRIVDSPIYPTSRVLGIDLGIKNFSYCFASQNEDSKVIIHNWSVENLTEKNGLDIQWTEDFQPSSMADLSIQLFNTLHEKFNPHVILMERQRYRSGIATIPEWTLRVNMLESMLYALHYAEKRNSIEQKIQYPFLLSLSPKSTYSYWASVLNTKASFSKKKSRVQMVKELIDGQKILFENEEALYKWNNGSRVEFKKDDMADSALIASGWMRWQAQLKHYRNFCKQFLKQ Q10425 EIF3B_SCHPO MOD_RES 23; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:18257517"; MOD_RES 135; /note="Phosphoserine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:18257517"; MOD_RES 136; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC25G10.08; CHAIN 1..725; /note="Eukaryotic translation initiation factor 3 subunit B"; /id="PRO_0000123534" MSEILIEEIKDQIVVKDEEIDVSELEVKLNVTKPVGYDTVVVIEGAPVVEEAKQQDFFRFLSSKVLAKIGKVKENGFYMPFEEKNGKKMSLGLVFADFENVDGADLCVQELDGKQILKNHTFVVRKLNQLEKAFSTPDEFSFEEREFKEREHLRSWLTDYYGRDQFISYYGNRVSVNWNRKSDVPEQIVDRENWTETYVQWSPMGTYLVSLHLRGIQLWGGESWGMCARFLHPYVKFVDFSPNEKYLVSWSYEPVRLPPIGHPARETMPFTDDDEGKHCFVWDIASGRILRSFKIPPQPEGSKDGKKVIWPIFKWSADDKYLARVTVGQSISVYETPSLALVDKKTIKIDGVQNFEWCPVSDALGRDSKEQLLAYWTPEITNQPARVALISIPSKSTIRTKNLFNVSDCKLYWQSNGDYLCVKVDRHTKTKKSTFSNLEIFRIREKNIPVEVVDLKDVVLNFAWEPKSDRFAIISANDQVLNSTNVKTNLSFYGFEQKKNTPSTFRHIITFDKKTCNSLFMAPKGRFMVAATLGSSTQYDLEFYDLDFDTEKKEPDALANVQQIGSAEHFGMTELEWDPSGRYVTTSSTIWRHKLENGYRLCDFRGTLLREEMIGEFKQFIWRPRPPSPLTKEDMKKIRKKLKDYNRLFDEEDIAEQSSANRELAARRRQLISEWQKYRDEVIARVAEERAITGQPAITVPAEEEEIIQETVEEVISEEIEPVED Q10426 RIK1_SCHPO SPCC11E10.08; CHAIN 1..1040; /note="Chromatin modification-related protein rik1"; /id="PRO_0000097338" MALCVHSFWATAVDTATSCHFISSENCLVLLQALKINIYLCSEVHGLQFFTSIPLFSTVKHIRPYRPPGLDRDYLFVVLNDDTYFSIYWDEDYQKVIVDHPPVRYRVTFPWNRNAKSYCLVDLRMRAIFLSIDEISMICIRILSAEERLKTGRSIDSGFPFSFPVHLIYDMCILNDSSTPTLVVLHSDGLDCYVTAFLLDLSSKSLGKGIRLFERVKPSMIMPFGKRGLLVFESLFIHCMYRGNFVTINGPCTTYMHWTPLKGQKMHYIVCDTNGYLFGVYSSILGKNKWSLVMERLPIPPFDFITSLNSIHEGLLFIGSKNSESKLINLSTLKDVDSIPNLGPIHDLLVLKNDIEKSFLVCAGTPRNASLIYFQHALKLDILGQTKISGILRAMVLPSYPEHKLFLGFPSETVAFNIKEDFQLELDPSLSTKERTIALSGTNGEFVQVTSTFLCIYDSAKRSRLVYIEKITNAACYQEYSAIVINGTALAIFKKDTEVARKVFESEISCLDFSAQFQIGVGFWSKQVMILTFSDNSSISCAFQTNVPSLPRNIILEGVGVDRNLLLVSSGSGEFKSYVLFKNNLVFSETKHFGTTPVSFRRFTMNIGTYIICNNDCPHMVYGFNGALCYMPLSMPQSYDVCQFRDNSGKDFLISVSLGGLKFLQLNPLPELTPRKVLLEHVPLQAIIFQNKLLLRTLENRYEDYESYKENYHLELVDSYDDNSFRVFSFTENERCEKVLKINESSLLVGTSIIEQDKLVPVNGRLILLEFEKELQSLKVVSSMVLSAAVIDLGVYNDRYIVAFGQQVAIVKLTEERLMIDSRISLGSIVLQLIVEGNEIAIADSIGRFTIMYFDGQKFIVVARYLFGENIVKAALYEGTVYIIATNSGLLKLLRYNKDAKNFNDRFICESVYHLHDKVSKFQNFPITNTNSFLEPKMLFATEIGAIGSIVSLKDKELELEELTRKIRKLKFSYLSSMDYESIEADLISPVPFIDGDLVIDVKRWASSELFRLCRSVEHRESLNSYQKVQALLEEIQSLC Q10428 2AD1_SCHPO MOD_RES 96; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 99; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 109; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 542; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC188.02; CHAIN 1..548; /note="Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform"; /id="PRO_0000071469" MKGIKSKMLSRGKSQDTQKSSKKKESKKSNSHDSSKAPKESPSTDPNGSVIGAQNDFLTVPKHSGKKVPIDTTPTPRDEILLENVRTVRKQRSSLYHISENRNLVRLPSFTDVPVNKWHSLALEKLEQCCVVFDFNDPSTDLYGKEVKREALQDLIDLISVRKEAIDESLYPSIVHMFAVNVFRPLPPPSNPPGEIMDLEEDEPALEVAWPHLHLVYDFFLRFFESPSLNTSVAKVYINQKFIRKLLVLFDSEDPRERDFLKTTLHRIYGKFLSLRAFIRRSINNLFLQFVYENEQFNGIAELLEILGSIINGFALPLKEEHKIFLSRVLIPLHKAKSLPLYYPQIAYGIVQFVEKDSSVTEEVVLGLLRYWPKVNSSKEVLFLNEIEDIIEVMEPSEFLKIQVPLFHKLATSISSQNFQVAERALYFFNNDYFVHLVEENVDIILPIIYPALFEISKSHWNRVIHSMVCNVLKLFMDINPSLFDEVDAEYSESRRKKEDEEIIREERWTILENIAKENAMKLKSQNPTTVHSTTERLKKLSLDYTNG Q10429 CND3_SCHPO SPCC188.03; STRAND 153..155; /evidence="ECO:0007829|PDB:5OQR"; STRAND 413..415; /evidence="ECO:0007829|PDB:5OQR"; STRAND 776..778; /evidence="ECO:0007829|PDB:5OQR" HELIX 3..9; /evidence="ECO:0007829|PDB:5OQR"; HELIX 17..24; /evidence="ECO:0007829|PDB:5OQR"; HELIX 33..42; /evidence="ECO:0007829|PDB:5OQR"; HELIX 52..69; /evidence="ECO:0007829|PDB:5OQR"; HELIX 78..86; /evidence="ECO:0007829|PDB:5OQR"; HELIX 87..89; /evidence="ECO:0007829|PDB:5OQR"; HELIX 94..108; /evidence="ECO:0007829|PDB:5OQR"; HELIX 116..129; /evidence="ECO:0007829|PDB:5OQR"; HELIX 135..145; /evidence="ECO:0007829|PDB:5OQR"; HELIX 146..148; /evidence="ECO:0007829|PDB:5OQR"; HELIX 158..169; /evidence="ECO:0007829|PDB:5OQR"; HELIX 173..182; /evidence="ECO:0007829|PDB:5OQR"; HELIX 190..195; /evidence="ECO:0007829|PDB:5OQR"; HELIX 196..198; /evidence="ECO:0007829|PDB:5OQR"; HELIX 202..210; /evidence="ECO:0007829|PDB:5OQR"; HELIX 219..221; /evidence="ECO:0007829|PDB:5OQR"; HELIX 224..235; /evidence="ECO:0007829|PDB:5OQR"; HELIX 240..252; /evidence="ECO:0007829|PDB:5OQR"; HELIX 254..257; /evidence="ECO:0007829|PDB:5OQR"; HELIX 262..266; /evidence="ECO:0007829|PDB:5OQR"; HELIX 275..288; /evidence="ECO:0007829|PDB:5OQR"; HELIX 290..293; /evidence="ECO:0007829|PDB:5OQR"; HELIX 300..304; /evidence="ECO:0007829|PDB:5OQR"; HELIX 308..324; /evidence="ECO:0007829|PDB:5OQR"; HELIX 327..330; /evidence="ECO:0007829|PDB:5OQR"; HELIX 336..348; /evidence="ECO:0007829|PDB:5OQR"; HELIX 353..355; /evidence="ECO:0007829|PDB:5OQR"; HELIX 356..372; /evidence="ECO:0007829|PDB:5OQR"; HELIX 378..394; /evidence="ECO:0007829|PDB:5OQR"; HELIX 399..412; /evidence="ECO:0007829|PDB:5OQR"; HELIX 416..434; /evidence="ECO:0007829|PDB:5OQR"; HELIX 492..506; /evidence="ECO:0007829|PDB:5OQR"; HELIX 515..524; /evidence="ECO:0007829|PDB:5OQR"; HELIX 526..530; /evidence="ECO:0007829|PDB:5OQR"; HELIX 535..549; /evidence="ECO:0007829|PDB:5OQR"; HELIX 553..569; /evidence="ECO:0007829|PDB:5OQR"; HELIX 572..589; /evidence="ECO:0007829|PDB:5OQR"; HELIX 592..597; /evidence="ECO:0007829|PDB:5OQR"; HELIX 598..609; /evidence="ECO:0007829|PDB:5OQR"; HELIX 615..632; /evidence="ECO:0007829|PDB:5OQR"; HELIX 636..648; /evidence="ECO:0007829|PDB:5OQR"; HELIX 650..652; /evidence="ECO:0007829|PDB:5OQR"; HELIX 656..670; /evidence="ECO:0007829|PDB:5OQR"; HELIX 674..696; /evidence="ECO:0007829|PDB:5OQR"; HELIX 704..717; /evidence="ECO:0007829|PDB:5OQR"; HELIX 720..722; /evidence="ECO:0007829|PDB:5OQR"; HELIX 741..752; /evidence="ECO:0007829|PDB:5OQR"; HELIX 760..771; /evidence="ECO:0007829|PDB:5OQR"; HELIX 780..794; /evidence="ECO:0007829|PDB:5OQR"; HELIX 802..820; /evidence="ECO:0007829|PDB:5OQR" TURN 43..46; /evidence="ECO:0007829|PDB:5OQR"; TURN 187..189; /evidence="ECO:0007829|PDB:5OQR"; TURN 211..215; /evidence="ECO:0007829|PDB:5OQR"; TURN 258..260; /evidence="ECO:0007829|PDB:5OQR"; TURN 267..273; /evidence="ECO:0007829|PDB:5OQR"; TURN 349..351; /evidence="ECO:0007829|PDB:5OQR"; TURN 753..755; /evidence="ECO:0007829|PDB:5OQR" CHAIN 1..875; /note="Condensin complex subunit 3"; /id="PRO_0000095045" MSCIQIISSSQTSIAGHRKLCNKLFTLRTQEGFETDILRALNIILTVKKGNSNADRVLRFLVTFVNYLQQKDPEIDIVQPILKHILRGLDAKDKTVRYRCCQIIARVVNCVKEIDDDLYNTLKEKLLSRVLDRESIVRLEAVVALSRLQEDTGDEENDVRNILLFLLQNDPSSEVRRSVLLNIEVSNSTLPFILERARDVDAANRKCVYARVLPKIGDFRYLSIKKRVRILKWGLNDRDESVEKAAADMLAYQWIENADNNLLELLERLDVSNNSDVAVLAIKKFFDVRVDSLSQLEFPEQFWLELTAESSLLARTFNEICIEKNYTDLLDKMPEVVQLTYYIERQYVSLRDKSSYDESCFIIEQLLYIGLSQDMVDEIGRRKLLKSLTNSLSTMALPDSLISLHIELLRKLCSSENDFCSLLVEIITEVFEQGHSQNQTEEQGNSNAPELNKNDYEGEEITVSQKSPSPSLPPNELNEPEPDDMDGYKEAFNELRCLSYVQCLFENITSSLNENLYMVDMLKTLIIPAVRSHDLPIREKGLECLSLVCLLNADLAFENVPLYLHCYEKGSVVLKCTAIRTLTDMLIQHGKAKFTEYEDAISSILFEALGEFENAELQTLGAEAIAKLLVILHYRDELFLKPLIIQYFEPNTVDNHALRQVLGYFFPVYAFGAHENQWRIATIFCDALLSLLEIYRDLDEDDVQLSIGHIAQQMLDWTDNEKLYERKTQTGDDYIALNHNVHLHLANMIFESLPNASEGKERKFMISLLGKLKIPTDLPSSDYQRTKRKLETYESHGFTMDSTSLSILAKFERMLLQNEEARSKFEETEEERLMENAEENEHAGAEAISGEIIPDTVEANMEDEEEVYVKQEEDL Q10430 SPC25_SCHPO SPCC188.04c; CHAIN 1..238; /note="Kinetochore protein spc25"; /id="PRO_0000116881" MSLANFPTIELDYDSLKSKISNFNSIFDRFLQEERKKLLNNKNEYLRQLSEINEAQKKAEKSLEQTEARKQNFTELLEKEHEEQAITEQEIFSFQEKLDAMLKRKQKLSEELDHYRAIISSKRELRAQEMEAKRKQDSYNNPELKFWEDYLGLKMEGVHDEVIRFIFTNIDEKDWNKQFSFQINLAERDYKVVHCHPPLPHVDDLVNKVNRTRDFYQFLKDMRKGFRELHRKDLSQLI Q10432 CCQ1_SCHPO SPCC188.07; STRAND 133..138; /evidence="ECO:0007829|PDB:7CUJ"; STRAND 243..249; /evidence="ECO:0007829|PDB:7CUJ"; STRAND 268..270; /evidence="ECO:0007829|PDB:7CUJ"; STRAND 283..288; /evidence="ECO:0007829|PDB:7CUJ"; STRAND 305..312; /evidence="ECO:0007829|PDB:7CUJ"; STRAND 330..335; /evidence="ECO:0007829|PDB:7CUJ" HELIX 142..154; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 156..163; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 169..187; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 189..192; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 219..221; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 224..234; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 251..263; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 289..291; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 292..295; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 296..299; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 313..322; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 339..345; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 354..365; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 397..416; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 421..423; /evidence="ECO:0007829|PDB:7CUJ"; HELIX 433..435; /evidence="ECO:0007829|PDB:7CUJ" TURN 235..239; /evidence="ECO:0007829|PDB:7CUJ"; TURN 346..349; /evidence="ECO:0007829|PDB:7CUJ" CHAIN 1..735; /note="Coiled-coil quantitatively-enriched protein 1"; /id="PRO_0000116882" MSEINDFTNSIIINESDTKYEVYSEVNSSNRWIAKEDCPSPLEDVWLLKLAGHKRKLEEPLSCMRNEEPASKQREIEKFLRTDLDHSENDFLTQEVDEFPSTQQLFPIPLQNDTAFDSSEESITKSSKSSFSVLDIGLPMSALQRKMMHRLVQYFAFCIDHFCTGPSDSRIQEKIRLFIQSAHNIAKHPSLYDTEVRNPSAAESTNSHVSLDASNFSSYAENSSKFLFLQELFKNLSPSYSKTFFLFISNQFLANTLTQWLKSQNIDAELWAEEDAKTSQHPAIWICVSKKAPSASHFLQSCPDLSATIFYDIEAYMSVTSSLPSIQSLVLRLIHLGSIEHAIKCFQSSYNASFLVNIVGVVATLSSSSEENSEASNLSTLFEKSGNFEEILGSESHSSITEKTRDIAKNVATWLKNGENFSSWPLPPLMDLASLSVAEPRDSQPSVSQVNDTFVKSSDSTFPSSQSMQSPSKLHSLTSNATDLLSSSSLKKNFFSQQEADEVELSNNYDLQGAAVQYLQRRLRMVEDELHEAINSKNVQQSRSEELEQQISKLTDNLQEYRNTVRELKLDLEKSKKKNEDLSKLEVEKVEEIANLKKELTHLAKQQEFGFKYVQEFSNEDLQGKLIEANEKNYKLTQLLKTQKEDADFITNQYQNASTFAAEQSKEVAKLQAECKRLQAINSKVMEEVKVYNDSRVEALLAKVSSLEETLKILEQKSLPKFTPHNQSPRIIDSN Q10434 CAPZA_SCHPO MOD_RES 31; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12B10.07; CHAIN 1..256; /note="F-actin-capping protein subunit alpha"; /id="PRO_0000208645" MEKEAIYKLIRESPPGEVNQVVHDIRDIGLSDEEAIHEQLKLYHEDYNSSVSISDDEKVIISADNRLEGNRYYDQVLQKSFTINYETMEAENVEDYTEAIKIPDEIVKQIKKVASDHYLSDVTFGIIKKSDEVESFTIVLVSSKYNPKNYWNGSWRCICNYNVSEKKLEGRSHIRVHYYEDGNVWLDASRPISATVEETSKLYEVLAQVENGIQQSFNVELSSLNDKKFKELRRQLPVTRQKINWENVSGIRMRNT Q10452 GSK3_SCHPO ACT_SITE 157; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 38..46; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 61; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated on tyrosine residues. {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:8524294}. MOD_RES 191; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 192; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:8524294"; MOD_RES 335; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:8524294" SPAC1687.15; CHAIN 1..387; /note="Protein kinase gsk3"; /id="PRO_0000085985" MNHGTKIPVDPFRIIKETARDGSTGEVKQLSYTSSKVVGSGSFGVVMQVHLIESDSKAAIKRVLQDKRFKNRELQIMRIMKHPNIVDLIAYYYTTGDNSDEVYLNLVLEFMPETIYRASRLYTRQKLSMPMLEVKLYIYQLLRSLAYIHASGICHRDIKPQNLLLDPENGILKLCDFGSAKILVAGEPNVSYICSRYYRAPELIFGATDYTHAIDIWSTGCVMAELMLGHPLFPGESGIDQLVEIIKILGTPSREQIKTMNPNYMEHRFPQIRPQPLSRVFSRSVPLDALDLLSKMLQYTPTDRLTAAEAMCHPFFDELRDPNTKLHNSRNPDASPRHLPELFNFSPFELSIRPDLNQKLIPSHARDALPVKLDDFVPIPIHRARID Q10475 IF4G_SCHPO MOD_RES 83; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 452; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 455; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 456; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 459; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 866; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 882; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 884; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 886; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 911; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 919; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 921; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 923; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1333; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17C9.03; CHAIN 1..1403; /note="Eukaryotic translation initiation factor 4 gamma"; /id="PRO_0000213333" MSSKPPSNTPKFSYARALASSQSNKSNSTKASENNTATAEKQAVKPSGVEPTNTSRANAQKKTESTGKITSEADTEKYNSSKSPVNKEGSVEKKSSEKSSTNNKPWRGDNTSKPSANSSAERTSSQHQKPETSSQIGKDNAAPVENVNEKSTSQETAPPVSTVPIQFGSITRNAAIPSKPKVSGNMQNKSGVSSYSSKSQSVNSSVTSNPPHTEEPVAAKPEASSTATKGPRPTTSASNTNTSPANGAPTNKPSTDINTTDPATQTTQVSASNSPALSGSSTPSNTSSRSNRQNHGNFSEKRHYDRYGNSHPSYNKYSHYQHGFNYNNSGNNRNESGHPRFRNSRRNYNNQGAYPTYMSNGRSANQSPRNNPQNVNNGSTPIQIPVSLQTPYGQVYGQPQYIVDPNMVQYGPILQPGYVPQYYPVYHQTPYTQNFPNMSRSGSQVSDQVVESPNSSTLSPRNGFAPIVKQQKKSSALKIVNPVTHTEVVVPQKNASSPNPSETNSRAETPTAAPPQISEEEASQRKDAIKLAIQQRIQEKAEAEAKRKAEEKARLEAEENAKREAEEQAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEENAKREAEEKVKRETEENAKRKAEEEGKREADKNPEIKSSAPLASSEANVDTSKQTNATEPEVVDKTKVEKLKASEGKSTSSLSSPSHSTSSKRDLLSGLESLSLKTNPKSEQCLESLLNSQFITDFSALVYPSTIKPPSTEEALKAGKYEYDVPFLLQFQSVYTDKPMKGWDERMKETVASAFSDKSSRGMYSSSRQSSRSGSNTHSHAGPGFGGPSERKGISRLGIDRGFSSSGAGFGSGSNYKSAPSRGVSHHGHGGMSGSHRGSQRGSRRGGGERDKPDPSSLTIPVDQVAPLQLSANRWQPKKLTEKPAETKGEDEEALLPPEVVQRKVKGSLNKMTLEKFDKISDQILEIAMQSRKENDGRTLKQVIQLTFEKATDEPNFSNMYARFARKMMDSIDDSIRDEGVLDKNNQPVRGGLLFRKYLLSRCQEDFERGWKANLPSGKAGEAEIMSDEYYVAAAIKRRGLGLVRFIGELFKLSMLSEKIMHECIKRLLGNVTDPEEEEIESLCRLLMTVGVNIDATEKGHAAMDVYVLRMETITKIPNLPSRIKFMLMDVMDSRKNGWAVKNEVEKGPKTIAEIHEEAERKKALAESQRPSSGRMHGRDMNRGDSRMGGRGSNPPFSSSDWSNNKDGYARLGQGIRGLKSGTQGSHGPTSLSSMLKGGSVSRTPSRQNSALRREQSVRAPPSNVAVTSANSFELLEEHDHDNDGGQKDSNSKTSS Q10480 PNU1_SCHPO ACT_SITE 142; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10047" BINDING 174; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250" COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11406279}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11406279}; TRANSIT 1..?; /note="Mitochondrion" SPAC17C9.08; CHAIN ?..322; /note="Nuclease 1, mitochondrial"; /id="PRO_0000019921" MSSNLIKSFGLIAIGAISGVTFTHFYYKGYQGSDVPDLTPRYTKFDSAGRALESIYDFNATKFFQYGIPGPVADQRVNHGYMSVFDRRTRNPFYTAETITQESLNQRKGNRRYSEFVPDDNIPEMFQAKLGDYRGSGYDRGHQVPAADCKFSQEAMNETFYLSNMCPQVGDGFNRNYWAYFEDWCRRLTSKYGSVTIMTGPLYLPKKNERGQWEVQYRVIGNPPNVAVPTHFFKVIIAEKSGEPTSSPSVAAFVLPNKPIADNFPLKNFAVPVEVVERASGLEILSNVPKGNRKQLCSEVVCQLNVKEFVESVKQKQKNQGK Q10482 STM1_SCHPO CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-histidine(out) = L-arginine(out) + L-histidine(in); Xref=Rhea:RHEA:71063, ChEBI:CHEBI:32682, ChEBI:CHEBI:57595; Evidence={ECO:0000305|PubMed:33189720}; MOD_RES 119; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17C9.10; CHAIN 1..271; /note="Vacuolar arginine/histidine antiporter stm1"; /id="PRO_0000072277" MSVIAPSFDMANILTELSSFLGALSLGCWVVLLIPQLLENYKNQSGESISDLFLIIWLIGDFFNVLGSIYGNVSSTVLVLSFYYIVSDSTLLMQIYYYRWKAARRIASREHEPLLQSRSLEEGLHAPIGKQQIWWDRLSTRQQFGVMGCVVIVSTIVGNLIISSASSDKSDDDLNAWPFTAGCISSVLYFCARIPQIIKNHKAKSTEGLSIIFFVLASVGNTSYAFSILVFPASDYLNYTYANLPWILGAFSTIFLDIYIFYQFIKYRNHY Q10484 SCS22_SCHPO MOD_RES 236; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 237; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 281; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17C9.12; CHAIN 1..319; /note="Vesicle-associated membrane protein-associated protein scs22"; /id="PRO_0000213482" MALECDSTIVFPRPLTRLVKCDLELRNTAPYPIGFKVKTTAPKQYCVRPNGGRIEANSAVSVEVILQPLDHEPAPGTKCRDKFLVQSTELKPELQGMDIADIWTQVSKANISERKIRCVYSEGPSTANAHANAHHQPAQTTTTSIPTSATDNYTTVNGNVNQSYSKGIDGTALPSTHANPVAAPSTATTQHTQLPKTSAVSHQKPHEAPSTAVKAPTATVAENEPYPKPQSVPTTTSPNNENNALRSTANVINNTRQSTATSPSMFAGNSGNQIGLARVSSSFGRPTSGAKVVPQIHNTVTVQTAFLLAIICFLIGLLF Q10585 SPD1_SCHPO PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation. {ECO:0000269|PubMed:12695334, ECO:0000269|PubMed:14701809, ECO:0000269|PubMed:16252005}. SPAC29B12.03; HELIX 33..36; /evidence="ECO:0007829|PDB:6QH1" CHAIN 1..124; /note="S-phase delaying protein 1"; /id="PRO_0000072110" MHSSKRVMTTKTHVEQPESSMRPQLPESIQGSLMDVGMRVRKSISTGYKSKQTTFPAYNPPLYNTVSENIALKNTAFSYEPNGTKRPFEQAIPNYNWANPPQDFEEPEWLKPFDVVMEGTNERL Q10659 SPO14_SCHPO SPBC3H7.01; CHAIN 1..395; /note="Membrane glycoprotein spo14"; /id="PRO_0000051225" MAELHLSFPAYSLCWINNHQMAVGGGGGTTKSGVKNKLKLLSYEDYEPEVGEGHTKFIEHGEIELKHSDDAVMSLGYFKNELIAGINNTIDGKLIDHLRLYGRKDKLFEEKNALRLTDFDNDEQYQRLCLFEPLHDAICISCTNKSFFIISKNDHKVLFEKHGSDVYDVSSTEDKLAIAVDDRVEIYDWNTFELVQVLYMPVERATVRGVSFLPNQSIVAAYNYIKDSKRFASLVRFDYSSKNQLWRFGMIRDLKNAKGVTCFCCDKENGMIIVAGADCSIRFMSLDLTKLSQVYKHSLPVTDMQLSPDSEALVSVSADGLLCLQFVGKFKNLSAVKLEDAGVILRLSLMFPFVLAILYFYLQLLFPDEKLDAIHRFFSFILHIFSKYTIRNYDL Q10951 BYR4_SCHPO MOD_RES 326; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC222.10c; CHAIN 1..665; /note="Protein byr4"; /id="PRO_0000065032" MTEVECWDDDPDFASDVDNASLFTQSIATTSASTSVDDGFSFDDSISRLNSLSISDVPSAHSRVEQWNQQVHNLNHELSSNKNRISSNVEGYEDDFSFDEEGEEGNNEFNTLRPNKYQDADVDEFNTIRASETASQRPPIPFSSDTLKKTYLSSENDARYPSVSDSPYCESEGFSSFEDDFEIDPDTDLNSILHRKQNRMDPKASFSSVEQSSLRTPSSAHNDDGFWDDFDIDFNNETESIFRKKIRSPNTINQKHPYISSTISYQPNVHQDAKYYPLCKDIFPSLANENPHSDNPNLKYSSKTLSKRDTSSHYPETLKASSKHSSPVKGNSSISSTWTPSNLKIYHSKNSMGLMDLDALKTVASNSKYRTKPKNCKTYGDGTELDTLDELPVDYEFELKLRKKQTTKVSGTPKSKHAGSTQEWHSHTTPRSTSKHENNLNNITNSAKNEHIRSQRQHKTHAAPSKELTKESLSNDQLSVKEKRRHHKKAPTLIQNLNSPRTPKIVGKMRYNPTKHCWEGNDYAIRDFDTPISPSRPALISNISTKKGIQVVGNMVYDPTRLRWIDNSISGQEAEDPFSGFDDLEDTDSTSQYLNENSGSFNGSINSIINFPDMSEIYDVGPEFEKKQFSEDIQWRKRIDGWFFSFKNDDRSRLWELYNILNAEQ Q10988 UVE1_SCHPO SPBC19C7.09c; CHAIN 1..599; /note="UV-damage endonuclease"; /id="PRO_0000215029" MLRLLKRNIQISKRIVFTILKQKAFKGNHPCVPSVCTITYSRFHCLPDTLKSLLPMSSKTTLSMLPQVNIGANSFSAETPVDLKKENETELANISGPHKKSTSTSTRKRARSSKKKATDSVSDKIDESVASYDSSTHLRRSSRSKKPVNYNSSSESESEEQISKATKKVKQKEEEEYVEEVDEKSLKNESSSDEFEPVVPEQLETPISKRRRSRSSAKNLEKESTMNLDDHAPREMFDCLDKPIPWRGRLGYACLNTILRSMKERVFCSRTCRITTIQRDGLESVKQLGTQNVLDLIKLVEWNHNFGIHFMRVSSDLFPFASHAKYGYTLEFAQSHLEEVGKLANKYNHRLTMHPGQYTQIASPREVVVDSAIRDLAYHDEILSRMKLNEQLNKDAVLIIHLGGTFEGKKETLDRFRKNYQRLSDSVKARLVLENDDVSWSVQDLLPLCQELNIPLVLDWHHHNIVPGTLREGSLDLMPLIPTIRETWTRKGITQKQHYSESADPTAISGMKRRAHSDRVFDFPPCDPTMDLMIEAKEKEQAVFELCRRYELQNPPCPLEIMGPEYDQTRDGYYPPGAEKRLTARKRRSRKEEVEEDEK Q10990 CDT2_SCHPO SPAC17H9.19c; CHAIN 1..490; /note="Cell division cycle protein cdt2"; /id="PRO_0000050905" MNMDIGKALSDVGGLRDITSRANNSLPPTPDSSPAAPSKKHKLYDFLESRGKIETPRKRIVFEKKPLLHKPVHIQKKPAQLCKELLIRQLGGSRSHPFSTKTSRHVGGRLNLETYYSRPSECLMMLNQLPFCLGFANNESLLAVCTETGALELFDSRFYDRQNEENQPSARRIHGWLAHNNAIFSVNFSKDDSLLATSSGDQTSKVFDLSTQQCITRLGRRGVDGYHSHSVKQVNFCNDSPYNLVSCSRDGSIIFWDMRTHGITIDGEHFQKPVLRIRKAHENSGRDCSITSATWLPQSTSQVISSCSANSALKLWDLRTVHTVRPLPAATTPELTTSKRDFGVTNVCTSPDGERIYAASRDSIIYEYSSRHLNSGFCKTYKDPRLRISSFYVKLACSPDGATLACGGGVQDKTSGVVVFDTTRNCSSSAMLTGGHTKDVTAVDWSSEGQLASISDDGSVRVWNSSLHGSAANLREKNFSEIFYWGFSEK Q11120 OFD1_SCHPO BINDING 142; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P40032, ECO:0000255|PROSITE-ProRule:PRU00805"; BINDING 144; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P40032, ECO:0000255|PROSITE-ProRule:PRU00805"; BINDING 156; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250|UniProtKB:P40032"; BINDING 210; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P40032, ECO:0000255|PROSITE-ProRule:PRU00805"; BINDING 221; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250|UniProtKB:P40032, ECO:0000255|PROSITE-ProRule:PRU00805" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 = [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate; Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; Evidence={ECO:0000269|PubMed:24550462}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + O2 = [ribosomal protein uS12]-(3S)-3,4-dihydroxy-L-proline + CO2 + succinate; Xref=Rhea:RHEA:54160, Rhea:RHEA-COMP:13817, Rhea:RHEA-COMP:13818, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85428, ChEBI:CHEBI:138052; Evidence={ECO:0000269|PubMed:24550462}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:P40032, ECO:0000305}; SPBC6B1.08c; STRAND 309..315; /evidence="ECO:0007829|PDB:6E0T"; STRAND 360..362; /evidence="ECO:0007829|PDB:6E0T"; STRAND 395..405; /evidence="ECO:0007829|PDB:6E0T"; STRAND 421..428; /evidence="ECO:0007829|PDB:6E0T"; STRAND 443..447; /evidence="ECO:0007829|PDB:6E0T"; STRAND 468..472; /evidence="ECO:0007829|PDB:6E0T"; STRAND 476..484; /evidence="ECO:0007829|PDB:6E0T"; STRAND 488..492; /evidence="ECO:0007829|PDB:6E0T"; STRAND 503..512; /evidence="ECO:0007829|PDB:6E0T" HELIX 278..284; /evidence="ECO:0007829|PDB:6E0T"; HELIX 290..292; /evidence="ECO:0007829|PDB:6E0T"; HELIX 295..308; /evidence="ECO:0007829|PDB:6E0T"; HELIX 319..334; /evidence="ECO:0007829|PDB:6E0T"; HELIX 341..343; /evidence="ECO:0007829|PDB:6E0T"; HELIX 377..379; /evidence="ECO:0007829|PDB:6E0T"; HELIX 381..391; /evidence="ECO:0007829|PDB:6E0T"; HELIX 437..439; /evidence="ECO:0007829|PDB:6E0T"; HELIX 497..499; /evidence="ECO:0007829|PDB:6E0T" TURN 285..287; /evidence="ECO:0007829|PDB:6E0T"; TURN 354..356; /evidence="ECO:0007829|PDB:6E0T"; TURN 407..409; /evidence="ECO:0007829|PDB:6E0T"; TURN 432..435; /evidence="ECO:0007829|PDB:6E0T" CHAIN 1..515; /note="Prolyl 3,4-dihydroxylase ofd1"; /id="PRO_0000315938" MGDTQQPTVLDRFAPHALDTSEAERLSREYHKNGPYNHVVIRPLINDTLLRNVRKELMENIHFTEKVTDIYRVWQTGDLANLDGLDKKEQNMLKYLRQVRDALYSEEFRSHVQKITGCGPLSASKKDLSVNVYSKGCHLMNHDDVIGTRCISYILYLVEPDEGWKPEYGGALRLFPTLQPSFPAADFCHSIPPQWNQLSFFRVKPGHSFHDVEEVYVDKPRMAISGWFHYPQPGEPGYDANYCDNTVSTLQSLTMKQMDLELPRFSYYPVVKPEPLSKQDTDILSNYINPLYLTPDGIEKLSKRFFQDSVIVLVEFLNQEFANTLLKRIIDAERQPTPMHSSEVSFPWKTAIPPHKHRYLYLDHEEFGPDIILPMDLQRLPAFQRWIQLVSGLPLRSFHQVGRRFRPGSDFTLATTNDTALLEATLCLSPGTGIANTDNGAYDIYMIGDEDPDVDAAVYRGDQQDDSILLSLPAAWNVFSLVYRDEGVLQFVKYVSRQAESSRWDIYSQWNPVAE Q12126 CRK1_SCHPO ACT_SITE 133; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 17..25; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 40; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037, ECO:0000269|PubMed:9857180}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217; Evidence={ECO:0000305|PubMed:8557036}; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 165; /note="Phosphoserine; by CAK"; /evidence="ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9857180"; MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19F8.07; CHAIN 1..335; /note="Serine/threonine-protein kinase crk1"; /id="PRO_0000085879" MDIEKSDKWTYVKERKVGEGTYAVVFLGRQKETNRRVAIKKIKVGQFKDGIDISALREIKFLRESRHDNVIELVDVFSTKSNLNIILEFLDSDLEMLIKDKFIVFQPAHIKSWMVMLLRGLHHIHSRFILHRDLKPNNLLISSDGVLKLADFGLSRDFGTPSHMSHQVITRWYRPPELFMGCRSYGTGVDMWSVGCIFAELMLRTPYLPGESDLDQLNVIFRALGTPEPEVIKSMQQLPNYVEMKHIPPPNGGMEALFSAAGHEEIDLLKMMLDYNPYRRPTAQQALEHHYFSALPKPTHPSLLPRKGGEEGIKHVSSDLQRQNNFPMRANIKFV Q12701 KSG1_SCHPO ACT_SITE 223; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 109..111; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 128; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 178..180; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 184; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 227; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 241; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:22976295}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:22976295}; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC576.15c; CHAIN 1..592; /note="Serine/threonine-protein kinase ksg1"; /id="PRO_0000086226" MRNTHNPNETEASEDAENDTQSESDLSFDHGSSEKLNRASLPKTQNSAIPQSNALNTTPNESTSQIDSSPKIPSAVPHISTPNPSSGASTPNIKRVSDFKFGEILGEGSYSTVLTATENSTKREYAIKVLDKRHIIKEKKEKYVNIEKEALCILSKHPGFIKLFYTFQDAHNLYFVLSLARNGELLDYINKLGRFNEICAQYYAALIVDSIDYMHGRGVIHRDLKPENILLDDNMRTKITDFGSAKILNSSHGSHEEDTHHADKPQAHSRSFVGTARYVSPEVLSDKIAGTASDIWAFGCILFQMLAGKPPFVAGNEYLTFQSILHLSYEIPPDISDVASDLIKKLLVLDPKDRLTVDEIHQHPFFNGIKFDNTLWELPPPRLKPFGHTSVLSLSVPNASNKHENGDLTSPLGVPSMVSASTNAAPSPVGTFNRGTLLPCQSNLEEENKEWSSILQDDEKISKIGTLNVYSMSGINGNDAFRFFSSLFRKRKPRTFILTNFGRYLCVASDGEGRKTVKEEIPIKSVGMRCRMVKNNEHGWVVETPTKSWSFEDPNGPASAWVELLDKASSISLPFGNHSVTSFSRSIARSAV Q12702 2ABA_SCHPO MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC227.07c; CHAIN 1..463; /note="Protein phosphatase PP2A regulatory subunit B"; /id="PRO_0000071441" MDDIEDSLDQWKFAQCFGDKGDVEDITEADIISAVEFDHTGDYLATGDKGGRVVLFERNHSKKGCEYKFFTEFQSHEPEFDYLKSLEIEEKINKIRWCKRTNRAHFLLSTNDKTIKLWKLYEKNLKVVAENNLSDSFHSPMQGPLTTPSQLRLPRLNHHDMIIAAYPRRVYANAHAYHINSISVNSDAETYISADDLRINLWNLSISDHSFNIVDIKPENMEELTEVITSAEFHPINCNHLMYSSSKGNIKLLDLRQSALCDNPCKLFEDQEDQDSKSFFSEIISSISDVKFSQNGRYILSRDYLTLKIWDVNMEKAPVKTIPLHDVLRSKLCDLYENDCIFDKFECTFSGDDKHVLSGSYSNNFGIYPTDSSLPGDRGQIVLQADKAAFRARKSAANNVPKLNAVKNNDWRSQPQAAMGSASVGLDPDNLDYNKKILHASWHPFEDSVAIAATNNLFVFSKL Q12705 PP2B_SCHPO ACT_SITE 180; /note="Proton donor"; /evidence="ECO:0000250" BINDING 119; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250"; BINDING 121; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250"; BINDING 147; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250"; BINDING 147; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 179; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 228; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 310; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250}; Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBP4H10.04; CHAIN 1..554; /note="Serine/threonine-protein phosphatase 2B catalytic subunit"; /id="PRO_0000058835" MTSGPHNLEDPIVRAIRQKNQAPSHDFTIFVQEDGSSVSTLDRVVKNVQAPATYIPTDVEFFDINEPDKPDLHFLRNHFIREGRLSEEQTLYIIKKATEILKSEDNLIEVDAPVTVCGDIHGQYYDLMKLFEVGGNPANTQYLFLGDYVDRGYFSIECLLYLWALKIWYPKTLWLLRGNHECAHLTDYFTFKLECTHKYNIKVYEACLQSFNALPLAAIMNKQFLCVHGGLSPELHTLNDIRMINRFCEPPTHGLMCDLLWSDPLEDFGSEKSNKHFIHNNVRGCSYFYSYQAVCTFLENNNLLSVIRAHEAQDVGYRMYRKTKTTGFPSLMTIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVSEMLISMLNICSKEELYETDLKESAPTQHKQPAPSENENKADQEIDIEARRQIIKNKIMAIGRISRVFSVLREERESVSELKNVSGTQRLPAGTLMLGAEGIKNAINSFDDARKLDIQNERLPPSNSRRRSTDLKAFEEVMNSSEDDTSIDHLVERFADKKSSL Q12706 PSK1_SCHPO ACT_SITE 215; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 97..105; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 120; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22976295}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22976295}; PTM: Phosphorylated by ksg1 and target of rapamycin complex 1 (TORC1), affecting the kinase activity of psk1 in a nutrient-dependent manner. {ECO:0000269|PubMed:22976295}. MOD_RES 102; /note="Phosphotyrosine"; /evidence="ECO:0000255"; MOD_RES 248; /note="Phosphoserine; by ksg1"; /evidence="ECO:0000269|PubMed:22976295"; MOD_RES 392; /note="Phosphothreonine; by TORC1"; /evidence="ECO:0000269|PubMed:22976295"; MOD_RES 415; /note="Phosphothreonine; by TORC1"; /evidence="ECO:0000269|PubMed:22976295" SPCC4G3.08; CHAIN 1..436; /note="Serine/threonine-protein kinase psk1"; /id="PRO_0000086588" MPVFMFDEHDNLNENYNSHLSSDDEIAEEGYDFEELEASASTITSSSDLKDGKNAKDEKGTVEFKVAAHGDFISSKGDNYVPSGKMRPADFQPLTVLGRGSYGKVLLVKQKNTGRLFAQKQLKKASIVLRAKGLEQTKNERQILEEVRHPFICRLYYAFQDHDRLYLILQYAPGGELFSHLAEQRMLPEDVVAFYTAELTLALIHLHKLGIVYRDLKPENCLLDAEGHILLTDFGLSKVAENGADCRSFVGTEEYCAPEILLEQPYDHAVDWWSMGILIFDLLTGSPPFTANNHKRIMEKITRAKPNIPFYVTSDARDIINKFLKKNPKQRLGADGPEKGYDAIKKHRIYRRIDWNKLEKRMLPPPIVPCITNPEAAENFSVEFTKLPLSTTPILHEEFGNLTIGSHSSAFQGFTYVASPNFLNCEFLSNNAVSNH Q1MTN3 PIC1_SCHPO MOD_RES 171; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC336.15; CHAIN 1..1018; /note="Inner centromere protein-related protein pic1"; /id="PRO_0000255436" MGSNGSELWFNKELEYSQQLTNGKMKEFFFLVSETMDWLNEHMLEVSKLQLESDIYELVRTPTKIKEKYSTPRLSPVHRCALPTPRMRLTSIQHQLEEAAVEGYKSGESNTVKEPKELHTATNTETQFDDDRDSTKLSSEYVKDDIVNKSTKGGVSPIKETRLPTNLPAFSPTSVERRFTEWNVPLRETSPSPSETADSPNKLPKQKHPAYSFVTLPKREEILKRPASLHSRVESTNSFINQLNRRRTKDNLTNNPEISLDEPIKALPSTTSDAPSSLLNTNVSSSPSKFRKFLSSVIPAKTDLSAKESLTSSTRLSTSYKTRKRSSGVAFSSETVTSSSKERKRSVENEMLKPHPTIFESPPEITSFDKSNAVEAEALTAKLKSNEERLPVSSQPGSDAKSQEFDFFEAKIPDSIAKLNELTASNENHYELKTYDRAERLRQKIQEVSSNKRLIPSTPPTKKPINAVLDAAKNSAAKDLHLAKMKLNNKNDESSLSPAKSHAVITQAPKIPLISTFTRLSTRKSSNDFNSSNSRPSSNALKSDANENTDSSLPPSKKEFIEKSLHKLSEPLHDDSRQNSDHNFAPHSRPIAIRVATASQRELEQTEKRKAKNGAANASNMESRSSENETHRFKKFYGKERELSNNEFPSRQTKTVTSANSSNIRDMEHTISDKPRSEPDAIPSSKSMHSNKPFEEKSEKPTTKRLVTNPSNVNASWHSNMLKRQEDLRKKKPLTDNGATSRHMLKSGLTRVTSKPTQRFANELAEDMSLAFHSTIPKKMEPDSVTSVTQPSVGSLRNNFDIGTTNSQNEDRKKKIAAQKNKNPVHGNVGLTNQHGFKTMHHNVNPFTKQNGIMKGKLPSSSTSQSNKPFIEKASMHAPAKGRNSSMQEPSSKSPLLKTPKSNYFPGYGSLSPNTSVELPEINSDYSDDSDDEGNKKKVNLPSWAESPELREQLKRQQKWDPDKIFGMIKPLQMDEYFRSKDRSKIRFRPRSSSADWSSQDRLTQAEIDNYKKNMGFL Q1MTQ0 BRL1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305}; SPCC1919.15; CHAIN 1..692; /note="E3 ubiquitin-protein ligase brl1"; /id="PRO_0000352846" MSVVNESRKRRRLIHSEKETRRLDLGEEDDLELFQKEAAWRRSREYEHLTVLEKKLYEYWESLVLKLDHYVAAALENHEQSFEELEKITASLYQPDDNLQTLDLSLAEFSLIKDAQNYLNKYASYFQAHEPTLQKLAKFGSFKLKETPNVHEWIDQRQVHFTSMINYRTSQLKLALLKRKLSFFREALNSAELEWKRVQQDQLTSASERSIENIADDIPASEPKAILENGEGCLNDNDNISKLKNNFQSQADLMQANINSKLDELSQKSTRAAQLYVDIMGITDERVSREPHYLELKGVLSSNEEKIESINRDLSSLFEDIQFFISQRTKRQKDIIDLKLACVKEKQQLIKTLESSLTQIRNERDSLVAKQQMQYTNNLFFDDMMLLLSNLSNARVAILEGYSNRLCIWDRIERSKTGEMNNVLDEKEEISASSALEKLIKNNSCLEAELPSMYAAFDQSQSRLLKKYEELETKEKKALEMHYEKARATQKYFAAMKARDILMTEKKTLKLAENKEHDYIGKLQEREHALTKYESSLKAELEVYKQIKEIYGKHSVEVLTEDKHLQVKQTKLTQKLEDLIESVQKSGEKLMIMHQKLFHLQEEHTILSIKASYNKKESHLINQAYETQEAQVYKGMLKCSVCNFSNWKSKLIPNCGHAFCSNCMEPFYEHKTSTCPQCETPFSVSDILTIHL Q1MTQ1 TEA2_SCHPO BINDING 218..225; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1604.20c; CHAIN 1..628; /note="Kinesin-like protein tea2"; /id="PRO_0000259608" MSSSSSKPVNTGLVTPRRYSTMTGIRTGPSQSGTGSIPYSPTSPLSRNFSNYSIPMLRSNSTQTNVNGPTAFDLGVTEKLMSPGTLDRYTRPALYPSKDLDYLKNEYVNYESTTSQQTNSKGLKESNFVGSGIITSIRIRPIGKNQGVWSHGKLSNDPYGREYIRQQTSTSSSTIQQEYLFNNVFGMESKNYDIYKRSVKSVVRNVFSGYNGIVFAYGMTGTGKTYSMQGTENEPGIIPLAMNDLFEMVENNSDDDTFQIRISYLEIYNERIRDLIGNSDEEPRIRENASGEVNVTPLTRVLVTSPEEVSQVIEQCNAIRKTAATDFNTYSSRSHAILQVFLIRNNPTAHTSQISSLSLVDLAGSERASAHHERRKEGAFINKSLLTLGTVISRLSAAANPSLTSNSGHIPYRESKLTRLLQQSLSGQSQISLLATISIESNHTMETTNTLKFASRAQNLPQDIRQAEAVTNVQAELASLHSALEKNAQEVEYYASLVKQLTSDLEERDTYIAMLEAERSQGTAISRARLRMEELLSDHNFEIADLRDELQDKEQIIYALRYAQKQRDIADFNQSLAKFPHKILKKNVTRGSRSSSDQFSNETKTEILPDDQQQSKKDSVTQETQLLS Q1MTQ7 KLP9_SCHPO BINDING 94..101; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" PTM: Phosphorylated by cdc2 and dephosphorylated by clp1. Dephosphorylation is required for the interaction with ase1. {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:19686686}. MOD_RES 605; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 611; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 613; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC15D4.01c; CHAIN 1..633; /note="Kinesin-like motor protein 9"; /id="PRO_0000353837" MIQIFLRVKKAQPSSDASNKYGFLTVLNDYEILLESPEDSHAYRVSKSKTLEKASFTKVFPPSCTQLDVFSTICAPLIADSLVNMNDTLLFTLGVSGAGKTYTLFGPSDRPGVAFLALDALFYAIKGREASPQTVEFLRSQLEKCKIVEASKFLRGEAPLDIKVPNTEYYASHFPKIEEKNYQYAIYLSFAEIYNDRIFDLLEKASFFGHRHALSLKKSSTSDKKSIAGIQKVFVSNTTEAYKLIQKVLQLRKSTSTKSNSVSSRSHLIMSIELFKVCTKSNKFESCQIDLVDLAGSERTRSAETSGLLLREGASINRSLLTLGQCLEALRRKHEGKQHIIPFRQSKLTELLFHSGHLSGLAGINMLVNIDPFGSFDENAQVMRYSANAREILPPPLNENSGSQSPSHSLLQKSKNTSSTKALTSHLEQLQQENQQLRMLLADADSEMMNLEYEIRQQMTREMEERVSEVERTFLTKLLEESAQGIEYTDQKLEKMGGWMKKLQDENSEKTETIAQLEQIIEELHEELRSLEEESIKESSATQQNENQHKRSSRKLLYEDKQAIQEAHTINTKRKLWPQSTLIQAPNSDDEENVPSPSPKKKVVSPIKPLSPSRRPPLTSLYSGTTDIDINEL Q1RKN3 TLH2_SCHPO BINDING 1213..1220; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 1240..1247; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:15591066}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; SPBCPT2R1.08c; CHAIN 1..1919; /note="ATP-dependent DNA helicase tlh2"; /id="PRO_0000255585" MVVASEIAKVASKTARDIAGCFTCQCGTQFDNVERIVQHFKECRYRDETCKDDDIVVYEPSSFVQDEKKDKPIIVEAASEATSEEACNSSKERQLPALSALSALSTLTTSANDDLWTARLIWQSTNDTKLDNSPSSNYTDLNHKLANYGLSILSIHALMCVECECLLNVIHTAQHMQIVHKLELNEDLLWFQELRTLKLKSPTNVLQTHSSQTHVYPYIRGLPVLLNGYECVPCTKNGTGFVHAIMDTFRHHVRRTHGKVIKLENCIRRTALQTVKNKYAQRCQFFKVDYVPLNGGEEEEEEEGEEKEDAQNIKERMVDFCFSKFMEKNQQRREQQDKGENKKRQDDVDQATDNNTNTILEDDEKDNDEEEEEEIVNAREKNLLNQQFNWTAIVKKLGENWDQLVRFEYTNGIVTLDTIVNQLIRYYYRGFRHLSGMTMGMRRMFTQGGSYSAQERGLCRLEQKDTVVRYAQSAALYLIFLLRRPSADSGIRRHLEAMCGATVERKEGGSNSSSNISNVANFDSAEDDNDNDNDNDRDSNNNNNNNNTNTDDDDKLAYLELHEALKLAFLQQYDFSKNVQDLEIMEFLACMSLHKDGTSKYAYEISACFAPLIYTCRLVAACELQRLIDEKQIDLLSIPSFQTAGSIAYAHVFCFITLGQRNLYDVLYETQKVVRDIIRTEGYANTLQGLSPSTVLFQPRSNSMYPCIGDAFNNMVRLDLSELTALYEGMFAKVQDLLKELCFDMNVEKLLPISLLRSIGDDINNSKLGYSFFKESIEIRSSHSVLLRTILKNSELCHRFFPSMSKKDLTKLFGGVSDQQRNECDNYSNHYNDNSNDNDNDVFLKLHWSKSAIKKYETKASIFNELLFCLVYISAGQPARAQEMVYWTLRNGKYKTRELYLMFGRLMIYSRYDKTRNMKFAEKPIPRFLSEPLSILALRYYVLVRPLEALMKYVTTADRSKVAVYLDFMFVIAGERLQRDLPYRIFPKATYQCIQKPLGFRNYRHIAHYFKEKNIEEEMTRESYFDLQAGHTRNTALYIYGRTMDNLHYLPSDYFANFFRASYKWQELLQIRDNPTHGLLVETKHPFIKRVDQLEEALNEKLARLVGEQMVEGDKEKDKTNEEKNKDEVKAEMTQPVVNQDSHDLQDQLATTPTAPTAFHYRPGLLQPSQTSVQHCCWALSQYYGLEAKFRSLKQFQSVYFSLLNRMNLITVLPTGGGKSLSFLIPALIEKKRQTPGKVMNMVTLVLVPMMSLRQDMMLRVNEKGLLVCSGNWTAFKDVRLTLETQLPDLFILTYESALTNSGLRFFESLATLGRLARVVIDEAHLLLTSGAWRTALSRASRLSGLYAPLHLLSATFPRQLEMVARQTFCTNFYVLRETSTARENIFYFLHPYDNTEFLLDLRTLMKRTKVFEGDGRAIIFCRTKKDVEYIHRRLHQSDLFAHTHVTIYTGDVSDEERQMNFDAFRNANGKTRIMIATKAFGLGINYMGVRLVVHYGLPASSMDYVQETGRAGRDGKYAIAALFYEKYDSTWSSYVEDSMKNFLNDNTMCVRSFLASEMDGECVCCASFANCVYCSRCSDSLLGEESTVSTMYGVKPTLPETPKPAIATHSRYNASFSSSPPPQPGNSSGMSAMNTNTTSTTPVSLSELSEITLFPSSVSPTWKKSFGNANTNLKYGLEDMSLSHRRGHKRTYDEHLNNVQQGVNHDMNRVHGSVGGMSGIVGIGIGIGDGDGDGDVDSRTIHFAEYKSRVQAVKKQWVDSTDISAQLERFFRVYKDECLSCTLGNPDTEIRAHTGKACPVRLSTCYKCGKADHNLRECKLRIRFQGLCLFCGLTKFEHADSDMAYTSDCRSWARKANLISLVYYAWNNVQYRRTIADKFLQGDVRDQAFYGFVCCSTTTNSAFVLVIHYLLSDVLQIM Q2L4W6 SPO5_SCHPO SPBC29A10.02; CHAIN 1..567; /note="Sporulation-specific protein 5"; /id="PRO_0000300506" MNGIITPQKQKQLMSSPSRDPLSTTELSTPTSQTTVDVNDTKKSEGLDSTIILLTPGTSPNATPGSSELGLSKKPNSIKNNTYSTAAQAAYLNRRAADQSTVMTTDPISYANNNINNGTLPQQNAYYANSYYPSYYAQSQAISNNRPGVSGFRPAFNSVAPCYGSQWQTHQSVHPYHVNNTHQYLKPYVQNVYPQMPSLNQPGLHIVNQPTYLAPVPSATVPTNSVSLSMPSFSQGQKNIPAAINQEMSVGTTKENTNYLSQLVGLHPAIPPAIPSMFPMSHDNKKSNMESTSRTRNVYIRGLPPNTSDENLLLYTNRFGKVSSSKAIIDMETNLCKGYGFACFEEEKSALICISAMTLCGYQCSFAKESFSARLQSLQDTESTNLYISNLPLHWNESDISTLFKPSKIISNRVLRDSKEQSRGVGFARMQDRKTAEDIINKFNNFVLDPALPPLQIRFADSTDQKKFKGQTQKRRLWRAREYSVLTKGMTANNAFSKVEEFANNSMPSKVGMYVPLESNTVYQHSPTYDTYGWQSMYPSYSVYPSNYENSRSTTPYHAHPATSAAN Q4LB35 FOL1_SCHPO BINDING 472; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P9WND1"; BINDING 511; /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"; /ligand_id="ChEBI:CHEBI:72950"; /evidence="ECO:0000250|UniProtKB:P0AC13"; BINDING 546; /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"; /ligand_id="ChEBI:CHEBI:72950"; /evidence="ECO:0000250|UniProtKB:P0AC13"; BINDING 565; /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"; /ligand_id="ChEBI:CHEBI:72950"; /evidence="ECO:0000250|UniProtKB:P0AC13"; BINDING 637; /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"; /ligand_id="ChEBI:CHEBI:72950"; /evidence="ECO:0000250|UniProtKB:P0AC13"; BINDING 677; /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"; /ligand_id="ChEBI:CHEBI:72950"; /evidence="ECO:0000250|UniProtKB:P0AC13"; BINDING 712..714; /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"; /ligand_id="ChEBI:CHEBI:72950"; /evidence="ECO:0000250|UniProtKB:P0AC13" CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000250|UniProtKB:P53848}; CATALYTIC ACTIVITY: Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841, ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3; Evidence={ECO:0000250|UniProtKB:P53848}; CATALYTIC ACTIVITY: Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949, ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019, ChEBI:CHEBI:72950; EC=2.5.1.15; Evidence={ECO:0000250|UniProtKB:P53848}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0AC13}; MOD_RES 281; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1734.03; CHAIN 1..733; /note="Folic acid synthesis protein fol1"; /id="PRO_0000343164" MKSLVNLWGIYPFIRNNSLHGFAKIPRIVSTIPRQLRFSSLRHPTRQMDLIHDTVVVENLNTFAVVGQDQWKRKEPQPVQIDVYMRNNVQLAGEKDELKSTIHYGIASKLLRKEIEGSFFTTPKDLVNKIASLCFEDVIDTSHVSIKLTLPKCVLRSKNGLHYYAERERNSTSNFVDRIEFSDLELATILGIHAFERQEKQRVCLNISFANTEVEALEIARAIAEYVEQSAFLTIEALVVNLSKYLCFTKNLDDISIKAEKPSAITFANASAVQIYRTRSYFLQESLHKYESTKNKIAYLSFGSNIGDKFEQIQTALSMLHKIEGIRVLDVSPLYETEPMYYKDQPSFLNGVCKIETRMSPINLLRACQSIEQEMGRIKTILKGPRCIDLDIVLYEDCVYESEVLTIPHLGLQEREFVLRPLLALSPDLVHPYTHQPLQEALDKLPSQGIRLYSSFDNKKIINGALTMGILNVTPDSFSDGGKVSQNNILEKAKSMVGDGASILDIGGQSTKPGADPVSVEEELRRVIPMISLLRSSGITVPISIDTYYSKVAKLAIEAGANIINDVTGGMGDEKMLPLAASLQVPICIMHMRGTPETMKALSIYEKDIVEEVAVELSSRVEAAVQSGVHRYNIILDPGFGFAKTPKQSAGLLGRLHELMKKPQFKDMHWLSGPSRKGFTGYFTGDASPKDRIWGTSACVTASVLQGVSIVRVHDTKEMSKVVGMANAIRYVP Q4PIR3 NSE2_SCHPO BINDING 195; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"; BINDING 197; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"; BINDING 214; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"; BINDING 219; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00452" PTM: Autosumoylated. SPAC16A10.06c; CHAIN 1..250; /note="E3 SUMO-protein ligase nse2"; /id="PRO_0000218992" MSEAQLKTSLEALSQNLLPGNQNHCSFDFQLKEIDDSIKQVIKCALVAAEIKNNECLDMLDSGIRELLDAKQRLLLMQQSVDTLANKTSENISDFENKSLLDIYTQIFKELIQEYEEKSDYGKYGTQGEYIEFKKTIWHEQNTDGSDFPSMKTFFNVMNTEEQEADEVMVYSATFDNRCPLTLQPIVHPILSTACNHFYEKDAILSLLNPTCVCPVVGCEARLQRSLLKEDEILERRLRRAQEISNLKEA Q53EK2 NSE1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8WV22}; SPCC550.05; CHAIN 1..232; /note="Non-structural maintenance of chromosomes element 1"; /id="PRO_0000114115" MEKERQDGLSDKHKFILQYIMCRTAGVDNEQVRELVQEQYGETATVEDVINELNNSLHNFDFKIKRVQDQLDGRLTLHFQNLSGDPVSQMATPYPPVQIELMRKIIEWIMKCDDYQYSLTTLQIQKLSRKEMGLAPSVIESHLHTFERDGWLRQREGIWTFTNHALAELDAYLHNEYESNLYECNACREIVIAGYVCDCGYCLHVYCCKHLAHVNCINCNTPWANATVIGRW Q6BDR8 NSE4_SCHPO SPBC20F10.04c; CHAIN 1..300; /note="Non-structural maintenance of chromosome element 4"; /id="PRO_0000214099" MSSIDKRDLRKRYRNLINKVQESRLELVDEENNNLYETITTANDLFSSVDAPTEATLDALLLTKTVDLASIKARQLHIGRPKFNIELFTKNIKQFLNYPTSHSNVTRIQEIDTAWSRLGKLASNCEKQPASLNLMVGPLSFRKKERNIQRRERLQKAPNVLTQPTMLNERNITTQENNTTKNVLHISRLLQAHQPVNFLKFITNPQSYPQTVENLFYVSFLFKEGKAALVENESGILMLETRIPPTDDQVVAGEIRNIQLVLDMTMDLYENIIKEYNIKESIIPTRAPVETSTNSNTWYG Q6E434 TRF1_SCHPO SPBC19G7.13; STRAND 154..157; /evidence="ECO:0007829|PDB:6K5S" HELIX 102..116; /evidence="ECO:0007829|PDB:6K5S"; HELIX 120..128; /evidence="ECO:0007829|PDB:6K5S"; HELIX 133..152; /evidence="ECO:0007829|PDB:6K5S"; HELIX 161..163; /evidence="ECO:0007829|PDB:6K5S"; HELIX 168..186; /evidence="ECO:0007829|PDB:6K5S"; HELIX 194..205; /evidence="ECO:0007829|PDB:6K5S"; HELIX 214..233; /evidence="ECO:0007829|PDB:6K5S"; HELIX 239..246; /evidence="ECO:0007829|PDB:6K5S"; HELIX 251..258; /evidence="ECO:0007829|PDB:6K5S"; HELIX 269..287; /evidence="ECO:0007829|PDB:6K5S"; HELIX 291..293; /evidence="ECO:0007829|PDB:6K5S"; HELIX 294..297; /evidence="ECO:0007829|PDB:6K5S"; HELIX 300..314; /evidence="ECO:0007829|PDB:6K5S"; HELIX 410..422; /evidence="ECO:0007829|PDB:6K5U"; HELIX 428..435; /evidence="ECO:0007829|PDB:6K5U"; HELIX 450..466; /evidence="ECO:0007829|PDB:6K5U"; HELIX 473..477; /evidence="ECO:0007829|PDB:6K5U" TURN 444..447; /evidence="ECO:0007829|PDB:6K5U" CHAIN 1..485; /note="Telomeric DNA-binding factor trf1"; /id="PRO_0000290649" MSKRSLDPSDDFKGQKRLAIDPESTALEQDRQMLQQLSEQNSELEPQNVAPNAEIPLGFDLSGIQFNMTPDFYLRMNQGMDYAFNQPNPIATPQQLLRTSLIPTLGNLSNIILSILGKPVQEASAIVTNPASEMGMAFTKVMNMFRMVKDIYTEESFIYSSAIGMRTPSQRSTTRRANLAIFLAAVYGALQIGFFHLNENFLEVFAPDESNILTNQGTLYMELKTQAYISAMAQAERPKGDILNDLFPSDMAHRFLIRRNAKLDDKLTYVEKQIIEKCTARKERLANFSPQEALNEVYPWGKFLSEIACYIHNNYSSISAIPIPANSFKRRSKKNGLRFKAGEAESSPSESGSDLTDSLAFGIPSSTFDGSSETQNVSSVVLYDQVRHMTNNNLNNKRTRRVANRRSWTKEEEEALLDGLDLVKGPRWSQILELYGPGGKKSEVLKYRNQVQLKDKARNMKLFFLKSGQVVPAALQCVTGDLRRD Q7LL22 NSK1_SCHPO PTM: Phosphorylated by cdk1 at prometaphase arrest. Phosphorylation prevents nsk1 kinetochore and spindle targeting. Dephosphorylated by clp1 at anaphase onset controls its relocalization. SPAC3G9.01; CHAIN 1..462; /note="Kinetochore protein nsk1"; /id="PRO_0000304077" MAYKLSLSAVEPLLIFPAAPFSTKKEKSTFQNNLISSDVFSSALKPLSPLKSLVADFSTHSNPSKDNQLISPPKINHREFLNEEKESDTQTRYLKQLINICNSPSKNHETSLSPSKSTIDNNERKLDNEIDNYKHDVKYSPYKGQGKTSNPSQGTTKCPGIFEEDNFFSVSPKRRKNLFEKYGKTDLGKPARVPSPKKSLSSTIKSPPSRVKLPTSILSKSPPLKVPNKNRSSTFSPLRTPTSSSKTFVIVDHSTPSPPSIRTKLEAFAPNSTFATQKRLRRLATLESSPALRSTLKSLQSKSSPVKLLKLKEEKAKIKNQLFKSEEEKDPVGKQKLPLESSLSPLDHSSAEKEMQKAPAKNKRRRTGSLETGLYPKESPTPSKKRSKRVLWSLKHIVSPGNREKHSLNSTPESIMKKDTKWPQNLAKNNINSEPNTPTKSNIDTGKAHSARAHKTRKNIQS Q874R1 RHO4_SCHPO BINDING 21..28; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 70..74; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 200; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC16A10.04; PROPEP 201..203; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281273" CHAIN 1..200; /note="GTP-binding protein rho4"; /id="PRO_0000198943" LIPID 200; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MSAFKKSGSKSETSKKLVVVGDGGCGKTCLLIVFSSGTFPERYVPTVFENYITDITYGPNSKVIELALWDTAGQEEYDRLRPLSYPNSNVILLCFSIDCPASLNNVTEKWYPEVQHFCPRTPIVLVGLKADLRKDRNATEVLRTQGLTPVTYQQAQSVALSMNAPYVECSAKENTGVNEVFQLAVGLTIKKSFSFSKKSCVIL Q8WZJ7 C1TC_SCHPO BINDING 50..54; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 97..99; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 168..170; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 193; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 268..272; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 374..381; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:195366; EC=3.5.4.9; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; EC=6.3.4.3; SPBC839.16; CHAIN 1..937; /note="C-1-tetrahydrofolate synthase, cytoplasmic"; /id="PRO_0000315626" MALLLEGTSLARKVREELREQISSIKSVDPYFNVSLKIIQVGGREDSNVYVRMKTRAANEAGISCEHVNFPEDITEYDLLLAIKGFNEDPTVHGIIVQLPLPAHINEQIITEAVAPEKDVDGFCETNLGKLTKREGQPLFTACTPKGIMCILKHYGINVQGKHAVVIGRSNIVGRPMSILLEKANATVTLCHSKTESIADIVRTADIVVAAIGIPHFVKADWLKKGVVAIDVGINSIPDATKKSGYRLTGDIDFENAKEVASAITPVPGSVGPMTVAMLLQNVVESAVRFRKMSRKRKPTLLPLKLQTPVPSDIEIARSQTPKNIGDLASEIGIAKSELEFYGSHKAKVNLEILQRLAHRRDGHYVVVTGITPTPFGEGKSTLTAGLVQALSNLDKLAIACVRQPSQGPTFGIKGGAAGGGYSQFIPMEEFNLHLTGDIHAITAATNLLAAAIDTRMFHENTQSDAALYKRLTLVKGNKREFAPVMFRRLKKLGIDKTNPEELTEEEQRKFARLDIEPSTISWNRTLDVNDRFLRKITIGENPTEKGFTRQTGFDLSVASECMSVLALATDLKDMRERLGRMVVASNKSGEPVTADDLGVGGALTVLLKDAIKPTLMQTLEGTPALVHAGPFANISIGASSILADRIALKLAGTEVDEDAKKEAGYVVTEAGFASDIGMEKFFNIKCRTSGLKPDAIVIVATVQALKLHGGGPPVGPGKPIPEVYKREDVDLVRKGCANLAKHISNARKYGLPVVVAINKFSSDSPNEISAIREEALAAGATDAVDSNHWAEGGKGALGVARALINACENVDSEFRLLYDVHEPIEKKIEIIAKEMYGADGIELSPLAKERLETFTKQGYNNLPICIAKTQYSLSHDPDLKGAPTNFTVPIRDMRLSAGAGFIYPLAAAISTIPGLPTKPAYYNIDIAENGDIVGLS Q92340 SHU1_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC1F8.02c; PROPEP 200..226; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000389138" CHAIN 21..199; /note="High affinity heme transporter"; /id="PRO_0000116632" LIPID 199; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MISLKIYFVLIFLFLKGINSAYVSNEEGETVDFTFSGFYANLTYPNEISELNYVEGNYLSTRIVRFNGSFYCDTTILSETNNVTGSCYVANCANDTVLEICDSGKEVHFTDMSGTTWSADTFTENLYWFCGGDGNKPNMTTAAAMNSDIDSYYVYGNWTIDTADSTVADYTCNYTHFQEAGDIEKGDVYTASADSSDSSSASSTIFKPSYFISCLLSVGLYLVLNF Q92341 STR3_SCHPO MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 38; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F8.03c; CHAIN 1..630; /note="Low affinity heme transporter str3"; /id="PRO_0000084881" MEAKETHSISDHEVELQDAKPEEKSENGNFVFEKAFSSDEEKGSGYNTNETYSKMDNSLQHRGVSKIEAVRDSIYQNKRGMYLAYAFGIAILACSWASAIQSSTTYSYQVYATASFNRTSMISTLEIATAIISSVCKPILGKFSDITSRPMTYTLVLLFYVIGFIVVASSSTISAYVIGSVFISIGSSGLDYLNTLVVGDLTSLKWRGFMTALLSTPYIATVWFTGFIVQGIIDSNWRWGYGMFAIIMPAVMTPAVIILMYLERQANKDENIKKIINYQTEEKNKNKQSKWQKLWKAVLEVDLFGLILLGVGWSILLLPFSLTSYAKNGWKNPSMIAMMVVGGVILIAYSGYEMFIAPYPSCPRRVMNRTFITAVIIDFFYYLAGYLQSMYFTTYTWILYDWSYRDWTYFNNTMTIALCVFGVFAGAMHRVFHRYKYLQIIGLVIKIVGYGILIRPNFAATGKVDLAWSLILIGMGGSFSVVGSQVSCQASVPHQDLAIASSLLPLYTNIGGAIGAAIASPIFSNKVPKYLREYLPSSINDTQVYNFYSDSSLIREYPVGTEIRDGAIKAYSRSMFFLLVPAVSLSFIPLAAAFWQSNFYLGNQQNAVEGDQDHKKKGDKETTQEEKIII Q92351 PCP1_SCHPO MOD_RES 906; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6G9.06c; CHAIN 1..1208; /note="Spindle pole body protein pcp1"; /id="PRO_0000058259" MSERDFNTQSPKFKDENANSVISQSDFLGKSLKNNNDDYSDFRGSYLNDKSSFQTPLRNGSYQPKGSLEFTPLLQSSNKNSDKYNGSLGDKGSFDPNSYGLSAISKQATQEALSISQGNDSYDVSKLTDLSKNSEIDHTDGELPANAALTLREQEKVLEKVSRENFGLRIKIVCLEKRLESMAPEQIKEAVKDNVELHAERANLQLQLKRTESLLQKSEDKNFKLEEKVDYLSKVNDVEQSQNVKVFTERIRFLENALEKVQREKDSLSTEMEEDKSNKEVDYEYEIRQLQNRLDELSEELDVAQDLLTEKEDEIATLKRQIEEKENSSSAFENEENSSYVHLQEDYAILQAKCDEFADRIQVLTADLEKEKENQIMHESEASIGLTDSMQVHTLQEQLHKANEEIEFLHDQISRMNEEGKNFEDIMLQFRSLEEERDVLESKLQTLEDDNNSLRLMTSSLGNQIESLRTQNREIDEEKNHLRLLASKNSDKALAETNIRLQEVTKELETLRMKNSNDLNEIHDLREENEGLTLKIDSITKEKDRLINELEQRIKSYEVNVSELNGTIDEYRNKLKDKEETYNEVMNAFQYKDNDLRRFHESINKLQDREKELTSNLEKKNLVISSLRETVAMLEKERESIKKYLSGNAKDLDNTNLMEILNDKISVLQRQLTDVKDELDVSEEEREEAIVAGQKLSASFELMSNEKQALELKYSSLKNELINAQNLLDRREEELSELSKKLFEERKIRSGSNDDIEKNKEINVLNSELADKLAQIRHLESDKMELDKLVHHLNRGIEEANIEENAVKKRLCLLMGCDYSSVSILQIVSQIEHFVNQQIQTIRSLKQELRHDFVQFSGKKEQELSRSFEKFGLGTETKHDILAQRNRNVSEKMNDLENAAQKFFSSPDRKNGYLYPSEHTSKIEYLEKTIEDLKLALQDELKNRNLLMDDISSYNKQTTKLQEKIKWLERERSILIDELESYRSNQFNYQNNLVQDKNELEERLKEIQKELEVYNNHFMKQAELMTSNVTDESQLMLKTLREALQSKTNNIDHLSTILERNRKEYKSLLDDYNQLRARYKNLQSNTPQSTQSGQYESEIKGLSKLTKYLQSKCRREHSLRLDLAFSKKFILMQLTGYETCNKINLRMLQKIGISPDPDLSKKHIKLKSLIIVVCSIERMKRMKNEWLKQAQLKQSLQRAAAKAKTANY Q92355 SEN1_SCHPO BINDING 1134; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 1155..1159; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 1407; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 1445; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 1574; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" SPAC6G9.10c; CHAIN 1..1687; /note="Helicase sen1"; /id="PRO_0000080723" MAENLSDQDCFEKLSSSKEGQHWFCSGLLTQYIQPTFFWFAHDETPSFKWVLNAYHERLRSCTSCIQAYYELRNESLAKGSYSFTGFSITDLQEKWNKWDIIRVLEDFKALEDETIDFTSLPCLIFETLLNPKLFTCKNIYKNAIDAFNGLLSDWCSNIFLPGYLLFFYEASHPDVLEWVHSFFKENTEIRISSATVDAVFNTVVFESQNSSDSDCNFVSISSPEFWERTYMFLELLPLQSITAACESILKDYLLNLVKTSESLSSQQMSCLRICCNSSSFWSAADSFKEVSSFLKNLLKNVTATPFEVSDMNWAYIIASFFRTCLNDFVSVFPEWLKGFVEEKRTIGFIIYSVLDALFDLLSLDYSSPSFLNNTLSLMNANSITILQDYPEYMLKLRLHSLLYDIAFISWSHKAITKNPSFVFDPSYELSPFWKLDNLQEEKISDVLFSKISSCCFAHDIEISENSTPSGTMVQFAELWQVMSEYISGFLKGFSEKSSTEISNMLGDSSKFDTVVSFLLSPTQPLYVSAFHIVQIITNCTKNRNEALKKLVAMDFRGIVHGLADAVLNWQSILSFFPALRIMRFLSITNKSLSSDNSAFTENDIPTLGAYWQCIWNILDLVFSNVARWSLNNPADTVKALMKLTLKFVDDLFQNDGIFIKLLAKFDSLILLGETSESLFSFIMWLKINDLELRGIVINSLCKLFTKFSNFDYLFEDRTVTFLTDFIIRKQKAHLSADQCKQLANVLTQASPEAKTVLEQHRLSEMRKTKKQTELTNSAHVIKPSPTPQITVKQNTTKSSSAPRMGMLEQLKQEYLTKRNFESKLKSSAVSSRKPTFNEVKPANLLAEDLSDNEDDIDRKQGLFSLAKANKIPEIRQQERRQVQLLSNSTIKMHPSQIRMMTNRNVANVKARLFPSMTDFYKEILSWEPANQSPNPVLKFHKLDGKIIDSFKTVEHYMEVLQPMIFMECWSQIQSTKLDLKFSPVEGIMVERTAVNNFVDIGVSVAPKDLYGYPLYDTEVVSLAFNKEDASSMKGLCCFAKVERIVRQTNGVLVVLRTLPSMEILNKLQGNCALWFLKLTNLATFTRQYAGIRGLPYFHLADDIIRARPCSQPVKHSSSEIKAAMKRYQVNEPQAKAIMCALDNNGFTLIQGPPGTGKTKTIIGIISALLVDLSRYHITRPNQQSKSTESKQQILLCAPSNAAVDEVLLRLKRGFLLENGEKYIPRVVRIGNPETINVSVRDLSLEYQTEKQLLEVNQGAIDLGSLQELTRWRDTFYDCIQKIEELEKQIDVARDVAEDTKSLGKELQNKINEKNLAEQKVEELQSQSFTKNKEVDLLRKKAQKAILKQADVVCATLSGSGHDLVAHSSLNFSTVIIDEAAQAVELDTIIPLRYGAKKCILVGDPNQLPPTVLSKKAASLNYSQSLFVRIQKNFSNQMCLLSIQYRMHPDISHFPSKKFYDSRLEDGDNMAEKTQQVWHVNPKFTQYRLFDVRGKERTSNTMSTYNLEEVEYLVNMVDELLNKFPDVNFTGRIGVITPYRSQLHELRRAFKVKYGKSFMSTIDIQTVDGFQGQEKDIIFFSCVKSYSKHGIGFLRDFRRLNVALTRARSSLLIIGNMETLKTDDLWGSLVDDALSRKLVESPHIDSEGRLITISRTSEKRMKNEEFVEPPSKKLANSEPSKEIRQRS Q92356 SYB1_SCHPO SPAC6G9.11; CHAIN 1..121; /note="Synaptobrevin homolog 1"; /id="PRO_0000206746" MSEPYDPYIPAEPSAAVRSGNAAASSTPNMKTAAIQQQIDDTVGIMRENISKVSERGERLDSLQDKTDNLAVSAQGFRRGANRVRKKMWWKDMRMRLCIIIGIIILLVVIIVPIATKFHGK Q92358 BQT1_SCHPO SPAC6G9.13c; CHAIN 1..132; /note="Telomere bouquet protein 1"; /id="PRO_0000116629" MHLLTTTLISFEQNKVEYLTQIAIYTQTPVCTDSNCEHARFLKHSLIQVSIERIEYLYSIFPNIWQFALLCQGQNKESLIHMEEDASTNFKLRYYVLPWSRRLQGYQSITVQNGSHVPLVKRLEKWRIFVEC Q92370 TRPG_SCHPO ACT_SITE 108; /note="Nucleophile; for GATase activity"; /evidence="ECO:0000250|UniProtKB:P00900"; ACT_SITE 197; /note="For GATase activity"; /evidence="ECO:0000250"; ACT_SITE 199; /note="For GATase activity"; /evidence="ECO:0000250" BINDING 80..82; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P00900"; BINDING 112; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P00900"; BINDING 158..159; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P00900" CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; CATALYTIC ACTIVITY: Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48; CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; SPBC1539.09c; CHAIN 1..759; /note="Multifunctional tryptophan biosynthesis protein"; /id="PRO_0000056865" MSEKVDVGESVKGDASENAVKEVAERPIVMIDNYDSFTWNVVQYLSNLEKRYPIMVFRNDEITVDELEKLNPLKLVLSPGPGHPARDGGICNEAISRFAGKIPILGVCMGLQCIFETMGGKVDSAGEIIHGKVSKINHDGLGFYQGIPQNISVTRYHSLAGKISSLPDCLDVTSWTENGVIMGARHKKYAIEGVQYHPESILSEYGKEYIQNFLNLTAGTWEENGIVMPTKNNAFNAAMRENSNSVSSTKIRKQESILEKIHAQRLIDIAESKRKPGLSVGDLQTYLNLNIAPPCINFYERLKQSKPALMAEVKRASPSKGDIKLDANAAIQALTYAQVGASVISVLTEPKWFKGSLNDLFVARKAVEHVANRPAILRKDFIIDPYQIMEARLNGADSVLLIVAMLSREQLESLYKFSKSLGMEPLVEVNCAEEMKTAIELGAKVIGVNNRNLHSFEVDLSTTSKLAEMVPDDVILAALSGISSPADVAHYSSQGVSAVLVGESLMRASDPAAFARELLNLSSSEISNGKKTSTPLVKVCGTRSLLAAKTIVESGGDLIGLIFVEKSKRKVDLSVAKEISHFVHTTNRKHISPKKAVTGQSWFDHQYENLASSPHPLLVGVFQNQPLEYIRSIIAEVNLDIVQLHGQEPFEWIHMLDRPVIKVFPLNSSEISRPNYHIVPLIDAYVGGESGGLGKKVDWEAASFIPVSYVLAGGLTPKNVQDAISVSRPAVVDVSSGVETDGKQDLEKIKAFINAVKEL Q92372 RFA1_SCHPO SPBC660.13c; CHAIN 1..609; /note="Replication factor A protein 1"; /id="PRO_0000097266" MAERLSVGALRIINTSDASSFPPNPILQVLTVKELNSNPTSGAPKRYRVVLSDSINYAQSMLSTQLNHLVAENKLQKGAFVQLTQFTVNVMKERKILIVLGLNVLTELGVMDKIGNPAGLETVDALRQQQNEQNNASAPRTGISTSTNSFYGNNAAATAPAPPPMMKKPAAPNSLSTIIYPIEGLSPYQNKWTIRARVTNKSEVKHWHNQRGEGKLFSVNLLDESGEIRATGFNDQVDAFYDILQEGSVYYISRCRVNIAKKQYTNVQNEYELMFERDTEIRKAEDQTAVPVAKFSFVSLQEVGDVAKDAVIDVIGVLQNVGPVQQITSRATSRGFDKRDITIVDQTGYEMRVTLWGKTAIEFSVSEESILAFKGVKVNDFQGRSLSMLTSSTMSVDPDIQESHLLKGWYDGQGRGQEFAKHSVISSTLSTTGRSAERKNIAEVQAEHLGMSETPDYFSLKGTIVYIRKKNVSYPACPAADCNKKVFDQGGSWRCEKCNKEYDAPQYRYIITIAVGDHTGQLWLNVFDDVGKLIMHKTADELNDLQENDENAFMNCMAEACYMPYIFQCRAKQDNFKGEMRVRYTVMSINQMDWKEESKRLINFIESAQ Q92373 RFA2_SCHPO PTM: Phosphorylated in a cell cycle-dependent manner. Hypophosphorylated in G1, becomes phosphorylated at the G1/S boundary, it is maintained in this state through the M phase. SPCC1753.01c; CHAIN 1..279; /note="Replication factor A protein 2"; /id="PRO_0000097274" MAYDAFGKPGYGPDFNSAFSPGMGGGAGFNEYDQSSQPSVDRQQGAGNKLRPVTIKQILNASQVHADAEFKIDGVEVGQVTFVGVLRNIHAQTTNTTYQIEDGTGMIEVRHWEHIDALSELATDTYVRVYGNIKIFSGKIYIASQYIRTIKDHNEVHFHFLEAIAVHLHFTQKANAVNGANAPGYGTSNALGYNNISSNGAANSLEQKLAEYSLTPAQMTVMQAIHSAPETNEGVHVRQLAQSVGPGIDLTAVTDFLQQEGIIYTTIDENHFKSVLQDQ Q92376 KLP1_SCHPO BINDING 575..582; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" SPAC3A11.14c; CHAIN 1..832; /note="Kinesin-like protein 1"; /id="PRO_0000125385" MVIENTKDISINTGYKRQEDALNTDSEDLIYRPKKIIKTNQEDAVHDLKYENFVSKNHVLQSDINGKKRDSNRDKAAVVTAPIASTHESNYEESVSKFKESWLPQLKDLIESHKTICESTLAYESDQAMASSNTLKRIKDLKSKPKNIIQLERLHMLSNGEHRLLSKDETDDIESAYLNLRSHLQVQEQVYAEKDHEYSLQLQSYREAAEKAKQDILETKENLSSELSISNIQLKEAKERLEAANASYQKLRREHKELALYHEKKTHSLVCNLNGERKSFGDFVENEVKSYKHEYANICESLRRALVLIQGSCTEKILRFKEKILDLLEMKQQEENDRISHIEYENDLTVKKLKRRISELEMAVKEYESEKSYSEKEYEEKISSLRIELEDKLAEIDMLRNKLLKEEHKHHSTSEKLEELSKYVASIQDKERNNGQNALELQARIQQLERRNEDMYNKLLAEEIIRRKLHNDIQELKGNIRVFCRVRPLLPSEESEYCIADVLQFPDKDALEPQKLILKGPNVESSLGHTYDRNYEFSFDRVFAPESDNSSVFEEISQLIQSAIDGYNVSIFAYGQTGSGKTYTMSSQDGMIAMSIKHIFNYLSTLREKGWVYKLRGQFLEIYNETIYDLLNKAEMLKNPKHDIHHDEKERRTTVDNVSIIDFNEEDTVYKMLNRAGENRFIAATKANERSSRSHTVFMLYIDGENSRTKQICKGTLNLVDLAGSERLSYSQAVGDRLRETQAINKSLSCLGDVIHALGNASNSTTKEKSHIPYRNSKLTYLLKYSLGKGAKTLMFVNVSPLKSQFMDTLNSLRFATKVNDTKVGSIKHYKR Q92383 MAG1_SCHPO ACT_SITE 170; /note="Proton acceptor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21; SPAPB24D3.04c; STRAND 61..63; /evidence="ECO:0007829|PDB:3S6I"; STRAND 121..123; /evidence="ECO:0007829|PDB:3S6I" HELIX 17..23; /evidence="ECO:0007829|PDB:3S6I"; HELIX 27..36; /evidence="ECO:0007829|PDB:3S6I"; HELIX 50..60; /evidence="ECO:0007829|PDB:3S6I"; HELIX 65..76; /evidence="ECO:0007829|PDB:3S6I"; HELIX 80..82; /evidence="ECO:0007829|PDB:3S6I"; HELIX 87..92; /evidence="ECO:0007829|PDB:3S6I"; HELIX 95..101; /evidence="ECO:0007829|PDB:3S6I"; HELIX 105..120; /evidence="ECO:0007829|PDB:3S6I"; HELIX 126..129; /evidence="ECO:0007829|PDB:3S6I"; HELIX 134..141; /evidence="ECO:0007829|PDB:3S6I"; HELIX 149..158; /evidence="ECO:0007829|PDB:3S6I"; HELIX 171..180; /evidence="ECO:0007829|PDB:3S6I"; HELIX 189..196; /evidence="ECO:0007829|PDB:3S6I"; HELIX 197..199; /evidence="ECO:0007829|PDB:3S6I"; HELIX 203..212; /evidence="ECO:0007829|PDB:3S6I"; HELIX 213..215; /evidence="ECO:0007829|PDB:3S6I" TURN 44..47; /evidence="ECO:0007829|PDB:3S6I" CHAIN 1..228; /note="DNA-3-methyladenine glycosylase 1"; /id="PRO_0000194881" MTLDIEEKEEIVTSLTKAEIHLSGLDENWKRLVKLVGNYRPNRSMEKKEPYEELIRAVASQQLHSKAANAIFNRFKSISNNGQFPTPEEIRDMDFEIMRACGFSARKIDSLKSIAEATISGLIPTKEEAERLSNEELIERLTQIKGIGRWTVEMLLIFSLNRDDVMPADDLSIRNGYRYLHRLPKIPTKMYVLKHSEICAPFRTAAAWYLWKTSKLADYTKPVRPKKH Q92398 SPM1_SCHPO ACT_SITE 149; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 27..35; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 52; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; PTM: Dually phosphorylated on Thr-186 and Tyr-188, which activates the enzyme. {ECO:0000250}. MOD_RES 186; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 188; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC119.08; CHAIN 1..422; /note="Mitogen-activated protein kinase spm1"; /id="PRO_0000186341" MDRRHRVYRVFNQEMYVEPNFKVVKELGQGAYGIVCAARNVASKDQEAVAIKKITNVFSKSILTKRALREIKLLIHFRNHRNITCIYDLDIINPYNFNEVYIYEELMEADLNAIIKSGQPLTDAHFQSFIYQILCGLKYIHSANVIHRDLKPGNLLVNADCELKICDFGLARGCSENPEENPGFMTEYVATRWYRAPEIMLSFSSYHKGIDVWSVGCILAELLGGTPLFKGKDFVHQLNLILHQLGTPDEETLSHISSSRAQEYVRSLPKQRPIPFETNFPKANPLALDLLAKLLAFDPNRRISVDDALEHPYLAVWHDPSDEPVCDSVFDFSFEYIEDANELRRVILDEVLNFRQKVRRRSHPTNPTVNIPQPAQTVPSNDNGSFNVSSSSSSQTSNKKRHDHSYNETAAIDHKSDDNRHN Q92462 PUB1_SCHPO ACT_SITE 735; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; MOD_RES 156; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 178; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 180; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC11G7.02; CHAIN 1..767; /note="E3 ubiquitin-protein ligase pub1"; /id="PRO_0000120332" MSNSAQSRRIRVTIVAADGLYKRDVFRFPDPFAVLTVDGEQTHTTTAIKKTLNPYWNETFEVNVTDNSTIAIQVFDQKKFKKKGQGFLGVINLRVGDVLDLAIGGDEMLTRDLKKSNENTVVHGKIIINLSTTAQSTLQVPSSAASGARTQRTSITNDPQSSQSSSVSRNPASSRAGSPTRDNAPAASPASSEPRTFSSFEDQYGRLPPGWERRTDNLGRTYYVDHNTRSTTWIRPNLSSVAGAAAAELHSSASSANVTEGVQPSSSNAARRTEASVLTSNATTAGSGELPPGWEQRYTPEGRPYFVDHNTRTTTWVDPRRQQYIRSYGGPNNATIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKRDFRRKLIYFLSQPALHPLPGQCHIKVRRNHIFEDSYAEIMRQSATDLKKRLMIKFDGEDGLDYGGLSREYFFLLSHEMFNPFYCLFEYSSVDNYTLQINPHSGINPEHLNYFKFIGRVIGLAIFHRRFVDAFFVVSFYKMILQKKVTLQDMESMDAEYYRSLVWILDNDITGVLDLTFSVEDNCFGEVVTIDLKPNGRNIEVTEENKREYVDLVTVWRIQKRIEEQFNAFHEGFSELIPQELINVFDERELELLIGGISEIDMEDWKKHTDYRSYSENDQIIKWFWELMDEWSNEKKSRLLQFTTGTSRIPVNGFKDLQGSDGPRKFTIEKAGEPNKLPKAHTCFNRLDLPPYTSKKDLDHKLSIAVEETIGFGQE Q96TL7 RAP1_SCHPO SPBC1778.02; STRAND 470..472; /evidence="ECO:0007829|PDB:5WE0" HELIX 499..507; /evidence="ECO:0007829|PDB:5YC2"; HELIX 647..662; /evidence="ECO:0007829|PDB:2L3N"; HELIX 666..676; /evidence="ECO:0007829|PDB:2L3N"; HELIX 680..688; /evidence="ECO:0007829|PDB:2L3N" CHAIN 1..693; /note="DNA-binding protein rap1"; /id="PRO_0000097171" MSFTFTKSDGSSILFAVSKNFEHIRGFKNAIDCFKGKIEFLSFDKVDPTKHDYYLVAEDERVSDLDIPKGFFERNPEFRHKMLKIAWITQCIEQGKLLPTESFEVELNQDDVNRTHDGFRKRELFTLEDEKILIDHVHKNDINRFGTKVYEELARKYPQHSLESWRQHYKYMKKRLPPVSDSDESNYCQRIIVKPYSSQKDYTQSTHEQTLSSPISKSASVSKSENKALVNNKRYSDSYFYFSKMRRISIDVDYVDEDLNLINAYLSQFGKKRSLNELCALLSRRFSNRHTFSEWRALFMHFFPFINSEGVDPAILSDRETSAMLDETSDNEVADIDDQMIERKYLFSASEPNTVKSTNRLIFSERKAYAADDSIDNTPSKVPIVNSLSDPRTNRPFFYSNPDSMYRSISNPLHLVDSQHLSPLNRKTHFNNPIGQPQFTCLDDHEKTLRETSFRSLDDMSLRKSNSDNIFVKPGEDLEIPLLSDYSDSENISEKSSDDEEAFEKQVTSSYSSPIKVKSQGKSSKGSSGLDVREHEGSDDDAEVFVDRSPESFGATKVAHTSLEGNAASHKKVEENMQQPVTKKQKKYRMVNEEAHTGPTIIIPSDNNEKVTTLPAGHVPSEEKGKFINLAMHELQNEVSILRSSVNHREVDEAIDNILRYTNSTEQQFLEAMESTGGRVRIAIAKLLSKQTS Q96WV9 CDK9_SCHPO ACT_SITE 166; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 42..50; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 65; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; MOD_RES 211; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 212; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 565; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 577; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32H8.10; CHAIN 1..591; /note="Probable cyclin-dependent kinase 9"; /id="PRO_0000085808" MKRSSSVSVEDEKSARRKLDVVPKLHFVGCSHLTDYHLMEKLGEGTFGEVYKSQRRKDGKVYALKRILMHTEKEGFPITAIREIKILKSIKHENIIPLSDMTVVRADKKHRRRGSIYMVTPYMDHDLSGLLENPSVKFTEPQIKCYMKQLFAGTKYLHDQLILHRDLKAANLLIDNHGILKIADFGLARVITEESYANKNPGLPPPNRREYTGCVVTRWYRSPELLLGERRYTTAIDMWSVGCIMAEMYKGRPILQGSSDLDQLDKIFRLCGSPTQATMPNWEKLPGCEGVRSFPSHPRTLETAFFTFGKEMTSLCGAILTLNPDERLSASMALEHEYFTTPPYPANPSELQSYSASHEYDKRRKREQRDANSHAFEQTANGKRQFRFMTRGPSDPWYGIRRPNYNSQPQYQRGSYNREGGNMDRSRNVNYQPKRQQNFKPLTSDLPQKNSEFSETNAMNQTSNHSHADGQRYYRPEQDRSQRLRNPSDYGRQGRQSSQSQQPAWNVSSRYQNNSKVQTTSRASENADTNKTQHNIKYIDSYVPEYSIARQSANQKTNEQHPSSTSLHQQSTSDLKSPSFHENSNVDDTPK Q9C0U7 VPS5_SCHPO BINDING 244; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 270; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 284; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250" MOD_RES 55; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCPJ732.01; CHAIN 1..576; /note="Vacuolar protein sorting-associated protein vps5"; /id="PRO_0000213803" MLGHNIYEEDDAFNPFADSVSPLNPPKTDQEPSAEGVEEESPNVQASPPKTHIYTSPRKRSVNLKSLPFETLTLDSAPLGPLQFSDAPSMAPENNRLEVGLNTKINPLKGSSPALNADFSANKPWISEVNSFSPSPIGATENPTIPNSEQTVDTLDAASSSAPNFTHTVSSASSQKQGSTSLTDTENQKAHPAAAPQSLTPFYIQVHDPHTVKEITKSHTVYSVSTRLEEHNQPSVSNVTVQRRYNDFAFLYQLLSNNHPGCIIPPIPEKQVVGRFDDEFIEQRRAALEVMLRKISAHPVLRDDYSFKLFLEAETFDPRMTHRTTLIESSSSPLRSGPSTSGLLDSFTSAFHTSGSSKFSEQDPILIEAKDTLDSLETQLKSVYHALLLSIDQRIQFASAIHDFGEAVGNLSLVDLEPTLSSKFDGLSQLQVELRFVQERKVAQDNLTLGTTLEEYIRYVESAKNAFTTRQKLWQTWQSSVQAVSRAKTQLEKCKKQAKSQQKSLPYLEEQYEKYRAKAADLEKEFSESTTLLKRDLSSLTTSRVDDLKASVETWLESAIESQKEIIERWESFLDQ Q9C0Y4 AGLU_SCHPO ACT_SITE 481; /note="Nucleophile"; ACT_SITE 484; ACT_SITE 647; /note="Proton donor" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; SIGNAL 1..24; /evidence="ECO:0000269|PubMed:11298744" SPAPB24D3.10c; CHAIN 25..969; /note="Alpha-glucosidase"; /id="PRO_0000018581" CARBOHYD 37; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 67; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 99; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 116; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 139; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 146; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 209; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 245; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 249; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 331; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 406; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 429; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 462; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 470; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 520; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 523; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 589; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 648; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 801; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 810; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 821; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 885; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 915; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 934; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 942; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 954; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 966; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MMISTAYQSLFLTALFSAISIAVGNVYQTLNVIGDRNVTIPTNGIPQRLSVYDPYRGVNCQGYQAVNISESQNGVTAYLALLGEPCYAYGTDYPLLFLNVTYEEADRVHISIKDANNTQFQFTSRKDLWDAPLYSPSYNNTNLLYNFSYNANPFEFWVTRKSDGEVLFDTRGQKLVFEDQYIELTTNMVENYNLYGLAETIHGLRLGNNLTRTFWANDEPSPVDQNMYGSHPYYLEQRYKADGINSTLNETTYTSSSHGVLMLTANGMDVLLRQDYLQYRMIGGVIDLFVYSGSTESPKETVKQFVQSIGKPAMHQYWTLGYHSCRWGYTNITEIMDVRQNYIDADIPVETFWSDIDYMEKYRDFTVDPVSYSKSDMQTFFSDLVSNHQHYVPIIDAAIYAANPYNHTDDSYYPYYAGVEKDIFLKNPNGSIYIGAVWPGFTAFPDFTNPDVVDYWKDCLINLTYAFGSNGTVPFSGIWTDMNEPSSFCVGSCGSAMIDLNPAEPLTGISKQYSIPEGFNVSNVTEYSSAYSASLSNYYATATSSVFQIVSPTATPLGLKPDYNIDWPPYAINNEQGNHDIANHIVSPNATTHDGTQRYDIFNMYGYGETKVSYAALTQISPNERPFILSRSTFLGSGVYGAHWLGDNHSLWSNMFFSISGMIVFNMMGIPMVGADVCGFLGDSDEELCSRWMAMGAFSPFYRNHNNIYQISQEPYTWSSVAEASRRAMYIRYSLLPYWYTIMAKASQDGTPALRALFVEFPNDPTLADVDRQFMVGDSLLVTPVLEPNVEYVQGVFPGDNSTVWYDWYNHTEIVRQYNENVTLYAPLEHINVAIRGGSVLPMQQPSLTTYESRQNPFNLLVALDRDGSATGELYLDDGVSIELNATLSVSFTFSDGVLSAVPTGSYEVSQPLANVTILGLTESPSSITLNGQNVSSFQYSNDTEELLITGLQNITSSGAFANSWNLTL Q9C102 GLT1_SCHPO ACT_SITE 69; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" BINDING 1139..1191; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 1192; /ligand="[3Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:21137"; /evidence="ECO:0000250"; BINDING 1198; /ligand="[3Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:21137"; /evidence="ECO:0000250"; BINDING 1203; /ligand="[3Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:21137"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine + NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58359; EC=1.4.1.14; Evidence={ECO:0000269|PubMed:7773104}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250|UniProtKB:Q12680}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:Q12680}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q12680}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q12680}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for glutamine {ECO:0000269|PubMed:7773104}; KM=0.07 mM for alpha-ketoglutarate {ECO:0000269|PubMed:7773104}; Vmax=0.05 umol/min/mg enzyme {ECO:0000269|PubMed:7773104}; SPAPB1E7.07; CHAIN 1..2111; /note="Glutamate synthase [NADH]"; /id="PRO_0000170789" MAVLSSVQPINHNSALVEARDEQVNTTACSDDLLNAPPYEYDTEGNPSWAGALPKAQALYDPAYEKDSCGVGFTCHIKGQVSHKIVTDARLLLCNMTHRGATGADTRDGDGAGVMTGMPYTFMQKEFGQIGCTLPKSGEYAIGNVFFSPEADVCREAMTAFTQVAEKLGLAILAWRSVPCDNSILGPAALSREPTILQPCVVLKAAYDGEAEFDTDLFERQLYVLRKQSSHLIGKEKWFYICSLHRETIVYKGQLAPVQVYNYFLDLNNAEYVSHFALVHSRFSTNTFPSWDRAQPMRLAAHNGEINTLRGNKNWMHAREGLMKSSRFGEEFASLLPIIERGGSDSAAFDNVIELLCASGVVSLPEAVMLLIPEAWQNDKNISDEKAAFYEWAACQMEPWDGPALFTFADGRYCGANLDRNGLRPCRFYLTSDDMMICASEVGTVGIEPDRIVQKGRLYPGRMLLVDTKEGRIVDDKELKHNIASRYDFRSWLDQELIDMNSIVDSLIESTSVDLTPIVDDVPLADDKTMLAFGYTLEQINMIMAPMANGGKETLGSMGNDAAIACLSDQPRLLYDYFRQLFAQVTNPPIDPIREAIVMSLQCYIGPSGNLLEINQSQCRRLRMPTPILTVEEFNALKNVDRIYPDWKVASIDITFFKSEGVAGYAAAIERICSEADTAVNEGYKAIVLSDRNVNSERVPLASIAACGAVHHYLVQNKLRSRVALVCESGDAREVHHMCTLLGYGADAVCPYLAMEALTKLVRQNAMKPGITEETAIKNFKHAINGGILKVMSKMGISTLQSYKGAQIFEALGIDNEVINKCFLGTASRIRGVTFEHIALDAFALHERGYPTDQSIRSLQIPDMGDFYYRDGGEQHVNHPKAIASLQDAVRNKNEAAYAEFSRTHYEQTRRCTLRGMLDFDFDSSQAIPIEQVEPWTEIVRRFCTGAMSYGSISMESHSSLAIAMNRLGGKSNTGEGGEDPARSQRLANGDTMRSAIKQIASGRFGVTSWYLSDADELQIKMAQGAKPGEGGELPGNKVSESIAKTRHSTAGVGLISPPPHHDIYSIEDLKQLIYDMKSANPRARVSVKLVSEVGVGIVASGVAKAKADHILVSGHDGGTGASRWTGIKYAGLPWELGVAETHQTLVLNDLRGRVVIQTDGQIRTGRDVAIACLLGAEEWGFATTPLIALGCIMMRKCHLNTCPVGIATQDPELRKKFEGQPEHVVNFFYYVAEELRGIMAKLGFRTINEMVGRSDKLKVAEPINNKSKLLDLTPLLTPAFTLRPGAATYNVRKQDHRLYTRLDNKLIDEAEVTLEEGIPSVVECEIINTDRTLGATLSNKISKRYGEEGLPTDSIRVNVFGSAGQSFGAFLAPGVTLQLEGDCNDYVGKGLSGGRLIIYPPRVSPFKPEENMIIGNVCLYGATSGHAFISGVAAERFAVRNSGAIAVVEGVGDHGCEYMTGGRVVILGSTGRNFAAGMSGGIAYVYDMQMDFAGKINTEMVDISSVTDAAEIAFLRGLIQDHRHYTGSQVADRILSDFPRHLSRFVKVLPREYKAVLEREAAKKEEAKRLQYPKAFMPGNPIRQQIEETNAQIADVEDTLGATVKKSAPLDKLRGFMKYQRRSEHYRNPLKRTNDWKELSVRLREDELRVQTARCMDCGTPFCQSDYGCPISNKIFTWNDLVFKQQWKEALTQLLLTNNFPEFTGRVCPAPCEGACTLGIIESPVGIKSVERAIIDKAWEEGWIVPRPPAERTGRRVAIIGSGPAGLAAADQLNRAGHHVVIYERADRPGGLLQYGIPNMKLDKKVVERRIQLMIDEGIEVLTNVEVGKNGDVSLDELHKVYDAVVLASGSTVPRDLPIPNRDSKGIHFAMEFLHKNTKSLLDSELKDGNYISAKGKDVIVIGGGDTGNDCLGTSVRHGAKSVRNLELLPIPPRERAFDNPWPQYPRVFRVDYGHAEVQAHYGQDFREYSILTKSFEKDEDGNVKGINTVRIEWTKNSKGRWIMKEIRNSEEFFPADLVILALGFLGPEEQATAGMNVDRDARSNISTPTKSYETSVPGIYAAGDCRRGQSLVVWGIQEGRQCAREIDLKFQGKTFLPGDGGLVKRTVNC Q9C103 EME1_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).; EC=3.1.21.10; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11719193}; MOD_RES 400; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB1E7.06c; CHAIN 1..735; /note="Crossover junction endonuclease eme1"; /id="PRO_0000086966" MTLQSTDSAIVIDSEADVDISSSQASPSKDNIALSEHNVITVLDTPQRSTQCDSLLKSFSTPLVSGSEDVLPSPRDALNITNKKSVTDNLLLSLTSSNQSTNTNLNPSSRVEIINLNSSPPNSLSSQPKHQEFHLFHTPTIPRTTQLSSKTSSPIVIPDDNEQVASPLSKKAASLTSSPLKDFQSSPPLSTVLQKSHSLHDILLDTNDDDHFPFTQSPLTKTKSFNDALTSSSSILKPCMPSIASPTSNRLSHAPSTPNLFPNQDSSNTIDLINNRSKTSVENQERTFNLTSDVHLDSPTSPSKHSSIEPNTSQEDSFQELPSLNKLSIQSRAFKKMRLPKISRTTDTPPASTSNSNKKNLDKLKKMRKLCSRSLEPYELDSNTQRKRKRYEDSLKKSKTLDKVDSLNRKMAKELDRKNSKELQKINKVKRTKEECLSEIILLSPDDWASSWYSTVRSQLDSYNCQFVVNSNQPKDSIMWKRKVNNVFNSSTNRFELSIEHEQIEPFALLRLKCRDFIKYIEEDQADTFFHEMSEKFKGCKLILLLEGIPNYFKSLKAELNRQYAAAVNSGTRPLLFGSLSKYQNFTKEKLESEIVRFSFEHSILINTSNDEKETAQWIVSFTGDIALSRYKHFSKFSARASTTEIGHVKSADRIENSLNFMLRQILRVTPNIANAICDQFDSIPSLIHHLKTHGEESLTNVVIQSSISERNLGPVLSRRIYNTFLCKEASSDAP Q9C107 MCL1_SCHPO SPAPB1E7.02c; CHAIN 1..815; /note="Minichromosome loss protein 1"; /id="PRO_0000051073" MAGNRLVPRYAHTDGLTRLAYTRDGKFLLTVGSNQVIRKFQVGSDEEPDSIDNHQDPITGIAVAENYFCTCSEDATVCVYPIDSPTEHTLLARTTLPIRDVAYSVDGNWIAIASDETAVKVVSSTDSSQIFSLRPAKASNKHVTYSPNGNFLAVSSCNGILYFYDTQTRELIKFLTNTIASLEAESEICSKAAWHPKNGTFAVASTDHFVSVISPDDWLPLYKLLPKENHSGVTDISWSSNGMYIAASFKKGGILIWDTQSHEVVVELPYSTVVALAWQPFENVLSFTTNQGILYSCPDVIPKSILKEENDPTKPLTSSKSKNRTSKELDDLFGSDDEQSQNVNDLDGNSANEENEFINHDGLDSSLDLDGDSYMVDENDLNLAKKRKQKALIDRTTTIENGSSKRRLLQASIHKPVHTGSTPWQGNRRYLCLNLVGFIWTVQQDAEHNTITVEFHDETTHRKYHFVDDQKFEMACLDHEGALYASPATESSPGVIYYKAHVDWSRKSEWAMALPMENESPVTISLSSSVVLVCTSAGYVRVFSRQGFPISIHRSKHLPFVACSSFQDTIITIANDGLSSDGNSRLVYSIEDISRDEMLQTGDGVALPPQGTLESVFFSDVGDPYIYDSTGVLLVLMHWRIPGQAKWIPVLDTNELERRKSRQESYWPVTVADNQFHCILLKGASRYPYFPRPMFTEFDFRIPCNTNNPDASTSVPVLEELQLRNKLFLTLLEDSIGDGDVTEDEKISIARLEANIDKALLQLIQKACLEERIERVYELTKTLRRTTSIAAAQKIALHHSLTNVAEKIGNLLSNV Q9C115 REC25_SCHPO MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A5.18c; CHAIN 1..150; /note="Linear element protein rec25"; /id="PRO_0000297689" MVKGSVTNTSSIVKQFEKSSIKHETETIAFAKQFINECIREFQEQKDNVVEEKNTDQNHQNQNQEGVIIEIYQELLQKVDLISSELRQNLSSLQLRFQEVERDTGHDLLNVLNSLSQEARLAQKVLEEDGSQQGSQLIQGLLTCFQSTGN Q9C1W3 ERG1_SCHPO BINDING 15..16; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534"; BINDING 35..36; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534"; BINDING 43; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534"; BINDING 114; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534"; BINDING 130; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534"; BINDING 293; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534"; BINDING 306; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q14534" CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25282, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15440, ChEBI:CHEBI:15441, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.17; Evidence={ECO:0000305|PubMed:33223513}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25283; Evidence={ECO:0000305|PubMed:33223513}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q14534}; SPBC713.12; CHAIN 1..457; /note="Squalene epoxidase erg1"; /id="PRO_0000209850" MATQDADIIIIGAGITGCALGAALGRQGRKVLVLERDMSEPDRIVGELLQPGGIEALEKIGIADAVEGIDGQWTSGYQIFYGDSNVSVPYPSKPNGGAYQGIGFHYGRFVMNLRKALTSTPNVTVTEATVNELLRDETGEVITGVVTSSKKSESPVEYKAPLTIVCDGCFSKFRKAFIDHPIQVTDHFLGLILTNPDYIAPGRGHVILSKVAPMVLYPISSTEARILINYPGKNLPPMETLKKYVLESCVPNMPEKLRPSLKAAVYNDRLRSMPNQFLPPTVNRTKGMILVGDSNNMRHPLTGGGMTVCFHDAYLLSRFISPSAVPDLLDYERILNQMNKFHWKRKGYSFVINVLSIALYKLFTPKNRYMKALESGCIDYFKRGGNCVEGPIRLLGGLDHSPSHLIGHFYAVCLYGIYQYVLSGPALLMPVRIIESLLIFLQASLVIIPYILSEMSS Q9HDV4 LID2_SCHPO MOD_RES 722; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP19A11.06; CHAIN 1..1513; /note="Lid2 complex component lid2"; /id="PRO_0000200599" MICQLLWHEHNSMGSGREKKIRKLGDNFSLPYLKFDCDHNDKNYRASNRPFGLSTGLSVQLNASNMTDPFKFLLDNWHTIFKNGAIKLLPPEGWQIPVVLDQGAFEFQSKRQCLNKGCLNYEKNYDYFKKLKAFHESRGLYFYHPPIIGNRPVDFLRLRNAISKFTNSGSSLNNEILHKVIIYLRLEDTKEVRQVLTRCYDRYIKPFERDSSPSFKSKRSESSTRKIRNTRSSAQQESPIPETSAQSPVQTIQVNGSTSLKRPLIERGEQCEYCGLDKNPETILLCDGCEAAYHTSCLDPPLTSIPKEDWYCDACKFNISDYDPRKGFKWKLSSLKERSAEIFNTLGERNSSSKLTNLTEDDIELFYWSSLAESNSGFAPLELEGLSQAYTSTIQSSLPSKEVFPLEKYSSEPWNLHNLPFENPCLFNYSFSDLSSLTITRLSIGMVFYTHGWTKSSLSTGLLHHHRFGDTVTWYVLPPDESDAFERYLISSYPQYTMEDLNRSNGLPVIVSPSSLIENGFHPIAIDLRPNEFLVVSPNSYHMGFHQGFSSFESVNFATVNWIKDGLLNSSISVLKSMRIPSSVSYEAVIISMVLSKNPCFSSEWLIKCFEDMIANESASKNEIMKLVPNIQALKLESSVPLEIRCSNCKQPCFLSFMQCHEPKKFICLGDCVKEVSLNATSWMLFYRWDVHELSNLAERFVSLIRGPEEWTNRLRSVLSTSPKPQLKVLKSLLVDAEKAMLTTPETVNLRDFVQNANSWIDSVNECLKVASLKRKKDKKPPLFKAHDHWNNTSNLKDSAVLFKVLQTSRSMAFTCQEIENMKQKAFDLLEFRNRLINSFSGPLDKNTCQRLLTEAELLGFTIPELGIIQKYLIQFEWLDMFYSFETTRTTDSDLERLITYGVSAGIPEDNDYMIFAKAMKGRAEIWENQVYDTLSKSNISYDKLSLLRDEAMNLCVNKELFSKVVGILNNAEEIKNKIATLCERSQEKDFALRPSIDEVKEALASAEKLPILSESTVTLQKMYDVVLEWIRRGKRLFGKANAPLEILGQHLDYVEKRNSASLSLNDRPGPPMEPASRETSPDSEGRLTIRKKKGCIFCFCRLPESGVMIECEICHEWYHAKCLKMSKKKLRQDEKFTCPICDYRVEIPRLSNRPKLEDLQSLYKDVKLLPFQPKETETLRKVVDLASKFRQEMQALAHNPFGLTMAEVPLARFYLRKMEGAEILLVDETNLFRQKLHECVPIAPNPPPIIGESKSTRKPRPTKRQRQIMKQVAEGLLPASAIAPPKSSNEKKSSNNVKAVEAETKSKSEKSPKKNGTNISDANNKNESHVSLMKNWKLGSPAFVTLVKEKNSSCLCGEEFSPRDSFIDCTICERRFHYDCVGLNNEIADSVSKFTCPICMEQSGGIYPWQLRPRNGMHPDHISGFSKEVETDPKLGSSGYTLNNSKFDKAAVSKTLSAQDVSRLQKVSCGEHLYFGTDVFTPLGDMATSASMFSLDDSSEKTDAFTENFLNV Q9HDY0 YPT71_SCHPO BINDING 17..23; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 33..40; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 66; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 124..127; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939"; BINDING 158..160; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32939" MOD_RES 208; /note="Cysteine methyl ester"; /evidence="ECO:0000250|UniProtKB:P36586" SPAPB1A10.10c; CHAIN 1..208; /note="Ypt/Rab-type GTPase ypt71"; /id="PRO_0000121314" LIPID 206; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P36586"; LIPID 208; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P36586" MSAQKRVFLKVVILGDSGVGKTCLMNQFVNQKFSREYKATIGADFLTKDVVVDDKLVTLQLWDTAGQERFQSLGMAFYRGADCCVIVYNVNNSKSFDSVENWRQEFLYQTSQDECAFPFIIVGNQIDKDASKRAVSLHRALDYCKSKHGSNMIHFEASAKENTNVTDLFETVSRLALENESSRDDFVNDFSEPLLLSKPLNNTSSCNC Q9HDY1 ASE1_SCHPO MOD_RES 537; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB1A10.09; CHAIN 1..731; /note="Anaphase spindle elongation protein 1"; /id="PRO_0000363368" MQTVMMDDIQSTDSIAEKDNHSNNESNFTWKAFREQVEKHFSKIERLHQVLGTDGDNSSLFELFTTAMNAQLHEMEQCQKKLEDDCQQRIDSIRFLVSSLKLTDDTSSLKIESPLIQCLNRLSMVEGQYMAQYDQKLSTIKEMYHKLESYCNRLGSPFVLPDFENSFLSDVSDAFTESLRGRINEAEKEIDARLEVINSFEEEILGLWSELGVEPADVPQYEQLLESHTNRPNDVYVTQELIDQLCKQKEVFSAEKEKRSDHLKSIQSEVSNLWNKLQVSPNEQSQFGDSSNINQENISLWETELEKLHQLKKEHLPIFLEDCRQQILQLWDSLFYSEEQRKSFTPMYEDIITEQVLTAHENYIKQLEAEVSANKSFLSLINRYASLIEGKKELEASSNDASRLTQRGRRDPGLLLREEKIRKRLSRELPKVQSLLIPEITAWEERNGRTFLFYDEPLLKICQEATQPKSLYRSASAAANRPKTATTTDSVNRTPSQRGRVAVPSTPSVRSASRAMTSPRTPLPRVKNTQNPSRSISAEPPSATSTANRRHPTANRIDINARLNSASRSRSANMIRQGANGSDSNMSSSPVSGNSNTPFNKFPNSVSRNTHFESKSPHPNYSRTPHETYSKASSKNVPLSPPKQRVVNEHALNIMSEKLQRTNLKEQTPEMDIENSSQNLPFSPMKISPIRASPVKTIPSSPSPTTNIFSAPLNNITNCTPMEDEWGEEGF Q9HDZ6 DAM1_SCHPO PTM: Phosphorylated by plo1 at Ser-143 during prometaphase and metaphase to promote chromosome biorientation (PubMed:22375062). Dephosphorylated in anaphase (PubMed:22375062). {ECO:0000269|PubMed:22375062}. MOD_RES 143; /note="Phosphoserine; by plo1"; /evidence="ECO:0000269|PubMed:22375062" SPAC589.08c; CHAIN 1..155; /note="DASH complex subunit dam1"; /id="PRO_0000127661" MEKYQKATQNPLENVDNVKIESENAIPSNLQAFTKSLAVLDDNVSEFRKRMNHLSATKQILDNFNESFSSFLYGLQINAFCVDYENAPLSESFLLQAKKDQFKATLMTRTGHSISDPPYDGGVISHDPNFATADETFATNDTSFIERPETYSASR Q9HDZ7 ATG18_SCHPO SPAC589.07c; CHAIN 1..373; /note="Autophagy-related protein 18"; /id="PRO_0000050872" MHFFVRKYRGKAALLSIGTFDGYKIYNCDPFGKCFHKIQGATSIVEMLFSTSLVALVEKDDGNNRKLKLINTKKSTTICELTFPTPLLAVKLNRKRLLAVLEEQIYVYDISNMLLLHTIETTSNVFAVCALSPNSENCYLAYPDSRDHEPRTEGESSSPNVSNSAVSGQVILWDVINCKQITKIEAHKDSLACLAFNSDGTMLATASDNGRIIRVFAIPSGQRLYQFRRGSLPAQIYSIAFHPDSSLLTVTSSTQTVHIFRLKEVYSNLERQGLLPSSPPPKESLLRRSSRSLIGTVGGYLPQSVSGMLDPERDFAYAHIPGDKVTSIAAFGPDNTIVNVATYDGNLYSFRVNLRTGGECAMVNHFCVGLTAA Q9HFE5 AP1M1_SCHPO SPBP16F5.07; CHAIN 1..426; /note="AP-1 complex subunit mu-1"; /id="PRO_0000193777" MASAIFVLNLKGKVIISRDYRADIPMSVVEKFLPLKSEVEEEQGFSTPCLTHEGINYIYIHHNDVYLLALSKMNSDAMEMLVFLRKMADVFIDYFKELQEESIRDNFVLVYELLDEIMDFGFPQTTETKILQEYITQTSNTVKKHAPPPIAMTNAISWRSEGIHYRKNEVFLDVIESVNLIAAADGTVIQSEILGKVRLKCYLSGMPELRLGLNDKVLFEAAGRTIKGNTVEMEDVKFHQCVRLARFENDRTISFIPPDGEFDLMSYRMSSNVRPLIWVECESIVHSGSRIEFMVKAKAQFKKRCIANNVQIIIPVPEDADSPRFQTSNGHVQYAPEQAAMVWNIKKFAGGKEFFMRAEMGLPSVKNEDIQVQKKRPVQLKFAIPYFTTSGIQVRYLKITEPKLNYHAMPWVRYVTQNGTEYSIRQ Q9HFF5 PDS5_SCHPO SPAC110.02; CHAIN 1..1205; /note="Sister chromatid cohesion protein pds5"; /id="PRO_0000058279" MIKLQFQRNIVPTHDNPLTTSEILKRLRDLLGELTSLSQDTIDRDSVLPVARSLVNNNLLHHKDKGIRSYTLCCIVELLRLCAPDAPFTLSQLEDIFQVILKILSGLMNQESTYYPQIYEILESLSNVKSAVLIVDLPNAEEFLVNIFRLFFDLARKGTTKNVEFYMLDIINQLINEINTIPAAALNILFAQLISGKGVRQTIGSSDSTNHGPAFQLARNIFHDSADRLQRYVCQYFSDIIFDSRDSLSDSMTTPEFIFSHNLVLQLWKYAPTTLLNIIPQFENELQAEQTSVRLVAIETVGLMLQDNAIWSDYPRVWSAFCGRLNDKSVACRIKCIEVASNALQNSLATSEIIENVVQMLQSKLADTDEKVRVATLKTIEQLTFETFKMQFSVQALKLMGDRLRDRKLNVRLQAIRTLSQIYNRAYQDLIDGVEYSIQMFSWIPSSLLEVFYVNDETTNAAVEICMAELVLQYLSSDTQTRLNRLFLSIKYFSEKAMRVFILLLQRQVKYSELLNYYIECCKNYNGGVMDNDEESITNKLKKVIDIISSKSSNPTLTEATFRKFAELNDRQSYKMLLQTFSIKSEYQVVLKSIKYLFKRVSETLSTASLECFRIFVYRSALFAFNKSNVHEIIQLLNEPVKYHNFLKPSEALLQHLPLIHPNIYGEVVIEVENIIVSSGIESDPKVIKALSQFSKRKKNFSIQTTTAEILRKLCLHGTQEQAKQAATIIAITETKEFKLDMITNIVENLEYNGGLPVRLMTLGQLFLYTLEEVEKVADQVTEFLVKKVIQRFPEKYDDTHNDEEWCTYEKLDNLTMCKVLAIRVLVNRLRAAAGGTEALNIGAPIIKLLKVLLMADGELSPFKNTPKISRAYLRLTASKYFLKLCSIPFYAEHIDFSSYVQISLLCQDENFDVRNLFLTKLQKQLQLKKLPISYYPLLFLTAVDPEEEIKTKASIWIRSQVAFFQKTHDFTMEYVATYLIHLLSHHPDISSIESENSLDFIAYIRFYVDTVVNSENVPIVFHLMQRIKQSYDVIEDGNNYIYVLSDMAQKILQVKSQNFGWSLTTYPKQIKLPYEILRPIPSIDEKKRIFNKIFITPKMESQIEHAIRTPVSSFAKQTTNKHANLKQKKTHSSKSDKKSSRRRKNEKRRKLNEQNPNIRNVPERSSSRFQGIRINYSEAPSSSEEISEEEEEISEEDFDEIEDL Q9HGK2 HOP2_SCHPO SPAC222.15; CHAIN 1..216; /note="Homologous-pairing protein 2"; /id="PRO_0000096447" MAKAKEVKAKPIKGEEAEKLVYEYLRKTNRPYSATDVSANLKNVVSKQVAQKALEQLRDTGLIHGKLYGKQSVFVCLQDDLAAATPEELAEMEKQIQELKDEVSVVKTLYKEKCIELQALNNSLSPAEIREKIQSIDKEIEETSSKLESLRNGTVKQISKEAMQKTDKNYDFAKKGFSNRKKMFYDLWHLITDSLENPKQLWEKLGFETEGPIDLN Q9HGK9 CENPT_SCHPO SPBC800.13; CHAIN 1..479; /note="Inner kinetochore subunit cnp20"; /id="PRO_0000310364" MASHNYETPLKSSSFQHLVGTLSQRRHFTPSRSRYTPRSAQRTVTPHKRRALARRNSLARRRSNVFSATTPRDILRMLSRALAKNPVPSPAESESSERRHTPQTNSQKSQKTPRLSSNKRRTLKNDAKQRNSQSPGTDTSDANLTIQSIEAPRRAPQRLSDFFTPDGRRVSNIRDSLISEKRLENNIDQVQESALSTASSNRLIDLKNDEVPIFRIPLSDYETDDMDDGTPLQRHVATLNQYQSPIFNLGPDILEDEPSYSSRASRSRQSSLSSRLSELPSKRASLEILRRENTFPADPIQEFGEKAYNERELMEEISNFEPLLDDNLLENANEAVNSPVVDAPMDADSALEIPNDEDNGEILNKLKDSPFKKPKRRYSKSSTLVLPETNIRKLANSYSQKKIAGSVIEELTTASELFFKQIANDLSAFADHAHRKTIDTQDVVLLMKRQRKISEKKSLSSLMQQYLSREIAPPAIKRT Q9HGM8 KU80_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPBC543.03c; CHAIN 1..695; /note="ATP-dependent DNA helicase II subunit 2"; /id="PRO_0000255456" MSDKECTVFVLDLGKDMGTCHHGRSHSDLEWTLSYFHDELSHKFLANRKTDVVGIVGYKCDDTKNDLAEQEAYWNISVLYPIQTALFSKLQSVSQTLKPSNTMQGDLISAIVVSFDLMARHCKKNKWKKKMIVLTAARGIIDFSDYIGIAEQLLQHDVFLGVYGVDFDQEDINYSEPLKESQKKENEVRIQEFVESCHGQYCTFQQIYNNIGKPWVRKVRPVAIFRGTFSIGNRDSKDTSISIQVERYPRTRLTKPPTSSAFYENDMSKNYECLNIENSNVENKSMESDAVSTVRSYMVRDPKTNDSFEVKREDLESGYSYGRTIVPISRSDEDVLALDTIPGYEILGFIPKSSLPIYYTISDTNIIVPKDDFESKLNFSAFVQSLEREHRYALARFVSKDKGVPVLLVLMPYVEFKRHYLVDIQLPFAEDVRPYSFSEFEKLSNEEDMRQIDFAVSNYIDNMDLDSSDCGFNPPFEPENTFSMIPHRLQQAISYYANSPEGDLPQPNIYLTRYTNPPKSLLDNCILDLKLIKEKLTVNVPVKPKYSSQETAFDTGAPISEEQIEELLNSGLDEQEGEKLLVLHVSEKDPVGTFTEVLKNPFGLEDALTEMEKVIKNLIDKSKYDLALQSLQSLRLHSILEDEVERFNEYLTRLKKDVMQNNKPKENELINKIRSSGLDIILHDELTRHDNFNNI Q9HGN1 GCN2_SCHPO ACT_SITE 772; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 562..570; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 585; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P15442}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P15442}; PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P15442}. SPBC36B7.09; CHAIN 1..1576; /note="eIF-2-alpha kinase GCN2"; /id="PRO_0000085962" MDAAKRLELCKEIQENEIEALKAIFMDDFEELKVRNAWNVTNGHVYCIHLCSRSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLNDWQSDLSSQFASLEEERAVQLKHDRERAEVDLQLRLKREKDALFEEEQTLQNKIQDELQRRSYETPQSSSKKKTNSKETTSLETLPTSIYFDCSISVRDCHDSLVTFNRVLPLYTISHSNLSTLTLVKPESKEISLQDCVFLLRTVRISTPYWSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGYGWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDMNASHPFNINSQSITNILPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSHVIRLGTAVLPPVEQGTFSKSARPSYGGQQDGIIDLLYRKSVSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEANDTVTEIISSDSESLSQSLNMAVDFRQSSSLPADKLSSLDIHFEDDYNSSADEEDPEASDISFQYSNTSDKEGSSDKDSSIEEASSVKTQENGLNATLYIQMEYCEKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESEAIPPKVGEEFIQEGLRLLSNPNTPYYLKLLKVLFGQVPDRHKDFTYDFNLSEESGVLSKVSDRGWDSLLACLVRDHVVKVFRRHGAKERESHILFPKSSQYDKDQASVSLLDKNGTLLQLPYDTVLPYARNVARNAVEEEKTYLISDVFREAKGGGRPKAIKEISFDITTNSDNLDWYDAETIKALDEVLTEIPSLTESCILINHADILSSILDYLQVSKDKRRMATHILGQINQRLTLSQVRNQLRIESLVPSTTLDDLSLFDFRENYEEGASKLRKIFGKEMPQKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGGLMFQAINLAEKSELICAGGRYDKLVRFFDPPLMRTARKKHVVGICFALEKLVFSMLRYIRFHNSKQSSKHSPSPTLKSVGPWAPRRVDVLVTSIGKDSILEKCSLLQELWALNIQADIVLRGASSLEEIVTHYRSEGINWVLVVRQKNTQMEHSVKARNILKNEDDEIRFDEVGMWLLGEINERKRNESMLQSKRILDSAQQDVAKFVDTSQSNLDVQLISLKDVNDRKYKWKHKQNAMNKVYDLVQSAIRESSEDAIALAVDCDSEAMEKLRSTTTLDEESWKRLIESCPASQREYMQRLQKKLVTLAEQDKKRVWICSFRTNEIYLYGLK Q9HGN6 DUS1_SCHPO ACT_SITE 109; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" BINDING 24..26; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 80; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 148; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 176; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 211..213; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 235..236; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH + uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543, Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88; Evidence={ECO:0000305|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378; Evidence={ECO:0000305|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH + uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543, Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88; Evidence={ECO:0000305|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382; Evidence={ECO:0000305|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH + uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541, Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88; Evidence={ECO:0000250|UniProtKB:P53759}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374; Evidence={ECO:0000250|UniProtKB:P53759}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH + uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541, Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88; Evidence={ECO:0000250|UniProtKB:P53759}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370; Evidence={ECO:0000250|UniProtKB:P53759}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853; Evidence={ECO:0000269|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857; Evidence={ECO:0000269|PubMed:34798057}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q5SMC7}; SPBC36B7.04; CHAIN 1..399; /note="tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]"; /id="PRO_0000316225" MASKKLHGRDFYNKIGRPKRILAPMVDQSELPWRILARRSGADLCYSPMFHSRLFGESEDYRNKVFSTRTIPEERPLIIQFCGNDPEIMLKAAKIAAPYCDAVDVNLGCPQGIAKKGKYGSFLQENWNLIESIITKLHTELSIPVTAKIRIFPDPQKTLDYAKMILKAGASILAVHGRLREQKGHFTGIADWEQIQMLRKNLPSETVLFANGNILHAQDIDRCIKYTGVDGVLSAEGSLYNPRIFLPPSSPLMTLYPRIDDMCEEYLNIIREFKLESDYSSLSAIKGHLFKLMRPLLSIHTDIRSKLAQGCTPRDFETFPPVVAMLRKRLLECEEKGEINEDKDVKESVKDSMGYPVIPWWRVQPYIRPLEVPLVTKRKPVEVTADEGPVKKKVNASVA Q9HGP5 CAPZB_SCHPO SPAC631.01c; CHAIN 1..268; /note="F-actin-capping protein subunit beta"; /id="PRO_0000204641" MNSEDAALDLLRRLNPKDISKNLDTILSVAPDLADVLLSSVDQPLKVNTCSESGNQYLLCDFNRDGDSYRSPWSNKYDPPLEDGLVSTDRVRKLEVSLNEAIRVYLDLYYEGGVSSVYLWDQDDSYAGAVLIKKASTSNSSGWDSIHVFECLPTTETNVYDYRLTSTIILFLSSGSEEQSALPSKALNLSGHLTRQTSQRLPAADDDTEIANVGKLVEEMETRMRNFLQDVYFGKTKDIINQTRSIQPVSDAQPNDSALRSVLNDLSI Q9HGQ2 TRM4A_SCHPO ACT_SITE 309; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" BINDING 167..173; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 203; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 230; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 256; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" CATALYTIC ACTIVITY: Reaction=cytidine(48) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(48) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54136, Rhea:RHEA-COMP:13806, Rhea:RHEA-COMP:13807, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192, ECO:0000305|PubMed:30646830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54137; Evidence={ECO:0000269|PubMed:23074192, ECO:0000269|PubMed:30646830}; CATALYTIC ACTIVITY: Reaction=cytidine(34) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(34) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42940, Rhea:RHEA-COMP:10291, Rhea:RHEA-COMP:10295, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.203; Evidence={ECO:0000305|PubMed:30646830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42941; Evidence={ECO:0000269|PubMed:30646830}; CATALYTIC ACTIVITY: Reaction=cytidine(60) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(60) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51160, Rhea:RHEA-COMP:12902, Rhea:RHEA-COMP:12905, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51161; Evidence={ECO:0000269|PubMed:23074192}; CATALYTIC ACTIVITY: Reaction=cytidine(61) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(61) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51164, Rhea:RHEA-COMP:12903, Rhea:RHEA-COMP:12906, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51165; Evidence={ECO:0000269|PubMed:23074192}; CATALYTIC ACTIVITY: Reaction=cytidine(62) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(62) in tRNA(Asp) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51172, Rhea:RHEA-COMP:12904, Rhea:RHEA-COMP:12907, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:23074192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51173; Evidence={ECO:0000269|PubMed:23074192}; MOD_RES 54; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17D4.04; CHAIN 1..688; /note="Multisite-specific tRNA:(cytosine-C(5))-methyltransferase trm4a"; /id="PRO_0000211824" MGRKHYSSKKNRSKKGEFVNWDLIERKNENFEKYYRLQKLVTEDDFILLKQKLTEQLPTTFRITASIPHATQVRDYFIEHYYPLIENARTEDAKIPLPVSLPWYPDGMAFMLDISKEVIRKSPHLKALQEFLVLETEAGDINRQESVSMVPPLLLNVESHHKVLDMCAAPGSKTAQLLEALHKPTKKEDITTLLPSGIVIANDSDNKRAHMLVHQIKRLNSPNVLIVNHDASFLPNFHLSSPDGKKFLKFDRILADVPCSGDGTFRKNIALWNEWSLKTALGLHATQIKILMRGLQLLEKGGRLVYSTCSLNPIENEAVVSAVLNATRGSVRLVDVSSELPQLKRSQGVDNWVVCDSDLNIYPSFDTLPKELYEKMPPTLWPLPKKELAELNIQNCLRIYPHFQNTGGFFVAVLEKYENLTSSMKTAVDDNKVFLREQKLPSEQASKKRKQDTQETSSDSKLAEVKPKGKNGGNRFHELDPFVYIKEDDQALEKIYKKFGIDEAIIKKNQFFVRNVNGVPTKAIYISNDLFRNVIENNRNRVKFVHGGLKIFVRQDFGSLSREIAEKNGTCVFRVQSDGANLASHFIAESCLFHTTLSDLFILLDHEAVTIDDFPEDSLFRKEYNHLDLGSTLLHVDLAKEESVIKKQVYIPLWKSVRICNVLLSNSEKRTLKLQIEGPQSSIHKHNT Q9P371 SST2_SCHPO BINDING 341; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 343; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 354; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 356; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 397; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 404; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 406; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; MOD_RES 192; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19B12.10; STRAND 263..266; /evidence="ECO:0007829|PDB:4JXE"; STRAND 288..296; /evidence="ECO:0007829|PDB:4JXE"; STRAND 299..307; /evidence="ECO:0007829|PDB:4JXE"; STRAND 309..312; /evidence="ECO:0007829|PDB:4K1R"; STRAND 317..320; /evidence="ECO:0007829|PDB:4K1R"; STRAND 335..342; /evidence="ECO:0007829|PDB:4JXE"; STRAND 344..346; /evidence="ECO:0007829|PDB:4JXE"; STRAND 369..374; /evidence="ECO:0007829|PDB:4JXE"; STRAND 379..385; /evidence="ECO:0007829|PDB:4JXE"; STRAND 401..403; /evidence="ECO:0007829|PDB:4K1R"; STRAND 411..413; /evidence="ECO:0007829|PDB:4JXE"; STRAND 420..423; /evidence="ECO:0007829|PDB:4JXE"; STRAND 428..431; /evidence="ECO:0007829|PDB:4JXE" HELIX 269..282; /evidence="ECO:0007829|PDB:4JXE"; HELIX 323..331; /evidence="ECO:0007829|PDB:4JXE"; HELIX 352..364; /evidence="ECO:0007829|PDB:4JXE"; HELIX 389..396; /evidence="ECO:0007829|PDB:4JXE" TURN 375..378; /evidence="ECO:0007829|PDB:4JXE"; TURN 416..419; /evidence="ECO:0007829|PDB:4JXE" CHAIN 1..435; /note="AMSH-like protease sst2"; /id="PRO_0000358323" MNILQGSEAPLSYEEIASRAGAFDFNKNIPLKNWLRTSTTISKQAHVYVSEHDYSNGVFLLFRYCELFMKCQKHPDAAAYKKELFDYYQGVRNALEEIELIKPIVKEQYEQYQCQKNDLDDLKKLSMKDSQPSLEKPVSYVDEPILEQWALSDLQILPPSSTDLLSPDSQKLSKSSSDLPQFDYPSLNSSPTFNSNLPISSSRFEKTSLSDSKLVSPEPLDDNKDIQFIKKPIYTRTSEPRPKPAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTHCSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPGHVREINSKLQVVDLRVK Q9P373 ATG4_SCHPO ACT_SITE 74; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q9Y4P1"; ACT_SITE 232; /evidence="ECO:0000250|UniProtKB:Q9Y4P1"; ACT_SITE 234; /evidence="ECO:0000250|UniProtKB:Q9Y4P1" CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:P53867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549; Evidence={ECO:0000250|UniProtKB:P53867}; SPAC19B12.08; CHAIN 1..320; /note="Probable cysteine protease atg4"; /id="PRO_0000215868" MELMARFLERYLHFAPTNTEPPGTLIWFLGHSYKIEDSQWPEKFLYDSFSLITITYRSGIEGLENMTSDTGWGCMIRSTQTLLANCLRICYPEKQLKEILALFADEPSAPFSIHQFVTMGKTLCDINPGQWFGPTTSCSCVARLSDQNPDVPLHVYVARNGNAIYRDQLSKVSFPVLLLIPTRLGIDSINESYYDQLLQVFEIRSFVGITGGRPRSAHYFYARQNQYFFYLDPHCTHFAHTTTQPASEETFHSATLRRVAIQDLDPCMIFGFLIRDEEEWHSFEANQKYFADIVQIFDSEPQPVETHDDFVLDENVEDHL Q9P376 FCP1_SCHPO ACT_SITE 170; /evidence="ECO:0000269|PubMed:11934898"; ACT_SITE 172; /evidence="ECO:0000269|PubMed:11934898" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11934898}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11934898}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11934898}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11934898}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:11934898}; SPAC19B12.05c; STRAND 165..169; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 175..179; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 203..209; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 214..222; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 237..242; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 293..298; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 309..311; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 495..502; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 526..530; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 533..538; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 540..542; /evidence="ECO:0007829|PDB:4XQ0"; STRAND 555..557; /evidence="ECO:0007829|PDB:4XPZ"; STRAND 578..580; /evidence="ECO:0007829|PDB:3EF1" HELIX 151..162; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 183..188; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 197..199; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 226..234; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 247..257; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 282..284; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 301..303; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 398..415; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 417..427; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 434..436; /evidence="ECO:0007829|PDB:3EF0"; HELIX 445..470; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 479..488; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 512..519; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 543..551; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 559..568; /evidence="ECO:0007829|PDB:4XPZ"; HELIX 574..577; /evidence="ECO:0007829|PDB:4XPZ" TURN 172..174; /evidence="ECO:0007829|PDB:4XPZ"; TURN 194..196; /evidence="ECO:0007829|PDB:4XPZ"; TURN 210..213; /evidence="ECO:0007829|PDB:4XPZ"; TURN 262..266; /evidence="ECO:0007829|PDB:4XPZ"; TURN 271..273; /evidence="ECO:0007829|PDB:4XPZ"; TURN 327..329; /evidence="ECO:0007829|PDB:4XPZ"; TURN 471..473; /evidence="ECO:0007829|PDB:4XPZ"; TURN 508..510; /evidence="ECO:0007829|PDB:3EF0" CHAIN 1..723; /note="RNA polymerase II subunit A C-terminal domain phosphatase"; /id="PRO_0000212567" MSKRLTPIHLPNSLNYPIEIASCLVPQGSYVKKGTPLLLYRFFTKVKEDQEDGSEVYVDREFVEQFECPVEGELVEWAVKKEESIENFSKIVAKLHEPCTHEVNYGGLCAICGKNITSQDYMGYSDMARANISMTHNTGDLTVSLEEASRLESENVKRLRQEKRLSLIVDLDQTIIHATVDPTVGEWMSDPGNVNYDVLRDVRSFNLQEGPSGYTSCYYIKFRPGLAQFLQKISELYELHIYTMGTKAYAKEVAKIIDPTGKLFQDRVLSRDDSGSLAQKSLRRLFPCDTSMVVVIDDRGDVWDWNPNLIKVVPYEFFVGIGDINSNFLAKSTPLPEQEQLIPLEIPKDEPDSVDEINEENEETPEYDSSNSSYAQDSSTIPEKTLLKDTFLQNREALEEQNKERVTALELQKSERPLAKQQNALLEDEGKPTPSHTLLHNRDHELERLEKVLKDIHAVYYEEENDISSRSGNHKHANVGLIIPKMKQKVLKGCRLLFSGVIPLGVDVLSSDIAKWAMSFGAEVVLDFSVPPTHLIAAKIRTEKVKKAVSMGNIKVVKLNWLTESLSQWKRLPESDYLLYPSYDLPDRNLSEHSYSSSSDDEQRISELNDRELDEIDWQAADQDVENALKDLSDDNDFDTGSISASQSQPEALEVNTPIKRKADLIQPSYNYDGEKRRKENDNHEGYDLLPNSSTKGEESAENENELDDLADIMEAELSKDTA Q9P377 FKS3_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000250|UniProtKB:P38631}; MOD_RES 885; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19B12.03; CHAIN 1..1826; /note="1,3-beta-glucan synthase component bgs3"; /id="PRO_0000121723" MDYKKGEHSPSSSIQILSDDATINSNYAYGEQLQSNDQYNNIQHPAPSFANPFIHEQDDSYSDILEEEPDEDAYDSPERPSSTEEFISQDESNISAGSSFMFPYNRGHPLSKRHDSIMVDEFGHEYIVEGDSIASADEAIDYDALYASWTAETKAPILAIDIENIYIELAMKFGFQWDNMRNMFDYLMVMLDSRASRMTPQEALLTLHADYIGGPQSNFKKWYFACKMDQFDLKSGVLSFISRDPSTQVPYKDMSSCEALWISRMDELSNYERIEQLALYLLCWGEANNVRFMPECLCFIYKVAYDYLISPSFKEQKNPAPKDYFLDNCITPLYNLMHDQQYEIRDQKYVRKEKDHASIIGYDDINQMFWYSKGLKALLLSDGSRIMDADVASRYFLLADIQWQRVCYKSFRESRTWLHFLHNFSRIWILHISVFWYFTVYNSPTIYTPNFHYLEGTQPARAAKWCAPALAGAVASFISFLALILEAYFVPRNNPGAQPVIPRLIFVSILIALNIVPAAFIFGFSNATQQHYRSREIVGYVHFFFSIGCVAYQSFIPLPFLLGPRFKFRSSSRKYLANSYFTNDIASLPWGRTLLSAALWITVFIAKFVESYYFLTLSVRDPIRFLQRMKPYDCYDFMIGASLCSHQPKFLLSLVYLTDLVLFFLDTYLWYMLISTMFSIAYSFYMGSAIWTPWRVIFSNLPRRIYFTLLAYKDLSTEFKPKIYVGQIWNSIMISMYREHLLSLEHLKGLLYQQVGSEYFGKQTFQSPKFFMEAAKGLNKWDAFFRRNSEAERRISFFAQSLGGKIPDAVPVPKMPSFTVLIPHYGEKILLSLREIIREQDPMSRITLLEYLKQLYPNDWDNFVQDTKLMAGDVGVEETKSDVKSEKGKKQGTVKEDLPFYCIGFKSTAPEYTLRTRIWASLRSQTLYRTASGMMNYSRALKLLYRVEQPNLLDDCDGNFERLEHQLEQMAYRKFRLCISMQRYAKFNRDEYENAEFLLRAHPELQIAYLDQDPSEDGEEPKVYATLINGFCPFENGRRLPKYRIRLSGNPILGDGKADNQNMALPFVRGEYLQLIDANQDNYIEECMKIRNVLSEFEEMDCATLTPYTKKGNARHPVAMLGAREYVFSENSGILGDVAAGKEQTFGTLFSRSLALIGGKLHYGHPDFLNTIFMTTRGGVSKAQKGLHVNEDIYAGMTALQRGGRIKHCDYFQCGKGRDLGFGTIINFTTKIGTGMGEQSLSREYFYLGTQLPFFRMLSFYYAHAGFHLNNVFIMISMQLLMLVFVNLGAMYHTVEICDYQAGAAINASLYPPGCYMLKPVLDWIRRCIISIFIVFFISFLPLVVHDLLEKGVIRAVARLCKQIFSLSPMFEVFVTQNYANSIFTNLTYGGARYIATGRGLATTRVPFSVLYSLYTGSSIYLGSRLIMMLLFGTMTVWTTHYVYFWVTMFALVICPFIYNPHQFSFVDFFVDYREFLRWLSRGNTKGHAHSWIGFCRLARTRITGVNRKVKGSPSNKLTMDMPRAGLRNVIFTEVFLPACFAFFTICAYTFMNSQPGLEDKSRAVNGFIRIWIMAALPIAISTAALLILLMFSCMLGPLLRKCSKRYGAVLAALAHAVSVFGLVFTFEALWFLEAWSFSKTVLGCIVIFAIHRLVFKLVVVFLLPREVASGENNYSWWDGHWFGRKGIPYMPIQFIREFMCKVVEMNLFAMDFILSHCILFSLTPILCIPFIDIPHSVLLFWLHPSRQIRPPIYTRKQNQLRRRTFYRYSLLFFALLCTFVAMIVVPLVLDQKLSYQFKFENSVKFFRLMQPSLGVLPNTNKNTSE Q9P378 GAS1_SCHPO ACT_SITE 157; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 258; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 88; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 156; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 157; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 198; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 203; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 290; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135" SIGNAL 1..19; /evidence="ECO:0000255" PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. SPAC19B12.02c; PROPEP 517..542; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000377426" CHAIN 20..516; /note="1,3-beta-glucanosyltransferase gas1"; /id="PRO_0000010491" CARBOHYD 35; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 91; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 249; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 279; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 406; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 484; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 502; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 509; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 70..99; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 212..345; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 230..261; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 367..419; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 376..439; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 395..400; /evidence="ECO:0000250|UniProtKB:Q06135" LIPID 516; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MKFSILSLAVAGLVGLAKASVSPVHVDGRYFFYENGTRFFLKGIAYQPNVDDSDTEGTLFVDPLSDGDACSRDVPYFQELSVNAIRVYAVNASLDHSACMQAFQDAGIYVLSDLAQPYEAISSSDPTWTVDLFSRYTEVVDSLAPYDNMLGFIAGNEVIQNNTNTNAAAFVKAAVRDVKSYIKSSGYRQIPVGYSTNDEEVTRDPMAYYFDCGDDDDHVDFYGINIYEWCGDSDFVSSGYQERTEEFSNMTVPMIFSEFGCIEVRPRTFSEIVALFSDNMTDVWSGGIAYQYFESENEYGVVTVSGDSVSTLTDFPYLSSRYASVIPSASYESTMSATLTATMSCQATNSAWMAATSLPPTPSEAVCECMDSTRSCVINDDVSSDDYSDLFSYVCNEISCDGITANGTYPGQYGSYSYCDAKQQLDYVLDAYYSAKGDCDFSGSATLVSASSATGTCASYLSAAGSSATNAISLTADSNAVSRNSSASTMSTSYTSGSGSSNSSGSSSNSSSKSSSGASSYNLNMVITFLSVVIGGTAVLFI Q9P380 PTR2_SCHPO MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 23; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 25; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 33; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 35; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 44; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 45; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 53; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 54; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 594; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 618; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC13A2.04c; CHAIN 1..618; /note="Probable peptide transporter ptr2"; /id="PRO_0000064319" MSSIEEQITKSDSDFIISEDQSYLSKEKKADGSATINTADEQSSTDELQKSMSTGVLVNGDLYPSPTEEELATLPRVCGTIPWKAFIIIIVELCERFAYYGLTVPFQNYMQFGPKDATPGALNLGESGADGLSNFFTFWCYVTPVGAALIADQFLGRYNTIVCSAVIYFIGILILTCTAIPSVIDAGKSMGGFVVSLIIIGLGTGGIKSNVSPLMAEQLPKIPPYVKTKKNGSKVIVDPVVTTSRAYMIFYWSINVGSLSVLATTSLESTKGFVYAYLLPLCVFVIPLIILAVSKRFYKHTPPSGSIFVRVGQVFFLAAQNKFNLEKTKPSCTTTVGRVTLKDQWDDLFIDELKRALRACKTFLFYPIYWVCYGQMTNNLISQAGQMQTGNVSNDLFQAFDSIALIIFIPICDNIIYPLLRKYNIPFKPILRITLGFMFATASMIYAAVLQAKIYQRGPCYANFTDTCVSNDISVWIQIPAYVLIAFSEIFASITGLEFAFTKAPPSMKSIITALFLFTNAFGAILSICISSTAVNPKLTWMYTGIAVTAFIAGIMFWVCFHHYDAMEDEQNQLEFKRNDALTKKDVEKEVHDSYSMADESQYNLEKATAEEEIMKST Q9P3A7 CDC48_SCHPO BINDING 267..273; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P55072"; BINDING 368; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P55072"; BINDING 404; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P55072"; BINDING 541..546; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q01853" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; Evidence={ECO:0000250|UniProtKB:P25694}; SPAC1565.08; CHAIN 1..815; /note="Cell division cycle protein 48"; /id="PRO_0000084586" MNAPSTMTDKKPEVEHLQGENPPKDTYSAEDTATAILRKKRKPNSLVVDDATNDDNSVITLSSNTMETLQLFRGDTVVVKGKRRKDTVLIVLTDEEMEDGVARINRVVRNNLRVRLGDIVTINPCPDIKYAERISVLPLADTVEGLTGSLFDVYLKPYFVEAYRPIRKGDLFVVRGSMRQVEFKVVDVAPDEFGIVSQDTIIHWEGEPINREDEESSLAEVGYDDIGGCRRQMAQIRELVELPLRHPQLFKSIGIKPPRGILMYGPPGTGKTLMARAVANETGAFFFLINGPEIMSKMAGESESNLRKAFEEAEKNSPAIIFIDEIDSIAPKREKTNGEVERRVVSQLLTLMDGMKARSNVVVMAATNRPNSIDPALRRFGRFDREVDVGIPDPTGRLEILRIHTKNMKLADDVDLEQIAAETHGYVGSDLASLCSEAAMQQIREKMDMIDLDEDEIDAEVLDSLGVTMDNFRFALGSSNPSALRETVVEVPNVRWEDIGGLEEVKRELRETVQMPVMYAEKFLRFGVTPSKGVLFFGPPGTGKTLLAKAIANECSANFISVKGPELLSMWFGESESNVRDIFDKARAAAPCVVFLDELDSIAKARGASAGDSGGGDRVVNQLLTEMDGVNSKKNVFVIGATNRPDQIDPALMRPGRLDQLIYVPLPDEEARFSILQTQLRHTPVAEDVDLRAVAKATHGFSGADLEFVVQRAVKLAIKDSIEEDIKRENETGEAPADDVVMDEDASVSQVQRHHVEEAMKMARRSVSDAEVRRYEAYAHQLLTSRGLTGFQFDSADSNTNGPSFGNDGADDLYA Q9P3V0 WTF4_SCHPO SPCC548.03c; CHAIN 1..366; /note="Meiotic driver wtf4"; /id="PRO_0000193221" MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIVIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV Q9P3W2 HSV2_SCHPO SPAC458.06; CHAIN 1..364; /note="SVP1-like protein 2"; /id="PRO_0000051032" MSTINTVSLNQDASCMSVALDTGYKIFQINPLKLRAQRQFNDGGLSIVKMLFRSNVLLLVGGGGNPKYAPNKLIVWDDVKERPVKELELNFEIKGICFDGKLLAIATASKLFLYQFGNNLKLQRCLDTQNPKGLCAMVTTVEKTAIVFPSRKVGQLQILFLFKDHMNTSIVPAHDSEISCLGISKTGSKIASSSTNGTLIRIWNSETGEKICEFRRGYQHTAVCQLAFSPDELLLACASKKETLHIFSLHGSPNTIRQLTSEEPYEEASEFKSSTTEPRQTHWKRKLLKLIDSGKRAHWRIQLYQSNPVLLHWLDEMTILICYKDAAYQKLKLTIEESSKSVEHANQHVCFHYDYTLEADGSLC Q9P3W4 DIL1_SCHPO PTM: The N-terminal part is acetylated. {ECO:0000269|PubMed:20404563}. SPAC458.04c; CHAIN 1..360; /note="Dynein intermediate light chain dil1"; /id="PRO_0000116845" MDELLEKLLNDLKKKEPKACSIICIGEDLDIIQCMNEHGCFSGGSYSELSNDCETVNFRGIAYKCFFTKDQVKVNFWQISHLTGGLFNFLVSQALNEHGLDLLWIIMVVAQTLSALVSFPEKLLNILRNMKTILINTEETVRNRFEESQNKKLVALLDKNSTTLDISSGILLNFTVVLKQLKHALGLHTSVDNSQEFILQFLRTTLLSVPTSSIVSISADPTSWNNLNVLMKYNFMFQKFKPRDFHAQTIQSETMFIPPCWDTISKIQSVNHEFNIALFKQTAKNFYDTLDISLLLGLFDKSISMLNCHSSKISDGDIPYKSHQVFLQELQNKYSEIKTYSSNKLNKSSIKSSLWKDLIQ Q9P5N0 ABC3_SCHPO BINDING 151..152; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /evidence="ECO:0000269|PubMed:28193844"; BINDING 614..621; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 1260..1267; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPBC359.05; CHAIN 1..1465; /note="Vacuolar heme ABC transmembrane exporter abc3"; /id="PRO_0000093471" MITANKGLSLVLLIPNLFALVSGGLQYVFDVRRRIFRPHFSQFWTIWMKFFSIALVIITQIYVGYKTKNIGWNFFSVVTYCFVLFLQFAEQSTLRVPMASLLIFWLLKVVTSLLILLFSPYIAITSMARLLTLITLFCSLVCFISEVYVPPCNRVWYSDDTNEVEEKGIRPSEVRYANIFSKLSFSWISSFIKFGYTNYLKESDVWLLPPDERSGNLIIGFEDWWIYHSKNKRRSLFLWKLLFFNHWKLVALITITKLIQDVLAFVQPTLIQKTILFISSYTSPNPESPSRGFIIAILVLVANFLQTLLLQQYNQLIMLLGMRWKTELLASIYRKSLLLSSSARQNRSIGDIINYMAVDTQKISDLPIYLFIIVSGPFQIALALSNLYHLMGYSAFTGVAASVILFPCNIIVANVYKKFQSILMKNKDSRSKLMTEIINNIRSIKLYAWETPFLQKLLHIRNTKELSMLKKIGFITAIGDFAWIFTTIIVTTVAFGAFIIFHGKTQALTADIVFPAVSLFNLLQFPLAMLPTVISSLLEASVSVSRIYEFLIAQELDYNGVQRFPATEIPHEICLEIKSGTFSWSKKTLKQQVTPTLRQINFVAKNGELTCIFGKVGAGKSSLLEACMGNMYKNSGSVFQCGSLAYAAQQPWIFDATIRENILFGSEFDPELYEKTIHACCLKRDFEIFTEGDQTEVGQKGASLSGGQKSRISLARAIYSQADIYLLDDVLSSVDQHVSRDLIKNLFGPEGFLRTHCVVLTTNSLNVLKEADSIYILSNGKIVEKGNYEHLFVSTNSELKQQLSEFNDEKDTQPLPEHTTSYPSTQISLAPSIHVEGLETYSSSERKDSSNKYKSRKRNPIRQKVTEDDKGKCVAQTDELVQRGKVKWHVYWMYFKSCSIGLILLYFFFIISGIMMNVATNVWLKHWSEENGKSSSELNPSPYFYLGIYLFFGFLSCAFISSSSLTMTVLCGIRSGRYLHDSMLKTILRAPMGFFETTSSGRILNRFSNDVYKVDEVVSLTFMFFFRNSIQVLFILGVICYSAPLSLLLIVPLFFLYLYNRAYYVRTSRELKRLDNVTRSPLYAHVQESLSGLSTIRAYGMQETFVEENDLRIDTNHRVWFMFFSSSRWQAIRVECIGDLIIFCTAFYGILSAIKGSPNPGLVGFSLSYAIQITQGLSFIVQQSVDAENNTVSVERILEYINVKSEAPEIIPENRPPCEWPTDGAVSFNHYSAKYREDLSFALNNINIEISPREKIGIVGRTGAGKSTLAMALFRIIEPTEGKIEIDNEDITKFGLYDLRSRLSIIPQESQIFEGNIRENLDPNHRLTDKKIWEVLEIASLKNCISQLEDGLYSRVAEGGANFSSGQRQLICLARVLLTSTRILLLDEATASVHAETDAIVQQTIRKRFKDRTILTVAHRINTVMDSDRILVLDHGKVVEFDATKKLLENKDSMFYSLAKESGLI Q9P6H9 REB1_SCHPO SPBC1198.11c; STRAND 188..190; /evidence="ECO:0007829|PDB:5EYB"; STRAND 237..240; /evidence="ECO:0007829|PDB:5EYB"; STRAND 273..275; /evidence="ECO:0007829|PDB:5EYB"; STRAND 443..446; /evidence="ECO:0007829|PDB:5EYB" HELIX 158..174; /evidence="ECO:0007829|PDB:5EYB"; HELIX 179..185; /evidence="ECO:0007829|PDB:5EYB"; HELIX 193..205; /evidence="ECO:0007829|PDB:5EYB"; HELIX 211..221; /evidence="ECO:0007829|PDB:5EYB"; HELIX 228..230; /evidence="ECO:0007829|PDB:5EYB"; HELIX 243..258; /evidence="ECO:0007829|PDB:5EYB"; HELIX 259..261; /evidence="ECO:0007829|PDB:5EYB"; HELIX 264..271; /evidence="ECO:0007829|PDB:5EYB"; HELIX 278..289; /evidence="ECO:0007829|PDB:5EYB"; HELIX 296..306; /evidence="ECO:0007829|PDB:5EYB"; HELIX 318..331; /evidence="ECO:0007829|PDB:5EYB"; HELIX 335..341; /evidence="ECO:0007829|PDB:5EYB"; HELIX 346..355; /evidence="ECO:0007829|PDB:5EYB"; HELIX 357..359; /evidence="ECO:0007829|PDB:5EYB"; HELIX 370..380; /evidence="ECO:0007829|PDB:5EYB"; HELIX 395..402; /evidence="ECO:0007829|PDB:5EYB"; HELIX 407..417; /evidence="ECO:0007829|PDB:5EYB"; HELIX 426..441; /evidence="ECO:0007829|PDB:5EYB"; HELIX 449..456; /evidence="ECO:0007829|PDB:5EYB"; HELIX 462..475; /evidence="ECO:0007829|PDB:5EYB"; HELIX 478..481; /evidence="ECO:0007829|PDB:5EYB"; HELIX 484..498; /evidence="ECO:0007829|PDB:5EYB" TURN 290..293; /evidence="ECO:0007829|PDB:5EYB" CHAIN 1..504; /note="DNA-binding protein reb1"; /id="PRO_0000197088" MDTSVLNPELQIHGFIGVDSLQSSRKRKNDFDDFPLNKGLKTNNNDYSGSIEPKFSPALSIKEDGKNDRNFEALMSLQAQDSNLSEQNTSIHLDALASSSIALGNDNVDSSAFLSKVNKGVNAMRNSTSNQTNDSILISPSEITNMDPFLKGSARWTAEHWDYLERRMQNFCQTYSLDHTQVADSLHEKRLHGPLSSLVKLLVQEMPSFTRRTILRHLRALYNIPGYEKYSRKNSSGRGDFGVQETAIISQEVHNFIMDQGWSEYQFCNQIWAGKCPKTIRMFYSNLYKKLSHRDAKSIYHHVRRAYNPFEDRCVWSKEEDEELRKNVVEHGKCWTKIGRKMARMPNDCRDRWRDVVRFGDKLKRNAWSLEEETQLLQIVAELRNREDLSSDINWTLVAQMLGTRTRLQCRYKFQQLTKAASKFELQENVWLLERIYDSLLNNGGKIHWENIVKEANGRWTRDQMLFQFINLKKMIPSYDNLPLLEATKSAIDDFKVVLSGFSN Q9P6I7 ADE_SCHPO ACT_SITE 212; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03145" BINDING 19; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03145"; BINDING 21; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03145"; BINDING 209; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03145"; BINDING 290; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03145"; BINDING 291; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03145" CATALYTIC ACTIVITY: Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+); Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2; Evidence={ECO:0000255|HAMAP-Rule:MF_03145}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03145}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03145}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 uM for adenine {ECO:0000269|PubMed:18673302}; SPBC1198.02; CHAIN 1..367; /note="Adenine deaminase"; /id="PRO_0000256237" MSNLPIYNFIRKLPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAYTTPSTLLASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAYEYFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALKRNDFENGIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWISGKRKEELLSSVQKCVKEYTAEIQQPKTLETAVEVQA Q9P6L5 SLA2_SCHPO SPAC688.11; CHAIN 1..1102; /note="Endocytosis protein end4"; /id="PRO_0000071944" MSSFRLQSDHMQSDASLMTSVRKATSIDETAPKRKHVRSCIIFTWDHHTARPFWTAIKVQPLLANEVQTFKALITIHRVLQEGHKSALVDSQSEKGWLKTCERQYDGESSPKGYSDLIRDYVDYLLDKLSFHAQHPEFNGTFEYKEYISLRQVDDPNEGYETVYDMMNLQDHIDEFQKQLFSNFKRSNKNECRIAALVPLVQESYGIYRFLTSMLRALYSTVDAPETLEPLKHRYKSQHHRLRQFYADCSNLRYLTSLISVPRLPHDPPDLEGDDNIPDLPKRPASIAPQPTGASTIAPQPTGTSPSPPVEMNFPDTSDITPAYSEPEPIQDFWSDPTLDQQLAAQQAAQQAAQQQAELAAQQAAAQQAQLAAQQAAEMERQRMAAQQHQQALEAIQMAQAEQQRIAQEQLAQQQFQMQTQGQLAELEQQLLATRGQLEQSNVLLNQYDARVRTLENELSQAGVNLQEQIHQNDDLIESLKNQILTWKNKYEALAKLYTQLRQEHLDLLSKYKQIQLKASSAQEAIDKKEKMEREMKNKNLELADMILERDRARHELETMHRSQRDKQESTERELRLLQEKAASLERNKSSEVSNLLSRYNTEVAHLEDALHSKDRELANLGVELKSTENRYRQLLQEKEEELEIQKAAVDESLLQLSKLQLDRNDIDQAMDTQIDELLKSQLEKLDDIVDSVLATGIQRLDTSLYELDSPMHAGNQYATPEFILSTIENASNNATDFSTAFNNYFADGPNADHSEVINGVNLFSTAIYEVANNAKGLSRTTGDDQGSDRFVGLSRDLVNMAKRFLSSLFSVNTRKMDVNVKTDLVIGENIELQRYLQQLTQYSEKFLNKESENTVGLLNAPGENIEELVDNQLAETAQAIQQAILRLQNIAAKPKDDSLSPSELQVHDSLLSASIAITEAIARLIKAATASQAEIVAQGRGSSSRGAFYKKHNRWTEGLISAAKAVARATTTLIETADGVVNGTSSFEHLIVACNGVSAATAQLVAASRVKANFASKVQDHLEDAAKAVTEACKALVRQVESVALKAKEVQHEDFSSLGVHEYRRKEIEQQVQILKLENDLVAARRRLFDMRKTSYHVAEE Q9P6L6 DPOZ_SCHPO BINDING 1381; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1384; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1400; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1403; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1432; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 1435; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 1446; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 1451; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P14284}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; SPAC688.10; CHAIN 1..1480; /note="DNA polymerase zeta catalytic subunit"; /id="PRO_0000361055" MRFSIEYIDWELSPCDPAYDFVGKDLPTANEELTTVPVIRVFGLNEEAETVCCFIHNVFPYIYVEYSSFAETLDLEVPDFLSQLQTSINYALALAARANPETYKPAVQSVQLVKGIPFYGYSFCFQKFLKICLFSPKNRDRLVDLFRQGAILNKVIQVYESHLPYLLQFMVDHNLYGCAPIDLDDSIIKRDDLLSFCNVEVHVSPNAILNACWLSERNIHTDLYETHASSPNSLLVTSLAEIWKSEASRRNLTSSDETNSFSKLHQSQFGLKEESSHEPRSSQHWKNEVAMKDLLKNLIKSKLESSSDVNTPLIFDPWPELPTIYSAIHTKDYVRPSQNDISVSQISVDEKICTSYESLPKIQLEQNTAPVIESSFEQLDSELERILGDTLFDSFPYVEPNVDRSKFPKSPLNSSQEVTIHSSQDRQSPPSSPLKDVPSQINPFSPSLRLKGGSPITKREIEFCRDLPNRPTSSEPNQGDTRKAGKRLKYSRNLDDYHICTQIPEDYSPKFLSQHESFVYKQQPPSTDDLYGTMKKLKIPFSIPTNVHYSSEKDIPSYSQEYLGKSHYPIGVSSRYLPEFQSDGSVSEKVRLNPLKLSNFHGERTWQYIKPAPLAVDLSNLESKEAVSEEIQSPQRLSRSKVFRKDPYSCVRILALELFCCSHGGLTPDPTKDSIECCFWAYQEDVNSSMIDRVGFIVVDKSASNSSFGRSFPSCTVLVVNSELELINEVIGLNRQLDPTIVCGYEVHNSSWGYLIERASYRFNYDLPEQLSRLKCTSKANFAKKENAWKYTTTSSINIVGRHVLNIWRILRGEVNLLNYSLENVVLNIFKKQTPYYNQADKVHLWQSSRFHEKQILLNYMLNRTRYCLEILSACAIVTKIREQARIIGIDFMSVISRGSQFKVESIMFRIAKPENYIFPSPSAKQVAEQNALEALPLVMEPKSDLYNNPVVVLDFQSLYPSIIIAYNLCYSTCLGPVKIVNGKVKLGFMFHSSNPNIVNLIKNDVYISPNGYAYVKENVRKSLLAKMLEELIETRNMVKRGMKDCDSDYVNKVLNSRQLALKLIANVTYGYTSASFSGRMPCSEIADTIVETGREILSYSLEYINTLDFCHAKVVYGDTDSLFVELPGATKEQAFDIGQQLANNITSRFPSPIRLKFEKIYFPCFLLAKKRYVGFKFESVSQKAPIFEAKGIETVRRDGTPVQQQLLRRCLEILFKTKDLSTVKKEFQNVCYQIMSGNVPVMDFCFSKEVRLEKYKELSTAPPGAVMARRLMTKDPRREPQYGERVPYLIIAAAPGTTLANRSVAPEEFLSSSFSQLDINYYINNSLIPPLDRFLNLLGASAQSWYHEMPKPRTSLKLTETVKGGIQKKTLDTFLMEKLCSSCLKNNIEIIPDKINSLCSDCLKNPCATISKAVTQHNAYNKKLSLLFDICRGCSKLSSSDPVLCKSNSCKVYYDRAKTENYAKVQAEMLTKTLGSLDW Q9P6M1 GST3_SCHPO CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; MOD_RES 228; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 232; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC688.04c; CHAIN 1..242; /note="Glutathione S-transferase 3"; /id="PRO_0000185986" MIVLHHLKNSRSTRIVWMLEELKVPYEIKVYDRVDGRAPPAYTKLSPLGKSPIVVDDGVTYIESAAILEHLVRKYGPSFKPSEEDVAELEKYELWMHFSEASLMPFIWASHVLDLSVNMTPIFFRYIVRQFVNGIKSKYLSKETFLNLDYIDNHLASNEYFAGEQFTAADPQMCFPIFAAQRDYLSQKPYKNIKRWMRVVSDRPACRIAAEKVEDNTLTLFSDVERYSHPPTPPPEQVRSDE Q9P6M8 PABPX_SCHPO SPAC1610.03c; CHAIN 1..710; /note="mRNA export factor crp79"; /id="PRO_0000081719" MNNSKLSVPGQYEDESSTIYVGNIDSRLSDEEIIKHFSKYGQVESIFRRLLDSFYPKEKAKPFKPPKNGVQYGFVKFVNAESIEEVLKDAKGMTLGQRKLTIKARVVNPAKLTDKKFKPNDTSITANVFNPSIQNNTDEENVKPGLKQSQIKEFIPNVEERNWETVRGINSRNPKPETTLTIPSLGLEDISMQVVPNAFASTLPLSILNLPAEVTPIDLYNHFKQAGVVKGTAVSQFLDQRGFRYGEVIMDSVESCQNAIEKLNNVPYKGSILEVSIKNKASSSVKSIPTTPTGESLWPFPSENANKTQINIENATCSKMTWIMGSPTKEKSQWGSVSTTGVSNQQNHPAAWNPDNKPQSIVHWDSLRESSPSIPNSPIDPSNLYVKNLDDTVITCKSQLEDLFSPFGSILSSMLACYPNSGISKGYGFVAFRQIEAAVRAKDTLNGMMVGKKRIFVCFAERKSDRIRRLQAFFANKPTSEQTAQQDNKALFVKPERSSTVTIRKPIESSTNKISENPTTLSSKVENKNEPKTGENKEPSQTNEYVNCKQENKELSGQLSGNLDIKKEAGKLSHDGEQGNLLKPLVFHANTKLNNRGSAKMGSTATNLKKIQDMLHNKKLSNAYFVPRARATTCTTLTYVTVEPSHFQDEDCNESTNMLSLVGYMDSYPEATSNIQKMNSYHIKDSNKENFLSTTKVNNNSPTTIQLTQI Q9P6N1 MG179_SCHPO SPAC823.16c; CHAIN 1..335; /note="Autophagy-related protein 21"; /id="PRO_0000050881" MPSIILYCSWNQDRGFLSIGSENGYQVYRSNPFTLCFSKKANGASICEMLYESSLLAFVNISPESTRLLKLVDIKRDIVLCRIFYPSPVLSVRFTWNRLVVLIKGSIYVYNLKNMELINTLNTSKGNVIAFAVHENYVAYNSPTNPGDIYLASLDTAIPVTLIHCHSSAVQVVDFHPRGHLIATASAKGTVIRVITTSDGELVTELRRGYIPASIVSISFHPVEPFLACASENGTIHVFKISKQPSDPNSSPTSSVTVSSSWSKYLTSNVAKVWDTRKEFATAKIPEASFYGKIIFSSSGPHIQVASYSGHYYRFAVNLKNGGNCALLERYIFDD Q9P6N2 PTF1_SCHPO ACT_SITE 12; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q58989"; ACT_SITE 14; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q58989" BINDING 12; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q58989"; BINDING 14; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q58989"; BINDING 176; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q58989" CATALYTIC ACTIVITY: Reaction=D-ribitol 5-phosphate + H2O = phosphate + ribitol; Xref=Rhea:RHEA:47648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15963, ChEBI:CHEBI:43474, ChEBI:CHEBI:57695; Evidence={ECO:0000250|UniProtKB:P53981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47649; Evidence={ECO:0000250|UniProtKB:P53981}; CATALYTIC ACTIVITY: Reaction=D-sorbitol 6-phosphate + H2O = D-sorbitol + phosphate; Xref=Rhea:RHEA:24580, ChEBI:CHEBI:15377, ChEBI:CHEBI:17924, ChEBI:CHEBI:43474, ChEBI:CHEBI:60084; EC=3.1.3.50; Evidence={ECO:0000250|UniProtKB:P53981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24581; Evidence={ECO:0000250|UniProtKB:P53981}; CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; Evidence={ECO:0000250|UniProtKB:P53981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46085; Evidence={ECO:0000250|UniProtKB:P53981}; CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O = D-erythrose + phosphate; Xref=Rhea:RHEA:66376, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:27904, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P53981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66377; Evidence={ECO:0000250|UniProtKB:P53981}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q58989}; SPAC823.14; CHAIN 1..229; /note="Pdp3-interacting factor 1"; /id="PRO_0000339407" MAQKKQLYVFSDFDGTITLQDSNDYLTDNFGMGNANRVNLNQQVLDGSISFRDAFAKMLDSVHLSYDEALEVLKKNVAIDPSFKPFYEWCKSQDIRVIILSSGMEPFIRALFEQYLGKEEASSIEIVSNDINVHPDGQWNIVYHDDSHFGHDKSLTIRPYAQLPESKRPHMVYCGDGVSDLSAAKETEHLFAKKGRDLIKYCEREKISFSEFETFADIHKDLQKLFFSS Q9P6N4 PEP5_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P12868}; SPAC823.12; CHAIN 1..906; /note="E3 ubiquitin-protein ligase pep5"; /id="PRO_0000361017" MSTFIKNWKRITLFQVKAIEENIDRLTSSFSSNGELVVFATAFGDVSIYNSSFKSLQSIKVEDESSIQQILWLDNKTFLLFSNVEGGTGTNSTVIIYAFSQADENEPPQFVLVTTHKFSINESPYPIIAVSQSPIDKTIACGFGGGLVSCYHGNPLRERGIKNSYSHNLGEPITGLTYLDDQSSVLFIATTNKTYSLSGKSLSCLDNTGVSLNCSSSCKTTPLQSREKNSSSFVCTRSSGLTFYDSKREKICFTFPGEKHYMTVMGSILALCYTPTLGTDSSTNEGLKKSFSSSSSIRKADASRNPAFPPRLLLVDLSRNLIVWEGHLKDVAVSILPLKHGFLVVTADDNVFELKRITLQEEISLLCQKMMYNLAISLAKKENMDIEFRESLMRDYASFLFRRGDFSASMDWYIRSIKSIDIPSVCLEFLKAQEIKQLIRLLEELIKTGLATSDHRLLLLSCYVEIHDSPSIRKLIDIGEIDFDQAFKICYDSNLLDEAKHLAIRFNNNERVLDVLVESEQYSEALRFFESLPPSNLLPLLLKYGRVLLDKLPEKTTNIFIQFYSNSHRGDLSTSESKGELKTAKSLRQTYLSLLPYAQVANFSLPPSLYEISPSQEENQRAALFSEDVSYTAPSPQTCFHIFLNHNSELISFLEGILPNASPNYKTLINTCLFEAYIRESFASSNVEKQEFWQEKSNSLLKKVEKNVDLNAVFLISQILGFDDGVRFVQGKSGQTLDIFRSFCQQNDIERALKMVRVHGPDQQELYIMMLNCFASLENVDSWYQDINEIVNIIVSQRLISPTQLLDILGKSVNIKLEHISDSMQSVLDNYRESISKQNEAIEMGKRDIEEITSQLSILRTRAFVVQESKCSTCGIDLELPMVHFRCGHSYHQRCVEDECIRCRWL Q9P6P3 PPK15_SCHPO ACT_SITE 257; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 136..144; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 159; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 33; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 56; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 291; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC823.03; CHAIN 1..534; /note="Serine/threonine-protein kinase ppk15"; /id="PRO_0000086140" MDSDSPILPLSNNPPAARTHDHSQRNNHARHVSSSGTTLFAPVKPATKKYNYRRVSPHGSYISPLEAMTVKLADTYSICNPKFQFSSEQNPRRPLTKPSEGVHNHGFDNVNHDYVLYVNDLLGTDEGRKYLILDTLGHGTFGQVARCQDLKTQQIVAIKVIKNKPAFYNQCVMEVSILELLNNKYDPEDKRHLIRLYDQFMHKNHLCLVFELLSINLYELIKQNQFRGLHLSLVRSFATQLLSCTSLLKQARIIHCDLKPENILLQDLSSPIVKVIDFGSACHERQTVYTYIQSRFYRSPEVILGLHYNCGIDMWSLGCILAELFLGLPLFPGNSEYNQLCRIVDMLGNPPTWMLEMGKNSKKYYNSGFVNGRKTYELKSIEQFSIENNKTEQPGKQYFGEKTLDAIVLNYPRRKTTPKLTPEEHEERLCFIDFIKQFLELNPLKRWTPDQAKNHPFITGASFSQYCIDKQKPLLTTQRTRNRSHTIGNQAVVPPSLQRASTYVSNEPEEFVHTRPLPQYYPPANENENVDEFF Q9P6R0 TF3B_SCHPO BINDING 3; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"; BINDING 6; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"; BINDING 22; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" SPBC13E7.10c; CHAIN 1..492; /note="Transcription factor IIIB 60 kDa subunit"; /id="PRO_0000119345" MGCPNCGSTTFESDTASGNTYCTQCGVVVEQDAIVSEVTFGEASTGAAVVQGSLVSNDQTHARTFGGPYRNQGSVESRELTIANGRRRISALAIALKLNERHIEAAVRYFTLAINNNFIKGRRSQYVVASCLYIVCRISKTSHMLIDFSDILQINVFKLGSTFLKLCRVLRPNLPLLDPSLYISRFASLLEFGPETHRVANDAIRLVARMNRDWMQIGRRPAGICGACLLIAARMNNFRRSVREVVHVVKVADITIQKRLDEFKLTESGDLSIADFRNIWLEGQSDPPSFTKNQKFQQYGAQKVSNIDHTQEYMSPIKRTPDFDGNEVKSEELSQTVKVESQETPVHLKADEREIRKEVTETLKGDELRKISLQVNVKFSEEEVTLEDVDDDEIEDILLDKDEILTKTQVWMELNKDYLAEEEAKNLKLQEDLKKGIVRQPRKRRRYRPRDSTSDGIADTAAESAKEMMQQRAFSKKINYEALDMLFDEEQS Q9P6R1 VRP1_SCHPO SPBC13E7.09; CHAIN 1..309; /note="Verprolin"; /id="PRO_0000364026" MAPAPPPPPPAPAPAAAAPAPPLMTGDRSALLNSIQKGKKLKKATTNDRSAPVVGGGVVGERKSNTPKSFAAPPVPTGAPSLPTSSNNTQQAEERPSMPALGGLFAGGMPKLRHIGKSSASAAPPSAPAPPTPQSELRPPTSAPPRPSIPPPSPASAPPIPSKAPPIPSSLPPPAQPAAPVKSPPSAPSLPSAVPPMPPKVPPPPLSQAPVANTSSRPSSFAPPAGHAPNVTSESPKFPNRGPSIPSASVPPVPPSSYVLQQRPNRVDDHGRFHFKDDSYLPIPHPFLGVPKVYRGGSGTTVPLNLSSF Q9P6S5 ASK1_SCHPO MOD_RES 136; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27.02c; CHAIN 1..307; /note="DASH complex subunit ask1"; /id="PRO_0000211316" MNNLEQLERLEQSITLALYEIDANFSKCHRTVTTKILPIVEKYAKNCNTIWDSSKFWKQFFEASANVSLSGVEEPVPVESNPSDQDVMSNSTEADLQLHTKNEHLEKRHSFVGKSDFPDAAVQGDNTKNEDFVQSTPKKMDVSLEDISLDDAALTPIPARMQTPLRKPENNPHTGRSALLHRVLDTNWQVQVTPREPKNLQSQEVMDIDSSPFVSPSPISMKMDMPSLNDRNSSHALSLFAEFEHESYDSINPSGMSPPKTIQFSPHTMGVGSSQQANERSLSLQRKLETLNDSNDSFVKEEDSWEL Q9P793 MIT1_SCHPO BINDING 581..588; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPBP35G2.10; STRAND 9..14; /evidence="ECO:0007829|PDB:6FTO"; STRAND 32..39; /evidence="ECO:0007829|PDB:6FTO"; STRAND 42..47; /evidence="ECO:0007829|PDB:6FTO"; STRAND 51..56; /evidence="ECO:0007829|PDB:6FTO"; STRAND 1286..1289; /evidence="ECO:0007829|PDB:5IKF"; STRAND 1306..1308; /evidence="ECO:0007829|PDB:5IKF"; STRAND 1330..1332; /evidence="ECO:0007829|PDB:5IKF"; STRAND 1337..1339; /evidence="ECO:0007829|PDB:5IKF"; STRAND 1342..1345; /evidence="ECO:0007829|PDB:5IKF" HELIX 18..20; /evidence="ECO:0007829|PDB:6FTO"; HELIX 22..24; /evidence="ECO:0007829|PDB:6FTO"; HELIX 57..62; /evidence="ECO:0007829|PDB:6FTO"; HELIX 66..77; /evidence="ECO:0007829|PDB:6FTO"; HELIX 1223..1230; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1241..1253; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1293..1301; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1324..1326; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1348..1350; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1353..1364; /evidence="ECO:0007829|PDB:5IKF"; HELIX 1370..1381; /evidence="ECO:0007829|PDB:5IKF" TURN 27..30; /evidence="ECO:0007829|PDB:6FTO"; TURN 48..50; /evidence="ECO:0007829|PDB:6FTO"; TURN 1312..1314; /evidence="ECO:0007829|PDB:5IKF"; TURN 1334..1336; /evidence="ECO:0007829|PDB:5IKF" CHAIN 1..1418; /note="Chromatin remodeling factor mit1"; /id="PRO_0000339420" MPKEDDSLCKIVVRREPLDVLLPYYDASETTVQKILHENDSTLSVKFLAGVEALIKKDELDKYKNGKACLRVWLKHKSRKRYHGYMTSTDKDEEEKNDYLLKSNGSKVLRDSTRTKKFKFGKEFHCALNPSFVSDETASDSATSSSSDTNKKVNRKEHNELSLSHLSFNDTSDFGSSDLSSSEIESTENDNKAPYFSLLYSDGFDFIKFLHVCVCVKCHGREHRSSGKNFVYCDHCSNVYHYDCSPLPSLNKETRNYSQQNGFICPLCSKNSKDVLCNTGFVSGVSSGQDLVIPPSLADRESLSILVNYCKSIRFRCFRCRRVEYFFYLDSNPLSIQRTITHFIKKLVCNECSMHPCDIEEIIAWRTLNSLYPSKATLSNNFVSTSDLSFWSREYFVRSKGKSYLHCFWCSASWLAGISLAKKKNFDGLENASYDATKPIIPVSYTIIDKVWDVQYRSGKNARTAKYKTKKHQLKAISEVTFAFVSWRGLTYYMSNWEPPPKETDRNRWKAWLKGYSDLLECLWIEKAPTASINIDLPFTNLEWHSQPSFIKGGTLMPYQLKGLNWLYLRWYTHHPCILADEMGLGKTVQVISFISVLFYRHKCFPVLVIVPHATVANWERELKKWAPFLQINVLVGSEKNRSLVRDYRLINQKDPKHVSTHVLVISASNVEREISLLRKFQWKVLIVDEGQRLKNDQSSLFYYLSSVKSDFKLLLTGTPLQNNVRELFNLLQFLNPMKINAAELEKRYSIIDTEKVTELHQILKPFFLRRVKSEVLDNFPTKVEVIIPLSMTPVQKGLYKSILSKNLSLLRNITGYANTSSSGGQRTTSLNNILMQLRKTLAHPYIYSPDIEDRNLPYELAMRSLEEASCKFLILRLLVPKLITRGHRILLFSQFIQQLDILEDWFEYKNIAYARFDGASSEMERQSAIDSFNAPNSELSCFLLSTRAGGVGINLASADTVIILDPDFNPHQDMQAIARAHRYGQKKKVLVFVLTTRDSVEEKIIQNAQKKLVLDHLIVESLDQNHNSEKDLESILRHGARALFEEAGDEPSIKYNEYSVELLISEAEKQEDTSTDESDIKSNKFGFFRVWDNKHISSNHYEVKENVLVDEEDVWSVILKQREKDAMLEKTDETTSNRRLRAHHKIHYGEDLNIYDNSDDTDYTVNDRSSPGSPFPIETETISSITDTLSDKQKLKYDSSVNIENLNDESDSQKSADVHFDSILAKSLLATTPKEDEFNKTLSTINLEVANKLTSSEYINDSEMQLIDDPVFYPPYEIIEKNHQLVGRSLSKAVLDNFFLLSSLSDNVRCRCCGIKHLPAHCPLSIVPLEICFLCGTPHFSGRDTCPMLRNKEAIYRLKDSLSKSREPFHIKKQAMARLNSFLQKKEEPTVSSSAKTNELSSKVIIKESIINEAKTL Q9P7A0 SGO1_SCHPO PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. {ECO:0000305}. SPBP35G2.03c; CHAIN 1..319; /note="Shugoshin-1"; /id="PRO_0000055451" MNFQFINSNINNEDKLPMESLKKKFLKQNREIIKINTQLSIKIRESENEIQDLIQENFTLKSYLVKLEARFRNQSQTEDLLKNFFPEIQTIHKKISQVQSLLKIIEKKCSSDFLEANVKSQFTTCENKDSKEDYQILHNKRLEYVSFNDELKSLETGQPLYCFQDFQKKVHGPPALSEKPGKCILKDKTNAHVNKIPQDEVNYSLPQKNITIFSKELKENEFESINEGETEEEKAKTSNVCVCIPCKSAEQITDLKGQATGDSSPCDFEESQPRINGREKLRRSVKVINYAIPSLRTKLRRDFDLPSDRKRKRHPRGKA Q9P7C3 MNS1_SCHPO ACT_SITE 387; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P31723" BINDING 504; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P32906" CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000269|PubMed:16079177}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000269|PubMed:16079177}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; SPAC2E1P5.01c; CHAIN 1..521; /note="Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase"; /id="PRO_0000210320" CARBOHYD 114; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 167; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 300; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 342; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 378; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 499; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 330..373; /evidence="ECO:0000250|UniProtKB:P32906" MVKRRTVKYFLRRILALFVLCVPIYYLYTTVQRPPGYTKLKGSTRRKALIKKTFIESWTDYETYGWGKDEYYPIIKRGRNYLRKGMGWMIIDSLDTMMIMGLDEQVLRAREWVNNSLTWNQDDEEVSVFETTIRILGGLLSSYHLSQDKLYLDRAVDLADRLLAAYNTSTGLPRSNVNLGTRKSRKRTREYFVSTAESGTVQMELRYLSYLTGDPKYWITADKTMEVLLGDATWSHTGLVPITVNLITGAYVGRNIRLGSHGDSYYEYLLKQDLQLFSSGTVYRKAFDLSVDGIIEYLLNYTTPNHFAYIAELPGGLEHAQLPKMDHLVCFLPGTLMWGATNGTSLEAARTSKNWGTRQERDVKLAQELMRTCYEMYNMTATGLAPEIVFFDVDQTKNEIYSKRRDQHNLMRPETVESLFILYRITRDEIYREWGWNIFVSFLRYSRLPGRDAFTCLDSVESKKVKDQRDKTESFWFAETLKYLYLLFEDDFSILPLTNYTFNTEAHPFPNIENNMDLYTV Q9P7C7 PRP11_SCHPO BINDING 462..469; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305|PubMed:14713954}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000305|PubMed:14713954}; SPCC10H11.01; CHAIN 1..1014; /note="Pre-mRNA-processing ATP-dependent RNA helicase prp11"; /id="PRO_0000055146" MSRRTRSRSPPRRSYNRERRDYRKYDDSEDQKGARYNRYVDDVSSRRDRHDSFRSHESNKIRRDNSWKHDKYSYEKRYQERDREYARSKNIPDQYIGRSPRPTSHRHAEEKEVDNKTKSDETNPVLQGSATEIKPQPRRSRFDRTERVGASLSVSEIQSENPRVDVIPKDKAVENNHQRNAEKPVASDKITDAKLLARLERVRAWKESKAKQEASKKEEHKLNTKPQVTAKDQNAMPSTGISGFEINRQKDTSDMKRNNRVHMDDEDGPRRMNLEDYQELWDQEDRGMLGNEQAASMEEDEVDPLDAYMASLVGTTDTIRPGLLNTEVIDPNANDDERMVISETLEEEENLLALAAKRSKKKDVITVDHSKINYEDFKKDFYVEPEELKNLSPAEVDELRASLDGIKIRGIDCPKPVTSWSQCGLSAQTISVINSLGYEKPTSIQAQAIPAITSGRDVIGVAKTGSGKTIAFLLPMFRHIKDQRPLKTGEGPIAIIMTPTRELAVQIFRECKPFLKLLNIRACCAYGGAPIKDQIADLKRGAEIVVCTPGRMIDVLSANAGRVTNLHRCTYLVLDEADRMFDLGFEPQVMRIINNIRPDRQTVLFSATFPRAMEALARKVLKKPVEITVGGRSVVASEVEQIVEVRPEESKFSRLLELLGELYNNQLDVRTLVFVDRQESADALLSDLMKRGYTSNSIHGGKDQHDRDSTISDYKAGVFDVLIATSVVARGLDVKSLQLVVNYDCPNHMEDYVHRVGRTGRAGHTGVAVTFITPEQEKYAVDIAKALKMSKQPVPKELQTLASQFLEKVKAGKEKAAGGGFGGKGLSRLDETRNAERKMQRKAYGEDEEDVETEAEAKSPLEKITPEKSTGDPTLDRVRAAVGGIAARAFANQTAQSNKLTQPISIIKTDGDEYKAKMEINDYPQQARWAVTNNTNIVHVTELTGTSITTKGNFYLPGKNPEPGEEKLYLWIEGPSELVVNRAITELRRLLLEGINHSLEGGNKPSASGRYTVV Q9P7D4 ACON2_SCHPO BINDING 105; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 198..200; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 394; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 457; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 460; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 484; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 489; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 619; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P20004"; BINDING 680..681; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P20004" CATALYTIC ACTIVITY: Reaction=(2R)-homocitrate = cis-homoaconitate + H2O; Xref=Rhea:RHEA:26101, ChEBI:CHEBI:15377, ChEBI:CHEBI:58174, ChEBI:CHEBI:58884; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P20004}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P20004}; TRANSIT 1..30; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP4H10.15; CHAIN 31..918; /note="Aconitase-ribosomal protein bL21m fusion protein"; /id="PRO_0000316198" MATFARMKLCLSGSSQAIPSKGISLVAARFQSTASRASYVTPPYEKLMGKLQQVRKFLPGQKLTLAEKVLYSHLVNPEESFSGVSPSDIRGSLYLKLNPDRVAMQDASAQMALLQFMTCGLEKTMIPASIHCDHLIVGHRGANSDIPDSIANNKEIFDFLQSAAKKYGIQFWGPGSGIIHQIVLENYAAPGGMMLGTDSHTPNAGGLGMIAIGVGGADAVDAMTNTPWELKAPKIIGVNLTGAMSGWTTPKDLILHLAGKLTVRGGTGHIIEYFGPGVASLSCTGMATVCNMGAEVGATTSIFPYTDSMRRYLIATHRAEVADAASEVHSEYNYLAADTGAKYDQIIDINLSELTPSLNGPFTPDLSTPVSKFGEAIEKNKWPKKLSAGLIGSCTNSSYQDMTCVVDVVEQAISAGLKPKVPFLVTPGSEQIRATIERDGITERLEEAGATVLANACGPCIGMWKRTDDIASGEPNAILTSFNRNFRSRNDGNPSTMNFLTSPVIVAAKIFSSDLAFDPTHDTLQTPDGKAFKFRPPQGVELPSAGFIAGDSSYIPEPNPQPVPETEVTIDPKSDRLEALEPFEPYQGGEMENLKVAVKVKGKCTTDHISAAGKWLKYKGHLSNICNNTLIGAMNAATGEVNRAYDNGKGMTIPELMWKWKKDGQPWLVVAEHNYGEGSAREHAALQPRAMNGRIILTKSFARIHETNLKKQGVLPLTFVNEADYEKIDAEDKVSTRGIEQLLEGVLDQPITLVVTKKDGSVVEIPCKHTMSKDQIEFFKAGSALNLIREKAHSGVVNQKVIDSIKQQPDHYADAYIFNRHFVIAKGDQLGLPFHLKGVQVGDTIRLDKIASFGSRDFTLFGNPYVDPSLFTIEAVVLSFPKSALSVRVKHKRRHRHDRVMKHKQTYTILRVTELKLN Q9P7F2 CAO1_SCHPO ACT_SITE 321; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P12807"; ACT_SITE 407; /note="Schiff-base intermediate with substrate; via topaquinone"; /evidence="ECO:0000250|UniProtKB:P12807" BINDING 319..330; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P12807"; BINDING 404..409; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P46883"; BINDING 458; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:P12807"; BINDING 460; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:P12807"; BINDING 616; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q43077"; BINDING 617; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q43077"; BINDING 627; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:P12807" CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:16946276}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q43077}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077}; PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}. MOD_RES 407; /note="2',4',5'-topaquinone"; /evidence="ECO:0000250|UniProtKB:P12807" SPAC2E1P3.04; CHAIN 1..712; /note="Copper amine oxidase 1"; /id="PRO_0000316036" DISULFID 340..366; /evidence="ECO:0000250|UniProtKB:P12807" MAYYPHLPYHHHHHTSVPGERLSDPLDPLSADELKLAVEIIRHEYPSKHFAFNVVTLEEPPKAKYLHWKYSKEDAHKPERIALAVLLEKGVPGILEARVNLTKAEVIQIEHITGVCPILTADMLVNTEQIVRKDPAVIEQCILSGVPPDQMDHVYCDPWTIGYDERYGNTRRMQQAMMYYRSNEDDSQYSHPLDFCPIIDTEDQKVVAIDIPPVRRPLSKHKHSNFNKKDIEAELGKMREVKPISVTQPEGVNFRMKGRYIEWQNFRMHIGFNYREGIVLSDISYNDNGHIRPLFYRMSIAEMVVPYGNPEHPHQRKHAFDLGEYGAGYLTNPLALGCDCKGVIHYLDAHFVNNTGEVETVKNAICIHEEDDGVLFKHSDFRDKFRTTISARGIRLVISQIFTAANYEYMVYWIFHMDGVIECELKLTGILNTYAMNEGEDLKGWGTQVYPQVNAHNHQHLFCLRLNPMLDGYSNSVAVVDGVSGPGEPGSKENYYGNAFTTERTVPKTVKEAICDYNSDTSRTWDICNPNKLHPYSGKPVSYKLVSRETPRLMARPGSLVSNRAGFARHHIHVTPYKDGQIYPAGDYVPQTSGEPTKGLPEWIAEEPDASVDNTDIVVWHTFGITHFPAPEDFPLMPAEPIRLLLRPRNFFLRNPALDVPPSKNVTTSEVKQAHHHGNLHMMDMMKSLTDATSEFAFGEKFCEKHKGDHFF Q9P7F8 GET3_SCHPO ACT_SITE 56 BINDING 27..34; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03112"; BINDING 231; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03112"; BINDING 258; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03112"; BINDING 268; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared between dimeric partners"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared between dimeric partners" SPAC1142.06; STRAND 21..25; /evidence="ECO:0007829|PDB:2WOO"; STRAND 27..31; /evidence="ECO:0007829|PDB:2WOO"; STRAND 46..48; /evidence="ECO:0007829|PDB:2WOO"; STRAND 50..54; /evidence="ECO:0007829|PDB:2WOO"; STRAND 80..86; /evidence="ECO:0007829|PDB:2WOO"; STRAND 142..147; /evidence="ECO:0007829|PDB:2WOO"; STRAND 150..152; /evidence="ECO:0007829|PDB:2WOO"; STRAND 222..231; /evidence="ECO:0007829|PDB:2WOO"; STRAND 251..260; /evidence="ECO:0007829|PDB:2WOO"; STRAND 292..298; /evidence="ECO:0007829|PDB:2WOO" HELIX 11..15; /evidence="ECO:0007829|PDB:2WOO"; HELIX 32..44; /evidence="ECO:0007829|PDB:2WOO"; HELIX 60..65; /evidence="ECO:0007829|PDB:2WOO"; HELIX 89..98; /evidence="ECO:0007829|PDB:2WOO"; HELIX 111..117; /evidence="ECO:0007829|PDB:2WOO"; HELIX 123..138; /evidence="ECO:0007829|PDB:2WOO"; HELIX 157..159; /evidence="ECO:0007829|PDB:2WOO"; HELIX 160..172; /evidence="ECO:0007829|PDB:2WOO"; HELIX 179..189; /evidence="ECO:0007829|PDB:2WOO"; HELIX 200..216; /evidence="ECO:0007829|PDB:2WOO"; HELIX 232..248; /evidence="ECO:0007829|PDB:2WOO"; HELIX 269..288; /evidence="ECO:0007829|PDB:2WOO"; HELIX 309..318; /evidence="ECO:0007829|PDB:2WOO" TURN 154..156; /evidence="ECO:0007829|PDB:2WOO"; TURN 219..221; /evidence="ECO:0007829|PDB:2WOO"; TURN 289..291; /evidence="ECO:0007829|PDB:2WOO" CHAIN 1..329; /note="ATPase get3"; /id="PRO_0000317079" MSFDPLPGTLENLLEQTSLKWIFVGGKGGVGKTTTSCSLAIQMSKVRSSVLLISTDPAHNLSDAFGTKFGKDARKVPGFDNLSAMEIDPNLSIQEMTEQADQQNPNNPLSGMMQDLAFTIPGIDEALAFAEILKQIKSMEFDCVIFDTAPTGHTLRFLNFPTVLEKALGKLGGLSSRFGPMINQMGSIMGVNANEQDLFGKMESMRANISEVNKQFKNPDLTTFVCVCISEFLSLYETERMIQELTSYEIDTHNIVVNQLLLDPNTTCPQCMARRKMQQKYLAQIEELYEDFHVVKVPQVPAEVRGTEALKSFSEMLVKPYVYPTSGKE Q9P7H1 FLP1_SCHPO ACT_SITE 286; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; PTM: Phosphorylated by cds1, chk1, pmk1, and cdc2 upon Hydroxylurea and H(2)O(2) stress treatment. Phosphorylation regulates the nucleolar-to-nucleoplasmic transition. Is able to autodephosphorylate. {ECO:0000269|PubMed:11683392, ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:22918952}. MOD_RES 453; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 468; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 470; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 513; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1782.09c; CHAIN 1..537; /note="Tyrosine-protein phosphatase CDC14 homolog"; /id="PRO_0000094874" MDYQDDGLGEMIEFLEDKLYYTSLSQPPKAELYPHMHFFTIDDELIYNPFYHDFGPLNVSHLIRFAVIVHGIMGKHRQAKKSKAIVLYSSTDTRLRANAACLLACYMVLVQNWPPHLALAPLAQAEPPFLGFRDAGYAVSDYYITIQDCVYGLWRARESSILNIRNIDVHDYETYERVENGDFNWISPKFIAFASPIQAGWNHASTRPKKLPQPFAIVLDYFVANKVKLIVRLNGPLYDKKTFENVGIRHKEMYFEDGTVPELSLVKEFIDLTEEVEEDGVIAVHCKAGLGRTGCLIGAYLIYKHCFTANEVIAYMRIMRPGMVVGPQQHWLHINQVHFRAYFYEKAMGRAIQQATAAEPLATPPRHPLNATNGTSQSNISTPLPEPTPGQPRKVSGHNPPSARRLPSASSVKFNEKLKNASKQSIQNENKASYSSYEDSEIQNDDETRTVGTPTETISVVRLRRSSSQSNIEPNGVRSPTSSPTGSPIRRTSGNRWSSGSSHSKKSAQRSVSMSSLNNTSNGRVAKPKPSKSRLIS Q9P7I2 KCC1_SCHPO ACT_SITE 154; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 37..45; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.17; MOD_RES 192; /note="Phosphothreonine; by autocatalysis"; /evidence="ECO:0000269|PubMed:10617667" SPACUNK12.02c; CHAIN 1..335; /note="Calcium/calmodulin-dependent protein kinase type I"; /id="PRO_0000086089" MQQTYKPNTSALKDGAPKATVDQKQLLPCKYRVGRVLGGGTYATVREAVHIETNKMYAAKIMNKKMMEKKQDFVKNEIAILKRVSYEHPNILHLVDFFETVNNLYLITELATGGELFDRICAKGSFYEADAAALMRTTTSAVKYLHDNGIVHRDLKPENLLYRSKDPNSDLLIADFGLSHFYEDSQYYMLMTACGTPEYMAPEVFRRTGYGKPVDMWAIGVITYFLLSGYTPFARPSQVEVIEAILANEYTFNDPCWSGISETAKDFIKKCLENDPSKRLTAADALKHPFLSEKRPATSNLLPNVRENFNARKTFRTAYNAVRAFNTWKKLENKH Q9P7J7 ADA2_SCHPO BINDING 8; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 11; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 26; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 32; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 35; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" SPCC24B10.08c; HELIX 68..80; /evidence="ECO:0007829|PDB:2ELK"; HELIX 86..93; /evidence="ECO:0007829|PDB:2ELK"; HELIX 99..109; /evidence="ECO:0007829|PDB:2ELK" TURN 81..84; /evidence="ECO:0007829|PDB:2ELK" CHAIN 1..437; /note="Transcriptional adapter 2"; /id="PRO_0000324663" MPPQKYHCNVCAQDITRSIHIRCVECVDFDLCIPCFTSGASLGTHHPSHPYRIIETNSYPIFDENWGADEELLLIDACETLGLGNWADIADYVGNARTKEECRDHYLKTYIESDCYPLASVELPGPVDRIAFAARKRARIEAFQPPPIIPQKPLASTPQCHEIQGYMPGRLEFDQEYMNEAELPIKDMNFDDDLHESAKHEMQLKLTMLNIYNSRLTRRAVRKQTIFNHNLLDYRRLQANEKRMSKEERNLLNKTKAFARLLTGPDYQKFVNSYHEQITLKKQISDLQEWRQMGLTTLEQGHKYERDKTQKFLLSKASASYDKQLRHVKSFNQTTSAPFQVRDIQKIVPRKPATPTMFSASADRQLLSEDEQALCSKLQIFPKPFLALKFALISASLTSKKPFQKTDAVNLFKHLDANKVEQVYDFFHNARWIGAPT Q9P7J8 GAD8_SCHPO ACT_SITE 353; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 236..244; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 259; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12805221}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12805221}; PTM: Phosphorylated by ksg1 and target of rapamycin complex 2 (TORC2), affecting the kinase activity of gad8 in a nutrient-dependent manner. {ECO:0000269|PubMed:12805221}. MOD_RES 387; /note="Phosphothreonine; by ksg1"; /evidence="ECO:0000269|PubMed:12805221"; MOD_RES 527; /note="Phosphoserine; by TORC2"; /evidence="ECO:0000269|PubMed:12805221"; MOD_RES 546; /note="Phosphoserine; by TORC2"; /evidence="ECO:0000269|PubMed:12805221" SPCC24B10.07; CHAIN 1..569; /note="Serine/threonine-protein kinase gad8"; /id="PRO_0000085957" MSWKLTKKLKETHLASAIGLNSGGSSFTRGLKNSTLSSTSSRKSSDEKSRKSSEDKRSPQSTVVQPGLLQVTIIEARNLKLPSGHVPANYGVSIDNSLLAPPLSNGSGHARSRSHAWWLPYIVVEFDKNEILVDALNTASLENPCWDYQATFDVSRYSKLSLNIYLRSSSSRSRNGMGNDAFLGGIKLSPSFIVNKLTDEWVPLHGGSGELRVQMLYKPNQSTPLTIDAFELLKVVGKGSFGKVMQVRKRDTSRIYALKTMKKAHIVSRSEVDHTLAERTVLAQVNNPFIVPLKFSFQSPGKLYLVLAFVNGGELFHHLQREGCFDTYRAKFYIAELLVALECLHEFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMAKTDRTNTFCGTPEYLAPELLLGHGYTKVVDWWTLGVLLYEMITGLPPFYDENINEMYRKILQDPLRFPDNIDEKAKDLLSGLLTRAPEKRLGSGGAQEIKNHPFFDDIDWKKLCAKKIQPPFKPSVESAIDTSNFDSEFTSEIPMDSVVADSHLSETVQQRFANWSYQRPTTIDTSDDINTIAPGSVIR Q9P7M3 SLX1_SCHPO COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:19596236}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:19596236}; Note=Divalent cation. Mg(2+) is preferred. Has Holliday junction resolvase activity solely in the presence of Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:19596236}; SPAP27G11.15; STRAND 224..227; /evidence="ECO:0007829|PDB:4ZDT"; STRAND 234..236; /evidence="ECO:0007829|PDB:4ZDT" HELIX 207..214; /evidence="ECO:0007829|PDB:4ZDT"; HELIX 237..240; /evidence="ECO:0007829|PDB:4ZDT" TURN 181..183; /evidence="ECO:0007829|PDB:4ZDT"; TURN 199..201; /evidence="ECO:0007829|PDB:4ZDT"; TURN 229..231; /evidence="ECO:0007829|PDB:4ZDT"; TURN 242..244; /evidence="ECO:0007829|PDB:4ZDT" CHAIN 1..271; /note="Structure-specific endonuclease subunit slx1"; /id="PRO_0000349133" MDLCNFYCCYLLKSNRTQSSGAVYIGSTPDPPRRLRQHNGEIVGGASKTKHGRPWSISCLVYGFPNKVSALKFEWNWQNLGISRYTKDCDFRSKKQKTIMYCLKGLKHLVDSDTWRRWPLNITFLNKTAFSKWNQLGKTYGNINVYFDEEWLNGFHEKVIQKTYDHKLCLRKTISEPVKCNLCYECIESDELRANCPFTDCNSINHLTCLASSFLTEECQVLPIEGMCTKCKRVLRWREFLSTVFTTSLETDERDFESENRIEIIDLELEK Q9P7N2 AP1S1_SCHPO SPAP27G11.06c; CHAIN 1..162; /note="AP-1 complex subunit sigma-1"; /id="PRO_0000316201" MSIKFFLLVSRQGKVRLAKWFNTLSIKERAKIIRDVSSLVITRKPKMCNFVEYKGEKIVYRRYASLFFVCGIEQDDNELIILEVIHKFVECLDKYFGNVCELDLIFNFEKAYYVMEELLLAGELQESSKTNVLSAVLAGDAESEADAQQDSLQKLVGSVKKR Q9P7P2 HOP1_SCHPO BINDING 337; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 339; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 351; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 354; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 359; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 362; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 379; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"; BINDING 382; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" SPBC1718.02; CHAIN 1..528; /note="Linear element-associated protein hop1"; /id="PRO_0000353843" MNSYKEEILQTKSDFTLKNLIFFAISTLCYKRALFNENCYKKVNFEIEHFKGADFDCQLKPTVVSLQAGVDKEADSFLEMMKTYIFSLVSMKVPFTVYLIISSQCKSILEDDAVEKEIFSFTINPGSEEKICCESFVSYQRSERFVIKLFLSGNVKTECKDEEKVVQIITKMERFQLSKGEATKAGVFLNTVETKDCMSWLNRGEFKDIVSFYESNNGIAISHCSHAFVPISTEKIMINKESSLFDSQEKIDSQLEKFLQPLKYDEIGSTQILDEQSVEKSLSQGKCEKMQNESRGLREIKNNNPCEEVKKSNWLKKNISGSDKVDKAEKKKALLNCECGDSTEDSEMFQCERCDGWVHCACYGFESDSDPRQPNQLLCYTCLLVDSESSLYDRMTMLVAYRRAIRCIWASEYQGFQKLAARLNCSYADAKRIEERLVNENIIYKEKKRKWIYFTNKSPEMVSYLREKYFTPSRWISHLNFQNYRQENQRVNMRSFLRPERMEVIERPKKVSKTSNTKETDTMKPLRI Q9P7R0 ARO1_SCHPO ACT_SITE 260; /note="Proton acceptor; for 3-dehydroquinate synthase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; ACT_SITE 275; /note="Proton acceptor; for 3-dehydroquinate synthase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; ACT_SITE 825; /note="For EPSP synthase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; ACT_SITE 1182; /note="Proton acceptor; for 3-dehydroquinate dehydratase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; ACT_SITE 1211; /note="Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143" BINDING 46..48; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 83..86; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 114..116; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 119; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 130; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 139..140; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 146; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 152; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 161; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 162; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 179..182; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 190; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 194..197; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 194; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 250; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 264..268; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 271; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 287; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 287; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 356; /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"; /ligand_id="ChEBI:CHEBI:58394"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143"; BINDING 870..877; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03143" CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03143}; SPAC1834.02; STRAND 1055..1059; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1079..1084; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1094..1097; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1118..1121; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1129..1131; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1152..1157; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1176..1182; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1190..1192; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1208..1215; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1240..1246; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1258..1263; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1267..1269; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1295..1299; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1324..1327; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1331..1333; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1345..1350; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1363..1365; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1376..1385; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1387..1392; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1416..1420; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1439..1446; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1464..1471; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1482..1487; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1491..1493; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1509..1518; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1522..1525; /evidence="ECO:0007829|PDB:5SWV"; STRAND 1538..1540; /evidence="ECO:0007829|PDB:5SWV" HELIX 1045..1050; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1064..1067; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1071..1074; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1085..1087; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1100..1111; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1125..1127; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1136..1148; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1162..1170; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1194..1204; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1219..1235; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1247..1249; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1250..1255; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1278..1287; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1308..1319; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1334..1336; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1337..1340; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1359..1361; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1367..1372; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1395..1406; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1424..1435; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1448..1455; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1474..1478; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1497..1508; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1527..1534; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1542..1558; /evidence="ECO:0007829|PDB:5SWV"; HELIX 1564..1572; /evidence="ECO:0007829|PDB:5SWV" TURN 1068..1070; /evidence="ECO:0007829|PDB:5SWV"; TURN 1075..1077; /evidence="ECO:0007829|PDB:5SWV"; TURN 1355..1358; /evidence="ECO:0007829|PDB:5SWV"; TURN 1407..1409; /evidence="ECO:0007829|PDB:5SWV" CHAIN 1..1573; /note="Pentafunctional AROM polypeptide"; /id="PRO_0000140861" MSNESNIITVPILGKDTVRVGFGIHQYICTEILENFKSSTYVVITDSNIAPLYLEKIESTFNKSIKDAKAEARLLTYVIPPGESSKCRAMKAEIEDWLLTQSCTRDTILIAMGGGVIGDLVGYVAASFMRGIRFIQMPTTLLAMVDSSIGGKTGIDTPLGKNLVGAFWQPLRVYVDMVFLHTLPPRQVINGLSEIIKTAAMWNENDFQLLENNSAVLLDALNKPSVPGEYKFDSIKPLLQKIILSSIRTKCEVVTLDEHEGGLRNLLNFGHSIGHAYEAILYPQILHGECVAIGMVKEAELARYLGILKPNAVGRLTKCLVSYNLPISVNDPKVKKYASFKHCPVEKLIEYMAVDKKNQGSKKRIVILKAIGETYEKHATVVSDDDIRFILSRDVKVDEFTKSSWDVVVTPPGSKSISNRALVLAAMGNGTCRLTNMLHSDDTQFMMSALESLGAATFSWEDGGETLVVKGNGGKLAVPKEELYLGNAGTAARFLTGIAALVSSKDGAKVVLTGNHRMKVRPIGPLVDALRANGCEINYLEKQGSLPLDLSSKNGLKGGIIELAATVSSQYVSSILMCAPYASQPVTLKLVGGKPISQLYIDMTIAMMASFGVNVTKSTTEENTYNIPCGKYQNPPHYEIESDASSATYPLAIAAITGTKCTVPNIGSASLQGDARFACDVLRPMGCTVEQTATSTTVQGPPKGTLKPLESIDMETMTDAFLTASVVAAVACNVSEGDPVTRITGIANQRVKECNRIAAMVHELAKFGVRTGELEDGIYIFGKNYKELKKPEEGIYTYDDHRIAMSFSVLSLICPSRTLIIDKACVEKTWPYWWDVLHQSFGVKLTGATSVASDPLKGSISKNASIILIGMRGAGKTTIGKIIAKQLNFKFLDLDELLEDYLEMPIAEVIFRMGWDAFRLEEHKVLRKFITEHPEGYVAASGGGVIEMDESRNLLSNFVKEGGIVLHVHRNLEHIKSYLSEDQTRPTYKDQESIDDVYKRRHVWYRECRSHYFISPVLSNQVIDEKIQYSMSRFLDVVTGSSQVLQKFKTKKRSTFLTLNYPRIEDALPTLRDVTVGCDAIEVRVDYLKDPKSSNGISSLDFVAEQISLLRCSTTLPIIFTIRTISQGGLFPNDKEEEAKELMLSAMRYGCDFVDVELGWSSETINILYQHKGYTKLIMSWHDLSGTWSWARPHEWMQKVELASSYADVIKLVGMANNLNDNLELEEFRTRITNSMDIPLILFNMGRFGQLSRILNKFMTPVTHPLLPSKAAPGQLTVKQLNEARVLIGEILPEKFFLFGKPIKHSRSPILHSTAYELLGLPHTYEAFETDTVDEVQKVLNLPDFGGANVTIPYKLSVMKFMDELSDEARFFGAVNTIIPIRIGDKLVLRGDNTDWRGIYDTFANALDGVSLRDTNGLVIGAGGTSRAAIYSLHRLGVSRIYLLNRTLANSYRVQDVFPPDYNIHIIDSDNIPSEELSSVTLSAVVSTIPADIELPEKVASVIKALLANKADGGVFLDMAYKPLHTPLMAVASDLEWKCCNGLEALVRQGLASFHLWTGMTAPFDAVYQKVIE Q9P7T4 MRC1_SCHPO PTM: Phosphorylated by rad3 and tel1. {ECO:0000269|PubMed:14585996}. MOD_RES 604; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:14585996"; MOD_RES 645; /note="Phosphothreonine"; /evidence="ECO:0000305|PubMed:14585996" SPAC694.06c; CHAIN 1..1019; /note="Mediator of replication checkpoint protein 1"; /id="PRO_0000096573" MASLDENADELHRMDSSDEASINDDQEDILDTPRTRVRKMLASVDMQLSSNAVSEASLDKESTVGNLENQKNRSYSSEIYLHSDTNFLSNFDSAYERVRRLLNQQGGKSSLQKKEVEQIETQEGGDNAKGSPSSENKDSDRNSRLQQLIEKKRNALKKEQEDLIQNSATSHSKSDNLDSESADDSDLADESELSKKYTSDRKIRNASKKALLELHRNTARLTRETALKPEVVVKKKVTLREFFQKIGFKNDNQLENKAISEEEANSTEPPNVEKEEPKPSVDRSTGIVNSEDIKELSVEDDSLELKEITPEALDIGQTSLFTTLNQTQVKKEDNKKFLLKEINAKLNEDDIDSELEIEVKPKTTALDNIEKSKLSEENEHGIKGKLKQLAEIKLSKDGKPFENEFNIKSFNRNLVKRAAVMAKLQRNQLEEELKAKGIYKPTIQGEKEEEEDPLERARNDAEKIRQLEKASGNASDEGELNDEEEVISSSNTPSTKAKTTNKVIISDVIIEATQAEPKRRQKNSRVVFDEEDLTGDSHGSSNMKISESDDESNGDMIRDSFDRLSSESIKDSQKTEELHDSFGINDEVDQSTSLYVQNSQPSASQLTIVDATYSQPPPRWESSSRDDKTNTSSTQPSQVDSLVPTQLDSTIPTQIDSVQRNKDQDDEEILEERRESRRDSKTFLSRTMLYNKDTGKADSAWASDLIEEQAIESDDEYAGIGGLSDDGLSDSDAELEVQNMIDDETTIQKGEVASMAQFAKDQEMDRDEKLVKQLMKDVTTGALRKRNRNGFAALDDSDDEDYSNLRREKLKELRRQKLLEDGNLNVLEGDKRKAFLATVEDSLVSSKDNLTWLDATVEDSGVGSSDLGDEYLYSEQSLNHEEEEQMEEELSEIFSSGGPNVVDRVYLKKSSTRHTSDNNSLEEVLPIFPGVRKLVSNSQSEKIGDLSNDNSMGAKSYKTPIISSTQRPQGRKFRGLMNQSSKADISRTVDAGSIKVVPNSQSANPPRLLASLNNYSDFD Q9P7V2 ABC4_SCHPO BINDING 648..655; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 1246..1253; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:Q9C8G9}; SPAC30.04c; CHAIN 1..1469; /note="ATP-binding cassette transporter abc4"; /id="PRO_0000331223" CARBOHYD 386; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 510; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 615; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 691; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 790; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 815; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 923; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1007; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1355; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MENFHHRPFKGGFGVGRVPTSLYYSLSDFSLSAISIFPTHYDQPYLNEAPSWYKYSLESGLVCLYLYLIYRWITRSFTVKQTVGSEFSGLRKAHGILLWLLSILFLGMTAFMFVNDAFPTAFSDPPVKICLLAYSVHLFLLHSLRMIYPRARPTLYHAAVLLNLLLLPPIFHFYSYPFFFVDHPPLSSYSPFLWFYFFITIVGNFIPLFTPRVWYPLFPEDNYQPSAEQVCSMFNFACSYGYLNPLVLTAKRRVVEVDDTPVIPDYDKNKAWTYRFERMKTPSLFITIHKIFWRQILGMGVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNPLVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVIRSRFVQNKSGDSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATFVVFTTIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRVSDFLNDPDEVDPVNTIEDTSQEIGFFNASLTWVSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNGSAFPVTDKSSPLLFLAEQAASASEAAAPDLAAIPIPNEVDDAEAADEKDGKLVEEEQRVTGDVVFSEIFSYMKHFGSGFYVAAVLLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNNKFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAIAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYSKLPQEPAPTIAGQVPATWPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRMCDGSGITFLPPETRGSKSA Q9P7V9 UBP9_SCHPO ACT_SITE 50; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 375; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 505; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 549; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1703.12; CHAIN 1..585; /note="Probable ubiquitin carboxyl-terminal hydrolase 9"; /id="PRO_0000080610" MSLLRWMGMNSPGSTDRRKSTWEAELPKPSIRPETLTDRFYGLTNYGNTCYVSSVLVSLYHLKPFRDSLNSYPLPSAPPNFKSVCTKTNHPESSSSRHSKKKSMENRKSSLYGSNGINSCGCVDISNVGSESGTKHQIVVGESNCSAYGMKENIYTCLKDLYCSVSCCDCRYGICSPERFIQVLRRDNEAFRSTQQQDAHEFFNFLLNSVTETLDEYYGNHSDVMHPKWVHSLFEGTLTSETKCLTCENITSRDESFLDLSIDIENHTSVTSCLRSFSASEMLSSKNKFHCDVCKSLQEAEKRMKIKKLPKILSLHLKRFKYNETQEGHDKLFYTIVFTNEMRLFTTTEDAENAERMYYLSSVIVHVGGGPHRGHYVSIVRTKTYGWVLFDDENVTPVNENYLQRFFGDQPGQATAYVLFYTAADEEDDDVSEVDTKESIKPMSIPSQLKQESVEVSNLSSTPRSNSTITYPDMDPMVASFSSQYSHKTLDRDINSRSYFDREPSLDAERFHSRSVDASPKAVRRESRSFFPSLTRKRSKFFGSSQSNSPKDSPLRDTHKSSDEHSESKHSHTLPWQFSRSRSKR Q9P7Y8 MID2_SCHPO MOD_RES 379; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPYUG7.03c; CHAIN 1..706; /note="Septin ring organizing protein mid2"; /id="PRO_0000096484" MLMTASQQDQHAKMYLADIHRALRIPSPIPSTDYECSDYASTIASISRESTMRNFNRSNISSTAPSFAESEDAEDGDSFPYDQTLSNSSSFDDHQSLLPFSTEVRRTPTYSVMNETDSSSTSVEDVNKENILSLNDSCLIKLSDDEASNKSSRSSTPRNSIKSNSSNQGHGDIPIPKKNPARSVCNSKLFNEDTLPAEFEEVSISPPVKLELPTHSHNSSDTSFTNSIVSSVSDMVGLGEGINSIASFGFSEDSSSFQDIKTPPRLSFADENRENCRTDIYRSDSIHEYEEPLTSSITSLDSPHVLDENAPIPLLPKVVSLPDPRFTNVLSAFDALTRTYLLRQNSKVVHATSQKQEMQTSRRVVNSCYMPESLSRNLSSSLQQTGGSGRLFVRLMEIRNLTIPLASGMTTRFTYTISGKHIQVPWNALHSTTKIENEYTFDESISSSIVCTLRAAYDPPKVRTRSTLGKVFSTNKRKSMTTDPVSEALHGFVSEDGTFGEVTINTDSVSRTALGRCQSMVLPIMNKWTVDPAAKDVKPLPRKVGELEIHVFFLPALPVSLKELPASIESAMYDLKLAEWDRTLLCDGYLCQQGGDCPYWRRRYFQLIGSKLVAFQQFSKVRRATIDLSEATHIVDDNHYSDEEELEGYLYFESGFRIIFSNGDYIDFYAETVGEKDEWMSTLRQHLGQCSMVHKNWTKSFLSLSF Q9P7Y9 SIN1_SCHPO PTM: Phosphorylated; under environmental stress. Either Ser-61 or Ser-62 and Ser-298, Ser-299 or Ser-301 are phosphorylated as well (PubMed:18076573). {ECO:0000269|PubMed:10428959, ECO:0000269|PubMed:18076573, ECO:0000269|PubMed:18257517}. MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 404; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 502; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 530; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573" SPAPYUG7.02c; STRAND 258..260; /evidence="ECO:0007829|PDB:2RUJ"; STRAND 265..267; /evidence="ECO:0007829|PDB:2RVK"; STRAND 290..292; /evidence="ECO:0007829|PDB:2RUJ"; STRAND 308..310; /evidence="ECO:0007829|PDB:2RUJ"; STRAND 312..314; /evidence="ECO:0007829|PDB:2RUJ"; STRAND 346..351; /evidence="ECO:0007829|PDB:2RUJ"; STRAND 357..363; /evidence="ECO:0007829|PDB:2RUJ"; STRAND 378..382; /evidence="ECO:0007829|PDB:2RUJ" HELIX 279..281; /evidence="ECO:0007829|PDB:2RUJ"; HELIX 317..330; /evidence="ECO:0007829|PDB:2RUJ"; HELIX 338..340; /evidence="ECO:0007829|PDB:2RUJ"; HELIX 371..373; /evidence="ECO:0007829|PDB:2RUJ"; HELIX 385..394; /evidence="ECO:0007829|PDB:2RUJ" TURN 273..278; /evidence="ECO:0007829|PDB:2RUJ"; TURN 282..285; /evidence="ECO:0007829|PDB:2RVK"; TURN 343..345; /evidence="ECO:0007829|PDB:2RUJ" CHAIN 1..665; /note="Target of rapamycin complex 2 subunit sin1"; /id="PRO_0000218770" MELTREKVLLLTFLRMQYSHILPDSIENRVISTEAPEWELDKSLQDLLIHDYDYSKTSFSSSPPIVANDTVSNVRKPSDTKQVNGAGGQVNHSRAEDSDYATSDLSESSDVGDDDNSCIFSFSKVPMQKDVASIKEEERLDPKISTLNNIDAIANLKLTNMVESSQAVNLTSSKQSSINQQSSVSTDYDDLRSISEESFHLSQGEIPLTFPMNSSLTDTEADAVVAVDALFPGKQRGTHNTVNKARSVSNAKAPTSALRALLEHKENSSQNGPLAENFATFSGHAESNALRLNIYFPSSESPSKPLFVELRKNVLVSEAIGYILLQYVNQQLVPPIEDEAQNPNYWNLRIVEDDGELDEDFPALDRVGPLSKFGFDAFALVKATPAQIKENQAAYPFKSKHPTSIPEANNKTHIRHTSSTSSQSQKQAQDVKDTLNTSHVVQVRLPPYGDNARFCNIEISKTTRLAMVLNQVCWMKQLERFKYTLRVAGSDTVLPLDKTFSSLDGNPTLELVKKKVRDKKGSTQQLPTSSPQNSVYGSIKKDAQSSTYNATDIMSSNTYQEFLVWKRQPVSFMGRHERLLAIDGEYVHIMPSESKNIFETPKTSSIHAGSIILCKQSKKSPCNFKMIVSKNRETKRYDFEVLSALEAAIIVSRIRALMNTVKKIN Q9P802 MIS18_SCHPO BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01129, ECO:0007744|PDB:5HJ0"; BINDING 28; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01129, ECO:0007744|PDB:5HJ0"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01129, ECO:0007744|PDB:5HJ0"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01129, ECO:0007744|PDB:5HJ0" SPCC970.12; STRAND 21..25; /evidence="ECO:0007829|PDB:5J6P"; STRAND 31..34; /evidence="ECO:0007829|PDB:5J6P"; STRAND 38..42; /evidence="ECO:0007829|PDB:5J6P"; STRAND 47..51; /evidence="ECO:0007829|PDB:5J6P"; STRAND 58..60; /evidence="ECO:0007829|PDB:5J6P"; STRAND 68..71; /evidence="ECO:0007829|PDB:5HJ0"; STRAND 73..79; /evidence="ECO:0007829|PDB:5J6P"; STRAND 85..93; /evidence="ECO:0007829|PDB:5J6P"; STRAND 103..107; /evidence="ECO:0007829|PDB:5J6P"; STRAND 111..115; /evidence="ECO:0007829|PDB:5J6P" HELIX 35..37; /evidence="ECO:0007829|PDB:5J6P"; HELIX 43..45; /evidence="ECO:0007829|PDB:5J6P"; HELIX 55..57; /evidence="ECO:0007829|PDB:5J6P"; HELIX 96..99; /evidence="ECO:0007829|PDB:5J6P"; HELIX 108..110; /evidence="ECO:0007829|PDB:5J6P" TURN 26..28; /evidence="ECO:0007829|PDB:5J6P"; TURN 80..82; /evidence="ECO:0007829|PDB:5J6P"; TURN 100..102; /evidence="ECO:0007829|PDB:5J6P" CHAIN 1..194; /note="Kinetochore protein mis18"; /id="PRO_0000116562" MSQTETSHSGYIDFKKESQPSVFQCKKCFQIVGDSNAWVISHREYLSFTLSDAVENSVRVEDTFKRSDDGLCVYSELSCTRCNEVIGKVYNSTPIYLDDIRDMYTFSMDKLQAYQLGNKTVNPEGLTRYQVDLEMREDIIKLKSFCLSLYEKFELHDETLRSVKETISSLKKPKIEGKEGKKEKARTYSKRTRK Q9P805 DCP1_SCHPO SPBC3B9.21; STRAND 23..39; /evidence="ECO:0007829|PDB:5J3T"; STRAND 44..59; /evidence="ECO:0007829|PDB:5J3T"; STRAND 64..74; /evidence="ECO:0007829|PDB:5J3T"; STRAND 77..80; /evidence="ECO:0007829|PDB:5J3T"; STRAND 87..90; /evidence="ECO:0007829|PDB:5J3T"; STRAND 93..98; /evidence="ECO:0007829|PDB:5J3T"; STRAND 102..110; /evidence="ECO:0007829|PDB:5J3T" HELIX 3..9; /evidence="ECO:0007829|PDB:5J3T"; HELIX 12..19; /evidence="ECO:0007829|PDB:5J3T"; HELIX 84..86; /evidence="ECO:0007829|PDB:5J3T"; HELIX 111..124; /evidence="ECO:0007829|PDB:5J3T" TURN 40..43; /evidence="ECO:0007829|PDB:5J3T"; TURN 99..101; /evidence="ECO:0007829|PDB:5J3T" CHAIN 1..127; /note="mRNA-decapping enzyme subunit 1"; /id="PRO_0000339336" MEDENILRNAVNLQVLKFHYPEIESIIDIASHVAVYQFDVGSQKWLKTSIEGTFFLVKDQRARVGYVILNRNSPENLYLFINHPSNVHLVDRYLIHRTENQHVVGLWMFDPNDMSRIFNIVKESLLR Q9UQX0 SODM_SCHPO BINDING 50; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:P04179"; BINDING 96; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:P04179"; BINDING 181; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:P04179"; BINDING 185; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:P04179" CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000250|UniProtKB:P0A0J3}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11350071}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:11350071}; TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000269|PubMed:11350071" MOD_RES 129; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1486.01; CHAIN 22..218; /note="Superoxide dismutase [Mn], mitochondrial"; /id="PRO_0000032887" MLRFLSKNSVAAIRNVSIARGVHTKATLPPLPYAYNALEPALSETIMKLHHDKHHQTYVNNLNAAQEKLADPNLDLEGEVALQAAIKFNGGGHINHSLFWKILAPQKEGGGKPVTSGSLHKAITSKWGSLEDFQKEMNAALASIQGSGWAWLIVDKDGSLRITTTANQDTIVKSKPIIGIDAWEHAYYPQYENRKAEYFKAIWNVINWKEAESRYSNR Q9UQY9 SPO4_SCHPO ACT_SITE 182; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" BINDING 46..54; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 95; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 264; /note="Phosphothreonine"; /evidence="ECO:0000305" SPBC21C3.18; CHAIN 1..429; /note="Cell cycle protein kinase spo4"; /id="PRO_0000086673" MLSMLLPFGNSGVYASDVDREDRPEIAKLVQAFPTIEEDYHVVKLVGAGSFSSVFKAVDRHFDSYDNSYWISSQIEDQMPHDKTKRPKNHFVALKRIYATVLPSRIQTELEMLHELRGSDCVLNMITAVRHQDQVLIVLPFIQHAEFRDFYMKYSLPEIGAYLRDLLKGLAHIDAKGIIHRDIKPGNFAWNPYTQRGVILDFGLAQWQEADAPTENCCVDKLRKLKQEGKYYDYFPFEKTIADPPEGYLLHDPRPTKRADRAGTRGFRAPEVLFRCQNQTSSIDVWSVGVILLCFLTHRYPFFRCEDDIDAIVELAHIFGRNGMSNCALLHGQIWSDNIPTLLDQKHNWLDLIASITKNDENLILETSSDYQVALAIDLLDKLLELHPSKRVKAKTALQHEFFNACGVTRSGFEAENPFRSDFPSTVEQ Q9UR17 VTC1_SCHPO SPBC21B10.04c; CHAIN 1..122; /note="Vacuolar transporter chaperone complex subunit 1"; /id="PRO_0000057948" MSTQPLLQTTPGKRIALPVRVEPKVFFANERTFLSWLSFAVVLGGLSVGLLNFGDRIGKISAGLFTIVAIGTMGYALGIYHWRASAIRRRGSGPYDDRLGPTILCFVLLAAIITNFVLRMLF Q9UR39 HST4_SCHPO ACT_SITE 184; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" BINDING 65..84; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 153..156; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 192; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 195; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 214; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 217; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 273..275; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 303..305; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 323; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPAC1783.04c; CHAIN 1..415; /note="NAD-dependent protein deacetylase hst4"; /id="PRO_0000110278" MKVEEHVPLIQESRKRKCQSSENASKRQQLLSKLPLRLHTGNENVDLSPLVSAIRKAKRIVVVTGAGISCDAGIPDFRSSEGLFSSLRAEYKLNCSGKELFDGSVYRDLKSVNIFHAMIRKLHMLSNNARPTDFHLFLSQLAQESKLLRLYTQNIDFLETRLEGLQTCIPLPQSAPWPTTIPLHGTLEVVSCTRCSFLKKFNPDIFDRNGVTVCPDCKTENEVRRIAGKRSVIEGCLRPRIVLYNEIHPDSESIGSVCSQDLKSRPDCLIVAGTSCKIPGVKRIIKEMSNCVHKQKGNVIWLNYDEPTKDFLNLCDLVVQGDLQIAIRRLKPLLDAPSWKLKSHSAKRTSKQKSSEQTKITSSTKITKAIGLNTKSNDSSKKDNTSFQLHQVLNSIEIPKVEIKQEVEYATPSPL Q9URT4 AMS2_SCHPO SPCC290.04; CHAIN 1..697; /note="CENP-A multicopy suppressor protein 2"; /id="PRO_0000083474" MMEKSLNTVTSLPLRVIYCIDRASAIRCLAKSQHAVPIQVLKEVEPKKVICQVDIQHVIQTVCRCSPELSCKSQGDFSVYFLDHTEPDELFVGLGYWSSLLLSPTLNAGTSNSDTVWVNGFIVEFGIQRSIEIKLRFQSLQNSFEVGTPETHTSSKFLSSTLPPSLIFDPSSSEKSDSISGSLFDTNYTCPVNINGLSKQKSVRELKSPSRPSALAETNVEELELDSLFHASNDISCSATSFSEPYILDHQAALDHPATDPVCSASSTTVNSAVSTKKRRRESSTISPESAYVAAQLQNPSEREQVHEFIKEQVRIARGRIEKKFTNVRGKNRIEEQLTLSLQEGKIPPYCQNCGTIKTANWRNATYMNITLMLCNACGIYWTSRRSMRPRNLWSTYKAFETEKPLENDAFAQLELAVYKLSQQRKLSISIFRELENAGRHSPLNRLTSLDSTHSAPDPNHISKPSVVNQQKSRGGPRTAKLKNDLRRIQSSPIVAPTPDTSFREPLSEIGSNDSWLVLPNSLSANIQNDVLRKTDFMCTDKENVAFPLKTTTKPMPKVNKEETEPTLPVCDSEKENDDLECYFRTPPKPTTLQKQQQSPSPWRSELFLSDPDQNVLTPRHKPKFDLSKALSSVAKSNNIENSPQLPERYDFSLELGLNSQLDNEERRDIPLMTDLVMPSSPPMVPADRHLSVENTC Q9URU2 DNA2_SCHPO BINDING 450; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 679; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 682; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 688; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 954..961; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; PTM: Phosphorylated at Ser-219 by cds1/check2, leading to association with stalled replication forks. {ECO:0000269|PubMed:22682245}. MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:22682245"; MOD_RES 219; /note="Phosphoserine; by CHEK2"; /evidence="ECO:0000269|PubMed:22682245" SPBC16D10.04c; CHAIN 1..1397; /note="DNA replication ATP-dependent helicase/nuclease dna2"; /id="PRO_0000080710" MFNDQSKTTSSVKGICATTDNNHGNLKKTNSTPFRKNYLLNGRTKLKLENFAYNASTEISSPKISEKKHSSLPIKRKNTFNESSTSFSPFTKAHKEITDDLKPDKSFTRKSDLNSQDMPVCFQETSKDLCRSSSTQHLLDHQTTDSTIIDMKPVSTNSKSDVFTLYTDETVLLRRCASDNKPLINNNLSSSNVSENQSRSFGSYDEVKNQGNNLHKVPSLVSIIRNARSSEQSRIAANSSCLLKGSDTEIDEDDFALEAEDLAALDSLERQYSQLPNSTVTASAKDIEKTAKVNHVGGDLQSYCSATKASDATINEEPVNLALDKACNSLPDINSDFIDDWDDSCDGCTPGELCEFSSEYTVLEVHEDFIFHEGNHFRQLKLILEANDILHQLFLRGDWTETSIFVGDSIRVEATFDKDNTAIVDNDKGLIIIHPKILMSATAVASSFPCLRKAVISDRVGIYGPPTKAMVTGNILHDFFQHALYRGIDALENVDINLETSIKTYISDIYFADLSLDEIREELDARLPLLKSIVERYLISKKNDNNNESIHISRLLDIEESIWSPRFGLKGNIDATVEVVLTEKPESSSTLTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENSTIKNLVASNSQLRGLIMTRNSLAQHNFRRSLPEMISNRKICDHCSLVSECLFFQKMSDKGVANSNGLTESWNEWMREVKDEDLEFYKKWEKLLNQEERLLLLKRGDVLTFDTEELEAYGKTLYPLYITKEDIVCLEIDDRVFHYKFAFLNDNGYPRNFLHSGFSVGERVFISDEHGHWSLAKGHIVHIQDSCIEVRTRHRLHIPWLKMPNFDFKKNQVFFGNYEDSKLSFIGSNHTRYRIDKDEFSSGIASIRGTLMSSVLPDAPLIIRDMIIRLKPPKFCNSALIDPEFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHKIHPLVKEFCLTEGTTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKDGLSLSLFKLLSEKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQKKLILPKAHLSDGLPDSSSSLHWVNKLINPSHSVIFFNTDDILGVESKTNNILENHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKSFTEIEINTVDRYQGRDKDIILISFVRSNSKNLVGELLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLEKNKWIFTLNENDIATKFDENSSPIKDCSQVATTNNAKVIIRKNQRFFNSDNLCEKAILPQLEF Q9URV2 APC1_SCHPO SPBC106.09; CHAIN 1..1458; /note="Anaphase-promoting complex subunit 1"; /id="PRO_0000215874" MLELKTNVIQDPELKDSLDLQENDRVEIIGDAVHYIVNDHLNRVFNYTVDQQKIHAALITTFASGKKAIVVILDDIGYVYYVGDNNNDSYIINVPFSTESAWSSPSGLYLQRHRSSDENLNTDLPHIFCLNDPLDELTLIKFDGKKILSLFDSIVYVVGEIVVTHNKKEKKLSFWRSRFIDPESDQSIKSSRNRRRESSFSREKNPDLTRSDSIHYTANTRLSEKFEEQGLAYSTIFSHIESFPITGSTSFDSILGNGVLVITTLVKELEKGYMMLFRLVRDRSPYFLDSLQLHAINLSAIKSKHLQKIVVLSSKGKVSLESPMSPSLPIEGTFRSFRVHGATLYLEDTDGVQRYISLDNRASNSLVKWCLSVIRYVLPLREYEIFYTGHLYALFAFKLSHDEAFISSILACFTFFSRDKVHVEPIEDCNEAYSLSSKFHFKKEILIASQLSSHLDYSTFKNYLMPLAITLHFISEELRLDSVVKPRKDQLVALLLQITTWLKWPRYCEYYNFDIAETFLSIPLSIQVDVEEPVGPTSILQWIIECLRSQSTVPFYGLESYGLPHSCSTMFPQTLSLMQLLDCLLNPNMTLQNLVEEMVRLGISRKRCERYPFGILCIIFTVLEIAAEEYSPNWESEELRLVNRLDVDSFLHPKTPKWVFNKQDQEVKEIKALTSTVTDSTLVDTQSFHPYKVVTDMIFREDRRLAEVNKLLNYSSQITIMTEHFDVDLSSVPMQQKVAQCICVRTLSVPIGAGMLTYGSKNPLPTEKVTPRLFNFTLHLHPGTLIIQPNKEFVTQELTEWPEFNVGVALGLSISKFSKEINTSWIMFNRPETLTAYHAGFLFGLGLNGHLKALATWHSFIYLTSKHDTTSIGLLLGLASSYLGSMDAKVTKLLSVHISALLPVGSNELNISPLTQTAGILGIGLLFHDSCHRRMSEVTMEEILASNESELKNEGYKLAAGFSLGLINLGRGSNLPGMSDLKLVSRLQVGISSQATFQSLEAGSPGAIMALTMIYMKTNDLEVAKKIDIPKSRYLLDFYRPDLILLRVAGKNLIMWDEVKADYEWVKYQIPDIMLSQFDLQEKKVLSSDDLLLYNVLAGICFSLGLRFAGTGNPKAKEILINFLDSFIRLCHLPAKTHDERVTAVTVIRCTQIVALSSSCVMAGYCDLDVLRRLRVLHGRMEPVNYGAQMATHMALGILSLGGGRYSLSRSNLAIAALLISFYPQFPRTTQDNRAHLQAARNLWALAVEERCIIPRNQDTKQPCIVPLNVVQKSGAVQKLEAPILLPPYDSISSVSTLGDKYWNLKIDLDNNSDYRELLRESQTLTLMPYDRTSSKEEPLNLFPKLKDTSSPLWNLVKTSRLFQSSNSPLNVASLQESNNKTSLGVKLLLSMDFDNLTRDRLLSLQILLQFFESCWTGVLLNKFHSRQYLFLSRDLVEDLSLRVWEYVYSHNHNEESV Q9URW7 VPS17_SCHPO SPAPJ696.01c; CHAIN 1..549; /note="Vacuolar protein sorting-associated protein 17"; /id="PRO_0000339647" MSSQHSTDDLMNSHVFSGGFSTLDDKGFQDVPIHTDMPGSISVEPSSEDANVGSVNGNINETPVFEADRLIAEATMNPSAASSTTGENSISQTGSGPFLRIRIVDIEAENSKDPVIKMNVQTTLPAYRSKLYKNVRRTHAEFKKFAKYLISTHPECLIPAVPEAKTSVSSGIKEDLIYLKSGLQSWLNYVSTNPNLLYDPELQLFVESDYGYSPLINTGNPTSGLKRKALKQFPLPPDPCQALANLRPIVKSFYKNAKDAEIKLEKLVNRKQSLALTHADLGQSLIDYSVEEQHNGLANALNRVGKMLQAISDVRIMQSSKQLVTLADSLCYASDNAFVVKEILSNRHILMRDLISSKNQTNSYLSAANRLQDSPKISKARTDDALQALEVARVHEKLLSDKVDFVTLNLVKESKTYTKKTSVSLQKAIREYVEKEAYYERRLLSIMESIRPHIRNIDPFGGLSRLGREEYPRRLSNPPPSQKTNQDAWTNRKRPGYSSSFDGSSQSTFNPSNNDGAHNTSENADELVEPPIGNERLDPKSVANLLNAI Q9URY1 PPK16_SCHPO ACT_SITE 148; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 37..45; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 60; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 231; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC890.03; CHAIN 1..672; /note="Serine/threonine-protein kinase ppk16"; /id="PRO_0000256818" MKKNEKANISASYNDLIATICNPRISDVGTYRIESVVGEGSFGKVYLAAHLLTNTKVVLKSSCRKQAIILAREIHHHRRLLHPNITRLYEVVCTEDRIYLAMEYCPNGELYDWVAREKRLDEKTTCRIMWQLCCAIQYLHRQGCVHRDLKLENIFLDKAYNVKLGDFGFSRDSDCSRRTFMNTRCGTVAYCAPELVQGHKYIGECVDIWSLGIIMYALLIGRLPFDEDDVSLTEQKIINECPQYPETLSKNSSSLLKSLLCKDYRLRPSIDQIISHPYFKENGYHSSSIRDPRPSSKAEEKVRKRLEFVGVDMDQLNASISQQRCDMFYGWWLLLLEKEMRKENKKKKGLFHLHKGSSSAVHIAPATPSLKTAQVSVMSNNQDSLKSRHTSSDSSNSLLSTFRSWLFDPKQKHTADTLSSSAIRPRTPSPSAENYLTQENFDSDNLSESLDNSVENLTVFPSINSFGRRHSNLPQTTHVDTGEQNTPFTPPLLKTVNLDGNKDFTFPSNSQNSPSKSSNLSINIDIPPSPLQNTVISPQPTRRSRTPIRSLSGRSSVASSRNSSRTRSYSNVSSASSNSLISIISSKPSSSTVQRQTPFHSPFERLHKSFHFPSGEPFNTRINATAIFTVGSGRKNPQSSSSLMFNQSSVKEEEEPEETSFSDSSKHFTDLL Q9URY2 ALP7_SCHPO MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC890.02c; CHAIN 1..474; /note="Microtubule protein alp7"; /id="PRO_0000064570" MSDIVSSSTDYSRRSPSSSSIGTNETDHTGFHEKRQGASSESLIPPAQRSSEESMPAPKLFPKLTSKPNPQLNLKDTLNKRVSDRLQALELNKSFDFSGTPRPMHPISHPLSQHKTPEFKHRKRNVESILTPKNPSLFSSSNAASQRGSLNTAPSNFAYSHSSSLQTSASSRPPVLSNGSFPRQTNTAPLNPPVHLKDNIRNSATPSTSQADIPTQYPINSTQKQQAKYEAEIEGYKAKLAGTYHEISVLQNTIVNVSGQLIAVNDQLQQLRSGKASTSPSTKDTNMRLVEGHNEETLALQRGKYTQEEVDKLIQERMEKVAEDLHAQYSAKHTQKINAFKANYARKYEATIQELQNQIGTAPNAPKISNSNWEEERRALKADNQTLQKQLEKAIQERQDMSDFLNNFKADMAKSDKLLMQQQSQQTGDLETLRLQLQALQEELRVEREERQQLIQMSEDLVIAMDQLNLEQKS Q9URY5 FHP_SCHPO ACT_SITE 124; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P24232"; ACT_SITE 167; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P24232" BINDING 114; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="proximal binding residue"; /evidence="ECO:0000250|UniProtKB:P24232, ECO:0000255|PROSITE-ProRule:PRU00238"; BINDING 216; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P24232"; BINDING 232..235; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P24232"; BINDING 301..306; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 421..424; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P24232" CATALYTIC ACTIVITY: Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate; Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.12.17; CATALYTIC ACTIVITY: Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate; Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.17; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q03331}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q03331}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:Q03331}; Note=Binds 1 heme b group per subunit. {ECO:0000250|UniProtKB:Q03331}; SPAC869.02c; CHAIN 1..427; /note="Flavohemoprotein"; /id="PRO_0000280219" MSSVEVNRENADVANTNRQANLAEGYEIKELNESQKQYIRSSIPILESSGVNLTKAFYQKMLGNYPEVLPYFNKAHQISLSQPRILAFALLNYAKNIDDLTSLSAFMDQIVVKHVGLQIKAEHYPIVGHCLLSTMQELLPSDVATPAFLEAWTTAYGNLAKILIDSEKKVYQSQPWNGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYKRSEENVNRPLLCFAGGIGITPLIPIIETALLDGRKVNFCYSSRNYVSRPFKQWLEQLKLKYKENLKLKEFFSEESSVTKEQIVDEVMTRIINEEDLEKLDLSECDIYMLGPNNYMRFVKQELVKLGVEPNKVQSEFFGPYIP Q9URZ4 CAT1_SCHPO MOD_RES 29; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 30; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC869.11; CHAIN 1..587; /note="Cationic amino acid transporter 1"; /id="PRO_0000054179" MSHSDFNMEPEYVSFSDKDTKSILNESKSSLKDVKPSLEEKSYITPGLVDDVEPKGKNFVVRFFDDFKPAKATGEDGTALKRSLKSRHMQMISIGGAIGTGLYVGSGSSLADGGPASVIINYSLIGIMMFFIVYALGEMAVAYPVAGGFNTYATRFIDPAWGFAVSWNYFINYFVTFPLELTTCAITFRYWTDINSAAWISIFLVVIIIVNLFGVRAYGEVEFILSTVKVVATFGFIILAIIINCGGVPTDHRGYIGGSIIKHKPFRHGFKGFCSVFTTAAFSFSGTEVIGLAAAEVDNPQKALPHAVKQVFWRIAIFYVVSLILIGLLISPDDPNLMGNGSTSVSPFVLAIKEANIKGLPSVFNAVIIISVVSVTNSSTYTAGRTLHGMANLKQAPSFFKYTDRLGRPLLAMIVVLLFGFFAYINEADKNGNDVSDTVFNWLLALSGLSNFFTWGSICLCHIIFRLAFKKQGHSLKELGFVSPMGIWGSCIGLFFNILCLMAQFYVSLFPIGGKPNANDFFQGYLAAPVTLAFFIGYKIYDRSHIPSLDKLDITTGLKTYENLDEEEDEPTTASKRIFKKISSVFC Q9US03 KAR3_SCHPO BINDING 473; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 475; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 479; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 543; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 566; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 567; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 568; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 569; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 570; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119"; BINDING 778; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17119" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P17119}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P17119}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + a kinesin associated with a microtubule at position (n) = ADP + phosphate + a kinesin associated with a microtubule at position (n-1, toward the minus end).; EC=5.6.1.4; Evidence={ECO:0000250|UniProtKB:P17119}; SPAC664.10; CHAIN 1..817; /note="Kinesin-like protein 2"; /id="PRO_0000125386" MEEEGHKSLTSHLPQSSSSLSQSREIAKEFTSNIPPPTIKTNSSSSNILKPRLSLQNEVNQLKPAKFPSKMLPPGSLASVKSSSLAKKARPFTASSNPRMPKSAHPISSRSVSASSHFGRPASAVSSSLNSSDDVRSMSDESMESYNDEKSVNASALRTTEDRLRSMEMAYAQLSAKVIPSPSKRPANYKFYEQRIAMLEESLEVERSRTSELQEQFSVALREKAEAEANKIVSQKGMESLEIMLNSMKSENHQRMAMLEENHARVMETAELQHQAELQDFASNIEQKANSLIMEYKNELQSAEEHFSHKIKELTSENELKISRLQEEKDSLLKKVQEGASLAMQRVQNKHDLEKKRLQSAIQPLQEENNSLKQQIEQLQRELASETVVKENLKSSLDQQSANVQKLESTNRALESTIKTLEEDVYTMKNKIIELEGILKSANVERDGLVEKLIAEETLRRKLHNTIQELKGNIRVFCRVRPPLGDGESAQIAFPDQNSEASTIEIVAQAPGSSLTGNGIKQYAFNFDRVFSPETTNEDVFNELSQLIQSAMDGYNVCIFAYGQTGSGKTHTMSSNTGMIPSSVRMIYNRSTSLKERGWEYRMEGQFLEIYNETIIDLLASGNEEEKGKKKLEIYHDTKAGRTTITNITSEPLDTPEQVTWLLDQASKNRSVAATNANEHSSRSHSVFMLHLNGSNSTTGETCRSTLNLIDLAGSERLSSSQSVGERLKETQAINKSLSCLGDVIHALGSGKEGTYIPYRNSKLTNLLQYSLGGNSKTLMFVNISPLKQHVPETLCSLRFATKVNNTQIGTARKVTK Q9US04 GGT1_SCHPO ACT_SITE 441; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 165; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 459; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 461; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 483; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 511..512; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 532..533; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}. SPAC664.09; CHAIN 1..440; /note="Glutathione hydrolase 1 heavy chain"; /evidence="ECO:0000250"; /id="PRO_0000247898"; CHAIN 441..630; /note="Glutathione hydrolase 1 light chain"; /evidence="ECO:0000250"; /id="PRO_0000247899" CARBOHYD 156; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 180; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 315; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 397; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 417; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 612; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGINTSSAQSSGAASIARSSVNVKSGNRHLSSNKKSATSALEERASRPSILVTFLVLAGTILSLYIWPILSPDLFFANQRCSFKYKNKGSQRVVVEGKNGVVATEEETCSQIGVGILKAGGNAVDAAIASGICIGAVNSFSSGIGGGGFMLIRHPNGTAHSLNFRETAPAGASKNMFHGNSTLSQVGGLSVAVPGEIAGYERAWKMYGSLPWHKLFEPTIRLMRDGMPMPKELASRIRRPEFSYFKTHPDWSKIFAPEGVFLHVGEKFYRPALASTLEEIAKFGPEVFYTGKIAERLVKFVQQQGGILTMEDMANFSVVVEEPIYGNFYDREVITCGSPCSGEALILGLNVLSKVDLSEGTSILGCEMTDIGVHHLIETMKWMSAGRTVLADPTFYNNTDHVEQLLSLEYADEIRNNISNERTFDFTHYKAEYDFPNDHGTTHLSVIDKDNMAVGLTASINLMFGSQLLEPETGIILNDHMDDFASPGIVNAFGLSPSPYNFIAPGKRPQSSAVPTILVYNGEVEMVLGGSGGSRIVTAVLDTIIKKYKWGKSLLESVESPRFHHQLMPNIVYIDETVEIEVLRALEKFGHIVDLIPVQYPFSEIQAVFRTNGTLYGLSDSRKQAVAAAY Q9US24 ATG12_SCHPO SPAC1783.06c; CHAIN 1..132; /note="Ubiquitin-like protein ATG12"; /id="PRO_0000212483" MTGLVDQQELEKRLATEEDSQNEDIENQLPSIETIINTYREKENRRVNLRFKAIGRTPLLRKTVFSINASQRFEKVTRFLKKELGLPMNSSLVLYVNSSFAPSPDEIVGNLYDNFAIDSHLLINYCINVAFG Q9US25 HRP1_SCHPO BINDING 415..422; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" MOD_RES 142; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 145; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1259; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1260; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1264; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1783.05; CHAIN 1..1373; /note="Chromodomain helicase hrp1"; /id="PRO_0000080241" MEPEHSNYDLKNHPTSVQESTLNGSAVTDPQFGNTTNSLPSMNGLLNHENSFASQQSLSSSAFDDSEIVTSTANSTVVSSALSTPKIDDAQNSDDVRVDGTRRSSRAKRPVYRDFSYTEIDEHEIPIPKKRKSKPAPKQKKSVASDDEDAYDKRHRFSINSASGTEIRTSLRSSKGKSVNYNEQEFYDDFEDEEEEVEEQVEEEYEPIIDFVLNHRKRADAQDDDPKSSYQYLIKWQEVSHLHNTWEDYSTLSSVRGYKKVDNYIKQNIIYDREIREDPTTTFEDIEALDIERERKNMLFEEYKIVERIVASETNEEGKTEYFVKWRQLPYDNCTWEDADVIYSMAPNEVYQFLQRENSPYLPYKGVFYNTRPPYRKLEKQPSYIKGGEIRDFQLTGINWMAYLWHRNENGILADEMGLGKTVQTVCFLSYLVHSLKQHGPFLIVVPLSTVPAWQETLANWTPDLNSICYTGNTESRANIREYEFYLSTNSRKLKFNILLTTYEYILKDKQELNNIRWQYLAIDEAHRLKNSESSLYETLSQFRTANRLLITGTPLQNNLKELASLVNFLMPGKFYIRDELNFDQPNAEQERDIRDLQERLQPFILRRLKKDVEKSLPSKSERILRVELSDMQTEWYKNILTKNYRALTGHTDGRGQLSLLNIVVELKKVSNHPYLFPGAAEKWMMGRKMTREDTLRGIIMNSGKMVLLDKLLQRLKHDGHRVLIFSQMVRMLNILGEYMSLRGYNYQRLDGTIPASVRRVSIDHFNAPDSPDFVFLLSTRAGGLGINLNTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVNVYRFLSKDTVEEDILERARRKMILEYAIISLGVTEKSKNSKNDKYDAQELSAILKFGASNMFKATENQKKLENMNLDDILSHAEDRDSSNDVGGASMGGEEFLKQFEVTDYKAEDLNWDDIIPEEEMERIEEEERMLAAQRAKEEERERREEEERENDEDHPSRTYKRTTKSITKRQQRREEMVREKEIRLLYRAMIKFGLVDERFDTIVKEAELQATDPKRIYSLSADMVKACDEAVERLGADDTKNKQPRKAILIEFKGVKNINAETVTLRVKDLTHLHRAYKGLDPLKQIIGYPIRSVHSWNCSWGIKEDSMLLAGINKHGFGCWQAIKNDPDLGLHDKIFLDEAKNDKESRYVPSAVHLVRRGEYLLSVVREHPDLFVVKTDQPTKRKYNRKAPTKSSTRQTTLDGSISNTKKSSRTKKKKEEETNRGDETSPEGTVGEDEVEEEPRQAEPPKRALRSNSGKAASNKRTTRNSMKTHSAMDTLTAVAALDAELDNMSNEKAKEEVDHVKSENGESVNEPNTEDLSLETEENTTVSDISPLVKNEA Q9US26 CENPP_SCHPO SPAC1783.03; CHAIN 1..351; /note="Inner kinetochore subunit fta2"; /id="PRO_0000290638" MSGRRYSQISQQEGSSSSDDSDSQQKKTKRTVAHRSPNTTLNGMPRVDSRARPNENSGQSKSSNGRVDTDRKMDLLRKRSNLVHQTLLLEKEVRVRRNAINQRDDSFLSGFIKSLLEIDSSVVIYNTENPDNPKTKQVMPSAEPKKHVKLNSSISSIRFTQHEFEAESEKIIHHSLKGDIEYLPSFKFLLEIKVRTIDYALLFITYKIPHFARKELSSFSDSAIQCLDIVALLRAFSLFAHHYSYRCNTWFYLSKHMKKVASANMDAQCFYVQNSFYKITILYEIKFDDLGFVQPNYCISYILKNQNEKIVSITSKLLNQLDKRFSEFVSLFGFREGSLLLLQALFKPHLG Q9US36 KLF1_SCHPO SPAC1039.05c; CHAIN 1..781; /note="Zinc finger protein klf1"; /id="PRO_0000310842" MTKAKKSRAYQEGDIRYKCDFQGCTKSFTRKEHARRHFRSHTNSKAFICPHCSSSFTRSDVLNRHVNQKHVKQNDAGSQTHPKHDKTLISSSDQELPFPSYVEADVQDAAYTDLKSHIDQPILPDQPIISDNFNEGLQSAIAQTGNNYMFTTSRRNNSISGSITIPESDQQINLQNKFLSTPSIKNNANKSLSPQDSISIFGTSPFNAYQQNTDNFVCWLFDNMEKDAPTESVSNFTDGINAKQLNLMPVLDSPTIDFLSSHFRVDDKLVAKDLLSLSAYSSLIQVMNNNYQLSEEALQYITRSRVNLWIAHYWKDFHPRWPFLHRGTLKVDEAPVELLLAMITMGMHFVGDAFAYSIAVSIHSTLRFSIYTHPDFKPPASLWVYQALLIAEIFEKMTSTVEQHNLSQIFHGVTIESMQNGLSSKDTVTEKIPKNMTGTNIAQHKWHQWVDREASKRIAFFSFVLDSQHVILFGYRPLIDITSVGLPLLCDEALWNADSYEAWTSLLNENDPPHFFPVLKMFLTNEHLPPKLSPWNMMIVLHGLTTIGWILSRENLGIVENIMQNNGTNLKNWRILLKASYKFWLRTYRVFFLNNGTLPLNHPYVRGCLATYELAHISLHTNIVALQTYAKSIVSTSRRLYASTSRYVSAWLASDDSEVSIKHAVDMVEAFLGGDMEYDVQNETGLHRPWCLYVSTLILWAYGYVSDGRCEMLEPGNNDCKSQLNAYLMQMRTGLSEKAKDHVYVRSKTLPLLKCVIDVLCPARWGLLVDGVRILSKLVQL Q9US52 BQT2_SCHPO SPAC1002.06c; CHAIN 1..118; /note="Telomere bouquet protein 2"; /id="PRO_0000116801" MFQGKCAFFDETVPSALIALWQLHNGEAKFLAEGYENFDYAFSMHLRKHVRLPNYKSVQCRSPWWIAEQVAVSRSKSYVSEPVIHLNVMEPLYVDHRIRSVYLQPLPSTLSFLNGELP Q9US55 GLU2A_SCHPO ACT_SITE 524; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q9C0Y4"; ACT_SITE 527; /evidence="ECO:0000250|UniProtKB:Q9C0Y4"; ACT_SITE 600; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q9C0Y4" CATALYTIC ACTIVITY: Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3); Xref=Rhea:RHEA:56000, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:139493; EC=3.2.1.207; Evidence={ECO:0000269|PubMed:9774332, ECO:0000269|PubMed:9813085}; CATALYTIC ACTIVITY: Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55996, Rhea:RHEA-COMP:14355, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:59082; EC=3.2.1.207; Evidence={ECO:0000269|PubMed:9774332, ECO:0000269|PubMed:9813085}; SIGNAL 1..25; /evidence="ECO:0000255" SPAC1002.03c; CHAIN 26..923; /note="Glucosidase 2 subunit alpha"; /id="PRO_0000372782" CARBOHYD 262; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 563; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 822; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRYHGICWFIFQAAIIFAIFGSCQGAFRHQFKTAEQDGFARRNRDLAKFQKENLNWNGLFQLNSISYNSGVVSGVFEQQSENGENQHLFPFSISFLKNDVVRFQMDEKSRLEGTVEYEKNILTKRRFDASTELGFNERAEVYGKDAHLLEQTSTSLTIRYGSHGRFTVIVTFSPFKVEFQRDGEPQVVLNERHLLNMEYYRPKSSRTPEQEANGMWDETFDNFHDSKPKGPESVGLDIKFVDYGNVYGVPEHTSSLSLKETNNSDAGYTEPYRLYNVDLFEYEVDSPMSQYGAIPFMQAHKPNSDVAVFWSNAAATWIDVEKESGPSPHSQSTSTHWYSESGTLDLFIFLGPKASDVYESYSALVGRPLLPPLFSIGYHQCRWNYVSEEDVLNVDAKFDEVDMPYDTIWLDIEYASKRRYFTWDKATFPNPKAMLEKLDSKSRKLIVILDPHIKNDPNYFVSKELIDYNYAVKDKSGVDNYNADCWPGNSVWVDFFNPEAQAWWGSLYEFDRFESDKNLWIWNDMNEPSVFRGPETSMHRDAIHYGGWEHRDIHNIYGHKCINGTYNGLIKRGEGAVRPFILTRSFFAGTSALAANWIGDTMTTWEHLRGSIPTVLTNGISGMAFSGADVAGFFGNPDAELFVRWYETAIFYPFFRAHAHIDTKRREPWLYGEPYTSLVRELLRIRYRLLPTWYTAFYNSHTHGFPILYPQFLMHPEDEEGFAIDDQFYVGDSGLLVKPVTHPSIDKITIYLADDEVYFDLHDHTEYAGKGHQVVPAPLGRVPVLLRGGNILITRERIRRAAELTRNDPFTLTIAVSKIGKNASGFLYLDDGVTFNYKKGEYLIRHFSYENGILTMKDSHSNPPVSPKYSSSQKHLKVERINIYGEQTRKSIKIRKIIDSEVTEWDVSVDDSGCIRNPQLFLV Q9US60 KLP3_SCHPO BINDING 84..91; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"; BINDING 233..240; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" SPAC1834.07; CHAIN 1..554; /note="Kinesin-like protein 3"; /id="PRO_0000125387" MTSIKVVCRIRPTNQLEQDLGGNNVIYPLNDSTVHIETSDYSGNFVFDRVFHPSSTQNDIFSYSIESTVDDLFLGYNGTVLAYGQTGSGKTYTMMGIENNFEKEGMTPRMLRRIFDKIRDSPSTTEYEVKVSYMEIYMEKIHDLLSEKNDRLTVHEDKLQGVYVQGLKTIYVSSETEALDILNKGMGSRAVASTSMNAQSSRSHSIFVLEVVQTDTESGETRRGRLFLVDLAGSESVGKSGAVGQTLEEAKKINRSLSTLGMVINSLTDSKLSHVPYRDSKLTRILKESLGGNSRTTLIINCSPDSYNATETLSTLRFGHRAKSIKNKAVVNSELSVDEMKRQLYIYKDALSRCVCGARINNNLDYNNCHSNVWSGEHSLTLSNLAEKSNLKEAEIIQGNRTIQESNNDRDESTVASIHRHNFDSDSINRLYAEAQLELKQRDGVLSSTKQQLSDLMTALGDAQERYVELVKNHRVNSNLTANNSLNDKPGFTIEQKDKNFSINNERNNFLQKLSTLDSSLAALVNVQRKLIKALISKERPQNGTVIKKIQGGT Q9USG8 MU190_SCHPO BINDING 485; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 485; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 491; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 544; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 544; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 546; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 546; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 546; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 549; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 552; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 552; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-ProRule:PRU00041}; MOD_RES 1005; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP31B10.06; CHAIN 1..1188; /note="Meiotically up-regulated gene 190 protein"; /id="PRO_0000278538" MSTHSGDSTKQQHYRSSDPYSGRRPIPTIPKFFRDRKQRAEKKEEQQREQTENEKLFDPITQRDVEINDVHFDYAKTYDDPSFTVPNQSIQGSSLPSEKPYLSSNQPTNVYKQHQDDLAPPEADNQITRDVPISDEKTNILFFPSPSIDLSYVSKEVKQKTGQYSLFAYIFSLVISWFFTHSIIISAVLPLAISSCMYLWMQNIYAVAKDAEWGAEQKRGEYARLNLIPESAEWMNHLLEKVWPLINPEMFSSVADQIEDVMQASIPSFVENVRVASLDQGSHPVRVVSIRSLPSGEASESFSEKQASEAEHKDEPEQQRKQFYNFELCLAYHAKPVEDATSTSARASNLHLRIVFYPGIKGTVGFPLPIWVEIKGFVARIRFRCELMPEVPFLKNVTFSLMGLPELNVSAVPVAEGGVNIFGLPLISKFVNDAISAAANEYVSPKSMTIDLSKTLLGDDIKKEVNALGVIFVHINRAEDLSKQDVNGLSDAYITVGFHKFGKPLYCTRVVKQDLNPIWNEYAFIPVFPDQVKAGEKISIELWDSDRFSPDDVVGRTKIGLHLLIQDSGKMHERCDTLTGISEDTSLPGRVFYEIGYFPRAEFKPSLKTSGHDITIPRSMRDDPAFQNPHGSLDNKEEEAAVTTAPDEEYPSGILSFTVHQAVNLQMNHPTGTFGNVSGNYNTSPAQSVGDVTAEEGSELPSSYVCVDLDDTLVYKTRTKVFTSNPIYNAGSEKFVKDWRNAMLCFTVRDFKLREHDSILGVVNIPLATTLTTSSQLTKWYPIQGGIGFGSVRISILFRSMKLKIPRNLLGWDIGTLEFMDRQIVAEGTGSVSDVSFSSIRVNIAGVKITAKSSTSNSSSTAEYHVRSRHAVIPVNNRYRSAVVFEFRKQLQRKHNVFAMVWLVDLEDNVEQNIRVPIFTSSKPAHVLQNMIDFDHPDKESEFKIIGYLSTRICFHRGLDDSHEQLVDNDDEAAIFETYRCLKSMGLRRGYVKDMKNPLADQRASLDESRETTTASSKFESDDSVDTEDEETTTDRTPIECTQTVSMVDPNVNGDIQGRNSLGTMNSNERNLEQEFISLGYASKNRPKAHAQEGTNQPGASENVEPVLADDSDAVTIHSNISSDDQKRKLVNADDRELEKRLHRGPYNSKIVRTGEWVKDGAKMGWRNLRRKFALNGRQPDVETEISK Q9USH7 PSY1_SCHPO SPCC825.03c; CHAIN 1..284; /note="Syntaxin-like protein psy1"; /id="PRO_0000210269" MNKANDYTLGVEMIPLSMGEFFEEIDHIRDAIRQIEDNVGRIEMLHQQSLQEIDEANIAATTRHLEGYTSDTRRLQTSVQLAIRSLESQNMQLPPDNDTATRKTQTEAVKKKFMDQIRHFLQIEKTYRAQYEQRMRRQLEIANPRATEDDFQTAINEENGGQVFAQALLRSNRSGEARTALREVQERHADIKRIERTIAELAQLFQDMATMVQEQEPMVDKIVTDAVNVRTNMGEGTQHMDRAIKSARAARKKKWICFGICVVIICVIVAVLCGVLIPVLGNRH Q9USH8 GLU2B_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPCC825.02; STRAND 387..392; /evidence="ECO:0007829|PDB:4XQM"; STRAND 395..400; /evidence="ECO:0007829|PDB:4XQM"; STRAND 403..407; /evidence="ECO:0007829|PDB:4XQM"; STRAND 410..419; /evidence="ECO:0007829|PDB:4XQM"; STRAND 422..427; /evidence="ECO:0007829|PDB:4XQM"; STRAND 434..436; /evidence="ECO:0007829|PDB:2LVX"; STRAND 438..445; /evidence="ECO:0007829|PDB:4XQM"; STRAND 450..458; /evidence="ECO:0007829|PDB:4XQM"; STRAND 461..468; /evidence="ECO:0007829|PDB:4XQM" HELIX 469..471; /evidence="ECO:0007829|PDB:4XQM" TURN 381..385; /evidence="ECO:0007829|PDB:4XQM" CHAIN 24..506; /note="Glucosidase 2 subunit beta"; /id="PRO_0000014209" DISULFID 86..108; /evidence="ECO:0000250"; DISULFID 431..460; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"; DISULFID 445..472; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" MKFSQWYTLTAPLLISSLYTVNAANDLRGVASDKSDLYKPDAKGNWKCLGSDKLISFNQVNDDYCDCPDGSDEPGTSACHNGKFFCKNTGYISSYIPSNRVDDTVCDCCDGSDESLIKCPNTCAQKAREYLATLEEHNRLVKNGLKIREQWALESAKKTDEVKARYKEISDSLVAVSAEKTQLSEKVEKMKRSTDLGAEAVLPLDFQDLRVALLSLVDERNEMQERLDILTNLLDELTLLYETDKFDETMKEAILSFEDLKEQEIRRKVSSDDVHNYLESCNNHLSMLTGPSEDITFSSLIKDIKKILNSLVWNIKLSLINFGILSPSASSTPLTDSESYRRFEAAQRDLDAAEENEKSLEKEHTKLMHELEYHHGWDLYRAIKGMETKREIGGYTYKVVFYENVFQDSILLGNFASQEGNVLKYENGQSCWNGPHRSAIVTVECGVENEIVSVLEAQKCEYLIKMKSPAACSPDQLKQSLLNTQNSANENAVNGMEDKESSVDEL Q9USI6 MYO2_SCHPO BINDING 170..177; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 1044; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC645.05c; CHAIN 1..1526; /note="Myosin type-2 heavy chain 1"; /id="PRO_0000123480" MTEVISNKITAKDGATSLKDIDDKRWVWISDPETAFTKAWIKEDLPDKKYVVRYNNSRDEKIVGEDEIDPVNPAKFDRVNDMAELTYLNEPAVTYNLEQRYLSDQIYTYSGLFLVAVNPYCGLPIYTKDIIQLYKDKTQERKLPHVFAIADLAYNNLLENKENQSILVTGESGAGKTENTKRIIQYLAAIASSTTVGSSQVEEQIIKTNPVLESFGNARTVRNNNSSRFGKFIKVEFSLSGEISNAAIEWYLLEKSRVVHQNEFERNYHVFYQLLSGADTALKNKLLLTDNCNDYRYLKDSVHIIDGVDDKEEFKTLLAAFKTLGFDDKENFDLFNILSIILHMGNIDVGADRSGIARLLNPDEIDKLCHLLGVSPELFSQNLVRPRIKAGHEWVISARSQTQVISSIEALAKAIYERNFGWLVKRLNTSLNHSNAQSYFIGILDIAGFEIFEKNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYMKEEIVWDFIDFGHDLQPTIDLIEKANPIGILSCLDEECVMPKATDATFTSKLDALWRNKSLKYKPFKFADQGFILTHYAADVPYSTEGWLEKNTDPLNENVAKLLAQSTNKHVATLFSDYQETETKTVRGRTKKGLFRTVAQRHKEQLNQLMNQFNSTQPHFIRCIVPNEEKKMHTFNRPLVLGQLRCNGVLEGIRITRAGFPNRLPFNDFRVRYEIMAHLPTGTYVESRRASVMILEELKIDEASYRIGVSKIFFKAGVLAELEERRVATLQRLMTMLQTRIRGFLQRKIFQKRLKDIQAIKLLQANLQVYNEFRTFPWAKLFFNLRPLLSSTQNDKQLKKRDAEIIELKYELKKQQNSKSEVERDLVETNNSLTAVENLLTTERAIALDKEEILRRTQERLANIEDSFSETKQQNENLQRESASLKQINNELESELLEKTSKVETLLSEQNELKEKLSLEEKDLLDTKGELESLRENNATVLSEKAEFNEQCKSLQETIVTKDAELDKLTKYISDYKTEIQEMRLTNQKMNEKSIQQEGSLSESLKRVKKLERENSTLISDVSILKQQKEELSVLKGVQELTINNLEEKVNYLEADVKQLPKLKKELESLNDKDQLYQLQATKNKELEAKVKECLNNIKSLTKELENKEEKCQNLSDASLKYIELQEIHENLLLKVSDLENYKKKYEGLQLDLEGLKDVDTNFQELSKKHRDLTFNHESLLRQSASYKEKLSLASSENKDLSNKVSSLTKQVNELSPKASKVPELERKITNLMHEYSQLGKTFEDEKRKALIASRDNEELRSLKSELESKRKLEVEYQKVLEEVKTTRSLRSEVTLLRNKVADHESIRSKLSEVEMKLVDTRKELNSALDSCKKREAEIHRLKEHRPSGKENNIPAVKTTEPVLKNIPQRKTIFDLQQRNANQALYENLKRDYDRLNLEKHNLEKQVNELKGAEVSPQPTGQSLQHVNLAHAIELKALKDQINSEKAKMFSVQVQYEKREQELQKRIASLEKVNKDSLIDVRALRDRIASLEDELRAA Q9USK8 AGS1_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378, ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.183; MOD_RES 1643; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1644; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1651; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1653; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1738; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1812; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1281.01; CHAIN 1..2410; /note="Cell wall alpha-1,3-glucan synthase ags1"; /id="PRO_0000080328" MHGLQGLCFRRAVIALALLLFHSVFAAPYSEDEEPWNLNQNKNASSVLEYSGEWADHDFFPSPDNWRMSFITVILDRWYDGDPSNNDIEKTPFEYDISEVSFRNGGDIVGLELSLDYLEGLGTQGIYIAGTPFVNMPWGADQYSPLDYTILDHHLGTIDQWRSTITAMHERGMYLVVDLTVATLGDLIGMVGHLNDTSGVDFNLNEYNAMWKTSEYRYVDFNFTNVYNTSCEYPRFWGEDGGPVSIQFKGCYVSDYDHYGDTEAFGSHPDWQRQLSKFASVQDRLRDWKPDVAEKLMHLSCLVISMLDVDGFRIDKATQMTADFIVDWSMYVRECAAKYNKKNFLIVGEVTGSSSYGSIYYNRGRQPDQRPPNVTAAFNYTSDESQYSLRDSDHYGFDGSAFHYSIYRALLRFLGMDSKMEIDFDVSSVLTTAWNGIQINEDAVNINTGTVEPLHMYGVANHDVFRWGAIENGTARLILGTMITSLLFPGIPLLYYGDEQGMYVLDNSANNYLYGRQAMNSARAWYIHGCYNGSATSYPTVDLSPAQRGCQDSWNYLDHFDIASAHRNVYRNIHSIRRHYLSLSEGWRFDHIANWTDDVYFPDSQPYASPMGLYSVLRGPMKEIQDFDSITNASNVSKSEVWVLYANRNDTHLWSYDCTDEDSAIIGPWKSGTTLRNLIYPYDTIELEDSWNSSWGCIPNIELDPYAFKLYVPEEDFIENDPIITSLTPEHDARVVASGNEIDLTIEFSRSMDCDSIKNALSVVSSTRPKNTTAVIDVDSSFCRNYSEDASTSLHGQTAGRFAWYGTLTNIDPGIHRISLKSVPTSDFSSRTLSTDNFLIRVGSTNNPIVHYSANYSDTLLIMQDGDLYINHSAPGAVLFRYSTDFQSHWSDWEEYNGGLTKVQASNWTGTRRQGWEGHHIHVQYWSDLGGSANHMQQSDYGFKYRRFLPHMFLEGDFNEYGYDSGVENRFLQKSDFYWEAGFISETYPAAIQLNVWGMNPDGIPDKTRVYGSQGNSTVLSRSDPASLVGNNITIYHPPPHGYLSYKILLRDDDMIYRLAPSGEWGVSIAIYVLCIVIPPLSAIVVSWAFKNSFYTVKFNKHGNNDLGKFYPLKSLVPFRKKNDLDSPAKVTPVVSGVSARKKKCVLIATLEYDITDWKIRIKIGGLGVMAQLMAQHLKHEDLVWVVPCVGDVVYPEAEEASPIEVKIIDQTYTINVYHHYLDNIKYVLLDAPVFRRQTSKEPYPARMDDLGSAIFYSAWNQCIAEVIRRNPIDIYHINDYHGALAPCYLLPDIIPCALSLHNAEFQGLWPLRTPEEKEEVCAVYNISQRVCTKYVQFGNVFNLLHAAVSYIRIHQKGFGAVGVSNKYGKRSWARYPIFWGLKKIGKLPNPDPTDTDEIVDDKAVAITDIDPDMEKSKVEHKRLAQEWAGLEVNEKYDLLVFVGRWSSQKGIDLIADIAPSLLESYKVQLICVGPIIDLYGKFAAEKLDVLQKKYPTRVFSQPKFTQLPPYIFSGADFALIPSRDEPFGLVAVEFGRKGALGIGARVGGLGQMPGWWYSVESSATPHLLKQFEQACQQALSSSQRTRARLRARSAKQRFPVSQWKAKLEALTDGCIKCSQKYGRNSRSRSSFYSLIHESFSRSSEVLPTSSDTNLDAKRAEEAEMIMIETPPTAEANTGAKLDRSLSLGSRRGPGHTTEDDASDGLDTIQEESMTAGDSTSGGSDISRYRAERLNPDSHSPSEYSFDSGDYEFDPQRSYYYDDLFDDDTTIRNAPSFRPQMGSFDAEHAVGATFSQDDLSDPARSVDSDSVSPPLPPFVAGSNPNARNNNNPYFYGNLHTESSLSLASVMSGKEKRDFSLTRVEETFTDEDGQALRSFSEKLQKLNAKNSKDDLCIEQYLMKSERSFFHERRAIKLGLQKPNKLHVNELSSHSGTEESESLSNGQTSYDDIIAMTDESNYTQLGDDDFKTIHGLKKFMLFKIYDWPIYSIFLALGQILAATAYQLTLFTGTSNIQTYEIYSVCAFFIGASFVWWFMFARLPSYYVLSIPWLFYAVALFLVGLPAFDTVAPGRVWITNVAAWIYAIASASGSIFFSLNFGEEGAVQTRIWVFRACLVQGVQQVWSAALWYWGAHLNKRLTAGEANTFKMSPAIPSITWPLSAVSILIFALLFKGLPEYYRQLSGSIPAFYKSLLRRKLVVWFCISVFLQNFWLSSLNGRSWSYLWDIGNIHQWQIFLLIVAFYIVLWALLLGVLAWISRTHSWIICVFGVGLGAPRWLQQFWATSNIGLYLPWAGYSGPYLGRTLWLWLGVLDAIQSVGIGMILLQTLTRRHVASTLMTGQIVGAVATMIGRGASPNREGPANVFIDFTKWNHGDGSSILASAPFWINIICQLAICVGYLAFFRRENLSRP Q9USL5 DOM34_SCHPO COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P33309}; SPCC18B5.06; STRAND 38..40; /evidence="ECO:0007829|PDB:3MCA"; STRAND 72..74; /evidence="ECO:0007829|PDB:3MCA"; STRAND 81..83; /evidence="ECO:0007829|PDB:3MCA"; STRAND 106..108; /evidence="ECO:0007829|PDB:3MCA"; STRAND 128..130; /evidence="ECO:0007829|PDB:3MCA"; STRAND 137..143; /evidence="ECO:0007829|PDB:3MCA"; STRAND 146..152; /evidence="ECO:0007829|PDB:3MCA"; STRAND 157..164; /evidence="ECO:0007829|PDB:3MCA"; STRAND 203..212; /evidence="ECO:0007829|PDB:3MCA"; STRAND 240..244; /evidence="ECO:0007829|PDB:3MCA"; STRAND 256..258; /evidence="ECO:0007829|PDB:3MCA"; STRAND 291..295; /evidence="ECO:0007829|PDB:3MCA"; STRAND 308..310; /evidence="ECO:0007829|PDB:3MCA"; STRAND 312..315; /evidence="ECO:0007829|PDB:3MCA"; STRAND 343..346; /evidence="ECO:0007829|PDB:3MCA"; STRAND 361..368; /evidence="ECO:0007829|PDB:3MCA" HELIX 24..32; /evidence="ECO:0007829|PDB:3MCA"; HELIX 119..125; /evidence="ECO:0007829|PDB:3MCA"; HELIX 176..196; /evidence="ECO:0007829|PDB:3MCA"; HELIX 213..227; /evidence="ECO:0007829|PDB:3MCA"; HELIX 231..236; /evidence="ECO:0007829|PDB:3MCA"; HELIX 237..239; /evidence="ECO:0007829|PDB:3MCA"; HELIX 250..254; /evidence="ECO:0007829|PDB:3MCA"; HELIX 260..266; /evidence="ECO:0007829|PDB:3MCA"; HELIX 270..287; /evidence="ECO:0007829|PDB:3MCA"; HELIX 296..304; /evidence="ECO:0007829|PDB:3MCA"; HELIX 323..338; /evidence="ECO:0007829|PDB:3MCA"; HELIX 351..358; /evidence="ECO:0007829|PDB:3MCA" TURN 199..201; /evidence="ECO:0007829|PDB:3MCA" CHAIN 1..390; /note="Protein dom34"; /id="PRO_0000326089" MKLIQKNIEKNGSGWITMCPEEPEDMWHLYNILQVGDQLKASTVRRVVKVGATGSTSGSRVVMKLRILVENMDFDTKAAQLHIKGRTTEYHPEVKMGSYHTLDLELHRNFTLYKNEWDAFALDRVDAACNPSRNAEIGAVVLDEGLANICLITDYMTILRQRIDQVIPRKRRGDSSAYQKGLDKFYDSVFQSINSEFDFDKLKVVILASPGFVARGLYDYIFSMAVKLDLKQIVKSKNKFVILHSSTGHIHSLNEILKDPAVESKLADTKYVQEIRVLNKFYDVMNEDDRKAWYGPNHVLKAFELGAIGELLISDSLFRSSDIATRKKWVSLVEGVKEINCPVYIFSSLHESGKQLDLLSGIAAILTYPVDEEDISEDEEDEESQNFEHS Q9USM3 SFH1_SCHPO MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16A11.14; CHAIN 1..418; /note="Chromatin structure-remodeling complex subunit sfh1"; /id="PRO_0000205960" MAQACKTTYSSRLKTGNTCLIQKNVAVSTRSHSSYTGRNSLRNVPAVNYAAFEQGEDFETPVETPEKEEEKFETDDRGLAVGRPTGNNIYPRFATKTRHIYVTDEQLKCAAEERDVYIPIRLDIELPNNYRLKDTFLWNMNEQVMTPDVFAQILCADLDLSTNVYGTQISSSIRAQIEEYAPVAEVPMPKGQEMLVVFNIQVQLAQLSYNDQVEWNLTSPLTPEEFSVLTCNDLGLSGESRPEIAYAIHECLLKLKKNACEGDLPDYDSDAVPGTKAGPRQDMDTLGALWQPVLETVSLEDAKKNENNRENLVKQWRREASKFGGFAADVSAERWRAAALGNLSQSETANLPSASVSDAQTLLEQERPRWRCRWCNVLGTGTFCVRRGPEGNKSLCNACGVAYAKTGQLPYWRKSLYT Q9USN7 HST2_SCHPO ACT_SITE 138; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" BINDING 35..55; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 118..121; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 146; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 149; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 170; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"; BINDING 210..212; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 235..237; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 255; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPCC132.02; CHAIN 1..332; /note="NAD-dependent protein deacetylase hst2"; /id="PRO_0000316618" MVKNTVKHVDSSKHLEKVASLIKEGKVKKICVMVGAGISTAAGIPDFRSPETGIYNNLQRFNLPYAEAVFDLSYFRKNPRPFYELAHELMPEKYRPTYTHYFIRLLHDKRLLQKCYTQNIDTLERLAGVPDKALIEAHGSFQYSRCIECYEMAETEYVRACIMQKQVPKCNSCKGLIKPMIVFYGEGLPMRFFEHMEKDTKVCDMALVIGTSLLVHPFADLPEIVPNKCQRVLINREPAGDFGERKKDIMILGDCDSQVRALCKLLGWSDELEKLIDTSVETLTEEISLLSVDSTIEKNASEQKKDDNSVNPFTKIEEKKKDEVTLLVSDDE Q9USP0 EI2BA_SCHPO SPCC11E10.07c; STRAND 31..33; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 73..75; /evidence="ECO:0007829|PDB:5B04"; STRAND 98..100; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 137..143; /evidence="ECO:0007829|PDB:5B04"; STRAND 162..167; /evidence="ECO:0007829|PDB:5B04"; STRAND 189..192; /evidence="ECO:0007829|PDB:5B04"; STRAND 205..210; /evidence="ECO:0007829|PDB:5B04"; STRAND 212..214; /evidence="ECO:0007829|PDB:5B04"; STRAND 220..223; /evidence="ECO:0007829|PDB:5B04"; STRAND 240..243; /evidence="ECO:0007829|PDB:5B04"; STRAND 255..258; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 307..311; /evidence="ECO:0007829|PDB:5B04"; STRAND 317..321; /evidence="ECO:0007829|PDB:5B04"; STRAND 324..326; /evidence="ECO:0007829|PDB:5B04"; STRAND 328..330; /evidence="ECO:0007829|PDB:5B04" HELIX 19..29; /evidence="ECO:0007829|PDB:5B04"; HELIX 35..46; /evidence="ECO:0007829|PDB:5B04"; HELIX 55..58; /evidence="ECO:0007829|PDB:5B04"; HELIX 63..72; /evidence="ECO:0007829|PDB:5B04"; HELIX 77..94; /evidence="ECO:0007829|PDB:5B04"; HELIX 101..109; /evidence="ECO:0007829|PDB:5B04"; HELIX 115..129; /evidence="ECO:0007829|PDB:5B04"; HELIX 130..132; /evidence="ECO:0007829|PDB:5B04"; HELIX 146..157; /evidence="ECO:0007829|PDB:5B04"; HELIX 174..184; /evidence="ECO:0007829|PDB:5B04"; HELIX 194..196; /evidence="ECO:0007829|PDB:6JLZ"; HELIX 198..203; /evidence="ECO:0007829|PDB:5B04"; HELIX 226..235; /evidence="ECO:0007829|PDB:5B04"; HELIX 246..248; /evidence="ECO:0007829|PDB:5B04"; HELIX 299..302; /evidence="ECO:0007829|PDB:5B04"; HELIX 313..315; /evidence="ECO:0007829|PDB:5B04"; HELIX 331..339; /evidence="ECO:0007829|PDB:5B04" TURN 59..62; /evidence="ECO:0007829|PDB:5B04"; TURN 95..97; /evidence="ECO:0007829|PDB:5B04"; TURN 110..114; /evidence="ECO:0007829|PDB:5B04"; TURN 170..173; /evidence="ECO:0007829|PDB:5B04" CHAIN 1..341; /note="Translation initiation factor eIF2B subunit alpha"; /id="PRO_0000156059" MVESDSSGIVRHSQGEFDIVQVYKKFLQDDPEITMPVAAIEALVQLLSRSQAKTISEFMDILQNGSNTLKEGVQNNISLSAGCDIFQRFVTRSLHDVGDFEQCKRHLVENGKLFIQRARACRQRIAHLGYPLIRDGSVILTHGFSRGVAAVLLAAAKRHVRFKVFVTESRPSGSGCLMTRTLKNACIPTCMVLDSAVSFTMNRVDLVLVGAEGVVENGGLINQIGTFQLAVFAKHAHKPFYAVAESHKFVRMFPLSQYDIPFSRPILEFDDPSPETVHPEPEPIPTPSDAIHNELIMNEEQIRNNPTLDVTPPEFVSGLITDLGIIDSKSGVSEELIKLYL Q9USP2 YND1_SCHPO ACT_SITE 145; /note="Proton acceptor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000269|PubMed:12686557}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12686557}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12686557}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:12686557}; Note=Divalent metal cations. Ca(2+), Mg(2+) or Mn(2+). {ECO:0000269|PubMed:12686557}; SPCC11E10.05c; CHAIN 1..572; /note="Golgi apyrase"; /id="PRO_0000347282" MVRKYGIFIDAGSSGSRLLIYSWDYDTDSSLSDKVKKLPLIETGIGDGGKWSLKVQPGISSFANNPKHVGKKHLKELLDFAAHAIPKDVHKETPVFLSATAGMRLLGVDAQNKILSHACRYIKKNYDFDIPNCSNSIRVIDGKAEGMYGWLATNYLLKTLEEKDTSTVGFLDMGGASVQIAFELPPSQLKNYKDSISTVHIGLQNGQQLEYPLFVTTWLGFGANEAYRRYLGLLIESENGKVGNTLSDPCSLRGRTYDIDGIEFAGTGDLKQCLKLTYNLLNKDKPCSMDPCNFDGISIPPVDFANTEFVGVSEFWYTTNDVFDMGGSYHFPNFYKKVDEYCGTEWETMLSRLYNKELTPSTDENKLEKLCFKASWALNVLHEGFDVPKSNTSSNDAKDGLSVIPAYHSPFTSLEKIERTEVSWTLGQVLLYASNQQLLAKPEYANYYMDPYGKLIASPSKHWMRLFPNKLFFILSFIFCLFFLFSLVLFGYDPKRRQRFKKFLLRLQRRKAPYIMSANGSYEDIADFSDDLEMSSPSKWHGPPIRTTSSHVLADRLSFTASRERTPRSPFP Q9USP6 CLC1_SCHPO MOD_RES 229; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC9B6.08; CHAIN 1..229; /note="Clathrin light chain"; /id="PRO_0000205775" MSQFPALEDFDDGLVTAPVDDSKNNTDFLEREKLALGEDAGQFETPEDKDALLNFENDSEAEQTRFEQNFPPIDAEMQASGTFSAPKAPYMGQAEVHPPEDESGDPEPVRKWKEDQMKRIQERDESSKKLRESNIEKARKAIDDFYENFNDKRDKVIAKSRKEQEKLLEENESKSTGTTSWERILKLIDLSDKPEAHGRSTERFRELLISLAKDSNAPGAAGTTVSSSS Q9USP7 MBO2_SCHPO MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 396; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC902.06; HELIX 182..194; /evidence="ECO:0007829|PDB:6GDJ"; HELIX 200..219; /evidence="ECO:0007829|PDB:6GDJ"; HELIX 223..249; /evidence="ECO:0007829|PDB:6GDJ" CHAIN 1..397; /note="Gamma tubulin complex adapter mto2"; /id="PRO_0000116779" MSEHNYQSDREVAEDPFLNYEASANQLSSNSRESTPRGSPWRAGMRSASLMTEPLEDSMYSDNNYLDNGVSFTKDENPLYSPSWPSLADANVNSMKSNNAIQEHKAAKFVSEKSLEKVSTADNNLVLQELENLRERLNQVELQLSERPSSYLGYHNNLSPYRSPNSYPSLLPSTHSPHSPAPLSTMQTALMRLRTYHPSPIILKPVEQAVNHAITLVNTSPSSVVDALCRSLAELCLGLVQEAIDASILSQQESSNSLDLVRHTPPLNYTSSVDSSPQRMASDSYGRPSLHLNDPFPSVDLQSNELSHHNVRTTLFSDDSRFHSKIHTHSTPPSQMYSAASHFRYRSDPSTRHVSNSTNKSSLHPSPTSLRVAHPIIPQRASPASQSFPSLQDTPSP Q9USP8 IDH2_SCHPO BINDING 129; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 139; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 160; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 247; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P50213"; BINDING 247; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 273; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P50213"; BINDING 277; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P50213" CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; Evidence={ECO:0000305|PubMed:7903653}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; TRANSIT 1..27; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC902.05c; CHAIN 28..379; /note="Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial"; /id="PRO_0000014433" MSMLSTLRTAGSLRTFSRSACYSFQRFSSTKAAAGTYEGVKNANGNYTVTMIAGDGIGPEIAQSVERIFKAAKVPIEWERVKVYPILKNGTTTIPDDAKESVRKNKVALKGPLATPIGKGHVSMNLTLRRTFGLFANVRPCVSITGYKTPYDNVNTVLIRENTEGEYSGIEHEVIPGVVQSIKLITRAASERVIRYAFQYARQTGKNNITVVHKATIMRMADGLFLECAKELAPEYPDIELREEILDNACLKIVTDPVPYNNTVMVMPNLYGDIVSDMCAGLIGGLGLTPSGNIGNQASIFEAVHGTAPDIAGKGLANPTALLLSSVMMLKHMNLNDYAKRIESAIFDTLANNPDARTKDLGGKSNNVQYTDAIISKLK Q9USQ2 ALP6_SCHPO MOD_RES 286; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC428.20c; CHAIN 1..832; /note="Spindle pole body component alp6"; /id="PRO_0000078133" MSEIHVKTALSRLADKYLQNSKNPSVPYTIETIVSFFQEIIHSISPDTFQLDIDDILYKIYSKIPPEENNDALFSKLSNLVSRLKSQTVIHNKSQILYFLYLLSPISQSSRDVSSHLLDESISNPINIPSTEVESSNFGQTRYDQVPENPQITDWDEGLENESSISIAHDSSRLNRSTETSSVQHTLITEADLLSSISYVLQGISTEYVQFKNELALLSKRIPVQYLLQMRALSETGLLYQELKVFSNYDPSVSQSIDGDNVSKAFINDQSLALQSLKSVISKELTNFLALIASLDSQIRADASLEKPMVTIRRCIAWTQVAKLKLRILSSVVNDNMNQENKKRLIQVVSKYNVHGDPLIQELSDKILTEITGPLYEMIENWIYKGELVDPYQEFFVKEKNGSESHDHQGQGDVVWKGKYFLDKELIPSFLSEELVDKIFLIGKSLNFARYGCGDFDWAQEHYQKLVKKLSYRDPHSLETVVDKAYTESINHLVYLMEEVFHLTDHLKAIKKYLLLGQGDFVDLLMESLGNSLDQPANTLFRHNLTASLESAIRSSNASYEPEYVLKRLDARLLELSHGETGWDVFTLEYKVDSPINVIITPYCSRQYLKIFNFLWRLKRIEFALAHSWRRVNLGERNVFRNLDYTKFEWHFVSCHLAEMIHFVCQLQYYILFEVIEISWQELQLAMEKPNATLDTYIEAHEKYVTSITHKGLLGGGKSRNEDSFLHQLHDILKVILNFHDAIELLYNFSCSLSNRIRINVPISTDALAAQYTPIKNELSNFTEEFQVRLQKLLHGLASHKDPEMRFLSVRLNYNEFYVSHRRRHDKDVTSQ Q9USR4 REC27_SCHPO SPBC577.05c; CHAIN 1..125; /note="Linear element protein rec27"; /id="PRO_0000297692" MKKRSETLGSDQSSSEIIEHVLEELNLKNIERRVKKYDQIESEYKTNIENEKKAFIKDVSQVQQKIKEFEIQKANQIKQLNEEKLSIEARKQQLEIEIRNQLLQYAEKLRIVVKTPMNQPTNTEV Q9USR9 CENPC_SCHPO SPBC1861.01c; STRAND 500..507; /evidence="ECO:0007829|PDB:6O2D"; STRAND 517..525; /evidence="ECO:0007829|PDB:6O2D"; STRAND 540..547; /evidence="ECO:0007829|PDB:6O2D"; STRAND 551..558; /evidence="ECO:0007829|PDB:6O2D"; STRAND 563..568; /evidence="ECO:0007829|PDB:6O2D"; STRAND 572..587; /evidence="ECO:0007829|PDB:6O2D"; STRAND 590..595; /evidence="ECO:0007829|PDB:6O2D"; STRAND 598..602; /evidence="ECO:0007829|PDB:6O2D"; STRAND 607..612; /evidence="ECO:0007829|PDB:6O2D"; STRAND 614..616; /evidence="ECO:0007829|PDB:6O2D"; STRAND 618..626; /evidence="ECO:0007829|PDB:6O2D" HELIX 495..497; /evidence="ECO:0007829|PDB:6O2D"; HELIX 526..528; /evidence="ECO:0007829|PDB:6O2D"; HELIX 628..633; /evidence="ECO:0007829|PDB:6O2D" TURN 548..550; /evidence="ECO:0007829|PDB:6O2D" CHAIN 1..643; /note="Inner kinetochore subunit cnp3"; /id="PRO_0000116879" MTMNETSAIPARQRENQFFEIGVVGRKTGFTVPRDVKKGDDGFEDMDAYFLSDGSIHLDEDNGDIEQDMPPVTRLQPTSPMAVNAASDEASHASSSDSSDKNPDIPSSPLLMNSRALRASRGSSGPLIVPIDHSAFQAEDEGTADKTKVDGNKLSIQPRKANRIVDFSRIKASPDRKKFEPRRSTELPSKIPSSTPKDDNVQESPAFPDENITALQKNVANFTSIKDSGGRDNLYIQTISKPRRSYVQNNKSEQTIKPSKQNKQKEEKKTISQGNKPNSRDEDSELSIDVPLSMLNRSLANNSQKNKKRTPNKPLQESSINSVKEGESNPVVKRKRGRPRKNKLEIGNSVQTSEATQVKGAKKPAIRNAKKMSNEKDDSLNSQSDSASGEFIKTIARNNLQEIKQVEREDTLVGVRRSKRTRIAPLAFWKNERVVYELHRDENRIPALPEVKQIIRVDDPSPSIRQGRKKRHAKRSGVEIKSNLEAKSNDVEEYDAFYKDEINCEVLSWNEQNPKASEERVVGYSLPSVNLQQISNQQLKFASLFKEEPSFAAGVVEMPAGAEKPVKPSKHNIMSFCILQGKIEVTVNATTFRMKKDGVFIVPRGNYYSIKNIGKEAVRLYYTHATDTLENKRRGIGDFPNER Q9UST6 SPC24_SCHPO SPBC336.08; CHAIN 1..198; /note="Kinetochore protein spc24"; /id="PRO_0000246667" MSDSPIELMRSTLAGFQIAPDVKTISNIQDIRAQIQSFREKELEGSQTKFKVLSRKLEISTQAMESLKQTAESSQHAEEILSREKEKFRIAKLLNITENEIMSLESQLQKMKEQLLQLEERENTSEDICQSEENANMLKLNFYHSLGFDLETAENTGNKRVIIHTENDLQTVQISNKYSPYFYSNYFWDLLDDSKDKK Q9USU3 FBH1_SCHPO CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9228070}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9228070}; SPBC336.01; CHAIN 1..878; /note="F-box DNA helicase protein 1"; /id="PRO_0000271430" MSAQHLHSCKFYRLPLEIIPLICRFLSVQDIQSFIRVFPSFQTILDSSNDLFWKKKNYELRIRRNRLLRGSYAAGVSSSAMNGFVNGTQISSTPAEREYYSKSDEIKNICGLPPGPMKVEQIGHAIDHLVSETHTVDHLGSSIKASFFHIDDVPLEWISSICMQVQSFFSPAAREAISSLKSRTTTSNLLLSLFVGILFEDDLWYFFNTLYMLSSTSAIEFAYFLDSIFTVVRTDYEHYRDPLSQTLITSCTRIHNIVAVIESPYDEPNTKGLTSEQKMIVECQLNPGEVLKVKAFAGTGKTKALLEFAKSRPKDKILYVAFNKAAKEDAELRFPFNVKCSTMHGLAYGAILAQADLPQAKLERQLSNSTIASLLSLQVAFPKANRKNNPGTPSASLVASHIMFTLNRFMHSTDWQLGFRHISKRSLEVTKLSKEKLLAYTKKLWSLIVNFEYTHAPLIPDAYMKLLHLYEFPNIFSKYDYILFDEAQDFTPCMVDLIYRQKHARIVIVGDAHQCIYGFRGANACAFNENLYPSTKQLCLTKSFRFGNSVAKYANFLLSLKGENVKLKGVQNDHAYWSSASNPNNVSGAFRFFPHTIIFRTNKELILQSIRLSVSLPKEIPIAILGSMRKKAFQLLRSGSELAHGQRPSHPKLKDFSSWGEFEVHVKNSAEEDAELALVYDMADELFSESFLSRLDNCEKRLMDSKDDGDNGIILATAHQSKGLEWDNVQLGNDFRPKFDSVSFSRIGSSRYLQEEINILYVALTRAKKRLILNDTITKLYALECGLVRFAGGILTEDQLQPGKVALFVDWQIDKFSFFYETPAEGYNLLVEANEKSVWDIFFGVLSGAWQNYIANTSERLKRSMLFIENQLFAVHDQ Q9USU5 GAS2_SCHPO ACT_SITE 156; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 263; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 87; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 155; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 156; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 197; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 202; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 295; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135" SIGNAL 1..19; /evidence="ECO:0000255" SPBC29A10.08; CHAIN 20..459; /note="1,3-beta-glucanosyltransferase gas2"; /id="PRO_0000353132" CARBOHYD 34; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 68; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 90; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 146; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 160; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 212; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 218; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 254; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 284; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 308; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 334; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 344; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 354; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 370; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 423; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 69..98; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 211..350; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 235..266; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 374..427; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 383..449; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 402..409; /evidence="ECO:0000250|UniProtKB:Q06135" MVSFTKFTLQLLSASAAFAYFEPLTIKGRKFFKNDTQFYIKGVAYQPAVDAEETSTIVDPLAEVNYKNCTEDAKIISNLGANVIRVYAVNASLNHDKCMEAFRNESIYVFLDLANPKTGIDRDTPTWNTDQFSSYQSVIDTFQKYNNTGAFFAGNEVVNNASNAPAVAYVRAAVRDSKNYIKSKKYRTIPVGYAGADIPVVRTELAAYLSCNATKLNNDTNSETDFLGYNMYEWCGHSDFYTSGYAARTQELENFTIPIFLSEFGCNKVTPRVFTEVQAIYSDNMTNVWSGGIVYEYSQEVNDYGLVNVSSTGERVLTTDYNNLKKQWASISPNITYKHSYNPNGTIPECPSRNKTSWAVSANAFPVTPNTTICSNAVKNLKCSANGTPSGSKISQVLSELCYYDNKACSSISSDPYEGTYGNYTGCTGVQQLSIALNAYTQDHGADSCSWGGVGELKA Q9USV1 SFR1_SCHPO SPBC28F2.07; STRAND 250..255; /evidence="ECO:0007829|PDB:3VIQ"; STRAND 265..270; /evidence="ECO:0007829|PDB:3VIQ" HELIX 181..212; /evidence="ECO:0007829|PDB:3VIQ"; HELIX 215..245; /evidence="ECO:0007829|PDB:3VIQ"; HELIX 274..280; /evidence="ECO:0007829|PDB:3VIQ" TURN 246..248; /evidence="ECO:0007829|PDB:3VIQ"; TURN 260..263; /evidence="ECO:0007829|PDB:3VIQ"; TURN 285..287; /evidence="ECO:0007829|PDB:3VIQ"; TURN 292..295; /evidence="ECO:0007829|PDB:3VIQ" CHAIN 1..299; /note="Swi5-dependent recombination DNA repair protein 1"; /id="PRO_0000097710" MSQTINSELNENATSQCKEDLKVSLSESDLRDSQGQLGIENPPKCNNSGNHSDNLGFIEQSETVHPENEKALTPDLRDTKIHTSLPITTPFSKKRAREAKNILLKPFKSPLRQTASPQVADTNLKPSLAVTNLNSDETNTSSEPVTSPLRTTPNSIKRQKRLFKSPISNCLNPKSDPEITQLLSRRLKLEKEVRNLQEQLITAETARKVEAKNEDKDLQTLIQKWKNAAQQAAEVLFKPMAERIRLAGGVTQSFRIEEGENKGQIQEVRTEFTMSMFLNQFGVPVHLMSFDEENGDWKS Q9UT08 2AAA_SCHPO SPAP8A3.09c; CHAIN 1..590; /note="Protein phosphatase PP2A regulatory subunit A"; /id="PRO_0000071413" MQTENQVNDLYPIAVLIDELKHDEITYRLNALERLSTIALALGPERTRDELIPFLDESIDDEDEVLSALADQLGNFVDYVGGPEYAHVLLSPLENLAATEETVVRDKAVDSLNKVCICLSQEQLEQYFVPLVQRLSTAEWFTSRASSAGLYCAAYSQSENPAVKVSLRQSFSHLCHDEAPMVRRPAATNCAKFVFLVTKQEAIDEFIPLFNSLSNDDQDSVRLLSFDIMVSLAEVLKSDSEIRHYLLQPLRSFVSDSSWRTRYMVAANFVKLAKVVGPSLIKDELIKPFVLLMKDTEQEVRRAIATQIPGFCELLDKRIVLEEIIPVIQELINDPAQHVRAALGMNIGALAPQLGKEKTTEYLLPMFLELLKDENPEVRLNIISKLEVVNKVVGIELLSQSLLPAIVTLAEDKQWRVRLAIIDYIPLLAQQLGVEFFNEKMGNLCMSWLEDHVYSIREAAIKNLRKLTEIFGLEWATETIIPKFLAMRSHPNYLYRMTTIFAISEIAPALNAEVIEKQILPTLEQLVNDPIPNIRFNVAKAFEVLKPVLAAGGDSTVYEQQIIPLLEQLTKDNDPDVQYFATQALEQTND Q9UT18 THI9_SCHPO BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 uM for thiamine {ECO:0000269|PubMed:18201975}; MOD_RES 585; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9.10; CHAIN 1..591; /note="Thiamine transporter thi9"; /id="PRO_0000054169" MPSSQISHQDPELGQTSSGSSSIKEKAEPQLYAGPIDPARRPDVFQEGFEDVSVTDDDNDNELLRKMGYQPVLHRSFEFFESFAASFASLDVVSGVRLTFSWGISFGGPAAYWSAMLVTGFCSIVTAACLAEICSALPAAGSIYLWAAESAGPRFGRFVSFLVAWWSTTAWTTFVASITQSTANFIFAEVSTFNNPWPTNDSDVKFRAVQWIVAEVLLVFTILLNQVPPRYYKWIFKASMLLMFIDYVMNIIWVPVATSKKPDGFRSAKWVFTETIYDQAGYIKEVDDANGNPIASLSKIVPKGWQWCLSYFATAGVIVGYDASGHIAEETKDASIKAARGIFYSTVTSFIVAFSLAILYLFCCPDLDTFTAILYNDNSPQPFVNFYSYLLGRGGHVVMNVVIILEIFLNGVVSVLACSRLVFAVSRDGVLPFSNWISQVSKTGQPKNAITVIYIVSALLLCTILPSAVAFTSLVSAAGAPSFAAYAVLAFCRLFITRDKFPKGRWSLGWLSKPCLVITLVYNLFALVVNVSPYTYPVTGPSFNYAVVIMGGVSIFAIICTIVIPKSRWVANRYRYESDSEHSASVKELKV Q9UT19 METE_SCHPO ACT_SITE 703; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P82610" BINDING 19; /ligand="5-methyltetrahydropteroyltri-L-glutamate"; /ligand_id="ChEBI:CHEBI:58207"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 126; /ligand="5-methyltetrahydropteroyltri-L-glutamate"; /ligand_id="ChEBI:CHEBI:58207"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 442..444; /ligand="L-homocysteine"; /ligand_id="ChEBI:CHEBI:58199"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 442..444; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 495; /ligand="L-homocysteine"; /ligand_id="ChEBI:CHEBI:58199"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 495; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 500; /ligand="5-methyltetrahydropteroyltri-L-glutamate"; /ligand_id="ChEBI:CHEBI:58207"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 523; /ligand="5-methyltetrahydropteroyltri-L-glutamate"; /ligand_id="ChEBI:CHEBI:58207"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 526..527; /ligand="5-methyltetrahydropteroyltri-L-glutamate"; /ligand_id="ChEBI:CHEBI:58207"; /evidence="ECO:0000250|UniProtKB:O50008"; BINDING 572; /ligand="5-methyltetrahydropteroyltri-L-glutamate"; /ligand_id="ChEBI:CHEBI:58207"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 610; /ligand="L-homocysteine"; /ligand_id="ChEBI:CHEBI:58199"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 610; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 652; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:O50008"; BINDING 654; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:O50008"; BINDING 676; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P82610"; BINDING 735; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:O50008" CATALYTIC ACTIVITY: Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000305|PubMed:16436428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21197; Evidence={ECO:0000305|PubMed:16436428}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; MOD_RES 182; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 441; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9.09; CHAIN 2..764; /note="Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase"; /id="PRO_0000098703" MVKSAVLGFPRIGKNRELKKATEAYWSGKTSAEELLATAKQLRLEHWKLQKAQGVDIIPSNDFSLYDQIMDHSFSFNVIPPRYRLSGLSSLDTYFAMGRGMQRAATADKAAVDVPAGEMVKWFDSNYHFLRPEVSEETDFKLSSTKALDEFLEAKEAGIITRPVLVGPVTYLFIAKAAKGSSIKPIELLPKLLPVYVELIKKLTEAGAEYIQIDEPILTLDLPQEILASYKEAYETLGKIGKLILTTYFGSLQSNADVLKGLPIAGVHVDVVRAPENLDRALAVLGENQIISVGVVSGRNIWKTDFQKATAIIEKAISAVGSERVQVASSSSILHIPHSLSGEDQINPEIKRWFAFAVEKCAELAILTKAANDGPASVRAELEANAADCKARAESPITNVEAVRERQSKVTPQMHERKSPFETRYAKQQASLKLPLFPTTTIGSFPQTKEIRVTRNRFAKGLISQEEYDAFIRKEISDVVKFQEEVGLDVLVHGEPERNDMVQYFGERMEGFVFTVNGWVQSYGSRCVRPPIIVGDVYRPAPMTVKESQYAQSITSKPMKGMLTAPITILRWSFPRDDVHDSVQAQQIALGLRDEVLDLEKAGIKVIQCDEPALREGLPLRRAEWDEYLKWAIDAFRLATAAVQDDTQIHSHFCYSDFNDIFDAIQRLDADVVSIENSKSDMKLLNVLSRYTSCIGPGLFDIHSPRVPPVSEFKERIDAIVKHVPKDHLWLNPDCGLKTRGWPETTADLKNMIAAAREAREQYA Q9UT23 MPH1_SCHPO BINDING 93..100; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:22844101}; SPAC9.05; CHAIN 1..834; /note="ATP-dependent DNA helicase fml1"; /id="PRO_0000310751" MSDDSFSSDEDWDELDTQVVDKIENEYHNNTIGLNGYSVDEYFDANDSNRYRLQHELDESAAQQWVYPINVSFRDYQFNIVQKALFENVLVALPTGLGKTFIAAVVMMNYLRWFPKSYIVFMAPTKPLVTQQMEACYKITGIPKSQTAELSGHVPVTTRNQYYQSRNVFFVTPQTILNDIKHGICDRTRISCLVIDEAHRSTGNYAYVEVVHLLSLSNKNFRILALSATPGNKLEAIQNVIDSLHISRIEIRTENSIDISQYVQKKEVDFFPVDLSAEITDIRDRFSSILEPMLQKLNKGNYYRIQNAKDITSFTVVQAKQAFLAMSGQNFPANQKWDILNTFDALATFAYPLNLLLNHGIRPFYQKLREVEEECFVGRSGYKKRIINHENYRPLMDDIEILLRDQSFVGHPKLEHLERIVTEYFEKEQTKDTRIMIFVEIRSSAEEILRFLGKFYPNVRPAIFIGQSAVRKAAGMSQKLQNETVKQFQKGEVNTLIATSIGEEGLDIGEVDMIICYDASASPIRMLQRMGRTGRKRKGYIYMLLTRGKEEAKWERAKDAYRTLQDNIVSGRGLSLSEKSYRILPEKFRPVCDKRVIEIPKENEEVVVAPKKVQLRTKIKKKFFMPENALNGFITASALGKPKRALAKSEESPFEICPVTYSIEQEKKLEKYKRVCLRGLDIHRNRRLSQLSVTGRIPHSLATKSIHSFLKHLNTIDSQKAQEWRREINNQFQVSNINSTDRDTKQPKMHDFRQPLHPNPMTTLKRKGQHNSFSYDKSTLFYDNNNNLEEDLPDVNISISSRNEEASKTKPFDDRQQRLQQLVEKRKRMKGMLI Q9UT24 BRR2_SCHPO BINDING 542..549; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 1387..1394; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC9.03c; CHAIN 1..2176; /note="Pre-mRNA-splicing factor brr2"; /id="PRO_0000290645" MSSAHPKGDSKEPPKHGNSKEKPNYGQSQYSYSAMSNLVTQADRRFVSRRDAEPTGEPESLVNRVSIADMGSRARIEKPSTLPLELTQEVQEVRLPRKDAESLEIGIRQPEREKRSSAILKYFDSFEILKYNPLTDETREVYDYILSFIQQYLGDQSPEILRSAADLIIELLKDSSLDEQGRKKQIEEVLSTELPQDRFSQLVNLGNRLTDYTVEQEEELNEEGVNESGVPVLFNEADEEEEAVEAMEEDEVAEDEDVVLETSISQEEEKKNIENPDTEVTFISADTKKVTEIPTVHPREIDAFWLQREIAKYFADAVVCQEKTNQAFEALSADYDLGELENELMSIFDYEHFYLVQLLTKNRWTIVSCTMLKRAATDEERLGVEEQIRAAGRSWILEALRPGAITIPDDGLNELNNNVVEKAEPAPVSEIPLSKTLTSHKIVPKHQVDLENYVFTEGSRLMSNKAVKLPEGSFRRTGKGYEEIHVPAPNKAVLGADERLVKIKELPEWSHQAFLNTQSLNRIQSHLYPIAFGTDENILLCAPTGAGKTNVAMLCILNELQKHLREDLSFNLQNFKIVYIAPLKALVQEMVNNFSKRLTPYNIRVAELTGDSQLTKQQISETQIIVTTPEKWDIITRKANDLSYVNLVRLVIIDEVHLLHDERGPVLESIVARIFRHQEETLEQVRLVGLSATLPNYTDVASFLHVDPKKGLFYFDSTYRPCPLKQEFIGITEKTPFKRMQTTNEACYEKVMQHAGKNQVLIFVHSRKETAKTARFIRDKALEEETIGHLLRSDAASREILRAEADSTSDENLKDLLPYGFAIHHAGMRREDRQTSEDLFADGTIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGIWTELSPQDVLQMLGRAGRPQFDTYGEGIIITAHSELQYYLSLMNQQLPIESQFMRRLADCLNAEVSLGTVRSIEDGVDWLGYTYLYVRMLRSPALYSVGPEYDDDKYLVQKRADLLHSAAILLEKCKLLVYNRQSGTLTATELGKVAASYYVTHNSMAIYNRLLMQTTSFIELFRVFSFSDEFKHIPVREEEKVELAKLLERVPIPIRERLDEPAAKINALLQSYISRQRLDGFALVADMVYVTQSAGRIMRAIFEISLRRGWSSVATLSLDTCKMIEKRLWPTMSPLRQFPNCPSEVIRRVEKKEFPWQRYFDLDPAELGELVGVPKEGRRVYNMVQSFPRLSVEAHVQPITRSLVRVELVINSQFNWDDHLSGTSEAFWILVEDVDGDRLLHYEQFFLLKKYKDDEHIVNFTVPLLEPLPPCYFIKIVSDRWLHSITKVPLSFQRLIMPEKFPAPTPLLDLQNAPVSSLNNPSFISLYPNFKFFNKIQTQVFNSVYKTNDSVFIGAPNGSGKTVCAELALLHHWSQEDYGTAVYIAPIQEIVDRRYEEWYGKFSDLGDGKVLVKLTGERSQDLKLIQVADLIFCTPSQWDSLSKRWRSMRSIQKVDFYICDELQLLGGFYGPLYEIVISRIRYMAVQLEKNIRVVGLSVSVANARDLGEWLGTSPQCIFNFSPKDRPNPLTIHLQSFSITHFPSLMLAMSKPIYRSLKNFISQRKSTIVFTPDRKVAKQLAFDLVTFSMADEDEYLFSLMENEAFNKVEDAALQQSLKHGIAYISEITSSNDQNIVQYLYRHGLIKVLIASRDVIYSLKAKSNAVIVMGTQYYDGKEHRYIDYPISELLQMLGFTASIGSSELSQVILMTVTTKKEYYKKFLNEPLPMESHLQVWLHDAFVSEISTQTIESKQDAVDWLTWSYMYRRLVANPAYYGLQDITHESVSEFLSDLVETTMNDLSEARLITVDDEDDSCVALNLAMIASHYGITYITMQTFALSLSERTKMKGLLEIVTSAAEYEQLPIRKYEDIVLERIHSRLPVRLSNPNYEDPHTKSFILLAAHFSRFELPPGLVIDQKFILTRVHNLLGACVDTLSSEGHLIACIRPMEMSQMVTQALWDRDSPLKQIPYFDDALIERCNKEGVHDVFDIIDLDDEKRTELLHMDNAHLAKCAEFINKYPDIDIDFEIEDSEDVHANSPSVLIVQLTRELEEDEEVDTTVIAPYFPAQKTEHWWLVISDDKTLLAIKKITLGRSLTTKMEFVPPAMGTLKYKLSCFSDSYMGVDYEKEFECNVLEPLDTEMEDGE Q9UT35 GDA1_SCHPO ACT_SITE 256; /note="Proton acceptor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.42; Evidence={ECO:0000269|PubMed:14612233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000305|PubMed:14612233}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:14612233}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:14612233}; SPAC824.08; CHAIN 1..556; /note="Guanosine-diphosphatase"; /id="PRO_0000209918" CARBOHYD 372; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTPTMKSIARRKALLIALSIFAVTFILWNGFPGSSNRPLPSSNDEFHYEDIELPSGYRSEGEVVDLLNPKDELEEPLFSEEPLFPVTTSIPTKTAVSKPKIAPTSAAKDVTFSSSIDSDDCSVAYDNSKPVRQYVLMIDAGSTGSRVHVYQFNNCNPSPKLEEEFFKMIEPGLSSFAGDPEGAAASLDPLLDYAMENVPEEYRRCSPIAVKATAGLRLTGESEAKAILKSVRQHLENDYPFPIVKDGVSILEGSMEGIYAWITINYLLGTLGGKATHSTVAVMDLGGASTQLVFEPRFASDGESLVDGDHKYVLDYNGEQYELYQHSHLGYGLKEARKLIHKFVLNNAEALKESLELLGDSTSIIHPCLHLNASLTHPDSKSEASEVVFVGPSLAHLSLQCRGIAEKALYKDKNCPVRPCSFNGVHQPKFTETFTDSPIYLISYFYDRMISLGMPSTFTIEDMKYLANSVCSGPTYWQDAFSLTDALKELKEEPEWCLDLNYMISLLSVGYEIPNNRQLHTAKKIDNKELGWCLGASLSMLSEQNNGWNCNVKEEI Q9UT43 ATC8_SCHPO ACT_SITE 684; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0" BINDING 684; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 684; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 685; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 686; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 686; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 794; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 843; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 845; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P32660"; BINDING 848; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 866; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1022; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1023; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P39524"; BINDING 1102; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1103; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1104; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1181..1188; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 1216; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1222; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 1243; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 1246; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"; BINDING 1247; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191" CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:Q12674}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q12674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000250|UniProtKB:Q12674}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q12674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:Q12674}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; MOD_RES 954; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC821.13c; CHAIN 1..1562; /note="Phospholipid-transporting ATPase dnf1"; /id="PRO_0000046240" MKSSGIAGDSNGFETNFLNETTNREEDGAFNWNAADDGTNERREDIHVRFQDSALPLGIDENELDEIDINGDSKKLDSVEVDESHDVNSPSDSRLKSSFKSVLELTANSMVSVLTPSTKTEQTSKGKGKKKKAHVSFLEGPVEEIPLDDIEPTSPREASPVFNGRPPIPPEFLKSRHKEFTIPNPLQFISNFLSNLFSRDTRYLKSSHGRIIIINPYDDSSQIDERTGKPYMQNSIVSSRYNKYNFVPLQIIAQFSKTANCYFLLIAIMQMIPGWSTTGTYTTIIPLLIFISIAILREGFDNYRRYRQDRVENRIQTQVLRHVDVDPPIVEEHSSFFRRRRWRRSRSQESASRSTIRSTDEREPERTSEDPPQLPPSPSSPSSPALSVKPNIDPQPPLYNSTLTTTRSIPANKPTFFWASCDRKDVRVGDIIRLTSDQTLPADVIALSSPNPNGAIYIETAALDGETSLKTRLVNSTLRSLCKDINDLIRLSGTCTVEDPNGDLYNFNGSMKLDSIQGEIPLSNNDVLYRGSNLRNTSELFALVIFTGEESKIRMNAVRNVSVKAPSMQKVTNRIVIFIFALVVSMAIYCTAAYFVWQKKVERKLWYLTNSKLSFVPILVSFIILYNTMVPISLYVSMEIIRVFQTFLVQSDIDLYYPENDTRCEVRSSSILEELGQVTHVFSDKTGTLTDNIMLFRNLSVGGFAWQHVGAENPKLVSTSQKSDDLDGEAKPPQLENIQGTTIQLLQYVHDNPHTTFSKRVRIFLLNLAICHTCLPSFDEENQIYKYQSISPDELALVHAAQQLGYIVIDRDIDSLTIRLHYPLDPHSHPIAKTYRILNIIEFTSKRKCMSVIVRMPNGRICLFCKGADSAIIKRLRLSNLAKRKDKSVTKAEQARKSIEIDKAIIRNSQSTSRPSLTASRPSLSRRRNDYINNVTSWLDERREKMGVVRPRASTSILETRRRPAVGRHSLAGGERLMEDKKYLSKQEEAEGSIYESLNHNDAKLFENTFEHVHAFATDGLRTLMYAHRFIDESEYQSWKLVNDAALNSLSNRQQLLDEAADLIEKDLEFAGATAIEDKLQVGVPESINSLFRAGIKFWMLTGDKKETAINIGHSCGVIKEYSTVVVMGSLDGVEGSDETVSGGQRLSLDRPPTNDPASLMIHQLISCMNAIHSNSLAHLVIVIDGSTLADIENDPELFLLFINTAVEADSVICCRSSPMQKALMVQKVRNTLEKAVTLAIGDGANDIAMIQEAHVGIGIAGREGLQAARSSDFSIGRFKFLIKLLFCHGRWSYVRLSKYILGTFYKEQFFFLMQAIMQPFVGYTGQSLYESWGLTCFNTLFSSLCVIGLGIFEKDLSASTVIAVPELYQKGINNEAFNWRVYFGWCSIAFIQAFLVFYVTYSLFGMKELNDNNIFAYGQLIFTAAIFIMNFKLVFIEMQYINIISIIVLVLTSLAWFLFNIFISEHYPDKNLYLARSQFLHHFGKNPSWWLTMLFVMVCALTIDIVAQMLRRTLRPTDTDIFVEMENDAFVRSRFEQESGEFLQANAPSVDEIEQYLKSRD Q9UT45 ENG1_SCHPO ACT_SITE 492; /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"; ACT_SITE 569; /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"; ACT_SITE 573; /evidence="ECO:0000255|PROSITE-ProRule:PRU01352" BINDING 496; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 567; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 569; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 573; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1"; BINDING 650; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /evidence="ECO:0000250|UniProtKB:A0A023I7E1" CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000305|PubMed:12665550}; SIGNAL 1..20; /evidence="ECO:0000255" SPAC821.09; CHAIN 21..1016; /note="Primary septum glucan endo-1,3-beta-D-glucosidase"; /id="PRO_0000012132" CARBOHYD 37; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSSYLRSFIFGLLTISLAQCSPILKDTKDTKFSTGSNISLKKRDTNVFDSVVDTINPASYFGTVSHPVTPAGVSTDSLSSPIETNKFFDNNLLGSRTNFMYADPFRYWWQSSDTMGGICIAHTDDNQRVMDTDDTIPSYYYEPIGICSLGFGASGITSNTDPIVDEIDQMSARFTFSWDSSSMQLTLTEGMAVTTAVYTNAIPQIFSSTLYINDFVEVPGTSAVQKYRVTMSDNHVWLIYIYGDSLTLTESTSQMLVGSNTFNGYIQIAKIPLGDGTAEALYDTYAGVYITGISISGYVEDAVGYYSFDFTTAGDTSVEPLFFLLPHQVDTAVSGTKVTSIVLASLVSGDMNAAAGNSITFAEAIPQDIGFLPWSPTGGQIGYSEEALEIIAEVAGTELGEDFSANSNLNSMYYSGKVLAKYAMLCVTINDILGDETSSEQCIQKLEAAFARFVDNQQIYPLTYDNTWKGVVSVAGLSGDSLADFGNSYYNDHHFHYGYFVFTAAVIGHIDPDWINTGNNKEWVNFLVRDVANPSSNDPYFPKHRMIDIYHGHGWASGLFESNDGKDEESTSEDYNFFFGMKLWGQVIGDSDMEDRANIILGIERNALNKYMLYADGNVQPTSMQPNYVAGITFMNKITHTTYFGTNIEYIQGIHMLPITPISAFIRGPSFVLAEWNALLASVIDYVDSGWRSLLYANLAIAEPEESYEYFSSSDFNTDYLDDGASRAWYLAYAAGLWANDAVYYPVSSSSTTTTSTSTGSVTTTSTTATASCTLPISYTSTPTTTSISGTCNGATFDASLYVCDGTVLCPIVNGVSYQNCNGACYNPSQYGCDNGALGPVQSSSTTSSITPTPTTTSSITPTPTTTSTTTTAQSTGMQLCGSNYYDASSYYCDNDQLCPIIDGVDYLSCNGACYNPSQYVCSDGSLSPNTVTTTKATTTFTPTPTTTTTPTPTTTSATSTNVIAQCGSAWYDSQSYICYGNILCPIINGSPLLACGNACYDSSIYGCSNGALVAA Q9UT49 CID13_SCHPO BINDING 110; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 112; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:12062100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333; Evidence={ECO:0000269|PubMed:12062100}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; SPAC821.04c; CHAIN 1..578; /note="Poly(A) RNA polymerase cid13"; /id="PRO_0000120313" MDNANCVGGCKFETRSFQYRRRIPYSLGADPLPPVHPLSLKNLVDIDTDLISSQLYELYDSIILNDSGLERRYAFVQKLEQILKKEFPYKNIKTSLFGSTQSLLASNASDIDLCIITDPPQCAPTTCEVSAAFARNGLKKVVCISTAKVPIVKVWDSELQLSCDCNINKTISTLNTRLMRSYVLCDPRVRPLIVMIKYWAKRRCLNDAAEGGTLTSYTISCMVINFLQKRDPPILPSLQMLPHLQDSSTMTDGLDVSFFDDPDLVHGFGDKNEESLGILFVEFFRFFGYLFDYEHFVLSIRHGTFLSKRAKGWQFQLNNFLCVEEPFHTSRNLANTADEITMKGIQLEFRRVFRLLAYNCNVDDACSQFTFPSLTDTSFMDDYVNELQLEIVPGFSHGRDSSDTSCTESPPEPSHFAWAFDPYNATASPYYNQNINSSIDYSSIYSNDVPAIPPNVPYTFVDPYTYACYINNNSYLPPSYMDFYTWYNSPYPKSSHHFDERHGGDRHEKNLSNSRRYSRNKFHKKKQSSGPFQYYPDAFSFTPTDNNSPPSNSSSSEVVSPVSLHSEPVLSTVQAFKS Q9UT72 RFP2_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; SPAC343.18; CHAIN 1..205; /note="E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp2"; /id="PRO_0000358873" MNLHGLELPGRDQRLSPEVIDLTEDIEDDGADVSEVTLLDLTRIPEFQPRRRIRTSRNHLDANLSNVPTINSIPSPVTRPPVAVGGGIFYGARRTRNRSQTQRRTLLENGFRNSRKKAQDSSNSIAERVSPPPGFCYDVHPHNNIACAKCGNELVSDEKKSIFAAKCGHLFCSTCAKELRKKTVPCPVQHCRKRITKKFIFPLYL Q9UTB5 PSD2_SCHPO ACT_SITE 159; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; ACT_SITE 373; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; ACT_SITE 488; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208"; ACT_SITE 488; /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208}; TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208" PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208}. MOD_RES 488; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208" SPAC25B8.03; CHAIN 22..516; /note="Phosphatidylserine decarboxylase proenzyme 2, mitochondrial"; /id="PRO_0000316032"; CHAIN 22..487; /note="Phosphatidylserine decarboxylase 2 beta chain"; /evidence="ECO:0000305"; /id="PRO_0000316033"; CHAIN 488..516; /note="Phosphatidylserine decarboxylase 2 alpha chain"; /evidence="ECO:0000305"; /id="PRO_0000316034" MRPRQRFRRFHPRWSKVNLRGFGGVGALKGVKALNGMNVRVSMRLKWISNRIHRIRRSRRLGRLSISVRPNGSWQVYLLSSLPLRSLSRVWGQFNRAHLPTFLRTPGFKLYAWVFGCNLSELKDPDLTHYRNFQDFFCRELRPETRPVDPVSPVVSPVDGRIVCQGVVDNNRIQHVKGLSYSLEALLGGISSSNPLVVNFEDEITPDLIQKHEQFAEQHSISLNSNNRYRKADASAAVVDEHSDEEALLCAFTDHPHFYLNDSRNSLNYFCPFSAFEDISNSVRSSCGKRLSPSSNFDLNNLGGDDDLRSESSSDFESAPASILEHEPTNWDDWVQEADVTDIDSLPWHNIRPGNKLFYSVIYLAPGDYHRFHSPADWVIESRRHFSGELFSVSPFLARRLHNLFVLNERVALLGRYEHGFMSMIPVGATNVGSIVINCDPTLSTNRLVLRKKSLGTFQEAVYKNASPVLDGMPVSRGEQVGGFQLGSTVVLVFEAPADFEFSTYQGQYVRVGEAL Q9UTE3 SEB1_SCHPO MOD_RES 343; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC222.09; STRAND 17..20; /evidence="ECO:0007829|PDB:5MDT"; STRAND 84..86; /evidence="ECO:0007829|PDB:5MDT"; STRAND 390..392; /evidence="ECO:0007829|PDB:5MDU"; STRAND 400..404; /evidence="ECO:0007829|PDB:5MDU"; STRAND 407..411; /evidence="ECO:0007829|PDB:5MDU"; STRAND 432..438; /evidence="ECO:0007829|PDB:5MDU"; STRAND 443..450; /evidence="ECO:0007829|PDB:5MDU"; STRAND 462..466; /evidence="ECO:0007829|PDB:5MDU"; STRAND 469..475; /evidence="ECO:0007829|PDB:5MDU"; STRAND 490..495; /evidence="ECO:0007829|PDB:5MDU"; STRAND 511..513; /evidence="ECO:0007829|PDB:5MDU"; STRAND 522..527; /evidence="ECO:0007829|PDB:5MDU" HELIX 4..16; /evidence="ECO:0007829|PDB:5MDT"; HELIX 23..35; /evidence="ECO:0007829|PDB:5MDT"; HELIX 36..39; /evidence="ECO:0007829|PDB:5MDT"; HELIX 40..53; /evidence="ECO:0007829|PDB:5MDT"; HELIX 56..58; /evidence="ECO:0007829|PDB:5MDT"; HELIX 59..79; /evidence="ECO:0007829|PDB:5MDT"; HELIX 92..113; /evidence="ECO:0007829|PDB:5MDT"; HELIX 116..118; /evidence="ECO:0007829|PDB:5MDT"; HELIX 119..131; /evidence="ECO:0007829|PDB:5MDT"; HELIX 137..150; /evidence="ECO:0007829|PDB:5MDT"; HELIX 419..427; /evidence="ECO:0007829|PDB:5MDU"; HELIX 439..441; /evidence="ECO:0007829|PDB:5MDU"; HELIX 451..460; /evidence="ECO:0007829|PDB:5MDU"; HELIX 482..484; /evidence="ECO:0007829|PDB:5MDU"; HELIX 496..498; /evidence="ECO:0007829|PDB:5MDU"; HELIX 501..509; /evidence="ECO:0007829|PDB:5MDU" TURN 487..489; /evidence="ECO:0007829|PDB:5MDU"; TURN 514..517; /evidence="ECO:0007829|PDB:7MI2" CHAIN 1..620; /note="Rpb7-binding protein seb1"; /id="PRO_0000081902" MSGIAEFDGILDSLEHSKTGISGSKILKLTNLSMENVSENAQFVASVYKYAKRAPVTHKLGALYILDSIVRSFQDGAKKNNESFENPVDASFSGGWCKAAEITDSLVADAIQHAPSAHLPKILKLCDIWEKASTFPPEKLESLRSKLKDAMASTEPVSVDSAAAPSQSTNPEGNGGSVGSQAAAPTSRPVENDAASILEALAAFAQKAPVPSAAEESVSTPPQPAVAPSVSAVVPNLPVHPATAINAQSQSGNPLSNPLFQPSNVPQSIPSGPMGMKTGSVNDTQSQQITLMNVLASQNVPPAQIDSIMKAAFPNYNAPFQPAGVGSVPLPAPTSSQSLRLGSLHRSRSPSPRSGRPRRSPSPSHLSIPSTLPPADGVPKPTPDGFPRRFERDPTIPPDSIKVYSRTLFLGGITRSVREPVLRSMFERFGSVQSLILNHNYRHGFLKMFRRDAAEKAQVAMENVPFADTTIRTKWGVGFGPRECSDFSTGISVIPIRLLTDADRTWLVTAEYGGTGGLPITPGIALDEPDIEIGLGISSKAISKRGKDFAMRRDERFRGRKPYRGGPPIHHGERHFDSGNDWHGNPSTVPPPTNPYNPGYPYMDPNYSSGYVSQPPWQPQ Q9UTE5 E2AK2_SCHPO ACT_SITE 417; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 177..185; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 200; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; PTM: Autophosphorylated. SPAC222.07c; CHAIN 1..639; /note="Eukaryotic translation initiation factor 2-alpha kinase 2"; /id="PRO_0000085950" MRFFNAHKSAEDGNYSETTNAISLKNERQSRDLSVNKHGRMLLTALLENFCQLYDNNPAKSKRLFALICHTLQKIGILEEEYIEELAAVRSNYQDALHHLILQAREAIRLDDAEERLLALPDPTNVFEKFPQETALSKFSVDGLNVRQFRFRDLTLESWLQSRNSRYIEDFEEYSLLGRGGFGSVYHVRNKIDGAEYAMKKINSTFQQMSYSKIFREIKCLAKMDHPNVIRYFSSWVESTTEATQMPIVMSKNSSRVLGTSSYCDVNGMDSIIFEPTESSALTDDILFAEDPGTESIISTSRKSSYSSTTESSNFENLESPRNLHDSNVSTFNNTTILDDDYSSSMHISKTGPTHSFIIYIQMQLCFDDLESYLIRRNHFLSFPLCKEQIQLHTDLFRMIINGVMYVHEGVNLIHRDIKPSNIFLAKSLPEDRGSVPLISYNDKNDLKEYITPKIGDFGLVVENKKNTETALSFLERNHLPNLQDETQHIGTATYAAPELLDAMSSQHNKFTKKIDTFSLGMVLFELLHPFQTNMERATKLQDLRRGNLPEEFVEQHICESSLILWMTAKDPTKRPSLLEVLNCGLLLPNQVSMPNISNIVSTNHLDVETQMKLIMDENQRLREQIAVLRSRIQHLETR Q9UTG2 PUB2_SCHPO ACT_SITE 639; /note="Glycyl thioester intermediate"; /evidence="ECO:0000305" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; SPAC1805.15c; CHAIN 1..671; /note="E3 ubiquitin-protein ligase pub2"; /id="PRO_0000120333" MENIRFEVQLTILHVEGLWKNGLLRSLKPYLLISVDDDQFIKTNVASGTLRLSWGFTQKLTVSPQSIILLQLFDEKQKNETSDGFVGLGAAVVNSFLPFNNPKDDYKTRITLRSPSGSYRGSVVCLFKRSKFLPEELPADKSQICTDIIDDASGCAWETRIDEFGHVYYLKSPQLSVISAISHEKLENLTPKQLKEVFSQFLFNNQSKSSLKINLEYKVIKHLLEHYPLALSVRQQVAVEKGPLPAGWEMRLSEDYHVYFVDHSTKTTTWSDPRDNVVASDSVSENTDSIQQINDEYQRKIAYMYDRPEMAVNDAQLQLKVSRATTFEDAYDIISKLSVSDMKKKLLIRFRNEDGLDYGGVSREFFYILSHAIFNPGYSLFEYATDDNYGLQISPLSSVNPDFRSYFRFVGRVMGLAIYHRRYLDVQFVLPFYKRILQKPLCLEDVKDVDEVYYESLKWIKNNDVDESLCLNFSVEENRFGESVTVDLIPNGRNIAVNNQNKMNYLKALTEHKLVTSTEEQFNALKGGLNELIPDSVLQIFNENELDTLLNGKRDIDVQDWKRFTDYRSYTETDDIVIWFWELLSEWSPEKKAKLLQFATGTSRLPLSGFKDMHGSDGPRKFTIEKVGHISQLPKAHTCFNRLDIPPYNSKEELEQKLTIAIQETAGFGTE Q9UTG8 DAD2_SCHPO SPAC1805.07c; CHAIN 1..94; /note="DASH complex subunit dad2"; /id="PRO_0000211596" MLQARIEEKQKEYELICKLRDSSNDMVQQIETLAAKLETLTDGSEAVATVLNNWPSIFESIQIASQHSGALVRIPPSTSNTNASATEQGDVEEV Q9UTH0 NU132_SCHPO SPAC1805.04; CHAIN 1..1162; /note="Nucleoporin nup132"; /id="PRO_0000290669" MSSILGKRKNEEVVSFSPLKRISVEKSLLDSTAYNNSLDWLRSKNFKVSCLLKHFNSKIINDHPLSGSCYTDIGYALINSRKACFILSYRQSLGTAEPPTITFPLPEEDSNGFSGQNALTAFVPSDASDKEPGLLIVMPISGRIAYWTSIGNALAQSYICPQGMESLIKLLPKEKCEHLCCSNPMKFIISTNFGRLFSVQLRDPAGQPDVSVQLFASDISTFSTILQKMKIFNYPSIHIIALKSPPLFSPYQHLLYVAEASGLLEIYDLKLENKLVSGMNLSPIFKQVLREGCPDASGLEVLDLTICPTNGNLVSFLVCWKNSINYRYMIISLDFSDISSPSVMNIHPLYSFSSKSLESSKLHYSSSGNSLFVVLTDAVIIVHVQEDDKDIVSRTSWEEVIRMNTNVSGGIFMSTCYKYVLGKYSIPTESCFIATPYSGIAEIEVHSLEHPANNESLVKSKLEEAVFYSFLPGNPIDFSCNYLRSIKKPELERIIVDLGMDILNSRSTHLPPLFASLMQHLSCRLNSLNNLVRYIRSMSLDVDRQVLYKLRVMGEKCNSVRYLWNTIDTEFSTVSHSLIFQRIIYRLTQSASSDNALREWFLHNIESIDQLIAQAHEFCIDSGSRVQELPLEVLDVIMEANEVILAIQSSALAYRRESQKIYKLSIDTFGEEVPWTSTPETLVLLCRQFELTRSALVQSHQGTSDVENTFKIKDKGVLRNVVSNLEVQLVALTEVCFDAYSERIRWIEQRCGKDASEIQDVKEAFAVNRRFWVQTLSDIGKGSSAIRIAEKYSDYRSLVELCYQLYEDNELTDALNNYLDLFGIKFAFILYDYFVENGMALELLNSDRFNKSYLKQFFKSRDYNQISWMHDMRLGDYDAASHRLLQLATKQEKLVDKKESELSLSKLFLYAVPSNSGNIRDLVLVEQKLEQLHIQKMVSKSVMPVVERLRSQGKKYQLVEAVVDDLIGAKVAPVIARQVMQRVVKKFIAGQVVEATELLEYLSFSLYRREDLVEGEVTDYYLALRLLLTTRLTDDAKRFYENTIWRRAVLHDNWIQVLDTQGKNDAIIETQFRMSALYRTLEAVTINGLFHEGLIRPGSLSSCKFEGYDPQNLISIYPPARFGDVTEVTKVLNRESVKLDHYLTKTNLNTCYISMCLSCDTI Q9UTH9 DUS3_SCHPO ACT_SITE 340; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" BINDING 245..247; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 308; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 380; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 411; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 460..462; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 483..484; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA; Xref=Rhea:RHEA:53364, Rhea:RHEA-COMP:13539, Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89; Evidence={ECO:0000250|UniProtKB:Q06053}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366; Evidence={ECO:0000250|UniProtKB:Q06053}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH + uridine(47) in tRNA; Xref=Rhea:RHEA:53360, Rhea:RHEA-COMP:13539, Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89; Evidence={ECO:0000250|UniProtKB:Q06053}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362; Evidence={ECO:0000250|UniProtKB:Q06053}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853; Evidence={ECO:0000269|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857; Evidence={ECO:0000269|PubMed:34798057}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q5SMC7}; SPAC16.04; CHAIN 1..617; /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]"; /id="PRO_0000316227" MAELETGAVPIREEFLVKQDGNKKRKRKERGQNKRREKIHVKENNALCPAISIGNECPYKENCKFPHDVEAYLATKAPDIGDKCPIFERYGVCPAGFKCRWLAGHVVINADGKYELIKKPDGQFTLFTVNTVGKEVQRKLRTKQLDLSKAESIISAVLGEEKPDPSSKVSNIPEENRDATSAISEGKETESVSLEETGVLKNQTVSVNVDLKEISSQARSNIALPTLRPQEKNLIDWRDRKILAPLTTVGNPPFRRLCGSLGADTFYSEMAMCYPLMQGHQPEWALVRGLNYEREMMRGGRRGILGVQLATGKLWQATKTAQVIAEQCDGVDFLDLNCGCPIDLVFRQGAGSSLLENPGRLLRNLQGMDAVSGQIPVTVKLRMGNKDDHPVVKNLIGRIFNETNTSAATLHGRSRQQRYSKNANWDYIGEIASKVKSMNERIDELPEDSLRTQPLSLIGNGDCYSWQDWYDGVNKGVDTVMIARGALVKPWIFEEIEARQFIDKSSTQRLEMLEQYCNNGLEYWGSDSQGVNTTRRFFLEFMSFFHRYTPIALYEVQRPRLNDRPPLYTARDEMETLLASNKVTDWVKLSEFFLGPTPERFTFTPKHKSNSVEEAEG Q9UTI4 MOA1_SCHPO SPAC15E1.07c; CHAIN 1..172; /note="Monopolar attachment protein 1"; /id="PRO_0000076264" MAINNENELEYKLIKKNKNPKISNSKKKNSTRPALQDKTNQTLPIHQNQAFSNILPSDFSIIKTPETKTADDFPVNGYEGLNILKFDLELFYKLKPVATSTPKSCMRTGSNLFLNETVKHVPDERLVSNIKNTQTKDSITRDSAYYHRKTMTESIIKTLAAFDAEVDEIILF Q9UTJ8 RAD50_SCHPO BINDING 13; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 36; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 37; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 40; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 41; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 41; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 42; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 65; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 67; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 157; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 157; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:G0SHW7"; BINDING 674; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"; BINDING 677; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00471" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q92878}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878}; SPAC1556.01c; CHAIN 1..1285; /note="DNA repair protein rad50"; /id="PRO_0000138647" MSCIDRMSIMGIRSFDNRSRESIQFFSPLTLIVGQNGSGKTTIIECLKYATTGILPPNTKGGAFIHDPKICGEKEVLAQVKLAFRNTNQVKMICTRSLQLSVKKTTRQQKTLDGQLLILKDNERTTISNRCAELDSQVPLSLGVSKALLDYVIFCHQEESFWPLSEPANLKKRFDEIFESLRYAKALDQIKGLKRDQETQVKVDQATLTHYRSDKERAEKIELRVHESLKRISCIRSKVEELDQEITETARLQDELFKSTEEYEQQMITIRHLESQSDIINTTINDLKSQMTITDESSEDLEKLHSNFAEKVKEEQELYKSLEKKRSDLESLLKSRRELLEKLTGDLGKIQGEIESLEKLKVKKSTMINEIVHRYNINEINEEGIMTEVSKYASLVNKNYEISSGKLKERQVAVRARIEGIKAHEMFLNNRVSEINSSLEKQLTTQKELRSRFEILFPVKLQREDFTKDVEKSDLWIKSLRQEYESKNLLELLDKHQTALSSVENRLDEISEIVDSYHKYSGVRTKLQVFEENKTNKSAILANQLMTLKSSFSEVMSYELKDDDNYNEELDKLVEDVRKKLQEKEEAESSLRSVRERLEIRISLSVQSINDLTENKKIKTKTLKSYSGTFASMISEIKALESEIEENRKTLHSLQFGSTFYEKAIEICVDQHACQLCQRSLDKEEEKLFVEHCHSMIDVIPSKSAEVYSHLETLTKTFKNLSEAKPIFDEIELLDKRLSETKTELSDLQGDLQGLDIRKDEIQSELDTLYLRRANLEKLQLLVKDISNLEEEIRTIDRETEVLRIELPSSIAHHNLDEIYAEREKLLEKRGYLRKQIERTKLEETSFKKKIDDAVLANNEQKLKLTKLNFQVNELEQLEKDINKSSEDCDLQKKKLLEVSSKQGSQAPFLNELESEYEKLEADIQEMAQKSRTEILEANEYLHQLNEWNSELRIDVSTKFKCIKEKKSNIGEEVRIIASKIESTDDNLRKLQERLADLRTRERNASDNLRLRALMRQLEEAVTQKNYLLSQQSHDDRESFRERMQILKSKYGALNAERAGLLGECKQLENSITKDKEELNMEFKDADERFRRQLIKTKTTGKANEDLGKYAKALDVAIMQLHSMKMNEINRIVDELWKQTYCGTDIDTILIRSDSEGKGNRTYNYRVCMVKGDAELDMRGRCSAGQKVLACIIIRLALAECLGVNCGILALDEPTTNLDEENICSLAKNLSRIVEFRRKQANFQLIVITHDEQFIRLVNSDAYCSYYYRVKRDTNQKSMIVKEPL Q9UTK4 NU189_SCHPO PTM: Nup189 is autocatalytically cleaved in nup98 and nup96. {ECO:0000269|PubMed:26137436}. MOD_RES 724; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1051; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1486.05; CHAIN 1..963; /note="Nucleoporin nup98"; /id="PRO_0000204857"; CHAIN 964..1807; /note="Nucleoporin nup96"; /id="PRO_0000438989" MFGQNNSSGFGGGTGAFGQNNQQTGGLFGSNSNTPGNTLFGSQNTSTTGFGQNTTQPLFGSNTNGGLFGNRNNTTTTGGTGFGMSSGTGMFGQSNTPAFGGTNNATNPSGGGLFGSNTANNNANTGTSFSFGSNAGSTGFGNTASNTGTGGGLFGSQNNAGNTAGNTGFGSQGTGGGLFGSSTTPATTNAFGTSGFVSSNANAVNGTANPPYAVTSEKDPQTNGTSVFQSITCMPAYRSYSFEELRLQDYNQGRRFGNASSTNTTSAFGSTPAFGASTTPFGQNLSGTTNNATPFGTSNATNTTPGSGLFGGGSAFGSNTTNTGFGSGTNNASGGLFGQNNNTTSTPSTGLFGGSTFNQQKPAFSGFGSTTNTTNTGTGTGLFGSNNATNTGTGQTTGGLFGGAATGTGTGFGSSTGGFGSNTNNQPNSGTMGTGLFGFGANNNTANNNTAPTSTFGGNNSSNFSFGANNNAATKPSGFGFGSTTTTPASGGFSFGQNANNAPKPAFGSTATTAPKPAGTGLFGGLGAGANTNTATNATGTGGSLFGNANTAGSNMFGSANSSTPGTGLFGSTQTNNATSNTGTGLFGSNNANTTNTGGSLFNKPSTTTGGLFGNTTAQQPSTTTSGLFGASNTNNQAQTSNFGTGLFGGSQAGQQQQPLQASIDQNPYGNNPLFSSTTSQVAPTSIQEPIASPLTSKPTPKKAASLPQFWLSPRSHNTARLASISSFAKSAVMNSTSASGKPKSLHLFDSLNDDVLLSADAFTPRQNIKKLVITHKISKDDILQNGVKNGNDAKSDSKVQEKAPQNEADGSLKKDEHVVLSDDYWMKPSIEELSKYPKEKLCSVHQFSVGRTGYGQVAFLKPVDLSGFEKLEDIPGKVVVFERKICAVYPVEGSSPPLGEGLNVPAIITLEKTWPLSRETREPIKDPQNPRYIQHVKRLHRIKDTEFIDFNDGKWIFKVQHFSRYGLLDDEEEENDMSSTSNEAGNLKKYDQPNLKVSGKNDSFVTHHTPGAFPNDSKNKELNRHFLKVDDSAPLDDTFMSKKVKLDFSSDSNVSERGDYDDNAKKVDEVISIEKVDGYSKENNVPLSEDDLSNSSESSNESVYSLVEESDASLAADNMDIEDISEESDREELSSMRFGAQDFHGLVVTDNWRDQLNLSVQRSALIKAAFPESQSNANLKNSRGIYYNEHDLVTDIFGNQNLDTDRPWQSLDKPGAFIPSKFHFTANGSCIYVLKSSDVKIRSIYDFIPTKDPNGTKLLEYQLDQTEVYLDLSGTHAASPRSSMTVKPLSLCSSGYESIVWDLTSILFDPKNYSLPSELSSEAREVLYQKLVRESLSEWITKTLEHETTTLAKEAETSEERIYILLTGNLIGQACEEAVQSQNNRLSTLIPLVNSDVDIQQEVKQQLEEWRKHGDLPFINKFTRLIFELLSGNTDIAEGCGTKGDEDYVQSIPITKNMTWLRAFGLKLWYNTDISIGEAMQLYVESLQKFPEIMQKPIATSAVQGIEVYDIIYLLLKAYAMGTSLEELTIPESAKCSPLNYRVVWQLAIYLSKARSLCDFSDRVVDINMAEDLKPISVHSDQLTLAYASQLEASGQWLWSLFVLLHLENVETRTSTITSCLARNLRGGLGAGAVEMIEKLCIPESWLNEAKALYARYVGDHLNELYFLQEAALYEDAHKVLLDTLAPQAVISGNKTQLKKALEGFNGQTDGLASWRFGGQIYSDYLDLLEGNFDANQELKLFTLRKISVALKELNATNLLQKAALHKISRFVNALCNEESLTDAICNLPLPLADSLANLQNISVQF Q9UTK5 ALM1_SCHPO MOD_RES 1706; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1486.04c; CHAIN 1..1727; /note="Nucleoporin alm1"; /id="PRO_0000064565" MSSGGLEDDIQLVHEFLDVSFEDIKPLVSVNGFAVFISAIKTKVKDINALKDQLVLQEVNHEHKENVLTKKINFLEQQLQSSNNQAEESRNLISVLRNENESLKTNLENQNKRFDALTTENQSLRRANSELQEQSKIASEQLSIAKDQIEALQNENSHLGEQVQSAHQALSDIEERKKQHMFASSSSRVKEEILVQEKSALVSDLASLQSDHSKVCEKLEVSSRQVQDLEKKLAGLAQQNTELNEKIQLFEQKRSNYSSDGNISKILETDPTSIKELEEEVETQKRLTALWESKSSELQSEVAALQEKLTSQQSLYNNVTEELNNNKQQLLISENSLRELQEKYDSVVSELQVVKENKNTSVSAGVGLFSPLAQKLSAVQNPEFSFTKVYSDNMKLQQKVSSLKLQLDRLTNKFSSFCEQVKQRIPVVKQQRSEIVRNNIYMNFLSESLETSNNNLTKVQAELLSTKMRQEACYLQLTASRTQCSDLSREVICLMAELDHLNETKSRNVPATVQVALDEYAQNPSTASETLVNKELANFSSIKEAVSKTLELREKVRALECDVEIQKQTVQYQISNAVKENSNTLSEQIKNLESELNSSKIKNESLLNERNLLKEMLATSRSSILSHNSSAGNIDDKMKSIDESTRELEKNYEVYRNEMTAIQESLSKRNQDLLSEMEAIRKELENSKYQQQLSTDRLTNANNDVEAFKKEAKELRSINQNLQDIISRQDQRASKFAEELLHVNSLAERLKGELNASKGEKDLRKRTQERLISENDKLLAERERLMSLVSDLQTFLNQQQLSDAARKVKFESEKESLSLSLQKLKESNEKMSNDLHSLQKSLEKSGIEYSSRIKTLMLEKQSLSEDNRKLLDNQQMMEIKLQELNGVIELEKQRFSTLEAKFTQQKNTSYSEREALLESSLSDLQSKHTSLESQYNYSLRNIEQLQAASKLAEEMVERVKTEYDEYRLQTSESLEKNHLKITSLEQRIVILQDEIASSSLRCENITKDSETRVALLLEENKHLNNELSSHRNAEKQHLEKENDYKQQLLLVTEDLRKTREDYEKELLRHADARSTLQKLREDYTKALEQVEDLNKEIALKAGINESQPFPISEKEDPLRQEVYVLKKQNAMLLTQLQSSNLNFAEITSPSPDLDSVMKLGLSDLQNHVKRISKEMEIISCQRQLLFLENKKLKRTVESSNRVIADLQRGITEKDVSSTSESVGERSNYLNMVALLNESNKSLRENLERNEEVITELREKIETLKTDLANFRLNKEQLESQLQTEKAAVKKLENSNEEYKRHNQEILLSLNSSTSTSSDASRLKNELVSKENLIEELNQEIGHLKSELETVKSKSEDLENERAQNQSKIEQLELKNTKLAAAWRTKYEQVVNKSLEKHNQIRQQLSQKTSELEAKVAECHQLNEQLNKPSATPTATTQSEPSTVSLEEFNSTKEELSSTQRKLSEIMDILNTTKEELEKVRQNSNKSEGTSKDTEIPNEEEMERKKVMQQEVLRLRSRIAKELQKNELLRKQNQVLQDQVKALQETVVSSEEAESASVHADTKDLENLKKTEEMLSVTFQVIFNESISDFSTSTADFTTFVQKEWEKRREILQKDVEEQVAQSHQKQLDNIRKELEMRNKLKLSMLEKNLARVRAELEQSKKKDSPAILSLEASKNTDSNKSNSEVPAAQVKEKKLIAKTHSVDTNSPPKRSSSDAGMDVSNDVKKAK Q9UTK7 DSC2_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305}; MOD_RES 264; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 266; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1486.02c; CHAIN 1..372; /note="DSC E3 ubiquitin ligase complex subunit 2"; /id="PRO_0000314098" MSSANIVPSNMGITKFLLLTISTSSVVAGVFALKPFFHINFGLHLLSHYQYWRILLWQFIYWNSTEVFQALFIIYQARDVERLLGSHRFASFCVYMFILGMFVTPIFSFLYSLLFKNLDYIQPGPTFLIFAILYQYYYIVPSTVFVRLFNIKFTDKFQMVIPMIGLAFSHFPSTFINAFLGWTMGMFYHLSLLPGTSWRLPIRFVKPALSPTHVFIRPPYSDMQNASTFNPETLFALPTGLDAERTENENQVENPVSNADANDSPTRQNARATAIASSSNTAASFRNRQQISHPPLGRTSSSSVLPTGPASQLYDMLSGRSERPELGNIREEDINTVQTIMQTSRAQAIQALSQTNDVQRAVELLLEQTADY Q9UTL6 JAC1_SCHPO TRANSIT 1..49; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC144.08; CHAIN 50..225; /note="J-type co-chaperone jac1, mitochondrial"; /id="PRO_0000363388" MLKQAGNQSFRPFISFAQKSLFNRQITGNHWIFARFKFYPLNKIVNYNHFHSSSCQSEAKNFYKQFEGDISDPPPKGPFDIDLGALKSSYLRKMKTLHPDVAQGKDAALAQRDSAELSKAYNTLKAPLTRAEYILQLQGINPVSEDISNSDPEFLMEIMDVHENISASRDSPEKLLQLSQENQGRKVQEINEIRKAMESSNWDSALLYVNRLRYWNTIDKILHDL Q9UTM2 CO111_SCHPO BINDING 323; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0"; BINDING 329; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0"; BINDING 342; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0"; BINDING 430; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0" TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: Specific enzymatic cleavages in vivo by mitochondrial processing peptidase (MPP) yield mature proteins including rsm22-1 and cox11-1. {ECO:0000269|PubMed:16835444}. SPAC1420.04c; CHAIN 40..753; /note="Rsm22-cox11 tandem protein 1, mitochondrial"; /id="PRO_0000352836"; CHAIN 40..568; /note="Ribosome assembly protein Rsm22-1"; /id="PRO_0000352837"; CHAIN 569..753; /note="Cytochrome c oxidase assembly protein cox11-1"; /id="PRO_0000352838" MPILTCRYKILFLYNLRNCFTFQNQRCLIPYGTTTTIRWYNANFQAVQNNFSDYKNELISSHRPEASSLLDFLVKDQKKSGDISLHTKFNLYVDDLLKKSEKGQIKKFINDIKKDLATESQLPLSAPFKDESTRTMTDPQVLAYIHQSMPYQYASLYSVLTDLKIVNSDVSCKSQHILDCGKGPGIGALASYSVFPTPNSVSIVEENPFLKKIIYDIHHNIYPSTSPNPTSPVTLNRLPLGKKDSYTLVIASNKLLEMKSEKELFDYLRSLWSLVSNDGGLLVLCERGTKRGFSLIQRARTFLLQKSKNTSDKQFNAHIVAPCPHDGRCPIDIENGVRANICSFKQHFFLSPFSRLYVPRSHRRSSDRSHYSYVVIQKGITRPLNNTTQRFKNDEDLLENVNVTSPTLKNWPRIIRPPLKRDGHVIIDVCDSDARLRRNIVPKSQGKLAYRLARKSAWGDLFPLEGKVQSTSPSSKITKHLKDASSTYSINPPSYNKPKVERNTTADPIFVGKRFYSTNRHKAFSRFADFNSHRFPCIFTSFSCYNCISGTRKYSRQYSRDKFHYNQRTTIYYLVAISIFALGLTYAAVPLYRLFCSKTGYGGTLNTDQSRMNAERMVPRKDNKRIRVTFNGDVAGNLSWKLWPQQREIYVLPGETALGFYTAENTSDHDIVGVATYNIVPGQAAVYFSKVACFCFEEQKLDAHEKVDLPVFFFIDPEFADDPNMKDIDDILLSYTFFEARYDTNGNLLTKLN Q9UTN3 CID14_SCHPO BINDING 298; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 300; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 364; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 389; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 407; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 408; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 492; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O13833"; BINDING 496; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O13833" CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000305|PubMed:16478992}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333; Evidence={ECO:0000305|PubMed:16478992}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O13833}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O13833}; SPAC12G12.13c; CHAIN 1..684; /note="Poly(A) RNA polymerase cid14"; /id="PRO_0000089746" MGKKSVSFNRNNYKKRKNERTEPLPRRIFKNDKPSKFKSKRKEKDKNSDAYDEMLLNNNFTLLDQEEPMVEIGSKKSRNDNDSEGIRDKGGVEISNKNDPYIQFGKADPLEPLEKPDLPEEAIKRGEPTILLGIPKREGRKTNPVHDKAVENNSDFIKFDWNSDEDEDSVSNDKSKNNESLKKSSKNEIPGFMRQRGRFFHEANEKSDSNRKRKRQAYELDSQSCPWHRQYKVEREVSRIFHQDILHFIDYITPTPEEHAVRKTLVSRINQAVLQKWPDVSLYVFGSFETKLYLPTSDLDLVIISPEHHYRGTKKDMFVLAHHLKKLKLASEVQVITTANVPIIKFVDPLTKVHVDISFNQPGGLKTCLVVNGFMKKYPALRPLVIIIKHFLNMRALNEVFLGGLSSYAIVCLVVSFLQLHPRLSTGSMREEDNFGVLLLEFLELYGKQFYYDAVGIAVHNGGFYFSKKKMGWLKPNQPYLLSIQDPVDFQNDVSKSSRGLLRVKATFANGFDLLTSKLYALASRIEREGVNRVKDFPSILSTILSVDEGVRQHREHMLKCYKNNPVPLEPLVEVDALASIDVDKLPLQDVGLQYVEDESDSDETDAAKDDLFKVNESIETNGHENFQKQALTSTGEQSSSNSRANPSKLFNISSDDSEDEVPIIEDTTASDEESRAKKIRKRF Q9UTN6 SNF21_SCHPO BINDING 442..449; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPAC1250.01; CHAIN 1..1199; /note="Chromatin structure-remodeling complex subunit snf21"; /id="PRO_0000074359" MRAEKQYTRNEVEETIVRWKKLKESGATEHDNTEYAQLCDVLRSAQSEIEARRDLKGHIKRCFSSVDKNTEKLILKQQVLAYKKLSQNLPAPDDCILSVLLRLSKDEQLLQSIVKQPLQNSKVDGKVRRDFGSCQITPSAKQQRKYLQYQISEDDAIKNRMFRRMSDLESYPAVMRDVAELKDDNERLNLDTIKRNALVELKKLRLIKQQESLRHQVMHCQPHLRTIVNAVERMSCRRPKLVPQATRLTEVLERQQRSDRERRLKQKQCDYLQTVCAHGREINVRTKNAQARAQKANRAVLAYHSHIEKEEQRRAERNAKQRLQALKENDEEAYLKLIDQAKDTRITHLLRQTDHYLDSLAAAVKVQQSQFGESAYDEDMDRRMNPEDDRKIDYYNVAHNIREVVTEQPSILVGGKLKEYQLRGLQWMISLYNNHLNGILADEMGLGKTIQTISLITHLIEKKRQNGPFLVIVPLSTLTNWTMEFERWAPSIVKIVYKGPPQVRKALHPQVRHSNFQVLLTTYEYIIKDRPLLSRIKWIYMIIDEGHRMKNTQSKLTNTLTTYYSSRYRLILTGTPLQNNLPELWALLNFVLPRIFNSIKSFDEWFNTPFANTGGQDKMELTEEESLLVIRRLHKVLRPFLLRRLKKDVEAELPDKVEKVIRCQMSGLQQKLYYQMKKHGMLYVEDAKRGKTGIKGLQNTVMQLKKICNHPFVFEDVERSIDPTGFNYDMLWRVSGKFELLDRILPKLFRSGHRILMFFQMTQIMNIMEDYLHYRQWRYLRLDGSTKADDRSKLLGVFNDPTAEVNLFLLSTRAGGLGLNLQTADTVIIFDSDWNPHQDLQAQDRAHRIGQTKEVRIYRLITEKSVEENILARAQYKLDIDGKVIQAGKFDNKSTPEEREAFLRSLLENENGEEENDEKGELDDDELNEILARGDDELRLFKQMTEDLERESPYGKNKEKERLIQVSELPEFYQREEPEKTTDLLQEEPLGRGARRRTPVVYDEAVRDAQWMAEMDMESEARPTRGRPKRNIASVDETPALTLNGKPKKKRGPAPDTLTSEHRSLLRRVCLEIYKAVNELEDDNGRPLNKLFLELPSKKLYPDYYMIIKSPIALDAIRKHINGTFYKTLEAMKSDLMTMFNNARTYNEEGSFVYEDANKMQTAMETKIEELEEDGTLATLRGMEAEATSQLEDRIENEA Q9UTR5 RGF2_SCHPO MOD_RES 746; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 747; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1006.06; CHAIN 1..1158; /note="Rho1 guanine nucleotide exchange factor 2"; /id="PRO_0000080971" MLRNGAQNGNINSESHESFGKAAKGFRIFSSFSSSQKLFQRRSSGSITHSPTALSSTTSLNENDGNHFRPASSLSFSPSSLSRKDSGPGDGLEVNKKNNFYRRSSSTDDFGISHARSRKEIQSLGRPHTRQSFSVSDVSNGSSYPNIRKNSVHVNAPMPSFPEGSTAVLLKHHSGSKSASAISNIAPSHSNSTSSRRPYIHPAFLSQVAVEFRKRLNIGDRVKDGLLYKDAFLGSEAVDVLMHIVRTTDRNLALLLGRALDSQKMFHDVTYSHRLRDSLKEVYQYRRIISPPPGLSSMDSNGSSIENNFLYTKRRANTSDSFDSVLSDSSTTPTISSSVQVNSLAFITSSLSAITKEPEAPETEYNPHGVFTLLTECYSSTCSRNRLCYSISCPRRLEQQARLHLKVQPVLSGGSTSITDKQEEDHRLWSENVPKQVVDQIDVREWKRQEIIFEVIYTERDFVRDLEYIRDFWIKPLSTSNVIPENNRQQFIRCVFHNIMQIHAVNSRLSNALNRTQTLQPVVNTIGDLFLDYVPKFEPFIKYGANQAIAKFEFEREKSTNRNFANYVHEVERLRESRKLELNGYLTKPTTRLARYPLLLSGVLKYTDKDNPDTENIPRVIEMIREFLTKLNYETGKTENRLSLLQLNEQLSCSPADRAKLTLFDPSRLLIFKGVVKLKASSYSNGDTENDIHMFLLDNFLLLCKIKIQMKRRVHKLHLRPLPLELLSISYIEDSPSRGSLPRRPSSALLTNPISITKSNPPPVKAYGLQLVFIGARGFSISLYLNTLIARDQWKQHIEKQQDIIRKRHLVFESRGICCQSWFTGNKLLCAVAYDAGRKLLFGTYKGLYISSRKSNNGSCLEPIFKLQLPNISQLDVIEEHNVLLLLAEKILYELPLDALDSVEQINSKSLRRVTGHVSFVKTGFCMQRILVCAVKSTVLNTTLRIYEADRALKNKKTQSLKKPFGNQATLKIFTEVQMPMEALSVHFLKTKLCVGSFKGFDIISLENAVFQSLLNPADTSFRFLEKREDIRPIAMFRLRGEFLLCYSDFAFFVNTNGWKSRQSWMINWEGQPQGCALCYPYILAFEPDFIEIRNAETAELVQIIMGQNIKLLTDGRGLISEGGEILYSTEPIPFSSGENPIVHSLILPPANAAGPAL Q9UTR6 OCH1_SCHPO CATALYTIC ACTIVITY: Reaction=Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.; EC=2.4.1.232; Evidence={ECO:0000269|PubMed:11231017}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P31755}; SPAC1006.05c; CHAIN 1..396; /note="Initiation-specific alpha-1,6-mannosyltransferase"; /id="PRO_0000080562" CARBOHYD 345; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLRLRLRSIVIGAAIAGSILLLFNHGSIEGMEDLTEISMLEDYTPEAANKDYVGQQEEEELLYDQPSYIEEEEDPDLEAYLSDLEREELEHSLEELDEENNYKLHLRYSFSQLQDFDEENEAVHMIVPKDTYEFEVPYHADIPKLIWQTSKDPFDREVMKYTRFWRINHPSYSHAVLDDEQSKALVISSFGDSSVSKISQAYAMMPLPVLKADFFRYLVLLAKGGIYSDIDTAPLKHINNWIPREYRKRNIRLIVGIEADPDRPDWNDYYARRVQFCQWTIAAAPGHPILWELVRRITDETWKLHDSKKLSKNGESVMEWTGPGIWTDAIMDYLNWQYGPFSVENITNLEEPYLVGDVLILPITAFSPGVGHMGSKSPNDPMAYVQHFFAGSWKDD Q9UTR8 RED1_SCHPO SPAC1006.03c; STRAND 312..314; /evidence="ECO:0007829|PDB:7Q72"; STRAND 317..320; /evidence="ECO:0007829|PDB:7Q72" HELIX 194..208; /evidence="ECO:0007829|PDB:7QUU"; HELIX 212..217; /evidence="ECO:0007829|PDB:7QUU"; HELIX 222..231; /evidence="ECO:0007829|PDB:7QUU"; HELIX 290..299; /evidence="ECO:0007829|PDB:7Q72" CHAIN 1..712; /note="NURS complex subunit red1"; /id="PRO_0000362152" MSRSINLDELRKKALESKKKNEEDESNDSDKEDGEISEDDPVIDQSNSVPPMKVPTFPEQIPQLPPFDRFPGTNANFFPFGAPFMLPPALMFGPNTVPFFPQTASSNKTFSKRKRSSENSFNNRNKAKSSETSDSSNTSQSFKENRALKDTATSRPLALSSDTSYQKSEKAKSEKSPFLSTSKNSDANYSKTTNQKEAEKAVSQLFEVGVRFNDFIAEGIEPSVVHTLFLKLGLDSSSASSQGSLTLSADKAARSAKLRKIDSNLSDTHILPGDNGTPTVLPERKNLISLPLLKQDDWLSSSKPFGSSTPNVVIEFDSDDDGDDFSNSKIEQSNLEKPPSNSENGLTMSRSDYLALLRNKEEEIRRMTKLILRLESNKKPYRSPTSAADMKLPSVPVAAVDNKSKTHLDTFEKVVDLSSKADFVEAGPSISSSGASSSAATTNSDTTEQILEAPWLRKTEQIAVVHEEHPAQIKKSEIDILNNLIEKEEGELTKYQTLVKSKTEILTQLYTRKKQLLEQQGKGNVACLPKESDLSMDSITEVSAQADENSSQILSSKTSNAPNGTTETDFEDKVPLVDYISPFYRFKSYRFNQQFVERVPLKYRSLTYSNKIEPMKVFCKYETTGGVCNDDHCEASHFRDIKMTDDEIIQDLSRYIEGNDEIEKESYKSGLDIVMKNTDENTDFVDVATRIVEYHNLWKSERMTIPVAKVSI Q9UTS6 DYLT_SCHPO SPAC1805.08; CHAIN 1..111; /note="Dynein light chain Tctex-type"; /id="PRO_0000195156" MSCPIDSKKLEEICLEAAQPVLKASEYDGDKTAEMNQSVIYAVLNALNKETQSYKWIVSSTLVQKLPEDHPSRGVHAAHAACWNCEKDGMTTIKESGEAIDVVLSIMWISI Q9UTT1 UBP71_SCHPO ACT_SITE 239; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 481; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:28947618}; SPBC713.02c; CHAIN 1..1129; /note="Ubiquitin carboxyl-terminal hydrolase 15"; /id="PRO_0000080614" MVLSNVDAEEVNMDSSMELEESSQEPLRADNYEEIYNSLVHHEPDLEEAAHASYSWVVKNFSTLEDKTYSPLFKAGHTTWRIVLFPKGCNQTEYASVFLEYLPQCKVEAIRKYEAELAAGKTPTIDPEIVNDETYSCCAQFALSLSNVQDPTVMQINTSHHRFRSEVKDWGFTRFVDLRKIAVPTPEFPVPFLENDEICISVTVRVLQDPTGVLWHSFVNYNSKKETGYVGLKNQGATCYMNSLLQSLFFTNIFRKTVYKIPTDNDDSRDSVAYALQRVFYNLEKQREPVSTTELTRSFGWNSFDSFMQHDIQEFNRVLQDNLEKKMKGTEVENALNDIFVGKMKSYVKCIDVNYESSRVEDFWDIQLNVKGMDTLEDSFRDAIQVETLTGDNKYYAEGHGLQDAHKGIIFESLPNVLQLQLKRFDYDMLRDMMVKINDRHEFPLEIDLEPYLSETADKSESHVYVLHGVLVHGGDLHGGHYYALIKPEKDSNWFKFDDDRVTRATIKEVLEDNYGGEPAGRAKGYNGNPFKRFMNAYMLVYFRKSRLDHILSPVTAEDVPFHVRNTLDEEHRVVERKLLEREEQQIYRRVRVLTTDGFKKYHGFDMTDFSASDDDPVLITTKIKRNANIWDLQKHLAGLLNRDTSGIRIWLMTNRQNRTVRVDLPLDKKTILVDQICDMHIRKDMDMRVYVEFLSEHNQLLADFGATDDNDFDTYIFLKIFDYETQQISGLADLHVSKNSPISSLSEWIREHLKWSSDVPITYYEEIKTGMVDVLDPNASFEKSEIQVGDIICFEKKLVHDSSSDTSHPYKSALDLYDFMAHRVVITFEPRYSDDTNNGVFDLVLTTHTNYTDMARAVANKLNVDPNYLQFTMAHLPSRTPRSVIRNPSKFTLQNAIPSTYSHNQNVVMFYEVLDITLSELERKQLIRVHFLSNGISHETQMEFYVDKEGTVEDILRQVTQKVPLNAEDASRLRLYEVYNHRILKSHLPTDGIYDLNEFSTAYVEVTPKEEQMQLKTDDAVSIVVQHFFKDLSRLHDIPFYFVLLRGETLKDLKKRLQKRLGYNDTQFSKVKLAVLQAQSFGKPYYLTDDDEVLYGELEPQSHILGLDHPPANGSAQYHGMDQAIRMK Q9UU89 ITPA_SCHPO BINDING 11..16; /ligand="ITP"; /ligand_id="ChEBI:CHEBI:61402"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148"; BINDING 39; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148"; BINDING 51; /ligand="ITP"; /ligand_id="ChEBI:CHEBI:61402"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148"; BINDING 67..68; /ligand="ITP"; /ligand_id="ChEBI:CHEBI:61402"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148"; BINDING 84; /ligand="ITP"; /ligand_id="ChEBI:CHEBI:61402"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148"; BINDING 143..146; /ligand="ITP"; /ligand_id="ChEBI:CHEBI:61402"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148"; BINDING 171..172; /ligand="ITP"; /ligand_id="ChEBI:CHEBI:61402"; /evidence="ECO:0000255|HAMAP-Rule:MF_03148" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; CATALYTIC ACTIVITY: Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148}; SPCC830.10; CHAIN 1..188; /note="Inosine triphosphate pyrophosphatase"; /id="PRO_0000316234" MTILQSILFVTGNKHKLADVKNILGDRFEIKNHDYDLPEIQGSVKEVVLEKCKAAAEIVKGPVLVEDTWLGYKAMNGLPGPYVKWFLNSVGPDGLYRMVSAFDTKEAQAGCTFGYTKGPGKPIHLFEGILDGQVVPPRGSNGFGWNSIFQPNGHKHTYAEMTDEERNSCSHRYLAAMKLRDFLESEKN Q9UU96 GRC3_SCHPO BINDING 338..345; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPCC830.03; CHAIN 1..736; /note="Polynucleotide 5'-hydroxyl-kinase grc3"; /id="PRO_0000087595" MVKRQRIESSNVPLSAFAVRQLTLSKAARKKDNSSGKKRSVSEEESQDKYEDEMKTEGEFPSYKHTLVQVVVPGVDHRTKLHSESSKNDSEITPDINRSKVNPQEYSEFSVASPQTISPSLPLNLDDETVSENVPHSPQSSNDAIPVIKITEENSFRVKDTLYVGLHKDQKLAMVGTFIFRSVRGKFQLFGATYSSACMSWFPLNAPLAFATPVFSAIDNALPAMQISEYEEDSLNLRSFAVPSYSPKEHEYELEPKDILPNFETVIAFRENENGLSKIARVLPFAKRLFSFKNLLQDASSISNNFEITPESWCSFSNQLLFSTSKSDYVVPRLMVCGPKGSGKSSFSRYITNRLLQQYRHIAYLDLDPGQPEVVPSGHISLYYINSPLQGPVFARMLFPTYMLRLHLGDISPQKDPDHYIACVTRLFAEYKDYIFNQEISQKEIIPLIINCPGWIRGGGAELLSSIVDICQPTEVVYMSREDMKSSHREKKSIYQHKEYMPDFLSSRDEFQLTLLESTWQYLPDPNVNKVTSADNRMLGLLSYLYFNCNLQRWDFTTSLTACQPIATAFKGSSKGIDAVNIIGEPLNVNDVAKTINGTLMALYACDTASLDNSNTQRIVSSPEGIPLIINDGLPLDPNTSHCLGLIVLRTIDLKRNEFHFVGPLNLELIKDAYAKSLKIVLERGRLELPVYAMLDHRLAQYSELPYLDRNHDRVAVGAHRRRVRRNIIRRSTFVG Q9UUA2 PIF1_SCHPO BINDING 332..339; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03176" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:12409464, ECO:0000269|PubMed:15302919}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:12058079}; TRANSIT 1..25; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 80; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC887.14c; CHAIN 26..805; /note="ATP-dependent DNA helicase pfh1"; /id="PRO_0000013268" MFSCQSLYKFSHSFRKRIPVMFQRAQQKSSLLHTQNESSHQPSLNKLGGFSSASLNFNSSRSSTNDDQQTFSSQSDNLPSSPITLPAKRGRSAASLKQLDNTVGFDVSKPSLPVFENSGLGSKYSTEIANGVYIDENDFDDDLLLENDIDQKPIPWSSSPIEHTKLTKSMLSSEKRSKNHLSKIYEDHTSEKGASSVISSNITRQGIKRSRTLPWAVDPYRYGDPDPKRTSTSADISQHTVSNDSSNKLSNGRSSSLDSLAKKRMSKSKSTPQISKKFSVPLNSASKSPIGSSLFKTSDSRKKSVPSIFLSDEQKRILDMVVEQQHSIFFTGSAGTGKSVLLRKIIEVLKSKYRKQSDRVAVTASTGLAACNIGGVTLHSFAGVGLARESVDLLVSKIKKNKKCVNRWLRTRVLIIDEVSMVDAELMDKLEEVARVIRKDSKPFGGIQLVLTGDFFQLPPVPENGKESKFCFESQTWKSALDFTIGLTHVFRQKDEEFVKMLNELRLGKLSDESVRKFKVLNRTIEYEDGLLPTELFPTRYEVERSNDMRMQQINQNPVTFTAIDSGTVRDKEFRDRLLQGCMAPATLVLKVNAQVMLIKNIDDQLVNGSLGKVIGFIDDETYQMEKKDAEMQGRNAFEYDSLDISPFDLPDVKQKKYKLIAMRKASSTAIKWPLVRFKLPNGGERTIVVQRETWNIELPNGEVQASRSQIPLILAYAISIHKAQGQTLDRVKVDLGRVFEKGQAYVALSRATTQEGLQVLNFSPAKVMAHPKVVQFYKQLASVNGLPIRNENKAPVQMRGVKNK Q9UUB1 RIB4_SCHPO ACT_SITE 94; /note="Proton donor"; /evidence="ECO:0000255" BINDING 27; /ligand="5-amino-6-(D-ribitylamino)uracil"; /ligand_id="ChEBI:CHEBI:15934"; BINDING 62..64; /ligand="5-amino-6-(D-ribitylamino)uracil"; /ligand_id="ChEBI:CHEBI:15934"; BINDING 86..88; /ligand="5-amino-6-(D-ribitylamino)uracil"; /ligand_id="ChEBI:CHEBI:15934"; BINDING 91..92; /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"; /ligand_id="ChEBI:CHEBI:58830"; /evidence="ECO:0000305"; BINDING 119; /ligand="5-amino-6-(D-ribitylamino)uracil"; /ligand_id="ChEBI:CHEBI:15934"; BINDING 133; /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"; /ligand_id="ChEBI:CHEBI:58830"; /evidence="ECO:0000305" CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000269|PubMed:11856310}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:11856310}; KM=67 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:11856310}; Vmax=13000 nmol/h/mg enzyme (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:11856310}; SPBC409.13; STRAND 20..24; /evidence="ECO:0007829|PDB:1KZ1"; STRAND 54..58; /evidence="ECO:0007829|PDB:1KZ1"; STRAND 79..88; /evidence="ECO:0007829|PDB:1KZ1"; STRAND 91..93; /evidence="ECO:0007829|PDB:1KZ1"; STRAND 117..126; /evidence="ECO:0007829|PDB:1KZ1" HELIX 29..47; /evidence="ECO:0007829|PDB:1KZ1"; HELIX 51..53; /evidence="ECO:0007829|PDB:1KZ1"; HELIX 62..64; /evidence="ECO:0007829|PDB:1KZ1"; HELIX 65..75; /evidence="ECO:0007829|PDB:1KZ1"; HELIX 94..113; /evidence="ECO:0007829|PDB:1KZ1"; HELIX 127..133; /evidence="ECO:0007829|PDB:1KZ1"; HELIX 142..156; /evidence="ECO:0007829|PDB:1KZ1" CHAIN 1..159; /note="6,7-dimethyl-8-ribityllumazine synthase"; /id="PRO_0000134856" MFSGIKGPNPSDLKGPELRILIVHARWNLQAIEPLVKGAVETMIEKHDVKLENIDIESVPGSWELPQGIRASIARNTYDAVIGIGVLIKGSTMHFEYISEAVVHGLMRVGLDSGVPVILGLLTVLNEEQALYRAGLNGGHNHGNDWGSAAVEMGLKALY Q9UUB6 UBLH2_SCHPO ACT_SITE 83; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 159; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPBC409.06; CHAIN 1..300; /note="Ubiquitin carboxyl-terminal hydrolase 2"; /id="PRO_0000234561" MSWTTIESDAGVFTDLIENLGVKDVEVDELYSLDVDSLRQFPDIYGIIFLFKWNSKVDKPDGTMDYDSMDNIFFAKQVINNACATQALLSVLLNHSDEIDLGTTLSEFKDFSKTLPPELKGEALGNSEHIRCCHNSFARSDPFISEEVRAATDEDEVYHFIAYTNINNVFYELDGLQAAPINHGSCTKEEFAEKAVSVIQARIANYDPAEIRFNLMVICKDKKASLLTREDLTDEEKAASIAVEDEKRLRWKRENQLRRHNFVGLFVELSKLLVKDRIDKNTWNSTLETAKAKYASQKRP Q9UUB7 SWI5_SCHPO SPBC409.03; STRAND 32..34; /evidence="ECO:0007829|PDB:3VIQ" HELIX 3..29; /evidence="ECO:0007829|PDB:3VIQ"; HELIX 36..67; /evidence="ECO:0007829|PDB:3VIQ"; HELIX 72..75; /evidence="ECO:0007829|PDB:3VIQ"; HELIX 76..79; /evidence="ECO:0007829|PDB:3VIQ" CHAIN 1..85; /note="Mating-type switching protein swi5"; /id="PRO_0000072351" MEKSQLESRVHLLEQQKEQLESSLQDALAKLKNRDAKQTVQKHIDLLHTYNEIRDIALGMIGKVAEHEKCTSVELFDRFGVNGSE Q9UUC6 SMD3_SCHPO SPBC19C2.14; CHAIN 1..97; /note="Small nuclear ribonucleoprotein Sm D3"; /id="PRO_0000122219" MSLCIKLLHETQGHIVTMELENGSTYRGKLIEAEDNMNCQMRDISVTARDGRVSHLDQVYIRGSHIRFLIVPDMLRNAPMFKVGPGRSVPLPTRGRR Q9UUD1 SREBP_SCHPO PTM: In low oxygen or sterol conditions, undergoes proteolytic cleavage by rhomboid-type protease rbd2 and is released as soluble transcription factor from the membrane. {ECO:0000269|PubMed:15797383, ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872}.; PTM: Processed form is phosphorylated. {ECO:0000269|PubMed:15797383, ECO:0000269|PubMed:18257517}. MOD_RES 898; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 899; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19C2.09; CHAIN 1..900; /note="Sterol regulatory element-binding protein 1"; /id="PRO_0000317067"; CHAIN 1..407; /note="Processed sterol regulatory element-binding protein 1"; /evidence="ECO:0000269|PubMed:15797383"; /id="PRO_0000317068" MQSSIPSVSVSVASPAMETPTKASPDSKSPNSVGAIPSSSPLASSTKASTSTPFVENCSNLLCDLASIVEDSPPTLTNTSLSPHSFSLSDMESSMSNWLNPFAFDNTMNSAPPLFTSTNMGSPNSLENSTNPLLSNCGSPNSFQNETFTGPSLNEFDADDKIQRQMKILHSVDTIDPSTVQNYPSADMSNPEVKLKTEEIITPMDTTCKPEPSAKKIKLSPSSEDSCSIPETLPFSAPKSRGSLSPSETPDFVAGPGGKPKKTAHNMIEKRYRTNLNDRICELRDAVPSLRAAAALRCGNSLDDEDLGGLTPARKLNKGTILAKATEYIRHLEAKNKELQKTNKQLSDRLAFYEDPSMAPPSNDTRAVNSVNVVSSSDYSVHQSSRPNLTQRAFTSPTLNTMGRTALNGMVGLGLFNYFGNDSSQSVYGLFALPPFLMSPFTGTVLFNMLKIGVVLLGLFYLLHDNSLFKGFKGEKKSKVSTRSSMSPSSILFRKTVFEKYCLLDHSTSTISLFFGLLIFTLKSAYGYLTHRLSALYTSSENWVYSEQQLAEVRNMEKLLDAQLMGGDAKVDRLRLLMVFASSFSLPPSSHTCALQAMYCQLIFSNTSVPSAIVSKCVAFFWNAAKKQHSKSSVHAELRELPECTANLIENSHADDVFSPNMVERLWVLAKCTRDSAQMSDSIISSLSDVLVLSPLEVLASWYAADLLDALLMESLSRKVEISEIEEIISLCPKNSSIIRHALLAKLVLFPENTADSLNEVLAAYKNTLDLCSQDKRKQSSVLKINLSKLFTLHSCLSLALQRLGYGDVSKRMYQEIFVPDSDADITPLSFIISWTALNTFAPICTSPKENDVVEKMAMYVRTAIGTLKIQDLKLSRKLINSCIDIGSRLQEDLGYVSSA Q9UUE5 NUP85_SCHPO SPBC17G9.04c; CHAIN 1..675; /note="Nucleoporin nup85"; /id="PRO_0000290672" MESSDEVDLPVYHLQNAPIENGKLNDWRSKGRTVAFKLHPFLRKGLAYINNKEFDENTLKSDKFEEVESLVYEFSTPSTLIEPNYLLTAWHELWEELQDTYMTPILDSEANLLLLTQFYGKISSLFRSKIIQVLEELQSRINEGEKDCQPVLDSLWEVESAWRCAEAIYFPPSSPYTLSTGILDWVNAYDPQPIADDGLEIMAYRIPYQHPEFWPYVNKTAIRGLFEQTISCLEMSGLTKEWPVLKETVDELIDILRYSPCTHQKRIRSVSDFERRWKLWRSRLANLRHVVKKHRDIDSEVLDDFVVLLDILNGNKEVIMLSCAHWQEYFSALAFLYGPLDCKNPEDISLLYQLATGEDSKFYVNGTIEYEQICVNLCSNEPLNAIKHAYLLDLGLAVHLADLLSKSGHLRDYITEEYPITLREHLILEYGQCVLESRNLWQTSFAYWKCVADSGYQRIKACIPYVPLSDVDAKETALQLCKQLKLRDEAQLVLTHWADELIARNHYGEALIALDNAANYSALNRVTWELFDICIAEKKSFSPDKDELLYELFSSPKACTPTLASIISPAATIHQYFFYLQHKKELNASELLVGLLTMVDFPSSRFPKLLELLHEFLNNPLQSNSTDFKLSLVNVYDCIAVLQDQQSTVKDQQLLLSIHERLSSAISWYFLHLKK Q9UUF3 SIW14_SCHPO ACT_SITE 189; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:22384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:37772819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22385; Evidence={ECO:0000269|PubMed:37772819}; CATALYTIC ACTIVITY: Reaction=1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:79723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946; Evidence={ECO:0000269|PubMed:37772819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:79724; Evidence={ECO:0000269|PubMed:37772819}; CATALYTIC ACTIVITY: Reaction=1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + H2O = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:79699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:74946, ChEBI:CHEBI:77983; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:37772819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:79700; Evidence={ECO:0000269|PubMed:37772819}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.13 mM for inorganic diphosphate (pyrophosphate) (at 37 degrees Celsius and at pH 5) {ECO:0000269|PubMed:37772819}; KM=1.64 mM for p-nitrophenylphosphate (at 37 degrees Celsius and at pH 5) {ECO:0000269|PubMed:37772819}; Note=kcat is 0.44 sec(-1) with inorganic diphosphate (pyrophosphate) as substrate (at 37 degrees Celsius and at pH 5) (PubMed:37772819). kcat is 1.24 sec(-1) with p-nitrophenylphosphate as substrate (at 37 degrees Celsius and at pH 5) (PubMed:37772819). {ECO:0000269|PubMed:37772819}; MOD_RES 156; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17A3.03c; CHAIN 1..287; /note="Inositol diphosphatase siw14"; /id="PRO_0000315935" MAIVFPFQLEKKLISITSDRDQISMSIPEVSSHDSCLNDCHSVNSEEQAKPVCCLELNAHKDGIKVVDTSNDASTFSNSPLVPDNFGVVYPGIIYRSACPRASNFNFLESLHIRTIISLRQEEYSEEDLHYFTKHHINYYHIAMPGSKHRKNDCISSSSNPDISDVDDLVRKTLQLLLNKENWPVLLHCSRGKHRTGIVIGCLRALMNWPVGNRLQEYISFSHPKEREVDEEYIQNFSSDPSLKSSLNDLKRYISDSSSELADVVLSSESPTVQAATVNETCRSPGS Q9UUG0 FAS1_SCHPO ACT_SITE 270; /note="For acetyltransferase activity"; /evidence="ECO:0000250"; ACT_SITE 1361; /note="For dehydratase activity"; /evidence="ECO:0000255"; ACT_SITE 1828; /note="For malonyltransferase activity"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).; EC=2.3.1.86; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; MOD_RES 1122; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 2073; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC926.09c; CHAIN 1..2073; /note="Fatty acid synthase subunit beta"; /id="PRO_0000180281" MVEAEQVHQSLRSLVLSYAHFSPSILIPASQYLLAAQLRDEFLSLHPAPSAESVEKEGAELEFEHELHLLAGFLGLIAAKEEETPGQYTQLLRIITLEFERTFLAGNEVHAVVHSLGLNIPAQKDVVRFYYHSCALIGQTTKFHGSALLDESSVKLAAIFGGQGYEDYFDELIELYEVYAPFAAELIQVLSKHLFTLSQNEQASKVYSKGLNVLDWLAGERPERDYLVSAPVSLPLVGLTQLVHFSVTAQILGLNPGELASRFSAASGHSQGIVVAAAVSASTDSASFMENAKVALTTLFWIGVRSQQTFPTTTLPPSVVADSLASSEGNPTPMLAVRDLPIETLNKHIETTNTHLPEDRKVSLSLVNGPRSFVVSGPARSLYGLNLSLRKEKADGQNQSRIPHSKRKLRFINRFLSISVPFHSPYLAPVRSLLEKDLQGLQFSALKVPVYSTDDAGDLRFEQPSKLLLALAVMITEKVVHWEEACGFPDVTHIIDFGPGGISGVGSLTRANKDGQGVRVIVADSFESLDMGAKFEIFDRDAKSIEFAPNWVKLYSPKLVKNKLGRVYVDTRLSRMLGLPPLWVAGMTPTSVPWQFCSAIAKAGFTYELAGGGYFDPKMMREAIHKLSLNIPPGAGICVNVIYINPRTYAWQIPLIRDMVAEGYPIRGVTIAAGIPSLEVANELISTLGVQYLCLKPGSVEAVNAVISIAKANPTFPIVLQWTGGRAGGHHSFEDFHSPILLTYSAIRRCDNIVLIAGSGFGGADDTEPYLTGEWSAAFKLPPMPFDGILFGSRLMVAKEAHTSLAAKEAIVAAKGVDDSEWEKTYDGPTGGIVTVLSELGEPIHKLATRGIMFWKELDDTIFSLPRPKRLPALLAKKQYIIKRLNDDFQKVYFPAHIVEQVSPEKFKFEAVDSVEDMTYAELLYRAIDLMYVTKEKRWIDVTLRTFTGKLMRRIEERFTQDVGKTTLIENFEDLNDPYPVAARFLDAYPEASTQDLNTQDAQFFYSLCSNPFQKPVPFIPAIDDTFEFYFKKDSLWQSEDLAAVVGEDVGRVAILQGPMAAKHSTKVNEPAKELLDGINETHIQHFIKKFYAGDEKKIPIVEYFGGVPPVNVSHKSLESVSVTEEAGSKVYKLPEIGSNSALPSKKLWFELLAGPEYTWFRAIFTTQRVAKGWKLEHNPVRRIFAPRYGQRAVVKGKDNDTVVELYETQSGNYVLAARLSYDGETIVVSMFENRNALKKEVHLDFLFKYEPSAGYSPVSEILDGRNDRIKHFYWALWFGEEPYPENASITDTFTGPEVTVTGNMIEDFCRTVGNHNEAYTKRAIRKRMAPMDFAIVVGWQAITKAIFPKAIDGDLLRLVHLSNSFRMVGSHSLMEGDKVTTSASIIAILNNDSGKTVTVKGTVYRDGKEVIEVISRFLYRGTFTDFENTFEHTQETPMQLTLATPKDVAVLQSKSWFQLLDPSQDLSGSILTFRLNSYVRFKDQKVKSSVETKGIVLSELPSKAIIQVASVDFQSVDCHGNPVIEFLKRNGKPIEQPVEFENGGYSVIQVMDEGYSPVFVTPPTNSPYAEVSGDYNPIHVSPTFAAFVELPGTHGITHGMYTSAAARRFVETYAAQNVPERVKHYEVTFVNMVLPNTELITKLSHTGMINGRKIIKVEVLNQETSEPVLVGTAEVEQPVSAYVFTGQGSQEQGMGMDLYASSPVARKIWDSADKHFLTNYGFSIIDIVKHNPHSITIHFGGSKGKKIRDNYMAMAYEKLMEDGTSKVVPVFETITKDSTSFSFTHPSGLLSATQFTQPALTLMEKSAFEDMRSKGLVQNDCAFAGHSLGEYSALSAMGDVLSIEALVDLVFLRGLTMQNAVHRDELGRSDYGMVAANPSRVSASFTDAALRFIVDHIGQQTNLLLEIVNYNVENQQYVVSGNLLSLSTLGHVLNFLKVQKIDFEKLKETLTIEQLKEQLTDIVEACHAKTLEQQKKTGRIELERGYATIPLKIDVPFHSSFLRGGVRMFREYLVKKIFPHQINVAKLRGKYIPNLTAKPFEISKEYFQNVYDLTGSQRIKKILQNWDEYESS Q9UUG5 MLR1_SCHPO BINDING 58; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 60; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 62; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 64; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 69; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC926.03; CHAIN 1..184; /note="Myosin regulatory light chain 1"; /id="PRO_0000198764" MFSSKENSLGAKRAPFSSNTTSSQRVAAQAAKRASSGAFAQLTSSQIQELKEAFALLDKDGDGNIGREDVKTMLTSLNQDASEDSINHMFESINPPINLAAFLTAMGSMLCRISPRNDLLEAFSTFDDTQSGKIPISTMRDALSSMGDRMDPQEVESILRSYTSHGVFYYEKFVDAIAGSKDSN Q9UUG9 TSC2_SCHPO MOD_RES 1036; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC630.13c; CHAIN 1..1339; /note="Tuberous sclerosis 2 protein homolog"; /id="PRO_0000065657" MNNKSLLDLSSEPAIKDTDILSYFDANLPFKKRHQIVRSIYHGLKYYIYSSTSIIQVWQNIQDFISTKNDNAAFRELVYNLMMRYVSTQKHLSIIERHTFFQTIEKDPFQDIAELQLRLKSLSVLTDEGHKISGIENRVGPLLSAWFNQYLQWQSQATELQGKDADSKLVHLLFFKSLFKFSTNLVKFQWFLVPEPQMLQLVNSVVQICNHARLEDVVTEVLMFFDSMIRYSVIPKASLYDTVLILCSTYISTYSYSKLAQSVIFNLISSPVSNLAFENVFNILQYNRSNVNAVRGAVRLMRFLMLQEVKNDAIASITLSSSIEFTEFPLGFNENVDFEILGTVYLFLRTPSILNRLNFLDWHRILNILMYCSQYLPLKASTSKEAFSKTAAFANIYDRVLDFLDFEALIPLLQQFQVKLVFFLKDVLPVLKPKIRKKLLRLFETYNLIFPCNQYWVFNLEFLLGIYQCKTFDLEDRALLFKLVEDACSVADENSAPILCSKFLFPVIESFSKESDDCVVSPVYNMLFFLSVNFQNPGLKDCIDHIFQQLISDTSSVTVRRLATSTLIRLFYYYYDLRDAVPIQETLAKMLEILETPSFPFVSRMLCLQFFLRFRANGTSIYICENIDLNEPFKVLNVDSELIPAVYPISDSFVNSATVEKHIWERKENDLIKISNHSTEYGKDFVTFPTSSLLRFYRKSMATESNWTILMFMITHLADQISNRSMFIGALEEIYNLLDFMCDIVFERVSISAEIPSNIRKANIMIPILQNVQMLFVYHDQFSRAQEDELVSVFFAGLQKWNEACHVSIHSLMLCCYELPVSIRKQLPAILVTLSRLITKPDLSVHILEFLCSLARLPDLIANFTDADYRQIFAIALKYIQHRDFTKESKDSNDTESILKNSYSSYVLALAYSVLQIWFLSLRLTERKKFVPWILRGLKLASEGKPLEDLCLVQYDMMQQFCYSNSDINNQTSTFVDSDVESETWIRGNSLFTINVSVNSGFLEAVIRRPTGTTQYTFRNEASLQKFLWEENLTSSKALTRGLLCTPSSFVSHFLDPHGISLYNQPLLLPSNDDSVRRAISVFDRIPVIESLKAGLVYVGYQQRREADILANTNPSEDFLTFLNGLGTLFELKTDQKVFAGGLDRENDIDGAFAYCWKDKVTQMVFHCTTMMPTNIEHDPGCTLKKRHIGNDFVTIIFNESGLEYDFDTIPSQFNFVNIVITPESESIRRTGRQIKFYKVKALTKYDIDFSLFRRYKIVSSDALPAIVRDVTLNAAVFSHIYHRSAGDYVHIWAERLRQLKRLREKFQASVLPEDYNLDEQTKTKLQNGTNFSDFTSYL Q9UUI1 LSM6_SCHPO SPAC2F3.17c; STRAND 15..21; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 26..34; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 40..49; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 52..62; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 67..72; /evidence="ECO:0007829|PDB:6PPQ" HELIX 4..12; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 64..66; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..75; /note="U6 snRNA-associated Sm-like protein LSm6"; /id="PRO_0000125577" MDSSPNEFLNKVIGKKVLIRLSSGVDYKGILSCLDGYMNLALERTEEYVNGKKTNVYGDAFIRGNNVLYVSALDD Q9UUJ1 ARP2_SCHPO BINDING 156..158; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 210..214; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 301..306; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" SPAC11H11.06; STRAND 6..10; /evidence="ECO:0007829|PDB:8UXW"; STRAND 12..19; /evidence="ECO:0007829|PDB:8UXW"; STRAND 26..30; /evidence="ECO:0007829|PDB:8UXW"; STRAND 33..38; /evidence="ECO:0007829|PDB:8UXW"; STRAND 51..54; /evidence="ECO:0007829|PDB:8UXW"; STRAND 65..68; /evidence="ECO:0007829|PDB:8UXW"; STRAND 70..72; /evidence="ECO:0007829|PDB:8UXW"; STRAND 75..77; /evidence="ECO:0007829|PDB:8UXW"; STRAND 102..107; /evidence="ECO:0007829|PDB:8UXW"; STRAND 130..136; /evidence="ECO:0007829|PDB:8UXW"; STRAND 148..155; /evidence="ECO:0007829|PDB:8UXW"; STRAND 160..166; /evidence="ECO:0007829|PDB:8UXW"; STRAND 176..179; /evidence="ECO:0007829|PDB:8UXW"; STRAND 238..241; /evidence="ECO:0007829|PDB:8UXW"; STRAND 247..251; /evidence="ECO:0007829|PDB:8UXW"; STRAND 297..301; /evidence="ECO:0007829|PDB:8UXW"; STRAND 368..370; /evidence="ECO:0007829|PDB:8UXW" HELIX 55..59; /evidence="ECO:0007829|PDB:8UXW"; HELIX 60..64; /evidence="ECO:0007829|PDB:8UXW"; HELIX 79..91; /evidence="ECO:0007829|PDB:8UXW"; HELIX 113..125; /evidence="ECO:0007829|PDB:8UXW"; HELIX 137..144; /evidence="ECO:0007829|PDB:8UXW"; HELIX 182..195; /evidence="ECO:0007829|PDB:8UXW"; HELIX 203..205; /evidence="ECO:0007829|PDB:8UXW"; HELIX 206..216; /evidence="ECO:0007829|PDB:8UXW"; HELIX 223..231; /evidence="ECO:0007829|PDB:8UXW"; HELIX 253..256; /evidence="ECO:0007829|PDB:8UXW"; HELIX 259..262; /evidence="ECO:0007829|PDB:8UXW"; HELIX 264..267; /evidence="ECO:0007829|PDB:8UXW"; HELIX 274..282; /evidence="ECO:0007829|PDB:8UXW"; HELIX 290..294; /evidence="ECO:0007829|PDB:8UXW"; HELIX 302..304; /evidence="ECO:0007829|PDB:8UXW"; HELIX 309..324; /evidence="ECO:0007829|PDB:8UXW"; HELIX 330..335; /evidence="ECO:0007829|PDB:8UXW"; HELIX 346..348; /evidence="ECO:0007829|PDB:8UXW"; HELIX 349..360; /evidence="ECO:0007829|PDB:8UXW"; HELIX 365..367; /evidence="ECO:0007829|PDB:8UXW"; HELIX 371..377; /evidence="ECO:0007829|PDB:8UXW"; HELIX 378..384; /evidence="ECO:0007829|PDB:8UXW" TURN 92..94; /evidence="ECO:0007829|PDB:8UXW"; TURN 172..174; /evidence="ECO:0007829|PDB:8UXW"; TURN 287..289; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..390; /note="Actin-related protein 2"; /id="PRO_0000089076" MESAPIVLDNGTGFVKVGYAKDNFPRFQFPSIVGRPILRAEEKTGNVQIKDVMVGDEAEAVRSLLQVKYPMENGIIRDFEEMNQLWDYTFFEKLKIDPRGRKILLTEPPMNPVANREKMCETMFERYGFGGVYVAIQAVLSLYAQGLSSGVVVDSGDGVTHIVPVYESVVLNHLVGRLDVAGRDATRYLISLLLRKGYAFNRTADFETVREMKEKLCYVSYDLELDHKLSEETTVLMRNYTLPDGRVIKVGSERYECPECLFQPHLVGSEQPGLSEFIFDTIQAADVDIRKYLYRAIVLSGGSSMYAGLPSRLEKEIKQLWFERVLHGDPARLPNFKVKIEDAPRRRHAVFIGGAVLADIMAQNDHMWVSKAEWEEYGVRALDKLGPRTT Q9UUK2 GCN5_SCHPO ACT_SITE 191; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q92830" BINDING 195..197; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q92830"; BINDING 202..208; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q92830"; BINDING 234..237; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q92830" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:14988732}; CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q03330}; SPAC1952.05; CHAIN 1..454; /note="Histone acetyltransferase gcn5"; /id="PRO_0000211199" MSNSLNDQTRPPDSSVVDSTSSNFPNASNDSVHDKPVKQDEQSNPNVREAIANSDGQESLAVKENKDTESSSSHFVPNGVSNSKKRKLVATDLDVDFDISSVRVTEKPSVLEEKSGVIQFRVVSNDDTADSMIMLTGLKNIFMKQLPKMPKEYITRLIYDRNHLSMTIVKDNLHVVGGITYRPFEQRGFAEIVFCAIASNEQVRGYGSHLMNHLKDYVRGTTTIQHFLTYADNYAIGYFKKQGFTKEITLDKSIWVGYIKDYEGGTLMQCTMIPKIKYLEANLILAIQKAAVVSKINRITRSNVVYPGLDVFKDGPAHIEPSQVPGLMEVGWCKEMEELSKKPRPKPFFAVLEMLFTEMQNHPSSWPFMQPVSKEDVPDYYEVIEHPMDLSTMEFRLRNNQYESVEEFIRDAKYIFDNCRSYNDSNTTYYKNADRLEKFFQKKLRETEYSHLAD Q9UUM2 SWI1_SCHPO MOD_RES 528; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 536; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 970; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC216.06c; CHAIN 1..971; /note="Mating-type switching protein swi1"; /id="PRO_0000072348" MELDEVIQGIVSAIGGFDYSDDEKVYVLGDEALACLKDLKRYLQVVDEKYKVWQIRSLLSSLQLVTNDICPILSDWDKDITNYRNWRIALACVELLVPLTWPLETEHETFRENVDVLYNLRQAQSNYKNSILSYKKGSVLSAILAVLLKPLSTPAESRTLRDKGIIRIVLLLFRNILQIDELKTKNETIISFAKAHILDLIVTLVSNLDEFEHFDVYILEIVYNLIRGCKPSALFSDASLTNSQTELNSLLLKESTQNRYLKRNAHTRHNRFGTMLSVQTEDRRFTIASQNIKTDGLDELDSHKRFRKRGTRRKHFDDINKSFFINTEAGTALRNFAVEFLEAGFNPLFQSLLKDLEREDPRVLPIHKMQLLYVQSFFLEFMRFSSKPKKTEEIYSNDYSFGLAASVFDQRALIMHNRLMVESFEMKQWSTFQASMLSMTQLLFTLRSMTLCSSEIYQRIADNLLSNIFYQEEILLLVYSALKHFKTQSFGYLDAITELTIVLLKELEKFSSAKQYLYVKKRRRNQKSVDSNVLESDEDEESSLINANAAVEDRLFDFGRYESRYCDNGCIDSFVLFLQCYQDLDSKQIHRAISFFYRIFVKQKCHVYLYRLDFLRVLDKMFNDHVYFSTTNSARQDFEQFFVYYMRKLSDALKDVPALFIELPFPKLTDTFYYLEYGKSPLFSIHGSRKGPLYETVPGLSHLEKVAAVVACLINENKSDLLDELKVQLNCLISERKLITLADENKYINEGGNDGERMGKNLKGDTDSFNTALLKDGKFRLLLELCGFEESDNNIDVQALWKLPNSVIIDELVEHAMLLRRFTDDPPTFEGTKPEDLLVRKQRGNVRLPSSSEGETSDEEIEFEADDPITFANRREALNKITDRKRKKMKTNETIIDHTTRKKKENHLRSAKYIVDSDDDSETDIAFFQSEAALREKNAQKASALFKRIDDLEMEGKLQEIEQLSENSSSD Q9UUM7 HOB3_SCHPO SPBC725.09c; CHAIN 1..264; /note="Protein hob3"; /id="PRO_0000192959" MSWHGFKKAVNRAGTSVMMKTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDAGSKDGVSAYYRQVVEDLDADTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDNSVREDYSNGLLDDKVEQVLQSMRDLSIAGLNNSQ Q9Y705 SPC97_SCHPO SPBC365.15; CHAIN 1..784; /note="Spindle pole body component alp4"; /id="PRO_0000078132" MVRSISSVLAKEESENGSPIPALEEGSVYHVSLKSEGVSPFSDRIQLNYLYDGKTFSDPSNLNIHQQEACLINELLNAFMGMEGVFVHLQDMKASSEFETIIMPPSFYILPGFDLGIKDIASEMLEMGSHYLSITAFIESRSHFEYGFVNHALCAALRKFVMDYVVLIMQCENQSRIDPNFSLQTLRLYTLPTSRSLRQVYLILRDLLLSMEKNASSSDDLGLSNIDDLLEQLNEGNDISHVVNATRSKKKVCKGGQVISFLTESLTKYAGDPVARKILTYLLREASRPYTKMLNEWIHLGLVNDPYDEFMIKIHKGITSMQLDEDYTDEYWEKRYVIREDQVPPQLLDLQNKVLFAGKYLNVVLECRKGVNNLASLNAKDDTQNQLLWPSTFDDDNFTLNIMNAYVYANESLLQLLQSSQSLYAHLYSLKHYFFLDQSDFFTTFLDNAQHELRKPAKYISITKLQSQLDLALRQPGTITATDPHKEYVTVEVNQTSLIDWLMHIVSISGLEEGTSSQGNEVWNESITKQADVGNETRNFESEHNRSTQGTSKVGSDKDINGFETMQLCYKVPFPLSLILSRKAIIRYQLLFRYFLLLRHVEMQLENSWVQHSKNSAWRLNSSNAKIEQWKRNSWLLRTRMLSFVQKIIYYTTSEVIETHWGKFMGELENARTVDNLMQEHIDFLDTCLKECMLTNSRLLKVQSKLLNTCAMFASYTSTFTRSLYLLENSEESFDEGRMDKMEEILRRYEDSFSRHLKSLVNACNYFASTETAALLSLVMKLTG Q9Y709 SKP1_SCHPO SPBC409.05; CHAIN 1..161; /note="Suppressor of kinetochore protein 1"; /id="PRO_0000271429" MSKIKLISSDNEEFVVDQLIAERSMLIKNMLEDVGEINVPIPLPNVSSNVLRKVLEWCEHHKNDLYSGTEEESDIRLKKSTDIDEWDRKFMAVDQEMLFEIVLASNYLDIKPLLDTGCKTVANMIRGKSPEDIRKTFNIPNDFTPEEEEQIRKENEWAEDR Q9Y738 MIS12_SCHPO MOD_RES 190; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:12773390"; MOD_RES 192; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:12773390"; MOD_RES 213; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:12773390" SPBC409.04c; HELIX 3..7; /evidence="ECO:0007829|PDB:5WWL"; HELIX 9..36; /evidence="ECO:0007829|PDB:5WWL"; HELIX 41..44; /evidence="ECO:0007829|PDB:5WWL"; HELIX 46..77; /evidence="ECO:0007829|PDB:5WWL"; HELIX 84..89; /evidence="ECO:0007829|PDB:5WWL"; HELIX 103..155; /evidence="ECO:0007829|PDB:5WWL"; HELIX 166..187; /evidence="ECO:0007829|PDB:5WWL"; HELIX 196..212; /evidence="ECO:0007829|PDB:5WWL" TURN 95..98; /evidence="ECO:0007829|PDB:5WWL" CHAIN 1..259; /note="Centromere protein mis12"; /id="PRO_0000096492" MLVELLEFTPLSFIDDVINITNQLLYKGVNGVDKAFSQTRFAKKAPQEIEEGLHKFEVLFESVVDRYYDGFEVYTLRNIFSYPPELKGYMRTFGKDVDYSITTEQDAAMDQAIQEAAEKLVVKMQLRRDLRMRLSRKREKKTEIEKHLERISFLNKVPENWQVTLPETTDFLLDQLGNLQHAVKRVVEASPTVHSREVDERITYLEKGYERLSNPIDQQKDFWSHHLSKLESTANTETANNIHKLLLSSEKDVGHTDEP Q9Y794 ORC4_SCHPO BINDING 541..548; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 582..589; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 405; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 406; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP23A10.13; CHAIN 1..972; /note="Origin recognition complex subunit 4"; /id="PRO_0000127090" MSSSPFTNLGNLDTEAIYENKENEYQTNITNETSNVQNLSSGNDDQQYPNSTNDDANNGLTASQAKLQDIAAVTLFQDNNISTTTLAPPSPSPLRLNEAPRRRGRPRKYPPKPIDEGSEPIIKRKRGRPPKIKSSSPSTKLDDPLKPKRGRGRPRLHPLPVVQPSVDEGTTQNNLQMGLDEPNIIEGFAEGHANLSELKPKRGRGRPRKIKPEEGSSSQNGLSPLVVLPAKRGRGRPPLHRSEQKIANTPISNNVTVESTGTNLHTHSQLNPENEQSSSEFYSLNPQSEIRKEVVVTDQPLFSTADVPVKRKRGRPPLNKPKILFGTSTENKIDENRPKRGRGRPRLERPSGLPLDSKSQSLFKRKRGRPPKIASGIVPLSAFTRKHEDMLHDSDALSLKHFAITSPNNQQFLNNQQRESAPLLPRKRGRPPKKRQENAEIRNITPGLTDSSVHSSSATPQSESSSPNSVSPLLPSSDRLPLLRQSQFTPPPKKPNFEVAIISPKKSQHKLYPNPVVESVFNDVPYSEIDSQLHTIKSTIAARLCGKSHIPLVGHMDEQTKLYQWVRQTIVLGEGNSVIIVGPRGSGKSVLVDDILSRAAQEINEKSYVVRLNGTYQTDDKLALREISRQLSIELESIESDEALKSEMNFSDTLTKLLATLSHPVDLGIAEDVMTTSAAVIFVLEEFDLFVQHSRQMLLYNLFDIAQSRKAPILIIGLTTRYDCSESLEKRVKSRFSHMVIPMRPPSSLSEFEQILKSVLYVSDEGGKDQIITCWNQRVDELLSDTRSHLHKLVQHHYFASRNLKLLYVDLLFPILSMAPDRPLLADEDFANISLKVSDHKVELVKNLSLLELALLICAVRFEARDIPACNFNSAYQEYRQLHQSSVINAAASGALAHSSRLWGRDVALEAWETLGSIGLIIPVHPSTNVSGALSRQCQLWQPEVDINVVSVGLREHRRLPSHYYRWLKEVI Q9Y7J4 ARPC3_SCHPO SPBC1778.08c; STRAND 154..156; /evidence="ECO:0007829|PDB:8UXW" HELIX 7..10; /evidence="ECO:0007829|PDB:8UXW"; HELIX 43..54; /evidence="ECO:0007829|PDB:8UXW"; HELIX 65..83; /evidence="ECO:0007829|PDB:8UXW"; HELIX 89..101; /evidence="ECO:0007829|PDB:8UXW"; HELIX 126..149; /evidence="ECO:0007829|PDB:8UXW"; HELIX 159..162; /evidence="ECO:0007829|PDB:8UXW"; HELIX 163..166; /evidence="ECO:0007829|PDB:8UXW"; HELIX 169..171; /evidence="ECO:0007829|PDB:8UXW" TURN 113..117; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..174; /note="Actin-related protein 2/3 complex subunit 3"; /id="PRO_0000124047" MPAYHSSFLSLTDVPTTGNIAMLPLKTKFRGPAYPADESQMDIIDECIGLFRANCFFRNFEIKGPADRTLIYGTLFISECLGRVNGLNYRDAERQLNSLALENFSIPGSAGFPLNALYAPPLSPQDAEIMRTYLTQFRQELAYRLLSHVYATEKDHPSKWWTCFSKRRFMNKAL Q9Y7J6 PPK21_SCHPO ACT_SITE 179; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 65..67; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 84; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 134..136; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 140; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 183; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530"; BINDING 197; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:O15530" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 220; /note="Phosphoserine; by autocatalysis"; /evidence="ECO:0000250"; MOD_RES 538; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1778.10c; CHAIN 1..551; /note="Serine/threonine-protein kinase ppk21"; /id="PRO_0000086157" MMDLEHKRISRSTLPDYADPDYFEARGERNPVKPQSSNVVPGTSHIGSIKSPADYVFGDIIGDGSFSKVRRATDKKSWKEYAIKVLDKKYIVKENKVKYVNIERDSMMRLNGFPGISRLFHTFQDDLKLYYVLELAPNGELLQYIKKYRFLDENCVRFYAAEILSSIEYMHSCGIIHRDLKPENILFDGNMHVKITDFGTAKILPPKYVNSPDYTTFPSSFVGTAEYVAPELLSRQVVSKSSDLWAFACVVYQMIVGSPPFHGSNPNNIFKKIMSLEYELPKLLPPDIVPLFSHLFRIQPSDRSTTQQIKQFPFFATITWDNLWTQDPPPMQSFRPNYNIAIPNAPAYYRSNVTAAAAANAAAAFASASIVKHQETARRQELPTVNRFTAPTAHYGYASLRSHQMPVDRLYYKLVPSSESIIESTSVFVSPIPSVPEGNKFPSGLSKMFLKRKQRVMLLTDVGRCAFVCKGKHERLFIEMEVNLKDSSVVVIFDENSSKRFLIEDKVQSWIIEDSSGDVTKYKDKILKFADVASSHQSRSSEENVEENEEE Q9Y7J9 MCP5_SCHPO SPBC216.02; CHAIN 1..968; /note="Meiotic coiled-coil protein 5"; /id="PRO_0000096291" MEKKQDNEVELYSIDLKNRNESAKIKLAYAKALEESILCETRKIEQEIKDQVVQKENKTYFNNKFDNRYKLRDLEKNLAEEEVRITEMLTIQRQDIAIERRKNTNCFSESSQVDQYSVTETNLQYATNIGLNLLQQLRYLRLQLSEKEDLHKKLSVDNAHLIKQLDLLSSNMKTLMKEKTKVQGQRDLLEQRLQGLMKKLTEVESLTVSLNDEKNKLTLELTNLRICLHELQLNAEKGETIDESEDSKNTLVTEDENDDSVFLESSSDKYFDSSSFDAEQEEKHDFPIDPFLSLESNVQTSVSQSSAVLKSINLAKQELVSVNHLVADDTKTPSPNLSSEIIENTKADIKKSIRSLNKAVSPENSIDIEDETDRDDEFICFLLSYQQLQKALKSNLGLFQLSCLYPLSLNHLIQSFFQSLTSQISIKDIDSKNKQVIKLFKPTKSSDRQEIFELAQFEPRQKFPIDTNSSKCDMSASTEMHLKDTEKFANFKLKENILNHSSIYERDVSYLPALNKGGRENYLNNRVSSYRLVKPILNSYGNHVLNRIQHDILENHFCCLKNVKDFVCGANTISMQWNLQKNMEFISSVFSLIKNEVNDTSANSVILRTDALSNVATTRLKRKLTSAIIDCSIPRRRLRHYSNPEIAEFKNFRLSTDISHSNVRNSKKLCSNGSMNCMRQGKAVFPRKIPYQEHDWEQWEKIAQSSMFKNRSIASRQSLETSDVTLDINMSSRHSNGTSSMLFKDFTKHNNWEASTYPSAPKNTRTYPTAEVEKTRHDSSQSARQLKARSTATTISISLSTVSDVFTLPRNNLKSKTNTKKCRDNLNLSGLSSSTCNANSVNKLMKHVMMGNEMMKYPRSESFKMFKKSHWRYFWINPHCEMLCWSKTNPFIEKGRKNQVKSVKIKGMTIIKAPDALKNANLHNEVIVMQTTDKPIVLKAKSKKIHNIWVQAIKQINHKAIFDTKPGI Q9Y7K2 TOR2_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22976295}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22976295}; MOD_RES 1539; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 2238; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 2240; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC216.07c; CHAIN 1..2337; /note="Serine/threonine-protein kinase tor2"; /id="PRO_0000088814" MKEFPGLKSRNEEIRNKAANDLYEYVIAYSRELSGEALVQFNNDVNKYVYTLIHSTDPLDRLAGVTAINRLIDYEGEDTTRITRFANYLRIILPGTDQKATVLAAKALGRLAVPGGALTSEFVNFEVKRALEWLQGERNENRRYAAVLILKELAKNTSTLIYAHIDSIFELLWHGLRDPKVTIRIASADALSEFLKIVRQRDSSIRLQWYTSILNEAQRGVAQGSSDYIHGSLLVYRQLFLKAGMFMHERYREVSDIILQFRDHKDLLIRKTVTELIATLAAYNPDEFVSNYLHVCMLHLLNLLKKENVKMLAFATIGKVAVAITNSIIPYLDPICDSIKESLKIHIRNKSASDAAIFQCISLLSIALGQAFSNYAYDLFDLIFASGLSEASYRALSDLAHNIPPLLPVIQERLLDMLSKILSGRPFIPPGCPPQYVARSLKSSKSASLKTGFFPNDVYILALKVLGNFDFSGYILNEFVKDCVVVYLENNDPEVRKTASITCSQLFARDPILSQTSDHAIQVVAEVLEKLLTVGICDTVPDIRLTVLNSLDSRFNKHLAQADKIRLLFIAINDENFAVRESALRIIGRLNVYNPAYVMPYLRKIMLKTLTILDYSTIIRTKEENAKLLCLLIAAAPRLIESHVEPILQILLPKAKDSSSIVAASIVNSLGEICQISGEVIVPFIKDLMPLIIEALQDQSSPIRRAAALKALGNLSSSTGYVIDPYIEFPSLLDILIGITKTEQDITIRRETIKLIGTLGALDPNRHRVLEKGTEKVVPEQKNIPPDISLLMSGIGPSSDEYYPTVVITALMSILKDPSLTIHHTAVIQAVMYIFKTMGLRCAPFLSQIIPEFIAVMRTCPTNILEFYFQQLSILVLIVRQHIRSFLPDLFKLIKDFWNPHSNLQFTILSLIESLARAMQGEFKPYLPSLLVMMLQIFDSDVSVDSVSTKKVLHAFIVFGDTLADYFHMLLDPILRLYERNDVSIGIKESIMITIGRLSMVINLSEYASRIIHPVMRMLSCNNASLIRVSMDTVCALIYQLNVDFAIFIPMIDKCLKMNGVTHETYSILVEQFLQEQPLPIKLNPYEKYDKPKLDVVASAADITSKKLPVNQEILRNAWEASQRSTKDDWQEWIRRLGVALLRESPSHALRACAALAAAYQPLARDLFNASFVSCWSELYDHFQEELVKSIEIALTSPHISPEIIQILLNLAEFMEHDDKPLPIDIRTLGAYAAKCHAFAKALHYKELEFIEEELVTKPSVDTIEALISINNQLQQPDAAIGILKHAQQHDKMNLKETWYEKLQRWEDALSAYEKREAAGAGNFEITMGKLRCLHALGEWDRLSQLAQENWIHAGHDARRYIAPLSVAAAWGLGQWEQMDEYISVMKSESPDKAFFNAIVALHRSQFEEAASYITRARDLLDTELTALVGESYNRAYSVAVRVQMLSELEEIITYKKAEDKPEVREMIKKTWVRRLKGCQRNVDVWQRMLRIRSLVISPRDNMEMWIKFANLCRKSGRISLAKKSLNLLLEDDENLDNSLVLKKTHPSIVYANLKFLWAVDDKRKALNSMQEFTSQLISDINVDPALFVQSTSVNTQKSQEEIQYYFHLLARCYHKQGQWQQEIENNWSEGSFDGVLQSYMYATQFDSKWYKAWHSWALANFEAVKFLEQSEEQIPSAAYEQYIIPAVKGFFKSIALSKGNLQDTLRLLNLWFKFGNNSNVINTLNVGISTVNIDIWLDVIPQLIARIHASSLSVRKSVHQLLSDVGRAHPQALVYPLTVAAKSQSSARQNAALAIMDSLKTHSPRLVEQARLVSHELIRAAILWHEQWHEGLEEASRLYFGDHNIEGMFAVLRPLHEMLERGPETLREISFQQAFGRDLVEARDCCIRFEQTGDISDLNQAWDLYYQVFKKIRKQLPQLTTLDLQYVSPKLLHVHDLELAVPGTYVSGKPVIRIVKFYPTFNVITSKQRPRRLSIKGSDGKDYQYVLKGHEDIRQDERVMQLFGLCNNLLLADPETFKRLLSIQRYPVIPLSPDSGLLGWVLDSDTLHVLIRDYRESRKILLNIEHRLIIQMAPDYDRLTLLQKVEVFEYALLSTTGQDLYRVLWLKSRSSEAWLNRRTNYSRTLAVMSMVGYILGLGDRHPSNLMLDRYTGNIIHIDFGDCFEVAMHREKFPEKIPFRLTRMLVNAMEVSGIEGTFRITCEHVMRVLRTNKESVMAVLEAFVYDPLINWRLAPAYSPSIDEKQSNEPNTLLGETIDGLHRKRLNEEGITLEERQKPEILNQRAITVLNRVSNKLTGRDFKPQQQLDVPSQVEKLILQATSIENLCLCYIGWCSFW Q9Y7L8 RSSA1_SCHPO MOD_RES 45; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC685.06; CHAIN 1..292; /note="Small ribosomal subunit protein uS2A"; /id="PRO_0000134368" MAQVGRPNILNATDEDIKQLLAANCHIGSKNLEVRMDNYVWKRRSDGVHILNLGKTWEKLVLAARVIATIENPADVCVVSTRTYGHRAVLKFAAHTGATAIAGRFTPGNFTNYITRTYREPRLIVVTDPRADAQAIKEASFVNIPVIALCDTDSILNHVDIAIPTNNKGRKSIGLIWYLLAREVLRVRGTLSRSAPWDVMPDLYFYRDPEEVEREEEAKKAAAAAAEEAQVEEAVAAAEFEITDSAAGSVDPNVLAAATAGQVGENTWEGAGDWNTTGAAQTSDWTAAAEAQ Q9Y7M4 LSM3_SCHPO MOD_RES 84; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC9B6.05c; STRAND 20..26; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 30..39; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 45..56; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 69..80; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 85..89; /evidence="ECO:0007829|PDB:6PPQ" HELIX 11..15; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 82..84; /evidence="ECO:0007829|PDB:6PPQ" TURN 16..19; /evidence="ECO:0007829|PDB:6PPQ"; TURN 27..29; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..93; /note="Probable U6 snRNA-associated Sm-like protein LSm3"; /id="PRO_0000125562" MESAQAVAEPLDLVRLSLDEIVYVKLRGDRELNGRLHAYDEHLNMVLGDAEEIVTIFDDEETDKDKALKTIRKHYEMLFVRGDSVILIAPPRN Q9Y7N0 BDF1_SCHPO MOD_RES 221; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 224; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 225; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 226; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 239; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 511; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1450.02; CHAIN 1..578; /note="SWR1 complex bromodomain subunit bdf1"; /id="PRO_0000211220" MSSESRENEVKAETKDEIANDGSPQLNGDNNIQSSDGHNDENEESLSRKRDSSGATVGDLKQEEKESMPKKEPEPTVKKIRGSGMPPPQQKYCLAIVRQLKRTKNSAPFKVPVDPIKQNIPDYPTIVKNPMDLGTIEKKLTSYEYSVPQEFIDDMNLMFSNCFLYNGTESPVGSMGKALQEVFERQLKQLPDAEQPAAAPVKKSKQKSASTAPPRTRRNSSVSSTSASVAASTAPKAASPAVLPEGKPRRRKNNSQMRFCSTVLKELYKRQYESFAFPFYQPVDPVACDCPDYFDVIKEPMDLSTIQSKLNKNEYSTLEEFESDILLMFNNCFTYNPPGTPVHVMGRQLENVFKEKWEARPKFDDATLVKQQEAETDALFDNGEEEEALMSEEEINGAKFAAVDKQISMLQDTLEAMKAKKMNRMRKPRRRDLTKEYGPITYAMQNELAERCNYLSAEQLSNVAEILREEMPWLRDTDEIEIDVGNMKPEVFHRIYRYVCKPDADSSEPASPVLMPTKPEKKKGRVLSETEQAEKIRRLQQQLDRFAGKTSPTSPESNNAANVSDSESDNESESSESA Q9Y7Q6 SET7_SCHPO CATALYTIC ACTIVITY: Reaction=L-lysyl(37)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67112, Rhea:RHEA-COMP:17189, Rhea:RHEA-COMP:17190, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:30773398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67113; Evidence={ECO:0000269|PubMed:30773398}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67116, Rhea:RHEA-COMP:17190, Rhea:RHEA-COMP:17191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:30773398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67117; Evidence={ECO:0000269|PubMed:30773398}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67120, Rhea:RHEA-COMP:17191, Rhea:RHEA-COMP:17192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:30773398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67121; Evidence={ECO:0000269|PubMed:30773398}; SPCC297.04c; STRAND 9..15; /evidence="ECO:0007829|PDB:5H6Z"; STRAND 19..26; /evidence="ECO:0007829|PDB:5H6Z"; STRAND 33..42; /evidence="ECO:0007829|PDB:5H6Z"; STRAND 68..71; /evidence="ECO:0007829|PDB:5H6Z"; STRAND 78..80; /evidence="ECO:0007829|PDB:5WW0"; STRAND 85..91; /evidence="ECO:0007829|PDB:5H6Z"; STRAND 96..103; /evidence="ECO:0007829|PDB:5H6Z"; STRAND 110..113; /evidence="ECO:0007829|PDB:5H6Z" HELIX 44..49; /evidence="ECO:0007829|PDB:5H6Z"; HELIX 51..53; /evidence="ECO:0007829|PDB:5H6Z"; HELIX 55..58; /evidence="ECO:0007829|PDB:5H6Z"; HELIX 64..66; /evidence="ECO:0007829|PDB:5H6Z"; HELIX 75..77; /evidence="ECO:0007829|PDB:5H6Z" TURN 16..18; /evidence="ECO:0007829|PDB:5H6Z"; TURN 92..95; /evidence="ECO:0007829|PDB:5H6Z" CHAIN 1..147; /note="Histone-lysine N-methyltransferase, H3 lysine-37 specific"; /id="PRO_0000317701" MRIPVIRSPLEIRDTERKGRGVFALEPIPAQTCIEISPVLMFSKEEYEQHGQYTVLNEYTYVWSEGKQGLALGLGSMFNHDRHPNVYWKKDNRNNYISYYTLREIKTNEELCISYGDHLWFEDEASSASRISPNEENEDFPLQNISL Q9Y7R3 CND2_SCHPO SPCC306.03c; STRAND 521..523; /evidence="ECO:0007829|PDB:5OQR" HELIX 421..425; /evidence="ECO:0007829|PDB:5OQR"; HELIX 491..495; /evidence="ECO:0007829|PDB:5OQR"; HELIX 525..527; /evidence="ECO:0007829|PDB:5OQR" CHAIN 1..742; /note="Condensin complex subunit 2"; /id="PRO_0000095044" MKRASLGGHAPVSLPSLNDDALEKKRAKENSRKQRELRRSSALHSITPRRESLNNSSPFNSSHQVPVLSNFEEWIKLATDNKINSTNTWNFALIDYFHDMSLLRDGEDINFQKASCTLDGCVKIYTSRIDSVATETGKLLSGLANDSKVLQQTEEGEDAENDDEDLQKKKERKRAQRSVKTLVKDFESIRAKKFELECSFDPLFKKMCADFDEDGAKGLLMNHLCVDQHGRIVFDSSDTVIKDLENKDVEAESQEAVVAAPIESHDTEMTNVHDNISRETLNGIYKCYFTDIDQLTICPSLQGFEFDSKGNLDVSLLKSLSDEVNMITTTSLVDNTMEKTDADAASLSSDSDGEEGHIVHALEEMAYDEENPYVDVVPKAMDESENPDFGVDTEVNMADGSTMNENYSIISTAAANGVYEYFDKSMKKNWAGPEHWRIQALRKNINNASTVFNSSNTAESSDNVSRSLSSTERKKRRELDNAIDFLQEVDVEALFTPATSSLKLPKSHWKRHNRCLLPDDYQYDSKRLLQLFLKPKMSVLPNADGEGQLQLNKALDDENDLDGIQPHGFDSDGSDNVDEGIPPYGFGDSDSPKQTPLLTPPSSSGFGDNLLLTARLAKPDMLNYAKRAKKVDVRVLKEKLWKCLDLENTIKENSINSHIEGSEMESEETNMPVKSFFSTVNQLEETYEKKELKDISTSFAFICVLHLANEHNLELTSNEDFSDVFIRPGPNLTTLEALENDV Q9Y7R4 SET1_SCHPO BINDING 897; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354; Evidence={ECO:0000269|PubMed:12589755}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:P38827}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:P38827}; SPCC306.04c; CHAIN 1..920; /note="Histone-lysine N-methyltransferase, H3 lysine-4 specific"; /id="PRO_0000186085" MDFNTSTRSKSQPVQRNNYKVLYDPELGIKENLGRKIIYRFNGVSKPPLVVRDPRLKNPIYARGIPKSGRPFLKSLQTINYDYNENSLGPEPPTQVFVSNISPLVTSEQLRYHFKSFGEVFDLDLKLNPYTGTSLGLCCISFDKRSSISVAAHSAKIAVQQANGLRFSGKPLSVVLDRDGSLCEEAFKKALNAVEKQFQEETLQKQRFEREDESSRQKLSAAMNEDIPPWRQPSKNSQTLSNGDLQHSKVQNVDQKSGFLTSSETDVPKNINDYIYLLIDDRFVPPDRVYYTDIKHHFRKFLYEKIYMNKDGFYITFNNYREASNCYRALDRTYVQNCRIKLKFHDIPSRTKEDGKKSAVRRVVLPPEEAYAEATSVVLRDLEAALLRDVKSKIIGPAIFKYLHSMPKPSVKEELQENLLVSSTSVPDVPLKIESTVGKLPSLPKFKKRVDSSKMNLSAGSKTKSKLQRRRRRRHEARPLHYQLNQMYNSSASEAESDQELLLSSGDERVERGKIGSIKSVKSDEATPVFSDTSDENDKFHRFRTKSKISKKKYEKMEVDYTSSSETESDASILSPSAAIPKSGSAIKDELISPKKEIDEVLALAPKWRINEFDETGSVYYGALPYNYPEDDVLLDLDGLQYLVKNDEDYSYLQEALKDEPLMDINDPNFWAYERKSCKFKNGDVKYGDTAILPEPKGYFRSNTSGSAKSEGYYIIPTTEKSLYLPLRNRSTIDTISHSTSRITSRMNRVNNRRLAAGVEKSQLPAEADLLRFNALKARKKQLHFGPSRIHTLGLFAMENIDKNDMVIEYIGEIIRQRVADNREKNYVREGIGDSYLFRIDEDVIVDATKKGNIARFINHSCAPNCIARIIRVEGKRKIVIYADRDIMHGEELTYDYKFPEEADKIPCLCGAPTCRGYLN Q9Y7S9 AMY3_SCHPO ACT_SITE 229; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:16751704"; ACT_SITE 253; /note="Proton donor"; /evidence="ECO:0000305|PubMed:16751704" BINDING 56; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 105; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 143; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 198; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P56271"; BINDING 227; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 229; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 232..233; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 253; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 322; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 369; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3" CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P0C1B3}; Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. {ECO:0000250|UniProtKB:P0C1B3}; SIGNAL 1..21; /evidence="ECO:0000255" PTM: N-glycosylated. {ECO:0000269|PubMed:16751704}. SPCC63.02c; PROPEP 539..564; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000255453" CHAIN 22..538; /note="Alpha-amylase 3"; /id="PRO_0000001358" CARBOHYD 181; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 235; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 282; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 305; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 438; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 447; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 498; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 51..59; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 172..188; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 263..306; /evidence="ECO:0000250|UniProtKB:P56271" LIPID 538; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MFGVYFVLLFLSSALIHVANAGSNAEWRKRIIYQILTDRFAVDDGSTDNPCDPDANQYCGGTWKGIENKLDYIEDMGFNAIWISPIDKNIEGDIDGAGYAYHGYWNTDYESLNEHFGTEDDLVSLITAAHKAGIWVMLDSIVNSMALAPPLADADYSSLNPFNKESYFHPYCLIDWDITDNETNVMDCWQDSGVLLADLDVESSDVSSYLSDHFKSLISKYDFDGLRIDAVKMMNYTFFPDFVDATGVYSVGEVFSYDPDTMCSYMSVLPGVTNYFLQLYINFSFTATGAGFTLIPTYQEVMASNCSKYDSTLMLTFIENHDLYRFPYYTSDQSQIMGALSFVLIWDGIPSIFYGQEQGFNGGEDPANRPALWLTDYDQSNPYYTVIKTMVAFRKFVITQDPDWVTSTYQSIESAVDHYVGQKNDVLVMFNNMGVTNNLTIYEVETNYTANEVVSDVFGHRTLTVGADKTLTASMTNGYPLIMYPHSKMSGFTLPTVNRTVMPSTSATATTTVYTSYYSPSYSARSFTGTGSIFTISSSSRLILSFKTLVFGLGVTAMLFVLFF Q9Y7T4 ATG1_SCHPO ACT_SITE 157; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 20..28; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 43; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104}; PTM: Phosphorylated (PubMed:17295836). Dephosphorylated under depletion of nitrogen (PubMed:17295836). {ECO:0000269|PubMed:17295836}. MOD_RES 346; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC63.08c; CHAIN 1..830; /note="Serine/threonine-protein kinase atg1"; /id="PRO_0000085652" MNLQTSTNQTIGPYVIRSEIGRGSFAIVYKGKHTETNRVISIKSVLTKKLTKKLLENLESEISILKEIRHVHVVELIDCIKAGRFIHLVMEYCSLGDLSYFIRKREKFNSIPSLAWINIDHPPVYKAGLNETLVRHFTQQLASALQFLRSRSLIHRDVKPQNLLLQPPPTAAYLEEHPQFVGSPKLPMLKLADFGFARYLQTSSMAETLCGSPLYMAPEILRYEKYDAKADLWSVGAVLYEMAVGKPPFKAPNHVELLRRIQKAKDVIKFPEEAFIHPDIKTLICALLKQNPADRIDYDGFFSSIVVTTPLDDASTLTGSDIQDAVKEINIPSSSPAYITDFFPKSNPGAPAPPGGLLRQAFQAQGSSIQPSEITGRRVPHRYAQDGNTLPYTPVFPPESAPAASIFPPRLTSKQPIPMASPAKLTSDTSNKSSAYVVVDHHPIISSTQLSNESLTHEQSINGNSPSPNEGVFQGSFSPESAPVNNHAFPHTSRMQIPYMKPNAFPSNPTYIASTPVTQLRRAFEQATAHVPQSGGGARNKSALERALNVANARLNEVVVDGMTDNGNTSLPTKESNLDNNVNIIQPSLPDTGKRLLDVLESIAMKSNSVYHLAEVKLAQIIPSLSDEMKPGDTLLDRPLTPFSLVMLAKESYVLYERDIELLQVAFDGVAAFWANSEERASPDCQQAIEWFRQRYSESLEKSQFLREIIISQSAAHSLPTTKPVSASQLIYHRALDLSRNAATSELSGNDAQACLQNYRLAAHLLESLLESNFSTPDGANDSNNSVTIRNLIALITKRQELLQSKQIQANVANKVTESVAKITLAPNLA Q9Y7U4 NSE3_SCHPO PTM: Sumoylated by nse2. {ECO:0000269|PubMed:15601841}. SPCC645.04; CHAIN 1..328; /note="Non-structural maintenance of chromosome element 3"; /id="PRO_0000057961" MSQLSFTGKSSSKGRSRLTQEVRPTASQIIADEEASDLDEYEEDLEGSGNEDDFGPSMSRSSRGRKRRKGDPLELQSQFEERNETDAINFQLLVRNVVRYAICSQTSHNTITRKDIVQKAFPEGTSRNLFQSVFEEADRQLQLSFGFRLVAVTQSNRKKDMAVSQLRRPATSNANSSNLHRYWVLRSTLPMELQKDSRLIVDSVLDTAYYGFLMTVIAFIAVSHCSVGHSELQSFLQELLTEEETTPLHLDITRSLSLLVRQGYLDRVKDDTHNQFVYYIGSRAVTEISIEGLKSFVTEFFPDSDIDMDALLTEYRQEYQNQSSSSAA Q9Y7U5 RGF3_SCHPO MOD_RES 293; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC645.06c; CHAIN 1..1275; /note="Rho1 guanine nucleotide exchange factor 3"; /id="PRO_0000080972" MKLSNELFHRSSKDHGGKSRICLDSSEDTYPPHSSSPPSFQKRLSFSDFSTTRLFSPPFLSKRSNNSPHRFSYSPPQHPASINSRRVASYTVQSSPSRTTYRQLPNEPQNSAAYTTYSSFPNALFDDFSPNNPLDTDPFLTSPGNKQNTVDSFRPLPETPVSPGGSLVHPLPRPPLPSSVSSHSSPYSTTSSTSLYSLYNDISLSCSPEPYLPLSPTRSPARTPSPIRLYSSDALRPQSPLSPSVEYLTPPNPYSLKSDISSTRQLPKIPVQDYASGKISSPLITRTHRRAQSETLFSSCREPWLVGKLYKWCKEEVFTALGGLVHEGVSRREVAQVMATLFTIHIASMEFLIAEIIAKNILGDWINYGLVEVINLEKLQIAFTSNEPPSGSGVLPFLTNGGCYSYICRSRSCPSKYQCYSCRCARNSSLEFTSLPGQSSDTWSIFWNISSLNSLPSSLSKREIARQNNIHELICKESDYVADLNTLAELFRDGIVQQQDAIVPSNRVADFIQSVFGNVESIRQLHSRLFLPQLIMRERLQGPVVSIIGDILLEWIHAAKSSYINYAKQFPLADETYKLECQRNTYFARWLAACRSDPRCRRLDFQHFLQRPTQRLQRYTLELDTILKHTEQSSWDFQLITQAVKELRATCEECDAVIATVLEANRIRDLSYQLLFKNHESVNLELRDPEREFFFEGIVQRRSDSRLDWLDIHLFLLDNYLIMAKARKDKRTNASRYVVSKRPIPLDLLVLSPKMDDFQLKSNTNKFLGSLAGNLPQESLTTKSKRKSKVNLELMFDATAEKNNENSMNSAVFEKSQLYPFTIRHLGAYTASYTLYVESLQLRKLWVEKINVAKKRHSQKINIKNPFALKVVSDVAFQYPPSDLVNGNEPLNSFNEITLVEGSSIDRALNEVAWKHPIVSEELLPEPIAYGDISCIAQFNDYEGHVSVLIATSTGIFLGAFGDSSDIRDWKKISSQRRVTQLGVVEEFDILLELRDKTLYAHKLSRIIEMGLIESKIAVVIGTPHAVSFFKIGKLSEGASVKRERTLVFYKEGLGNTTTIICCEPVIGLGHNYQKTYAFKRKDVTSFRTLDDFHVTANCHSIDCFKYSIALCHNKGIDVLRLDPKLAVGFPSPSVLNDTLFRNRINNSKPLGVFRIHDPSLFACCYQFGAVFVNGEGSMVNKECWFDWIGKPNSVTSCHGYLIAFNDEFVEIWNTRTRKLNQIIQGNDIKYYPSNSDWLANGKYIMFGMVHPQYHDRHLILALNKAKTNSFIIED Q9Y7U6 RGF1_SCHPO MOD_RES 381; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC645.07; CHAIN 1..1334; /note="Rho1 guanine nucleotide exchange factor 1"; /id="PRO_0000080970" MDYRHPNALGVNESSRAYEEIFGAPRKREPARTVSTPAFMEPAPVSKKPLPPPTRRLPRKPLPFRSTSLQPPSSQPPAPPTHQREASPVKNIEHSESFPSVFGTSNNHQIVPLTLKDGNDFGALYASLNTTPHFPQVSNHAPNNSNSPSLTWHTSSGDDSNQNPFFVRRQSQSSTSPVSDSVDENLLSAVSSVTESVETNLHLDQNYPYGSPVRSSKNPFLSSNSRLPTDDSSHTVGSHSFTSGTHPPIVSSNSAFTLPNAVTPAAQAPLIRSVSEYPANVSPPAQSLQLPKSTSNPADLHLSIASASSHKNIFSGLDVFSNVFHGPSTTLRDREHDMRNRSFDHSTLAHYEAVKQQRLGVEPTARSFTLSSYKSRASGNSLINDRSSTTTPTFVNSEASSPVHKNKRRRRIYAALLSRVASELLDRLQLGDITKDGLIYSNAFTGDHAVTVLMGIIHTSDRNLALLVGRSLDAQKFIHDVTYDHRLRDSHREIYQLQGTGYRPFLRANDNASINNKNHHKELEDNESGTRISPSTLGDTSFPNGIFTLLTHCYSPTCAKDHPCYSISCPRRLEQQHRLFAKMRANTEQSSSLAFDDKEQKLWIHSVPQEIAYSVSDRERKRQEVICEVIYTERDFVKDLEYLRDYWIKPLWASSCIPERKKEKFIRTVFLNALEVQAVNSKLAEALTKRQNYKPIVDNIADIFLEHVPKFEPFIRYGAGQLYGKYEFEKEKSSNPAFAKFVSDVERLKESRKLELNGYLTKPTTRLARYPLLLEAVLKYTDEGNPDKQDIPKVINIVRGFLSRLNVESGKAENKFNLFHLNQQLVFKPGEHYDLHLLDANRQLIFKGPLKKRSAGSTSSESASDVTLFLFDHALLIVKPKTINKRELLKVFQRPIPLLLLQLFLVDDNGLRIPYSSKQQLAAVSKAANGKPPSRFYPFSLQLLGRRGYEITLYATTEVSRDKWLEHIDNQQTLLQHRNQWFESVTICSNFFVGDNKVNAIGVYDSGRRLLYGTDTGVYVSLRKANSPLQFKPVRALNIPNISQLEVIEEYSLLLLLSDKVLYSYPLEMIDADTTQAPKKARKVSGHTTFFRVGICLGKVLVCAVKSSVLSATIKVFEPVTNYSKTRNMPSLKKFLTVNQDPLRIVKELYIPTESTSVHFLKNKLCVGCTRGFEVVSLDNLETQSLLDPADTSLEFVEKKENVKPIAIYRMNGGEFLLCYSQFAFYVNRDGWRSRPTWFVVWEGSPQNFALSYPYILAFEPTFIEIRHVETSELIHVISGRNIRLLADGRGKLGDGGEIFYACDQRGENCETSVVCSLRLTSAAAHAKEQHVDK Q9Y7Y7 GAS4_SCHPO ACT_SITE 157; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O74687"; ACT_SITE 257; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:O74687" BINDING 86; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 156; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 157; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 197; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 202; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="2"; /ligand_note="acceptor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135"; BINDING 296; /ligand="(1,3-beta-D-glucosyl)n"; /ligand_id="ChEBI:CHEBI:37671"; /ligand_label="1"; /ligand_note="donor substrate"; /evidence="ECO:0000250|UniProtKB:Q06135" SIGNAL 1..25; /evidence="ECO:0000255" SPBC342.03; PROPEP 433..456; /note="Removed in mature form"; /evidence="ECO:0000255, ECO:0000303|PubMed:12845604"; /id="PRO_0000315937" CHAIN 26..432; /note="1,3-beta-glucanosyltransferase gas4"; /id="PRO_0000315936" CARBOHYD 248; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 353; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 415; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 68..97; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 211..350; /evidence="ECO:0000250|UniProtKB:Q06135"; DISULFID 229..260; /evidence="ECO:0000250|UniProtKB:Q06135" LIPID 432; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255, ECO:0000303|PubMed:12845604" MGVANIIYALFLLGPSIFLKATAQTHPIVIKGNAFFDSKTNERFYIRGVDYQPGGSSSLVDPLASRSCKKDVEIFKKLGINTVRVYQVDNSADHDKCMNALSEAGIYVILDLNTYRHSISRAHPALSYNKVYLQHLFATIDAFKGYDNVLGFFSGNEVVNDEDTTAITWVKAVTRDVKAYIKKHSDRHIPVGYSAADVAENRLQLAHYFNCGDESERADFYAFNMYEWCGYSSMTVSGYYDRIKEFSNYSIPLFLSEFGCNTVEINDDTTPNRPFTEIEAIYSHDMTPVFSGGLVYEYSAEPNHYGLVVIDKDDERRVSRNFITLMKQYAKTPNPKGDGGYKKAGSPSKCPANSTQFNAWEKLPEMPEGAKIYMEKGAGEPLGIEGPTNMWSPFHDGDDDESTSRRPKPKNKPSNVTSTTSYTSGMTSSSESGSSKIGVAFCQALFITVLIATLSF Q9Y7Z2 ARF6_SCHPO BINDING 28..35; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 71..75; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 130..133; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPBC1539.08; CHAIN 2..184; /note="ADP-ribosylation factor 6"; /id="PRO_0000207417" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000255" MGNSLFKGFSKPFSRLFSNKEMRILMLGLDAAGKTTILYKLKLNQSVVTIPTVGFNVETVTYKNIKFNVWDVGGQDKIRPLWRHYFTGTKGLIFVVDSADSNRISEARQELHRIISDREMRDCLLLVLANKQDLPGALSPAQITDVLQLDKLKDRLWNVQPTCALTGDGLLEGLAWLSQNAKLK Q9Y7Z5 TTS1_SCHPO SPBC1539.04; CHAIN 1..279; /note="Tetra-spanning protein 1"; /id="PRO_0000351445" CARBOHYD 77; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 143; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MEPKQRVVKPLKERVLPVVKNTQFVWFSGQVIVLISSVLYALQAIPFRSAPPFLFKSAAFGAIVAYAIVLYKTYSPNLTSRASWNKHFFARLMLDDNVQYFILALSMLIDRPILFSLAPYAIYATFHISTYLRSVLLPAIYPNISDAKTASYASRVSNLLNQYTRSQFQPAMQLVASLETFLLFRLFFGVFLRKNSISRLVGYIFFLRMRYTNSHFTRASIKAVSLRMDRLVADNRVPPVIKNAWHTFKTYVSKFGASPVGTAQSRPTASSSTTAPSST Q9Y7Z8 MYO1_SCHPO BINDING 17..24; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 133..140; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" PTM: Phosphorylation of the TEDS site (Ser-361) is required for the polarization of the actin cytoskeleton. Phosphorylation probably activates the myosin-I ATPase activity (By similarity). {ECO:0000250}. MOD_RES 361; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 363; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 742; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 782; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC146.13c; CHAIN 1..1217; /note="Myosin-1"; /id="PRO_0000123479" MAILKRTNRAKAATAAAPNSTGKSNGIKKAVYTSTRKKTVGVDDLTLLSKITDEEINKNLELRFRNGEIYTYIGHVLISVNPFRDLGIYTMDILKSYQGKNRLETSPHVYAIAENAYYQMKSYHENQCIIISGESGAGKTEAAKRIMQYITHVSKSVGTEIERVSEIILATNPLLESFGCAKTLRNNNSSRHGKYLEMIFNSGGVPVGAKITNYLLEKNRIVNQVRNERNFHIFYQFTKSAPQKYRDTYGIQGPENYVYTSACQCLSVDGISDEKDFQGTMNAMKVIGITEPEQDEIFRMLSIILWLGNIQFQEGQDGGSVISDKSITEFLGYLIGVPVAAIERALTIRIMQTQHGARRGSVYEVPLNPTQALAVRDALSMAIYNCLFDWIVERVNKALVTSDNSVSNSIGILDIYGFEIFENNSFEQLCINYVNEKLQQIFIELTLKTEQEEYVREQIAWTPIKYFNNKVVCDLIESKRPPGLFAAMNDAIATAHADSAAADSAFAQRLNFLSSNPHFEQRQNQFIVKHYAGDVTYSITGMTDKNKDQLATDILNLIHSSNNEFMKSIFPVAEESNSRRRPPTAGDRIKTSANDLVETLMKCQPSYIRTIKPNQTKSPNDYDQQMVLHQIKYLGLQENIRIRRAGFAYRQAFDTFAQRFAVLSGKTSYAGEYTWQGDDKSACEQILKDTNIPSSEYQMGTSKVFIKNPETLFALEDMRDKFWDTMATRIQRAWRSYVRRRSEAAACIQKLWNRNKVNMELERVRNEGTKLLQGKKQRRRYSILGSRKFYGDYLSASKPNGTLWNTCGLSQNDHVIFSMRCEVLVHKLGRTSKPSPRQLVLTKKNLYLVITKIVDQKLTQQVEKKFAVSSIDSVGLTNLQDDWVAIRNKSSQNGDMFLRCFFKTEFITTLKRINRNIQVIVGPTIQYCRKPGKVQTVKTAKDETTKDYDYYKSGTIHVGTGLPPTSKSKPFPRLATGGSTAAARGPRPVVQNKPAATKPVSMPAAKSKPAPMANPVSTAQQTQNRPPAPAMQARPNTTQAAAPVTSTTTTIKQATTVSASKPAPSTVTSAASSPSNISKPSAPVANNVSKPSAVPPPPPPPPAEVEKKDLYLALYDFAGRSPNEMTIKKDEIIEIVQKEPSGWWLALKNGAEGWVPATYVTEYKGSTPQTTASSTNVAAQANNNASPAEVNNLAGSLADALRMRASAVRGSDEEEDW Q9Y802 LSD1_SCHPO BINDING 260..302; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255"; BINDING 301; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 328..329; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 908..909; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; SPBC146.09c; CHAIN 1..1000; /note="Lysine-specific histone demethylase 1"; /id="PRO_0000363001" MMDLSSKDALSDVLKDTHAQSSDPSLWAIFGHQSSDNVHEGGNESVSVEQEIFDLSQLSERPVSETVSKASIPTNINGLSQVKPSALEKSQEVLSLQKLPIKGRRPAGRRGRPALNTSNSLERNGTRYVSAEAPISVKSSIPAIPRVTFERLCYESAIASNLPPNALSPLEAEMLSEILENPTWLSLYLSIRNGICYLWHRNPTLYVSFNEALGIVREKKAFPLASLAFEFLSRNGHINYGCIYIISSLKLDESLSQKTVAIIGAGMAGISCARQLTNLFAQYEQDFLSRGEKPPRIVIYEASERLGGHIYTHMVPLSDNEVSEKSSLATTVNATNECMVNLLTDSLIGMPTLDSDPLYIISSQQLSLDAVHTRNREFILHDIENGRIDTEHVQRIFRLFDALLFYFNASASKQPLHSLITPPEQEFIQKLDQIGWYISIEAFPLQIKDTLSEFLGNSANTLTSLLHLTVLDLKIFEWFKEYLSQSLSVSLENVYPGSIPNLNLLLGENVASYSFKHGMADMLNSLASTPSPLPILFDQCVHTVKLEDNTVNLSFVNETTVSVDKVVICIPMDKLNTHLITFEPPLEEKKLKAIDRCHFTNVKKVILIFKTQFWEPNISIFGSLPQDSGRNFIFNDCTRFYEHPTLSVFVKVEGIDFMKDDDIVNGIVSQLKKVYKPKSEAINPIRTIISNWENNSYTNHSSYQISNLFLEEDYAILSEPIDNTVFFASEAISQKNSGSIRGAFDSGILAARDVLASLIGNVVLPNTLVIEENLEQPRKTYGTKRNAQQALGKEGERENKEKRISYHTEYLRLRQKRLDKEQQECDLLIAELLGPSPVPPSRPSANPYLLYQKTQWHVCKTLADQDKQRVTGDPEARATKNEIRAKLGKTWRALDSLGKQPWVDEINARRANYSTRLEEYQRQINSYNVRVAQIKSEHQRRCESQPIPEDEAKLKLLAEQEDEHLHPEKEGMSVENSDDDYHDDLDYEDSISEVFPDNFS Q9Y804 FAN1_SCHPO BINDING 529; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9I2N0"; BINDING 651; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9I2N0"; BINDING 651; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9I2N0"; BINDING 666; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9I2N0"; BINDING 667; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9I2N0" CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9I2N0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9I2N0}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:Q9I2N0}; SPBC146.06c; CHAIN 1..703; /note="Fanconi-associated nuclease 1 homolog"; /id="PRO_0000374000" MKRFFNEACDINTPDKSGVNENKLCFPPLKVVCQAPETTVKGQVANTNKHNVYSTKNSMYLLGFEEILNTVLDCEPHIFTDDELRVIENFKALDSDERYLFVRLFMRKRNKWFRVGHLTYPDCKDVIACCKQLVLKNFFEDESLMSTEEIIEILSLDELRSLARQTKVCGKSRSEISKEIIFLSKRQSVLHCNGQQFLSFDAFGVMHKQESFLRKQLLYQCKSCVKPKKILVDLFHRINIVYFRSSIYDEQSLTSLILARLNKFSYPNYVLSRTSNVFNCRAQCLEYVEVLELSKNLVPIFENTAASDKEALEQALNSFFEIYPIWSTYLNEDIREFWVEENRKVDTRLVRFSFSFRPGAVYTYLIHKSLNILAKSRLVEVEHEILDTLLSQNIYLVGKRGHWYNRKALLEYNFKTEDTNVLRYWKTLALSTCENGIEDKYTHLRYYFSLQRRLVRLRKCLKVSNTTELKSMKLINNNPSRLFLHGERIHNGDLSNRTVWRSKTNNAITVEELALQHYQSIGWEGIHAESSILLTLFALTFWDILFEDVPGVFQSPFQSAPLDLHTDSFYISRESTIMKRLEEIRNGKAGLIIKDNYIREHQRKTFCVGLNWSYTCEMLLEIVDCINDNGLAQIFLALTQDYKNSSSGIPDLCLWNPSKKKFMFSEVKSDNDRLSEAQKFWISLLISSEVDVEVCHVSMHKKK Q9Y812 CENPA_SCHPO PTM: Ubiquitinated. Is degraded through ubiquitin-mediated proteolysis when not protected by its association to the kinetochore. {ECO:0000250|UniProtKB:P36012}. SPBC1105.17; CHAIN 1..120; /note="Histone H3-like centromeric protein cnp1"; /id="PRO_0000221375" MAKKSLMAEPGDPIPRPRKKRYRPGTTALREIRKYQRSTDLLIQRLPFSRIVREISSEFVANFSTDVGLRWQSTALQCLQEAAEAFLVHLFEDTNLCAIHAKRVTIMQRDMQLARRIRGA Q9Y817 RAV1_SCHPO SPBC1105.10; CHAIN 1..1297; /note="Regulator of V-ATPase in vacuolar membrane protein 1"; /id="PRO_0000310740" MPLAFTNPGTPLKRTAAYDNVQWNQNRILTFGTRYTVLIIVNNYESYQNIQFGESIGAVALDQRTGFLAIAHGQVLDIYKPADSLKWTHHYNYITQLSEDITQLSWGYNFDLLLCASSYTKLINFSEDKPRLVWSQNRISDSFLSSTISSDACFIASIETKNPLAKVWQRTSPQGTVSSCDDFSYLVHPCRVRFSQWSKHLHPDASGSTPFLSTVGYDNVLRIWQVGSRFGSQLMHLSCFLNLRKYYKSDQPPYCCFIDKDDFTIALAHAISRHSGQVHKDRILNRLLALASGQPHIFLLFTFECLYIFSLVIDQETLSSFELINQVPTNFPKGALQPDGFIPIYRTSKHEFYDYNIILFFQNSAREYMFSLTDFFYSDFELRVSYDFYGHDYPIKSLTRTSNGHGIVSRDVNRICMFQSYISQDGKNQLICRFRLLLGESDFILPLYAGEYAAVLNLNSLKLWHCNEAIPPTLLCTCRQVPTSPIITFFILPVQNNDNSALCALTEGGHAWFWSVSNEAHDGSAVLRFIDRVNFTKNLNIASAVDVMGWSSTLNLSSLSSFDQEVFQSISKDGLLQTWMARVLGDDKAEISEISKVQTSIKSATMIKGSTSKKVAVVSENNRRLSIFDTRSSEFSEKEEFSSVFDDYGPINDLDWTSTPNSHSILAVGFLHDVILLCQNRRSYMNDIPCWSRIRRYNLLEYTNSLISDSSWLDNGTLVTAIGNGLFYFDNSLPEDQSLLFPASLKRSAKNIFDLAYQLNGILPVFHPQLLQQLLLRNQPFLFTNILLRFYLCLKDDVDMHFLLNMDCSEFYCCDEEISKDLLIKSLSQNSAEILNPAELDFEETSVSKHLGLYIDEMIKKLTALLKVKKVKTLTRSSQFLLLNLIEAFNKARALRDSLDLNGKRYCIMLNQYVLSKHQRQLTSLPTREMAWAFHSSNKAVLLDHTKKLHGKPLLWNAVEEYAIPFWLNEQLLKDVFLELSRNHYAEIDDRNPENVSLYHIALHKINVFRDLWRLASWHKESARTVKLLSNDFSKKKWKVVASKNAFALLSKHRYFYASAFFLLADSCYDAAKVCIRNLKSISLAIAMTRVYEGDDGPTLKRLINEYVLPLAVSQNDRWLTNWSFTILKQEKKALQSLVSPIRSLVSDNDFIQLYTSDKNDQEIHENKDSQRNSTNEPVRNKFPSDDPAFILLYECLRSSNVQIDESLEYRFVLHNANVYCQLGCDLIALGLLRNWKFQKNPATAHLETEDYMVTDKQSAVEKTHDSPKLGKTLMGQDIRPTPDDVPEFNESAFSFE Q9Y823 HOSM_SCHPO ACT_SITE 321; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:O87198" BINDING 43; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 44; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 44; /ligand="L-lysine"; /ligand_id="ChEBI:CHEBI:32551"; /ligand_note="inhibitor"; /evidence="ECO:0000269|PubMed:20089861, ECO:0007744|PDB:3MI3"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3MI3"; BINDING 103; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 123; /ligand="L-lysine"; /ligand_id="ChEBI:CHEBI:32551"; /ligand_note="inhibitor"; /evidence="ECO:0000269|PubMed:20089861, ECO:0007744|PDB:3MI3"; BINDING 163; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 165; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT"; BINDING 197; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 197; /ligand="L-lysine"; /ligand_id="ChEBI:CHEBI:32551"; /ligand_note="inhibitor"; /evidence="ECO:0000269|PubMed:20089861, ECO:0007744|PDB:3MI3"; BINDING 224; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 224; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3MI3"; BINDING 226; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU"; BINDING 226; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3MI3" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58884; EC=2.3.3.14; Evidence={ECO:0000269|PubMed:19776021, ECO:0000269|PubMed:20089861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930; Evidence={ECO:0000269|PubMed:19776021, ECO:0000269|PubMed:20089861}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O87198}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O87198}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19776021, ECO:0000269|PubMed:20089861}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:19776021}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.7 uM for acetyl-CoA {ECO:0000269|PubMed:19776021, ECO:0000269|PubMed:20089861}; KM=0.159 mM for 2-oxoglutarate {ECO:0000269|PubMed:19776021, ECO:0000269|PubMed:20089861}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1105.02c; STRAND 8..10; /evidence="ECO:0007829|PDB:3IVT"; STRAND 36..39; /evidence="ECO:0007829|PDB:3IVS"; STRAND 71..75; /evidence="ECO:0007829|PDB:3IVS"; STRAND 97..106; /evidence="ECO:0007829|PDB:3IVS"; STRAND 120..127; /evidence="ECO:0007829|PDB:3IVS"; STRAND 130..136; /evidence="ECO:0007829|PDB:3IVT"; STRAND 161..168; /evidence="ECO:0007829|PDB:3IVS"; STRAND 190..196; /evidence="ECO:0007829|PDB:3IVS"; STRAND 218..226; /evidence="ECO:0007829|PDB:3IVS"; STRAND 246..250; /evidence="ECO:0007829|PDB:3IVS"; STRAND 315..317; /evidence="ECO:0007829|PDB:3IVS"; STRAND 325..327; /evidence="ECO:0007829|PDB:3IVS"; STRAND 346..350; /evidence="ECO:0007829|PDB:3IVS" HELIX 25..29; /evidence="ECO:0007829|PDB:3IVS"; HELIX 44..47; /evidence="ECO:0007829|PDB:3IVS"; HELIX 55..68; /evidence="ECO:0007829|PDB:3IVS"; HELIX 82..92; /evidence="ECO:0007829|PDB:3IVS"; HELIX 108..116; /evidence="ECO:0007829|PDB:3IVS"; HELIX 143..156; /evidence="ECO:0007829|PDB:3IVS"; HELIX 169..171; /evidence="ECO:0007829|PDB:3IVS"; HELIX 174..187; /evidence="ECO:0007829|PDB:3IVS"; HELIX 203..216; /evidence="ECO:0007829|PDB:3IVS"; HELIX 232..241; /evidence="ECO:0007829|PDB:3IVS"; HELIX 251..253; /evidence="ECO:0007829|PDB:3IVS"; HELIX 263..273; /evidence="ECO:0007829|PDB:3IVS"; HELIX 275..281; /evidence="ECO:0007829|PDB:3IVS"; HELIX 284..286; /evidence="ECO:0007829|PDB:3IVS"; HELIX 287..297; /evidence="ECO:0007829|PDB:3IVS"; HELIX 320..324; /evidence="ECO:0007829|PDB:3IVS"; HELIX 329..331; /evidence="ECO:0007829|PDB:3IVS"; HELIX 337..340; /evidence="ECO:0007829|PDB:3IVS"; HELIX 355..364; /evidence="ECO:0007829|PDB:3IVS"; HELIX 394..399; /evidence="ECO:0007829|PDB:3IVS" TURN 41..43; /evidence="ECO:0007829|PDB:3IVS"; TURN 157..159; /evidence="ECO:0007829|PDB:3IVS"; TURN 307..309; /evidence="ECO:0007829|PDB:3IVS"; TURN 311..314; /evidence="ECO:0007829|PDB:3IVS"; TURN 374..376; /evidence="ECO:0007829|PDB:3IVS"; TURN 379..383; /evidence="ECO:0007829|PDB:3IVS" CHAIN ?..418; /note="Homocitrate synthase, mitochondrial"; /id="PRO_0000001049" MSVSEANGTETIKPPMNGNPYGPNPSDFLSRVNNFSIIESTLREGEQFANAFFDTEKKIQIAKALDNFGVDYIELTSPVASEQSRQDCEAICKLGLKCKILTHIRCHMDDARVAVETGVDGVDVVIGTSQYLRKYSHGKDMTYIIDSATEVINFVKSKGIEVRFSSEDSFRSDLVDLLSLYKAVDKIGVNRVGIADTVGCATPRQVYDLIRTLRGVVSCDIECHFHNDTGMAIANAYCALEAGATHIDTSILGIGERNGITPLGALLARMYVTDREYITHKYKLNQLRELENLVADAVEVQIPFNNYITGMCAFTHKAGIHAKAILANPSTYEILKPEDFGMSRYVHVGSRLTGWNAIKSRAEQLNLHLTDAQAKELTVRIKKLADVRTLAMDDVDRVLREYHADLSDADRITKEASA Q9Y884 SKH1_SCHPO ACT_SITE 206; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 85..93; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 108; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; MOD_RES 234; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 238; /note="Phosphothreonine"; /evidence="ECO:0000250" SPBC543.07; CHAIN 1..363; /note="MAP kinase kinase skh1/pek1"; /id="PRO_0000086655" MSKKPVLNLDTSNGFSEEYISHPERNDNQGIVEITDLVFSSESKLTQRKESRDSKTFVPSFLEELDDDHLHELVTNGGILYMNSLGEGVSGSVRKCRIRGTQMIFAMKTVLAAPNTALQKQLLRELKINRSCTSPYIVKYYGACYNNAECQLNIAMEYCGAGSLDAIYKRVRSQGGRTGERPLGKIAFGVLSGLSYLHDRKIIHRDIKPSNILLTSKGQVKLCDFGVSGELVNSLAGTFTGTSYYMAPERISGGSYTISSDIWSLGLTLMEVALNRFPFPPEGSPPPMPIELLSYIINMPPPLLPQEPGIKWSKSFQHFLCVCLDKDKTRRPGPQKMLTHPWVKAFERIHVDMEEFLRQVWSD Q9Y8G3 MEX67_SCHPO MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 130; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1921.03c; CHAIN 1..596; /note="mRNA export factor mex67"; /id="PRO_0000220541" MLRRKRERRNAVKENEMVIDTPLEKRRTPGKPRATREPPISVVITGHSKGSEDDLISFVWRKVKVRLMNISYSPASVTAVVKSQDFSRLNGLNGAAFAGDHLAIRRVDGASNVTQDYRKAKTKRSFRSVSAPSLSALATQAQRNVSKTLPQSTNETIEKLRQFLQTRYQPATKFLDLGNLQQDPLLKQMGILAEASTKSKMFPALMKVASLNFPDVISVSLSDNNLQSVTAVTTLAQTWPKLLNLSLANNRITSLSDLDPWSPKTKLPELQELVLVGNPIVTTFANRAMDYQREMVSRFPKLRLLDGNSINSEIIASQSTVPFPVYQSFFDKVETEQIVNSFLAAFFKGWDENRSALVNQLYSPNATFSISLNASNVRTNFSQKTDTKKWGAYKMKSRNLLYSQSQKESKSRLFNGHEEISNAVKSLPATAHDLSDRSQWVFDGWNLVLPSVGAAIKIVVHGQFEEPQNKRLLRSFDRTLLILPGGSTGILIINDLLVIRSFAGSLGWLPGQSSVRTSNNAMSASASKPSDIVQPRPEQAMLDTRQQIVLKIKAETGLNDYYAHMCCEQNNWDYNSALASFLELKSRNVIPAEAFS A0ZWU1 EAF1_SCHPO MOD_RES 247; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1223.10c; CHAIN 1..251; /note="Ell1-associated factor 1"; /id="PRO_0000307925" MNSLQKGSYKVIPGSSFSKNSNGLLSIKYNFIPESVDPSRRGVLEKAQEAYRLRLPSTFDDDRPHIFEGSCQRARNVDCVLIFNAKTKTFTLEHIDEIARLNALRNPKVSKTVPSNAITQSDNSQISESKSTSQSAVTTNSTRRKEKELEASKDGKIKPSSSNTRYPAISSKGPITTDTNDEPDMEVMELDDFAKELELGFDQEFNSIDDPSTVSQTASKPISLRGLSSQERDYASSAQAEGISSASEDED C6Y4C9 SPO13_SCHPO SPCC1183.12; CHAIN 1..138; /note="Sporulation-specific protein 13"; /id="PRO_0000389118" MMSNSQISKLFSSISNKENSNENALKESTNKQLNNANTLAITHLKEQLSREVQRREELEGLLEQSQKEMEDLSVSLFTEANEMVAKARQDTEVLKRELDYLRAKEKGRIGKLRSIQTAVRTSIEARKLLSYSNESNYH G2TRP0 MIM2_SCHPO SPBC409.23; CHAIN 1..72; /note="Mitochondrial import protein 2"; /id="PRO_0000416516" MAEVLDLEIDPISDGEDDTYSSELDDDLKDSIEQLERVLCLVVFPLLGKFLGRKFAFHAWARWLERRRLVSN O00084 UREA_SCHPO ACT_SITE 590; /note="Proton donor"; /evidence="ECO:0000250" BINDING 404; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 406; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 487; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="1"; /note="via carbamate group"; /evidence="ECO:0000250"; BINDING 487; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="2"; /note="via carbamate group"; /evidence="ECO:0000250"; BINDING 489; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 516; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 542; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 630; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_label="1"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000269|PubMed:8742356}; COFACTOR: Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000250}; Note=Binds 2 nickel ions per subunit. {ECO:0000250}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for urea (at pH 7.5) {ECO:0000269|PubMed:8742356}; Vmax=713 umol/min/mg enzyme {ECO:0000269|PubMed:8742356}; PTM: Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000250}. MOD_RES 487; /note="N6-carboxylysine"; /evidence="ECO:0000250" SPAC1952.11c; CHAIN 1..835; /note="Urease"; /id="PRO_0000067529" MQPRELHKLTLHQLGSLAQKRLCRGVKLNKLEATSLIASQIQEYVRDGNHSVADLMSLGKDMLGKRHVQPNVVHLLHEIMIEATFPDGTYLITIHDPICTTDGNLEHALYGSFLPTPSQELFPLEEEKLYAPENSPGFVEVLEGEIELLPNLPRTPIEVRNMGDRPIQVGSHYHFIETNEKLCFDRSKAYGKRLDIPSGTAIRFEPGVMKIVNLIPIGGAKLIQGGNSLSKGVFDDSRTREIVDNLMKQGFMHQPESPLNMPLQSARPFVVPRKLYAVMYGPTTNDKIRLGDTNLIVRVEKDFTEYGNESVFGGGKVIRDGTGQSSSKSMDECLDTVITNAVIIDHTGIYKADIGIKNGYIVGIGKAGNPDTMDNIGENMVIGSSTDVISAENKIVTYGGMDSHVHFICPQQIEEALASGITTMYGGGTGPSTGTNATTCTPNKDLIRSMLRSTDSYPMNIGLTGKGNDSGSSSLKEQIEAGCSGLKLHEDWGSTPAAIDSCLSVCDEYDVQCLIHTDTLNESSFVEGTFKAFKNRTIHTYHVEGAGGGHAPDIISLVQNPNILPSSTNPTRPFTTNTLDEELDMLMVCHHLSRNVPEDVAFAESRIRAETIAAEDILQDLGAISMISSDSQAMGRCGEVISRTWKTAHKNKLQRGALPEDEGSGVDNFRVKRYVSKYTINPAITHGISHIVGSVEIGKFADLVLWDFADFGARPSMVLKGGMIALASMGDPNGSIPTVSPLMSWQMFGAHDPERSIAFVSKASITSGVIESYGLHKRVEAVKSTRNIGKKDMVYNSYMPKMTVDPEAYTVTADGKVMECEPVDKLPLSQSYFIF O00087 DLDH_SCHPO ACT_SITE 489; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 75..84; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 93; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 157; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 187..189; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 224..231; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 247; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 281; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 316; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 357; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 363..366; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion" SPAC1002.09c; CHAIN ?..511; /note="Dihydrolipoyl dehydrogenase, mitochondrial"; /id="PRO_0000030300" DISULFID 84..89; /note="Redox-active"; /evidence="ECO:0000250" MLNSVIKRSALCRFKFTCLQVSECRPAQIEISKRLYSAKASGNGEYDLCVIGGGPGGYVAAIRGAQLGLKTICVEKRGTLGGTCLNVGCIPSKALLNNSHIYHTVKHDTKRRGIDVSGVSVNLSQMMKAKDDSVKSLTSGIEYLFKKNKVEYAKGTGSFIDPQTLSVKGIDGAADQTIKAKNFIIATGSEVKPFPGVTIDEKKIVSSTGALSLSEVPKKMTVLGGGIIGLEMGSVWSRLGAEVTVVEFLPAVGGPMDADISKALSRIISKQGIKFKTSTKLLSAKVNGDSVEVEIENMKNNKRETYQTDVLLVAIGRVPYTEGLGLDKLGISMDKSNRVIMDSEYRTNIPHIRVIGDATLGPMLAHKAEDEGIAAVEYIAKGQGHVNYNCIPAVMYTHPEVAWVGITEQKAKESGIKYRIGTFPFSANSRAKTNMDADGLVKVIVDAETDRLLGVHMIGPMAGELIGEATLALEYGASAEDVARVCHAHPTLSEATKEAMMAAWCGKSIHF O13453 PMP1_SCHPO ACT_SITE 158; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; SPBC1685.01; CHAIN 1..278; /note="Tyrosine-protein phosphatase pmp1"; /id="PRO_0000094917" MSQKLPPLKIYTSQLPLVSHKNMLENEEEASHSQLFTPCPVPPSFPKASKPNSNQPYPNGPVCIYPPNIYLYAKPTMPIIQSFDVVINVAKEVLHPFRTDGRHYRDSKHNLDIQVFDHIEYVHIHWDHDTQFALELDKLVSFVAYNAMQLNKKVLINCQMGISRSACLMIAFIMKTLNLNVSDAYEYVKERSPWIGPNMSLIFQLSEYQQIIRKNSSQGPYQSSSLKQSKRKSEGNLLFPEKPHSAQLPLVSPSTSESSMFTNLRRTRSSGSISNDAS O13600 SWS1_SCHPO SPBC11B10.06; CHAIN 1..209; /note="Zinc finger SWIM domain-containing protein sws1"; /id="PRO_0000223107" MQQGHFTSNSYHSKTLNSSSLPVSSKFSHTNDPDVEGVDNDSFSKALCNKDLDPSSTIRSVISSLLDSLQDKALQQSPNTSLSKLLLEDQDFGSLWLSLSFIFCNYWQPAMLILDSKSIHPLPLTDGEVLHRWECEVDSNNKTTIDLKYWYCSCSQFSYNAFNSSRSFDEPMPKNEQETWGGRCLSHHPTICSHILAASILRACHNLVI O13606 MEI4_SCHPO SPBC32H8.11; CHAIN 1..517; /note="Meiosis-specific transcription factor mei4"; /id="PRO_0000091906" MVENQGNVEAHGKPKKVILSLSLKESSKINDSQNVSNVSSKEKCETEALLREENKENLSSDSIRQMIFGDEMAGFVDTGEKPPCSYATLIGLAILQSHNKQLTLSGIYTWIRNTFRYYLNHDGGWQNSIRHNLSLNKAFIKVEKPKGKTLKGHYWTIDPDHMQNFVSVRLHRSHSTDSNSKKRPSSKCHEIKPLTTREIPLARKRSRLNSFNSSTSTSGSSSNVAAEVSNDASQPSNQDSSLNSNIVKPPLPPSNVQSNSSSSENVPKPNAETQEDLPTIDAHESSLYENVNDSRLYEVPACRNMALNTGYSDADPGYLRTSFRSNSHNSLPYSANEEEDVLQADFLVSQQSSMVSSYVSSRDPHSMPYYRREPIPLRPSSRFYEYTRPTYGRTDTSCSAPGAFCSTQINSPSSYINYSKCAPSSPTLSLQKHREHVKSLLYVPDLTPSFDGSDPWNPSSQLLSEPLFDQHSFQSSLDDLMSVTCFRDSPELNHESSGYSSAPLMPSNRAFINDFSL O13612 NEP2_SCHPO ACT_SITE 171; /evidence="ECO:0000250"; ACT_SITE 188; /evidence="ECO:0000250"; ACT_SITE 229; /evidence="ECO:0000250" MOD_RES 35; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 367; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32H8.02c; CHAIN 1..415; /note="NEDD8-specific protease 2"; /id="PRO_0000101736" MRSNSIFTKEIDSEAVKKSSNLRPPSTGSSNSNGSDTASPKKKKKGFFRSLFGSSSSGSKSCGSPFTRIWLEYFEVSLRKNDVDHFRPGYWILDTNIDFFYEIMLRQVLLKRPKEESQQIYLLRPAMVFFLAQAPNPLEIESALPPAMFDASFIFLPINDTNECGIESGSHWSLLVVSVEKGLGWYYDSMSNGNTNDCNLAIKNLGILLKKEFRVRHMKTPQQINDCDCGLHVCENTRILMYRLLQKPYVPKVDMNLDHSVVDSVRLRKALMEVITSLLAAYGSKVPKPSETHTDPEKDKKIFSKICKTEELLELPTLSAVTSDSAQPHSLPASMPSSQPQSRSESLPLTHPNSEPNPKLDSQPNSSPVRRPSLIKVKTASTSVLPTSILQRPPSIVPRPETAAIQHTQQSIEIH O13615 PRP46_SCHPO SPBP22H7.07; CHAIN 1..473; /note="Pre-mRNA-splicing factor prp5"; /id="PRO_0000051167" MTEAKNISDDTDVLSLTTNSLRTSKTLFGAEFGSVTSFDDTVAQNLKRTYKEHLEYGSVLGGTVGKRKNRHYEEDTIGSNALTVRADSENPSSQVITKFSDPNKKIAGQVSMQSLEKIKGVPEAAHRIAGESQASLVKRTLAEQIRPEWHAPWTLMRVISGHLGWVRCVDVEPGNQWFCTGAGDRTIKIWDLASGVLKLTLTGHIATVRGLAVSPRHPYLFSCGEDKMVKCWDLETNKVIRHYHGHLSGVYALKLHPTLDVLVTAGRDAVARVWDMRTRQNVHVLSGHKSTVASLAVQEFDPQVVTGSMDSTIRLWDLAAGKTLTTLTHHKKTVRALSLHPDEFTFASGSSDNIKHWKFPEGAFMGNFEGHNAIVNTLSINSDNVMFSGADNGSMCFWDWKSGHKYQELQSVVQPGSLDSEAGIFASSFDKTGLRLITCEADKSVKIYKQVDNATPETHPNLPWTPSNLRRRY O13637 SEC31_SCHPO MOD_RES 499; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1042; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1044; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC8D2.20c; CHAIN 1..1224; /note="Protein transport protein sec31"; /id="PRO_0000295446" MRLKDISKTATLAWSPRGVNDNQALLALGGYTGTEGSKNSDTLLELWNENPESQKPVGSIDVKTRFYDLAWEKSLDKPMGVIAGSLEDGGIGFWDPAAILKSDEASASIATYKSENGSILGPLDFNRLQPNLLASGDNKGDVWVWDIKHPQQPFALPKQNRSSEVHVVSWNNKVSHILASGNATEYTTVWDVKLKRQVLNLSYLGAAGVSAATGAVNSIAWHPNNATRLATAIDDNRNPIILTWDLRQPTVPQNILTGHQKAALSLSWCPEDPTFLLSSGKDGRAMVWNVETGESLGSFPRSGNWYTKSSWCPSNSNRVAVASLEGKVSIFSIQSTNTDKSQEASIKGATSIDDNEFFNNLPSIAGSQEPSFSLPLAPKWFKVPVGARFGFPNKIVSFSPNSKEVTITSAPDEVEQDEAKSFHSSAKFQTEKEITDFCQKGVEESASEEEAINWKLLMAVSKRASRSKFAELLGYKTLKPKNDEDDSKVDESVAKDSTTPNELSKNANNENYDDDSSFYGKLAESVQEVSIADKKDAEIVKDSFKIFNPEDSDLEKNITEALLTGDVLSAVKACLEEKKISEALFLSTFGGKECRKCVRDAFYELQEHKPSYMRLSACIADNDLQNVVDNAEVSEWKDIFVFICTYATDDEFAPLCSTLGQRLEDLEDEKSIRSAEFCYIASKSLQSYANLWLKQLATSTKTSKAASAYGAYVEQLTKLMDKVSMFRSIVVYKDDELSATKDWKLAGLYEVYIAYAKILSASGKFDDAMSYLNLVPTEFPGAKEEIQRLTMLLEPHAVPPIHQIKQTGYAPVQPKTSQASSILPTVPRTTSYTSPYATTSSHITPADVHPLPPPSTSTTAGWNDAPMLGQLPMRRAAPSMAPVRSPFPGASSAQPAAMSRTSSVSTLPPPPPTASMTASAPAIASPPPPKVGETYHPPTASGTRVPPVQQPSHPNPYTPVAPQSPVAAASRISSSPNMPPSNPYTPIAVASSTVNPAHTYKPHGGSQIVPPPKQPANRVVPLPPTASQRASAYEPPTVSVPSPSALSPSVTPQLPPVSSRLPPVSATRPQIPQPPPVSTALPSSSAVSRPPIATSAGRSSTAASTSAPLTYPAGDRSHIPGNLRPIYEMLNAELQRVSQSLPPQMSRVVHDTEKRLNMLFDRLNSNVLSKPLTDELLALATSLNAHDYQTASNIQTNIVTTLGDQCEHWIVGVTRLITLSKSTT O13658 YBCB_SCHPO MOD_RES 260; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 261; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27B12.11c; STRAND 304..307; /evidence="ECO:0007829|PDB:6O19" HELIX 293..298; /evidence="ECO:0007829|PDB:6O19"; HELIX 309..314; /evidence="ECO:0007829|PDB:6O19" CHAIN 1..738; /note="Uncharacterized transcriptional regulatory protein C27B12.11c"; /id="PRO_0000310375" MQKKVVQSASKNEELDPHYKRSSVPFPYGLPDYDAEYQFINHHMQQLLTRPVEGTHSASVHPSTSSTSHISSPSAFSVQNPNPNDAPFVGNIGLDASGFSSGGMSEYYPRSVSMQQSQDVHFQNTEIPYYHRSPSSDSFSPGVVASVNPNSNNSPTFYSNPPALSNIPIPLNNSPYRPEDAYFQLQGAGVKADINPYNLSPYSQYGPEGTAYSNAQAHHQDGAPLQRVCSAPDPPKTSMPPFGSAGSPSPNRSLNVSNNTTPPLSTVNKIIKKPKATTGKVKKRLPQAKRACAKCQKDNKKCDDARPCQRCIKAKTDCIDLPRKKRPTGVRRGPYKKLSDTSNNTKSTTASSGHSTQDSLSSKMLDPSSDNQFAMSSRQMDENGMAQYPSSAIKQELNLQPQILVSSASKNFQPNVTPPFAVHHDHFNSTSMDGVAVSNMDETGTSSAGSKPFNRKSRNRSFTNPVGMTEEHFLREYAQHSVANPSLLIHQIHGLPSEQVHGLLSHTELGNAMHNQPTYNESSIAAENVNNWMLETNDHENLSMQSHFEVPDLKMNHHDSSFFDRHIDQTAMPGQNQHGTVKNMETMHHFYPDVHNSEFPAAPNPVKSQVPYYYQSQAADDEEEDVPDHQPSWRGRIHSFSIATDSSQHVVERPCIHSLRGIHGQQDGGLEQHDGDHVNMLPDTHAEELAYTSMLLFHDIPTRDIRPDFNVHELVDHGTYPNFHQNQADSFKNHPFRQ O13665 FAR11_SCHPO MOD_RES 500; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 502; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27B12.04c; CHAIN 1..817; /note="Factor arrest protein 11"; /id="PRO_0000337251" MAATTASCISFSQFQRLKKLIDSPASKHKPMEFKGTSKDDLEDDLNSFFDCEEELFLSANKIFYSKLRVYQTVRHWSLKQNWSSMSLDQKRNFILHCHHELSSGELLRNSALYSILYIAAGAYDSVGSFEEHVHSISENVYLLREFDIPKTVYSLFIEWNRTRKHSFLDNSRDEGFLNLLLSLMFFFLTLNNTDKTWIHSIRSLNPPVLPTLVKLFIDITSDYQLNLDKVIHSSLKKLSFLIFKVCIRLWGSQSYLQEKKAGLAEVLNISTSQQKPKTTALDYEVFRHEMATKFSSFADSYYPVPLDREQAHILPTLNTDSFHKSSFISSTRLCSPENPSLLVNTAKTSKMSARREQFQTNQNLPFCFTPNLEKLTIPYSVTEAANVFQNKTKRTLAVEQLLSERELLRRFTLQQRLVADLHEFYNSVKGPAHSFETEDPVLKFVSQSYDDLFPYMDNFIQLAVQLFYHISKKVNCLYVEAFSSSDAVLQRIQDNAVVDSPTEELSEQAARNRKSNVKIEYTEDFATGFAISGEISHSINNLEFVLYSLSSLFLMMLKWFRLSHVLRFERLAFLLYENHFLEIFNRHLTEGDCNRNTEKDVKCVRGGFFSYSSKMYKYDRVSIPVITRASSSRNLLITMNCLRVLEKVCKYSNIRKEIIARSNLHENLKKLLAIPHDKLRLYALKVLKLSVPFLGLKWKQANMSIITQIYLNCSLDLRDSWMFHENGSDTYRSAQLQETFLAILIRFYHIRLYGKKCKSLYQFCILEEMRLKKSIEELAASNMMEYIPESLWSYSFERSDTGFFENEFAAMHINDIA O13681 IINMP_SCHPO SPCC737.03c; CHAIN 1..615; /note="Integral inner nuclear membrane protein ima1"; /id="PRO_0000116805" MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPFYAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDANDYEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLLDGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFLLRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISILNNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSKFSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNRRNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA O13682 SWR1_SCHPO BINDING 472..479; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPAC11E3.01c; CHAIN 1..1288; /note="Helicase swr1"; /id="PRO_0000074372" MTYEESEKNKNGLSSYIKKEGSSDLKVRVRFREPKLLVTHSGHITEQPKYEHLEQYLDSYVSLEDGDHDPKEAKELVFREVQLRHRINEFRKKGYFTAEAPVELKKAPSSNNIPISYRDNLLSHVNGYARSMHNDRKVRASRSRRISGMILAHFKRLSGADEKKAKEEDKRIRLLAKRTAWEIRKKWKVIEREVRRRRAERAAEAQRVAGKEQLANILKHSTDLLEARIERANINISAQTSESAVDWNYLLKTSDDLLSVDELKLKYSNPDLIKNIEREEEAEETSDDEPLSSEDEENEDEDITEESNLRKRKVSDKTRVVNKHPPSLRRSRRFFAKKSYNHVSDLDGEVIVMKKEDITDGVSTKKDLNDGDQNEVPLHDTGSSSSLSLLYNEDVASKKKRRVNDDGLARKKSIAGISEQRKFDEPNGSPVLHANKIQVPFLFRGTLREYQQYGLEWLTALHDSNTNGILADEMGLGKTIQTIALLAHLACEKENWGPHLIIVPTSVMLNWEMEFKKFLPGFKILTYYGNPQERKEKRSGWYKPDTWHVCITSYQLVLQDHQPFRRKKWQYMILDEAHNIKNFRSQRWQSLLNFNAEHRLLLTGTPLQNNLVELWSLLYFLMPAGVTQNNSAFANLKDFQDWFSKPMDRLIEEGQDMNPEAMNTVAKLHRVLRPYLLRRLKTEVEKQMPAKYEHVVYCQLSKRQRFLYDDFINRARTREILASGNFMSIINCLMQLRKVCNHPNLHEERPIVTSFALRRSAIADLEIKDLLVRKRLLHEEPMTKLDLSTLRLIRTDSEAFDTFVSDELNSLCATNAYNRISTFLRMQIDEECKPCQFKKSNFKEHFQNKIYQEQLDKLNFQKYLNESKCSHSPIYGSNLIRLAEKLPKHSTSIDYTLYAKDDPLYLLNTTKALRSCILSTEERASNMKEIIQRFACITPKAVVVDLPELFCKTIPRDLLYEVSRKINPLHQASTRLAIAFPDKRLLQYDCGKLQVLDRLLKDLVSNGHRVLIFTQMTKVLDILEQFLNIHGHRYLRLDGATKIEQRQILTERFNNDDKIPVFILSTRSGGLGINLTGADTVIFYDSDWNPQLDAQAQDRSHRIGQTRDVHIYRLISEYTVESNMLRRANQKRMLDKIVIQGGEFTTEWFRKADVLDLFDLDDESLKKVKADSDSGSTKNEENWEVALAAAEDEEDVQAAQVARKESALEQTEFSETSTPQAMLTKDSTPLSSDSATPGFERDSTEEQSNTNDMDEDRSELEEDLDETVGHIDEYMISFLEQEGTSDEW O13686 WDR59_SCHPO MOD_RES 24; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC11E3.05; CHAIN 1..1323; /note="Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05"; /id="PRO_0000310741" MRELQGDDSSRKSPPSDSVVKNSSPIDYEHSLKSLQDERTLNYPNKQFNSENPSSYYNMDDSGELCNFELEKDSLESMIHESSTALSAQSNTAQDGDQLASSSTISKDHSETLDNKLNDSKILIKKASNSFANFSESVRSSTIVAYSQTPTQRLQGLTSISSSSFDDGSYGSRRISFNSQGVSGRLRRNMDSTVIIPSEDEDLQLPSNSNSNVEYGPFDSTTFDRQLSIEVNQPVGAMSLSPCGRDIALASRYGLLVLDLDNPYNPPRMLRHSTPWEVADTQWNVHAARDQWVVSTSSQKTIVWNLALPNDRAIEFMLHGHTRAVTDMNWHRQNPDVLATCSIDSSVHCWDLRSPRFPVNSFYDWHNGATQVKWNYKNPHILASSHGRLVRIWDDRYGSAPLHTIKTSENITKINGLEFNRACETRLLTCAMDRTVKFWNYEKSTEEPEHLITTDSPVWKARFTPFGDGVILMPQRGDNSVHMYDCRNLDKEGPRAVHRFAGHTDQVKEFLWRCRGEDVFDRDLRDFQLITWSKDHHVRLWPIGNDILNSMGHDRTKPVPFKLTRLGAKYRTYSREPLKQSLINTECDSSDAMNSFDSNFGAERANTSDLSRGFVAFANRKKSKYNLPGSSGFMTRSTKSTNPMTPLNWLRGISMGRLGNADWEVPQNLGEELSWIGQKYSNVSFEKIDVAERTCTISLNAPILPDDGYAYIRLHVYFPNNYPISATPVFQLERSSAFNDEQFNYVFNTLTSISDQCISSHKYCMDACLSYLSGNLSVDEIWKLGFQKDNSDSSSESSADIFQDVFPSMPDFRGGDRGLSHKHQNIPLPKTCAAIFCGNDELVCFFTIKADESAAQATANRETHGRQKLFESFGVLDSSNSVADSDSTNYDDENSLNRGGTSESDSEFIWDVDESNSGSIVFPKSKTSINLNNINSASASIMGSRFGAADIFMSKRPSTKGSNRPSILLSKPSHDFHVVRIISMSKYLPVKRALAAEYVVDTGDKVTVCNKNAEVSAKHNYYRLAKVWLMLGRLLGHLSRTENKDHINDEEAFPWLKSPLAKWVVNSLLDYYASQCNTQMLAMLACVLDIPNPKKQSGNTSADQVLFNQPKQVTEKLGVQLNLPKTKILEKVSSHSLAQITALREKEPKDADSTYSKEKIFSATSTVHLQLMDYDKQNNDFVDAQEIAYTKLLQQKFIQWRATYAEQLDLWGFFIPKLEMLKFNAHEFSSPSEKTLVNHCNSCNSTTSNTRICEKCYSLVPRMSCTFCCLSIHGLCIVCGLCLHVMHEDCYKEWFSNGDSISQSCSSGCGCKCQFQHMSLEKV O13690 YDYB_SCHPO SPAC11E3.11c; CHAIN 1..942; /note="PH and SEC7 domain-containing protein C11E3.11c"; /id="PRO_0000317153" MSRNASNAYLKNGNSTPSNDKRSPSSLSQRSKTSTRSSKPFLQRLFPSTWFKNESSSRHPLTSIKENDTQTIGRRPSMRVKLFGKDKSKASMSTNDLPSHPRSQSVMGFSSSTSQLTGTSNSSRTRLNKDMRRDFGMTSMSSITSSTPTPSQLPVRPSTSLSFFDDIPLGPSFSAETILSSLSISTSNNAMSKTTPAPPLVTTKSISADQDDFYTCKEEVSTYEGLNSQIELSPVKSRDSQNKSAKNLSTAYRTVSGESRNLMVDPKVSPYGNSRTPLRDSSNYLRDRRSINRQSSLSIPKSTSETTRKTLALSNGGIDQSRVSSDSFKVDDSSAKMAAIDIWEGSQHIVSNDKALSWLVTDKPYNKAVLKHYISLYDFENTDILQSLRMICGNLYVHGETQELDHFLGEFSNQWCRTNPKGLFCNPQIVHSIAFSLLLLNTDLHIAELSASERMSRNQFVENTYRSIKQALNDSFDGNEEKKNAFFLSSYKSFASNESCNSPAIHSLHGNLSPGKSAELKKLHKRSLSSKVLEEAFSSYWMSALKEMYHSIKVSMILQPDRYLDMNFDFNDTNKINNPSSTANQTRHFHSVSEIKKLPMGTDELEKSMVRPSTAMYINRQNENAVSIDKSRDLQGTVNTKEIRSRSALSYQNDRPLATDLPSVIYNHKHPNVVSPFYVHPYIKQGILKFQSKESHKFRKKEVWSTVLAVLQRDVFTLYNLNTPNLSYDPKDLDISKVGKPVIKTTIIASLAKPFPSSEDAVVLKSTNSLYFDLETSSQLKLRFAGPSPKDAQGWIDALNYWAARSSKVPLLGGVTNVDYGWARCTGQRAQKSNAQLLKTKTDKIIVHKWQPQPVNTIPSSLSLGEQLSAFNNFMKLLKKTNDEHQNLHKEMLVVLSSQPKSTFRRAVENWKYKSDYLQLNLVRLRVYISVLEKYKSQAQNS O13696 IDH1_SCHPO BINDING 106; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 137; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 224; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P50213"; BINDING 224; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; Evidence={ECO:0000269|PubMed:10975257}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC11G7.03; CHAIN ?..356; /note="Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial"; /id="PRO_0000014430" MFKSLVRKSSAFQPLKYGGKYTVTLIPGDGIGRETSNAVTEIFKTANVPIEFEEIDVTGMEKNNKSSGDALHEAIQSLKRNKVGLKGILFTPFEKGGHTSFNVALRKELDIYASLVLIKNIPGFKTRHDNVDFAIIRENTEGEYSGLEHQSVPGVVESLKIITEYKSKRIAQFAFDFALQNGRKSVTCIHKANIMKLADGLFRRTFYDVANGYDAITPKDLIVDNASMQAVSRPQQFDVLVMPNLYGSILSNIGSALVGGPGVIPGANFGRDYALFEPGCRHVGLSITGRGEANPTAAILSACLMLRHLGLKDYADLINAATYSVIEEGKTLTKDLGGSASTGDFTHAILERMESL O13701 TAF7_SCHPO MOD_RES 308; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 310; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13F5.02c; CHAIN 1..393; /note="Transcription initiation factor TFIID subunit 7"; /id="PRO_0000118884" MVKLKIRAVQPPPNDSRSSTPATGPPPPIPKIKIKTREPKGPRLTKIRLKRVREPGLGYDSEASDREEDTYIEEQIILRLPPGEDCEYVRKAIENREVGRGADIWVKFKDQRRAVVHVNGHLYAAKLVDLPCIIESNKSFDKKVIFKAADICQMLIATERIEHENSVLNTQLKQADYIYPHGLTTPMHWVRQKRFRKRVSNRTIEAVENEVDRLLAMDERAESTSNELIDQAQLARDSSIALSEDTSFDGMAGLRGTSIDRDDQSVQTDMFDGMDEDDLAGQIEQGMLELSQDTRESTAEPRAAGEESASEEEEEEEEEEEEENEADDETRENKRQNRLVREFISELESSIQKRRKDADEATNPILRNRFLADVNRMVTELELKRTQLVDNPE O13702 GLD1_SCHPO BINDING 99; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 155..159; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 177..180; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 182; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 186; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 188; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 192; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 232; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 232; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000269|Ref.4"; BINDING 315; /ligand="substrate"; /evidence="ECO:0000269|Ref.4"; BINDING 315; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000269|Ref.4"; BINDING 333; /ligand="substrate"; /evidence="ECO:0000269|Ref.4"; BINDING 333; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000269|Ref.4" CATALYTIC ACTIVITY: Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH; Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6; Evidence={ECO:0000269|PubMed:20396879}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|Ref.4}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|Ref.4}; SPAC13F5.03c; STRAND 62..67; /evidence="ECO:0007829|PDB:1TA9"; STRAND 70..75; /evidence="ECO:0007829|PDB:1TA9"; STRAND 91..99; /evidence="ECO:0007829|PDB:1TA9"; STRAND 120..126; /evidence="ECO:0007829|PDB:1TA9"; STRAND 148..154; /evidence="ECO:0007829|PDB:1TA9"; STRAND 172..178; /evidence="ECO:0007829|PDB:1TA9"; STRAND 187..191; /evidence="ECO:0007829|PDB:1TA9"; STRAND 200..203; /evidence="ECO:0007829|PDB:1TA9"; STRAND 209..214; /evidence="ECO:0007829|PDB:1TA9"; STRAND 253..255; /evidence="ECO:0007829|PDB:1TA9"; STRAND 401..403; /evidence="ECO:0007829|PDB:1TA9" HELIX 78..81; /evidence="ECO:0007829|PDB:1TA9"; HELIX 82..86; /evidence="ECO:0007829|PDB:1TA9"; HELIX 100..105; /evidence="ECO:0007829|PDB:1TA9"; HELIX 107..116; /evidence="ECO:0007829|PDB:1TA9"; HELIX 132..139; /evidence="ECO:0007829|PDB:1TA9"; HELIX 155..167; /evidence="ECO:0007829|PDB:1TA9"; HELIX 215..220; /evidence="ECO:0007829|PDB:1TA9"; HELIX 223..245; /evidence="ECO:0007829|PDB:1TA9"; HELIX 258..284; /evidence="ECO:0007829|PDB:1TA9"; HELIX 289..307; /evidence="ECO:0007829|PDB:1TA9"; HELIX 313..321; /evidence="ECO:0007829|PDB:1TA9"; HELIX 322..324; /evidence="ECO:0007829|PDB:1TA9"; HELIX 326..330; /evidence="ECO:0007829|PDB:1TA9"; HELIX 333..347; /evidence="ECO:0007829|PDB:1TA9"; HELIX 352..364; /evidence="ECO:0007829|PDB:1TA9"; HELIX 371..374; /evidence="ECO:0007829|PDB:1TA9"; HELIX 381..391; /evidence="ECO:0007829|PDB:1TA9"; HELIX 397..400; /evidence="ECO:0007829|PDB:1TA9"; HELIX 407..428; /evidence="ECO:0007829|PDB:1TA9" TURN 87..89; /evidence="ECO:0007829|PDB:1TA9" CHAIN 1..450; /note="Glycerol dehydrogenase 1"; /id="PRO_0000314770" MIGPRLCAATPRFPLVSLAHRNSKVFALASSNAVAQRWGKRFYAPIETETPHKVGVEFEESKDRIFTSPQKYVQGRHAFTRSYMYVKKWATKSAVVLADQNVWNICANKIVDSLSQNGMTVTKLVFGGEASLVELDKLRKQCPDDTQVIIGVGGGKTMDSAKYIAHSMNLPSIICPTTASSDAATSSLSVIYTPDGQFQKYSFYPLNPNLIFIDTDVIVRAPVRFLISGIGDALSTWVETESVIRSNSTSFAGGVASIAGRYIARACKDTLEKYALSAILSNTRGVCTEAFENVVEANTLMSGLGFENGGLAAAHAIHNGMTAIHGPVHRLMHGEKVAYGTLVQVVLEDWPLEDFNNLASFMAKCHLPITLEELGIPNVTDEELLMVGRATLRPDESIHNMSKKFNPSQIADAIKAVDSYSQKWQEQTGWTERFRLPPSRHSPHLTDIHP O13705 SEC10_SCHPO SPAC13F5.06c; CHAIN 1..811; /note="Exocyst complex component sec10"; /id="PRO_0000118949" MSTKNALNDSQIKLLNSLNDNKGIPSTEFVEKFAESLYETQNDGSKKLSSIDGSIKSFAACLHELNRLKSRVGDRIRDYASASKQVQNEYHQKSNHLREKFAQVLELSRHLEDNVNDMRSGLVDAGQELERAENNRKRILSSAELLRYYLEFRSGKPQTLMDFFRTNNHDKMLLCAQRTRQLLALANEVDLPDSSETLARIEKFSEFLETNFLKFFNNEYRKPNWKGMASFGTILQEFNGGASVVREFVNQHEFFIAADKVQSRQGLEQDPIWLILPDPTQKIPPLIQTLSSLFSELCSVIEGDCAVIKRVFPNPELVLQTFFQRIFGQSIQNRLEEVMEIAKGKSNLAYLRTLQTVVSSLRKLVADLKTILENRGFSVSDNSPLSLALNQYMEDLLVPFIEVDDYLKREEHSLRSLFRLSLYKYTSYKIRLETPEPGLLRSLMTPLQGNMVAPTGVHSQFNTKTEGFLLRIADIQENLIQSGSFITEDYITIEKNHSHLNSEKVYSFIGWHAEALNRASILISSQDLSVVISSLVNLLDKLIREDYVFKELSSIQSYISSHDKSKNLDLHYLVDIRECKKIMGYFSAYLMSIVIPFTGVTASSRRETVNILSSSISVIECAVNDVFYATVHALGDHLEIILSPYRQISYAMTEEQIDSSTELRQSMTRNVQNYLDYIKNLYHRLGPYDPSLLALKQKTATMLAAMLISFAFRSKVTAAGALLLQNDINFFHSTLTSWGIDTVDAKFKLILQLLSLLMVKIDVLPAVMQDKRKAGFSEMNIHEVLRLRFDLPENLKLQLNKEEALLPPKSS O13709 ATG43_SCHPO SPAC14C4.01c; CHAIN 1..244; /note="Mitophagy receptor atg43"; /id="PRO_0000116680" MSSESKGIPIPRSDSNKTSDVSSWEEDYELISLGSSQDALQRSGIRSAHGDSGYASSPLRMEHLSSSTIIINNQLKKIDVNESIPENSTLHNKYELGAVESSTSSLSLLQSKEEDDSSNWETEDSESAVEEAELPTIFEGKTVISPSSSGTDHSEAVEYTVPTAPPIPDLRFQQSYLQSIQRANGSAFLVALITLRDHVLYPFLSGGMWVFVRHIFQFLKLQEKGFHFGQSLRRNLGLFSTFKD O13713 NAB2_SCHPO SPAC14C4.06c; CHAIN 1..307; /note="Nuclear polyadenylated RNA-binding protein nab2"; /id="PRO_0000352808" MTTLLETPGYSEKLHDSIEKKLSEYGWGEEAASLADFVLVMLSNGKTQTEINEELVDLIGSDFDTSFSLWLFNQIEELEKSKNASVESVSKIDEIDFIEKESTDKSQQSFSVPETSIQPQSSQTPNITSLREEKELPTGRVGQKLKLTSQKQRFNPMAASFNYSKSVMPAAKRALTQTQEVPLCKYADKCSRANCIFAHPTPAAAPGEGMVLSSEMCASGKECKAADCVKGHPSPATVTTLPPFMSMSTIPIPCKYKPCLNPACRFIHPTKSRNMTWRPPSKTEETSLSERSFAVNESEEQLHVPSV O13718 VTC2_SCHPO MOD_RES 181; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 529; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 583; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC14C4.11; CHAIN 1..734; /note="Vacuolar transporter chaperone complex subunit 2"; /id="PRO_0000116686" MRFSDSIEAGIYEPWRDKYMNYPELKHLLKTEEEAPSWGENDESKFVSVMDAQLEKVYAFHLEILKELNESVDWVKSKVSASQEPDGPPISKEEAIKLLERLDSCTETVKKLEKYTRLNLTGFFKIVKKHDKLYPGYSLRPVFQVRLRACPLGSVQFNPLLAEIFSLYNTLRDGLSAPSNSVQVKPKHEHNVDYNSSMYRRRTFRFWVHPDNVMEVKTYIMRHLPVLYYSGKQGFDKDQNGVSGILDPISTCLYLDNSNFDLYSQNLERSEQAYSLRLHWYGKLTPKTDIIVERMVRQGSTLSHSEDRFTIREKKVRELLSGRYDFRKVEDDHSTTASDQKKKLIEDVEQLIVDNHLQPVLRSVYTRTAFQIPGDDEVRINLDSDWVMIREDSLDIERPCRDPEDWHRHDIDDADFPYKHLRKGEYSRFPYSVLEIRECVRYDEDEPLWISELRNSHLISEIDGFSKYEHGVAILFEKYVSLLPMWVFSMDQDIRKDLQEVYSHPEGSAGSRNVYIKRRNQRVLKQNMTPEPSQPSPLVNRLKANEMHPVSEEPEDNREVYRNEHGDHFNFRSIPGLLKPSTYGSFKHHGKTFVTPPHIKKPEIPLRVSGPIKVEAKVWLANERTFLKWLHVVVLLGSLALALYNSAGERLGQAFGVVYTLLAIFIGFYAWKLHAKRSQMIKSRSPAPMTDYWGPLIVGTALAISLIVNMSFALKDAVYQNLIEPDRLLVKLFT O13719 LAF1_SCHPO SPAC14C4.12c; CHAIN 1..297; /note="SWIRM domain-containing protein laf1"; /id="PRO_0000116687" MKSSQTLVYSIPRNVEKDTCAAAIKAYQYLISPPPSPIPNDKVASTVDVPKCSTIPESPKDSIVEPKPTATPVAQLHSKVYDLYRDSPKIWLRRERQWLQRHSPAYRFSTPAAKRPRRQPSSFLDVHASNTRKRGSPDTPDSGHSTPHSKGDVHPGMPQHNTRFKQSSREFSSNTQAIDVANTPYELLPDYSPDMSVLDKRSHPRPLRSEWKGPPLDLSNDENRHLLHPAELQLAATLRLPCLVYLDNKRRIFAEWHNRRTQGLSFRKTDAQRASRVDVNKASRLWKAFHDEGFFDD O13722 TAF12_SCHPO MOD_RES 297; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC15A10.02; CHAIN 1..450; /note="Transcription initiation factor TFIID subunit 12"; /id="PRO_0000326091" MNGQHSSPGTPVQRPSAGPVNQAQFSQQRTNQLTSLLHTMTMYQQLAQNVGLNTPQGQVYLLQAQTIRRQLQGHAQSGQLPNQQLLQQLQSNGALQQGTPEPSNTRPRPQLNAQEQTMLLVRHRQLQTAQNYLTEMKEALGRIKNELSTNERLDTSAREALVKQESELTVKIAQFTAAISNGIRSIQQLQNRQASSANGNNTGTSTPVNASTDTRKSTASTPQLQQTQAQANAPQQRINPETSSVPETPVGVSAANVSNESTELATSATQQSGLANNVEKSQTPSYMSANHLPKVDSKSPIPFSVPPSRATLTGGYASGSIGLSTPGLSRAPHYELDNGNRLLSKRKLHDLLQQIDSEEKIEPEVEELLLEIADEFVESVTNFACRLAKHRKSDTLDVRDVQLHLERNWNIRLPGFASDDIVKSARKTGPTPSYQQKQNAIGTAKSLNKD O13725 NNRE_SCHPO BINDING 61..65; /ligand="(6S)-NADPHX"; /ligand_id="ChEBI:CHEBI:64076"; /evidence="ECO:0000255|HAMAP-Rule:MF_03159"; BINDING 62; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03159"; BINDING 128; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03159"; BINDING 132..138; /ligand="(6S)-NADPHX"; /ligand_id="ChEBI:CHEBI:64076"; /evidence="ECO:0000255|HAMAP-Rule:MF_03159"; BINDING 161; /ligand="(6S)-NADPHX"; /ligand_id="ChEBI:CHEBI:64076"; /evidence="ECO:0000255|HAMAP-Rule:MF_03159"; BINDING 164; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03159" CATALYTIC ACTIVITY: Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; CATALYTIC ACTIVITY: Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03159}; Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03159}; SPAC15A10.05c; CHAIN 1..242; /note="NAD(P)H-hydrate epimerase"; /id="PRO_0000119062" MSISCLSASAAKALDAELMSAGAFSIDQLMELAGLSVSQAVYREYPPSQYSQVLICCGPGNNGGDGLVAARHLWQYGYKPTVYYPKPSSPELYKRLCKQLDDLDIPVVKSHDSNHFSQLLRDSKLVVDSIFGFSFKGPVRDPFGSILAAIVESKIKVLSVDAPSSWEIDEGPQKEGPLKDFDPDTLISLTAPKPCSKFYKGKHYLGGRFVSKVITKKFNLSLPPYPGIDQVVDITNKPLSMV O13728 AIN1_SCHPO SPAC15A10.08; STRAND 148..150; /evidence="ECO:0007829|PDB:5BVR" HELIX 9..23; /evidence="ECO:0007829|PDB:5BVR"; HELIX 41..51; /evidence="ECO:0007829|PDB:5BVR"; HELIX 65..81; /evidence="ECO:0007829|PDB:5BVR"; HELIX 91..95; /evidence="ECO:0007829|PDB:5BVR"; HELIX 99..114; /evidence="ECO:0007829|PDB:5BVR"; HELIX 125..136; /evidence="ECO:0007829|PDB:5BVR"; HELIX 138..140; /evidence="ECO:0007829|PDB:5BVR"; HELIX 151..153; /evidence="ECO:0007829|PDB:5BVR"; HELIX 157..166; /evidence="ECO:0007829|PDB:5BVR"; HELIX 173..175; /evidence="ECO:0007829|PDB:5BVR"; HELIX 181..196; /evidence="ECO:0007829|PDB:5BVR"; HELIX 204..207; /evidence="ECO:0007829|PDB:5BVR"; HELIX 215..232; /evidence="ECO:0007829|PDB:5BVR" TURN 24..26; /evidence="ECO:0007829|PDB:5BVR"; TURN 33..39; /evidence="ECO:0007829|PDB:5BVR"; TURN 115..117; /evidence="ECO:0007829|PDB:5BVR"; TURN 141..143; /evidence="ECO:0007829|PDB:5BVR"; TURN 168..170; /evidence="ECO:0007829|PDB:5BVR" CHAIN 1..621; /note="Alpha-actinin-like protein 1"; /id="PRO_0000073448" MQANQWQSVQNRTFTKWFNTKLSSRDLPSVFDLRKDLSDGILLIQLLEIIGDENLGRYNRNPRMRVHRLENVNKALEYIKSKGMPLTNIGPADIVDGNLKLILGLIWTLILRFTIADINEEGLTAKEGLLLWCQRKTANYHPEVDVQDFTRSWTNGLAFCALIHQHRPDLLDYNKLDKKNHRANMQLAFDIAQKSIGIPRLIEVEDVCDVDRPDERSIMTYVAEYFHAFSTLDKVETAARRVERFTEVLMSTHDMKIDYESRMKRLLGSIARMQEYWHTVQFENNYTDVKSHSNNFAKFKATEKREWVKEKIDLESLLGTIQTNLKTYQLRKYEPPAGLKIVDLERQWKDFLSEEANQSKLINTHMREIKESMRIAFADRANSFSKMLSTISNEITNLQGDWRDQLDHVEFLQEHLGPLEVELASVKVLYDNCFQAGIEENDYTMFSYEDLEHEFGITANIIANKIKYLENELLEREKRTLSKQELDGITKVFRHFEKKKSNMLNEVEFYAALASLGLVYDTEEGTALFHRAANSEEGVTYERFTEIVMEELEDRDSARQVLYAFCDVADGKSYVTSDDLLRSQVRPNIVKFLECNMNKHSEGLDYLTWIKQLLAEDKEIV O13731 UBR11_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305|PubMed:28947618}; SPAC15A10.11; CHAIN 1..2052; /note="E3 ubiquitin-protein ligase ubr11"; /id="PRO_0000056143" MQLHDPPAPLSQPSASRLQKYLLESAEKHAYDSNEESKTHLLQEVFLSLLNYNEDNWKYFLKEKPGAITSDFRLSRLQHSEPECAQELQDKRSGSKVCGHVFRAGEVIYRCKNCGLDNTCVLCAPCFHATNHEGHETHVSISTSYSGICDCGDPEAWNVDLNCKIHNVPDDEEQKKPEEVIPLELQHSIRTTIHILLDFILDVFSCSPVNLKAQSTVGSILADEEASRLSSAKYGVADRPCNVFRVMLWNDEVHTFDAVVGSVLEALDSSNTAFGLEVAQRVDSIGRFAVATSASVHEAIRIANAISKENLAVNVRTARDFFREDICGILLEWFDDLLESHVCYFADYLQIIVCDEILKNWSPGLEKPAKPEVNFNNLPLEIVNDDDSEDDIYAAEELLDVIANLQDETGVTRIANLGGDEDFEADMTDPTIAGFDHPLDDDNDVNDLLDFETEREDIDDLTDEVMETEENEAAEADYPGVNRNTRQDDVQDISMETESQNETDESQNTENVDYNPQTHTPVPIPTTATQDVVTIRPEFNSQLLNNLRQIINARRRPRPAAVCQVSLREDYWKSPHPIPPSSYSFVESPSSILRLDYFLLFDLKFWKRLRGLLSKLYVVPFNRNLLFKRLMGIRFVIHYRSLATAFLFADREPDHSVMFLSVQFFTTPSLAEAVVKDYDFLTNLNATTLSLLTQSNRPSTLFSSDIEYTPTIQLNRQVLKTRRTYNLFSDLGYLLQHPQVKKLVVDDTRYVHQYIDLLRVFQGVIPQQRAILSHVQWDFPHGKNILFVMQRVAMLSNTVSSCFTQAPYERLFYAIKCIITSITHPKLDIAESLEPLSCIPSSSLTNFTQPLVPFSVSRDPISFYHPLHWMLSNLFSYCRVDASSHWDKDTLLALLDHPLRVCVLLAQIDCNLWIRNGRSILLTDAFYRQLNNIEVSYDKDILAIQTILMFVDPNLVLNAVVQRFEFTDWLYNLTYNEHPNYDTERIPAMLCKMLELLIALITEREQILHVDIQDIIRTRLAQQLCFGPLAYSALLSTISSNLVESLSFDKIREEVTSYKAPDGLHDFGVYSLKDEYYDLVDPYYFHYNKNEREESDTILKKRLAKKNNVSAESIIIEPKIRFLEKDGHDIFFAAVNASTFSLIIFRAIEYALVQAESFGSSDIGNTILGDALQLCLISMKIHEFSKSNDFCSRSCAERYPTDSSIMREFGGSAYCLAELCFAILKSPKYKDVHVKVNAVLAGLQKNDPSAYSNMLEATHFELSTTSSTSDSNEIEKTQEKKRLALEKQKKIMQQFRDQQASFLAQNTDFDIGEDQTEDEVTTEEPEEEVKYHEHIRGNCLLCQEECNDQAPYGVIGIIQGSSLLRKTDVHSEIILDEIYSVPPNLDRESHSRPFGKKYDTVVFNRSKDRLLSAYPPGNNIRGVFVSGCGHLMHLGCFKNYYVARSMYRNDVTAGLSEYYYKYSTAKFFMCPLCRSLSNVLLPMPQIPKMCLNIDTLNFPRSMNGWLEEIGTMSSSSFEYQLVRSSLSDTKDTFRSCFLRPWINSKIISAMLARLKIADGALIDQSNNRDVSDLYDRYCETTKLAMKLVKGSTFTNVSPHDLLNSLAYTVSSLEVSQRCSPKQSGATRSVWFNELGPLTLSFLPTLSDTVLKCVCDQIIKSDQQALLLMESQKLLVCKIFYRHSQLKSMLRNGRMSDHDQIQPFLLSNTFDDFVKISSLMLIFGKQDNILYYVKLFYLSEICKTIISMIKVVADSSVVPDLTINYSQQSKSQFYILCKNVLLWCGSSNNIEILDDESNLLRLMSLVEKYSLPFLRRVALVLYCMFDISLEFNEFSNNEDDSELERLSKLIKVPPLQELYSQMSSDENNQILELIAGWCEHLAQNTWGDSTISLEYPGIYELVKLPHRLENLIDSMQESVCCMCHKTPILPAICMLCGSVICFNARQNTVSSRRLTGECNKHAATCTGSVGIFFITKACGILLLDSISNTGTIMPTPYLDIHGETDLQLRRGCPQFLNQKRYDFVVREQWLRQTVLQKMARHMDMTEMQNWRMA O13735 FAT1_SCHPO MOD_RES 602; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC15A10.16; CHAIN 1..1385; /note="Actin-interacting protein 3 homolog"; /id="PRO_0000087198" MFNNGDNMSRERFSSNHSMQRQKTESRANFSRRLVPSDSNRKPVPNGASNSPLSRDAASHLISTIETSIMKLLVVTKELLESLTNWSKGTVNDSAVSSVYVTLIGEFLQTTKSFHEAGIETADLNDFPLELRSVLEQTLEKTPSSDALETNLPNVRELVMHLLQSLKYKQSLVKSRLNQSRSNLPQMTREANDNDVNRRNSRGSSQGSISSFRNPDSRKQYEETTSASLSAPGAFDALKQTNALERRASKRLSHMVKDQQNNEGSSQNLRNITVESVRGFLRDSSKPDNIMDSPSPKVSKRPSIVRQDSHDSNKLSRRPTINTSFDRKFSPKLTRTPSLTKSLDPGTPTSLKSPSLRKSPSSFVQKDVYSRSNSLRISQANRSNVFPGATDVTRSVSDHRILSSSTINDGEVAPPLPQRSRTISSPNSPLSATVLPSSTPILLPRGRSSTLSVNKKQFNADDGSTLNSPNSIRETEEYAASPKLEDIADEVETDATSQRELLERQIQKAESSEDTSEIESLQGKLSLPQVSSTQQEIQPSSSVPEAASNEIAEKEPAVTAIESITERKEEAPVISSSEKIESGTSISTSDTKGGLANFENDSLEELERLIQQNNAEQDEPSYKFHKYEYSSEESGSEDEFKSEKDTKGYVISNDDSTQVEEDSEDKSTPNTGASAKLINDPSSTITVSDVYPKKPASPVEITEPPSSALVSATSPTTNVPIVPEAVHLSTAFSTAPVSTIVSNISPLPTVAPPNVSGSPSETPISKPEKVPVVSQTEKALPKPLGVDTEKYYFLRYNNQTRKVKVESPLSNANELGELFSNVYKISFSGDSYELNIEDPDTKISYLLEDLSDLKYKSLVSFMFKEQDANKKREDFHSGEVSAIQHSSAQNTLDDHVNTTTHESPSSAFTEILERLKAIEQNISTNHTNDSAALKSSEDHSKLANNFSVPDSIDHKFYQQVKNMQLELASLKQISAAFFTRIPLKIKDFKKEINAFNEKGSLDFQFGRGFVLSSKDRIEREVKNVVEKFDEVNDQIELMRSDVLLRKVRPGLDQTSQLNEESAYLEKRIQTLERSLEEVTPIWKKQWERELNAIVQEQEFLDSHTVLISDLKRDLSALSTVLSNVSAIAELQAKSSIKSKPLTLKTATESEIKGYRDQIQLEVLNLKPDSEARLQAIERSELLQKKRLLQRVDEFSKEVKTFVENEKLNKIGGAEEADRIRTIQDEKVRKILWDDFVSSKRNGKNGGSFIEESSDTVLDEHVVPDNSAKATVAEIDYGSQVDTENFMLERSPLATPKPLKQPDFNIYETPIVRSTAHETDDEQTPSKYSDNRVESSSDTVFENTDLKYDNNVQMSKVTHHVRHDTISTDDYDAYEDAEDVEETSLT O13745 TFB1_SCHPO SPAC16E8.11c; STRAND 6..13; /evidence="ECO:0007829|PDB:8I53"; STRAND 15..27; /evidence="ECO:0007829|PDB:8I53"; STRAND 32..39; /evidence="ECO:0007829|PDB:8I53"; STRAND 43..48; /evidence="ECO:0007829|PDB:8I53"; STRAND 57..62; /evidence="ECO:0007829|PDB:8I53"; STRAND 71..76; /evidence="ECO:0007829|PDB:8I53" HELIX 40..42; /evidence="ECO:0007829|PDB:8I53"; HELIX 77..79; /evidence="ECO:0007829|PDB:8I53"; HELIX 83..103; /evidence="ECO:0007829|PDB:8I53" CHAIN 1..533; /note="General transcription and DNA repair factor IIH subunit tfb1"; /id="PRO_0000119260" MGDRVEALAIFRKKQGVLSIDSRLKWTGEGKTTPSVDIAFDAISNLQTTPASNPKVMIRVFIVVKEGEDPTSLVFHFTGTPNARENCDMITNELRNAIQRQREGSQSKPQGANVDRVNSTNLEKDIDLQESLLTNNPDLLQTFKEAVMKGHLSNEQFWSTRLHLLRAHAVERSQQRGPYNVLSTIKPKTVDNQMKVSLTGQQIHDMFEQHPLLRKVYDKHVPPLAEGEFWSRFFLSKLCKKLRGDRITPMDPSDDIMDKYLKDNEEVTKVSDEPIASHLFDLEGNDQNANVIAELRPDITMRIDKEALPFMKNINQLSERLLEKSLGNSKRFNNENEETYLKESGFHDLEEEASDSKVVLKIKGQDQLLENNFVPSKNQVGLEPLPSLEALQHLYQEDSISLNHIEHDSDSLAEAAMQLTQSMREKHEFETHGTASNLPIDIKNEIVLCHTVTIEFLHQFWNALLNTTFPDKKAMAPLQNALLNSKKRVEAIASQAQEQNVDPKLVYELVSCTLTSIDTSISEYQRRMSYPPA O13755 OSM1_SCHPO ACT_SITE 288; /evidence="ECO:0000250"; ACT_SITE 311; /evidence="ECO:0000250" BINDING 41..55; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=NAD(+) + succinate = fumarate + H(+) + NADH; Xref=Rhea:RHEA:18281, ChEBI:CHEBI:15378, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.6; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per monomer. {ECO:0000250}; MOD_RES 100; /note="Phosphoserine"; /evidence="ECO:0000250" SPAC17A2.05; CHAIN 1..513; /note="Fumarate reductase"; /id="PRO_0000316583" MRCLTIYTWTFRRLPFIPSTNSASFFSTLRFNMSTANNTQAIVIGGGLAGLSATNTILDLGGNVLLLDKNTAFGGNSVKAASGINAAPTQLQFDQHVSDSVNTFYNDSILSAKSKAKPELLRTLTSKSSSAVDWLSERFGLQMDQLSRLAGHSEPRTHRGTHPDYPFKPLAFVLVDQTEKFAASHPDRLQIKKNARVTRLLTNPNHDKVFGVEYMDLSDKSNHTVYGPVVLATGGYAADYSDDSLLKLYHPEALSLSTTNGPYCTGDGHKMVMSIGGSTVDLDLVQIHPTGFVDPKDPTALTKFLAAEALRGSGAVLLTSQGRRFCDELGYRDYVTGEMMKLKSPVYLVLNSAAAEEVANFIKFYSFKGLMKKMKAEELCSTLNCTKDELASTFSEYNRAAKGEIPDEFGRKYFGKTPLELTDTFTVGEVVPVLHYTMGGVQVDTQSRVLSTNGNVIDGLFAAGEIVGGIHGENRLGGSSLLACVVFGRLAGQGASSTMLRRFIASSTSTASS O13762 YF2C_SCHPO BINDING 276..283; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPAC17A2.12; CHAIN 1..897; /note="Uncharacterized ATP-dependent helicase C17A2.12"; /id="PRO_0000310749" MDSLSAYPPQSTFQQLQNDEELARRLQDEWNSSSPSSAPSSSSSQNQVELDEQFARSLQNSQSSSYSLPPFDHPPSKNPTSSSLSTRKRWRQKRLWSFKNFPFRPPTRLTSTPSNSSSLPSIPSSSSTPSISSIPHTTSSVSNDIPSVLGSSDHPIDLDNPEHLTPPSSFITAKQLSRLPTPLPPPSSSSLPTGTISTNSFCPYERKVQPEHVTKELHQLLQHNTPSPFDTIDLQLKNEQVQSAGLLVSLLPHQVEGHAWMESMEQSSKCGGVMADDMGLGKTIQTIALLLTQKSQDPLRKTNLIVVSVALLHQWAEELSTKVHPSKKLSVYIHHGSTKKNLDSYELSQYDVVLTTYSMLAYEMKQNDAFNNNNPATATPPPACSLLETSWYRIVLDEAHTIRNRDTLAAKCCVKLDAKYRWCLSGTPIQNHIDEFYSLLKFLRIKPYCVWSLFAKDISRPLKSYRADIVEAALKRLRILLASTVFRRTKETRVNNLPIVNLPPKTIRTVSVNLLPEERALYNEQMSSAQSLVDNYFNNDHDLSRYGFLLVSLLRLRQFCCHPWLVKSSSLDNSFRIRDSENVRNACKSLDPLTIERIATLQDFNCSVCLDPCLAPVFIIPCGHFTCQECMSMLVGQKYGSSSTSTIIAKCPMCRGNIVQDSLVDATILQAIHGPLNSLKQLELDMNQSFSEQESIKLRWENRIDQMFTKKFGKRASEWKSSSKLNQARQTILDIIGSKRNEKILVYSQFSQYLCLVSHMLKLENIRHVRYDGTMSANQRQKSLHSFNNDKDVLVMLVSLKAGSVGLNLTIANHVILQEPFYNPSIEDQAIDRVHRLGQQKPVTVYRFITKDTIEERIVSVQRKKRQLVKEALDSNENNPLSRLDKEELLYLFGLNS O13769 ULP2_SCHPO ACT_SITE 440; /evidence="ECO:0000250"; ACT_SITE 494; /evidence="ECO:0000250"; ACT_SITE 544; /evidence="ECO:0000250" MOD_RES 526; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A5.07c; CHAIN 1..638; /note="Ubiquitin-like-specific protease 2"; /id="PRO_0000101734" MRDSKDALDDKSGSFTSLLPPFGKQRGTSPNDAIPIKSPLERLANSVTSPEKPTVRTAIQKDSPRRKQIDDDQTPPKHLKRSFQNVTVVSPRKKKTIDVVELPFTKGGYGGFYDPRPGCLKFTTHEINVSYTDTSIPVIHIPVQLLKRCCWLQGWRDNLVESPVHAIHLTLKNRDMKRITIGDSASLLFLYNPLHVESARAGLDLLDQSDFSLTSPSSAKEFKQLLTLKQSTIIPRTPQKTVRSIVKQTSSPHSSKMPKHSLPSSPTPFNSNSGDSLLSRIKNSNQSSSERPTANNGAQEQNQSSSSAGNTSNDFSTLCSQGSDKTLLSDASCTTILVYPFSGTNSIAITNTDLTRLNEGEFLNDTIVDFYLRYLYCKLQTQNPSLANDTHIFNTFFYNRLTSKDKDGKRLGHRGVRKWTQKVDLFHKKYIIVPINETFHWYLAIICNIDRLMPVDTKLEEQDEIVMSSVEQPSASKTRQAELTSNSPAILIFDSLANLHKGALNYLREYLLEEAFERKNVHLKSTDIRGFHAKVPQQSNFSDCGIYALHFVELFLETPEQVIANTLDKSLRRTDAKNFDQQWNLQKINTMRCDLKGLIRRLSTEWSSNNERQSLSSGSNDEEDKENDDDLAILPITN O13774 GCH1_SCHPO BINDING 125; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 128; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 196; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16; MOD_RES 25; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A5.13; CHAIN 1..235; /note="GTP cyclohydrolase 1"; /id="PRO_0000119488" MEPGKKDYIDSPLRMQPASLSGASTPTIDLDGLSWPCQGTQRRIDTAEEEKVKKISNAISTILECLGEDPERQGLLGTPERYAKAMLYFTKGYEQNLTEVINEAVFQEDHEEMVIVRDIDVFSLCEHHLVPFIGKIHIGYIPRKRVLGLSKLARIANMFSRRLQVQERLTKQVAQAIQAVLKPQGVAVVMEATHMCMVMRGVEKPGSSTVTSSLTGIFQRSHKTREEFFRLIGKF O13775 SYEC_SCHPO BINDING 210..212; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 220; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 246; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 386..390; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 404; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 407; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 441..445; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; EC=6.1.1.17; MOD_RES 190; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A5.15c; CHAIN 1..716; /note="Probable glutamate--tRNA ligase, cytoplasmic"; /id="PRO_0000119738" MSVSVALKAKPIAYGAVACANYVNLSGAGSISVKYEDVALLDKQNKESNVSIQLNGSDSPVFGSKLALQTFSQVYPKLFIGENDRSLVESWVETASALAGNHNFLELSSLLAQLDDHLIMRSLFVGYSLTSADFSIWGALKSNNMAAGAVRTGQYFNLARWYKFMDSQNAVSVTMEEFTKAVNISKKQKSSGPNYEIGLPDAIDGKVVTRFPPEPSGYLHIGHAKAALLNQYFANKYHGKLIVRFDDTNPSKENSEFQDAILEDVALLGIKPDVVTYTSDYLDTIHQYCVDMIKSGQAYADDTDVETMRHERTEGIPSKHRDRPIEESLEILSEMDKGSDVGLKNCIRAKISYENPNKAMRDPVIYRCNLLPHHRTGTKYRAYPTYDFACPIVDSLEGVTHALRTTEYRDRNPLYQWMIKAMNLRKIHVWEFSRMNFVRTLLSKRKLTEIVDHGLVWGWDDPRFPTVRGVRRRGMTIEALQQYIVSQGPSKNILTLDWTSFWATNKKIIDPVAPRHTAVESGDVVKATIVNGPAAPYAEDRPRHKKNPELGNKKSIFANEILIEQADAQSFKQDEEVTLMDWGNAYVREINRDASGKVTSLKLELHLDGDFKKTEKKVTWLADTEDKTPVDLVDFDYLITKDKLEEGENYKDFLTPQTEFHSPVFADVGIKNLKKGDIIQVERKGYYIVDVPFDGTQAVLFNIPDGKTVNRYGVKN O13777 ICLN_SCHPO SPAC1610.01; CHAIN 1..217; /note="Splicing factor saf5"; /id="PRO_0000116797" MITKIDSLPKDLIRKVENGEKLLPNQEIVYFEEKTVPYKIRSDEESFPLGKLITLLVTSQSFILFDEEQNSGWKIPYETITLHAKQSKDKPYVYVQLEGEAIRPLLDHILKFERSSGTLHEAPSTEDENEFTDDFLELTLYVTDVDSCYQALCTCQSLHPDTFSSDNDVENASMGNPMSLFFDPNHQWVTAENVDTSACDNRFDSPESPVLKWHRTE O13782 FNTB_SCHPO BINDING 204..207; /ligand="(2E,6E)-farnesyl diphosphate"; /ligand_id="ChEBI:CHEBI:175763"; /evidence="ECO:0000250|UniProtKB:P49356"; BINDING 247..250; /ligand="(2E,6E)-farnesyl diphosphate"; /ligand_id="ChEBI:CHEBI:175763"; /evidence="ECO:0000250|UniProtKB:P49356"; BINDING 253; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P49356"; BINDING 255; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P49356"; BINDING 256..259; /ligand="(2E,6E)-farnesyl diphosphate"; /ligand_id="ChEBI:CHEBI:175763"; /evidence="ECO:0000250|UniProtKB:P49356"; BINDING 316; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P49356" CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000269|PubMed:10617635}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346; Evidence={ECO:0000269|PubMed:10617635}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P49356}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49356}; SPAC17G6.04c; CHAIN 1..382; /note="Protein farnesyltransferase subunit beta"; /id="PRO_0000119767" MDELSETQVMQNETATAVLPLLNGESQSFNLQKHLKYLTKMLDPLPSPFTVLDASRAWMVYWELSSLAILGKLDSSVCERAISSVRQLKGPSGGFCGGNGQDEHLLSTYASILSICLCDSTDAYSLIERDRLYDWLFSLKNPDGSFRVNNEGESDARSVYAAVCVSSLVGISMDDPLFEGTLQWLCKCQTYEGGLSGVPYAEAHGGYTFCALAAIALLGGLDNLNEIKLSTWLVQRQDPALYGFSGRSNKLVDGCYSWWVGASHVIVASGYGSASHKSLPNLFYNPEKLLGYILQCCQSTSGGLRDKPPKRPDQYHTCYCLLGLSSIAYDYRYHTSDGWSYKPSILHSSLSSLLPAHPIYCVPFGFEERIKSYFLSQESSKF O13792 SUB2_SCHPO BINDING 95..102; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC17G6.14c; CHAIN 1..434; /note="ATP-dependent RNA helicase uap56"; /id="PRO_0000055081" MASAQEDLIDYEEEEELVQDQPAQEITPAADTAENGEKSDKKGSYVGIHSTGFRDFLLKPELLRAITDSGFEHPSEVQQVCIPQSILGTDVLCQAKSGMGKTAVFVLSTLQQIEPVDGEVSVLVLCHTRELAFQIKNEYARFSKYLPDVRTAVFYGGINIKQDMEAFKDKSKSPHIVVATPGRLNALVREKILKVNSVKHFVLDECDKLLESVDMRRDIQEVFRATPPQKQVMMFSATLSNEIRPICKKFMQNPLEIYVDDETKLTLHGLQQHYVKLEEKAKNRKINDLLDSLEFNQVVIFVKSVSRANELDRLLRECNFPSICIHGGLPQEERIKRYKAFKDFDKRICVATDVFGRGIDIERVNIVINYDMPDSPDSYLHRVGRAGRFGTKGLAITFSSSEEDSQILDKIQERFEVNITELPDEIDVGSYMNA O13794 YSH1_SCHPO ACT_SITE 403; /note="Proton donor"; /evidence="ECO:0000255" BINDING 78; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 80; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 83; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 165; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 186; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 186; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 425; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" SPAC17G6.16c; CHAIN 1..757; /note="Endoribonuclease ysh1"; /id="PRO_0000238906" MSKRKEFDEDAPVDPSDLLEFINLGAGNEVGRSCHVIQYKGKTVMLDAGVHPAYTGLSALPFFDEFDLSTVDVLLISHFHLDHVASLPYVMQKTNFRGRVFMTHPTKAVCKWLLSDYVKVSNVGMEDQLYDEKDLLAAFDRIEAVDYHSTIEVEGIKFTPYHAGHVLGACMYFVEMAGVNILFTGDYSREEDRHLHVAEVPPKRPDVLITESTYGTASHQPRLEKEARLLNIIHSTIRNGGRVLMPVFALGRAQELLLILDEYWNNHLDLRSVPIYYASSLARKCMAIFQTYVNMMNDNIRKIFAERNPFIFRFVKSLRNLEKFDDIGPSVILASPGMLQNGVSRTLLERWAPDPRNTLLLTGYSVEGTMAKQITNEPIEIVSLSGQKIPRRMAVEELSFAAHVDYLQNSEFIDLVNADHIILVHGEQTNMGRLKSALASKFHNRKVDVKVYTPRNCVPLYLPFKGERLVRALGKVAVHKPKEGDIMSGILIQKDANYKLMSAEDLRDFSDLTTTVLTQKQVIPFFSSMELANFHLKQMFGYVKQSKTKAGQPQYTVMDAITLTLIQEHKLALEWVGNIMNDTIADSVITILLGIESSPASVKLTSHKCNHLHSHLDKPPKVSKEEDRIKKLMMFLDNQFGESMTKTEKGVEIKFEKYEASIDFSTMKVECSNEALRSRVVHVLSRAINTILPFSEASQNDVSEDDFENEESDDDKIFEQQTKIEDDVKNENKTEPVEEQKSEEKNEQPNLKKEELS O13800 RDL1_SCHPO SPAC17H9.03c; CHAIN 1..230; /note="DNA repair protein rdl1"; /id="PRO_0000116688" MNQVTQFSGNSANLMLYWILKSYYSRFDRIMWIDTLGTFNPAALPLPCLEKTMLVRSFDAQGLKDAVDELESNLKSSEDQAYALCIDSFSNPIGLLMAQGNISFAHAFMMTLGRKCRILTRKFRLAVYLSTSLVYIKQLHLSKPALGNSWPFCLDHSYILEDQQHNKCLVHCNQSRKDLLGCSQLFLLLKGSFTHEYLTIDFYNGTPVSVSSKLHVSPSLYHSSTLNSPS O13802 EBP2_SCHPO MOD_RES 272; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17H9.05; STRAND 120..122; /evidence="ECO:0007829|PDB:8EUP"; STRAND 160..162; /evidence="ECO:0007829|PDB:8EUP"; STRAND 168..170; /evidence="ECO:0007829|PDB:8EV3"; STRAND 174..176; /evidence="ECO:0007829|PDB:8EUY" HELIX 97..106; /evidence="ECO:0007829|PDB:8EUY"; HELIX 115..118; /evidence="ECO:0007829|PDB:8EUY"; HELIX 135..159; /evidence="ECO:0007829|PDB:8EUY"; HELIX 178..181; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..333; /note="Probable rRNA-processing protein ebp2"; /id="PRO_0000119999" MAGIESKQRRAQKKAAKAAMKEKKNKESNESSTSVEALNEKEMINTIKSPIIETADTADQENESEGSDEVELSDLEGIELEEDADLIRKRKLAINNTVALENIYERIKYPDDISFVENQAVTTKEPIIIENVEDDLARELAFYKQGVSSVKAAFAKLREANVLISRPHDYFAEMLKSDDHMEKVRQELIKEATAKKLSQQAKKQRELKKFGKQVQLAKQEERQREKKETLEKINLLKRKHTGGDLTTEDDFDIALSSASADTFKKGSRSTKSRPQPNPKRQKKNEKYGFGGPKHRSKSNDLDSLAATEFGRKGLKNIKSKKRPGKARREKARK O13808 GMF1_SCHPO SPAC17H9.11; CHAIN 1..141; /note="Actin-depolymerizing factor gmf1"; /id="PRO_0000310308" MSSEARMFTISDTTMKEIDRFRLRLKKSVMYAFILKVDKATKEIVPDGEIMDLQSIEEVADELSETNPRFILVSYPTKTTDGRLSTPLFMIYWRPSATPNDLSMIYASAKVWFQDVSQVHKVFEARDSEDITSEAVDEFLH O13811 PDI2_SCHPO ACT_SITE 51; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 54; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; SIGNAL 1..19; /evidence="ECO:0000255" SPAC17H9.14c; CHAIN 20..359; /note="Protein disulfide-isomerase C17H9.14c"; /id="PRO_0000034217" DISULFID 51..54; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"; DISULFID 170..173; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" MRLPLLSFVIFALFALVFASGVVELQSLNELENTIRASKKGALIEFYATWCGHCKSLAPVYEELGALFEDHNDVLIGKIDADTHSDVADKYHITGFPTLIWFPPDGSEPVQYSNARDVDSLTQFVSEKTGIKKRKIVLPSNVVELDSLNFDKVVMDDKKDVLVEFYADWCGYCKRLAPTYETLGKVFKNEPNVEIVKINADVFADIGRLHEVASFPTIKFFPKDDKDKPELYEGDRSLESLIEYINKKSGTQRSPDGTLLSTAGRIPTFDEFAAEFLDMSNAAKEVVLEKVKQLALEDSSRWTKYYKKVFEKILNDENWVHKEAKRLSKLLRQKSIALASADDFKTRLNILNSFLPGNH O13824 NMD2_SCHPO MOD_RES 60; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19A8.08; CHAIN 1..1049; /note="Nonsense-mediated mRNA decay protein 2"; /id="PRO_0000096872" MSREEQIKKLNQYLDNRELAFRAKDGDKNIFHTESQLDSSLKKNTAFMKRCKSSLTSENYDSFIKEIKTLSLKKFIPEITAAIVEGMMKCKATKDILSSVKIVWALNLRFSTAFTGPMLANLYCALYPNPGYSLCHESYFELKQNENEVSEKDRSSHLLKVRPLLRFLIEFWLNGVVGTPEDFVSYLPSTDSNDKKFRKPWFEEQNLKKPLVVLLFNDLMDTRFGFLLLPVLTSLVRTFSCELFTTEDFEDKETLELVNRLNPVVWRTYLRKSLNSYVDKLEVYCQKRKSLFEELNKQYQEQSIIRADPNNEKFQRLANFSKSIESEFSSYASLSEVLNRKASEDLLELNFMEKASSGTNSVFNASGERSESANVETAQVWDDREQYFFYEVFPNFNEGSIAEMKSSIYESSQEGIRSSSENNKKEDDLKDSTGDLNTTQVSSRVDNFLLKLPSMVSLELTNEMALEFYDLNTKASRNRLIKALCTIPRTSSFLVPYYVRLARILSQLSSEFSTSLVDHARHSFKRMIHRKAKHEYDTRLLIVRYISELTKFQLMPFHMVFECYKLCINEFTPFDLEVLALLLESCGRFLLRYPETKLQMQSFLEAIQKKKLASALASQDQLVLENALHFVNPPKRGIIVSKKKSLKEEFLYDLIQIRLKDDNVFPTLLLLRKFDWKDDYQILYNTIMEVWNIKYNSLNALARLLSALYKFHPEFCIHVIDDTLESLFSAVNNSDHVEKQKRLAQARFISELCVIHMLDVRAITNFLFHLLPLEKFESFLTMKASTLTNINNDMFRLRLIVVVLQTCGPSIIRSKTKKTMLTYLLAYQCYFLIQPEMPLDMLYEFEDVIGYVRPSMKVYMHYEEARNALTERLQAISDDWEEDDTRPVFQGANDGDISSNEESVYLPEDISDESETDEESSGLEESDLLDSEDEDIDNEMQLSRELDEEFERLTNESLLTRMHEKNPGFDVPLPLRASSLGSPYVTRNEESASESSHVMFTLLTKRGNKQRSQYLEIPSHSSLVRSTKNQQTEEIMERKRVKEMVLNFE O13829 RU17_SCHPO SPAC19A8.13; CHAIN 1..261; /note="U1 small nuclear ribonucleoprotein 70 kDa homolog"; /id="PRO_0000339243" MAEKLPAPLLALFAPRPPLRYLPPMDVPPEKRSTPRVSGIAKYLKYAQSHDQQYHPTESLEEKRLRLRDEKQKQQRERLRSMIKVWDPDHDRHVIGDPYKTMFLSRLSYDTKESDIEREFTRYGPIERIRVVRNKVTGKSMGYAFVVFERERDLKVAYKASAGLMLNGRRIVVDVERGRTVKGWLPRKLGGGLGGRHYTKERPRRERGSRFRGDSGFRGGYRGGFRKSSGGGSRFGRGPTRSSHSSDYGGRDSSPKRRRYN O13834 PTR1_SCHPO ACT_SITE 3194; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; SPAC19D5.04; CHAIN 1..3227; /note="E3 ubiquitin-protein ligase ptr1"; /id="PRO_0000120347" MRITKSPPKNQYSQPPPRVAEFIRQAQNEEVTSDLGLVSLCSEFRKNDWPYPRGDLYSWVPVLNRFDAILERIVEHYSLKDKVQTKPFDSDTLSILLEILSFSAHLLSHCANRSIYNSTVYLEYLLNSSVLEVIDSTLALLLHIVQKATISKRGKQLFSLSQDRLFRFLMFLPQDAMKTGFSQNYETLLFSNEIPQEWCSLELSYYKSSPSKDFSSASQPNSEGFSILKLPYNKVLGKPIEELLVKTLHDNQIPEQYSFDLLVSLMLRQNLYDINRRRLMIRIGLLALSNLVYAHSQAVQTRFLIADPEITTHLANLVSPDVDLPQNFKAVCFECFKAFFFKKSMIPSVLASLNVSVSYGLMMNLVRDFSKNLENPNFYYEREYVDSFYDFLQFMTSSPLGGNMACSAGLTSLLGYHLSVKTPQATYVVARSIVMLDHLIDGYSMAFPDFSESKGLDMLVDRVQYELEAGLQDIKSGKGNPEIVLNMDYAISYDRYFLLKNLLKFVLHLIQSGGSVVELRNLIDSSLISSLAFLLEHHEVYGSNLFASTTNIMSTFIHNEPTCYGIIHEKKLSHAFLDAVNRKILNSSDAITSIPLAFGAICLNSQGFDLFLEKNPIPQLFSIFTSLNHCKSLISSDNAAILGTYIDELMRHQPSLKDPIVKMIFKACDQVSALLDNFNPFQYINAKEYPYLLYLETFSSFLENIITNEGHARYLISKGIVSHVLNLIQHPVLAFGFIDSSAFNSFFVLLHHAVDFDAPEVFRPLLDCIITRCEEGITEFTIVSLKQATISLIKDSNMGHEDANNFLHFSIVGNLLTIFAELFSSHAALKKAGNLPLVQLFISPSRYAGIFDILCNIKSIATSLDIHICLGVSDDFVLCSDSLTTIVTDKDEKEKFETKKKELTQDSSFCKFQNIRSNFSQIAYGVSKFFTSLTRALGNTSVQDFNEYKMIHKLGSNIALVVDELINLSSKQITSHPQSLSIASLEASLIFVLGASSIIREDDSKVTLVLLISRLLGGCRTMDVLISLNETVSGFFRLSDRDPLSKSNRVLLALSSTLLNLILVFTSADFMSETSKTLNMALKSEFDMTDFNNSGSKLMHVLHARIFISVLHLWRSADDLHLPYITRALLTNVLSNCYQFEDGIKNVVDSINNLRTSIANGDIKEPLDVVTDDNTNSNFSLEETNASVTDMPESEKHENGIFQAYLLKEMPNDIVSQFEMLKSKQIELTVQMASYEGDLNQNLCDFLYTRDDVQMNADVQFSVTSGLIVEIKKLAQSTDCKAKNQLGPAVGLLSLFISHDFTQNKAKNCVLSELNFFLELLHSLNNGLPSDSHKTSIVCILYLLEVLLADSKKPDEFEFNSEDCSLKLTDGAITVDLASQKHIMSSVITLLSLNSANLGVVVSAFRVVVLLTSASEMIHTFVKLSGLPSLFKAMRACSGFCNESLHIPFISILRRLLEFDEVVELMMFDDLVNIFKLQGRARKTELHGFIRANAEMVLRSPECFIKILKDCCVLGHFTPESEHYYLELKESLPGVLQNGQTDLDPSKEQMSSVIVSFLLDELMDLTETRQFSDRSPNSEFTPENDSLYMYNVFLLQCLTELLSGYNACKRCFLNFQPRRKAPFFNLSRKYNSYLVGFFLEKLLPFGCIRLSENNEVRKAFSVSNWAISILVFLCAYSNEQQTQAVDEIRREVLTSVLKFYKSSSSFSENLEAYYCKLLVLAELCYRLCDAQTVSQKAPNHLLRRSQDQNVKTMIDLGYIPTLTNAISEIDMNYPVSRKVVRHILKPLQLLTKEAIFLSQTNPEALSGAAQDSMGDQSLSSSSEESSDSDREEPPDLYRNSVLGIFQGDIVNENDENYEDSEDDGVYEEMEFEDDQSGSADSVVSEDDADDVMYSDNDDMNIEFMVDEQDASSQNDDSSFDEASSHGDVISIDEEDLDNQGEEFEWEDEDNASSGYEDELDYNEDEVGENDSTTFEAMENAFTETSDNDDHLEEADHVSPVEIDFLENDENSSSEQDDEFQWEWNTETPSGADILSRHGALLRDLFPLPGLSRRVMIINSNDPSRSRPFLNNNASEGLLKHPLLLRNNLIHTPKATELWENLAEIDNHTASGAAFQRLLYYLALEIPNEDSSVLGWTSLKVSKHTDPLRATSDFIPLFSMQRWNSITSMFFAHASGSIALRITGSVLFALVPPALEKYNLENQKKEILENESKEEETRQPEVNIQPEEPINTSDMEGVTTEANEIGSYQEPSLINIRGREVDVSSLGIDPTFLLALPEEMREEVVFQHIQERHMESISDSSRRIDPSFLEVLPSDLRDELLFQEAVQMRLFDHATRNNNSVDHEVEMEEIDQGGTVSEHREKSVKPVKKIPVPNLLDRQGLYSLIRLIFISQHNGKNPYYDLIVNISENKQHRADIVGLLLYILQEASINDRASEKCYRDLTVKSLNNSQQKEVKKSTGLLESLCKVPVVNGISAPALILQQGIDLLSHLATWADHFASFFLSMHDFSGIASKKSAGRKNRESNVYKIAPINVLLGLLAREELFGNTLVMNTFSELLSTLTKPLLSFYKSEKLQKDSATTGYTNDQDSRGSTVPKQDPGTTASRKDKKILSPPNILDENLRLAASLITTDSCSSRTFQNALSVMFHLSSIPKAKILIGKELLRHGQEYGNSITNDLSRLCADVKSGKNESELQVALAPFCPASSNQAKLLRCLKALDYIFERRPKGQEQSPGNIIQLLEFYDNLKFSSLWEVLSECLSALRDHTSITHVSTVLLPLIESLMVICRLVFIELPEDVGKHISPILERFKTLFISFTEEHRKIINMMVFTTPSLMSGSFSLLVKNPKVLEFENKRNYFNRQLHEEAAKEQYPPLNITVRRDHVFLDSYRALHFKDADEVKFSKLNIHFRDEEGVDAGGVTREWLQVLARQMFNPDYALFLPVTGDATTFHPNRDSSVNPDHLSFFKFTGRIIGKALYDGRLLDCHFSRAVYKHMLHRSVSVKDIESLDPDYYKSLVWMLNNDITDIITEEFAVEKDVFGEKTVVDLIPNGRNIPVTELNKQNYVNRMVDYKLRESVKDQLKSLLDGFSDIIPSHLIQIFNEQELELLISGLPEIDIDDWKNNTEYHGYNVSSPQVQWFWRAVRSFDEEERAKLLQFATGTSKVPLNGFKELEGMSGFQRFNIHKSYGSLNRLPQSHTCFNQLDLPEYDTYEQLRSMLLTAINEGSEGFGFA O13846 SCS7_SCHPO BINDING 204; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 209; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 228; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 231; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 232; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 286; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 290; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 306; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 309; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q03529"; BINDING 310; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q03529" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q03529}; Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center. {ECO:0000250|UniProtKB:Q03529}; SPAC19G12.08; CHAIN 1..347; /note="Ceramide very long chain fatty acid hydroxylase scs7"; /id="PRO_0000362158" MASVTSEKCVILSDGTEYDVTNYLVANKDAADLLRRYHRQEVADILNATSKSKHSEAVVEILKSAKVPLKNKEFSDLVDQNIGVGYGNEFIVKPTDLDKDFEKNHFLDLKKPLLPQILFGNIKKDVYLDQVHRPRHYRGSGSAPLFGNFLEPLTKTPWYMIPLIWVPCVTYGFLYACTGIPFSVAITFFIIGLFTWTLVEYTMHRFLFHLDEYTPDHPIFLTMHFAFHGCHHFLPADKYRLVMPPALFLIFATPWYHFIQLVLPHYIGVAGFSGAILGYVFYDLTHYFLHHRRMPNAYLTDLKTWHLDHHYKDYKSAYGITSWFWDRVFGTEGPLFNEQGKISTKAK O13851 DLP1_SCHPO CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = all-trans-decaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:27802, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.91; SPAC19G12.12; CHAIN 1..294; /note="Decaprenyl-diphosphate synthase subunit 2"; /id="PRO_0000123981" MSFPFASLLKRPSAISSLLSLKKPGSWSSILLKAVGVLSRDSRWHSDLLKMLTEEMDSLNGQINTWTDNNPLLDEITKPYRKSSTRFFHPLLVLLMSRASVNGDPPSQQLFQRYKQLARVTELIHAANIIHINIGEEQSNEQIKLATLVGDYLLGKASVDLAHLENNAITEIMASVIANLVEGHFGSRQNGSVGLSNERTILLQSAFMPAKACLCASILNNSSQYINDACFNYGKFLGLSLQLAHKPVSPDAQVLQKNNDILKTYVENAKSSLSVFPDIEAKQALMEIANSVSK O13852 POZ1_SCHPO SPAC19G12.13c; STRAND 159..161; /evidence="ECO:0007829|PDB:5WE0" HELIX 2..18; /evidence="ECO:0007829|PDB:5WE0"; HELIX 28..30; /evidence="ECO:0007829|PDB:5WE0"; HELIX 31..43; /evidence="ECO:0007829|PDB:5WE0"; HELIX 45..47; /evidence="ECO:0007829|PDB:5WE0"; HELIX 54..64; /evidence="ECO:0007829|PDB:5WE0"; HELIX 93..115; /evidence="ECO:0007829|PDB:5WE0"; HELIX 130..157; /evidence="ECO:0007829|PDB:5WE0"; HELIX 164..174; /evidence="ECO:0007829|PDB:5WE0"; HELIX 176..178; /evidence="ECO:0007829|PDB:5WE2"; HELIX 179..188; /evidence="ECO:0007829|PDB:5WE0"; HELIX 193..206; /evidence="ECO:0007829|PDB:5WE0"; HELIX 209..230; /evidence="ECO:0007829|PDB:5WE0"; HELIX 238..241; /evidence="ECO:0007829|PDB:5WE0" TURN 65..68; /evidence="ECO:0007829|PDB:5WE0"; TURN 123..125; /evidence="ECO:0007829|PDB:5XXF" CHAIN 1..249; /note="Protection of telomeres protein poz1"; /id="PRO_0000116741" MNEKIRSQSVLNTLETFFIKENHYDMQREESSIVNACLRYLGYSKSMCHEKMPIFMDIAFIEYCFNLSLDPSSFQNLPITQTQPDSQQILWEYSLISNALERLENIELERQNCMREDGLVKYTNELLLNKETLNNEALKLYSCAKAGICRWMAFHFLEQEPIDHINFTKFLQDWGSHNEKEMEALQRLSKHKIRKRLIYVSQHKKKMPWSKFNSVLSRYIQCTKLQLEVFCDYDFKQREIVKMLTSNIN O13857 PLB2_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SIGNAL 1..19; /evidence="ECO:0000255" SPAC1A6.03c; CHAIN 20..662; /note="Putative lysophospholipase SPAC1A6.03c"; /id="PRO_0000024641" CARBOHYD 74; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 127; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 162; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 196; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 266; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 274; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 303; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 376; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 406; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 411; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 483; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 518; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 523; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 547; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 556; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 574; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 596; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 613; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLFNCFGILALLQILPALAYPPCREQMSDPYEFGESDLMRPGMHDTPLSLMQKREALAISLSKRDSVGSYAPYNVTCPSDYMLRPASDGISSGEQSFIDKRIPKINTQMRSFISNTGLDVDVNSVINDSDGPRLGLAFSGGGLRAMVHGGGVLNAFDSRNGNGSSLAGILQSAMYIAGLSGGSWLVGSVAVNNFANITYLRDNVWNLEHSVFAPHGDNVVENLAYYDDLDDEIDQKKDAGFDTSLTDLWGRALSRKLVDATQGGPNITFSSIRNQTWFQNADYPYPIIISDSRLEEEKAIPANTSIFEFTPYEFGTWDNGIKAFLPMEYVGTHLKNGVPPDHKCIRNYDNAGFVMGTSATLFNTFLLEWSQEVTSNSTLYDIIHKVFEKLSEDQNDIAPYPNPYQNFTTTNTTVKNPFERFDTIDLVDGGEDDENIPIWPLLHPQRFVDVIFAVDATYDDSNGWPDGSSIVTTYERIITYNANKSVDVRGFPYIPDEDTIISLGLNTHPTFFGCDGRNTTAGNHTVDNNTPPLLVYFPNYPWVYYSNISTFTMSMNDTLSSGILENAALSATQNNSDSFAVCLACAMIQRSLERKNMSTPSQCSSCFEQYCWNGTTVNNPSAVSNYAPTVLSASTTSGTSSVRAKPIVFYLFASLLTVSLLL O13858 SEL1_SCHPO SPAC1A6.07; CHAIN 1..636; /note="Eisosome protein sle1"; /id="PRO_0000304029" MSHASKNYNAQLTAAAASTALHGTKKIYNSNENDRAVNSFLGNRTSYGEAVNGSPQYDYMRSRMSTLGSANQPMAPPSLRNRSSVYLPTPAGPPQIPVNTGKRYTLTSSSANYMTKSERQMRPPKSYDFPPSQQVRPSTSRSPSYASYNSEEVNFQSYQDPRLLPRTSQMYMPDNNYSPAVKSPAAQRRSSSYMVPANSRGSPANYNTPYYPTAIPPPIEEYSPSVSLPTSPVAEESYNNVQRSSTVRNNTTQKSVLKKPSRKMSPAYTSSYRQNSPSSQVPPVSKKHVIIYENKEGSSSSESVYEDVFEDFDPSGSNQASLRSTSTIHYTPSSKRISVIPPNTSNIGSRVVSRSGQNNNQPAQPGQYNQQSQPVQSYQSGQSTQHFQPVQPIQPVQSTQYYQPSSPVQPVQNGVPAPPMQPVQSTQYYQPSSPVQPVQNVKPAQPAQPSLEDAAKRRVEEMLRQMDITPTASSTTANNAYASAEPHPSAFPDDMNSVFSDSSFERERDSGRGRSTNLFSKFKSGRSRSKASGEAPYSYPAPPVPSVNNAGARLTLRDSGAAPEATYSLRQPSNHAYSEGRSYTFTGGQPPSVPTMPYGSRFANDSDSMMGSTADFSSKKKGGKFKAFKKFFKMRF O13864 IMB1_SCHPO SPAC1B1.03c; CHAIN 1..863; /note="Importin subunit beta-1"; /id="PRO_0000120763" MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLWQSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICESVSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGCLVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAADILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVAMLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCHFAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQILDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPSFVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQTYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSESLTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA O13870 NOT3_SCHPO MOD_RES 248; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 249; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 251; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 369; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 385; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 433; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 435; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 449; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 471; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 474; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B3.05; CHAIN 1..640; /note="General negative regulator of transcription subunit 3"; /id="PRO_0000317310" MSARKLQVEIEKTFKKVTDGIAIFDEVYEKLSASNSVSQKEKLEGDLKTQIKKLQRLRDQIKTWASSNDIKDKKALLENRRLIEAKMEEFKAVEREMKIKAFSKEGLSIASKLDPKEKEKQDTIQWISNAVEELERQAELIEAEAESLKATFKRGKKDLSKLSHLSELESRIERHKWHQDKLELIMRRLENSQISPEAVNDIQEDIMYYVECSQSEDFAEDENLYDELNLDEASASYDAERSGRSSSSSHSPSPSASSSSSSENLLQDKAEAEEKVSADASVQDIAEKESLDADKELATNDQEDDEEENQAETQKDGAISNNENMQSEVQTTNPSASTSAVTNITKPTLIQNPSTPLSVSNSKVASPETPNATHTAPKVEMRYASAAAAAAAALAKESPSHHYIMQQVRPETPNSPRLNSTVIQSKWDSLGHTASPKMQTQPVRSVSQSSATTETNVKPTKEENADVPVSSPDYLKDLVNALNTSKEQHKGAIDKEKLTEALNISCVYVPDATDAAKPQYYIPKDPYPVPHYYPQQPLPLFDSSEMTELVDPDTLFYMFYYRPGTYQQYIAGQELKKQSWRFHKKYTTWFQRHEEPKMITDEFESGSYRYFDFEGDWVQRKKADFRFTYQYLEDDDDWTR O13880 VHT1_SCHPO SPAC1B3.16c; CHAIN 1..568; /note="Vitamin H transporter 1"; /id="PRO_0000121371" MASEWPETSRASSVEENPKLNIPEIVESVSDSKPSLKNQFSTTVIDSSDLNVFNDGAETTVKEQEFTSSELRRLQKLRLKMDLRIIPCLWILYFLSCCLRFTVSLSFTMNTAQGHSLIQTLSGYSAHYLALGLALFYVGYIIFEVPSNLMMAFIEPRIWVSRIQLTIGVVGACHAVLGTKHGNAQSYVALRFFLGVAESGLWPGLAYYMSRWYRGKHLGKRIGWYYTAAQIAAAAVSLVSAGFQKMDGARGLYGYQWMFLIWGVVAIAQALSIPWWLPAVASKEHRKSLSSFIPLPKWMKTLSPQRIGFLTPADKSLHSRYIAEMNVGKRWQWSDLLKSCLDLRVWPFILMYFGIVGVGNGIFNYCTLIIEEINPSFSGIDISLLNAPIWLADALGIVTVMPLYDRFHKKFSFFTGSCLIIIAGLAVANYAPRAWSRYGGLLMIGFGLGPTVPICMAWCSASMAKTYGDVGVASSLALVTGLGNLGSVVTTYALYSGWPGDPTFRKSNDVCIALIGVSIIACGIEFLLDKTGFGQFNASFNNHDHEVEDEQEMTDIKPALPSSQQADA O13896 RPC10_SCHPO BINDING 4; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 7; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 28; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 74; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 99; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 102; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472" SPAC22A12.05; CHAIN 1..109; /note="DNA-directed RNA polymerase III subunit RPC10"; /id="PRO_0000121477" MQFCPTCGNHLIVAVDEEGRNAFDCRTCPYHFPISTFLYSRHEFAQKEVDDVLGGEEAFESNQQTEVTCENTKCDNNRAYFFQLQIRSADEPMSTFYRCTKCKFQWREN O13903 RRP40_SCHPO SPAC22A12.12c; CHAIN 1..240; /note="Exosome complex component rrp40"; /id="PRO_0000352816" MAEVEEKGLLSYYFPGERIPDSIISQDGSIRLGPGLVFQKKDREEEIVVSKAGRLHQTGKNAMLIDSRTKRYIPATNDQVIGQIISRFAEGYRVDIGSAHIAQLNALAFENVTRKSRPNLNVGSLVYARVSLADRDMEPELECFDATTGKAAGYGELKNGYMITGLSLSHCRKLILPKNTLLQTLGSYIPFEIAVGMNGRVWVNSENLSTTVLICTAIRNCEFMSDEEQIKYCKDLIKKL O13907 ACL2_SCHPO CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8; MOD_RES 24; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22A12.16; CHAIN 1..492; /note="Probable ATP-citrate synthase subunit 2"; /id="PRO_0000340113" MSAKSIREYDGKAVLAYWLNRSPSISKEEYKTVSATPAVQLAQIQFPLPTLVIPAESTTYREVVEDVFAKVEQEHPWVKETKLVAKPDQLIKRRGKSGLLKLNATWDEAKEWIRERAGKNQKVQHAVGYLTTFLVEPFVPHPPNTEYYININSVREGDWILFCNEGGVDVGDVDAKARKLLVPVRLSEFPSRATIASTLLSDIPVEQHESLVDFIIRLYSVYVDCQFTYLEINPLVVIPTAKGADVFYLDLAAKLDQTAEFECGAKWAVARAPESLGIKTSGEESGAINADHGPPMVFPAPFGRELSKEEAYVQGLDAKTGASLKLTILNAEGRVWNLVAGGGASVVYADAVAVNGAADELANYGEYSGAPTDGQTYEYAKTVLDLMTRGEPRADGKVLFIGGGIANFTSPAVTFRAIARALGDYKDKLHAHKVSIWVRRAGPNYQEGLRVIREAGKKFDLPLKVYGPECHISGIVPMGLGKAPVEAEWQMA O13914 SYA_SCHPO BINDING 606; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03133"; BINDING 610; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03133"; BINDING 725; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03133"; BINDING 729; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03133" CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_03133}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03133}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133}; MOD_RES 389; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C11.09; CHAIN 1..959; /note="Alanine--tRNA ligase"; /id="PRO_0000075286" MTAESEVVNWPANEIRRTFLKYFEDHGHTIVPSSSVIPYDDPTLLFANAGMNQFKPIFLGTVDPSSDFAKLKRACDSQKCIRAGGKHNDLEDVGKDNYHHTMFEMLGNWSFGDYFKKEAIAMAWDLLTNVYGLKKDQLYVTYFGGHEESGLEPDLEARQLWLDIGIDESRVIPGSLKDNFWEMGDQGPCGPCSEIHYDRIGNRTVPELVNMDDPNVLEIWNIVFIQFNREKDGSLRPLPNRHVDTGMGFERLVSVIQNKTSNYDTDVFSPIFAKIQELTNARPYTGKMGDEDVDGIDTAYRVVADHVRTLTFAISDGGVPNNEGRGYVLRRILRRGARYVRKKFGVPIGNFFSRLSLTVVEQMGDFFPELKRKVDDVRELLDEEEESFSRTLDRGEKMFEQYAAAAKKTPSKTLQGNDVWRLYETYGFPVDLTHLMAEEAGIKIDEPGFEAAQARSKEISKQASKGGSSGDDLLVLDVHALGALSKMDDIPETDDVFKHNSVSLKSVIKGIYHKGGFQKSTEGFNSGEQLGLLLDRTNFYAEQGGQEYDTGHIVIDGVADFRVTNVQVYAGYVLHTGFLEYGNLTVNDSVVCEYDEIRRWHLMNNHTVTHILNLALRNTLGDGIDQRGSLVSQEKLRFDFSYKSSIPIDKLLLVENYCNNVIQDNLSVYSKEVALSKAKEINGLRAVFGEVYPDPVRVVCIGVDIDTLLQEPKKPDWTKYSIEFCGGTHCDKSGEIKDFVILEENGIAKGIRRIVAVTSTEANRVSRLANEFDARIAKLEKMPFSPAKEAELKKISVDLSKLVVAAVRKHAMKERIAKITKQVQEHVKAINAAEQKEVVNVVTEYFKENPDMSFVVAKVPISANPKALSFALTYAKKNLKDKSIYLLASDDTKVAHACLVSPEAMKKLTPQEWSQKVCHSIGGRSGGKGDTCQGVGDKPLSIDVAVEEAIEFFQGKLTI O13915 USB1_SCHPO ACT_SITE 109; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03040"; ACT_SITE 199; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03040" BINDING 109..111; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q9BQ65"; BINDING 195..201; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:Q9BQ65"; BINDING 197..201; /ligand="UMP"; /ligand_id="ChEBI:CHEBI:57865"; /evidence="ECO:0000250|UniProtKB:Q9BQ65" CATALYTIC ACTIVITY: Reaction=a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-uridine-RNA + uridine; Xref=Rhea:RHEA:46052, Rhea:RHEA-COMP:17384, Rhea:RHEA-COMP:17385, ChEBI:CHEBI:16704, ChEBI:CHEBI:85643, ChEBI:CHEBI:85644; Evidence={ECO:0000269|PubMed:26213367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46053; Evidence={ECO:0000305|PubMed:26213367}; SPAC23C11.10; CHAIN 1..265; /note="U6 snRNA phosphodiesterase 1"; /id="PRO_0000116673" MSLVCYESSSSGEDDDETISDNPRMLKVPKLQESFHELYKKKPKTFDSPEFHEGRIRGQKHIEGLWFVQTYLEVDLSKKVKKGIREFLNSQSRFQSLLCSEHNVPRRLHLSISENYRINYSTKNQLVHKWEQYTNNLNYRTLKFRLGKMCLLFNDEKTRMFLAFECKFSDENYKDLISHASDCMKEFTNRNLREDFLLHISFASSLTNEDEYQNWVSQDRESHFFKTMNEIINTKIQKDQFSESFIVDSLKLSIGHLIFTFPFCK O13916 HCN1_SCHPO MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000269|PubMed:20924356" SPAC23C11.12; HELIX 13..20; /evidence="ECO:0007829|PDB:2XPI" CHAIN 1..80; /note="Anaphase-promoting complex subunit hcn1"; /id="PRO_0000083923" MLRRNPTAIQITAEDVLAYDEEKLRQTLDSESTTEEALQKNEESTRLSPEKKKIIRERRIGITQIFDSSMHPSQGGAAQS O13918 ZHF1_SCHPO SPAC23C11.14; CHAIN 1..387; /note="Zinc homeostasis factor 1"; /id="PRO_0000206104" MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILGALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESVLPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGDALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHELHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS O13923 CORO_SCHPO MOD_RES 500; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 501; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 553; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C4.02; CHAIN 1..601; /note="Coronin-like protein crn1"; /id="PRO_0000050939" MSGRFVRASKYRHIFGQTCKKELCYDNIKLSNNAWDSNLLSVNPFYLSVNWNAGAGGALAVIPLNERGKLPDQVNLFRGHTAAVLDTDWNPFHDQVLASGGDDSKIMIWKVPEDYTVMEPYEDVHPIAELKGHSRKVGLVQYHPTAANVLASSSADNTIKLWDCEKGVAHVSLKMDVMCQSMSFNADGTRLVTTSRDKKVRVWDPRTDKPVSVGNGHAGAKNPRVVWLGSLDRFATTGFSKMSDRQIALWDPTNLSEPIGGFTTLDTGSGILMPFWDDGTKVIYLAGKGDGNIRYYEYENDVFHYLSEFKSVDPQRGIAFLPKRGVNVSENEVMRAYKSVNDSIIEPISFIVPRRSESFQSDIYPPAPSGKPSLTAEEWASGKDAQPDLLDMSTLYESKGTVEKAVSATVPSAGAQVQKHNEEKVETPKPEAQPVSKPKESAEEQKPSKEPEVKPTTPSASKVEEPSKKRDEDNHQKEETVTQPKREKTPVEKSFPKPASSPVTFSEDVKKEPSEEKKLEVSDEAPKAAPLAESKKVEEKEPFYVSKDKKDISAVNLADLNKRFEGFEKRYEEELAIRDWKIAQLEDKLAKLTEAIKEKCN O13930 SEC2_SCHPO MOD_RES 75; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C4.10; CHAIN 1..527; /note="Rab guanine nucleotide exchange factor sec2"; /id="PRO_0000097660" MPDVSNVRVKPNQHPYEKEVNGKLMSQEEILSQKLVAAIERQAALDDKYATEVHRNEALSERIRELEAKLSAKKSFDEELVKFHNLEEKLQLTETKCRNAESEKSRVENELEDLTSSLFEEANRMVANARKETVASEKRVNQLKKQLVDAETLLSSTQHQLTELKDVMHSMSDSHEQNNALHPPLSRTTSFVADNVSVGSFASSTSGLDILTGTSARESLDAKEISSDKHLNISGERPATFPNPTFIEGSDERRSASSLGHRTNNNQNQLIRFSTQIRSSSTSPPRSPLIISDSPSSSIIHNPHPTHPSASAMNYMNPCFLEFHAFFNYPMKFARSRSAYSTSANYSNTPPRNTVTPSTARSSTLSQNPSSSSNSIPLISRNLRDFSFFKRCLEEDIEPTLRLDHASGLSWLTRRSVFTAILESSLIINPLHSTSLLSSQPCSLCGFNRTQPLRQFEFRSRPDSTSHASCTYCVARLRSVCNFVAFLHQICKGVWSSCSLEKAWDECLKKREAMFLSRVGLAKELEG O13934 ATG15_SCHPO ACT_SITE 283; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037" CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; SPAC23C4.16c; CHAIN 1..424; /note="Putative lipase atg15"; /id="PRO_0000090370" CARBOHYD 187; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSQLLFLRRFFFLFCFIIRISCTGVFESVIKSSENVPDKVNVKLQHVFHYGLNEDSISYYRLDVAKKSVYAESESKLPLKMKKGYSVHLKDQSRDALTDYRYKSMKGIYSEANSPADLWEQEAIVIPDITDKETIYSLGKMSYNAYQKIPFDGDWLDLGPDWNITPPEGFGWEEDGLRGHVFSNDDNSTIIIAMKGTSIFGIGRGTSQKDRVNDNLLFSCCCARVSWAWSTVCGCYKNTYTCSQTCLEDEVQDDSRYYSASLDIFYSVKELYPDAQIWLTGHSLGGATAALMGLSFGIPTVTFEAPGDRMAARRLHLPMPPGLPDEESLVWHFGHNADPIYLGKCTGPTSLCWAGGYAMESTCHTGQECLYDVVKDKGWHLSITHHRMQTVLNDVIDAYEKLPDCSHTPNCVDCYLWEFPDDDS O13939 AP3B_SCHPO MOD_RES 638; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23H3.06; CHAIN 1..745; /note="AP-3 complex subunit beta"; /id="PRO_0000193756" MSNLSFFQTLSGLAENAKQIAKSSSLSFEENELSHSDLLRLLNSNSDAGKLEAINFILAQMMHGENMSLYFPDVVKLVASENPEIRRLVHIYLLQYAEFNPDLALLSVNTVQKTLYDKNPLTRSTAIRVMSSIRVPAINGIVLLAIQQCITDTADRVRQSAALAITKCYSLDPSYKSQLEEHIKTLLSDNSPIVVPAALFTFEVVCPEKLEIIHPYYHRICTLFPQMNDWDKVVALKTLVRYARLTLPEPSTPSTHSDLKELLESIKSCFFSLLPSTIIAGARAFYYLAPSNQMHLIVEPLLQLLLEKPIVRTTTLRYISQIVYKTPELFKNHIKSFFLIASDSDDTCLLKINILSRLLDAQNSSQILPELLYYINSHPNPSVASTAVKALGDFASANISMAPSCLNTLLLLLKSHNSLIVTEAASSLRLLIHNDPKEIYLQYLAATYETLEVPRAKSVTLWLISEHILIIPRLVPDVLRIAVKTFADETLEVKYQILELSVRLYVLSHSEEKQNDLESRDDVVSLLFNYVLSLIHFDMSYDLRDRARFYKELASTPSSEFTRRIVLESKGNSQKEIIASRDYCIGTASLCLNEDVMGYEPIPNWADVSDLPPDSVREGIKDVLPINPHTGNIYSNNSPGVKALSSDNFKRDFGDTNAINRPKFVGQQTLEEFYASETSESSEGEYETSTSESEDEETDDTSQEEDNEKNSTPDEDTENNNTSSISTKSIMDRPLTEPEPNYWQS O13944 OSH3_SCHPO MOD_RES 288; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 419; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 421; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23H4.01c; CHAIN 1..945; /note="Oxysterol-binding protein homolog C23H4.01c"; /id="PRO_0000100392" METVEIRSKSLLIQWLTVESNSLLSWQLHVKRKSIKFDIYHKKNDTSSLLDGSNKNTDRSILHTKRQHTHEAGIKKLSAAGLELFYQGERCMSEKPSEGSVYIENGGLYAFVFDNTFSKTKPKTVTFLLTAQPYNGPRIPNASVHGSPKQIISGTLLKKRRKKGQGYARRYFTLNMVEGTISYYANENSSVMRGKIPLSIAVISVAAETHEINVDSGVELWNLRAHTHQDWLRWCNALEKAKNSQTSSKLVVDERTQESSSNQLVSIYSRLRECLDIAQLYRTSRIKSASSHNFSVPEIRIQLPGDAKENKETRTSVEITAAENAQAAVTLRKVTRQLGSLLHELECFIQHHEYTKERTAQSSPSSRMSMDSNFEQHWYDAEDYESTTSQLNHYSESGAHAADATKSSVAHNEKVEDISDSDIPIMKTSSNSTSLDADRDSDTSSISDTSSNSSAPHEQLNATSLASTVDESSRSPPLPEVESNKENDIKRKQPFHDLMDSSSPDDSSFANAKSDEEVQKPSVSKNIADGAVISIPKPLTPKPSDSNSLYPLPHSKVGRRKNIPAITVPPPSILSILRKNIGKDISSIPAPVVSNEPCNLLQRCAEDLEYSNMLDKANECDDDIKIFYVAAFAVSNFSNMRHKERSVRKVFSPLLGETFELVREDRNYRFLAEKVCHRPLIIACHAESRNWIWNHSPKPIQKFWGKSVELNTLGPVTIKLACGTEFSFMKPACFLKNVAIGEKYVEPYDHMEIVDETTGDKAVIRFKSGGMFSGRSEDVLVTVIRSNGEEDPKCLQGKWTSHLDFVNTDEGNVIERIWEVGPLVDKPEDHCGMTVFAAQMNEITDLEKDKLPPTDTRLRPDQRYRENNDLDHAEPLKLELEQKQRERRKEMEEKDIKWEPRWFVPSVAGDDEDEDGSGPIWQLKKENNYWESRENSTWSSCPKLW O13952 NKP2_SCHPO SPAC23H4.11c; CHAIN 1..188; /note="Inner kinetochore subunit cnl2"; /id="PRO_0000351434" MNMEEQILNDYLLSQGRLQSIISLEQWRQLFPQRYREDPLIERLYEYCTQQRQKRLAKLRANIHLESQVIGKSRIDRMLATNVEKLQTVSHASTLHDVEEFYTSHSAKPLDISEINERLSEAVQSAYTKLNEEKERCTQLTLKMNSQIASLSDFQWSKEPNVDESIHLVESLIESLEKAAPSAIEELD O13955 VAM6_SCHPO SPAC23H4.14; CHAIN 1..905; /note="Vacuolar morphogenesis protein 6"; /id="PRO_0000372690" MHRAFSLYRVLELSKARVECVFELGGLVYVSNSNGDLDSYKIYNNEEEEAADFVMEHVDVYPNFTKKPITKVVSCATQDIFYALSDSQVYVYQISTFKKLFSFGAHCQNMCLYGDELIVLSSKKNLEIYEIQKNSKPNLTKTISLNDRPRSLAWVSPTMILVSLSNDFCAVNTETSRISSLNLAWQQSSSLGLGISYIGMSIKSNKLHITRISDDEVLLSKDSQGLLVNLKSLQVSRNPLRWPTVPQAVIYNSPYIITLHNQYIYIWNKETYAMIQQIGISNIYSTFSCHKNTFFTSNSYVWILTPEDFSNQIEALLNTENLNEAISVLSQITVSQFPKRDYYLRITKREKALRSFSSGDYDLAMRLFSEISESPSTVLGLFPGLLDNNYSDAISILSMAPSQNESIESNVLFPGNHSNSQTDLRNGDAVSTVANNKRLRSLSTYLTDSRRKANRFLSYDEEHYFLQKKNLFLNADGTLVAKEKLEKIAVQIDTTLFLIYMISSPALVGSLLRLPNRCETSVVETNLLSAKMYRELVEYYYGKSLHEAALDLLTKLCDEPTDTLSLKGKSNTTSKYEPILSYLEKLSPELDHLIFKYSRVPLSEDPQNSIVIFIDENSEASTISKGVVLKYLETISYKVSIIYLEKLLLDNKFNDTVFPTRLALLYLKRILELEETTDFKNQEVFKQTIEKLEDYLTNSKQYDANVVLQEINSQDEFLSTVSIILYRRLSRHQDALDVYLKILNDWEGALSYCNSVYSIDGETEPYYMLLAEISKNYKSGSLNILDFITKYSSRLDLNRVFPLLPKNISMKSYHSLFSSQFRQLFEELSNKETQSKLYQKRLEDLNEELTKVRSEKVVITREKTCLFCHKRLGKSVISIFPDGSVVHYGCAKKYVSSNHLPYEAY O13960 ECM33_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity). {ECO:0000250}.; PTM: Extensively N-glycosylated. {ECO:0000250}. SPAC1705.03c; PROPEP 399..421; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000417675" CHAIN 20..398; /note="Cell wall protein ecm33"; /id="PRO_0000014204" CARBOHYD 22; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 29; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 92; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 197; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 203; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 231; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 236; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 264; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 275; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 300; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 324; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" LIPID 398; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MLFKSFALTLLFAAARVQAASNCSSGPYNISAQGTLDELNSCTVLNGDLYISDAGNSGITTLTVNGIESVQGDVVVSDGQYLTSLSFPSLKNVSGAFNVNNMIRMNNLATPELTSVGSLNLAVLPNLQELQFNAGLSDSDSVVIDDTQLQAIDGISLDSVTTFQVTNNRYIQEITMEGLESAQNIQISANSKGVSVNFSKLSNVTTATFDGISNVFIGNLKSAAGNLYFSNTTLDNISVPYLTEIGQSFAVLYSPELTSLNFPNLTTVGGGFVINDTGLTSIDGFPVISEIGGGLVLLGNFSSIDMPDLSDVKGALTVETKATNFTCPWSNDDSVIKGDDFTCQGSVATISATSSYDLSSTVSATSGSATSATGSATTTSYSSDSSASSSSSSSHESSAASNGFTAGALVLGSLLVAALAM O13967 FKS2_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000250|UniProtKB:P38631}; SPAC24C9.07c; CHAIN 1..1894; /note="1,3-beta-glucan synthase component bgs2"; /id="PRO_0000121722" MSWHEQDYGFGTSSENSKINSDEFEDSMDVTEFNNPGEESTYPQANSWNDSNKTKDIAEYYDYSWSGQREANQQIPQPVPVQPRYPDEQNFSMNGETYPSEAYDYDYSGQEEAINAMNILQGNLERSNEYYSEGVPYSEEDLGAYAGGMTEDDQMYSNFNETGEFNLDIGSSKFSYLNAKNPYPAWIAENSIPITAENILEIFQELQAKFGFQYDSMLNMYDFFMVLLDSRSSRMDAENALKSLHADYIGGRNANYRKWYFSSSMDIDDSVGLQNCKFSSNGPKIKQAKKKQKRKSNKAETEGTNEPETSVQIDPLNVSMENWENEMKNLDCETQVRQLALYLLCWGEANNIRFCPECLCFIFKLANDFMQSEDYAKSEPIEDDCFYLDNVITPLYEFIRDQQFELLDGKLVRRERDHAQIIGYDDINQLFWYPEGIARIVTVDGTQLITLPKWERFHKLSEVDWKKAFYKTFYESRSWFHLVTNFNRIWVIHFTTYWYYTVFNSPTIIEKNFRQSVGPKPIPSCHWTSVSLGGAVATLLMLLATIFEWIHVPRKFPGSRPLLKRFLILILFFILNVAPTVFVFGFSTEEQQRTTGRLTVAIVHFIFSVFTFIYFSLVPLNNLFHRAYKSSSRTHLANRYFTADYARLQINDMCVSWGLWLLVFGAKFTESYFFLSLSFRDPILVLSTMKPYLCNITFLGSHLCIWQPKILLGIMYVTDLVLFFLDTYLWYILVNTVFSVARSFFLGISIWTPWRNIFARMPKRIYSKILCTPEVDSSYKPKVLVSQIWNSIIISLYREHLLAIEHVQRLIYHQVNSLDGDGSKTLKTPTFFVSQEDSSFNTEYFPAHSEAERRLSFFAQSLATPIPEPIPVDAMPTFTVLVPHYGEKILLSLKEIIREQDKLSRVTLLEYLKQLHANEWKCFVRDTKILAEEDALSNQDLNSQDESMKAEQLHKKFDDLPFYCIGFKNATPEYTLRTRIWASLRSQTLYRTVSGFMNYSRAIKLLYRVENPDVAQLFEGQMDVLEYELDRMASRKFKMCVSMQRYAKFTADEIENTEFILRAYPDLLIAYLDEDPPKEGETTPQLYAALIDGYSELDENKKRKPKYRIKLSGNPILGDGKSDNQNLSLPFYRGEYIQLIDANQDNYLEECLKIRSILAEFEAFDLKTNDPYAETNALYQNNPVAIMGAREYIFSENIGILGDVAAGKEQTFGTLFARTMAQIGGKLHYGHPDFLNAIYMTTRGGVSKAQKGLHVNEDIYAGMTALQRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQMVSREYYYLGTQLPFDRFLSFYYAHPGFHINNIFIMLSVQLFMVVLVNLGGMYHVVTVCDYDHDQKLTVPMRPEGCYQLNPVVNWLKRCIISIFIVFFISFVPLTVQELTERGAWRALTRLGKHFASFSPMFEVFACQTYAQSVIANLSFGGARYIGTGRGFATARLSFSLLFSRFAGPSIYLGSRTLLMLLFGTMTVWIPHLIYFWISTLAMCISPFIFNPHQFSWTDFFVDYREFIRWLSRGNSRSHINSWIGYCRLTRTRITGYKRRLLGVPVSKGVIDTSRAHFTNMFFTEIFIPLMLVPLTLVSYFFIDSQPGNPDPSKVTNPILRILILAFLPIIVAAVVSMTFAGMACMMGPLLDLCCKKFGAVLAALAHGITVFMFIIVFEVSWYLEAWCLAKTVLSMLCIIAIQRFFFKIIQVLFLTRELKHDGTNLAWWTGKWYSRGLGFHALSQPSRELICKMTELNFFAADFFLCHLLLFLMLPVLLIPFIDRWHSMMLFWLKPSKQIRPPIYSMRQNRLRKKIVQRYGTMFFLLLIAFLALIIIPLVVAKDLLANFEMDILRTYGLMQPRDTNWTENGTNWTTVNE O13974 OTU1_SCHPO ACT_SITE 143; /evidence="ECO:0000250|UniProtKB:Q96FW1"; ACT_SITE 146; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q5VVQ6"; ACT_SITE 247; /evidence="ECO:0000250|UniProtKB:Q5VVQ6"; ACT_SITE 323; /evidence="ECO:0000250|UniProtKB:Q96FW1" BINDING 246; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q5VVQ6" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q5VVQ6}; SPAC24C9.14; CHAIN 1..329; /note="Putative ubiquitin thioesterase otu1"; /id="PRO_0000300503" MSSLRLRLKYENQSAVETVEANATVGSFLDLVAAKFSLPRNSIALKFGFPPQDIPLVNSDVPLSTLVSSGQQILVLKNAATSFSTNEPAKPPIPNAATKPTFPPQTEISNPPAVSHQSKNTSQDPPYVSTPIGDIALRVMPDDNSCLFRALSKPLGFSPYELREIVANQVLSNPDIYSTAILGKPSIEYASWIRKETSWGGYIELSILSSHFGVEICSVDVKTGRVDSYNPQPATGQRTYIVYSGIHYDLAALAAVLWDTDVDVVLFDASDVTITPYVQQLASLLKNMHYYTDTASFSIRCTICGTGLVGEKDATAHALATGHTQFGEY O13979 MU105_SCHPO ACT_SITE 42; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q96AP4"; ACT_SITE 165; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q96AP4"; ACT_SITE 183; /evidence="ECO:0000250|UniProtKB:Q99K23" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:29476094}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.2 uM for Arg-Leu-Arg-Gly-Gly-AMC {ECO:0000269|PubMed:29476094}; Note=kcat is 7.2 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate. {ECO:0000269|PubMed:29476094}; SPAC25H1.04; STRAND 19..22; /evidence="ECO:0007829|PDB:7OIY"; STRAND 119..127; /evidence="ECO:0007829|PDB:7OIY"; STRAND 158..162; /evidence="ECO:0007829|PDB:7OIY"; STRAND 165..173; /evidence="ECO:0007829|PDB:7OIY"; STRAND 178..182; /evidence="ECO:0007829|PDB:7OIY"; STRAND 214..226; /evidence="ECO:0007829|PDB:7OIY"; STRAND 239..242; /evidence="ECO:0007829|PDB:7OIY" HELIX 4..14; /evidence="ECO:0007829|PDB:7OIY"; HELIX 42..57; /evidence="ECO:0007829|PDB:7OIY"; HELIX 59..65; /evidence="ECO:0007829|PDB:7OIY"; HELIX 73..85; /evidence="ECO:0007829|PDB:7OIY"; HELIX 90..95; /evidence="ECO:0007829|PDB:7OIY"; HELIX 107..116; /evidence="ECO:0007829|PDB:7OIY"; HELIX 131..146; /evidence="ECO:0007829|PDB:7OIY"; HELIX 197..204; /evidence="ECO:0007829|PDB:7OIY"; HELIX 208..210; /evidence="ECO:0007829|PDB:7OIY" TURN 34..36; /evidence="ECO:0007829|PDB:7OIY"; TURN 38..40; /evidence="ECO:0007829|PDB:7OIY"; TURN 174..177; /evidence="ECO:0007829|PDB:7OIY"; TURN 188..190; /evidence="ECO:0007829|PDB:7OIY" CHAIN 1..244; /note="Ubiquitin carboxyl-terminal hydrolase mug105"; /id="PRO_0000278504" MSKCLQQLKRQLQHFGIDGCSLADGDIDYFFTVTGIDRGWGCGWRNIQMLISWLQYTNPNWFKRNFSSGNYEINSLQSLLLSAWMKGIDAEGYAQLGDNLHGKWIGATEVYSLFTGLFVNVALVDFDFRSEASASNALFLYVKKHFESSNDTSNVSPCYLQFQGHSIIIIGFCSSLETLVVLDPDRYQSVQKKFVNIADFNHCYMRKKRSLKFSQFQLVHFKQNIFLNDFSSKLEVRSTRISDF O13985 YEG3_SCHPO MOD_RES 468; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 470; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 473; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26H5.03; STRAND 508..511; /evidence="ECO:0007829|PDB:2Z3F" CHAIN 1..512; /note="Uncharacterized WD repeat-containing protein C26H5.03"; /id="PRO_0000316555" MRAEVLQIRWHYDANDDHTPIYSVDFQKNSLNKFATCGGDSKIRIWQLITSESSTKVEYLSTLSRHTQAVNVVRFNPEGNILATAGDEGTIMLWVPTNTPITTLADDAEELALAKEYWKVKIVCRSMGSEIYDLCWSVDSNFLIAGAMDNSLRLYDAHTGQLLTQKFDHSHYVQGVCWDPLNQYIVSESSDRSICLYEIQEEKKNPKKFQLVLKSRICRIEYNVTKFELISVTKPLNNDESSGISEPIETSNNNESPVSKHEALSSTANIVKDGSLERTEPPNSLNSKISYSLYCNETLVSFFRRPAFSPDGLLLVTPAGRLRPHGQPNFEVPYTAYIYTRGSITKQPVACLNGFKKPVIAVRFSPIHYELNSFSNFSFTSVSFNLPYRMVFAVACQDAVYIYDTQTCKPFYRAVNLHYSNLTDIAWNDDGNVLLMTSIDGFCSVITFEPGELGVKSQHKISLPEKRSASPSSIDDSQDNTAGGPATTTLIPRKVESSKVSKKRIAPTPVYP O13992 SPO71_SCHPO SPAC26H5.11; CHAIN 1..965; /note="Forespore membrane adapter protein MUG56"; /id="PRO_0000278501" MNEEDTDFAWLHNNSAEHLRFLSHRIFIGPIPSNFIHSTSGFFNKRFQNYTKRQICYNVASPNEPPIDFSFLMHKSTDENPDTPSNLDSPSTQNVGSTNNTRASQSLLRRSSSFFRRRHRKNGTHASTDNNPFSESSTLQPQTAERTSQQAVRSAITETTNPSVSVQNSNSTSTSSAAMIIPHRDSQNSLEIAPLISPESQLSSLHPSSSRRHLISTPHVNRGTQFKRSSSCRNSRQPLLSGVDKHLTSNFTDANLIIKQSVVLARIESTFTVLPSDYNDSAAQRVPRKTISPWSQCLLVARQTDVENSIRLDFISKKLRKRLNGDVVHNLDVPHDKSYKSNYLFSVVLSPHQASWNIYNSFDNSMVLWCPYGKNKTLICLLNFQSSLLSFEWISIISRALLFSPRPSLLISVPAFHIHLRLNFPCFKDTTRPHTNETFVTTDDITQLSRTSTLSLSTASPRLVHDLVMKSWDISEDQFVESCLGVLEVNPEWSGIVKTWSKSHTLGLCWRMYDRLEWINSFSSLKYVGLLAAKDLYQLELRPKLHYPNHVTFRDGSKMDEPTPVEGYLIRLTSSTGRKTRYGRMFHKELYFAIFNNFLFAIQPDSVLPLSMLSKSLNLDDKLPFLSNNENDKYVYEFDPFKIANCRASGLNETIDSSVRESFLLLLQAERKRELDMLTIADSFLDLSRVESVCPVEDVEERNIFEITMTNGMKLVFQSYCERTRNLWINKITEVASYWKQRLFLDLQEYHDVRETNINILHIEQSIEPDVACYLNHWEVAGCVASTLIYHYCSMLGCRVIRMQGTLFKKKDALFEKCFAILIPGQLVFFQDATRTKFGKLCTKTHYRKRYSISLKNAFIYTGLSTMDEFARGPNDPQPHISRLPRCYEDGWQSFDRDDMLSFVIWSSGGVDYDLRPHHSVPDTAYGMAKDKLSKPKRFMFLARTRQERDVWAKRISKEINRGHS O13993 RPOM_SCHPO ACT_SITE 821; /evidence="ECO:0000250"; ACT_SITE 890; /evidence="ECO:0000250"; ACT_SITE 1061; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031, ECO:0000255|PROSITE-ProRule:PRU10032}; TRANSIT 1..30; /note="Mitochondrion" SPAC26H5.12; CHAIN 31..1154; /note="DNA-directed RNA polymerase, mitochondrial"; /id="PRO_0000031077" MLRRKIQTYLSRSHIRRGLCGLRFFQTQRLHTDYMPIEAYEPYKNELKSKIGKDFIIDLSYKSGTASLFEACVYNGDFLRSKQLLKSFIDHNKGDKILLPMINLYIREIIQRGSFELTDVLSNAKELLQQARLNGDSLTYALLCQASLNPTQRQLGLPVLHELIHNWRSANGKVIDILMHESVFSPEEVKLIMDQLNIPINNFTPSQLQLLGITNSTIVGESENGKDQNGDSSLKEKQPDVETTVTKSANLNALRSSLSSLLTESIDLPIDEVSLEFGNQGDTFNLARQKLLEKSAILSAAEVWKSEHESVLNRGNLQVPKNVSSLFYSWYVQLEQLFKEEISLIDDLALNESLDKKNDRLIYGPFLKLLSSKKLAALTIMEVAQLSTNPRYDRGARVTTLLGGLGRSFEREFLSEQIQRQEKNKSYKDKKRLKELFNDPRKFRQAVKNLRLSNTRDNIVLNPSVDSWPSAIVMKVGSVALCLLLSVAKIEVTAKDLSTGGILKQEVAAFVHTYQYSNGRKVGMIVPHVEFYKLLSRDIEKPHLHPQLLPMLVTPKPWTSWIDGGYYYSRQPLVRLKGALEQVDYLMKASENGQLDELFKAVSSLGKVSWRINQRLFNVLIRIWNSGEKFLSIPPREVKCDMPPYPKNSINPRDKVIWHTRRKELAALKTGAHSQRCDFNYKLEIARAFLNEKFYFPHSLDFRGRAYPLSSHLHHVSNDVCRGLLEFSTGKPLGPKGLNWLKVHLANLFGISKKDFATRQAFVDDNMQEVFDSADRPLDGNKWWSKADDPFQALAACFEIAEAVRSGDHESYISHIPIQQDGTCNGLQHYAALGGDIEGAKQVNLWPSDHPSDVYEAVAEIVRGFLKKDAEAGDEMANFLKDKVTRSVVKPTVMTNVYGVTYVGARKQISEKLENIDGMEKLKVADYANYLTKKVFEALRSLFTQAHEIQDWLSACCNLITHSLPADYIKEGIKDELTPVVWTTLLNLPIVQPYRNYKSRQIRTNLQTVFIEERDRTATVQPHKQATAFPPNFIHSLDATHMFMTCLKCSEQNINFAAVHDSYWTHACDVDQMNSLLREAFVLLHSNNIMERLKQEFEERYKGFLVSKKAIKANDEDLKAKFGNKSYIPLEFPPLPARGALDLKKVLESKYFFS O14001 PVG2_SCHPO SPAC27E2.07; CHAIN 1..389; /note="Pyruvylated Gal-beta-1,3-epitope synthesis protein 2"; /id="PRO_0000076295" MTKLWVNFFSQKLLRLLIPSIIVVFAFAALFAIYSPIQLGGINFYKRTNLFTVEELGEKELELSKTVTIDIYRKAMCMDDLEQSRKCTTFGLDPPISAHLFYTYNRDTGMNRVARQWNRRIPRVFHTIKGSNFIELSQFTAFEVELRVSHPNWAFVSWSHDDLNELVDKSYHNLHNAWSQLSREAKDQWGFLLGLYEYGGVWMSRSLQLKKNIDKFVYAAELSVKQFTENITSSTVEEFQPIFMAPKSLQYDFMIATPKHPFVLSLINELCKSEVLLKILSKRPYHGLDAAEALFAENRESITIREQEFFVNTYIDDGKVFVKNNPHIIFIPTEAFASTWDFLPSEESSEMCFADSPLFDPDYCISHSSKPDGNELAIYWSNSFDLITA O14002 MAK2_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; MOD_RES 1763; /note="Phosphohistidine; by autocatalysis"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"; MOD_RES 2232; /note="4-aspartylphosphate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00169" SPAC27E2.09; CHAIN 1..2310; /note="Peroxide stress-activated histidine kinase mak2"; /id="PRO_0000081409" MSLYKSLDVAIDYAISQLGEFQFQPIRTQSNPSSLLSACLVRAVHVETRRKVIFKFSQQTFKLENEYFLLRQLSSHPNGRNYAIAPAYILLLNETLGALIYDDPGPNILDEWLGNPNPLDLKLFLKFALGVSYVLCFLHEKKIVHGEIRLDTFHYDLNAPIHAKLLTIGSSVSPIRFTLSSLNWKRLYQVQNICHKLQFFSPEQIGNVGRPLDSRSDIYSLGILFYVILTKQYPWGGQSMRIVQSIHMRQFPSVLPRRPDAFPALDQLIQKMTAKSMNSRISSATDLCYTIVELMQEFSTITSSPLLDQKLLSINKPQQEKLKFPKLLLTNSSDYVRIFHELVAFSSKRDLLTSAKRVDKLPKQHLFKYRPVDNEATYCQVVTVTGEKGSGKSNLLNAVADEARKFGYFAMSSFKGHHFSPYSAIFKCVSLIMQQTLREEKQLVTDYFTSLWEFLGFQLIYMGELFEYVPELNSLLSPKYNLHCKRENYFKLKKRDPQQFRSASGRLGFMVCLLEILSFTSRVRPVIIILDELHLADHPSLSLIIGMISHRLPILLILAWDEPVMFKDFSKCLHEAPYAMVTDIRMNLFDRKNITEFLDSTLESPTQALGPLVLLMQKLSKGNPLVLKSLLLIAFANNGFAFHPKSSSWTYDLPVINRSFEALSSYDIPPLLASLLDALLPARCIEFLLWAALLVEPFPFELLRLITTSMHLFIPKEEILDFPLNVLQFDNDNESCQFSETFFREGILSKISLRRAESMHAQIAKELITGTAKEFYDIRTVHHILKGLGVIKKFDNTKPYILALKESADALMQFGSYEYATELLKSCLFLLPRNFWNSKLYTRKDLISIHISLAMCYWWSKDHENAIKVLKNPKLSSSNVYDYLPAFRLLTKIEYYKYQSLRSIDKAQELLSNLGLKLKEPTDDVLREFYDRLSTKFLECDFLVKQSEPLDRKRIDAISVILSECGFVLFNFSQPYYYYFSFLLAEMYLRYGNPSLRYSVMFLASYCFVTRRKPEFLLRISQVDSDLFVIKDRSAVAHAELIYWGLKRELCSTETGSAVTLESILLQCVMFGDKIYGAYCLACLMAQRVFRGDHIHQLLLDQENSETLLLLWDCEPPFTYYLMLIRNSLLALFGLTNNDDPNNILTTKQRTQKDLHDKLTSKKVPCTFCCWYYAGIIFLNTLFHHYEYVMSIAQEVRKLVDGKLYERYYLITRSFIGVAALQLLFYKKNISEFEREKVEDVAHWAQSSLSEMAKCFHAELYKLWVCLLEGLRQRNLGNYMEALRLFEKVTSMGASVFSPIEFPFVLELIGEFYYGRGHKFLAKSYITRALSCLKNIGCYGVENKLRSRYSDLISDVESRGTTVVSIATTTGDYAEKLKLLRNQDINDFSLGLASYSDIFDKPLVTLPVKKSSAVDESENDFYDRNDEESFDIVSLVSVIKCGQLLSSKLRLGPLLTTVIKLVIEYSQAKHAAIILKDASNYTLAAHGNVEKAESFEPPVILSQSDVKIPDSLLSEVFDHCRIVSLYTVSASQDAELLRWLQEEHDMDFFAIIPLQFKESVIGALYLCLSRRAIRTGNVTFLKLLSQQIAISVSNALLFQSLRRTITDNVTLIELQRLSYQRYKAIEEKCITLLDSLPCIVWTLDSDIGEIEYTNASKRNYFGVPEDCHDSLSWKTFIHPDHHHQFQEKLLNLKTLELGDIELLLRMEDGNYHWHLCRGLSFKEDANAKKWIVVCIDINDEKEAREAAMHAVNLKTNFLANMSHELRTPFSSFYGMLSLLSDTKLNEEQYDIVSTAKQSCTSLVQIIDDLLNFSELKSGKMKLEPDKVFDVEENIADCIELVYPSLSSKPVQISYDIYPNVPALLAGDSAKLRQVITNLLGNSVKFTTEGHILLRCMAIDEEINAEENQCKLRFEIEDTGIGLKEEQLKLLFNPFTQVDGSTTRIYGGSGLGLSICLQICKIMDGDIGVQSVYGEGSTFWFHVQLRNVTSKLSQKHFEESHERFANIRQSLKNAKILVVKSFTTSRSIFRSLFSLAVVDTTTIYSDIEQQLIDSLDKRQPYDFLCIEAASGQTEQIITQILSNQKLNKVLLIVLLPSIQRTKVRSDGDPFITSLNKNQSRIFCFREPIRISKLLQNFPALLSKWSTPTKLVEPSQFRASPRKVDQAVVLSSEEKEILQKKYALIAEDNLIARKLLTKQLSNLGFQVHAAVDGVELVKMYEAKQFGFYSVIFADYHMPIRDGAEAVMDIRAYERENNCSTPIPVIALTADIQKSAKQRCLEVGMNFYLTKPFTQKQLVNAVREFVLLEKSAR O14007 CBF5_SCHPO ACT_SITE 100; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P60340" CATALYTIC ACTIVITY: Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA; Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P33322}; CATALYTIC ACTIVITY: Reaction=uridine in snRNA = pseudouridine in snRNA; Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P33322}; CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P33322}; SPAC29A4.04c; CHAIN 1..474; /note="H/ACA ribonucleoprotein complex subunit cbf5"; /id="PRO_0000121981" MTDTHPGVDFMIKPEATSASKIDTAEWPLLLKNFDKLLVRTGHYTPIPCGNNPLKRPIAEYVSSGVINLDKPANPSSHEVVAWVKKILRVEKTGHSGTLDPKVTGCLIICNDRATRLVKSQQSAGKEYVCVLRLHDSVEGERNVASAIETLTGALFQRPPLISAVKRQLRIRSIYESKLIEFDNERNLAVFWASCEAGTYMRTLCVHLGLLLGVGGHMQELRRVRSGCLSENDDIVTMHDVLDAQWIYDNTRDESYLRRVIRPLESLLVGYKRIVVKDSAVNAICYGAKLMIPGLLRYEAGIEVNEEIVLITTKGEAIAVGIAQMSTVELSTCDHGVVAKVKRCIMERDVYPRRWGLGPQSMKKKTLKKEGKLDKYGRPNENTPADWSKSYIDYSDPNAEVAKPAPVVAPAAPTVEAEVNGVEDSKKRKSVESSEKDEDEAAKKEEKRRKKEAKKEKKEKKEKKEKKEKKKKSE O14010 MED22_SCHPO SPAC29A4.07; HELIX 6..38; /evidence="ECO:0007829|PDB:4H63"; HELIX 46..83; /evidence="ECO:0007829|PDB:4H63"; HELIX 100..111; /evidence="ECO:0007829|PDB:4H63" TURN 112..114; /evidence="ECO:0007829|PDB:4H63" CHAIN 1..136; /note="Mediator of RNA polymerase II transcription subunit 22"; /id="PRO_0000096378" MSSDSFQRQLVQRTNTLNSSIDNATLTILSRFQDILDIAINEGKDKYTVAPEVYQIECHTVSMVRAVEQLLDVSRQIKSYWLTNSLSTSFPTVDYSEPDLEKVKRTLTKLQNHLLEVSLIEPEASETTEAPTVSDT O14014 RGA3_SCHPO SPAC29A4.11; CHAIN 1..969; /note="Probable Rho-type GTPase-activating protein 3"; /id="PRO_0000075901" MIFRKSISKSPSSKGSTVCFRCGQAFQRRETPISFGGHMWHKDCFCCTKCDKGLEHSDQMLVQTSDGRPVCSSCAHTCTACRMRIKDYALMSGYDSYHRECFRCHDCRKQIIDSNFKRDNRTIFCNDCKQVRHPSRSSDESADYHNFEVDVTIKPTETKSSVESNKSLSIEIMSPQKPPLSPFGGSRDRLVSETPTNMSQAEGGNVPNDGQDSNLASNSADSLLPSAKNRSFSSFTSFESPMKYDDSFFPISPSISPLQKVNKQQQIESPTATFPLSKNTWKNRFHTFHKQSFTPVNDSSSSDSLKPTINEEALDDFAGSASPYKTMSLTDRAEPIVMNGHMRSLHNATSPFRPFSPSYRSSDTHSPRTRSPNVQTHKKTSSQPSDLSSFAQLLSPPQVLSPKPNGGGHKSFRHSHSLSETSQQTLVPSLGSNGEYHLPTNDHSSTPAQSERDSDVEELREQLENLTALTKKLSERLSSSTFDNSKFIRTEDKDTVRSAKLEICEKFFSFADVTDDPTLKDPKHQDLVAAANAYMAMLRESYGTEINNLLERRNELLDDYNNVQKILNESLEASVHLNTKNLELADLNNNLVKQIQHRVPPENQSNLEHTITTSSKNTTSSINPLTAVSSNSGQSSGRPGPLSPNLNVTTRIDIKGKKGSMHLQPRDVNRKVPFKSMHTKSKSADPVVGNEDRTQCDHVFHVNAIFKPSRCYICSESVWGSELRCFHCSISCHSRCLKRLFAESEHEKTMSETVSENSKWMPEMPTRMPPPGPSPTMFGRSLENQLKIEGSVLPQVIAMCVSCVDAHGLEVEGIYRISGSASQVRVLVDEFENGSIRMEHLTSDLFACTSVLKTYLHRLPEPVIPGTQYEELLEAEKIEKEEEKIERVVEVMKTLHPAHLSVFRFLIAHLGRVCKHAEKNLMNSKNVSTVFAPTLMRDKVNRFDLQHATKKSTALQFMLDNVDKILHNL O14027 PDX1_SCHPO ACT_SITE 83; /note="Schiff-base intermediate with D-ribose 5-phosphate"; /evidence="ECO:0000250|UniProtKB:O59080" BINDING 26; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250|UniProtKB:O59080"; BINDING 155; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250|UniProtKB:O59080"; BINDING 167; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250|UniProtKB:Q03148"; BINDING 216; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250|UniProtKB:O59080"; BINDING 237..238; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250|UniProtKB:O59080" CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6; Evidence={ECO:0000250|UniProtKB:Q03148}; MOD_RES 178; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 180; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 283; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29B12.04; CHAIN 1..296; /note="Probable pyridoxal 5'-phosphate synthase subunit PDX1"; /id="PRO_0000109364" MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW O14029 SEC16_SCHPO MOD_RES 790; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29B12.07; CHAIN 1..1995; /note="COPII coat assembly protein sec16"; /id="PRO_0000076312" MDIESDHEPKESSVDLEGRHDSIRKSFEADDIDVTDENTIFSTSRKEQSTIEPMDSFVENNIANSSSQQSVSEIDIQLPSSEPKEGVKEESNLIESNSLDNVQEINPQNTIGDKSAHTEEESSNDNLVKITAGTIISDIMDEPVVDEDDKLSEEDLSKEDLETTLKGDENYSSSQKEIYDNDETIPKPPSPEVEKIETSTSVENAYITNSQYNDTLDMEDQTSDLITTFEHENEDHEVHEVPSIHGMEGTFETVNLTSEAGNEKEFNNDSVVLNTTPKEMQISSLDAVDKLEDKPVSNDNIKANIESSTTVDRASSQLESENNESTFFVHNQNSSGQHQTLDFVASKPVTDTPELSKENTLVSSENLNDPKPNLPETEVDFGEPLEVEAPSFVVQNNSAVQPTTQKTSEDSTDLHTNEIPNVAQPPSSFEKENNKDTSKLENPDISSSPLSPTEDLFPNDPEEENLFSAALGLNSNTGSQPSETQSKPSIDPSESITVTDNQDSLLFSQLTNNALQAENATKVSENTINDEELIDDSEFTSLMSNFLESSTVQTNKYLPKSSASPPANAPIVSSDVHKNENAGTARRAPQSGAFVASKAKYSSPYDLPEEIVQVAQQKRSVSQNYNRQYSFQPRPATPSNPPRSLPPPSGQVNAPMSQTPNPISFAYQHGTPLATPTMRANSFNSYPASSAEPIRRPATTTVGHTPNLYSPKTNTYNSRHMAYEMTKSHINVISPGPSLQVNAPYTPTSGELGNKVSNPTKEFVSTSSYAPAANTRNAIIREPGILSPLSPRVQPVLSRRESIISMGSSASSYVPLEIAPRPMSSLEHTMNSAMSPGNLQRTANLYKPMTTPNAYNIKNSNQRETKYPYQPQAINYSEVTQPGSSSLPTSGEEANIIRSPGFTPLAAQKDATIYTPSHAQATLYGNMDNNDRDNEGIHDILQSDMEPVLPPHNSAYHANAPVSSHSEGLNNRLPISPLPPQLHKTGTPSHQHGFDTAETTAKQYAPSIPPNFNPNVSIDTMTEGVALPSATLDSDKSSLHKRSAELSRNNSPRPDFLPLPNQPLLHSNLHSPVSPVVDSNEDSRLKFLSTQRPAFSFGPCGTIVMAFSTPSGLYTTSGKGTKFIAGPIKIEKLGDVLTDEYRHLKEFKGPYLASNGKVDKHGKAEAIEWLSKYIDRLNQSLEYDDKNITLKDKLLLLQCLKMLLEVSDRKLIVEKLRPILLPSFEIPEPCNTATSVQELINPEINQDDSPIVASRYCTTSFLHRFYEYLLSGNKDEALTYALQQKQWPYAIIVAHSIDAKTFQGVVRTFCKSEVKESMLRSGVGVNLQLSLQLMSDAHASSMSEFSSSTSLLNLADQSQASNALVAWKELLYNIIANHYSDQKEALRVLGTLLLQENRVYAAHLVYILSLSPDVCSNKSNSLFELVGLSKHNLYPSHDDLFDVTQLTEVLELVFNVYSEKTPVFFTHLVPYRLYEAEVLAEAGEVSAARKYCELIGNYLNRVAKKSNNVDPGFVLRVRDLTQQILENSAGSEDISSSWLGRTVSRPRLDTVLSSLGSKFSKFVAGDPNFDVMRPATVGPGPFGKVASQKNLTVQTNTNNAAMESFYSDRPTSSGPSYQNRTPLTGQESMNMGVYSPYRRSTEIAENMSMDGNAYPYTPASQENPYTPRHSQEDNASVLSQQPLTFYSNVADNSYMPVSASQEPKMGMGTAFNMPTNEVHGVGAEMASPYQPLQPASAHLPNLQPTLAPINQNAYVPSNIAPAMGAMQSAPSAEAVAAPSESLNLNKDRSQQAKQAAAQNVADLVRQEEEKEKQKQKAKKNAESGKKGGAKGWFSKLLRRDESKDQPTVYKAKLGEKSHLHYDKELKRWVNDDGSDLSNQAAPPPPPPMALPKAGPPSAAPTSALPPAGPPAGATAISGNPGMPAPVPLTGKETAVPLSSMPNAPPSVASNAKLPPASNNRKVDPLEDILQAMPPPTTRKARGKTSKRYVDVMRNS O14044 PNO1_SCHPO MOD_RES 52; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2C4.11c; CHAIN 1..241; /note="Pre-rRNA-processing protein pno1"; /id="PRO_0000278359" MLAPTAAVNVTNEGENDNVMIDTTRGEIEFSDSAVNGTMDIEGAPKFAPAKTSAEKKRGAKPQMRRVPIPPHRMTPLRNVWPKLYPPLVEHLLLQVRMNTKSRSVELRESKATKDPGALQKGMDFVQAFALGFDIDDAIALLRLDDLYIDTFEIKDVKTLQGDHLSRAIGRIAGQGGKTKFAIENASRTRIVLADSKIHILGGFTNIRIAKDAVVSLILGSPPGKVYANLRNAAARAKERI O14047 PPK11_SCHPO ACT_SITE 127; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" BINDING 12..20; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 35; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC2C4.14c; CHAIN 1..312; /note="Serine/threonine-protein kinase ppk11"; /id="PRO_0000256817" MEKHQYRDLQLIGQGSFGSVFRAQDVESSKIVALKVVDLDATKDQIETLTQEINFLIDLNSVHITKYYASFVDGFRLWITMEYCDGGSCLDLLKLSGTFSERVIAEVMRQVLEALVYLHGQGKMHRDIKAANILTMKDGLVKLADFGVSGQLESLRDKNDDFVGTPFWMAPEVVKQTGYNYKADIWSLGITAYELATGEPPYSGIHPMKVLLLIPKHSPPSLERSKFSRAFCDFVSNCLKKNPKDRATAEYLSKHKFIKKYCPNTSVKEVVASYAKWKESELLPEATPYNSTMGNSANTIDEVVWDFGTVRR O14084 IMT1_SCHPO SPAC2F3.01; CHAIN 1..319; /note="Inositol phosphoceramide mannosyltransferase 1"; /id="PRO_0000014199" CARBOHYD 115; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 198; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGRKCRKLLLKGIPICGVILLILWGYSLYNTLRFMVPGKATEPFTLSLSDVSDDTSAPGEMEKIPRVIHQLWKDENIPERWSNTVNSCRRQHPDENGWQFILWTDEKIMSFMNENYSWFMPVFHSYPYNIQKFDAARYFILYHYGGVYMDLDIGCKKPMDPLLSKATFILPSTEPIGYSNDWFAATPKHPFLYQAIHNLSKFNHRYFTKYPTVFLSAGPLFLSYQFCKYLLTPHEPVRVLPALLYGNGPNSFFSHVTGDSWHGTDAKVFIWIDRNSKSVLFFAFLAAFAILFLCLRVVFKRRRKRGIAASHSQIQELYP O14091 SUT1_SCHPO SPAC2F3.08; CHAIN 1..553; /note="General alpha-glucoside permease"; /id="PRO_0000122532" MSVDENQLENGQLLSSENEASSPFKESIPSRSSLYLIALTVSLLGVQLTWSVELGYGTPYLFSLGLRKEWTSIIWIAGPLTGILIQPIAGILSDRVNSRIGRRRPFMLCASLLGTFSLFLMGWAPDICLFIFSNEVLMKRVTIVLATISIYLLDVAVNVVMASTRSLIVDSVRSDQQHEANSWAGRMIGVGNVLGYLLGYLPLYRIFSFLNFTQLQVFCVLASISLVLTVTITTIFVSERRFPPVEHEKSVAGEIFEFFTTMRQSITALPFTLKRICFVQFFAYFGWFPFLFYITTYVGILYLRHAPKGHEEDWDMATRQGSFALLLFAIISLAANTALPLLLEDTEDDEEDESSDASNNEYNIQERNDLGNIRTGTNTPRLGNLSETTSFRSENEPSRRRLLPSSRSIMTTISSKVQIKGLTLPILWLSSHVLFGVCMLSTIFLQTSWQAQAMVAICGLSWACTLWIPYSLFSSEIGKLGLRESSGKMIGVHNVFISAPQVLSTIIATIVFIQSEGSHRDIADNSIAWVLRIGGISAFLAAYQCRHLLPINF O14104 LYS12_SCHPO BINDING 79..81; /ligand="NADH"; /ligand_id="ChEBI:CHEBI:57945"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 81; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 97; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 107; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 126; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 133; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 196; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 198; /ligand="(2R,3S)-homoisocitrate"; /ligand_id="ChEBI:CHEBI:15404"; /ligand_note="ligand shared between homodimeric partners"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 198; /ligand="NADH"; /ligand_id="ChEBI:CHEBI:57945"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 232; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 256; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 260; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 289..293; /ligand="NADH"; /ligand_id="ChEBI:CHEBI:57945"; /evidence="ECO:0000250|UniProtKB:Q72IW9"; BINDING 301; /ligand="NADH"; /ligand_id="ChEBI:CHEBI:57945"; /evidence="ECO:0000250|UniProtKB:Q72IW9" CATALYTIC ACTIVITY: Reaction=(2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH; Xref=Rhea:RHEA:11900, ChEBI:CHEBI:15404, ChEBI:CHEBI:16526, ChEBI:CHEBI:57499, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.87; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40495}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P40495}; MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 91; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31G5.04; STRAND 6..15; /evidence="ECO:0007829|PDB:3TY4"; STRAND 39..44; /evidence="ECO:0007829|PDB:3TY4"; STRAND 72..78; /evidence="ECO:0007829|PDB:3TY4"; STRAND 104..110; /evidence="ECO:0007829|PDB:3TY4"; STRAND 116..118; /evidence="ECO:0007829|PDB:3TY4"; STRAND 121..127; /evidence="ECO:0007829|PDB:3TY4"; STRAND 137..141; /evidence="ECO:0007829|PDB:3TY4"; STRAND 148..156; /evidence="ECO:0007829|PDB:3TY4"; STRAND 190..195; /evidence="ECO:0007829|PDB:3TY4"; STRAND 224..230; /evidence="ECO:0007829|PDB:3TY4"; STRAND 246..250; /evidence="ECO:0007829|PDB:3TY4"; STRAND 275..277; /evidence="ECO:0007829|PDB:3TY4"; STRAND 282..284; /evidence="ECO:0007829|PDB:3TY4" HELIX 18..30; /evidence="ECO:0007829|PDB:3TY4"; HELIX 34..36; /evidence="ECO:0007829|PDB:3TY4"; HELIX 49..55; /evidence="ECO:0007829|PDB:3TY4"; HELIX 61..70; /evidence="ECO:0007829|PDB:3TY4"; HELIX 92..99; /evidence="ECO:0007829|PDB:3TY4"; HELIX 132..134; /evidence="ECO:0007829|PDB:3TY4"; HELIX 157..179; /evidence="ECO:0007829|PDB:3TY4"; HELIX 203..214; /evidence="ECO:0007829|PDB:3TY4"; HELIX 215..217; /evidence="ECO:0007829|PDB:3TY4"; HELIX 219..221; /evidence="ECO:0007829|PDB:3TY4"; HELIX 231..240; /evidence="ECO:0007829|PDB:3TY4"; HELIX 242..244; /evidence="ECO:0007829|PDB:3TY4"; HELIX 252..263; /evidence="ECO:0007829|PDB:3TY4"; HELIX 264..266; /evidence="ECO:0007829|PDB:3TY4"; HELIX 269..271; /evidence="ECO:0007829|PDB:3TY4"; HELIX 303..315; /evidence="ECO:0007829|PDB:3TY4"; HELIX 319..335; /evidence="ECO:0007829|PDB:3TY4"; HELIX 341..343; /evidence="ECO:0007829|PDB:3TY4"; HELIX 349..359; /evidence="ECO:0007829|PDB:3TY4" TURN 197..199; /evidence="ECO:0007829|PDB:3TY4"; TURN 292..296; /evidence="ECO:0007829|PDB:3TY4" CHAIN 1..362; /note="Homoisocitrate dehydrogenase"; /id="PRO_0000310374" MSATRRIVLGLIPADGIGKEVVPAARRLMENLPAKHKLKFDFIDLDAGWGTFERTGKALPERTVERLKTECNAALFGAVQSPTHKVAGYSSPIVALRKKMGLYANVRPVKSLDGAKGKPVDLVIVRENTECLYVKEERMVQNTPGKRVAEAIRRISEEASTKIGKMAFEIAKSRQKIRESGTYSIHKKPLVTIIHKSNVMSVTDGLFRESCRHAQSLDPSYASINVDEQIVDSMVYRLFREPECFDVVVAPNLYGDILSDGAASLIGSLGLVPSANVGDNFVMSEPVHGSAPDIAGRGIANPVATFRSVALMLEFMGHQDAAADIYTAVDKVLTEGKVLTPDLGGKSGTNEITDAVLANIHN O14107 DNI1_SCHPO SIGNAL 1..32; /evidence="ECO:0000255" SPAC31G5.07; CHAIN 33..234; /note="Cell fusion protein dni1"; /id="PRO_0000352825" MLFLHSVVQGTGTLCTLAAWILLALVMTGCQSSTTSKFQLFSLATNVAQINVGYFNMCVLSANATLICKPQFTGCPGLTSISLTDVRSKFLINEVHPWMIVFSFCVCGVSFLMGVVSSLPLIGRLEFLRNIRISLSFFSFFSILVTALFAHVAVSSFVMAVGNGTQNRVTASLGKKAMIFLWCSMGLVTLTGITDSIILLVTSRTKKIRKTILEKSKVLTPSSSFSSKSSTTKY O14115 TGL4_SCHPO ACT_SITE 284; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"; ACT_SITE 429; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P36165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P36165}; SPAC1786.01c; CHAIN 1..630; /note="Triacylglycerol lipase ptl2"; /id="PRO_0000116829" MSIPEESEINKDYTVQEDLDEFAKYTCVYKKRHDEKIEYITAQHDWNPVYEAVVPRKSKPGKDEKREGFMYPILRWPLMFTAFLCLTFVAFLYLLDRLYINCYEYFIVWRGEARRLRKLLQEAKTYEEWKERARALDKYFGNDEWKLDPVYDYYDYTLVQAVYSSLVKHREQKDWNALKSVLDVCVRSNFGGIDSSMLYSRTYSGTKKLVEDYVNELKVCLETVIDQRLYTAQERSKMFEYFSHNYGRTALCLSGGASFAIYHTGVLRALLNQDLIPNVITGTSGGGLLAALVCTRTNEELKQLLVPELASKYQSDIGNWLDATKRYFRTGARFDEILWAKTCMYFTRGSLTFAEAYKRTGRILNISVIPSDVHSPPKLINYLTSPDTVIWSAVIASCAVPGILNPIPLMTRSQSHRLIPHNFGNRFKDGSLRTDIPLSELRTQFNVHFSIVSQTNPHVQVFFFSPRGTVGRPVSHRKGRGWRGGYVGSAIEQFLKYDMIKWLHVIRSLELLPRPLGTDWSSVFLQKFDGTITIWPKTKFQDFYYILSPPSVERLGYMIDAGQAATFPKLDFIAARMTIEKLIEKGRMMDKPSKLGRSIDGTIGTSMSRGDIEISQESASISPEDIDIVN O14132 PIT1_SCHPO ACT_SITE 161; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 42..50; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 66; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 200; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 469; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3C7.06c; CHAIN 1..650; /note="Sporulation protein kinase pit1"; /id="PRO_0000086538" MKKYLWGTPTTNTVFTGKQPKYTKEVRKCISIDEVYNVVRKVGDGTFGSVYLATTKTPSKEVVAIKSMKKKLAKVSDATRLREVHSLLRLSENENIVNIFDLYIDQFRCLHIVMEFLDCNLYQLISTRKNDPLTLEQVQDIMRQIFKGLNHIHTNGFFHRDMKPENILISSNSDSSSFNVKIADFGLAREINSRPPYTEYVSTRWYRAPELLLRDSYYSFPVDIYAAGCMAFEIATLQPIFPGNDDFDQLYKMCEILGSPDEQSQNTGDKGGGIWDRAELLANKLGISLPKMAPLDFGDLFSPPWNLAFASMLSQLLKWDPAKRPTAEMCLDLEFCRVSAPADAVASKEEVNKNTDFRVSISYFPSSSSIPDECNTEEESRINPSTSKFLKQLNKGFNGFTKPFRKSRKQSKNRKNKSSVATQFSEESEDIADSITSSTFFPVLPQIRPSTPLNLKLRNFIISSSEDSTSPKAKEFDRPLPSTEFLVAINKSQEALLNNSPNSKSGSTQLSASTCLSDLISPQLSILSHEDKRENQSVNSESSKYSPRSSNHSPTLHSKDLHRDMATVNNYAKSPPSFHATQDLLRKTLAYTNSSGTSTVLSNDSSAISSTFLDRDFPDFGITSLAGSLTLPDSKIIDRSKTHVSTQLLP O14134 ELF1_SCHPO BINDING 477..484; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 726..733; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" MOD_RES 733; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1041; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1053; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3C7.08c; CHAIN 1..1057; /note="mRNA export factor elf1"; /id="PRO_0000093460" MTSSVLIQGYEEDDVLKLLQELLDAETSQSCADVGKKIAQLFSNDNPLVTLKTTGFLDGLERAARNKKSGFHREAAMIGFATVIKNLGTPSEVVFLPYLPTILDSFSDRGEVVRQAAKMAAQALLDCLPAGAVETRLIPSLISYLDDSSIKWPSKVAALQLLGSLASSSPKAVADYMAALIPCIKERMHDTKPEISRAAITCMLNLCSVVENNDIIPHIPKLVDCMAHPETLEACIKDLSATTFVATVESVALAVLVPILKRALAQRSQSMLRLTVIITDNLCKLVPDPAEASDFLPELIPDVERIAQTAAMPEVRALASHALTTLNKAAAAQAAKAANNSEKQALDSACKELREAVLKNTSVPHELANSIIDYVCDALAALYKSNNFDKDKWTSQLGVLYLSPLVGEELASQISSKIYDDLHAFYKSLNSVDGISNLTIEEEELVNTDFSLAYGGRLLLSHTNLHLYRGHRYGVVGHNGCGKSTLLRAIGDYKVENFPSPDEVKTCFVAHSLQGEDTSMAILDFVAQDKALLTMNVTRQEAADALHSVGFTAEMQENPVASLSGGWKMKLELARAMLQKADILLLDEPTNHLDVANIAWLEAYLTSQKNITCLIVSHDSSFLDHVCTDIIHYEGVKNQAKKLGYYQGNLSAFVKVKPEAKSYYTLTATNEKFVFPPPGILTGVRSNTRLILKMTNASYTYPNAKKKSLDNVTVGLSLSSRVAILGPNGAGKSTLIKVLIGEVIPQEGKVFKHPNLRVGYVAQHAFHHLDQHLEKTPSQYIQWRYAGGQDREVSEKESRKLTEEDRAQLQRDITVNGERRRVEALIGRQKLKKSFQYEIKWFGKPHKYNTWVSREILLENGFQKFVQAFDDMESSREGLGFRELIPEDIRAHFEDVGLPGDIADYSPISSLSGGQKVKVVIAACLWNNPQLLVLDEPTNFLDRDALGGLAVAIRDWEGGVVMISHNEEFVSALCPEHWHVEAGKVTGKGKTAVDDGKFEDLSEKDLKKIEAKATKKKKLTRNEIKAKERRARERELAWLQSPKGTEKPKSFFSDDEE O14141 NTPPA_SCHPO ACT_SITE 105; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q99210" CATALYTIC ACTIVITY: Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9; Evidence={ECO:0000250|UniProtKB:Q99210}; CATALYTIC ACTIVITY: Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9; Evidence={ECO:0000250|UniProtKB:Q99210}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q99210}; MOD_RES 38; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G6.03c; CHAIN 1..241; /note="dTTP/UTP pyrophosphatase"; /id="PRO_0000123090" MSNEKMDTSPPSYDSHFTLETSMHRQLKDKRIILASGSPRRKQLFEQMGFPNVETCVSGFPEDLNKSMYITPWEYAADTSVQKAIAVYEKLAAEEDSPDIVVSADTILILDSEIMEKPNDPKHHLAMLKKLRNSKTPHKVFTAVSVIVPMEVPIHPGYVMKTHLEETQVKFDPSITDEFLEAYVRCGEGSDKAGGYAIQGHGALLIESIIGDFSNVVGLPIRATFKLMEEALEQGDADNYD O14145 TPS2_SCHPO CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12; Evidence={ECO:0000250|UniProtKB:P31688}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P31688}; SPAC3G6.09c; CHAIN 1..849; /note="Trehalose-phosphatase"; /id="PRO_0000316232" MPSGAQGNTQSAAYKRIVNVSRNFQFKAALNKDTREWTFQHRSSGTALYSAIASLGDPSSPWDAVYVASPGPVQISEGNDHTVETKIDEAAVVHRSSSIVISPEDQEIFLKKATEYYRKKNIEADIVPVWGKVQRVPQAKSSSATITPSVSNKLSTAYQSIKSEALKDGPMYADSVLWDVLHYRIPTLDGYQQHNLWKNFTRWSQYFADNIVSNYRPGDLILIHDYSLFLLPRLIRKQLSDAPIVFFLHAPFCTSEVFRCLSKRAEILKGVLASNVIAMQTDSYTRHFLSTCSNVLGLETTSTHIDTSDGFRVVVFSSHVSIDVPRVYSRCNSKPVSLKIQQLKSLYPSDKKLIVGRDQLTKACGVTHKLRAFRELLIHFPKWRGHVVLIQITSLPVGNNYSNEELKKTENLVAQINSEFGSLDYTPVIHFHQLLDPDEYYALLSVANIACVSSVRDSMNTMALEYVACQQKNKGSLILSEFSGTAELLLSAYLVNPYDYSRFAETINYCLNMTEKERERRFSSLWKQATSQSSQQWIYKLINRAAYEVKALESHMTTPLLTYNILIKPYRNAKRRLFLLDYDGTLIESARNSIDAVPTDRLLRTLKRLASDSRNIVWILSGRSQKFMEEWMGDISELGLSSEHGSAIRPPLAGSWSSCAENLDLSWKDTVRDFFQYYVERTPGSYIEEKKHSISWCYQNANTTYSKFQSLECQTNLEDMLKHYDVEISPAKSFLEVHPNYLNKGSIVRRILKRSGSVDFVFCAGDDKTDENMFEVFLPTAFSNSHLIDEIDSTEYSGSHHTDDNSDANKVENVKVATFRVHIGLTDKPTLSDYHLPAPRDLGELLHNL O14146 VPS51_SCHPO MOD_RES 18; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G6.10c; CHAIN 1..159; /note="Vacuolar protein sorting-associated protein 51"; /id="PRO_0000304066" MSSKRRQALRDFYNLPGSNSSSSTVSTTRKPSSSNTVSPVEETALDKVDPEFSDPNFDSNAYVSKFMEKATPAELLQRDKSLVASIQGLSVDHRSLVYNHYKHLLEASDAINSFCKNLNTLLPALNDAYQACPKPTRKNGNNDTYSAPQSFNGNEFSAP O14154 MDE5_SCHPO ACT_SITE 226; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P56271"; ACT_SITE 250; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P56271" BINDING 105; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 143; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 144; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 182; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P56271"; BINDING 195; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P56271"; BINDING 224; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 226; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 229..230; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 230; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 250; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 254; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 318; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 365; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3" CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P0C1B3}; Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. {ECO:0000250|UniProtKB:P0C1B3}; SIGNAL 1..25; /evidence="ECO:0000255" SPAC25H1.09; CHAIN 26..513; /note="Alpha-amylase mde5"; /id="PRO_0000001357" CARBOHYD 162; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 357; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 52..60; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 171..184; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 260..304; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 454..488; /evidence="ECO:0000250" MKHNEVFGWTLKVLSFLLVVIPANALDKHGWRKQSIYSLLTDRFASTNPKPCNPEDREYCGGNWRGIIDKLDYIQGMGFTAIWISPIIKNIEGRTKYGEAYHGYWPQDLYTLNPHFGTEQDLIDLADALHDRGMYLMVDTVVNHMGSSDPRNIDYGIYRPFNQSSHYHPMCPIEQDKPLSLEQCWIGTEDMTLPDIDTENPQIIETLYNFIHDQVKQFKIDGLRVDATKHVRRTFWPGFCESAGVYCQGEEWTGQADLFCEWQEYMDGLHNFPVQGVAAESVIPLNDRALRKTAIAMNLVAHHCKDSTLLGLFLESQDAPRLAALNNDYTVLKNAMTLNLMSDGIPIVFYGQEQMFNGSHDPVNRPALWDQGYNTDGPLYQYTSKVNKIRRDLINSEDGEIYIRSITHAIMIGDHVMVMYKGPVITFITNYGAVDKEYLIKMPGSETMIDLLTCTLIEVEGEVMRTSIKKGEPKILYPYQLAFRDGFCQEQITLQEIDDVFMGRNEINGPDRK O14159 LCB4_SCHPO ACT_SITE 172; /note="Proton donor/acceptor"; /evidence="ECO:0000250" BINDING 113..115; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"; BINDING 145; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"; BINDING 170..173; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 177; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"; BINDING 202..204; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"; BINDING 266; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"; BINDING 272; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"; BINDING 426..428; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00783" CATALYTIC ACTIVITY: Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+); Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216; EC=2.7.1.91; Evidence={ECO:0000250|UniProtKB:Q12246}; SPAC4A8.07c; CHAIN 1..458; /note="Sphingoid long chain base kinase 4"; /id="PRO_0000314771" MDFGLTNNSIKAFEDQKLLHIHQSCVSYPSDTLICSIPVSAKNVDLNIPFKNILWVDKTGPNSVTLSYVSRSSKVATKCWVDFVENSDQFCEYLLDVAYKGIKRSRRFIVFINPHGGKGKAKHIWESEAEPVFSSAHSICEVVLTRRKDHAKSIAKNLDVGSYDGILSVGGDGLFHEVINGLGERDDYLEAFKLPVCMIPGGSGNAFSYNATGQLKPALTALEILKGRPTSFDLMTFEQKGKKAYSFLTANYGIIADCDIGTENWRFMGENRAYLGFFLRLFQKPDWKCSIEMDVVSSDRTEIKHMYEKSKNLAPMSESSDSDKTVSTSPESHLLTFEINDLSIFCAGLLPYIAPDAKMFPAASNDDGLIDVVIVYSKQFRKSLLSMFTQLDNGGFYYSKHLNYYKVRSFRFTPVNTGKRHYFALDGESYPLEPFECRVAPKLGTTLSPVAGFQLLDI O14161 CWC21_SCHPO MOD_RES 118; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4A8.09c; CHAIN 1..293; /note="Pre-mRNA-splicing factor cwf21"; /id="PRO_0000123502" MSYNGIGLPTPRGSGTNGYVMRNLSHVKKYDKNTNLQSNRNAKALEKRVQDPSISEHECRRQIESKLLLYREQLLEEVSSQHSTDAAASDSNTNFGTENPKPPKAIIKDEQSQSKTKSLDEADVEILVQKYREQLLKELQLQKSTEKGKNFESILQPQKRKETRGFHSKNDDDGRLEERDDLRSSVDDDYYDYPRYSERKSLNSKRHVDNYNENRRRHYDSYSSYDELERRRSSNESYSRRSELPRRDYNRHDERERYSYHRRRERSNSPSYTKNESIPVVDRDSSPEGGEIV O14172 MET8_SCHPO ACT_SITE 117; /note="Proton acceptor"; /evidence="ECO:0000255" BINDING 32..33; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 53..56; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin; Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76; CATALYTIC ACTIVITY: Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin; Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4; SPAC4D7.06c; CHAIN 1..264; /note="Siroheme biosynthesis protein met8"; /id="PRO_0000346781" MASKYQSVQPGGSLIIAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKAGLCKEVAWRIQEKQVEWRDRGFLVEDLSDDVNMVLTAIDDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLRQKLRDIVPEPENSRKRMRWMIEICELWSLEELAMLDENLINRLLGYFPKKTPSYREITTPAYSKIDNYIWFGAIIISGAVLLKHVSKAR O14175 DSC4_SCHPO SPAC4D7.11; CHAIN 1..281; /note="DSC E3 ubiquitin ligase complex subunit 4"; /id="PRO_0000116701" MDTIVLDQRGEVFSFFRSLDMLCYAIIAQQYFQDPTVLLLLLKVFVQLSYLTPKPFSQLNALPLFYPLLLNFLISLMVRMFFNLPTAGESLDGYLYGGSIINFIGEKNESSRIDFITSDLVLFCLQIFMALILIASNKRPTQASHIQASQSGLSNVDGDEEPSDLITEDSRDTQQGQRQEDLQRQLENERSRLIARFSHSLYSFQHGLSFGSPQNRNTPLQRQSADSYSTPVCIEVDSEDWKDLVWKSQYATENANTNSINNSPLSSNTTGVPNSVLTNPI O14177 DID4_SCHPO SPAC4F8.01; CHAIN 1..210; /note="ESCRT-III complex subunit did4"; /id="PRO_0000116658" MGLTSWLFGGGKSPQEQLRAHQRSLGRAERELDRERTKLDQRERALIQEIKGSAKAGNTGAARIQARDLMRLRNSRKKMMNAKTQLQAISLRLQTMRTSEQMMQSMRGATRLLTGMNKSMNIPAMARITQQFERENEIMEQRQEMIDENMDDALEEDDEEEADELVNKVLDEIGVDLSQGLPDAATQIGTVPELKTEDNLQARLDELAKR O14185 STG1_SCHPO SPAC4F8.10c; CHAIN 1..174; /note="Transgelin"; /id="PRO_0000116661" MTSQLEKEAREWIEETLHTKLNAQLDLLDQLQSGVILCRICKEALGANIRYKESNMPFVQMENISAFINYAQQVVHVPSQDMFQTSDLFERRNDEQVLRSIHSFSRYAAKMFPGKVRGLGPKLAEKKPRVFSAQQQREFREGVNSLQYGSFDMPTQGTEKIAFSRRRDPTGNMY O14198 MED18_SCHPO SPAC5D6.05; STRAND 2..10; /evidence="ECO:0007829|PDB:3C0T"; STRAND 26..41; /evidence="ECO:0007829|PDB:3C0T"; STRAND 46..48; /evidence="ECO:0007829|PDB:5N9J"; STRAND 55..61; /evidence="ECO:0007829|PDB:3C0T"; STRAND 78..83; /evidence="ECO:0007829|PDB:3C0T"; STRAND 91..93; /evidence="ECO:0007829|PDB:5N9J"; STRAND 95..104; /evidence="ECO:0007829|PDB:3C0T"; STRAND 118..133; /evidence="ECO:0007829|PDB:3C0T"; STRAND 136..148; /evidence="ECO:0007829|PDB:3C0T"; STRAND 156..160; /evidence="ECO:0007829|PDB:3C0T"; STRAND 165..174; /evidence="ECO:0007829|PDB:3C0T" HELIX 12..14; /evidence="ECO:0007829|PDB:3C0T"; HELIX 15..25; /evidence="ECO:0007829|PDB:3C0T"; HELIX 52..54; /evidence="ECO:0007829|PDB:3C0T"; HELIX 62..64; /evidence="ECO:0007829|PDB:3C0T"; HELIX 65..68; /evidence="ECO:0007829|PDB:5N9J"; HELIX 72..74; /evidence="ECO:0007829|PDB:3C0T"; HELIX 109..115; /evidence="ECO:0007829|PDB:3C0T"; HELIX 179..196; /evidence="ECO:0007829|PDB:3C0T" TURN 153..155; /evidence="ECO:0007829|PDB:5N9J"; TURN 197..199; /evidence="ECO:0007829|PDB:3C0T" CHAIN 1..207; /note="Mediator of RNA polymerase II transcription subunit 18"; /id="PRO_0000096367" MQELYLLGVVPSRRFEAVVNSLSKTLDGPKTILEFWVVYRPKDVPPNLPRQPDSWLRLCSNIESHDETDTEWSKNTQWSMYLEGNSEPKREDKCGIRPVNRAKLTNGSVTEFVEKMGYEFSHEYIIQGLEYFFFDTTVRIYQTLIPSQQRSIKPPFHPMNEEQPWILHVYTHVADASNQVAMAKAEANLTKVKTLLSAFCDLKNVRL O14200 PXA1_SCHPO SPAC5D6.07c; CHAIN 1..495; /note="PXA domain protein 1"; /id="PRO_0000116654" MAKLSSLLNPIISKILEIYVYSWYSGISKDALFPSQCEQVGGSIVHELEKRLSRQDAMDLLFYEIPFLLIKHIENTEEAKLRFALPQGQILEIDTIYHSLHPHIALEKEENELVYCRLLVEDILKYLLPATNSKSEIECVILREALAVQIHKSIQVASSPETMYKFIIYLSKAILQPSRRPWKESITTAVRWVWHAFRILLITRGVPYFSTAWFQFYLKLFSQKDNVSSSDLTRWFFFYTLLYPWIALVSAFVAETMTLCCIVTIFYDKNVNRQWKQYILTSVSNMDKGNPSGGSQSTNVTTFRRFSQSSYPRRSNYRRRISTSSKSLYELSPSKFKSIPITSNPPPMLNLSKGSTSVEPTFCETNASVALSTVTSTPVFSTDSSPLSSRTRENLLSLIPSAVSSPTKANTNKSHQRSFSIPKATKDSQTPSENSAATLKQAAIDAYSQIPVIPFFLPSDKLIMLVESEYRNKHIFYSLLNSFTMVMFPELRHTK O14205 VPS74_SCHPO BINDING 81; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250"; BINDING 90; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250"; BINDING 171; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250"; BINDING 174; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)"; /ligand_id="ChEBI:CHEBI:58178"; /evidence="ECO:0000250" MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC5D6.13; CHAIN 1..337; /note="Vacuolar protein sorting-associated protein 74"; /id="PRO_0000123824" MSGGLSRRRVAAASSDEERPEMRSVSHSKSHLEGYDDDHKIAFDPKDLEQGAEREKQPRLTLMEEVLLLGLKDKQGYLSFWNDSISYSLRGCILMELAFRGKLRMQKDVNRKRFPLADRVVELVDEKLTGEVLLDEAIKMIHTSELMSVTSWIDLMSGETWNVMKIGYQLRQVRERLAKGLVDKGILRNEKKNFLLFDMPTHPIADTSIKDSIKKRVVSVLTSRVIEIDNSPSFPEYLSFRCLRTVALACSSYAANVLENALDNLNYEDREKAFSRVDELLCDFSQWPFDLHASSSVGANLPELISEELSSVKEEQLLFIEVVAAVLQVFTHLDSLL O14210 IES2_SCHPO MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6B12.05c; CHAIN 1..295; /note="INO80 complex subunit 2"; /id="PRO_0000116664" MARRRSTRRALVETPSDLNAQDSDSLSVSTKEELGDDALAAEEGQSVLDEQEIEEALEEDDTNYEEDIIDDEESAQVDEEELEEEEEEEEDATPEPVVTSKKNSRSKPKNGGASKRKASRRTVVDEDSENLEGDEEDGSFSDLKDLYSNPMPAQTTPVSMRMTKRQRAIQGILEEGEEDELLELPPETSGRKKLTPEEMALRRIENARRRKNQSERRLEEEKMETINRLLKRQSNTGKPRRGRAPNNPTSDSISRSKAVPKDRINMYQPFQCVRFKSTKEGSSLGVPEPLIRFFS O14217 TOM70_SCHPO MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 129; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6B12.12; CHAIN 1..625; /note="Probable mitochondrial import receptor subunit tom70"; /id="PRO_0000106339" MSGISNAENGKAIVSSGVLNSVSAFVRRHRTFVYTIGAVAVFATVGGVYHVQQKKASHKRSKKLKAHQDKAESKVNEGKNEAAKVVKEEDLKSSETGKDVETAAAAAAAAKKKKKNKKKVKAKKVGDSSVDKIATEESVKSMTKEERAKLAAELKTLGNKAYGQKEYANAIDYYTQAITCSHDPIFFSNRAACYAAIGDFEQVIKDTSEALSLDSSYVKALNRRSAAYEQLGKLDEALMDSTVSCIFDGFANESMTATVERLLKKVAEKKSSALLKERPPKLPAASFIQTYLDSFHAQPKPLFDNKFDGDAALAEAYEYLEKGEYQLSYDKAKESCLGSFSSPSVNARTHNLVGTFKFVSGDSKGSMENFNAAIKLDRKFIQPYIRLSAAYLDENDNEKMWKVLNDAESVDKTDSDLYYHRAQVRFVSGEFAEAISDYQKSIALDDSFIYSHIQLGVAQYKTHAIAESMKTFEDCKKRFPNSSEVYNYFGEILLDQQKFDDAVKNFDHAIELEKREHLTIMSAMPLINKALAVFQWKKDISQAENLCRQALSADPECDIAIASMAQFLLQQGKAREALEYFEKSAQLARTESEMVNAFSYAEATRTQIALTEKYPQLVGRLSNPM O14228 PUR4_SCHPO ACT_SITE 1156; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 1284; /evidence="ECO:0000250"; ACT_SITE 1286; /evidence="ECO:0000250" BINDING 312..323; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 391..393; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 691; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 692; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 733; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 737; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 903; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 905; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000305|PubMed:967158}; SPAC6F12.10c; CHAIN 1..1323; /note="Phosphoribosylformylglycinamidine synthase"; /id="PRO_0000100404" MLVYYGGSALSVQSKKKILELTVSGVSDLNAVYFYLIYTKSNSSLNCESLRPILSDLQESEFKPDGTTMVYVFPRPGTISPWSSKATNIANVCGYKDVIRIERGIAYSVVFKDDISEEMLKSALNHLYDRMTEALRFKLPEEDEVFDKHEPAPLVRIELNCGQGGDKQAATERLNHANKKFGLALAPDEIDYLVECYTSEPSLKSREPTDVELFMFGQVNSEHCRHKIFNADWTIDGEKKDYSLFKMIRNTHLKNPQYTISAYSDNAAVFEGNSGTLFAPVNGIWSMKDEPVEFLGKVETHNHPTAVSPFPGAATGSGGEIRDEGAVGQGSLSKAGLAGYSVSDLNIPGYKQPWELDVGKPYHIATSLDIMLEAPIGSSAFNNEFGRPCINGYFRTFCMEVPRGDGTLEIRGYHKPIMAAGGIGRIRKQHAFKKSIAPGSPIIVLGGPALLVGLGGGAASSMNAGEGSEELDFASVQRGNPEMQRRAQMVIDACTTMDENIIQSIHDVGAGGVSNALPELVHDAGLGARFELRDIPCIEPSMSPMQIWCCESQERYVLSVKSEDLDTFKSICERERCPYGVVGYSTVEQRLILTDRLYNTTPIDLPMEVLFGKPPKMSRVAETQTIPLSKFDSSLKSYLAPSSDPILDAVERVLRMPAVASKSFLITIGDRSVTGLIARDQMVGPWQVPVADVGVTVTSYGKGINTGEALAMGEKPISALVSAAASARMAVAECIMNLVAASIPALDRIRLSANWMAAPSHPGEGAKLYEAVQAIGLELCPSLGISIPVGKDSMSMSMKWNEDGREKSVTAPLSLIITGFSPVDDLYSIWTPQLRKVEDIGSTSLIFIDLANGKQRLGGSILAQSYKQLGDEVPDLDNLDTFKNFINVITQLHKTNYIQAYHDKSDGGLFVTLSEMAFAGHVGIECELDSLSSDNIAALFNEELGAVIQVCDRDIAKVLELFAANGLSTCVHRIGKVLSGQAQTISFSRSGKIIFKSTRSKLHGIWHETSYKMQEIRDNPECARQEMENIADNNDPGLGYHLTFDPNVSVTADLALTSRPKVAILREQGVNGYLEMAYAFYASGFTAVDVHMTDILSGRVHLDDFVGIAACGGFSYGDVLGSGNGWATSILLHEDARNEFYRFFNERKDTFGLGICNGCQLFSRLKSLIPGAKSWPMFTFNESAQYEGRAVMLKIDETSGSKSIFTESMAGSSLPVVVAHGEGRAVFDSESDYEQFKKEGLDLIYYVNNYNERTSRYPFNPNGSRDAIAGVRSPCGRFLAMMPHPERVVLKVANSYYPHSKASEWGVHGPWIRLFQSARKWVG O14229 SFC1_SCHPO PTM: Phosphorylated. {ECO:0000250}. SPAC6F12.11c; STRAND 10..18; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 69..71; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 76..81; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 86..98; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 233..236; /evidence="ECO:0007829|PDB:4BJI"; STRAND 260..263; /evidence="ECO:0007829|PDB:4BJI"; STRAND 271..274; /evidence="ECO:0007829|PDB:4BJI"; STRAND 290..292; /evidence="ECO:0007829|PDB:4BJI"; STRAND 314..316; /evidence="ECO:0007829|PDB:4BJI"; STRAND 320..322; /evidence="ECO:0007829|PDB:4BJI" HELIX 23..28; /evidence="ECO:0007829|PDB:4BJJ"; HELIX 33..45; /evidence="ECO:0007829|PDB:4BJJ"; HELIX 47..49; /evidence="ECO:0007829|PDB:4BJJ"; HELIX 103..105; /evidence="ECO:0007829|PDB:4BJJ"; HELIX 216..231; /evidence="ECO:0007829|PDB:4BJI"; HELIX 237..241; /evidence="ECO:0007829|PDB:4BJI"; HELIX 246..248; /evidence="ECO:0007829|PDB:4BJI"; HELIX 252..255; /evidence="ECO:0007829|PDB:4BJI"; HELIX 256..258; /evidence="ECO:0007829|PDB:4BJI"; HELIX 283..288; /evidence="ECO:0007829|PDB:4BJI"; HELIX 323..325; /evidence="ECO:0007829|PDB:4BJI"; HELIX 332..336; /evidence="ECO:0007829|PDB:4BJI"; HELIX 353..370; /evidence="ECO:0007829|PDB:4BJI"; HELIX 378..386; /evidence="ECO:0007829|PDB:4BJI" TURN 29..31; /evidence="ECO:0007829|PDB:4BJJ"; TURN 82..85; /evidence="ECO:0007829|PDB:4BJJ"; TURN 249..251; /evidence="ECO:0007829|PDB:4BJI"; TURN 267..270; /evidence="ECO:0007829|PDB:4BJI"; TURN 329..331; /evidence="ECO:0007829|PDB:4BJI"; TURN 346..348; /evidence="ECO:0007829|PDB:4BJI"; TURN 371..373; /evidence="ECO:0007829|PDB:4BJI" CHAIN 1..456; /note="Transcription factor tau subunit sfc1"; /id="PRO_0000116669" MNSLKISDNEYALIEHPGFANNKDAFFQTLGGVQSIQKACQTSFQNPKQALLELNLRPKDKYHHPVQARVQSRNDLLVTIKKMDNSVQNVSRIRQVFLFRDMADFQYSTQNSPFVQKLDSTLRVLDYNAINKFSIDLTPVQRKHVDMPPPPVFSQTSLPMSYNFLQNPLVGRVRLPNGKTTIVNLKGQCRVWIITTNMGVESVPTCRHSKLGEPSKTIQEVIEALKPLFEKRPVWTRRALLNHLDPSYTHYLKFALPYLSYLWTSGPFRDTYTRFGYDPRKDSNAAAYQALFFKLKLNGKHKGTKTHVFDGKTLFPTNRVYQVCDIVDPTIAPLLKDTQLRSECHRDTGWYRSGRYYKVRDLMREKLFALIEGEMPSEVAVNMILNAEEVEESDRYSNFDEQDNTDLNDTVRGLNTSATDDRINDLMRNLMKRSQEHEGFEDLEEIDDDYDDIFGD O14239 RAX2_SCHPO SIGNAL 1..27; /evidence="ECO:0000255" SPAC6F6.06c; CHAIN 28..1155; /note="Polarized growth protein rax2"; /id="PRO_0000290655" CARBOHYD 44; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 61; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 103; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 118; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 124; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 156; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 182; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 190; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 213; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 224; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 306; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 391; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 413; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 419; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 510; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 519; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 554; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 562; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 607; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 630; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 713; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 722; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 743; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 769; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 793; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 807; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 824; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 840; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 848; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 876; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 893; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 899; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 916; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 945; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1009; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1030; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1055; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAIYSSFWIRLYFTFRFFCYFLTSVVASDVSFLGDFSGFNVLSNSSANTDLSSQFFEQTNNGSLSSLIDTSYSNSQICYSSWQGDLYVIVLDSEQQTVLLQSNFTSNPTSLEIFSSQNTSFFGNISAIFCDDKFPYAYATFTFSDKPSFTSIYRWNVTNSNVTIEHFYNVKGNVDSLFFLNNDSVAISGNFTEISPFSSSNGPQIAKLAFRSNNSFSQNSLNRNLSSVSCDLTDSYSLWDPSSSGLVSIYAWAPYLIDFNRIRFYNYESSENSVAFFSAINPADGTVLPLTHYDLETGLSSTCDVNCSLQNFANYQDFYFSKGYNSYQIEIQMFGNGEATENSAFGLSSLQFFETNQNSYFDDSYNQESCGFPGLNSLSSYEGNFEASFSNASMPYWIQTIAGEQASVSFFPNITVPTNGTVQLLIPGCTYDNTCSQRGSVIANVYFAKNKQPATKLVQQASDFDQYVSLYSGYLQGFSDNFRPYVELLPYKNSRMVTHSIRFLEQSYTNVSNGLVFVNTTTDVNKLPSIIEFPAASKLRGTAISQIKSLSNGNFSLYMTGNFSDNYGNNVVYMDSLNHLHSFPNNGLNGWVSYIYVSGDSSYFGGNFTHTGDGSIKLNYIAMYSETSRNWSSLGLGTNGPVTHIGSTSLFIDGKIESFISFQGDFNEVYTSEGYAISTSGFSLWNPSSKSWVSMEKLGFYMSGYLFDIPGFNSTQRIYSGNLSAIASYSTRNIAHFSSDSLNDTFIPCYVNAFPSYIRLEDIAYPFANNSMIAILGSEEMEDKCTAAVYFANSTEPIYPKRILSANCSSKFIVLEDCLIIYSNDTDESDIVKNTFVSFNTTSNSLGNTTALSQLKGHINSVIVDDSYNNIFFGGNLSEQSSGCVGFCIFEYNSSSWRNISHNLISAEVQSILWVNETYSSMYLAGKFVWDTSDVDYLLMYNFDNNTIMSCKGSSSIPGPVLLASLKSQSKDEYSVLLYGTEVSSSDTYLNVLNSEGAINSYSLDIHLNQSTINSIDFFESNQISQIPINDSIIVLSGLIVLDDSSKASAVYCVNKSCLPLLTAFKDNGEAGIVRKVVQQKSFSSSASKMIPVTTKYDHIGQPRYVVIISLGISIGVMFLIMSGSIVVEIIHWFFSEHVETLHDYSNFLKELKTQ O14241 ARPC2_SCHPO SPAC6F6.10c; STRAND 28..32; /evidence="ECO:0007829|PDB:8UXW"; STRAND 38..42; /evidence="ECO:0007829|PDB:8UXW"; STRAND 49..55; /evidence="ECO:0007829|PDB:8UXW"; STRAND 87..93; /evidence="ECO:0007829|PDB:8UXW"; STRAND 157..162; /evidence="ECO:0007829|PDB:8UXW"; STRAND 165..172; /evidence="ECO:0007829|PDB:8UXW"; STRAND 175..182; /evidence="ECO:0007829|PDB:8UXW"; STRAND 214..218; /evidence="ECO:0007829|PDB:8UXW"; STRAND 234..237; /evidence="ECO:0007829|PDB:8UXX"; STRAND 239..246; /evidence="ECO:0007829|PDB:8UXW" HELIX 9..20; /evidence="ECO:0007829|PDB:8UXW"; HELIX 34..36; /evidence="ECO:0007829|PDB:8UXX"; HELIX 59..64; /evidence="ECO:0007829|PDB:8UXW"; HELIX 67..75; /evidence="ECO:0007829|PDB:8UXW"; HELIX 76..78; /evidence="ECO:0007829|PDB:8UXW"; HELIX 101..112; /evidence="ECO:0007829|PDB:8UXW"; HELIX 114..118; /evidence="ECO:0007829|PDB:8UXW"; HELIX 121..139; /evidence="ECO:0007829|PDB:8UXW"; HELIX 144..154; /evidence="ECO:0007829|PDB:8UXW"; HELIX 187..203; /evidence="ECO:0007829|PDB:8UXW"; HELIX 207..209; /evidence="ECO:0007829|PDB:8UXW"; HELIX 224..226; /evidence="ECO:0007829|PDB:8UXW"; HELIX 247..249; /evidence="ECO:0007829|PDB:8UXW"; HELIX 255..263; /evidence="ECO:0007829|PDB:8UXW"; HELIX 265..296; /evidence="ECO:0007829|PDB:8UXW" TURN 141..143; /evidence="ECO:0007829|PDB:8UXW"; TURN 252..254; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..317; /note="Actin-related protein 2/3 complex subunit 2"; /id="PRO_0000124040" MLSLDYNNIFIYELLTERFSSENPSSIDQVVTDFDGVTFHISTPEEKTKILISLSMKCYPELVNYGTLDLLKQIYGAYVHEPEMGYNFSILIDLQQLPATDEEKEQLAMSISMLKRNVLAAPFHRAFTKQAELADLARKDPENAPMLDKQATSQELMAIHYRDEETIVLWPEHDRVTVVFSTKFREETDRIFGKVFLQEFVDARRRPAIQTAPQVLFSYRDPPLEIRDIQGIQKGDDFGFVTFVLFERHFTPQNREDCISHIQVFRNTLHFHIKASKAYMHQRMRKRVADFQKVLNRAKPDVELERKTATGRSFVRA O14248 TEA3_SCHPO MOD_RES 430; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 437; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 460; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 523; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 980; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 982; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 983; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 984; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1078; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1080; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6G10.02c; CHAIN 1..1125; /note="Tip elongation aberrant protein 3"; /id="PRO_0000119149" MVQKVLSRQSDNSQDVSAEQLDVVESGSIDQQNIRAWVVRKVKENDKRTSTNQSFKWEAVKPASCLDAANEKFMYLHGGREKSGISNSLFKLDLDSCTVYSHNRGEDNDSPARVGHSIVCSADTIYLFGGCDSETDSTFEVGDNSLYAYNFKSNQWNLVSTQSPLPSPRTGHSMLLVDSKLWIFGGECQGKYLNDIHLFDTKGVDRRTQSELKQKANANNVEKANMEFDETDWSWETPFLHSSSPPPRSNHSVTLVQGKIFVHGGHNDTGPLSDLWLFDLETLSWTEVRSIGRFPGPREGHQATTIDDTVYIYGGRDNKGLILNELWAFNYSQQRWSLVSNPIPILLSDSSSYKIVSKNNHILLLYLNALDAPKQLLCYEADPKNLYWDKDKFSDIPVLQHISMKPSNASNHTVSLGYLNDRPNHSKKNSVTSTSSSQFNNFLEQNQKAVRSARHRHYASLDEQGLHSLRNLSKTSGMNHSADFSLHEFGQADPFAYEIEKPIASLPLPNGNDTISRSSESSSPINESESNSLLKLQSDFKFSNSDDRVAWLEEQLLYCMQQGYTLKPPNLFQHVDEKLRLEKKEQLSYLEILKVIEQMLESNEQKFKKQIVSLASENAKLAAQRDAAVENANYSRSLIQKKTTDETVGSLIEKVGKLEYEVQGTLEEATSYYQKNTELQQLLKQNESASELLKSRNEKLCVDYDKLRSVFEEDSSKILSLQKENENLQSQILQISEELVDYRSRCEALEYGNYELETKLIEMHDRVEMQTNVIEASASALDVSNTAILSFEDSLRRERDEKSTLQQKCLNLQYEYENVRIELENLQSRALELESALEQSVSDAKYSKAIMQSGLSKLLSSINENKDNLKEFSKSKQKISYLESQLEGLHELLRESQRLCEGRTKELLNSQQKLYDLKHSYSSVMTEKSKLSDQVNDLTEQAKITQRKLSEVQIALADSKMNQQLSGKDSTDVHLPTDFSASSSPLRSYFNEEDSFNNASAAHSSKESDIPSGGVFTKYRNHFGNLMTSEETKAPDNNDLHKRLSDVINSQQKFLSLSPQVSKDYYDVRSKLNDTAGSFSGEEMRAIDDNYYASRIKQLEDDYQKAITYANCSDESFQQLSHSFM O14249 CLD1_SCHPO ACT_SITE 180; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P53264"; ACT_SITE 367; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P53264"; ACT_SITE 398; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P53264" CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a fatty acid + H(+); Xref=Rhea:RHEA:32935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:62237, ChEBI:CHEBI:64743; Evidence={ECO:0000250|UniProtKB:P53264}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32936; Evidence={ECO:0000250|UniProtKB:P53264}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC6G10.03c; CHAIN ?..428; /note="Probable cardiolipin-specific deacylase 1, mitochondrial"; /id="PRO_0000116702" MSQVKVAVRSEEAANSYTQTFGMSWRQWRQACSEEYAKQCEREVLHTVDFIRENEKDPERLVEVVDSKIYDNDGLVHEVCVSDKATGKANKRSIVYMHGYGAGLGFYFRNMDGLTKGVTKDFNSYFVDWLGMGNSSRPPFDIKGQTASEKVEETERFFTESLETWRIGHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPFASNDDAEVYNSVASSAVHAVMDEPPLSNVTNEVLQTQEETTGLEPSRPSKPKNPLPRFITFLWEQNVTPFSLLRLSGPLGPKLMSFWSSRRFSTLPPETFRALHNYCYSIFRLKGSSEYALGNLLAPGAFARRCIMNRLRMLKCRTIFMYGDKDWMDDVAGLEATNRLKEMNIEAEHHIISNAGHHCYLDNPEDFNEIVLKEIRMSLRSFSSISE O14253 NCBP1_SCHPO MOD_RES 29; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6G10.07; CHAIN 1..780; /note="Nuclear cap-binding protein subunit 1"; /id="PRO_0000373992" MSSYRGSTRPRKRTREGENYGFRPHRGNSQELLAARIKKDITFLADPRGNSVAADDINYVAMSLSREANDPETISTILDCIQTTAFIIPVKIPHLATLIIRASLRVPLILEKAAAYFCLQYFTNLNSFLYYEAKVDLRMLICMSFALQPGTLKPLFSLLADAISKETKPSVWGDNFLRIILINLPYFIAANNDLGKKDFANEILDQCEIYVRHRKSSITLSNPLSIHDNLSEEELDLLYKQLILSRENDFTFPYISQPWKFFESDFVHIVPVSPSIPEWTFQPTPQQNELPSFKRFFELFNNFEIRTTPDASDVAASIFRDISVDVINHLEFNRVEAAQVLTDLDVYFTYKTFALRGTPVNELPNLDPSESRWKAEDIIVEAVLGELLGSQNTTYKPVYYHSLLIECCRIAPKILAPTFGRVIRLMYTMSSDLPLQTLDRFIDWFSHHLSNFNFHWKWNEWIPDVELDDLHPKKVFMRETITRELILSYYTRISDSLPEELRCLLGEQPSGPNFVYENETHPLYQQSSQIIEALRLHKPLEELDIILQSEEIQNSETSAVRLVMSCAYSLGSRSFSHALNVFEKHLNTLKHFSRKSLDSEIEVVDELFSFWKLQPFNAVMWLDKMLNYSIISITSIIEWLIKQDVTIWSRSYTWSLVNTTFNKLAARLRRSVSNKEDSSLINEANEEKEIVTNLLLSALRALISENAENIWVSHWLNLMLKYVESNFLSVKKDTIEEANEPVQENTSEEQEDTKMQPVDAVDEQPSENNQTAADATNEEK O14255 GCS1_SCHPO ACT_SITE 580; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q80UM7"; ACT_SITE 778; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q80UM7" CATALYTIC ACTIVITY: Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082, ChEBI:CHEBI:132537; EC=3.2.1.106; SPAC6G10.09; CHAIN 1..808; /note="Probable mannosyl-oligosaccharide glucosidase"; /id="PRO_0000057714" CARBOHYD 39; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVSDMLGGNKRWILFGLLSFLLNCVLVSCSVEDIEKAANDSFLWGPYRPNLYVGIRPKIPDSLMTGLMWSNVDDYARFSKMRHSAEHGDDIGAFGWKHYDVRRGGQQVIDDFLMGIKLETDFVKLPEGNWALRVHGIPLPGAPTDLTTSLFFYAYVEGEGKVGTKVNHANHVYMEGKTPDLGKFRIQTFNRLGEHPVSPASVDLESMVMDKDFFAGFNVKKEGAWRTSELILYLLDTKMKVISDKEGYESLKDLPPAYSTLTLPNLPSEEGLQFIQKVFKGEFMFDIVFNYASSKKISEEMISQAIDKNLQEFEEKFQATFPLKAPYDTEKAHQIFAHTAFSNLFGNVGFFTGDSIVSKNPIELDDEDYEFMQGFESAAGKLAEGTAFHDIERSLFTIVPSRPHFPRGFYWDEGFHLLPVGLWDNDFSLEILKSWFSLVNEDGWVGREQILGEEARSKVPDEFQTQYPDIANPPTLILALKGYIERLQEQQGKLNNRFSGEGEDYSLDDLEYLRSVSISNPEKSVQFLRDLFPLLLRHYEWFRETQKGDFETWERECFSQVEGYRWRGRTYQHCLASGLDDYPRAQPPSTAELHVDLLSWMTSFTRSLHFVAEFLGETEEAEKLAGYENAMLRNLEDNHWDEEVQAYCDSSVDEYDDPINVCHKGYVTLLPMMLGLLPADSGRLTSLLKLIRDENELWSPYGIRSLSMNDVYFGTGENYWRGPIWINMNYLILSSLYQNYINTPGPNQNLARSIYEELRTNVVNNVFENWRQTGIFWEQYDPTTGKGQRTKDFTGWTSLVVNIMSENY O14259 SFP47_SCHPO MOD_RES 221; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 226; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 231; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC7D4.02c; CHAIN 1..415; /note="Ubp4-interactor sfp47"; /id="PRO_0000303943" MNSFSSNEYSTEISTEALNNWQQLVEQRISLELEYAAKLAKLTKSIKAIKQCAPLNDLTKQVCVELMQCNKKHLEASRYFQTHVKEFMKEYVDRENKFSNETISKSSAAALMTSMENFILFTNPVYHNKLQVPSKSDMEIANSLKITQPAEKNSGTANPISAYSLEHAELDERNNQLSEALSMLRLSPFVNNYYPSYQNRKDGKSLMENRGVVLSVDTVTSPISQSPKKLTPTTSPINSTSLSFVDAKKPGSKWPSQYDFPKKTKSTEIPFKTLPSLNINNERELTKHKLPIVKPKLAVFPSNQATASTLQLAPPPVQAIPTLRNPVNLDDKKESLLKYYATHPTITPDGFPIFAYVRALYAYKATLPSEIDLNVDDTLVVLNRQKDGWWKGLVVSPTVGRIGLFPSNYIEELEY O14270 FKHL1_SCHPO SPAC1142.08; CHAIN 1..743; /note="Fork head transcription factor 1"; /id="PRO_0000091900" MPVAEIKNATQQPSSTNRVQAYAKLEFEKFSFFVQTLQVTMGRKASNSSDCDVHLGDTKAISRQHAKIFYSFPNQRFEISVMGKNGAFVDGEFVERGKSVPLRSGTRVQIGQISFSFLLPEGSEEDGHLKETGITPLSLQQGKIAYSDEFGGKPTGSFHTVTSNQEKDLLFSHIKHESDLPLGLSPADTNISNATSIIEHPDAANAHTLASLNQPPKHLTVSPSSIQRLSPQPYVRPTSDERPIETDSSVSAPKVANHDEELKQGKSTSPSDTVLHPDLNGSPDTGDATQKPNLSYANLIARTLIANPNKKMTLGDICEWIANNWSYYRHQPPAWHNSIRHNLSLNKAFIRIPRRQNEPGKGSFWMLDPSYIDQFEGNFFRRTKKPTPSATPAAHPDTARENELAAIQTKGISAGKTEQLNPQKETSRSKTHTSRGENVEDRPQSLLQNGIQPIIMRDGKLALNPEFFKNANGEQQAPNEQAVQAISLLQQHINKQLGPAAANNPEQATAIANALAVALAQKLQKQQTQMQGPQQVQQQAKRRKAYTSQQLNPAPTAMPHPNITSPSPSISVTQRPAVNVGPPPYVRPSAPSKLPDTRQSIGDPLPPGAMANVSAGPSSVRSSSYNSTASESKSEITSHQNLHTIPINKPFTSDRPLYSSPNDTLERVETGNQGQRMNSIGNASSFSKRDIMENENGSFDTNAKNGNNVDDSSSVRGMNLPSNSSDALRGVKRPLDETSSSYT O14275 PPR4_SCHPO TRANSIT 1..16; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC8C9.06c; CHAIN 17..931; /note="Pentatricopeptide repeat-containing protein 4, mitochondrial"; /id="PRO_0000317702" MSKSFAYRHIWCFWRFNTPLLWFPQPLKYWPAFQQSHTFNSMSVFKNDNAIANQTTVNESDVKRNVEKINDIYECSNNTKSPCFPNSDSRIPLVNWKTSTNPTLQVRAYMLDLLLPFFTLDLLPFLNKVCECCNHMLLDNPKIKQDLPFAFCYLFSSYFSYKSSRQYTCSSEEISKVFRHLNRLGGSEYVLHLFAQIPKALCKELTDVRTLNHPLRSIFTFCFKNISNPPNLLKLLTKLYPRSDRANEVLYTQYLGFLTKRGDYQIAIYMFDEMYRTHHWSSFTACRLMIESLVRQNKFEEAISLYKKIIAKRPKIARDKKILNLLLYISTVSNRSPDAFKLALQSISNANQIPSFDVFSRLMSALVKYNMTEMILPLVKQYDHKFRNLYSPNIFLSIVQALVFCGDMVNIQRWYNMSRVNSELSRIKHLLNCFLNSSTVSLDVSMVLELLRDLKKKKIKVDERTLVICITIFSRRKDLFAMEKIHQYFSDQGIKTSNQAYAALLDAYIEAEDTEKIELYLGKIRRLGITEDVSINRMLMRLALDRLDWDLLEQCTKVAERKDPEGQDYLSTITMLYHVRQHELNLALRIFSGIQKPNVVHYSIAATVLGNLNQLDQLLLLEKRMESEGKAPTALSLVAFVSSYCKQGAEGLDEAKRYMSKNFQPDKRALLFNPRTANDMTYPPSLFSSLIKEYTSLGDIKEAKQVLSTYLEYFSKNITSKPDIPFAIASMRLYCSLHDTVLSRQFWDLILQVAQQNFITTDIAAVVDDKNIPSPSGVIPAYKSALNVAAETYFSFLASVNSFQELDQEWSRLEKLGFEYDDSLQNKRIIWLLYDDRLDAAIKRVYNIFLSSKRIEELIPDASSQNSIISFFLSPDSPLYFSTLKALRDKLDMAVEDDFVRISQGILVPTVKYLQTIRRDNEILFNLLAKV O14289 LEUC_SCHPO BINDING 359; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 420; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 423; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate; Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121; EC=4.2.1.33; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; MOD_RES 486; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 488; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9E9.03; CHAIN 1..758; /note="3-isopropylmalate dehydratase"; /id="PRO_0000076892" MSPSVASPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASFIHQPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNVRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKDAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFGDVSNGSPSIITNKNYDPSHDVEGDIGLSVDDATDAVTDADGIATNVAGSVSSGSAGIPKFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADGKEIPDFVLNREPYRHATVLVAHDNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQVKFSVDLVNQTITYGDKQVKFDVEPFRKHCLVNGLDDIGLTLQKETMIDAFEAAREENFPWMNIKRSRARLSPVKSNKQSSSRNDW O14317 RLA6_SCHPO MOD_RES 100; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1071.08; CHAIN 1..110; /note="Large ribosomal subunit protein P2C"; /id="PRO_0000339898" MKYLAAYLLLTVGGKNSPSASDIESVLSTVGIESESERVEALIKELDGKDIDELIAAGNEKLATVPSGGAAAAAAPAAAGGAAPAAEEAAKEEAKEEEESDEDMGFGLFD O14318 PHP4_SCHPO SPBC16E9.01c; CHAIN 1..295; /note="CCAAT-binding factor complex subunit php4"; /id="PRO_0000116506" MESSKSPSEVEKSSSASPAPQKPMIRVSKQWVVPPRPKPGRKPALDALGRRKAPIKPRPGPTSALSVEEAKFRVREKQYQDTIGKLQKENNELLEQLEMLQAQLKNSTLDSPKEVEVNSEVVKPDSATTENENRYVNQYNYPVEPPCAKNAVYTEIPIELDPHAFLGDSAKRIRVDSDSKDAKSVPSENGRIRVSMSPQNEINFTPENPAVMEKIRKRGVCNSVEGCLYSGSPKSVKRVRESEETKVYAQLLIDLHKSSKSAPMLKAGPSIAFKLPTMEPNFNDVRPVTSISSSS O14321 ERG6_SCHPO CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + zymosterol = fecosterol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21128, ChEBI:CHEBI:15378, ChEBI:CHEBI:17038, ChEBI:CHEBI:18252, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.41; Evidence={ECO:0000305|PubMed:18310029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21129; Evidence={ECO:0000305|PubMed:18310029}; CATALYTIC ACTIVITY: Reaction=lanosterol + S-adenosyl-L-methionine = eburicol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:52652, ChEBI:CHEBI:15378, ChEBI:CHEBI:16521, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70315; Evidence={ECO:0000305|PubMed:8586261}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52653; Evidence={ECO:0000305|PubMed:8586261}; SPBC16E9.05; CHAIN 1..378; /note="Sterol 24-C-methyltransferase erg6"; /id="PRO_0000124797" MSSTALLPPNTDQVLSRRLHGKAAEKKTGLAAIASKDVDEQSRKLQEYFEFWDRNHENESEEDRARRIDGYKSVVNSYYDLATDLYEYGWSQSFHFSRFYKGEAFAQSIARHEHYLAYRMGIKPGSRVLDVGCGVGGPAREITEFTGCNLVGLNNNDYQISRCNNYAVKRNLDKKQVFVKGDFMHMPFEDNTFDYVYAIEATVHAPSLEGVYGEIFRVLKPGGVFGVYEWVMSDDYDSSIPKHREIAYNIEVGDGIPQMVRKCDAVEAIKKVGFNLLEEDDLTDHDNPDLPWYYPLTGDITKCQNIWDVFTVFRTSRLGKLVTRYSVQFLEKIGVAAKGTSKVGDTLAIAQKGLIEGGETHLFTPMFLMIAKKPETDA O14328 KSP1_SCHPO ACT_SITE 137; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 15..23; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 43; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 354; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 357; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 378; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 404; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 413; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16E9.13; CHAIN 1..474; /note="Serine/threonine-protein kinase ksp1"; /id="PRO_0000256814" MKLLQKKGYKVERPLNKGSYGTVVLAHRLFRTPRCKDLKYAIKCIKKPAYTFLQEVNILRQLSRSRHRNIIHFVESFEDNVYYYVVLEYCPLGDLYECILNNDFPNAKNQPEMIKNIFLQIIDGVAHLHSHGIYHRDLKPENFLLSLSEDGSELVVKISDFGLACRDKISYDFGTGSDRYMAPEQFEEVDGAGYSPRAADIWALGICLLNLIFARNPFTYPHEKDPIFADYMLDAMTLFDVFPTLSQDTYNVLRACLCVSPEKRSLAKTREAVLAVTKWTTDDEELESFVNEEEEFRASDFMPAEDNVRCTQSDREPLRTPSVLTPANTIQRGLLPSKLPALSDVDENISTSSSPRSPASLAPVNNSERSYDSGLGESLNNMHIGKSIATAVPVNTKRSPYSCSAPAIVFPNSIKGNKDHLKFGRSWCDMDEEDEEDIVSFGSNDDFGASDELSSKHIGLADDWNVLSQWNDNS O14329 ZRG17_SCHPO SPBC16E9.14c; CHAIN 1..386; /note="Probable zinc transporter zrg17"; /id="PRO_0000317147" MTQNHNIPTAIQIQNPINNNVSVTISDQLPKPSANNPNLLSVDTRPTHRKGHHHKHSLSHQYFLPPKNRQPLEIPASYPIPTFKETFAILTFPQKLKLTSSILFFLVAVGVLLSGDATILLTLSCSLIVEGVLIIINVWRETLDSFLVWRHTCLRYPFGMQQMELLVDFSFSILLIFLGMNLLKEPAEHAIEDWGNLHHAGDHEEETVHIHLTISLFASAIISGFALLLDHPSAHIRELNSRFFHGLTLVPSLILVLLLSLGYQVGSFLSHLLSLTIAVTALVNGFSIAKSLALMLLLTYSNKEKVFECVSLIKEDTRIDQLNYAAIWQPHYNTCIANIGLTVSGGEREQAAVREDIIRIIQKTVGSIFGAGVQPKWEISVDIQRA O14335 SCR1_SCHPO SPBC1D7.02c; CHAIN 1..565; /note="DNA-binding protein scr1"; /id="PRO_0000046885" MSEATTATTTGKPSRSTKNPDAPRPYKCPLCTKAFYRLEHQTRHIRTHTGEKPHVCTFPGCAKRFSRSDELTRHARIHTNANSRRNAAAAAAANNSARSSNSPAGNLEPSTNNAGVHMTNASMNPNVNPSYPVFIPQVGMSVAPPVATAAVSMSYPHHYSASVQQQQATFVSNGQPHNLPAQAQPATIYGIPDALHTTQNGTTIHVTGTPPGAVSQRSEPDSRLSSMNEMQLLASAAANQLDAAPRITPTKSSGVNLMPLSNAPSPPKQMNVVGSLPSSSNTSPNHLASVPNRGLTSNSSTGSFTKYTNGSSNSLYSNSSMQTPYLPSKSNSSTSLHSMYGVGTTAYAPQSLRYAHYNYLPYSRPSVSNGFDDDSSSSDFAHFRYQRRSRPVSPCSTAPSSPTFSTRSFSPTPDVTPLVTPAHSPRLRPMDDPSCVQLPSIRSLSLRPSQVPLIPPLKCDPNAFSASTPASGAVSRTPSSVSLSSLSNVNSSMPHKPASQSNVGPVRISSNRRSRKFSSSSRVSVSNLLAGSPPSPSSSTKSASSSYSTTTPAFSIGPLTPMTKP O14340 YB35_SCHPO MOD_RES 384; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 394; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2F12.05c; CHAIN 1..1310; /note="Oxysterol-binding protein homolog C2F12.05c"; /id="PRO_0000100394" MEHPSPDSVSSTSSSDHKKAELSDSLKQLQLLQAFQAGDIKQVDNLLHNKSKDECTHALFISIQCANVQMVKHILSVFDVDVNAYDKNKNTPLHLAAMAGRQDIVEALLLHPDINYNLVNANNKKAYQVATSPQLMDFMKGFYVTYTKETAREFKKAFKERNLESMDYLMRHNEFNDAIDLNEVDIKTGQTYLHVATKAKDAELVKWLLDNGADPYRRDKFGKLPTDYTKDENMRSLLRSYSGNRDSSSAPAVPQHMSGYLKKWTNYKSGYKLRWFTLNNGVLSYYKNQDDASSACRGSINLKLARLVHDPKQPTVFQVIGKGSVRYSVKANSPVEAKKWIAAISSAIENDEEANKPNVTADNASFGTHDLAPAAHKFTQSNASGNSGWDDNESDIDRAQLPSRENFEFNVNIAKLQVETLHKLIDSAMQTEKVKKDPSLSQVFDGISNSFNTLHKTVLEMLDLQRQAEHYYKRKLDNAKAINALWAENLKTVVEEQDQIEERYHRSEAHRRRTKRAFRRLAASLKKRPSDKDNKLHIHYDDGAMSSTSYSTDFTDDEEETNTKDEFFDVDAHDNNHANKAEPSQTANNVHEIREPSFSSEHKPQPSLKTTTDVSSPETKQNIADIRKTTLTDQTEEFTERRDNNGSIPSKQPSDEQHLGKESLPSQQSTVSNHHRKESIPSKQPTEGQHARQESLPSQQTTETKHLRKESTPSKQPTEGQHTRQESLPSQQTTETKHLRKESIPSKQPTEGQHARQESLPSQQTTETKHLRKESIPSKQPSGGQQLRQESLPSQQSSESKQSTQHQQPVEVQKSIQSDVSAPKAKEVSEKPVSHQAKPSNASQLSRNTDDTQAKEAPKEASIPDNASTASTKVSNDSHLKPDADKKSVSSELTHASKPSLDEKTMQLAKQIAVSFHGYEAPTRENLDVNDDRPKISLWGILKGMIGKDMTKMTLPVSFNEPTSLLQRVAEDMEYTELLDQASHNKDPYQRILYVAAFAASEYASTLNRVAKPFNPLLGETYEFCHPQRGFRFIVEQVSHHPPVGAAYSESANWKYYGESSVKSKFYGKSFDISPLGTWFLELRHPSGEVELYTWKKVTSSVVGIILGSPSVDNYGQMHIVNHSSGINCVLDFKPRGWRGTNAHEVKGSVQSTDDTPKWMVNGHWNDKIFGQQPNGNKILLWQNHERPPRPFNLTPFAISLNALTPQLKPWLPPTDTRLRPDQRAMENGQYDLAASEKNRLEEKQRKKRRMREQGEMPPWSPRWFSAAKHPVTGEDYWQFNNEYWKIREEAGEAHLAGKEFEWPNVDDIF O14344 IMDH_SCHPO ACT_SITE 337; /note="Thioimidate intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; ACT_SITE 439; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156" BINDING 280..282; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 330..332; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 332; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="ligand shared between two tetrameric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 334; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="ligand shared between two tetrameric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 335; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 337; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="ligand shared between two tetrameric partners"; /note="in other chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 370..372; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 393..394; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 417..421; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 451; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 510; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="ligand shared between two tetrameric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156"; BINDING 511; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="ligand shared between two tetrameric partners"; /evidence="ECO:0000255|HAMAP-Rule:MF_03156" CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_03156}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03156}; SPBC2F12.14c; CHAIN 1..524; /note="Inosine-5'-monophosphate dehydrogenase"; /id="PRO_0000093680" MSAFKPYTEALEVLKKYEKKDGLSIDDLIRHNFQGGLTFNDFLILPGYIDFVPNNVSLETRISRNIVLKTPFMSSPMDTVTEDQMAIYMALLGGIGVIHHNCTPEEQAAMVRKVKKYENGFILDPVVFSPQHTVGDVLKIKETKGFSGIPITENGKLRGKLVGIVTSRDVQFHKDTNTPVTEVMTPREELITTAEGISLERANEMLRKSKKGKLPVVDKDDNLVALLSLTDLMKNLHFPLASKTSDTKQLMVAAAIGTRDDDRTRLALLAEAGLDAVVIDSSQGNSCFQIEMIKWIKKTYPKIDVIAGNVVTREQTASLIAAGADGLRVGMGSGSACITQEVMACGRPQATAIAQVAEFASQFGIGVIADGGIQNVGHMVKSLSLGATAVMMGGLLAGTTESPGEYYVREGQRYKSYRGMGSIAAMEGTGVNKNASTGRYFSENDAVRVAQGVSGLVVDKGSLLRFLPYLYTGLQHALQDIGTKSLDELHEAVDKHEVRFELRSSAAIREGDIQGFATYEKRLY O14345 PFA3_SCHPO CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:P42836}; PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:P42836}. SPBC2F12.15c; CHAIN 1..329; /note="Palmitoyltransferase pfa3"; /id="PRO_0000116499" MNLIHKVSTICQCVLVILAKYCMQIIALSLMSGVQWLAWGIYKINKNRVGIIILFLYIMIVTCYVLTNLTPPGSPSETSFDPNSTRQYMTLQNGKSRFCEKCQEYKCDRSHHCSQCNKCILRMDHHCMWFKNCVGFRNHKFFFLECFYLNLYSICVLYSTFVAITKTFTAEGANISAIYLVFWGFLFAFAVGMSIVMTAFTFYHTSLLIHNLSTLESMSSSWSRYTHSTQPFNVGWYENWCQIMGKSPFLWLLPFPNSIGEGVEYPLNANALPYLPQTEEKNDKLYKSSVPASIAGAEGWSSDEEQYAMKNRRWNPHMGQYEWIEDFLV O14353 BPL1_SCHPO CATALYTIC ACTIVITY: Reaction=apo-[methylmalonyl-CoA:pyruvate carboxytransferase] + ATP + biotin = AMP + diphosphate + H(+) + holo-[methylmalonyl-CoA:pyruvate carboxytransferase]; Xref=Rhea:RHEA:23668, Rhea:RHEA-COMP:10508, Rhea:RHEA-COMP:10509, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.9; CATALYTIC ACTIVITY: Reaction=apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]; Xref=Rhea:RHEA:11204, Rhea:RHEA-COMP:10511, Rhea:RHEA-COMP:10512, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.10; CATALYTIC ACTIVITY: Reaction=apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]; Xref=Rhea:RHEA:24376, Rhea:RHEA-COMP:10514, Rhea:RHEA-COMP:10515, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.11; CATALYTIC ACTIVITY: Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.15; SPBC30D10.07c; CHAIN 1..631; /note="Biotin--protein ligase"; /id="PRO_0000315970" MNVLIYNGNGASKICLLRTFQSLLPFVVPLYAMRFVDASTLEKEPWPASTALLVMPGGRDMGYCSSFNETIYRKITDFVKRGGAYLGLCAGGYFGSAVVDFRMPDSDLNVVGKRKLQFFPGTCAGPTFPGFTYDSEDGARRASIIVDGMQSSPVHTHIYFNGGGSFLETENYSNVKVVARYQETDFEKSAAIIYVKVGKGNVVLTGIHPEFSAEGSPILDKRDEKTRLELLSYILKLLGLKVPKDTSKCGQPTLTDQYLFPNNVETKRFIEKALTNKVKNQDEDTLYTFQFSDISSEIPEHQLANLDISADLSDSDNEIVKIWYGDEEKICKKAKPSFDLELYAKLINGCRFGLPIIVAPVIRSTQTLLDKNYRFLDSTNTGFTVLGNYQTAGRGRGQNMWVSPYGTLAFSFIINVDAKNFSTTPIALFQYLMALAVVRGIREYAPGYENIPAFIKWPNDVYVRVDKGGINFQGKQYMKLSGIIVTSNYRKNVLHLVVGCGINVSNLGPTVSLNTLVDEWNKNSDNPRLEKFSFEKLLASVLNQFDRYHRLLLEEGFSLILPEYYQYWLHSNQTVNLASGGKAIIQGITSDFGFLLAQLLNENNEPTTKVVHLQPDGNSFDLMRNLITRKT O14360 NAF1_SCHPO MOD_RES 361; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC30D10.15; CHAIN 1..516; /note="H/ACA ribonucleoprotein complex non-core subunit NAF1"; /id="PRO_0000116502" MYPHLPCKIPGLSLIYDDESKVEKSKQLSTNASSSNFVKEDQIPSNLSIDNINTPQGDPIDKNNLNTNTENNLPNIVNFQNISSANSGEIKQKDNEILFSSTEDINQHKENYQDENKIDLLDVALANPKDCVVPSSGLLMPKEEFISNEEVGIPATNSSEKSNVKIADEIAEVTHSNSSIGKSSADLSSDSSSDSESNTSFSETDVEEEKAEEKSDAESMAPSTPPKTVNELPEQIYEKPEIVLQPNSLIEPLGKIIQVLKREVVVKSDIDDEKIVFDEKTVLCFEDRSIIGYIHETFGPVSSPYYIVRFSTEEECSAINACMGRPVFYVPTMANKIDPEPLKYIKGSDASNVYDEEINPSEQEFSDDEAEVAAKQLKKKRKRKAKSMVSGNQALPGEANFQSLNQNNVRNYPFYQTNQGSNPPAKRFTQEPPSSSLYSLSESSINYSTQSPMYYNYNYPQPSFPPFHPIYNDSIGYYSQANPQMYYANQVSAPPPQGSFDPNSKFYRNSSDSYRK O14362 SMI1_SCHPO MOD_RES 500; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC30D10.17c; CHAIN 1..504; /note="Cell wall biosynthesis/cell cycle regulator smi1"; /id="PRO_0000209877" MSKNSFSSMANSVTSFFQSLTTPNRHADPSFRPSRREKQSRLPTPLQSVAASAYSGVNASQTGLLNDSRANSVTNLPNSSNTSQVGLNNISPAPVGYVPGSKTNELANNSMEMQEISPNGSASLPPPVSESWRRIDRWAEENYYELYCQLCYGATVADVDSLEYELECTLPRDVRESLYIHDGQDRGGQPTGILFGVTLLDIEEIEEESELWRRVAQSYAEATLAGKIDQAVASRQASFPPGAVQCVYAHPGWIPLAKDFVGNNIAIDLAPGPAGQWGQVILFGRDQDTKYVVARSWADFLAIVAYDMENGKWLVDEDDNSLRLIYGPPREQWSYLDILKYRARKAERRKFKKRDGKRTTRPIPKSIAKEDVTNSANSTAPSTGTTVLDDGLDNNYEDIPLYGPSKDEELIKKEELEADTDLGLINTSEINQPANLPDEPTAETSNPVSATTVEAVTTTADNKDEEKNDHVTEDVSQNSTIAEASSLQAQEEEKEIETTSVKQE O14459 RPB7_SCHPO SPACUNK4.06c; CHAIN 1..172; /note="DNA-directed RNA polymerase II subunit rpb7"; /id="PRO_0000073992" MPFFLKELSLTISLHPSYFGPRMQDYLKAKLLADVEGTCSGQYGYIICVLDSNTIDIDKGRVVPGQGFAEFEVKYRAVLWRPFRGEVVDAIVTTVNKMGFFANIGPLNVFVSSHLVPPDMKFDPTANPPNYSGEDQVIEKGSNVRLKIVGTRTDATEIFAIATMKEDYLGVL O14460 EF2_SCHPO BINDING 26..33; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 104..108; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 158..161; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 568; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 574; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 699; /note="Diphthamide"; /evidence="ECO:0000250" SPAC513.01c;SPCP31B10.07; CHAIN 1..842; /note="Elongation factor 2"; /id="PRO_0000091023" MVAFTPEEVRNLMGKPSNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGDARFMDTRADEQERGVTIKSTAISLFAEMTDDDMKDMKEPADGTDFLVNLIDSPGHVDFSSEVTAALRVTDGALVVVDTIEGVCVQTETVLRQALGERIRPVVVVNKVDRALLELQISQEELYQNFARVVESVNVVISTYYDKVLGDCQVFPDKGTVAFASGLHGWAFTVRQFANRYAKKFGIDRNKMMQRLWGENYFNPKTKKWSKSATDANGNSNQRAFNMFILDPIYRIFDAVMNSRKDEVFTLLSKLEVTIKPDEKELEGKALLKVVMRKFLPAADALMEMIVLHLPSPKTAQQYRAETLYEGPMDDECAVGIRNCDANAPLMIYVSKMVPTSDRGRFYAFGRVFSGTVRSGLKVRIQGPNYVPGKKDDLFIKAIQRTVLMMGSRIEPIEDCPAGNIIGLVGVDQFLVKSGTLTTSEVAHNMKVMKFSVSPVVQVAVEVKNGNDLPKLVEGLKRLSKSDPCVLCTTSESGEHIVAGAGELHLEICLKDLQEDHAGIPLKISPPVVSYRESVSEPSSMTALSKSPNKHNRIFMTAEPMSEELSVAIETGHVNPRDDFKVRARIMADEFGWDVTDARKIWCFGPDTTGANVVVDQTKAVAYLNEIKDSVVAAFAWASKEGPMFEENLRSCRFNILDVVLHADAIHRGGGQIIPTARRVVYASTLLASPIIQEPVFLVEIQVSENAMGGIYSVLNKKRGHVFSEEQRVGTPLYNIKAYLPVNESFGFTGELRQATAGQAFPQLVFDHWSPMSGDPLDPTSKPGQIVCEARKRKGLKENVPDYTEYYDRL O14466 DPM1_SCHPO BINDING 9; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 11; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 13; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 40; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 42; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 95; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 96; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 97; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 97; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 97; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 124; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 160; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 211; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3"; BINDING 217; /ligand="GDP-alpha-D-mannose"; /ligand_id="ChEBI:CHEBI:57527"; /evidence="ECO:0000250|UniProtKB:Q8U4M3" CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl phosphate + GDP-alpha-D-mannose = a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83; Evidence={ECO:0000250|UniProtKB:O60762}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Note=Binds 1 divalent metal cation. {ECO:0000250|UniProtKB:Q8U4M3}; SPAC31G5.16c; CHAIN 1..236; /note="Dolichol-phosphate mannosyltransferase"; /id="PRO_0000059173" MSKYSVLLPTYNERKNLPIITYLIAKTFDQEKLDWEIVIIDDASPDGTQEVAKELQKIYGEDKILLKPRSGKLGLGTAYIHGLKFATGDFVIIMDADFSHHPKYLPEFIKLQKEHNYDIVLGTRYAKDGGVYGWNLKRKFISRGANLLASTVLGTGVSDVTGSFRLYKKPVLETLMSEVTSKGYVFQMEIIARAREHNYTIGEVPIAFVDRLYGESKLGMDDILGYLKGVFSLLFI O36014 DNPEP_SCHPO BINDING 87; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 162; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 256; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 256; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 292; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 293; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 337; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 337; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 340; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 365; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 372; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 431; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.; EC=3.4.11.21; Evidence={ECO:0000269|PubMed:20044953}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; SPAC4F10.02; STRAND 39..41; /evidence="ECO:0007829|PDB:7DDE"; STRAND 56..61; /evidence="ECO:0007829|PDB:7DDE"; STRAND 65..71; /evidence="ECO:0007829|PDB:7DDE"; STRAND 81..87; /evidence="ECO:0007829|PDB:7DDE"; STRAND 92..103; /evidence="ECO:0007829|PDB:7DDE"; STRAND 106..116; /evidence="ECO:0007829|PDB:7DDE"; STRAND 127..136; /evidence="ECO:0007829|PDB:7DDE"; STRAND 142..156; /evidence="ECO:0007829|PDB:7DDE"; STRAND 182..185; /evidence="ECO:0007829|PDB:7DDE"; STRAND 196..198; /evidence="ECO:0007829|PDB:7DDE"; STRAND 218..220; /evidence="ECO:0007829|PDB:7DDE"; STRAND 227..236; /evidence="ECO:0007829|PDB:7DDE"; STRAND 241..244; /evidence="ECO:0007829|PDB:7DDE"; STRAND 249..254; /evidence="ECO:0007829|PDB:7DDE"; STRAND 273..276; /evidence="ECO:0007829|PDB:7DDE"; STRAND 282..290; /evidence="ECO:0007829|PDB:7DDE"; STRAND 298..301; /evidence="ECO:0007829|PDB:7DDE"; STRAND 332..336; /evidence="ECO:0007829|PDB:7DDE"; STRAND 352..354; /evidence="ECO:0007829|PDB:7DDE"; STRAND 362..365; /evidence="ECO:0007829|PDB:7DDE"; STRAND 370..372; /evidence="ECO:0007829|PDB:7DDE"; STRAND 393..396; /evidence="ECO:0007829|PDB:7DDE"; STRAND 419..424; /evidence="ECO:0007829|PDB:7DDE"; STRAND 426..429; /evidence="ECO:0007829|PDB:7DDE"; STRAND 432..439; /evidence="ECO:0007829|PDB:7DDE"; STRAND 460..464; /evidence="ECO:0007829|PDB:7DDE" HELIX 5..17; /evidence="ECO:0007829|PDB:7DDE"; HELIX 22..35; /evidence="ECO:0007829|PDB:7DDE"; HELIX 119..122; /evidence="ECO:0007829|PDB:7DDE"; HELIX 165..167; /evidence="ECO:0007829|PDB:7DDE"; HELIX 186..188; /evidence="ECO:0007829|PDB:7DDE"; HELIX 204..215; /evidence="ECO:0007829|PDB:7DDE"; HELIX 224..226; /evidence="ECO:0007829|PDB:7DDE"; HELIX 258..270; /evidence="ECO:0007829|PDB:7DDE"; HELIX 306..315; /evidence="ECO:0007829|PDB:7DDE"; HELIX 323..329; /evidence="ECO:0007829|PDB:7DDE"; HELIX 344..349; /evidence="ECO:0007829|PDB:7DDE"; HELIX 376..389; /evidence="ECO:0007829|PDB:7DDE"; HELIX 409..416; /evidence="ECO:0007829|PDB:7DDE"; HELIX 440..454; /evidence="ECO:0007829|PDB:7DDE"; HELIX 456..459; /evidence="ECO:0007829|PDB:7DDE" TURN 2..4; /evidence="ECO:0007829|PDB:7DDE"; TURN 48..50; /evidence="ECO:0007829|PDB:7DDE"; TURN 62..64; /evidence="ECO:0007829|PDB:7DDE"; TURN 161..163; /evidence="ECO:0007829|PDB:7DDE"; TURN 175..178; /evidence="ECO:0007829|PDB:7DDE"; TURN 255..257; /evidence="ECO:0007829|PDB:7DDE"; TURN 292..295; /evidence="ECO:0007829|PDB:7DDE" CHAIN 1..467; /note="Aspartyl aminopeptidase 1"; /id="PRO_0000173454" MTATAKSCALDFLDFVNASPTPYHAVQNLAEHYMSHGFQYLSEKSDWQSKIEPGNSYFVTRNKSSIIAFSIGKKWKPGNGFSIIATHTDSPTLRLKPKSQKSAYGYLQVGVEKYGGGIWHTWFDRDLSLAGRVMVEEEDGRVIQYNVHIDRPLLRIPTLAIHLDPSANSSFSFNMETEFVPLIGLENELAKEETSDNGDKYHHPVLLSLLANEISKSLETTIDPSKIVDFELILGDAEKARLGGIHEEFVFSPRLDNLGMTFCASQALTKSLENNSLDNESCVRVVPSFDHEEIGSVSAQGAESTFLPAVLQRICELGKESSLFSISMVKSFLVSADMAHAMHPNYSSRYENSNTPFLNKGTVIKVNANQRYTTNSAGIVLLKKVAQLADVPIQSFVVRNDSPCGSTIGPKLAAMTGMRTLDLGNPMLSMHSCREMCGSKDFEYAVVLFSSFFQNFANLEEKIIIDE O36022 MNN9_SCHPO SPAC4F10.10c; CHAIN 1..337; /note="Mannan polymerase complex subunit mnn9"; /id="PRO_0000316855" MRVYNKSRIVGQLLFVALGITFIYYLFTPSVNSNAKVQIENRGGNSYEIYDMNKITESSDPIRNKEEVLILTPIARFYPQYWKNLLELDYPRNLISLGFIVPSSKDGAKVHRELRNAINAVQKGPGDKRFADVKILIQDSDLSSGQSEAERHKFSAQKERRGKLAATRNTLLLSTLKPSTSWVLWLDSDIVETPSTLIQDLAEHNEDVLVANCFQKQGDKLTPYDFNSWVDSQTAQELASHMDRDEILLEGYAELPTYRMLMAKIYEEHKDPSTIMALDGVGTTALLVKASVHRDGALFPTFPFYHLIESEGFAKMAKRLGHGVYGLPYYLVFHHNE O36024 CENPL_SCHPO SPAC4F10.12; CHAIN 1..280; /note="Inner kinetochore subunit fta1"; /id="PRO_0000116724" MTLRDHHFYNVTYTAYRLSPLFGFEYSNLTEIGKKLTRFLRYGTDRTGYFTNSTRFADLIIEKATFTEFGNTSSFPKFLKLDISYETSSDLEVKRKGQMFFFESFRKFSHAEADRTRLSLEGNSVFFSLALVRMDGALWMAVEQFLQQEFDTQILPCLIAPEILLEFLKIWQNHVNSQTALPLELTWTTGNPNLSSVTISIRPEDLKKIFRSSSFFYPILMEHIKRCTSLDLTNSVFSLSKVNTDCAILTSSGKLKIFSKAQNIVFDVLLALEPMQLPEY O42643 PRP22_SCHPO BINDING 533..540; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC10F6.02c; CHAIN 1..1168; /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase prp22"; /id="PRO_0000055134" MDDLKELEYLSLVSKVASEIRNHTGIDDNTLAEFIINLHDQSKNYDEFKNNVLSCGGEFTDSFLQNISRLIKEIKPKDDIPTDNVNNGSNSVNGASHDLDSKDVDKQHQRKMFPGLSIPNSTNNLRDRPALMDNAMDELEELSTLAKTRRNDRDSRRDERHYLNGIRERRERSISPSFSHHSRTSISGQSHSSRSSRGPLLNAPTLYGIYSGVVSGIKDFGAFVTLDGFRKRTDGLVHISNIQLNGRLDHPSEAVSYGQPVFVKVIRIDESAKRISLSMKEVNQVTGEDLNPDQVSRSTKKGSGANAIPLSAQNSEIGHVNPLETFTSNGRKRLTSPEIWELQQLAASGAISATDIPELNDGFNTNNAAEINPEDDEDVEIELREEEPGFLAGQTKVSLKLSPIKVVKAPDGSLSRAAMQGQILANDRREIRQKEAKLKSEQEMEKQDLSLSWQDTMSNPQDRKFAQDVRDSAARQLTSETPSWRQATRNANISYGKRTTLSMKEQREGLPVFKLRKQFLEAVSKNQILVLLGETGSGKTTQITQYLAEEGYTSDSKMIGCTQPRRVAAMSVAKRVAEEVGCRVGEEVGYTIRFEDKTSRMTQIKYMTDGMLQRECLVDPLLSKYSVIILDEAHERTVATDVLFGLLKGTVLKRPDLKLIVTSATLDAERFSSYFYKCPIFTIPGRSYPVEIMYTKQPEADYLDAALMTVMQIHLSEGPGDILVFLTGQEEIDTSCEILYERSKMLGDSIPELVILPVYSALPSEIQSRIFEPAPPGGRKVVIATNIAETSLTIDGIYYVVDPGFVKQSCFDPKLGMDSLIVTPISQAQARQRSGRAGRTGPGKCYRLYTESAYRNEMLPSPIPEIQRQNLSHTILMLKAMGINDLLNFDFMDPPPAQTMIAALQNLYALSALDDEGLLTPLGRKMADFPMEPQLSKVLITSVELGCSEEMLSIIAMLSVPNIWSRPREKQQEADRQRAQFANPESDHLTLLNVYTTWKMNRCSDNWCYEHYIQARGMRRAEDVRKQLIRLMDRYRHPVVSCGRKRELILRALCSGYFTNVAKRDSHEGCYKTIVENAPVYMHPSGVLFGKAAEWVIYHELIQTSKEYMHTVSTVNPKWLVEVAPTFFKFANANQVSKTKKNLKVLPLYNRFEKPDEWRISKQRKGGR O42644 PYRG_SCHPO ACT_SITE 403; /note="For GATase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 532; /note="For GATase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 534; /note="For GATase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; SPAC10F6.03c; CHAIN 1..600; /note="CTP synthase"; /id="PRO_0000138282" MKYVLVSGGVISGIGKGVIASSTGLLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGEVFVLNDGGEVDLDLGNYERYLNVTLTHDNNITTGKVYSNVIQKERRGDYLGKTVQIVPHVTNEIQDWVERVARIPVDQSGEEPDVCIVELGGTVGDIESAAFVEAMRQFQFRVGHENFVSIHVSLVPVINGEQKTKPTQQAIRDLRSLGITPDLIACRCKQPLEKSVIDKISLFCHVGPEQVLAVHDVSSTYHVPQLLEDKLLEYLKIRFALDKISVSRELALAGENMWSSWKHLTQGYDHLFKKVTIVLVGKYTHLQDSYISVIKALEHSAMRCGRKLDLQWVEASHLEASTNTSDPLSYHKAWHLVCSANGILVPGGFGSRGVEGMIAAAKWARENNTPYLGICLGMQVAVIEFARSVCGIEGAFSEEFDKECENNVVVYMPEIDKDKLGGTMRLGLRPTFFQPNSEWSKLRKLHKMVDEVLERHRHRYEINPAFVSRLEQGGISFIGKDERGERMEIIEKRDHPYFVGVQYHPEYLSKPLKPSPPIFGLVAASAGLLDEFIQSGEEVEWSNFSHFNAESALADMNDSVEVTEEATVVTIS O42646 UBC6_SCHPO ACT_SITE 87; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388}; SPAC10F6.05c; CHAIN 1..227; /note="Ubiquitin-conjugating enzyme E2 6"; /id="PRO_0000082551" MASKGAYKRLMKEYLALQKNPVELVDAKPATENILEWHYIITGPPDTPYEGGQYHGTLIFPPDYPFKPPAIRMITPSGRFQTNTRLCLSFSDFHPKSWNPSWMVSTILVGLVSFMTSDEITTGGIVTSESTRRTYAKDTKRFNIMDNPKFLIMFPELIDKNREDIAKAAAEAALIEPQQIHSTPVSSNECKKNEPFNSKQSWVKSRWSIAVLVFFALALARFFGADS O42650 RIO1_SCHPO ACT_SITE 265; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q9BRS2, ECO:0000255|PROSITE-ProRule:PRU10028"; ACT_SITE 282; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:Q9BRS2" BINDING 148; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9BRS2"; BINDING 220; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9BRS2"; BINDING 270; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9BRS2"; BINDING 282; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9BRS2" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; SPAC10F6.10; CHAIN 1..497; /note="Serine/threonine-protein kinase rio1"; /id="PRO_0000317085" MVEELKNDAQTNEEESEYSDFSDGSDNDYFREDDIDWNQASSNYSARQENFGNNSSKINSVNDHVSTLSRYVNNIKLNDRFEAEDKSSIKDKSDRATSEQVLDPRTRMILLKLINNGTISEINGCISTGKEANVYHATNEDGKHFAIKIYKTSILVFKDRDRYVSGEFRFRHGYNKRNPRKMVRLWAEKEIRNLKRVAAAGIPCPEPILLKQHVLLMSFLGDKKGWAYPKLKDIDMTPGEATKLYQLVARNMRILFHVCHLVHADLSEYNLLYHKGKVYFIDVSQSVEHDHPQSIDFLRMDILNISTFFRRLNAGCLSLPQLFKFITEEGSCEKEAMKTRLNAIYEEEPTTEEYEEEFLKTYVPRTLDEVYDIDRDTEIVNAGGVNSLVYKHLLNTDFQKLDLNDTTKNQNDQILPNETSESDDDANSISSMENEEERTSDSKSSAKQGKGNGRAKETPEEKRARKKKTKEDKAEKRKSKIPKYEKKRKLKQSGRKK O42651 ATG17_SCHPO SPAC10F6.11c; CHAIN 1..411; /note="Autophagy-related protein 17"; /id="PRO_0000124564" MELLQQWTQQAKAALTQARQLCGDAHKFNEDAKTDLRNSIKQHQQLKELAKLTASQCTRLDSSTALIKQLLDLVQNYPTFNQLNVLHDRLESSLKRLRDCTLDPALGSEYTNLYAFVDDTALEDLKTRLRGVTDGVWNAFEKLAGLLEEDLCANYHKRLEAVSLDFLPPAYNDTAEELADLLLQVAQHYDQCSEALNIYDTLSDAEKKDLQEVLQSDSNHVPSVLTELRSGLDQTIHYFNAVQSYKSKVDSATSILEALAEELNKNQLTNQRHEAAHELMRAQTGLEIPQLAQELVQLERHYTHFAKAYTALLQEIHRRQTYENCVRSIVDEFVGRLEKEQQAEAKCRIDFFNQYGDYLPQTLWGAVTDPPLHFEIIEHQYTELPNVKVIPDKNDKKSKQREKSSTTASKR O42652 AATC_SCHPO BINDING 38; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 138; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 191; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 383; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P23542}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P23542}; MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250|UniProtKB:P23542"; MOD_RES 255; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250"; MOD_RES 385; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P23542" SPAC10F6.13c; STRAND 100..106; /evidence="ECO:0007829|PDB:6JPK"; STRAND 131..136; /evidence="ECO:0007829|PDB:6JPK"; STRAND 152..156; /evidence="ECO:0007829|PDB:6JPK"; STRAND 182..186; /evidence="ECO:0007829|PDB:6JPK"; STRAND 215..221; /evidence="ECO:0007829|PDB:6JPK"; STRAND 247..252; /evidence="ECO:0007829|PDB:6JPK"; STRAND 264..270; /evidence="ECO:0007829|PDB:6JPK"; STRAND 355..359; /evidence="ECO:0007829|PDB:6JPK"; STRAND 383..385; /evidence="ECO:0007829|PDB:6JPK" HELIX 6..8; /evidence="ECO:0007829|PDB:6JPK"; HELIX 16..26; /evidence="ECO:0007829|PDB:6JPK"; HELIX 51..62; /evidence="ECO:0007829|PDB:6JPK"; HELIX 77..87; /evidence="ECO:0007829|PDB:6JPK"; HELIX 93..96; /evidence="ECO:0007829|PDB:6JPK"; HELIX 107..122; /evidence="ECO:0007829|PDB:6JPK"; HELIX 124..127; /evidence="ECO:0007829|PDB:6JPK"; HELIX 140..147; /evidence="ECO:0007829|PDB:6JPK"; HELIX 167..176; /evidence="ECO:0007829|PDB:6JPK"; HELIX 199..211; /evidence="ECO:0007829|PDB:6JPK"; HELIX 230..233; /evidence="ECO:0007829|PDB:6JPK"; HELIX 235..241; /evidence="ECO:0007829|PDB:6JPK"; HELIX 260..262; /evidence="ECO:0007829|PDB:6JPK"; HELIX 274..289; /evidence="ECO:0007829|PDB:6JPK"; HELIX 297..308; /evidence="ECO:0007829|PDB:6JPK"; HELIX 310..340; /evidence="ECO:0007829|PDB:6JPK"; HELIX 349..352; /evidence="ECO:0007829|PDB:6JPK"; HELIX 364..374; /evidence="ECO:0007829|PDB:6JPK"; HELIX 386..388; /evidence="ECO:0007829|PDB:6JPK"; HELIX 394..407; /evidence="ECO:0007829|PDB:6JPK" TURN 88..90; /evidence="ECO:0007829|PDB:6JPK"; TURN 160..163; /evidence="ECO:0007829|PDB:6JPK"; TURN 191..193; /evidence="ECO:0007829|PDB:6JPK"; TURN 223..227; /evidence="ECO:0007829|PDB:6JPK"; TURN 254..256; /evidence="ECO:0007829|PDB:6JPK"; TURN 290..292; /evidence="ECO:0007829|PDB:6JPK"; TURN 391..393; /evidence="ECO:0007829|PDB:6JPK" CHAIN 2..409; /note="Aspartate aminotransferase, cytoplasmic"; /evidence="ECO:0000250|UniProtKB:P23542"; /id="PRO_0000309451" MSDYGFANIEEAKADAIFKLNAQYHQDEDPKKVNMSVGAYRDDTGKPWILPAVKKASKIVEEQASFNHEYLPIAGLPRFTKAAAEVLFRPNPHLLSEDRVASMQSVSGTGANFLAASFIETFYVKHTGAHVYISNPTWPVHRTLWEKLGVTVDTYPYWDAKNRSFDYEGMLSTIKSAPEGSIFLLHACAHNPTGIDPTREQWLSIFESLLSRKHLVVFDIAYQGFASGDLNRDSWALNEFVKYNKDFFVCQSFAKNMGLYGERTGCMHYVAKDASTKNKVLSQLCIVQRNTISNPPAYGARIAAEILNSPQLFAEWEQDLKTMSSRIIEMRKRLRDSLVALKTPGSWDHITQQIGMFSFTGLTPAQVQFCQERYHLYFSANGRISMAGLNNSNVEHVAQAFNHAVRELP O42658 PHS_SCHPO CATALYTIC ACTIVITY: Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin = (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920, ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96; SPAC27D7.04; CHAIN 1..96; /note="Pterin-4-alpha-carbinolamine dehydratase"; /id="PRO_0000063063" MNTSARLLALVSKSKNNWILQQGDTKLFKSFRFKNFIEAWGFMSCVALRAQQLNHHPEWTNVYNKVDITLTTHDTKGLTEKDLKLAEFIDTLAKDN O42659 APC14_SCHPO SPAC27D7.05c; CHAIN 1..107; /note="Anaphase-promoting complex subunit 14"; /id="PRO_0000058047" MDPFAGTGQSKSYRTFGNVFQRLSMSGNPKPLAKKPLLLPEASKAIEFWNYRDVIGGEEAEQERNERASRIAISRIASSRSSIPEYRQAIMQHLTKHVQQLDQLAEW O42666 BUT1_SCHPO SPAC27D7.12c; CHAIN 1..243; /note="Uba3-binding protein but1"; /id="PRO_0000065025" MEIDQNLFQFPISTRDAVHEKNCTLRVKSTKKRRSSTKDEETRGMHPHIKSSFRNGMNHARVIREEDMEVVFEPCFINLSKPVYVVNGIGGINEIHKLPILFSSFVLCFFGNVSGDYGYVDNVPLHISVISHFYPCLQSYNTDVIGITTDTVENICQWKAHLPRALQFSLPVISDSNNEICREMGMLHPLGGAKLALDAIVIIDSIGRRRDILPIRTTTCVSTLITAVQETVRFLAIENGRLL O42839 APC4_SCHPO SPAC19G12.01c; CHAIN 1..719; /note="Anaphase-promoting complex subunit 4"; /id="PRO_0000050949" MVSKSFKYPKKHKFEWINETNRVERVGSGLKRVILCPSMELIAILTCSNHLICCRSNSQRIWDVDFHDLEATELCWNHDGNLIVVGFKNGELKIIDSSTGHLVEQRPASRDLAVLMITWAMQETIVNEKRNDFLFDATAYMPLLGTLPSSAKEERIFSSKAIAQFFEPRKREGENNKKVELLSILDERGIRYINMFSSYKIGESDSLKSALNLGVPISHSITNDLAYHVLICKGGTNISLKTLYMPLLKNDLGSIVDIATMSTRMQHLVRYLEEVLNAMYEEFDNVFKSEASFIKTFDALVSKYSDTTFFSLQLELYQFIMNGIPSDLLKEWINERVGDRVLKNWERAMVNSYTSLIIFCQEFVIPACERLTVLLSSARGKSIWGHMKGNTLLDAKLVEDCLATLGYLQNNVFSFLNCLFEEKKYMKHFISWLNYAIVEFNTSEPSSIPPQEIIEHINETVIYIRHSLFRSKLTSYFMGTKPLQLRDPDYYSLKDFANQDDSNSVDDFVSFKTLKESLRDSFNVIFSYPSLTCQKQWLKTGDLVLFEGTDWNVSSLIPKSCNEKNQLFSLFFRKDTPNIFLIISQLMENTMLPVSGCHFGLDYAELLGSSLLDFQPATVLDMKLLNGSSILILGKLKEKCFLCEICLADVPLTFFEHQQKNSYLDAISHLPFIPLNSCLWLHEFEKDFLPSTLEYALSENSDYGVLISRESSRYRLFSF O42842 APT_SCHPO BINDING 130..134; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC23A1.03; CHAIN 1..188; /note="Adenine phosphoribosyltransferase"; /id="PRO_0000227902" MSDDRINYLKNKLVQYPDFPKKGILFEDIMPIFQDPRAFGILIDLLLEAVETEFNNIDVIVGLEARGFLFGPTLALRANCAFVPVRKPNKLPGDLVVVSYNKEYSTDSFAIQKGTIKPGQRVLIVDDILATGGTALAADELVTRLGGELVGHLFLLELTFLQGRKRLMAPTYTLLTGQDEAPDGSEFA O42848 RL16A_SCHPO MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23A1.11; CHAIN 1..197; /note="Large ribosomal subunit protein uL13A"; /id="PRO_0000133788" MSEFQKVVVIDAKGHLLGRLASVVAKQLLGGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFQKAVRGMLPHKTARGQAALEHLQAVEGIPPPFDKQKRVVVPAALRVLRLKPGRKYCTVGRLSSEVGWKYSDIVSKLEERRKVKSAAFYQAKLAKQKKIASAKAASSVNGKLAEFGY O42869 YF75_SCHPO MOD_RES 129; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 167; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 168; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 182; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 184; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 513; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 555; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G9.05; CHAIN 1..659; /note="Uncharacterized protein C3G9.05"; /id="PRO_0000351068" MQSIIIRQYRFLARYLEPEFVKDPALRNANARPREKLQRLSHIQFSELLTDVADELQRRINNDPKVRFLPPVDSYHPKRNHARQKLSSLAPTRLRDLCMDVFFEVQSRYSGALKEVSSNTPPNMTRAASQPPPQVQRLPASAPKHDLYSSANASSASLHPTEQRTTSSPTIPSYANRTHTDSPTSLSHRLPNVPDTNALNTVQANNSSTSSLSQGAQTGIDSSSNYLSRIEMLESSLAKSNSLLDSSKSEMEALKAKSISDATKHKNEIFQLEEKLHEASHEAEISIKKLNDAENRIKELENNPTLSFNPELEKNLKLMQELIVAESSKTQHIVELESCIDSLKAETERWKKVAINAKSAKIDEDIRLFTMTTVPMKSIRELISPNGFLDEQLYIRYFVEMNVFVASLRRDSPSQWMSTAKDIALTLEAIVSSLREKSLLEELPDLGKKVDDLCSFTNSLMEQVRLAVINGALLPIYHVDASACSISISLMDIAKTYGLTNTGKSSLSVGRNSLHPVDDLKALSVAKTLLSEKSKQFSETNQKLLDAISSDSSSSTIQQRVHEDINVIRDTLFDVSSPLELMRDRAAYAVIHNALQEMRRYCMQLIEQEGHGENFGFTDNNSVPPLTDLAFSAAKCFKDILRAIEDAEFSVQRTQFSTR O42871 ING1_SCHPO BINDING 231; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 233; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 244; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 249; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 255; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 258; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53"; BINDING 274; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9UK53" SPAC3G9.08; CHAIN 1..283; /note="Chromatin modification-related protein png1"; /id="PRO_0000362154" MADDTAYILSEYLQTLDNVPNETKHIFDEISVKEVAVHDIWKRIQAADSQIQSYIKSHGSLTPHPKEDALYSTIREEYQKAINIQNEKVQLADRARLGLTRHIKRLDDRLAKAGHGFTAAELLNAPDYYASSPYGGYSPSGASSARQTPAPSRSGASTAGRRRTSATTRGAIQNGVYHSPYTASLADSGSTRGQKVSNATATTQLETKADSTTPNEMVSEEDMEEDNEKYCFCQQGSYGQMVACDNANCEREWFHMECVGLKAPPEGTWYCEACRDQKLVDAK O42890 CAO2_SCHPO ACT_SITE 309; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P12807"; ACT_SITE 394; /note="Schiff-base intermediate with substrate; via topaquinone"; /evidence="ECO:0000250|UniProtKB:P12807" BINDING 307..318; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P12807"; BINDING 391..396; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P46883"; BINDING 445; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:P12807"; BINDING 447; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:P12807"; BINDING 593; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q43077"; BINDING 594; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:Q43077"; BINDING 604; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:P12807" CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q43077}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077}; PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}. MOD_RES 394; /note="2',4',5'-topaquinone"; /evidence="ECO:0000250|UniProtKB:P12807" SPBC1289.16c; CHAIN 1..794; /note="Copper amine oxidase-like protein cao2"; /id="PRO_0000064107" MAEESKAAEYFDPLDPLSFNELRYVVNLVRKSYPEKQISFDVVTLSEPHKEEYVHWRYSSAHEGIPDRRAYVIVLEKEVPGVFEGIVNLTTGKIEKWEHSVDTCPIITADLLAITDEIVRNDANVIEQCKICGVPESGLSNVYCDPWTIGYDERYGSGRRLQQALMYYKPGDSGHLRSIPLDFCPIIDVDQKKVIAIDIPKVRRPIPQDVNSDNNLKKLEQEMEAMKMLKPLRITQPEGVNFRIKGRYIEWQNFCFHIGFNYREGIVLSDVVFNEDGHLRPLFYRISLTEMAVPFGAKGHSHHRKHAYDLGEYGVGYRTNPLSFTCGCEGVIHYMDADFVNYRGEITTIKNAISIHEEDDGVLFKYSDLRDRNANISARSIKLVVSQVFTAANYEYLVYWIFRMDGVIECEIRLTGILNTNAINEDEDLKGHGTQVYPKISAENHEHLFCLRINPMLDGLRNSVATVDALRDKNGTLVSKYIIPETVTEAISNYDSSTGRTWDICNLNKLHPYSGKPVSYKLISRDTSPVLSQPGTTNSDCSGFAENNIYVTPYMDDQIFPTGDYAPQASDDTPKGLSKWISDDPNAQIKNTDIVVWHTFGMIHFPAPEDFPIMPAESIHLFLQPRNFFKHNPALDTSSSVNSTSEATSPNTHHENLRDTSQKRESHSTPHDYEPHVSDKNDKSVEDKLHFVQKDESRPKEPVVDAAQKHEGRSETLAQPGQQNANQSEEKQGGQNGSNGGHHHHHHHHYITGHVYGGYHKHSGSGGHLVDMMKNISDVTHDFAMGNFRYHKYD O42894 RRP46_SCHPO SPBC115.01c; CHAIN 1..226; /note="Exosome complex component rrp46"; /id="PRO_0000139977" MNRIGILSRSDGSSEWKQGSARVICGVNGPIDVKIRDERLNKATVEVLVQPVSGVAETLEKMISSRIVGILEDAIFLNTYPRTLIQVSIQIIEEDGTDTLAAVINGAVLALLDAGISLKYIPCAINCHWKNKITQDEPDVDGTINKLESIITICYSISSEPAKLIFLETAGPIPEEDFFRVLETAPLHAEEVSKKMKELLFETYNESDGHENEKNPKEDVEMDVVA O42904 PRP31_SCHPO SPBC119.13c; CHAIN 1..518; /note="Pre-mRNA-processing factor 31"; /id="PRO_0000058588" MSLADELLADLDDIEETTESTITDELGPDAKKRRLELQLEEGNGISAELENDLDITKISDSAQKLPSEVANKFNDNNENIYQLLNSTRLRDIIEGTEKYKGTEKQAITGNIEDDLEYHLIVDSNSIAMEIDDEILRLHRLVKEWYHDRFPELSSLVLNAFDYCKTVSSLLNDLDNSKTKLSFLPSATVMVIATTATTTVGKPLPDEMIKNVKNCCEAIQQLGEEKQKIIEYVQSRISVVAPNLSAVVGSTTAANLIGIAGGLTRLGKFPACNLPALGKRRLTTIGINNPAVSGDYGFLYMSEIVQKTPPDVRKQAIRMTAAKVALAARIDSIHEYPDGSFGISARKEVERKIEKLLEPPSQKPTVALPVPDDRPKRRRGGRRIRKMKEQYAVTELRRLQNRVAFGKEEAEVFNFDETEGLGMLGQEGEGKIRAVSIDSRTKLRLPKARKAQLQSMAQKNPLAASGLQSSLSFTPIQGIELVNPLLQRQQKVEEANKWFRDGVFTQIKKDSNEPKNKFS O42905 RTI1_SCHPO SPBC119.14; CHAIN 1..371; /note="DNA repair and recombination protein rti1"; /id="PRO_0000173893" MGSLPDQSSCEEFTDSQQDKMTKLLAMQLGPEYISRRSGPGGGSVTYLEAWKAIELANEIFGFNGWSSSIQDIHVDYVEETKEKKFNVGISVIVRVTLKDGSFHEDVGYGSIENCRVKALAYEKCKKEGTTDALKRALRNFGSSMGNCLYDKRYIQKILKMAPAQAEFNYDNLLRANKRPYARFAQKVSTPIESHANKSVKLEHKNSIEKKISNVDKPISDLIENDIHESLPALQNPPIQSHSETDLYADEELDSILMHHERPPIPESPRVEEFEELLNQFEGDEKVSVDKIDAHDKMTEAQVVKIPPVQFMNARVAAAENPHIKHEGMAFQLHKKSNSILKSSNIDHNRSMPIRRPSLTSNNSANTFSTK O42913 NRM1_SCHPO SPBC16A3.07c; CHAIN 1..342; /note="Transcription factor nrm1"; /id="PRO_0000352812" MDRSMEPLTPSRLNTLGERPTNEVYEYGKGKNVQHLFPITPMQRPLGKENAAPGTISPIAVRSRNVRAVEIADENACEEPVLKIKSVSSTESEEEKESSTEIGEKQEKETHLEPKTPVQTNTNNNHLDDIQCCAKNLRLRLELAMYKVQVNQTFSPLQDLPIVAKTKLHNCPNSEPVTSIWNQRSLSSGKPPSLHLSGNRRLSMGSPTKSIYDQNGLTTPRPIGSDDLTHMYDPYTSPLRTPSRTLSRSSSHYLWVRHGKLTRSVSLLQHKTPRRIRPKSLSKSNSTPLKHLSAQKPNSNYYTGPPTPVSISNTPENIHPSSSEVRRIASHSKQFSDYGLIR O42914 OGA1_SCHPO PTM: Phosphorylation by TORC1 upon nutrient replenishment inhibits STM1 and causes its release from dormant ribosomes. {ECO:0000250|UniProtKB:P39015}. MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 160; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 166; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16A3.08c; CHAIN 1..284; /note="Ribosome-associated protein oga1"; /id="PRO_0000116512" MSVASKNLFDLLGEETPAATTTEKKTAASRDKKRSDSPPVPRELVAQSTTSRKRDPNQPTPRERTVNKKADQPRRRRQAPQGNEAFAREGKEARANNAAHPVDATGAPSNRRNARARRGREFDRHSQTGRVDTKKATERGWGDLVNSAANPDVAENEGNTPSGAQTPAAEEENVKTLDEYLSERKSAAKPVGRTVEKLENATKVEKSAPEELFASLKKSASQKKSAAKESKPKKVLLDIEQTFTARPARGGRPNRAPRRGPSETASKTQQAPPTLSETDFPALA O42918 AMY4_SCHPO ACT_SITE 461; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 143; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 395; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305}; SIGNAL 1..24; /evidence="ECO:0000255" SPBC16A3.13; PROPEP 751..774; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000255454" CHAIN 25..750; /note="Alpha-amylase 4"; /id="PRO_0000001356" CARBOHYD 143; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 187; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 214; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 243; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 272; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 299; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 326; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 355; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 382; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 52..60; /evidence="ECO:0000250"; DISULFID 229..314; /evidence="ECO:0000250"; DISULFID 495..539; /evidence="ECO:0000250"; DISULFID 690..724; /evidence="ECO:0000250" LIPID 750; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MKLSLKDLALSIILVLGVAPPVQALSAEEWKKQSVYNVMTDRFATSKVVPHCDVKAEKYCGGNWQGIVDHLDYIRDLGFTAISISPVVEQLEGPEYHGEAYHGHRPKNYYRLNPHFGNEEDLKELSDALHGKGMYLMVDVAINHTISEYFEDDYFKNTYFDKTHIDHKCKEHCSCHHDKFPRPVPHNGTKPDHKPWKHEEHCHHGKFPRPVPHNGTKPDHKPWKHEEHCSCHHDKFPRPVPHNGTKPDHKPWKHEEHCSCHHDKFPRPVPHNGTKPDHKPWKHEEHCHHGKFPRPIPHNGTKPDHKPWKHEEHCHHGRFPRPVPHNGTKPDHKPWKHEEHCSCHHDKFSRPVPHNGTKPDHKPWKHEEHCHHGKFLRPVPHNVTKPDHKPWKHEEHCHHGKFPRPVPHNGTKPDHKPWKHEEHCSCHEDHSVHERPSAKGALEDYIQTFVETFQIDGIRFDAMGDKYRKYWPDFCKAAGVFCMGDLKSSDSLKVCDWQNDLEGLSNFPVRESAVKAFLMNNPEGIVDLADKMTDMRGLCVNPLLLGNFVENKDLPRMASISSDPATLKNAIAFVLMGDGIPMMYNGQELAMRGEEVPYNRPAIWEKGFPKRNPYYKFTSTINRFRKAMIESKDGEAFLNMQSDISIVDKRILLLRRGKVITVLNNLGSYYIHFHYTVSAEEHKWMDVLSCKSVPVQDNRQVFMVRNGEPMILYPEESAYEMGLCPSPIQLTEDYNSEGSLSINVEEAQTSKAPEQNRGFTNVLAALLLSLLMIL O42923 CIP1_SCHPO PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:16407405, ECO:0000269|PubMed:18257517}. MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 41; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 49; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 397; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 401; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 427; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 431; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 435; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 456; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 466; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16A3.18; CHAIN 1..490; /note="RNA-binding post-transcriptional regulator cip1"; /id="PRO_0000255601" MPNEIFPWKIRVDESRGLAGNSGTKKSNHEALSRLQSPLNSPKLQPIGSPQASRKTSGSGSSAPLYPKWSGALSLASSRAASPAPSDSFPTFGYSQLGGLENSSKGSALFNSANSIGTPYLSSRNSNSANEASAMAFHNVSPPSGAESSSESKSFSASGKGNKADTSAEPSLDAFNSTQIKAGSTANSNSTPVEPGEDTIPTAIVVKNIPFSLEKDTLLDHFKQLGIPRPYAFNYHYDNGIFRGLAFANFYRPEEAQVVVQTLNGYEINGRRLRVEWKRQLPAAEREKVEKAKKRQAEERRRKQQYKMFEVSFTDQGLNLNDTGTLETYSRLLLFAHQCIPSREITFETTSKDGNLLNAIRIFCLYFDLDYYARPNGEVLKLVVTHPNKKNTSVSQSQPASPNLRFNMPAPLATRFLQEHSLNGTKSAPITPPPSFAVPLTNQLRSIDDKIYGNESPLQKASTLSSPFNSKNDNDASTSASKQSFGVSHF O42933 PMT4_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; EC=2.4.1.109; CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; EC=2.4.1.109; SPBC16C6.09; CHAIN 1..778; /note="Dolichyl-phosphate-mannose--protein mannosyltransferase 4"; /id="PRO_0000121500" CARBOHYD 40; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 335; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MASKSEKAVKKAQKLSKEPSVELTDTKSSDNVTPKQKSPNSTEEDVSLNLKTLKAKKFKLAFVLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKYFFDLHPPFAKLLLALVAKLAGYDGHYLFDNIGDNYKDNGVPYVTIRAWPALLSSLVPPVVFLIMKESGYDLLACIVSSSLVLFDNAHVTEGRLILLDATLLFSMVCAIYCYVRFFKLRHTPFSRPWWAWLFFTGFFLSCTISTKYVGFFTFLSIGLSVCLELWYLWDIKTGLTVERFFQHFLARFFCLIFFPFLFFLFWFYMHFNILTISGPGDSFMSLEFQETLSDNPITANSTILNYYDIVTIKHMGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPIEAKLNVPVKNMDYIKLHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAGKKHEYTLFQVVMSDNTDPQRPLYTKASSFKLIHKLTHVAMWSDPKPLPDWAFKQLEINGAKNIQTGSIFWTFDDIIGLKDSRLKKEKKIPKKLPFWKKYLELQLTMFRQNNMLTEFHPYSSNPSDWFTLHHGIAFWAKSEENKQIYLLGNPIGWWIIAGTVLSTTVVAAAEILLRQRGIRTLPETVRNHFYRSTMFFYMTYVFHYLPFFIMGRQLFLHHYLPAHLAGSLLVGAFIQLACRKSFRSPVSAGVPIPKDVDEKGHSKCHRKYGHVIELICTLLLIFVVIYCFTFFAPMTYGDKSLSVDEWTRRKWLDSWVFQYQKQN O42936 LAS1_SCHPO SPBC16C6.12c; CHAIN 1..470; /note="Pre-rRNA-processing protein las1"; /id="PRO_0000211560" MDMKVVPWRLKEDFLYLMSCFYNEGQEGIPDLAALFRGVEIIQAWSTRGRIPHSVESTSQLVSSLISNDRSQKLALAVSISRFVSGLLDPIQQSQYAIPMAVLAKSIDLPTYFVELRHAITHEELPSLPVLRQAAQRALSWLYDHYWNPAATAESEDTYDYTETNELHKFEIKRKVKDLLKQWRSWRKVNVSANMFLPVEEHDYIQQFEALVQELVTTANLRLPYIPASFVDDEKDLDFAIETTNLDIVVSCFLEKRVLIPSRTMPISFFPKLKNVWLPLLQSIASKHSFFLPALFTTLWSEILEISQTVDSLVFLDLKEKEELTDKESAGCYLAKWYAYLMREAYTGQPWTSTLSVTQTDLASVLEICLQRSDPFTKIIIDELSILDKELENKFSPLFQYRSDMFDSRILDEQEFEDITLEQMKTELNKFSVRLNNIEAQADSSTMEFQGHVWYKPSVEPSPIGQIIES O42939 UBA2_SCHPO BINDING 32..37; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 35..59; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 56; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 64..67; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 80; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 125..130; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 166; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 169; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 430; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 433; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" MOD_RES 559; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 563; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16H5.03c; CHAIN 1..628; /note="Ubiquitin-activating enzyme E1-like"; /id="PRO_0000248628" MPTLMQLSNDMKPLTFVEALRNFKSAKVLLVGAGGIGCELLKNLLMSGVKEVHIIDLDTIDLSNLNRQFLFRKKHVKQPKAIVAAKTASSFNPNVKLEAYHANIKEDRFNVAWFRQFDLVFNALDNLDARRHVNKQCLLASVPLIESGTTGFLGQVQVIIHGKTECYDCNPKEPPKTYPVCTIRSTPSQPIHCVVWAKSYFFPQLFSNDQESDGIIDNVSANEMERREIAELARETTELNELRSSIGQSDNGFEKIFTKMFTKDIVRLREVPDAWTYRSPPKELSYSELLENAEKATSPWLNEQNVWNVAESFAVLRDSIRRLALRSKSSKDDLSFDKDDKDTLDFVAAAANLRAHVFGIQQLSEFDIKQMAGNIIPAIATTNAVIAGLCITQAIKVLQGDLNDLKNIYLAKRPTRVLHCEKTCKPNPYCPTCSFVLLQLGVNDKNMTLRVLVDDILKSRLHYSEEVSVLNDKLIYDPDFDDNLDKTFDDLGINPAKNTILTVLGDSAVEKDDDGEEATRVPLLIEVTFIDSNSTEGLPYQILSNATSIPLKQQPPSNSPEDSQVLTDEINEVNDFSSSERIVINLDEYDIIVDSKTSSHNKQLKRRPSNDTLTQEAKSKKQAKIHTM O42941 CYP7_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPBC16H5.05c; CHAIN 1..463; /note="Peptidylprolyl isomerase cyp7"; /id="PRO_0000064178" MATLTNLEPLATGTVILKTTRGDIQIELWCKEVPKACRNFIQLCLEGYYDGTIVHRVVPEFLIQGGDPTGTGMGGESIYGEPFAVETHPRLRFIRRGLVGMACTENEGNNSQFFITLGPTPEWNGKQTLFGRVVGDTIYNVVRISELELDANQRPVFPPKIISTEVIDNYFTDIKPRSTKEEREKIANELAHQEKQKERNKLLKSGRRNKAVLSFGDEVDMPIVKKPLRQKTPVSRSSDTTTELSKDLISSSSSIHSTYSSAQTGLTSAKVSSDEYARQVDTLDTKLNSSSKSKVQEEISRLKSELRDLEKSGGSSNSKPVVVRPKKRNILTEELEKYKKSKKVVLGKRKNLENDEESTLRALSSFQSKIRNAEDEDVMDSQYGSKIEDTPCSLHNVPGCFSCFDRLGEKNITETNSNWFAHRLVAENDPTRRTEELRIQRAEELKDVPSARPKKLLMKRDII O42945 DHX15_SCHPO BINDING 98..105; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC16H5.10c; CHAIN 1..735; /note="Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43"; /id="PRO_0000055144" MEPAQKKLRQESKNPYLAHLNNGDDSEEVVSSKGLTRRATTVAQAAKAEEGPNNFFNDKPFSQNYFKILETRRELPVYQQREEFLKIYHENQIIVFVGETGSGKTTQIPQFVLYDELPHLTNTQIACTQPRRVAAMSVAKRVADEMDVDLGEEVGYNIRFEDCSGPNTLLKYMTDGMLLREAMTDHMLSRYSCIILDEAHERTLATDILMGLMKRLATRRPDLKIIVMSATLDAKKFQKYFFDAPLLAVPGRTYPVEIYYTQEPERDYLEAALRTVLQIHVEEGPGDILVFLTGEEEIEDACRKITLEADDLVREGAAGPLKVYPLYGSLPPNQQQRIFEPTPEDTKSGYGRKVVISTNIAETSLTIDGIVYVVDPGFSKQKIYNPRIRVESLLVSPISKASAQQRAGRAGRTRPGKCFRLYTEEAFRKELIEQTYPEILRSNLSSTVLELKKLGIDDLVHFDYMDPPAPETMMRALEELNYLNCLDDNGDLTPLGRKASEFPLDPNLAVMLIRSPEFYCSNEVLSLTALLSVPNVFVRPNSARKLADEMRQQFTHPDGDHLTLLNVYHAYKSGEGTADWCWNHFLSHRALISADNVRKQLRRTMERQEVELISTPFDDKNYYVNIRRALVSGFFMQVAKKSANGKNYVTMKDNQVVSLHPSCGLSVTPEWVVYNEFVLTTKSFIRNVTAIRPEWLIELAPNYYDLDDFDNNKEVKSALQKVYQMAARSKKNARR O42954 MBX1_SCHPO PTM: Phosphorylated. Occurs periodically during mitosis. {ECO:0000269|PubMed:15509866, ECO:0000269|PubMed:18257517}. MOD_RES 372; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19G7.06; CHAIN 1..457; /note="MADS-box transcription factor 1"; /id="PRO_0000199443" MDINPPPSTAPSSPRRSIQRISDAKNKALTFNRRRLGLIKKAHELSVLCDAKVVVMIFDSKNACHVYSSEEPEEQRDALLQKFLNKDFVTVDPLRNINPNIPSDESLHNWRPKDKRIASVTTYSAQPSNNCSSATDSENDFQSFTIKSSTTYHTTPTTASENKKIESITIPDHASVYNDLPLSPTVKHSFVSPVSGDYSDSPLEPSSSSSFSVPPESLNPTLSFQHNDVPQTDNFIPFLTPKRQAYGQSSSRADRSSVRRSQSFKNRRNGKPRISRLHTSHASIDGLTDFIQSPSSGYLDPSSTPITPLDSAINQITPPFLPDNLGQENRGELYSHDNPTSMVYEHPKFDELPNGFIDTHELNILSRSFTASPNQILRESNMVNQDSFTDNPVDATWDALIGTTQIDLDLDYERSSIPSSTIPADQLKDGVPTNSVYRNNMVDHNLYPSLNIERNAP O42955 CCM1_SCHPO TRANSIT 1..49; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC19G7.07c; CHAIN 50..687; /note="Mitochondrial 15S rRNA processing factor ppr3"; /evidence="ECO:0000255"; /id="PRO_0000316605" MLNKCSGSLTLLAVRRFCGPCRRLHYHKDNPNNINIAKNLLNNNIQARCSTNEASWKLAQKELDLKIREYEQKLKDVKLNDINKKSPLNIPDEVWTKFISEVNSYDKEKENHLSTGNHELRRTTPLKIGPLLLTRIGLLKSKNTASNNYSVDHIVSNLANDNTLLNRQVSTEEWNSHLRHLLNIPKCFLGVDIVEIVNFFNYLPQTVISKSSLEIWKAVEESGMKVMPDLLVLLMESTNASGDFRKTVQLYHLYQKSNAPPNGLVYQSYAIALSSLGKHKDLVALYSEQKSVSITPSKDFLNACIKAFSRTKEFTKAWEVFNFMKFTATSISPSAETYGLMIQICSSQYNPEKALDLYNEMKLRPIDPLTPTTFVINNLIHALATDVRFQTVAFSLLQDLSHYGLRPNHSTLYELIRLIAYSGKLDYMKDILDNFWVRQKLLPSILKVEQIFHFIFRALISAEVQTSSVTPDYTHFKEEVRKIIDSSKEPLIPFLKRSTLTENDLFLNAIYTFEYAKRKFPEALNSRLVTDFLNIFLERGSVQLFKEIYQLEFREMSTMEGSSMKVAKITLTYIYAIKLALLFNDFEFGYAAWQEYWHCKIHKLLPKEDASYEQKVVLLTLSLLSKNKHTSLARSLLLSHLDKGWTWNKHSLGFMRKMCSVMNDQATVYLIDSITNEIGINQRFTRK O42956 ART1_SCHPO SPBC19G7.08c; CHAIN 1..483; /note="Arrestin family protein 1"; /id="PRO_0000303891" MTSPCTLIRQFSPLEIRPLPHLDFQAGFNGIPTSAPRLVGIVQVRSKEIHQPLALVQITLELWKIESVVIPSLGISNHLSDNKCLARQVLFPLHSEHPENNIPPNDNNYSISDLSIKSPPPSLTSDWIVDSYASDQDNPSVHTHNRTTPPIPPPHLPNASGSSVYQPPYTPFRSVSTTSSSNDTSITPFGDQTPILSSSSDPYATHRVWSMDLPFEIPFPENSEIPSTFELNRSGTICSTKYELRAHMSLLGVPDITTTVPVSLSRYDNLSSWGMYNSPTNIRQVSSDGRVVVEVSIPKLCIGPSDLVSVFVSIMPNNGSKIRVQQLSLSLVEYITFIHPSSSSPIVRKKKVLRYEEDLDDMKLTSEGLSKSLSKPFPDIDFEDANITGFTTTSDLYSVQYMLVIKVQLYRARNIEITNPIIVSPVERSRSQALLNEIQTRVLDVRQSHGGVVLEENVRIVRASDFSKNNMFAYLNDDIVLLS O42957 ULP1_SCHPO ACT_SITE 463; /evidence="ECO:0000250"; ACT_SITE 480; /evidence="ECO:0000250"; ACT_SITE 527; /evidence="ECO:0000250" SPBC19G7.09; CHAIN 1..568; /note="Ubiquitin-like-specific protease 1"; /id="PRO_0000101733" MIGKRNASKRTRQDDCITYEEYQRKRKKTFLNTFVNICSRTVTYAKLFLTKTPISELDRIAGEAIPSNSNSTNSKLEPSTKAPESRFSHINSKTERGYVTVESDMSSHNTLDRNSKPTVSHSYTNSSKDEKFLDPIALQNLFSPASDTHSQNIHDEALSPSSFRVSRSRYFPRPHRSSKNLSVSNRLQLAVFKETTSSTLSHGNSVEADEINSFNPTPFSSSPLHFTNSSPNPNSDIVTPDKQLDVVSEHARYKHLPFTATLRKKSPHDSTSRKASFRFVQSDQQPARNIVTSDIQNEKSLLLLIRDLKEKQTESFQDWNEVDFLQLKGLEISPPPTRPKFIPELEFPDNARKRALKYLNQSNSVSSSEPIITKFNIPITLKDLHTLRNRQWLNDEVINFYMNLISERSKIDSSLPRVHGFNTFFYTSLQRRGYAGVRRWAKKARVNIADMDAVFIPVHLDVHWCMAVINKSKKRFEYWDSLAGSPGKVFDLLRDYYIAETKGAVDVSDWENFMDDNSPRQRNGHDCGVFACKTAECVSRNVPVQFSQNDMPELRIKMAASIIDAQIY O42958 PAT1_SCHPO SPBC19G7.10c; CHAIN 1..754; /note="Deadenylation-dependent mRNA-decapping factor pdc2"; /id="PRO_0000372628" MSFFGFNTTLPKENMFPNEGQLEEDGIDFEETYDDLGNQLNEAGDELNDETFGVSAGSIGRDFDFSGTTAQASAQLEDEQYQINQQNIFAKPVKPASSELPQVSRLNGASQFPSREPASTAINKLSDLQPMASIWENIVPEKPAIIPPEVASLQDRLGAQPSEKVFSLQELEEQLLNSMTAPKPPSQPAIPIVPSEMAAQVTRENISSLDPAISAASIGNVTFGQPNIPSTTTDFAGLAAPNMVHPSQAIPNPVMQPSLVPQMPYPQNGMYNPSVAPPASLVNLFQQEQLIQNQNLDEKRQKLERDHMLMAQCAGLMTRSDKSFIARIQISQLMSEDPESDDFYYRVYSIIRGRKPSEEEASHFIQTYLGPSNNRRRGRRSENPMQKLQQQLQRLVSSAKERPKATQLSLEGALGKIAVNTVRTPRQLLNVKRPTEPASSNSSLNNFSGFSTKKDVLHAIEKVYDLLLDFEQALRKASTLETTDQEQIDTWKTTLSEKLESIWKALYINESLEASSKTRPPFISIISHPKGMRLLPRLFPHLSKEQQISILKVVVYNFDSLDIVLRGTFDVNGELPLDVVSEMSSFTQFIIPPLLTIVNELDLETINNLFSQLLNRTNAVYLIQTKIGLSFLTLFISRAEILKQSGTVNQNEKEEWENTFNVMFNRVKGHFSTVFPPPNARAYADESYPWEFLAACATAASSEQHFTLVSETRDRVLDNIITSKRAPSEIAVVRISNVNLFLNAMGLDARQLSA O42963 NUP44_SCHPO SPBC19G7.15; CHAIN 1..403; /note="Nucleoporin nup44"; /id="PRO_0000290671" MAFSFGQQGSSIKAPSIGSTGVFGQSNTTKPTAPFGSGSIFGSTNTNVGAGGPTGSSSAPPFGNSIFGKTQQQPTTSFSNTTTNAPQSTVFGQNAASRTGNSNTQPLFSWSTVNNPTKPVDETNATIPSSLLLSSGISPNATVSNAQYGPAQPPSVEEQVQKILNAWNLNHPDCAFQRFFYNKVPVEQAALYVKPPNYNQQKWDEAVANRPSNSVVPVLAVGFPDVQKRINMQIQQVNTYRIRMREIVETLGRLSNKHDLDFSIKLAEAKNRHVRLSERILRLAIKVHVLRHRGYALKPNEEELRKKLDDLTKSLNNPEIFGRLNEIWARITLIFEGEKISEDQRSNLAKGVVDWRKNSDQLEVITDVLRDHQVGLSYVVKLMQEDLATLNKQLTEHVPQSQK O42976 YGZ7_SCHPO MOD_RES 80; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC20F10.07; CHAIN 1..764; /note="Uncharacterized membrane protein C20F10.07"; /id="PRO_0000374037" CARBOHYD 23; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 118; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 240; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 330; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 364; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 376; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 442; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 554; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 627; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKEENGFAGFLNTAVNRLSGVLNDTAPTKSQSLKNGVNNEGNRGFSLFRNPRFMSDEKLSSEASSHSTLGQQQARDGRQSPSKEAPFGEGELKLENFENQENEADEAENEETSYSEQNHTENTEEIAEESRPLERTHSGSNHHEASSTGHLNLPPLENTLSQGSAITAPSRKVSITSSNGVSARLSGYAFANSKRNRDFHRIFKVLPPEDHLIDDYGCALQRDIFLHGRMYLSESHICFNSSIFGWVTNIVIPVTEIVSVEKKSTAVVFPNAIQITTLHARYIFASFISRDTTYQLIIAIWKNTHPFLTTLANGHGVMDASGNHHSGSSNQSINADSSAGSEGVDEGTSTEANDESSEDDDEDNNTDEANEDAQSNVSDESPKGEGSSHSDNVVLSDGNSVKKMNEDGADTSLLSVSEVTSHPPTEWTGSPLAHVLCSDVVNLSVSTVFNLLCGSDTTWIINFFKSEKLTEIKIGKWEKIDDKWNRKVQYIKPVAPPYRQTSCYITDTIQHLDINNYIEILSTTSTPDVPSGTSFVVKTLYALSWAHSSKTKLNISYSVEWSKSSWLKGPIEKGAQEGQASYVKDLLTAFENYKVSPKGRRKKITKHTKKKNKHASETSVAPEKVDNSSIEQSSSFLTKLYTFPFTIITWLMHPTHLLLVVMFSMLVLQWWYMQQILHAELPSTSSRSDSSRDLDFDHIPMDDTAFKLWITSRLDSVERDRDFVYENSDPNLEHGKIKIATDYMERRLKKLKERLRKLEASGYI O42978 LSM5_SCHPO SPBC20F10.09; STRAND 17..36; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 42..51; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 57..65; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 70..75; /evidence="ECO:0007829|PDB:6PPQ" HELIX 7..13; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 67..69; /evidence="ECO:0007829|PDB:6PPQ" TURN 14..16; /evidence="ECO:0007829|PDB:6PPQ"; TURN 52..54; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..80; /note="U6 snRNA-associated Sm-like protein LSm5"; /id="PRO_0000317307" MSMTILPLELIDKCIGSNLWVIMKSEREFAGTLVGFDDYVNIVLKDVTEYDTVTGVTEKHSEMLLNGNGMCMLIPGGKPE O42980 NESP1_SCHPO MOD_RES 329; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 340; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 351; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17D11.01; CHAIN 1..420; /note="NEDD8-specific protease 1"; /id="PRO_0000101735" MSSSPTVLELFDVCFKQEDVDSLKKPNWFTDVSIDYVDELIEHLWFPSYPNQANEILLLRPSLVFLLAEAAISPEELKVALPKKLMNCKYLFMPINDLDKHAAGSGGSHWSLMVASIPDGQCYYYDSLSNGKTKDCRSALARVSDLFKKKFTIECMPVQQQRNGYDCGAHVCAFTLELVRRLLHSPMPTSSMWNLSTFQPDVTAIREQLSRCLDHIINSLGTRVSGDFDEDFPTGTVFFDLESHLPLLDVALPVLPKSSDSSETSHESSNSNLKKSSESGSTNHHNNHESDKDLHHEGHHHHHHHHHHHHSHDDDPSSPAEKKQNHVPSPSEKIQDHVPSPSEKKQDRVPSPSNNKEDHLPLLSDEKLDKSAIDKIEPTPLPSVHMNSHIAKGELPKFHNSTDNPFLTPPEELVSGDFPF O43005 AP2B_SCHPO SPBC2G2.06c; CHAIN 1..677; /note="AP-2 complex subunit beta"; /id="PRO_0000193754" MSSSSSHFSSTAADLLAVFSSDNKDKSANKRISALKKAIAGISYGYDMSSLFPSVISSMESNNLELKKLCYLYLKIYASVKPTEAKRAVKLILNDIYSSNPMIRSLALRTLTSVNIKNFWVAAMDPIVRLLDDTDPYVRKTAAIGIAKLYSYDKKMVESSGLIDHLKEMLSDESSVVVANSLAALMNIVNSSTGFKLTFSREISNKLVKSLTDCSEWLQVAILDALIFYVPQKPGEAESFAERISPWLQHGNAAVCMGAVKVILYLTNYMKDDNRVKEYFMKTQPPLVTLLARKSSATQYVILRNIQIILEQCPEMFANDIHFFYCNFDDPIYVKLEKLDILTKIADIHNLDQILPEFVEYASEIDVELVRKSVKCIGYLAIKIEERKNDCIDSLIELMNTKVTYVIQEAVIVIRDILRKYPGSYKSLVPILYENLDSLDEPDAKSAVIWILGQYAEEIEDSITLLNDYLKGFFDEPLEIQLTLLTAVIKVFLKKPTAAADMVTNVLQWCTDEVNDPDLRDRGIIYSRMLSANPELAKKVILANMPPVNVGTGMYDPDTTEQLMLNISTLSSIYHKPPNRFVKGAQVAYCEPSPVLRLRTRDSNPSNTDSRESNHKKYNHFHQKSQTRRVMEQYDRNSWNPSPFSDESNSNTFSGKFDSADQENLGMPMTPETHLMD O43008 CRS1_SCHPO SPBC2G2.09c; CHAIN 1..300; /note="Meiosis-specific cyclin crs1"; /id="PRO_0000080417" MLTSKHEFSLFLNTPAINSKSEKEVISEGPLTTSNEIDVTFSESFSSHLINLRRVPSVNSIIEQEKKGLTKISPSILNQNIAYKEKRQQLFSVLYEETVGYVSMDTLCIAISLLDRCFTVKPTIPTTSFKIYAIGCLFIAFKLTSDYSVAKKSFCENLAPSLSTKNLEKYEKIVLALLNFDIYVISLPSVESFLTPLIFQHVFFKSLPSESCDQMMVEWQYLLVEVMKDCQFIEYRPTEILCASFWVLLEIIWPSAFDFKPFQHLCSLPTNGSADETYIKHSNRFHDLIISIQRIADMLA O43011 SYH_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21; TRANSIT 1..25; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 90; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2G2.12; CHAIN 26..563; /note="Histidine--tRNA ligase, mitochondrial"; /id="PRO_0000314755" MFVFTKNLFTTKFSSSLLNWRFLRTMADSLVDINERITSQGNLVRSLKSQGASKEDIDKEVAKLLQLKNLKLGGSEVSGKKKDTSFTLKTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPKVTSIKRFHIAKVYRRDQPAMTKGRMREFYQCDFDIAGNYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREMVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEADSLLSSNSSAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEASAPKIKSSAEKKKSADPEADRSNDDSIGVGSIAAGGRYDNLVGMFAAKKNAKIPCVGISLGLERIFSILRSKIPDEDIRANDVDVFVMAFGGGKEWTGFLKERMSVCKDLWANGIKAEFLYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENSDEGQLVPREEMVSVLKKLLKYD O43013 YBOE_SCHPO MOD_RES 336; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2G2.14; CHAIN 1..533; /note="Uncharacterized protein C2G2.14"; /id="PRO_0000303931" MSFNPAAGLLGKLKKLWNDTKNDYLEWERSQQGQISESVVKNHSPSKRKRRPSKEPSLSPKRRKNILNDQKKDEESIPNAGTQSQNFTHLSASKIRISDEDRIKPLVDLNQDHSFDMAYLTPASAPPPRFRFVPPKSDAKSHSAPRSLEGVTSLSDSHFNSLEANLKAISKDSNNKAHNNRYDESSLTNPEFSILVERLKSIEENLQSLQERISHCERSVSLSPSFAPPSNVKSPVQQHRSFVSSSARAKKNWGRQSNSPNSNKKTDHAYPGASMNTERGLIQNLEDSDDIHEESSDTLEEPLLINELNRTSFLNSNNNLKLNEAEENQNLLNLRSPKSSGKADNLTIKSSSNIDKVTSNDLYLDNNLQSHFKVTESQPTNLGRKEYSNSPFSIRARKDAATTSSSFESYHNTQTIQSPMKFTKATPLKDNESASVDESKVNVLSENQSLQADTATLEQLTPIPKARWNQLANKHPSLSNSAASPPVSSPGLRRSHIPVHEGLKHTRDGVAETKDALAKLREKMQERLKNHTS O43017 SWD3_SCHPO MOD_RES 379; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC354.03; CHAIN 1..380; /note="Set1 complex component swd3"; /id="PRO_0000051254" MDSTAQQFPLNHDLQVQKDQKGVVEEDEEQIHKRIRNYESHSGFSEYCTLFGHEKSVTCVSVSPNKRWIATSSSDGTIKIWSALTFRLECTLFGHYRGISQVKWATGSKYLASASDDKTIRIWDFEKRCSVRCLKGHTNYVSSIDFNPLGTLLVSGSWDETVRIWNLQDGTCLRMLPAHSEPIISVSISADGTLCATASYDGMARIWDVLSGQCLKTLVEPINVPLSNLQFTENRKYLLVSNLNSQIRLWDYRRNRVVRIFDSHVNTRYSMSWDCYSSKNIPKNTEALPNNDSSYPDDAESFMHDAYLLIPSEDGTIQITDPSTKIIIDDSIRHSDDPETSLLNVTSLGPFIITSGTDPYVRVWAPSLLLSKHEKDGFSP O43019 SRE2_SCHPO PTM: Undergoes proteolytic cleavage by rhomboid-type protease rbd2 and is released as soluble transcription factor from the membrane. {ECO:0000269|PubMed:27655872}. MOD_RES 344; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 345; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 356; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC354.05c; CHAIN 1..793; /note="Putative transcription factor sre2"; /id="PRO_0000356242" MCPSQHSSLKDIHRQLENTAISNPTENADPSSYVDGSNIMDFKHPSIVSSSASSSYPISHVPSVGTRGIPRSYSMASAYPYQVNSNSMDASTAFNLNQDVADKPMLARNSIDSSINTELGPLESNHWFTQAQDHSRQYSSSWDPSIDPFEVKNSLHDSTDLSITHHPHLPINHQGNTWKHANESLQSNQGPVPNTKFVGLETTQTDSYQQSSVNSVVKIEEADATYALREESGQFNTFTGAENPSISPHSLNPNFPQYTEKPALTLLQSPKQNSNYDTSNFQNSVSDSSMQFTNEGMPSPVKGIMSSDDAVAFNFSQYSTVYPQNAPENGNEFETPNKLKRTVSSPCASISSKRSYGDIAQDCSYISSKTNGGGPSDSPSSSSTSVRGSVNDSNSPISSSATFAIQSNGVEPVGLSTQEQNLSPLSKRSAHNMIEKRYRSNLNDKIAELRDAVPTLRSGYNSTTADELKGTYVPLSRKLNKATILSKATEYIKSLQSKNKKLIEENKILQKRLSEYTSVIQASLTAPSQPASLSLLGPPGNTPGHRNVPPILKRSSIGTPSQQAYFPDAPHNCHSVPQNSSYPRPPMQVNRSPIDSMQTIPHANFNEMHNAYSSRYPLKYSKSCNAVSHTSMMHPQEYGGSLPSSTVPSDYNQPQLVSPRAQADQQGLSYKNVGRAVLNGLVGLETVHMLTNPDDAGSSNRFSMSVLPISPSLHSILRFLLLLLAFLCFAMHILLTPEATLRKWASSIYLSFRLECVFISFLIFSVPIYDWGNYLNLRGKLLSELNLESGVAT O43024 DEF1_SCHPO PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P35732}.; PTM: Proteolytically cleaved by the proteasome in response to transcription stress; the resulting N-terminal form constitutes the activated nuclear form and the C-terminal portion is degraded. {ECO:0000250|UniProtKB:P35732}. MOD_RES 474; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 476; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC354.10; CHAIN 1..963; /note="RNA polymerase II degradation factor 1"; /id="PRO_0000339335" MSENKKFRPKKVGNTEQVSEKQHTDTALNISQDNKTSSSSAKRGAKGRRGTKGKSGPANSSQTSNIEGSNALELEFDRDSQLSVLQELFPSWTIDDLSFALEEADRDLELTILHITEGHASKWGEVKKKPIPKTKSKPTSHAPVSDNVSSTFRNATRKSKKPSASKDTSRGVRKSKAGAPSDPSSVHAPSSLEKPAGTGDLPSSEISTKAPASTTVSSSVDPGTINEDSSMKDHTTSNEQASVLTSANTAASTNTNGTAGGTSASAKSTSAADQAVASSKPIKKAWASVAKSKKKVTPAPAPAPESEPSKPSIAPSQPSKTNVSAAYEKPAELSSSSVPFPHKSQDSATPANVETTPSTATSAPKKSTAPFAINAVKPAPGLSNISSASLPKPSFAKQAAVGSQSSTTSMTTARLLSDRFPVVMPVANTAAIPEKVQVRFGSLTLGGEDKKSTKSSSDNIAQSGPRSSYFPKKTVSPKPEAKKEASKVAESTKIPKKQHTSAYESRAPQSKVPENLKESHVNETPYRGLHDVNLPASGNASSVSAIPPQVSAQTTIPAASTSATSGPVVGKQSAGYGGIYSPATHGISPQPYAGASLIPPSTGAAFNNETASSNAGETTALPYSSRFMNPVENRSANSPFDNFQHIDHSTELGYASNTSQQYQQTSHPAYTTMSPIEYGQAAPAAHYYNERNQYSQYDNVAGSASNTPDVHSVMHNKVASSNATSLPAAGTATPSPVVSQQQPQPYAFPPMYPIPYVSYGYGTMPYNNNKFGQPQQGYMSQSGFNDFPPIFGGHSNVYNRQQPGNVSGMSGTQTSNPINNATANTSGMTEKAAGHRDSVIGNGGVTGANSMSSTLGGLSSMSGMGRAAPGMFMGNVGSFENLSANAASPYGLPPQQTPLTNAATQQTTSFQSNANKVNNANSQPAGFPFNSGASTNAGSNGLGGYNAYNQSFINRPGGWYGNA O43036 RPA43_SCHPO PTM: Contains an average of four phosphates per molecule. {ECO:0000250}. SPBC3B9.07c; CHAIN 1..173; /note="DNA-directed RNA polymerase I subunit rpa43"; /id="PRO_0000073959" MPDLSLYKQTVDLYLSIAPGHSRDPLNAIQEHMDSMILSKLPRINGIVLAYDNIRFLEKSAKVMYDSPFSFIWVRVDVLVFSPKKGDCLEGKINLVSPSHIGLLILGIFNASIPRKSIPKDWIFIEPDTTEEQGRWKTNDGNILEPGKDLEFVVDGIQREAGLTMVQGTLANS O43038 VPS36_SCHPO SPBC3B9.09; CHAIN 1..467; /note="Vacuolar protein-sorting-associated protein 36"; /id="PRO_0000373858" MAFYLETTPSNLPVLDPSEEILLVQDQVGLYFGDEKSFRHNNGTLYLTKKHIFYVDSVDPKKNSLKIKISDIRDVQHTSRYFRSSPKIRLSLRHVEKSWACKICTFINVGDPINPCRNCGVANRFTIIKPKSDARFSQGLCTACTFQNYPDLNTCEICGNQLKNVDRNQLIQLSFRGSGSSKFYEAIKSETDEIEKQRYSNKYDTKVLRKAILEKSLRMGGIHDLEQSHEMQLAKNGRTLVHAFQDLDAFFSLAKDTMSLADQFAEKMDGLTGTQQSDKVQQLLNKSNQLGVLRGNHLDNVPVSANSRLYDIELCKSISEVLRTRLKADTDTVTMTQAWAIYNRSRKANLIPPTRFVKACELIDSMEVGITTSKMNSGLILFQLKTSNHSGKLLSAILEVMNPSTTALKCAMRLHWSIGVTLERLYQAEMDGYIVRDVYEESGSSLLYWKNEFDELSEELTKWFDES O43040 CTF1_SCHPO SPBC3B9.11c; CHAIN 1..363; /note="Cleavage and termination factor 1"; /id="PRO_0000081537" MSMTAGNVVFVGNIPYDVSEQQMTEIFNQVGPVKTFKLVLDPETGSGKGYGFCEFFDSETTAMAVRKLNNSELGPRKIRVEFPSNDPRRNQSYEYTERTDRYMEQQNAHESSYNSRFIPPVLHSTSSLPASQGGGMPSPAIYSSSMATNLNKNINSTSVPAYNFHNSMTSDFDSASQPHTDAYNARTFQYNKSSQNKGDYTSGTSISNPTSIPLAPSVVQVLSTFSAQELLNMLSKLQTVVHIAPEEARRLLIANPALPYAAFQAMLLMNLVDANVLQQVVVAVKNKNMHQPASATSSPPSVPQKIPSSNHKSQQANGSDQGNEGKRMALIQQLLALTPEQINALPPAQRDQILSIRRQHFRQ O43044 NU120_SCHPO SPBC3B9.16c; STRAND 5..10; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 20..25; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 57..63; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 67..69; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 72..78; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 82..87; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 100..105; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 110..120; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 125..132; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 137..142; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 158..162; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 172..177; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 179..187; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 192..197; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 204..209; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 237..243; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 248..253; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 257..262; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 267..273; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 287..289; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 291..293; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 296..301; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 304..306; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 308..316; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 323..328; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 345..353; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 358..369; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 372..381; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 389..394; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 484..489; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 519..524; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 526..529; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 531..543; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 642..644; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 785..787; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 806..808; /evidence="ECO:0007829|PDB:4GQ2" HELIX 45..54; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 122..124; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 145..148; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 165..167; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 418..427; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 433..442; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 452..458; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 463..477; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 491..514; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 515..517; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 547..552; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 556..560; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 570..584; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 589..604; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 611..622; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 624..626; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 629..640; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 645..657; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 671..702; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 708..712; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 718..738; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 762..764; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 769..776; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 789..802; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 811..821; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 825..831; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 832..834; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 839..851; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 855..863; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 877..879; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 880..888; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 894..908; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 912..924; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 931..948; /evidence="ECO:0007829|PDB:4GQ2" TURN 13..17; /evidence="ECO:0007829|PDB:4GQ2"; TURN 79..81; /evidence="ECO:0007829|PDB:4GQ2"; TURN 199..201; /evidence="ECO:0007829|PDB:4GQ2"; TURN 244..247; /evidence="ECO:0007829|PDB:4GQ2"; TURN 263..266; /evidence="ECO:0007829|PDB:4GQ2"; TURN 713..717; /evidence="ECO:0007829|PDB:4GQ2"; TURN 889..891; /evidence="ECO:0007829|PDB:4GQ2" CHAIN 1..1136; /note="Nucleoporin nup120"; /id="PRO_0000290667" MNELKHAVVPIDLQSFCLEGTLALWVPALENDSEDDSEAIETADDNEKLFKKECVAYDAGVYTSNKSKGSQTLRWSIFQNRTLTIFDVSLNSKKEPLSKFNVKIHFPSNVMKDGVAFSFSEHSDTTIIYAITHARVLYYIRLSKTWFQLPDARLDDDWCLCYRPISFLNQKPDLMAAISTSEICVSFFNGGLTKIILNPKDASHYEQHIDDSSYLFSLKKYLSLQAFKADYRSPNTIISMIFLSTYNVLVMLSLDYKLKVLDLSTNQCVETIELSQTILPLQSFPYLTSDHTTNSFIALYYPDNSHGSFSIYKLNANAHSFKLNVVIEKGIIPPSLPDDEFIPWMLSDFQLISSEGSQSKFLLIIAWKSNLNTVIQKCNLSLDQDESFSCVWSHSLDSFSLIEKTFFDVPTNMSSGDISEIWLQHIFAHNTSIESIQVALLSFQNSSSQVSKNKLDKFGALTISELKNAVLSSIVSTIQIEPNSDLTGYDYYEYKRLLYNEWERFAKLVAYLDHFGDEILSINFDPSNAVTYINYANKVAFIRDPYLIESFDEEPLTKLISSLETDDPSLIEGYQILDLGRSLHSCMSFSTLSEIRYSLRELVQDLPSYSLFDTLWVFYDKHIYPNVDPDYISTLIDTLVSLENPMRDIDSLIQRLRSFDIYNHSAQSPSLFLCASVARVLDSILKKFQVSIEGFIFLLSLITSQQDYELQSKFAGCDKLFLSLLEDWRLVSFLLENSALLLEKFEEEDVDSTNCNLNTMEALASVNTALQFFSALNYSECFSESQISPLHATVISSLSAIFIRDDTENDLVTELVEKLFLFKQYNACMQLIGWLNSDPIAVYLKALIYLKSKEAVKAVRCFKTTSLVLYSHTSQFAVLREFQEIAEKYHHQNLLSCYYLHLSKKLFEESAYIDALEFSLLADASKETDDEDLSIAITHETLKTACAAGKFDAAHVALMVLSTTPLKKSCLLDFVNQLTKQGKINQLLNYSMPTLRQDVDNLLERKAFQMINVESQPCWYNILFSWRYKHQNYRDAAAIIYEKLSRYISTTELIGKKERTFIIEHYLIVLNTLELLPKEDTWILVTDMSVDKEPDPNFLPQKLLTLDAIVAEYHLQLKDVAVQVTAEMSSAMNIDL O43050 ERG26_SCHPO ACT_SITE 144; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 148; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=4beta-methylzymosterol-4alpha-carboxylate + NADP(+) = 3-dehydro-4-methylzymosterol + CO2 + NADPH; Xref=Rhea:RHEA:33447, ChEBI:CHEBI:16526, ChEBI:CHEBI:50593, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64925; EC=1.1.1.170; Evidence={ECO:0000250|UniProtKB:P53199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33448; Evidence={ECO:0000250|UniProtKB:P53199}; SPBC3F6.02c; CHAIN 1..340; /note="Sterol-4-alpha-carboxylate 3-dehydrogenase erg26, decarboxylating"; /id="PRO_0000357024" MPMNSVLVIGSGFLGGHIIRQLCERENLRIAAFDLFENEKLLHELHGQFTMYTGDLTKQGDIERVFEEFHPRVVIHTASPVHNLARDIYFEVNVDGTANIIKACQKFNVDALVYTSSAGVVFNGADLINVDESQPIPEVHMDAYNESKALAEKQVLEASSESLKTAALRVAGLFGPGDRQLVPGMLSVLKNGQTKFQLGDNLNLFDFTYIENAAYAHLLAMDNLLSSNPTANGQVFFITNGQVIYFWDFARAIWAHAGHVPPYIIKFPRPVGMLLATAAEWVCYFLKKEPGFTRFRVQFSCANRYFNIQKAEDVLKYHPIVDLEEGIRRTLAWMDTEKKH O43053 ALG6_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a di-trans,poly-cis-dolichyl phosphate + an alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502, Rhea:RHEA-COMP:19520, Rhea:RHEA-COMP:19521, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267; Evidence={ECO:0000250|UniProtKB:Q12001}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30636; Evidence={ECO:0000250|UniProtKB:Q12001}; SPBC342.01c; CHAIN 1..506; /note="Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase"; /id="PRO_0000174160" MLSEFENGAPVQQFVSRFRSYSSKFLFFPCLIMSLVFMQWLISIGPYSGYNTPPMYGDFEAQRHWMELTLHTPVSQWYFRDLQWWGLDYPPLTAYVSWFFGIIGHYFFNPEWFADVTSRGFESLELKLFMRSTVIASHLLILVPPLMFYSKWWSRRIPNFVDRNASLIMVLFQPALLLIDHGHFQYNCVMLGLVMYAIANLLKNQYVAATFFFCLALTFKQMALYFAPPIFFYLLGTCVKPKIRFSRFILLSVTVVFTFSLILFPWIYMDYKTLLPQILHRVFPFARGLWEDKVANFWCTLNTVFKIREVFTLHQLQVISLIFTLISILPSCVILFLYPRKRLLALGFASASWGFFLFSFQVHEKSVLLPLLPTSILLCHGNITTKPWIALANNLAVFSLWPLLKKDGLGLQYFTLVLMWNWIGDMVVFSKNVLFRFIQLSFYVGMIVILGIDLFIPPPSRYPDLWVILNVTLSFAGFFTIYLWTLGRLLHISSKLSTDLRNKKEA O43059 SYP1_SCHPO MOD_RES 463; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4C3.06; CHAIN 1..818; /note="Cytoskeletal protein syp1"; /id="PRO_0000303951" MESLTKTEYVDAFLSNYSPNDSMSIFRQRLEQVRLDNDMLSQWIRERMDIERQYSDQLHKLAMNMQEKNNSSFAFNYAWKQLEGETLEISRYHSQIIGQIASQVYKPLIDYYTSSPQTATLRRLAERLSTVAEEMASSSVPGLKGLKKKGRDADTKSQNDLTASRATWDSDAPLAFEKLQIVDEERLLILKQVYLTIASLETDTALKQQEFFSKSMAVYSDLPIEGEIRQFMNSTSKVMSSASANKPSKSSGFHINNGKSKEEKSHGENESGGKLKNKMSTLFRRKTIMPKKDKKPSHKSNGRPNKLTAFFNKNSKASSISSAEEHPSNIDDSSIERRHYDSNHSSQIRDHPSTNNNASSYQNFNETSDEGEDNDATIRANNVRSSFLEAPLPVQPNVQAETVTPKISSKASPFNKPNSVHSEASRNTPSSIDRENASHSNPIMMHGNDFGGNFNNMQSRSTTTSPTSAVASPAPTENEDSNAAIERVANTLRKNPTISRRTRRAGTMDRYATASSDYMESNLGSLPNLSTLSLQSGPDSTATWHPEFPNSSGLSASIVEKYSGELSEDGLLHPSCSGHIFMKYTSDFNTPPPEMGVRVASEFPMSFTHLNDHAVKYGPSENTLSLIPELLLSPIKVTDFNLHLDSINGASCIPLTVVQKWKHDESSSSMIAFVKPNPVWRNLGSSLHIEKLVIIVYLGENVLVKSCQSSPAGEFSRKTSKLKLHLSNINISSSGFKILAKFAISPSAAIRKPVIEFRIRMVDSSNNPGLTKLFLKPDMFDTTSSSGGSQLESAYEETKVPTSYGIHVRECSVFADMS O43065 BTAF1_SCHPO BINDING 1383..1390; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" MOD_RES 144; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1826.01c; CHAIN 1..1953; /note="TATA-binding protein-associated factor mot1"; /id="PRO_0000074334" MTTRLDRLVVLLDSGSTSVVRETAAKQIGDIQKVHPDELYNLLGRVVPYLKSKNWDTRVAAAKAIGGIVENVPVWNPNRTSPVKKEETEDLPSFNGDTEEKPFIKTEEGAPASSQSQVVVSSNLTSNSEVSKLEEERLSTRSHSQEIKPIVDFGPDEETAKELNTELKGKFENSLLSFESFDIANVLKAGKKLLGSASRDYDVNPANYSTHYLQQLSNLKSRLDLAGEYLDDSIMNDLGDNVGSNSKGSPTTSIPEHKTSINNNKPEDTPTPSENVHLSARQRNALKRKARQMKNSQKVRVIDVAPTLVHQQNSTSSADKKTGADYNFTAQSRSDRLVVEHKAPIVPSAAVAVTSDSVWPFETLVELLLIDMFDPSWEIRHGACMGLREIIRYAGFGYGRVVGKSEAENEQLNKKYFDDLLCRIACVFALDRFGDYLADQVVAPIRESVSQVLGVALIYVPNDSVFSMYKVLHSLVFQNELGLTNTVWEAAHGGMLGIKYLVAVKYPLFFSHSDYLDSLINTVIHGLANHDDDVRAVSALTLLPIADKLVQEKLSSCKNLLKVLWDCLDDVKDDLSSSTSCVMDLLSSLCSFTEVMNLMQETANSDPEFSFETLVPRLFHLMRYTLTGVRRSVVYALTKFISVQTSCSWITGLTLRLCFQNVLLEQQEDISKSSCELAQRVMDILYRDGPESFSKLLYSHIEPMLKVSITPIGSFRRPYPLDTTLIVKPSGQPYAPSTSRERNNNISELSNSRTKHRAKDDPKGSFCFSVDEPMLNGDVEFVGEERMLKARLRASSLLGRIIGRWKRDEILLFFKPFLQACLTSSFSTPVVLGSRLIESFFEVEDNDLTIQKDELYHLLCDQFATVPRENYANLVSQLHVVRAQCNALLNTFLDVGRLSRSKIPSLAVVVKGDPEAGPIAFGIADAEKLVGPTYENLCKLLSPSQKAQSSKALNEIKYLIIDEISIYKIAKERQDIQCSASIASAMVTYDKLPKKLNSIIKGIMESIKKEQFSCLQMHSASAMMKLISACYKESRQVISEKIVRNLCAYVCMDTTETPIFHDSGKNGILSLHSIGTSDDNDEQVSGKLVDDSDDVSNDRKSSLSSVSDKDAAVLQRMGAQLTLQQMAQNFGSSLFSRVPVLSQCLFVPLQQYAESGFPSEVDQASCTVGQDLLDAMSILRFLVAYLDSGLQSEIVSTLPHLLATLQSNYSAVRNMASKCFAAITESNAAGSKALHLLVEDVVPLLGDASSTIHRQGAIECIYHVVQRLGVRILPYILYLIIPLLGRMSDADQDVRVLATTSFATLVKLVPLEAGLPDPPDLPQYLLDSREKERKFLEQMLNPSKVEAFSIPVPISADLRKYQQEGVNWLAFLNKYELHGILCDDMGLGKTLQTICIVASDHYNRQKLFEESGSPKFAHVPSLIVCPSTLAGHWQQELSTYAPFLKVSAYVGPPAERAKIRSKMKKSDVVVTSYDICRNDVDELVKIDWNYCVLDEGHVIKNARAKLTKAVKSLRSYHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKTFQERFVRPIAASRDAKSSSKERERGTLALEAIHKQVLPFMLRRLKEDVLADLPPKIIQDYYCDMSDLQRKLLNDFVSQLNINEELEDDETEKTQGTRKKKSQKAHIFQALQYMRKLCNHPALILTEKHPKRNAIVKQLAKENSGLHDLKHAPKLTALGQLLRDCGLGNSSVNSNGIDSALTNAVSEHRVLIFCQLKDMLDMVEKDLLQATMPDVTYMRLDGSVEPTKRQEAVTKFNNDPSIDVLLLTTHVGGLGLNLTGADTVIFVEHDWNPMRDLQAMDRAHRIGQKKVVNVYRLITRGCLEEKIMGLQRFKMNVASTVVNQQNAGLSSIGTDQILDLFNTTADEQQTVQNIDKEESEDAAGRGLSGTSKKALEGLPEMWDESQYDEFNLDGFISTLPKDAS O43066 PPK30_SCHPO ACT_SITE 187; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 63..71; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 85; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 872; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 875; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC6B1.02; CHAIN 1..953; /note="Serine/threonine-protein kinase ppk30"; /id="PRO_0000256827" MTEVYSKAPATVGQVKLSNNGTSNKAYSVPKSPAPVRTDLFSKIPAGTKIQVGSHSVIIQRYLSEGGFSHVYLALLENEKPFVLKRIYVPDKTALQLVHGEIETMKRLKGHRHIVNYIDSSALYSKSENRYEVYLLMEFCAGGGLIDFMNTRLQHRLTEGEILKILADVCDAVAAMHYLDPPLIHRDLKIENVLLVAPNSYKLCDFGSACEPLAPATTPDTIMFLEQNIAAYTTPQYRAPEMIDINRRQGIDEKSDIWAIGVLAYKLCYYTTPFEQVGNSAILKASFSFPPFPRYSDRMKRFIATCLQEQPSHRPNIYQTLKEIMEMQGTPLKLPDVYGGVNASTYNPPRAPLQRTPSGSLTPLSSRPAHTSLPPIPTVQTTSSNVPPVNRPSLKSKSPSVSNILSNQLSPISSANNDVMARLQPKSPIPATKSYSATIQTPRSPSLRRADSTSHIIKVPHLPDTSVKTAKTGASEIDVLSRYPSVEEIDKITDKIEVSKPLRNSGPLAFKPFEKISANKQTDLLQNKPEALLDLENRFLPKPSPKPSEFSSSVGSKQNLSMDIPSVQNVSTKQKSTNDTDNSKLKINKPLTGGYAPLPSRPNRMNHSVLNEKSNKEFVRGPRVLPPIEVSSSKMAGLDIRKEPFTPAVPSAKSGLKKDQSSEVANKDVVSKNKDNIAILADREARPQLLLDDNNDSSSSSSEHLISFNNHTGNKILSRQTTSSSIDSNNVQSNIEFLKGLNATHARSTSQVSHTQRLQQSISTSLERVKSNTKKESNSPRQVSKLKRPIGASNKILSGKFGEAFKKFEFGGEKMSRRRKSETKKNLVSILPDTEVDEYPKASNEWIVESEELPQVHETINQYRKSCETQRSRKSHEGSNDLERQPSSPDTVHPGIKRSHFIRERVKQLLSDANKHHQSPSDSETDRTPDSSSIHLPHIERLNLFHTKSESLE O43071 PRP17_SCHPO SPBC6B1.10; CHAIN 1..558; /note="Pre-mRNA-processing factor 17"; /id="PRO_0000278391" MLVANYSSDSEEQENSQSPNIQPLLHTENLAPAVVDNVKDDLIVSKGGNSRELARNVPVNEMVQPALGPANPFVTKEQDSIKNSITGYAEREYVPNFVFNQEYYANTHAIYGKRNFDDNEATTSTDLKRKSQKIKERREDPGDPSILEGDGAYKGPWAGYGSEQSSSPLEYSEYEEVESLDVKSEKDTESNNLGQNELLKEQLATPEVETHRSKEETILHKDRLFDYQNRSYMHVPNDVGINLSEEPGEQTCYIPKKHIFTWKGHTKGISCLRFFPISGHLLLSGSMDNQIKIWEVYHDRSLLRTFQGHARPIRDLSFSQDGRSFLSTSFDKTIKLWDTELGKCLNCFNSDRLTNCVKFQVDPDKPNEFLAGTADKRILQFDIRSPDIVQAYDHHLGGINSITFLENGKRFVTTSDDSSMRFWEYGTPVPIKFVADIAMHSMPRVALRPNGKSIACQSLDNCIYVYSAYEKYRQNKKKVFKGYSCSGYSLEVGFSPDGRFVFSGDSSGNACFWDWKTCKLMAKLPAHSGPVQSMAFHPQETSKVATSSIVDGSIKYWD O43078 ALF1_SCHPO BINDING 419..426; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 177; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC947.01; CHAIN 1..660; /note="ATPase-like fidgetin"; /id="PRO_0000290650" MDSDLDRILPIASRALLCEGNRDWAGAYVSYCKVLEEMKKSSAARDRMGLGPLTGAEACSWNGLYDNCLSKASKLRKTILESEMERQNYQLAAKLSKKAPVDLHPLRPVRSQTPAYTPMTTRMMYRQTRGAQSEVNLSTPKQIYSKHSPPSTSTSSIVSSSYGDAPSYLAPSKPNRSPPLKPEDPFASFNSSASAIAAASKSAAASASALSSDTGRSATMNSTTFPTAMKSQSTTKPTLSNSVSSPSIQVSNNQNANNSTPLSFHAPIPPLHVPAVPLTSASHSSSDGKSRKHPSPYKPYLNSSHDTLGSSTRPSSADTAGSPATSPPATADSKTIVSKTISASTTQQTEPLQQTTPSSDFEYAIMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSRRLKTEFLIQWSSLTNAAPDKQTGHSPRVLVLAATNLPWCIDEAARRRFVKRTYIPLPEKETRYKHLSHLLHNQVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDALLTTSAEMIPPISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFGSQR O43079 AP1B1_SCHPO MOD_RES 675; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC947.02; CHAIN 1..683; /note="AP-1 complex subunit beta-1"; /id="PRO_0000193752" MVPKLFQSSRFKAFKKSETSELQKGLVSQYAYERIDAVKRTIAAMTVGKDVSSLFPDVLKNLATRDITLKKLVYLYLINYAKTHPDLCILAVNTFVKDSEEYNPTLRALAIRTMGCIRVNKIIGYLADPLRKALKDEHPYVRKAAAVCVVKMYDLDREYCASNGFIEQLQALVSDPNPVVVANAVRSLAEIHDQDPEKGYFNVVYTMTDRLMVALSECNEWGRITILNSLARFRTSDIKEAEYVCERVVPQFQHANSGVVLSAVKVIMVHIPLFSSDFTDFLYKKMAPPLLTLLSTDSEIQYVALRNINLILQKRPSIFDVKTRVFFCKYNDPLYIKMEKLKIITMLACDENINETISELRAYVSEVELEFVKQTIKCLGDVALKVPSVINDCISIFLEIYELNISYMVQEVTVVMETVLRKYPQKIDLLLPYLSRVIEELGDPRARSSMAWILGEFSHVIPTSSKLLSEMISTMADEDLQIQLALLTAVVKLSLMNGKGNDEELVQKVLNYAINQSSNQDLRDRAFAYQRLLTPENVRKAQKIVCCEKPSVSYNNNLPEALLDALLCEITTLASVYHKLPESFIGQGKFGADAIQRRAVEELNIEEANVHEAIEKGANVENLLDLDFTDPGATSASDSPITSAQPQSGSNSAMDLFMAFEAPSTNNAEPVKARSATDDLLGL O43087 KMS2_SCHPO MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC947.12; CHAIN 1..457; /note="Karyogamy meiotic segregation protein 2"; /id="PRO_0000084311" MDEYIPFDDIVRQYDPDYTGKVSIQAFLEIVDDVDALRLNPEAPLLDNEQRQSAQDFIKDNSEIVVSTSEIKNLFYELTGLDPDTLPVNKLALRENGVLPRKSVAKPQKISENRIKRKDMFYQDASYITPRKGSPLSHSTPLSMFRTKNEYGSNKGFSHINKENADDSLIQQLYERIELQAAELRSKDEQVKELNARNAKLLEELDSSEEACKSCYTQAKTWEKKFREALRDSKEYAAQLQTIHEEYEQQQAHIVRMEELIHAVEKERKTETDYMKKESLSEQKERGAFMESNMILEEKVAHLQLENEQLRLFFKEKAPQPFQNHPPYQNLKITFPSPFFHIPYIPKTETLNDSQFAAGLSLLASELESQKNLLKKFENLKKKSSKDFLSPSTILSNAFSKVSLPNSLILRVLFFSLLFIIGIHIFYFLFFHVATIQQWPFLFWLPSTKFDNRWSPT O59666 ATU2_SCHPO ACT_SITE 529; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250" BINDING 13; /ligand="Cu(+)"; /ligand_id="ChEBI:CHEBI:49552"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"; BINDING 16; /ligand="Cu(+)"; /ligand_id="ChEBI:CHEBI:49552"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"; BINDING 742; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; BINDING 746; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420" CATALYTIC ACTIVITY: Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552, ChEBI:CHEBI:456216; EC=7.2.2.8; SPBC29A3.01; CHAIN 1..904; /note="Copper-transporting ATPase ccc2"; /id="PRO_0000314753" MYTTTLSVQGMTCTSCVASIQSMLEGVEGIEQFTISLLLERAIAVHDPSIISPDQIAEKIEDCGFDASVISSTEGEHGVMANYLLLSPMQAEQWTKVHNHINELQGVLSVNCSSSPDAAIRVIYDSEITGPRSIMKEILSMGVKCTFQPVDSSTSRILSLQRGSQIRVWKIRFIISISFSLAVMFLPQIFDSCDSMRAAFLVPHYFGICAGHIISLVLSLPVQFGVGRVYYSAAYHALKRGTANMDVLVSLGSTVAFAASIFFMILYSARHADNPAPIFFDTADMLLTFVTLGRYLESKAKGSTSAALSQLLSLAPSSATIIEDNEQIEILADLIERGDLILVKPGEIIPVDGTVVEGSSYVDESSVSGEPVPVHKTIDDELLSGTANGNGRLLVKATKSPRESQLAVIVDLVQRAQISHAPIQQFADRVAGIFVPVIVALSISTFTFWFLFTKYSSKYPSVFDDPMGKFAVCLKLTISVVVVACPCALGLSTPTAVMVGTGVGALNGIIIKGGEILERLNQVDTVVFDKTGTLTVGKLSVTDISIVDNLEELLDIPKNIFWAFVKASESSSEHPIGKAITEKASEFTDVSEIGIESFNAVPGEGVDVVLRWKERTFHALLGNSLLLEHNNVSIPDDFDSKLKLSSSSGLTCVRIAIDGQFVGFLGCMDQVRPDSYQTVSALKQLGKKVCLLTGDQKATARRVAQGLEIDFSDVYAEAVPSQKAEIIQKLKDQKHCVAMVGDGINDSPSLVLADVGIAPINGSGIALESADVILVRKGVLLDTAVSFDLSRVIVKRIKMNLVWACIYNFVMIPIAMGFFLPWGIYLNPMWASAAMMFSSLSVLASSLLLRRWKKPKSLIFSEADDVETESSTNSSVLQKVYTATRSIFGRNKSSNKYQPVANEV O59669 VPS71_SCHPO BINDING 102; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 105; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 113; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 116; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 121; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 125; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 129; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 134; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" SPBC29A3.05; CHAIN 1..139; /note="SWR1 complex subunit vps71"; /id="PRO_0000173559" MFVTPIEHAVQKRKKQKQRSVVDPVTRERQLKRNLADLEKDNFSDIRFEIPKDLLQRRVLPISVRRILSSRKTFVNYLDETPNSRYNTCVAKPSYKPPRKFCNVCGYWGKYACQNCGTSYCSKGCEVIHSETRCMKVYA O59680 CY1_SCHPO BINDING 102; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /note="covalent"; /evidence="ECO:0000250|UniProtKB:P07143"; BINDING 105; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /note="covalent"; /evidence="ECO:0000250|UniProtKB:P07143"; BINDING 106; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P07143"; BINDING 225; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P07143" CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P07143}; COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:P07143}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000250|UniProtKB:P07143}; TRANSIT 1..56; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC29A3.18; CHAIN 57..307; /note="Cytochrome c1, heme protein, mitochondrial"; /id="PRO_0000316219" MFQFVKKKNEFLKFARLGSRAFTQNAQKTHSKGSNIALVSSSLLSVGMIALYYNVYGPSLSAGTPKEEGLHFIQHDWPQSKVLSGFDHASLRRGFQVYREVCSACHSLNLIAWRHLVGVTHTADEAKQMASEVEYEDGPDDEGNMFKRPGKLSDFLPPPYPNVEAARASNNGAAPPDLSCVVRGRHGGQDYIYSLLTGYTEPPAGVEVPDGMNFNPFFPGTQIAMARPLFDDAVEFEDGTPATTAQAAKDVVNFLHWASEPELDIRKKMGFQVITVLTILTALSMWYKRFKWTPIKNRKIFYQRPIK O59697 PPK25_SCHPO ACT_SITE 175; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 59..67; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 82; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 38; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32C12.03c; CHAIN 1..423; /note="Serine/threonine-protein kinase ppk25"; /id="PRO_0000256824" MKPNTTNLRNECWDTFSIPKRSQNIKINQSTKHQRSISDFVGTAGPGRQVGNWIIKKTIGAGSMGKVKLVVNILTGEKAALKMIPFTPNNTSQTVRVQREALLGRLLRHPNICRVIDCIRTPACTYILFEYVPGGQLLEYILARGKLDEDLARSFAMQLINALVYLHKNFIVHRDLKIENVLLTQDSRQVKLIDFGLSNFYSKDDLLRTYCGSLYFAAPELLDAKPYIGPEVDVWSLGVVIYVMVCGRVPFDDVSVPMLHSKIKSGKLEFPSYISEDCCSLIAAMLNVNPRKRCSLEQAAKFPWLKKNSFCLYLPIPLTSIPSTPSIRSHVFKPPFNLKVLQLLHEHGLASIPELKHELYMAYIERKTTSLVCLYLLGVESLAPALRIPTALPPVYSRHQRHHSEILGAMDLTEKITAMQCPP O59706 SAP61_SCHPO MOD_RES 360; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC36.09; CHAIN 1..492; /note="Pre-mRNA-splicing factor sap61"; /id="PRO_0000352806" MSESVLETERYAHEELERLQQAIVDRQVANPKAPRERLRLEHQSAQFLNQFRETSKKLLVSHESSDRLKDQEVARINADDDLTEFYKSLGEIQEFHKKYPDHKVEDLSQLYSIKPSQPGIDEIDTLFRGEEMYGRFMDLNECYEEYINLSNVQHISYLEYLKNLEDFDQIPKPEKNQTYINYITHLYEYLVSFYRRTHPLSNLDKIIAVFDTEFDAAWEAGLPGWYSHNAEAEKDGKDSTEAFYCEVCQKFFGKITVFEAHKKSKAHNKAVKRMQSSSPSTTSNTNEKQKGPKAIARIEFLIKKLTSLLDDVRKDTRENVVRRQTLTAAERLAEVEAAEREAFEQSTPSVSVEGNQDEESDQDDEEKIYNPLKLPLGWDGKPIPFWLWKLHGLGKEFPCEICGNYVYMGRKAFDKHFTEQRHIYGLKCLGISPSPLFNQITSIDEALQLWQKYKVDSKKRETTMASLNEMEDDEGNVMSEKVYNDLKAQGLL O59710 ADRO_SCHPO BINDING 27; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 48; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 56; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 92; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 164..167; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 208..209; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 220; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 375; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 382..384; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P08165"; BINDING 382; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P08165" CATALYTIC ACTIVITY: Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6; Evidence={ECO:0000250|UniProtKB:P48360}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P08165}; TRANSIT 1..38; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3B8.01c; CHAIN 39..469; /note="Probable NADPH:adrenodoxin oxidoreductase, mitochondrial"; /id="PRO_0000337259" MLSRFIKRTYSTQTSSPVVGIIGSGPAAFYTAHRLLRNDPNVKIDMFESRPVPFGLVRYGVAPDHPEVKHVEHKFSEIAESTQFRFLGNVNVGTDVSLRDLTKNYDCLVLAYGAAGDKRLGIPGEDLSGVYSAREVVGWYNSDPRNQNLELDLSQVEDAVVIGHGNVSLDVARILLSNPAQLSPTDINPLFLKSLERSNLKRLHIVGRRNIFSVSFTIKELRELFALSSAVFFAPSFNYSTKWMNETDASGLDRPRKRLLKLLVSEIQKAVSEKRVAPYSKDKKCWNLEFGLTPVEILGHKGNVENVRFQITDSIRTDAESKFTTIPAQLFIRSIGYKSMPLPGMKDVGVPFDDAKGIVKNVNGFVRPGIYTSGWVKHGPIGVIATTMMDAFATADTITKDWKSKKEFLKNSKLGWDGLKKNIKTPVIHWKDWKVIRNAEIERGLRHESLSEKFRSNEDMIKLIYPGKK O59713 DPH1_SCHPO BINDING 130; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:O58832"; BINDING 239; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:O58832"; BINDING 368; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:O58832" CATALYTIC ACTIVITY: Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979, ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108; Evidence={ECO:0000250|UniProtKB:P40487}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P40487}; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:P40487}; SPBC3B8.05; CHAIN 1..436; /note="2-(3-amino-3-carboxypropyl)histidine synthase subunit 1"; /id="PRO_0000083378" MAEVKKSIPKRRFVGKKNRKENNLDGSNRDVENAALVTINSKRSAGRVATQIPEDILNDKAINEAIKLLPQNYNFEIHKTIWHIRLRKAKRVALQLPEGLLMFGCILSDIFEQFCQVETIVMGDVTYGACCIDDFTARALDCDFLVHYGHSCLIPVDQTPIKVLYVFVDIKIDLQHVVSSLKHNLPSNSRLALVGTIQFVGSLNSIKDALQIQDEDGKGGFYVVIPQAKPLSPGEALGCTSPYIEKGSVDALIYIGDGRFHLESVMIANPDLPAYRYDPYSHKLSIESYAHEEMKSIRYSAVEKARTAKKFGLIQGTLGRQGSPKVLENLKNTLRKNNKDFVCVLMSEIFPSRLGQFSDIDAWIQVACPRLSIDWGYAFPAPLLTPYEASAAFNVVPWKEVYPMDFYATNSLGNWTPNNPENRPLPNRKKTGPVSS O59715 DEGS_SCHPO CATALYTIC ACTIVITY: Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488, ChEBI:CHEBI:52639; EC=1.14.19.17; Evidence={ECO:0000269|PubMed:12633877}; SPBC3B8.07c; CHAIN 1..362; /note="Sphingolipid delta(4)-desaturase"; /id="PRO_0000185433" MAESTATTTAVPPPAEESWNADSEDVHQFYWTYTEEPHKSRRAAILKAHPEIASLNGYEPLTKWIVLGVVSLQFTCAYLLSQSSLLSWKFFLTAYFIGAFCNQNLFLAIHELSHNLGFKKTLYNRAYCLFANLPVGAPFAASFRPYHMEHHAYQGVDGMDTDLPTRAELILFDNVLGKAFFCTFQLLFYAFRPLVVRRLPFTLMHFWNIIVQFSFDYLVVRYVGWRALAYFFMSSFLAGSLHPTAGHFLSEHYNMTRTRLIASGPGKETPLETFSYYGPLNFFVYNAGYHIEHHDFPYVAWTRIGKVRELAPEFYDNIPDCKSWCGIIYQFITDSNVGMWCRVKRKQKHADIPTKSMHLHVS O59718 NEM1_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; SPBC3B8.10c; CHAIN 1..476; /note="Nuclear envelope morphology protein 1"; /id="PRO_0000315975" CARBOHYD 237; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 257; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 284; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 356; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNSIARLSDEINKAILATPLDDDEADKEKLANARGRASSATLRHYNRRRSSYSASSLSSLSSKPTEKEVPTRNEKPKHANIMRVVVYWIRVFLKRIYTFFVHSARVFLYHFLNEEKEFTLASFFWGLCRFVFFPVLLSYKRREMLPPQPSVRRPRFYSSYSYPSSHQDPAYSSFKRHRSSNSYSSSSNGNHVRFQPSIAEEEISFNSFSNSLNSEEDVCVSPMKPKEVSLMGKANSNRSGHSHQPQSTQFSPPANDNISKLPSSFTIVNDPLKSPSSSRLRIRNITLCADKIPRPLLNSKLPRKTLVLDLDETLIHSVSRGSRTTSGQPIEVHVPGEHPILYYIHKRPHLDYFLSNVSQWFRLILFTASVQPYADPIIDYLERDKKIFAKRYYRQHCALVDSSFVKDISICNIHLSRIMIIDNSPASYNAHKENAIPIEGWISDPSDVDLLNLLSFLHALQYVHDVRDLLGLRLAK O59721 PUS4_SCHPO ACT_SITE 115; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P60340" CATALYTIC ACTIVITY: Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA; Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25; Evidence={ECO:0000250|UniProtKB:P48567}; CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P48567}; MOD_RES 291; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 293; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 406; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC11C11.10; CHAIN 1..407; /note="tRNA pseudouridine synthase 4"; /id="PRO_0000121975" MTVTNTYNPTLFFTRVVFQRITKFTAKANEENEILFYALFVADLCLDMKGGLIAINKPSGRTSAQCLNELKKIISNSELAQYFRPAPPHPNDRNRRRRKSNRLPDIKIGHGGTLDPLASGVLVVGLGTGTKQLSSLLSCMKTYRATALFGCSTDTYDSAGKIIKIAVHIPTKEEILSGLDAFRGDISQLPPLYSALHIQGKRLYEYAREGIPLPESIKARSMHCEELILKDFIPKEEHTYTDPDEFASKEAIESEELLRPIEGGAERHDLLAKTEQDINPQDGDEKINAKSPTTNSVTDVAKDQTVTNPKKRKFEVTDLARGSRPAIGPIAVLDMTVSSGFYVRSLIHDLGRQVNSEAHMVDLVRLKQGSFALDDENCFDFSEFSAPGWEEKLAAAFKIDLKGDETS O59722 FAB1_SCHPO BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 85; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 90; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 93; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 111; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 114; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150; Evidence={ECO:0000269|PubMed:11895483}; SPBC3E7.01; CHAIN 1..1932; /note="1-phosphatidylinositol 3-phosphate 5-kinase fab1"; /id="PRO_0000185450" MSEVETPTAASPTFPVETSHRLDTLHTSSTEQIIKDSENVVHTTLKLPTSTLSREFWMKDERTNNCSLCETEFTLFRRKHHCRICGKIICKYCLKEAPGFIFRLQGSIKVCRPCASILVNNYSRSQLFNHSLNESKNRDLTEQHPFVTLDELNSNDQVLSSFGDLSSTFEMPNNIHPPEVAPMIAIPSSRSNYDSPGWAHHSIFLDWSKRNLDSNVINVEDSESGKYNALTITNSYDAGPSSVSTDYRPVNFGKVPSYSKLRKNKAFSSAKVSDMYLSADERNRLEDFSKGDRGLSFVNLSPNIKATSYDRLSTVINEPFISRSSSLTDERGLADSGNSYHHFSDSDDESLFNDGLGLSFHANSAIIKQRQQNVASIQRYGNESYLSNFLKAFLPKTVCDYLFPSSTIPDGLPALIENFNARVDKVNHPGGTEEPLPYQGKSRASSVVTSSKSTCILPPWILFSDSFNQLVCTFLGKLLFQMLNDEGVDSPMQWVLCLPKILLKMALDLGPDIRSGDDIDVRSYVKIKKIPGGSIQDCFLVNGVLFSKKASSKSMDRSLRRPRIALLTFSLDYACDEQRILSLDLIISQQEEYIINLVNRICMLKPNLVFAQGQIPSIALKYFEEHGVIAFHGLKESVLYDIARCCRADIISSIDKLSLCPRLGTCGRFQLRTYVVDENKGLRKTFAILDRCSERLGCTIVLRGADYNQLSKVKKIVELVVLIAYHIKLECALLRDKFVNMPELFETTYQSLSRKSLPSFASTAADKEKSQNHEKKSLNSDNQSLRPLENENQSVSSTQGSNSPLELINNLPASDDYSSITKALKTRFLTFSPFLSKPLPRLLNQVNYYQFIRNKLLKDVKLHPYSPTGSFVMKQSENDNVEESYEESYKFFCIDERYHFLEKQWTLYYSHSKLMFSPFSSQRIILLYSIINKETSVPCIGPERCLLEFYRETDCTLGQYIEDSCLNTNVSCGGEYCKTNDMLWHYRSYVHGNSRISVFLESFSCPVPGLEEKIIMWSYCKFCKKNTHITVMSEETWKYSFGKYLEFMFYNSQIRDRFEFCDHSVMAQHVHYFGYCNMALRFQRDLIEIFELFVPSVTLRNNPSYIKELKEKEYKRLKGVIEKCLSSVASRINQIKCDWVTDPEKFESCTSEISKFRTLLSSDYTELYSEFDSIYLNSSTSDYLSLNSILRVLQGKMVKWEQRFLDYQRLYLPSYKELSKIAAAQIKKVFLERPLSQTPLDLPETLENTQIDIYPSFKTESTDDQLEKVTQTNVASNKRVAPYADSMANVGSPESDCFSVATSSDIPKANIDFTNDISTQNTFPASPVSNSGFSRQTYPNISQRQGVNMLSHKRKSASTSDRRFVNASSTSGMNMPISSSISAKISSIQNSTKYSPRKPIPAKDVRVSSLVRRFEELSLQLQEKQKRDEELIKARRKRALPVVPSKPVVEVFNDLNEAFDDENSEDENGINDTKENRATESNFSGVDSMSKERENVSSNEDNSPEAFEDIFGILFKNESGLEEQQNLEPSSQMDKEGSKLPTSGPLADKTSVYRILSAFWNEWNSLNPPPFEFPLQPTEHMFSDSNVIIREDEPSSLISFTLSSPDYLSKMVEIEDSMDEALTNQGLQGSTQFKIENLMLKPTGTHLKYQFEEGSARLSCKVFFAEQFSALRRACGCEETFVTSLARCSLWESSGGKSGSAFLKTFDKKYILKVLSRLESDSLLNFAPAYFDYISKVFFHELPTALTKIFGFYRVDIRNPTTGTICKTDIMIMENVFYDECPSRIFDLKGSMRNRHVESTGKVDEVLLDENLVELIYESPIFVSEQLKSLLHSCLWNDTLFLSKLNIMDYSLIVGIDYTKKELYVGIIDFIRTYTWDKKLESWVKEKGLVGRGPEPTIVTPKQYKNRFRKAMDCYILASQDFETGEGFKFCE O59730 MAP1_SCHPO BINDING 10; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 15; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 24; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 37; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 41; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 53; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 192; /ligand="a protein"; /ligand_id="ChEBI:CHEBI:16541"; /ligand_part="N-terminal L-methionine residue"; /ligand_part_id="ChEBI:CHEBI:64731"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 209; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 220; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 220; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 289; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 296; /ligand="a protein"; /ligand_id="ChEBI:CHEBI:16541"; /ligand_part="N-terminal L-methionine residue"; /ligand_part_id="ChEBI:CHEBI:64731"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 322; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 353; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; BINDING 353; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174" CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03174}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03174}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_03174}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03174}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03174}; Note=Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the zng1 zinc chaperone. {ECO:0000255|HAMAP-Rule:MF_03174}; MOD_RES 373; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3E7.10; CHAIN 1..379; /note="Methionine aminopeptidase 1"; /id="PRO_0000148972" MATEIAKHICCGIDCNNEADRLQCPKCLNDGVKSYFCGQECFRNSWNIHKHLHRPPNVEKREDGTYNPFPKFHFAGSLKPVYPLSPIRKVPPHIKRPDYAKTGVSRSEQIEGRSFKLKRLTPKEQEGMRKVCRLGREVLDAAAAAVRPGTTTDELDSIVHNACIERDCFPSTLNYYAFPKSVCTSVNEIICHGIPDQRPLEDGDIVNIDVSLYHNGFHGDLNETYYVGDKAKANPDLVCLVENTRIALDKAIAAVKPGVLFQEFGNIIEKHTNSITEKQISVVRTYCGHGINQLFHCSPSIPHYSHNKAPGIARPGMTFTIEPMLTLGPARDITWPDDWTSSTASGRCSAQFEHTLLVTETGCEVLTARLPNSPGGPLK O59735 LAC1_SCHPO CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine + CoA + H(+); Xref=Rhea:RHEA:23768, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756, ChEBI:CHEBI:77636; EC=2.3.1.24; MOD_RES 41; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 361; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3E7.15c; CHAIN 1..384; /note="Sphingosine N-acyltransferase lac1"; /id="PRO_0000185534" CARBOHYD 359; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGNNTSRRSQSQKFKNIPSISAGSFSTMPVQHRGRRRRSKSIVGRAAQNAVLRSKEKTWIVPLILLTLLVGWYFVNPNGYIKYGIFLSYPIPGTNPAQYGKGRLDIAFCLFYALFFTFCREFIMQEIIARIGRHFNIRAPAKLRRFEEQAYTCLYFTVMGSWGLYVMKQTPMWFFNTDAFWEEYPHFYHVGSFKAFYLIEAAYWIQQALVLILQLEKPRKDFKELVVHHIITLLLIGLSYYFHFTWIGLAVFITMDTSDIWLALSKCLNYVNTVIVYPIFVIFVFVWIYMRHYLNFKIMWAVWGTMRTINSFDLDWAAEQYKCWISRDVTLILLTALQLVNIYWLILILRIGYRAFTTNDTHDERSEDEDEEVSDEKSSAKKND O59753 RAD14_SCHPO BINDING 116; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P28519"; BINDING 119; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P28519"; BINDING 137; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P28519"; BINDING 140; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P28519" SPBC649.03; CHAIN 1..289; /note="DNA repair protein rad14"; /id="PRO_0000274248" MENSSIVKSPNPTIEEQRNEIEKLKNLTGIEEVHVDGAKVNKRKRTFDEQSEITKDYIEYDFSKIEDTKGGYLLEEKKVEDLREKPAERELREQEERQKKLRLAPLNLDPETAPKCFECDSIELDTKYFDIFHCRVCHTCREKYPDKYSLLTKTECKLDYLLTEPELQDQELLPRLLKANPHQQGWSNMMLYLRYQVEEFAKKKWGSMEALDAEFERREVQKKEMKEKKFEKQLLELRKRTRTSNYSRMSIREKRKHVHSYDEEFEKPNEPGVIVQRCKCGLEIEQLEI O59771 KCY_SCHPO BINDING 12..17; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 39; /ligand="a ribonucleoside 5'-phosphate"; /ligand_id="ChEBI:CHEBI:58043"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 61..63; /ligand="a ribonucleoside 5'-phosphate"; /ligand_id="ChEBI:CHEBI:58043"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 91..94; /ligand="a ribonucleoside 5'-phosphate"; /ligand_id="ChEBI:CHEBI:58043"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 98; /ligand="a ribonucleoside 5'-phosphate"; /ligand_id="ChEBI:CHEBI:58043"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 129; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 135; /ligand="a ribonucleoside 5'-phosphate"; /ligand_id="ChEBI:CHEBI:58043"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 146; /ligand="a ribonucleoside 5'-phosphate"; /ligand_id="ChEBI:CHEBI:58043"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172"; BINDING 174; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03172" CATALYTIC ACTIVITY: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03172}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172}; SPCC1795.05c; CHAIN 1..191; /note="Uridylate kinase"; /id="PRO_0000158946" MYNVIFVLGGPGAGKGTQCDRLAEKFDKFVHISAGDCLREEQNRPGSKYGNLIKEYIKDGKIVPMEITISLLETKMKECHDKGIDKFLIDGFPREMDQCEGFEKSVCPAKFALYFRCGQETMLKRLIHRGKTSGRSDDNIESIKKRFVTYTKASMPVVEYLKSQNRLITIDAEQDPDAVFEDTVKALQPYL O59773 EAF_SCHPO MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 378; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1795.08c; CHAIN 1..994; /note="Chromatin modification-related protein vid21"; /id="PRO_0000065822" MKQKETKTSQIALVDGEKLSITDSFASLFTLDEEEENDSVDNEEIKLTKEKHEKLLLLFWLHCKFPNGLEWLHSSSDLLPEQVSEWFNFYQKYRFKRGRNFNLSARESVTPIVEEPIVPEEPDNLEGVSEETPLKETSLELSEEEIITSKSPIPSPETIHKNIDVEEKETIEPTTPVKEVETTAHAEEEKGPLTPDSEYAARQLTEELANKSSQEEGVDKQLRVVEATEKEHEEDGNEENVTVTKPVEVATDQVESKEVKKKEVSETTEPTAPPVTVAEVLEIEDKVPKVDEVEEVHSPEAKVTENDVENVQSGIDIEKTIQLLNNQEIPSEQQIISVDKATESPVQEVAVDVNEKPVDEIVEPSKLQMENKLPSEKSPTIDRTGVEAPLFELSVSMPLTLIPPSKFSEPVKPELSSEAWLLRTEMSPLHLRLKNAHKYVLSDNWSHAYREEIVRQSLHHLTVAKEKGIWSFRQPKRQNEMPRLKTHRDYVLDEMQWMSIDFSQERKWKIILAHRMANWVMDYHQASDKCTVCTPASLSKNKKPYMQENEHQKDSHEETFNEQIVSHFNLNDNNNNKVLSIPRDSLQFYNAVFSDDIFVTTNSEQIQNCVLNVPMYGPPTENNEYCEEISEKYPITPVSRFAYAKTKLKSTCAKASRKRLFNQLELSPPESFMEKKARSDENQLDGNKIKDDNQKLSSVGTFSVRPPYPPSSKDIRPEAPWLPEEDELLLLLLRRYSFNWEFVASRLTPPGLYIPLAEKRTAWDCFERWIQVDPRAANVQLTGSHARLAQQKLDESLRHSDKVSQHLSLRDEGTPNHLIKHNSYFLLPTVSRHYRPITIFEAIRKILKKREFAKKPTMTKRAIAPSAASTEKLPPVPSPLELSRLKSEREAQIQQIQAQRNFAQLQSQNRALRPQNAAVAAGAQQHNQQLAAFQAVAASQNSSNNSSAGVSPIAGRMVPRLQPYAVSSSLKLTPEQIHQLQQRKQTVPTTERTQ O59774 YPS1_SCHPO ACT_SITE 85; /evidence="ECO:0000250" SIGNAL 1..17; /evidence="ECO:0000255" SPCC1795.09; CHAIN 18..521; /note="Aspartic proteinase yapsin-1"; /id="PRO_0000255598" CARBOHYD 136; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 157; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 250; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 289; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 295; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 354; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 414; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 418; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 460; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 484; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRIWILIFFSFIKLVSSLQYTGNGVLALDFVAKTFPNQENQLEKRDYTYSPSGITSFPLDLQSYTYYTTTLSIGRPSISYTVAIDLDMPYTWLTYYNVMAFNPAYLGIVNSGTQWSTDELRYFLCKKESDSCYFGNASSSFHFVTSPSTFFIRYDDNITVAGINVQDSLSYSHYQALPDFQFGITLKEYVPSSMLPYKGVLGLAASTEINSIDYSDSISSFSPPTFLEQLVKEDILAYPAFSMYLDNQGNGSLLLGAVDTSKYQGQFVALKQTKLTHYAVSIYSVQFLNSTFFSNYSIITDAYFQTRETYIYLPAELAYSVMDNAGAYLSEGYFALNCDEIDLEAALIFQFGCNSTIKVPISLLVIGQVSNICLLGIRPSTDSEIVLGLLFFRNAYTFYHQSQKMIAIGQAFYNATSNLSAIVDQHIPGALTCSQYPTSVASTQLVQTSHFTSTSLSAVNISESVVYSYTSSSSMPSSAIPSFNISLISQNAVANAGNSFSPLSAMVIMMMSAVFLGLGII O59778 BIOB_SCHPO BINDING 69; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000250"; BINDING 73; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000250"; BINDING 76; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000250"; BINDING 113; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250"; BINDING 146; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250"; BINDING 206; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250"; BINDING 280; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:149473; EC=2.8.1.6; Evidence={ECO:0000305|PubMed:10525840}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22061; Evidence={ECO:0000305|PubMed:10525840}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine. {ECO:0000250}; MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 14; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1235.02; CHAIN 1..363; /note="Biotin synthase"; /id="PRO_0000185566" MFTRTIRQQIRRSSALSLVRNNWTREEIQKIYDTPLIDLIFRAASIHRKFHDPKKVQQCTLLSIKTGGCTEDCKYCAQSSRYNTGVKATKLMKIDEVLEKAKIAKAKGSTRFCMGSAWRDLNGRNRTFKNILEIIKEVRSMDMEVCVTLGMLNEQQAKELKDAGLTAYNHNLDTSREYYSKIISTRTYDERLNTIDNLRKAGLKVCSGGILGLGEKKHDRVGLIHSLATMPTHPESVPFNLLVPIPGTPVGDAVKERLPIHPFLRSIATARICMPKTIIRFAAGRNTCSESEQALAFMAGANAVFTGEKMLTTPAVSWDSDSQLFYNWGLEGMQSFEYGTSTEGEDGTFTLPPKERLAPSPSL O59786 HEMH_SCHPO ACT_SITE 385; /evidence="ECO:0000250" BINDING 200; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250"; BINDING 405; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250"; BINDING 408; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250"; BINDING 413; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250}; TRANSIT 1..40; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC320.09; CHAIN 41..423; /note="Ferrochelatase, mitochondrial"; /id="PRO_0000008878" MIRFCPSCFALKRTAPVLNHTSRLGNYFNNTFSKFSVNRMSVSSYSSDASSTVMDESPPNGVTKSVSGKGPTAVVMMNMGGPSNLDEVGPFLERLFTDGDIIPLGYFQNSLGKFIAKRRTPKVQNHYSDIGGGSPILHWTRIQGSEMCKILDKKCPESAPHLPFVAFRYAPPLTEDMLDELKKANVSRAVAFSQYPQWSCATSGASLNELRRKLIEKGMEKDFEWSIVDRWPLQQGLINAFAENIEETLKTYPEDVRDDVVIVFSAHSLPMSQVAKGDPYVYEIAATSQAVMKRLNYKNKFVNAWQSKVGPLPWMSPATDFVIEQLGNRGQKNMILVPIAFTSDHIETLKELEDYIEDAKQKGITGVKRVSSINGSMTAIQGMADLVAEHLKAKVPYSRQFTQRCPGCTSESCAERINFFQDF O59793 ESS2_SCHPO SPCC364.02c; CHAIN 1..384; /note="Stress response protein bis1"; /id="PRO_0000064936" MSLAKKIDDDEKQLVKPVNKEQTYKKPIPLEEDDYIEGLSYIIQQQYFPDLPKLKAEVVLESEEVGSFDAQNESRDEKLKYLIAKNSEDPLRKRLPSLAIHEITKAQLDGENKPISVASYQNKFTSEDNASFGELMEDESRLRAEQHKRRFGVHSQQPSNSIQTIGYSNSDAIKSIAWKEKDKSIKTWNYQPKNALMYTPETNHSSSLSQIKKQSTEIQADATGLSQSFLEAANQPSTDPIVPPSVNETDASVNGYPLVDVNFGQAVGSSSKSYFNIPERPRRERLHAMRVRDIRSHSTNTTITSVDSASTALNSYSTPNSVSRKLTNLTPAARRLVARSYLRSPLHGSSPSASRHTALRTSIPKFSWTPTPRVKSTAPTPKRV O59800 SLT11_SCHPO SPCC550.02c; CHAIN 1..354; /note="Pre-mRNA-splicing factor cwf5"; /id="PRO_0000081553" MSHGPKGDINKQEWEDVEFPSICERCLGDNSYVRMTKEPLGQECKICSKPCTIFRWIKERGQKPGKTQICVGCARYKNCCQSCMLDLQFGLPIALRDAALKLVESGPTNDINREFFAQNQQRLLSNGETAYDSQEASAAARNLVKKVEKRELHSRPPKRKLDDVESKQILKEARASDASLNAERPLFPVKKIINGNVSLSINMEPPKDKKIASLFLIGVEDELADYKIRKHFEQYGPLKSVVCSHRAKCAFVNFKTRSSAEIAAAASPDGNVVIEGFRLKVQWGKPRSLGGPEGEVRNAKLADLVMRGSSHGNKTSQKSTIKNIENEDHENTKSPAVAIPIDPNQPRYRSQIPR O59810 VGL1_SCHPO MOD_RES 115; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 934; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 935; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC550.14; CHAIN 1..1291; /note="Vigilin 1"; /id="PRO_0000310368" MEHLSNLEQPTTMDSYDFQKLTNDENLQGTESQVPSGSKSASTNGLLSAASSAAGSSFGLTPSAILQQKHENAQQGKKQNNSKSFSKKPAIDVHSEDAFPTLLSKTGPSKPRIVSWVRKTASNTSVAGSDSVSRDKIPFSASSRASSTKSTLSSVKETDFVTETLILSPDNQAPRMSFVGKPNSVAEIVRTVMHQTSTRINVSTASKTKNTTFLIQGKTSAVKAARRQILKLIGRRETKTMPCPVFVVGAIIGTNGQNLKSIMDRTSTRIQIPKRNNTANESSDDAKKPEKEENSAASTLDDLEPQYEMTTITIEGDFEGVELAQKDIEAIINERTSNTTVRISHISTELYSLLRGPDGKNIKELEEGRDLKVQIPFAYLDPSAPVNPIVLSGEKSAVRECALYLQGQAEELLRTTIPTMLPIPRRQHRFINGEKGVGIQDILRKSGCSVILPPINGDSDVVSVRGPALNISEGIRLTLERANSTIVDAVNITTAYASSKNPFDIASIVARLFLRSRKLIPLEEECAVQYHLPKREELQSNSNKTVIIEISGKSQEAVREGRAKLLALVNQFPESKFYKVTIDPLLQRYVIGSKGKNLQKLRNEHQVELLVGEYGEEDPDVIVCYIGADDGKSPDQIQKELADLAESVKSSAEASAKIVSEIIQVPSVYHKHIVGPKGTTLNAIIGKSEENVIVQLGKVSYRPDSTDDDVYIRGFSKDVERVVSEIKQVVRDAKNHEILHSHVEEFDFPAQYSKNVIGKNGSNVSSLREDLGVQINVEEGHIRIQGIKKNVEETAARIKSQIEALIDDTILRVNIPNDFHRQLIGSNGKYVRRLEEKFSVRVRFPREDDSSNSTGNELMKPTSPDEVVIRGGKKSVAAAKQELLELYEYEKSIAYTSTIDIPSKAVSRVVGRNGSTVENIRTQFDVKIDIGDVSTEETTPVSVRGAKADVENAIKEISAIAEEVKNLVEKVIKIDREYHRYLIGPNGSKLQNTIKECGGSTDKTETARLISFSNGNSEEERNSVVLRGDKEIVEALETRLLEIVEELKNQVEEKIEVPQRCISSIIGRMGSTRRDIERKTSTMLNIPNVLDPEETVTITIVGSPENCEKAKEMIQEKVASQYTQMITVPDTVYESIMKGILMKKLRSDLKVFVDTPEIKPVQPTEVVLEDHEDGVFPWKLVTHDYTGSSSSEWAVRGHKENVEKAIASLEKSIKQVMENCIAYLGIPTNLHRRIIGSGGSIINKIRKIAQVKIDVPRTPGDEIVVVQGSRAGVVKAKDLIFERLQENQNQE O59816 ODP2_SCHPO ACT_SITE 456; /evidence="ECO:0000255"; ACT_SITE 460; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000250|UniProtKB:P12695}; COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250|UniProtKB:P12695}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250|UniProtKB:P12695}; TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:P12695" MOD_RES 94; /note="N6-lipoyllysine"; /evidence="ECO:0000250|UniProtKB:P12695, ECO:0000255|PROSITE-ProRule:PRU01066" SPCC794.07; CHAIN 29..483; /note="Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial"; /id="PRO_0000020482" MLSANMLRRMHHGVAVTRMLLVSNGKVQVKKSALYPVMAKLARTYATKNYPAHTVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVENEGDVAAMADFTIEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPSNVSGEERGDRVFASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENFKPVVAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRAALNAMADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDSTSEKGFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML O59821 CSL4_SCHPO SPCC1840.11; CHAIN 1..181; /note="Exosome complex component csl4"; /id="PRO_0000079402" MNLVLPGQVVARGAPNGEGTVKRGDYIISTRTGIFDPEKNSVTYPRKVEETAVLPNVGSIVLARVSRINARQATVNISVVDDVCTKDEFQGVIHVQDIRATEKNKVKVQNSFRPGDIVRALVISLGDGSSYFLTTARNDLGVIFAQSSETGEQMFPVDYQHMQTKSGYTEMRKCAKPILDE O59823 VATD_SCHPO MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC965.03; CHAIN 1..285; /note="V-type proton ATPase subunit D"; /id="PRO_0000144243" MASKQRENVFPTRMTLTTMKTRLKGAQTGHSLLKRKSEALKKRFREIVVNIEQAKQKMGRVMQIAAFSMAEVGFAMGNNINFEIQQSVKQPRLRVRSKQENISGVFLPTFEMNLDESIDDFQLTGLGKGGQQIQKARQVYEKAVETLVQLASYQSAFVLLGDVLQMTNRRVNSIEHIIIPRLENTIKYIESELEELEREDFTRLKKVQKTKENAEKADSVTKEEHQGGSNTLQQTKDVGGAIAPAAEVGKEVINEVENSKDDTYSLPSTSTDDEEENDSDEEVIF O59824 YME1_SCHPO ACT_SITE 531; /evidence="ECO:0000250" BINDING 307..314; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 530; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 534; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 608; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000305}; SPCC965.04c; CHAIN 1..709; /note="ATP-dependent zinc metalloprotease YME1 homolog"; /id="PRO_0000317333" MSRVLHPIFLFGKTSFLYSGCSKFGGRLFNNSIVHGWLRTRSYALASGLHPLRKQKLAHFEDLANANMSDPYMQAKLYKELADNFPEAIISRYETQGVARNSACDRYYQEALRKKSWSRSLSNNISLSQSSSSPATSSFSDPKAFSAGVPKFTSDTSSTVSSTPSLNHSLQNSMPPSTPTPPPVWAPTIVSSALGTSSKTPVYVVVDEPRFTKFFRIFKFIAGLSVASYFVLLGMSIFAETSGLNNIMTNTTEQEPMEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDLAHPVVFIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSWTREEYLAMLDVTMGGRAAEELLYGKDKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMDNLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVKGDRDLLRNKLS O59825 TDG_SCHPO CATALYTIC ACTIVITY: Reaction=Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil.; EC=3.2.2.28; SPCC965.05c; CHAIN 1..325; /note="G/U mismatch-specific uracil DNA glycosylase"; /id="PRO_0000185779" MNDIETRDTGTKNDNSSEFNLSVKSHKRKRSFDDENLELEESREETSGGILKKAKTQSFSESLERFRFAHAGSNNEYRKTDVVKNSDTDNGLLKSAVETITLENGLRNRRVNVTKKSTLKASVKKSTLKKKNEVDPALLQGVPDYICENPYAIIVGLNPGITSSLKGHAFASPSNRFWKMLNKSKLLEGNAEFTYLNDKDLPAHGLGITNLCARPSSSGADLRKEEMQDGARILYEKVKRYRPQVGLFISGKGIWEEMYKMLTGKKLPKTFVFGWQPEKFGDANVFVGISSSGRAAGYSDEKKQNLWNLFAEEVNRHREIVKHAV O59828 ALR1_SCHPO ACT_SITE 38; /note="Proton acceptor; specific for D-alanine"; /evidence="ECO:0000250"; ACT_SITE 269; /note="Proton acceptor; specific for L-alanine"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; Evidence={ECO:0000269|PubMed:11244061}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11244061}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 mM for L-alanine {ECO:0000269|PubMed:11244061}; KM=2.4 mM for D-alanine {ECO:0000269|PubMed:11244061}; Vmax=679 umol/min/mg enzyme with L-alanine as substrate {ECO:0000269|PubMed:11244061}; Vmax=350 umol/min/mg enzyme with D-alanine as substrate {ECO:0000269|PubMed:11244061}; MOD_RES 38; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPCC965.08c; CHAIN 1..375; /note="Alanine racemase, catabolic"; /id="PRO_0000114604" MRGAKSVIDLHAIAHNYNVAKQMMLQKNPSGHVLAIVKANAYGHGAVQVARFLLKHCSSIDGFGVSSIEEALELRHGGIYNKIVLLEGFFTEEDELKLIDDYNFSIIIHSEDQVNSFIKYPFNRPVEIWLKLDSGMNRLGFTPSQFMKFYNLLSNNKNVSNIGKITHFAFADMLENPEHTLKQWDIFEKSVAHLPGPLSAGGSAIILGWLNTVCTDWLRAGIMLYGISPFLSKNKDSKTPESVNIKPAMKLVSTIISVKHVDKGQPIGYGGRYVATRDMKLGVVAMGYGDGFPRQVKDGCPVLVNGVKAPIVGRVSMDMLTVDLSDIPDVKPGDEVIFWGTPELTVADIAKYCSDTSPYELVTKLTRRVPLQYTY O59834 FCYS_SCHPO ACT_SITE 61; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q12178" BINDING 59; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q12178"; BINDING 87; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q12178"; BINDING 90; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q12178"; BINDING 159; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q12178" CATALYTIC ACTIVITY: Reaction=cytosine + H(+) + H2O = NH4(+) + uracil; Xref=Rhea:RHEA:20605, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16040, ChEBI:CHEBI:17568, ChEBI:CHEBI:28938; EC=3.5.4.1; Evidence={ECO:0000250|UniProtKB:Q12178}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q12178}; SPCC965.14c; CHAIN 1..162; /note="Probable cytosine deaminase"; /id="PRO_0000310831" MSSTELSEKDLAYLREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRVPDGDVTQHAETRAVGLITKTRRDLEKCTLYTSTEPCAMCSGAIFWSGIRRMIFGLSNENLIKLTQKSGECPPLYINSRDILGAASHPIEVVGPYIEDEAIIPHKGFWDGGR O59835 DPOD4_SCHPO SPBC12D12.02c; CHAIN 1..160; /note="DNA polymerase delta subunit 4"; /id="PRO_0000186053" MKKRTTQAKKSGQNTNIRDVFPHVVRSNSSQSHIGKKVSSEQSPTPDVTITTKTLDERIKEDDELSKEVEEAWNQIMAERISEPIHCENITKVEFILHHFDTTARYGPYLGMTRMQRWKRAKNFNLNPPETVGKILMLEEADEENRKRESLFYDLQTIPG O59838 HSP7F_SCHPO MOD_RES 38; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 39; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC110.04c; CHAIN 1..720; /note="Heat shock protein homolog pss1"; /id="PRO_0000078382" MSSRTNVVGIDFGNSKTVIAVARNRAIDVIVNEVSNRSTPSLVSYGERSRFLGEAAKSAEASNFRNTVGSLKRLAGRTYDDPEIKDIESNFISAKLTEVDGFVGAKVQYLNEETAFSNIQLIAAYFTKIKAIAEAELIGSVSDVVISIPAWFTDIQRRALLEAANIAGLNPLRLMNDNAAAALTYGITKTDLPEPESPRRVAIVDFGHSNYSVSIVEFSRGQFHIKSTVCDRNLGSRNMDKALIDYFAAEFKEKYKIDVLSNPKATFRLATAVERLKKVLSANANAPLNVEMIMNDIDASSFIKRSDFEELIKPLLERLTPPIEKALELAGIKKEDLYSIEMVGGCTRVPIVKEVIANYFGKGLSFTLNQDEAVARGCALSCAILSPVFRVREFHVHDVTTYPITFSWEPIPENPEEDSSLEVFSEGNPIPSTKILTFYRKAPFKLLAAYSKEAQLPGSIKQNIAQYLINDVVPNKDGDLSIVKIKVRLDLHGILVVEQAYIVEEQEVEEPVETSPEEEAEKKTDEPVKMRKVKKLVKVADLSVSVQEDRLPTEVLEKYREAEHQMIATDKLVAETVDRKNALEEYIYDTRAKLDDIYAPFTNEEESSKFKEMLTKAEDWLYEEGEDTTKAVYTAKLEDLMRVGGPIRQRYLDAEEAKRQKVQAEREAAKAATKSEAEKQKPSGKFEEGTGGRAPPPPPAEEVAPENEEVETMEIDEQKE O59852 INV1_SCHPO ACT_SITE 97; /evidence="ECO:0000255|PROSITE-ProRule:PRU10067" BINDING 94..97; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 113; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 158..159; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 227..228; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 280; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 366; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000255|PROSITE-ProRule:PRU10067}; SIGNAL 1..22; /evidence="ECO:0000255" PTM: Glycosylated; contains 67% carbohydrates. This is composed of equimolar amounts of mannose and galactose. There is also a small amount of glucosamine present. {ECO:0000269|PubMed:2187435}. SPCC191.11; CHAIN 23..581; /note="Invertase"; /id="PRO_0000033397" CARBOHYD 37; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 40; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 46; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 57; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 62; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 79; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 168; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 175; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 322; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 399; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 425; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 446; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 452; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 519; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435"; CARBOHYD 569; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000305|PubMed:2187435" MFLKYILASGICLVSLLSSTNAAPRHLYVKRYPVIYNASNITEVSNSTTVPPPPFVNTTAPNGTCLGNYNEYLPSGYYNATDRPKIHFTPSSGFMNDPNGLVYTGGVYHMFFQYSPKTLTAGEVHWGHTVSKDLIHWENYPIAIYPDEHENGVLSLPFSGSAVVDVHNSSGLFSNDTIPEERIVLIYTDHWTGVAERQAIAYTTDGGYTFKKYSGNPVLDINSLQFRDPKVIWDFDANRWVMIVAMSQNYGIAFYSSYDLIHWTELSVFSTSGYLGLQYECPGMARVPVEGTDEYKWVLFISINPGAPLGGSVVQYFVGDWNGTNFVPDDGQTRFVDLGKDFYASALYHSSSANADVIGVGWASNWQYTNQAPTQVFRSAMTVARKFTLRDVPQNPMTNLTSLIQTPLNVSLLRDETLFTAPVINSSSSLSGSPITLPSNTAFEFNVTLSINYTEGCTTGYCLGRIIIDSDDPYRLQSISVDVDFAASTLVINRAKAQMGWFNSLFTPSFANDIYIYGNVTLYGIVDNGLLELYVNNGEKTYTNDFFFLQGATPGQISFAAFQGVSFNNVTVTPLKTIWNC O60062 MET2_SCHPO ACT_SITE 163; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P45131"; ACT_SITE 403; /evidence="ECO:0000250|UniProtKB:P45131"; ACT_SITE 432; /evidence="ECO:0000250|UniProtKB:P45131" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine; Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31; SPBC56F2.11; CHAIN 1..489; /note="Homoserine O-acetyltransferase"; /id="PRO_0000155756" MESQSPIESIVFTDSCHPSQQENKFVQLISDQKIAIVPKFTLECGDILYDVPVAFKTWGTLNKEGNNCLLLCHALSGSADAGDWWGPLLGPGRAFDPSHFFIVCLNSLGSPYGSASPVTWNAETHSVYGPEFPLATIRDDVNIHKLILQRLGVKQIAMAVGGSMGGMLVLEWAFDKEFVRSIVPISTSLRHSAWCISWSEAQRQSIYSDPKFNDGYYGIDDQPVSGLGAARMSALLTYRSKCSFERRFARTVPDASRHPYPDRLPTPLTPSNAHWVVHNEGNRNRRERPCRSNGSSPTSESALNSPASSVSSLPSLGASQTTDSSSLNQSSLLRRPANTYFSAQSYLRYQAKKFVSRFDANCYISITKKLDTHDITRGRGSDSPKEVMKDLSLPVLVLGIESDGLFTFDEQVEIAKSFPNATLEKIISAEGHDGFLLEFTQVNSHIQKFQKEHLIDIMSQTNSFERLDSQVNDTNRESVFGEMEDITSW O60072 ASCC3_SCHPO BINDING 300..307; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"; BINDING 1157..1164; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P53327}; SPBC13G1.10c; CHAIN 1..1935; /note="RQC trigger complex helicase rqt2"; /id="PRO_0000102100" MEVELNYVVNHLEKLGPASFCDTPYSFSLSDSNAELGALSLKVDEILKTNYNLINPEDVTDSDNNEFALKDLTWLQNCCNEISQSSSTELDASVLFEAVIMSLKATEDQCAIQEDLLNLVGLDHIDLISDIVANSSNLIEEYMNQNDTSIAAQLSDGYTSEAGSSATHGQGLLDSLKSRPRRFSRSRDNRGPLFTGQQVFEVEKYPHVYGDKRLGNTISVIGKKFALPAGSEREDYQKYEEIIVPHAQRAPQMQGEKLLEISSMDILCRKTFLSYQTLNRIQSLVYPIAYKTNENMLICAPTGAGKTDVALLAMLQTISNYVESMNLMDESEPLDVHRDDFKIVYIAPMKALAAEVVEKMGKRLAWLGLKTRELTGDMQLTKTEIAETQILVTTPEKWDVVTRKSVGDTQLAEKVRLVIIDEVHMLHDERGAVIESLVARTQRLVETSQQMIRIVGLSATLPNYLDVADFLGVNRYKGLFYFSSAFRPCPIEQHFIGAKGSPKIVNSNIDEACFDKVLKLIQEGHQVMIFVHSRKETINSAKKLREQFFHEGEADLLDNSQHEKYSLAQRDVSKSKNKELKELFKYSMGIHNAGMLRSDRHLTERLFSMGILKILCCTATLAWGVNLPAYAVLIKGTQLYDPQKGSFVDLGVLDVLQIFGRAGRPQFESSAVAYIITTHDKLSHYISVVTQQSPIESRFTDRLVDNLNAEVSLGTVTNIDEAVSWLGYTYLYIRMRRNPLVYGIAYDELVEDPLLGSKRRELVSVAAGRLADNQMIVYNKKNGYLIPKDLGRIASNYYINYQTVSTLNNLLKSKMSEADIIALLSQCSEFSQIKSRENEHRELESLMENSSPCQLRDSISNTSGKVNVILQSYISRAHVEDFTLTSDTNYVAQNAGRITRALFEIAMSRTWASAFTILSLNKSIDRRQWSFEHPLLQFDLPHDLAVKVENQCGSLSLEELSDMSTGELGDLIHNRKMGPTVKKFISKLPLLNINVDLLPLTKNVLRLVLNITPNFNWDMRYHGNSQMFWIFVEDSNGLEILHHEQLLLNKRNVSTSHLLSFTIPVSNPLPSQLYIIAVSDKWLGAETVTPVSLSNVVFHDDSNPITELLDLQPLPITALHDPVLEGICAKRFSFFNAVQTQFFHTIYHTDTNIFVGAPTGSGKTMAAELATWRALHNYPKSKVVYIAPMKALVKERVKDWGHRLVEPMGISMIELTGDTNPDVKAVTNANIIITTPEKWDGITRSWKSRKYVQDVSLIILDEIHLLGSDRGPVLEMIVSRMNYVASQTNKKVRVLGLSTAVANANDLANWLNIRDGLFNFRHSVRPVPLEIYIDGFPGRAYCPRMMSMNKPAFQAIKTHSPTQPVLIFVSSRRQTRLTAKDLIAFCGLEDNPRRFLYMDEEELEMIVSEVEDKSLKLALPFGIALHHAGLTENDRKISEELFVNNKVQILIATSTLAWGVNTPAHLVIVKGTEYYDAKIGGYKDMDLTDVLQMLGRAGRPQFDNSGVARIFVQDIKKSFYKHFLHSGFPVESYLHKVLDNHLNAEIATGTIDCIQGAMDFLTCTYFYRRVHQNPVYYGADGDDQKSIDTYLSKLVVTAFNELEKSACIYRVNEETYAPTTLGRIVSYYYLFHTTIRNFVQKITENAEFDLALQLLAEASEFDDLAIRHNEDLINIEINKSLKYSAACLNLPMVDAHVKAFILTQAHMARLKLPVDDYVTDTSTVLDQVIRIIQSYIDVSAELGYSHVCLQYISLMQCLKQACYPSEIYRASLPGLNASSEKEARDYLNKFAGNKTDELYQMLCNDPNVFDIESLVNSLISYPKMNIEVSQSSSDKLLLYLRRLNQPLNPDFYIFAPLFPKPQSEGFFVLIIDSETQELFAIRRASFAGRRNDDSIRLSLRISMDIPPTCRNRNVKVMVVCDGYPLIYEHKIVLMI O60079 UBP12_SCHPO ACT_SITE 320; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 935; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 19; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 39; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1494.05c; CHAIN 1..979; /note="Probable ubiquitin carboxyl-terminal hydrolase 12"; /id="PRO_0000080612" MDSLSESSTSSYHGKRPRSLSEESQSSSNMDDISQKSISLGDASEISKNLPSIAEQKQLIGELVNNQPELELGQVDNYILSYSWYERLCSYLAEDGPFPGPVDQEDIADLETGTLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPEFPRETVNLGSESHPHLVVEVYPPIFSLTLLSTNAVDANESHKPKKISLSSKSTLEDLLEGVKYTLSLPSDQFRLWRVDTDQPLHRTIDPSSFIKINSKEIIDFLEKSKTLVELGMDSSCSLVAECMINETWPVDRALRLQFLIQQRNNQSSNEEQKQEKRVPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLGMGGQVASIFASLIKSLYSPEHSSFAPRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPDLYEVDEEKIKNTAEECWRLHKLRNDSLIVDLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTNLTPLAIEVVLESKAATIEDLVKYVAEKSGCSDYRKILVTETYKGRFYRFLTQLSKSLLMEISEEDEIYLYELERPYEDGSDDILVPVYHISDDSTNSANSYMSSRDFGHPFVLQLSDNEVTDASFISEKLKLKYQQFTTLKNLKNIDSLESLELGHEDEQVQKGPLDVDMDHSQTPLFEMRVFHDRFEKIPTGWNMSVSNLPLLTERDKKDLESTVDPLDAHSIEEEDDSEFKDVAPGSYPEPSKSNENTKLTAKENDRLLIQGDLLVCEWPEKSYQFVFSVAPSSPQMGRSLWLESKTILSDKKDDSEDSRTITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYRRKTS O60087 AMYG_SCHPO ACT_SITE 203; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 206; /note="Proton donor"; /evidence="ECO:0000250" BINDING 147; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.; EC=3.2.1.3; SIGNAL 1..16; /evidence="ECO:0000255" SPBC14C8.05c; PROPEP 17..28; /evidence="ECO:0000250"; /id="PRO_0000001479" CHAIN 29..450; /note="Probable glucoamylase"; /id="PRO_0000001480" CARBOHYD 383; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRTYWLFLLLGGVVSAESLLSPNKRSKEASMDEWTDQQKGIAMGHMLNNIGDSGMHAKDINPGCIIASPSTDSPDYYYQWVRDSALTIMTILDRFFEGDKGLEPIIVKYMDEMVRLQKVPNPSGDFYAGGLGEPKFNVDGTSYDGDWGRPQNDSPALRAIAFIKYMNYLFENGKEVHEVTVWIEAVLADLDYTANHWTEASFDLWEEIKDVHYFTLAVQKRAMQDGTAFAKRIGAPDQAALYQRTIEPIDLKLGEFWDPGMGVIKGYKGRVDRSGLDCSTLLASLYSNEFDMHILPTLLKLQETMTRDYPVNQGWKQAMGRYPEDVYDGVSKSIGNPWFICTSSAAEIIYKAIAYYDNKGLPELTEYNIHFFMKFAEFGDPYNWSVIRKNMHTYADNFLKAVAEFQHPNGSMSEQFSRDDGHQKGARDLTWSYSSLLNAIYRREAIKGSV O60097 SPT8_SCHPO SPBC14C8.17c; CHAIN 1..526; /note="Transcription factor spt8"; /id="PRO_0000358862" MEAEESESFSYPMLLPSDGLYPEDDDDADMDQDKNPEENVMNEKEDEDVDAVDEKSGEEDVEMDTMEDENENDEDTEQTSEKKETEETPKENPLEKLKQKASTASFYDVVPTLAIPMATSINAFAFTSDLKWLFTGGEDGYIRKYDFFPSINGDLSLTVAQRHPFVDTVTKAGILLNYWENAYDGNKPSSVYSLAAHSRGLWVLSGVNNGDIILYSTRHQEGYPVTSLKKHTAPVSCLALHGSEKKVLSGSWDKMVYYWDLNTGDAISTYNCESGQISNIVYRPSGAVNPWGSESDDMRSLFGTPASSSSYDALFDEEVEKAIEEETKSVQANEENETEKPSQTESTTNNDNIKAPSESSSEESNIFLTTSIDGVMNVWDHRMVDSVLKYPVPKGVPPWAMSACWSPDGNNIYIGRRNGIVEEYNIHSGKEPVRSLKMPLDSGPVSNVYSMPNGRHLVISSFDNIRLYDLQSKAGIGFLIIPGHHGGLVSSLYVDTSCQFMFSASGNRGWQGTTTEVFLGYQIMTS O60100 IMB4_SCHPO SPBC14F5.03c; CHAIN 1..1067; /note="Probable importin subunit beta-4"; /id="PRO_0000120775" MDAQFTLELTQLLFQSIAPDTTQITEATRALETKYLKEPGSLLSLFHIMGTCENPQVRQLAAIEARKLCHKYWSSVDADVQNQIRSNLLDITLKEPESIVRHAFGRVIAALAKLDLPEGKWNELSAFLVQATMDQNDSIREMAVYVLYSIAETVDLDNKLLLDFVNLFSQTITDSSRTVRVTSVQGLGAIAEVLESDDKKLLHAYRATLPGMLLVLQDVVQVGDVDASKQVFDVFNTFLIASGAIISKALGNIIEIITGIANSKQVDDEIRCMALSFIISCIRFKSRKLQALKLGKPLVLTLMEVATEETTDDIDEDCPARLALRSIDLLSTHLSPSQVFYPMFEAACAFSQSPQASYRKAALLSIGVAVEGSSESVAGNLPNIFPIIINGLCDNDMDVRQAALLALSQIAVEIPTEVSKHHAQLLPLVFELMSTQGVKVGKSACNCIDALLEGLDKSEISGYLPMLMERLVGLLEFSDTPDIKSCVAAAIGSAAFAAQDDFIPYFERTMASLSQCLHTTDDDEGYELRGTVMDTLGAIANAVGKQAFLPYTEQLIQLAYEGIQIDHSRLRECSFCFYAVLARVYKEEFAPFLEHIVPALFKSIDQDESDILSERIGAPTAEEISQLLDSVETNEEENDEELEKAMGVNSAIAMEKEIAADALGEICMYVGAPFTPYLEPTVEKLVACTTHFYEGVRKSALSSLWRCATTYYKVCNVPQWQPGLPLKVPVPDTVKNIFEAVRKCTFDTLEEEYEKTVATDILRNFAESIKTCGPVVLGDDYEKLCEVVMEVLQKQHIVQAGDVFDDDFEEEDIVSNEEVDDTEQDALLIDSACDVVIALAVALGGSFADSFKVFYPQIVKYYMSKNGNERAMAVACVGEVAGGIESAITPFTRDVFSLFMAALEDSEGEVRSNAAYSMGLLCQFSTEDLSSEYLNILQKLQPFFTQEVFRTALDNAIGCISRLILHNQNAIPVDQVLPIVFSKLPLKEDYLENAPLYHMILALYRQQNPCLVQHLGELIPVFASVLTGSPEQLNDELRSELLSMVKEIAPQYESVVSNYPQLVALLQ O60102 RLI1_SCHPO BINDING 110..117; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 382..389; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPBC14F5.06; CHAIN 1..593; /note="Translation initiation factor rli1"; /id="PRO_0000316194" MSESLTRIAIVSEDKCRPKKCRQECRRSCPVVRTGKLCIEVNPTDRIAFISETLCIGCGICVKKCPFGAINIINLPTNLESEVTHRYSANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILSGKMKPNLGRYDNPPDWAEVVKYFRGSELQNFFTKVVEDNIKALIKPQYVDHIPRAIKTGDKTVSGLIKARANNNNFEEVMDHTDLQNLLNREVGHLSGGELQRFAIAAVATQKADVYMFDEPSSYLDIKQRLKAGRVIRSLLATTNYVIVVEHDLSVLDYLSDFVCVLYGVPSMYGVVTLPYSVREGINIFLDGHIPTENLRFRSEALTFRLADASDEITADRTAEYNYPDHVIEQGDFKLTIKSGGFSDAEIIVLLGENGTGKTTFCKWMAKNSDLKISMKPQTIAPKFQGTVRMLFLKKIRAAFLNGKFQSEVCKPLSIDNIIDQEVLNLSGGELQRVAICLALGMPADVYLIDEPSAYLDSEQRIIASKVIRRFIVNSRKTAFIVEHDFIMATYLADRVILFEGQPSRDARCNPPQSLLTGMNTFLKNLDVTFRRDPNTLRPRINKFDSQMDQEQKNAGNYFFLEN O60103 DOA10_SCHPO BINDING 8; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 11; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 35; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 38; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 51; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 54; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC14F5.07; CHAIN 1..1242; /note="ERAD-associated E3 ubiquitin-protein ligase doa10"; /id="PRO_0000310692" MNADDEICRVCRCEGAPDSPLFHPCKCTGSIRYVHQECLVEWLGHSKKTHCELCKAKFEFTKVYSESMPRTIPFTILCRKLASTLKQRVIFFTRVLLTFFCWTVLLPLIFKHVWNLNFKIGDTYTIHARNKTFTAPQKPGYFESISQITSSPRLNTLIANTAEGQVLTFVVTFILITAFLVREWVLQNAVQVADELQGQQFENVNQNNQAQAAAAAAQNLREVREARQRLAMVMEHLRERQEQRNLELQRNGSFEEIERARQRFALLGDNIREPQEEENDVDVDEIFNRQQLNQPALDLNDANSSNSVPVEFNSLHSQNVDYRDEVDSLRPQFNVDEQSSISHSSNASENIVDGAVTQANGIESDFTRVDHEPIIVNNDDENGNNESENEEVIEEDNLNRNVIAEAQNQVVADEERNAVARAAQIAEADDADDFDGILEFLGLRGPITGFLQNCLVIAFVVSVFLTTAVGIPYMSGRLMVEWILFIIHRPTFILRFILSFVNILFDWTVGGAFNIVKILTKLPLLSTVFVKLKLQGIFSSSFQQVSNNMYSWIYDHVFSSSDHAYESLIYYMKTGHKQVVQSFSIFPVFRVCQMFAVILKDFVENYSNRPVDRVFTTLIGYCMFTFLGISYLNRKQFLFNDPQIRNVELAFREVLRQCGSIAKFGIIFSIELVVFPIFCGILLSMCLIGTFKKLAAENLLNVMTVYPAQSIFLAWFIGITFMFEFAVFISMVRKIVRPGVLYFLRDPNDPQFHPIREILEKPMLFQLKKIGFSAILYFAFIIGCVGSVIHLLKSTGIIFPIEFTTKPAVFEAPIDLLALEILIFLSIKLFKPLELTRSFWRTLVSTFCRCLRLSSYVMGQRYSDEEGYYPKQYFSFLRRIISKPSDTENQDDGDKQKAKKDFVQDGFFLWCPSKDVVPVRQGAMLIPVTENGYEIFGEKKKVEENADYTITYAPSNFYKRLIALLLFCWICSTLVTVLLVFVPLSLGRAIYAWCFPNVVKHDFYAYAIGFYSISFPMYAIHASVKFLKLDYLRSLMNKLNLKIVMRSLVMALKYLLLAFLGIFILPLLLGAIWELYVAIPFRTIFNRGTLALDAFQNWVIGLFMLRMIYFTVTSNEERFVSRLFQDAFRDRWTNPQILPLLKNVLIPFTSALIAAVVLPSVFTYVTYPFLSSIFPSASKTLMYRLMHPIFLALLGLALLGRRFVETSSKWSQGIRDDLYLVGTRLHNFGESAPPAISESAEK O60105 PUR8_SCHPO ACT_SITE 156; /note="Proton donor/acceptor"; /evidence="ECO:0000250"; ACT_SITE 286; /note="Proton donor/acceptor"; /evidence="ECO:0000250" BINDING 14..15; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250"; BINDING 82..84; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 108..109; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 238; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 300; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250"; BINDING 326; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 331; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 335; /ligand="substrate"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate; Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567, ChEBI:CHEBI:456215; EC=4.3.2.2; CATALYTIC ACTIVITY: Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920, ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2; SPBC14F5.09c; CHAIN 1..482; /note="Adenylosuccinate lyase"; /id="PRO_0000137898" MEDYGSYSTPLTARYASAEMSHLFSREMRINTWRQLWLNLAIAEKQLGLTQITDEAIEQLKAHVKITAPEFEIAAKEEKRQRHDVMAHIYTYGLAAPAASGIIHLGATSCFVTDNADLIFLRSAMDLLIPKLVNVINRLSQWSLRYKDIPTLGFTHYQPAQLTTVGKRATLWIQELLWDLRNFVRARNDIGFRGVKGTTGTQASFLALFEGDHAKVEELDKLVAKLSGFDNVYPVTGQTYDRKIDIDVLQPLASFGATAHKIATDIRLLANLKEVEEPFEAGQIGSSAMAYKRNPMRCERICSQARYIMNLIPNALNTASVQWFERTLDDSSNRRSLLPEAFLFTDSVLKILLNVISGMVIYPKVIQKHIRAELPFMATENIIMAMTKHGASRHECHEQIRVLSHQAGRVVKEEGGDNDLIERIKNTPYFAPIYDELDSLLDASTFVGRAPEQTESFVNKDVSQALAPFKSMITEEKVDLAV O60107 SNX41_SCHPO BINDING 103; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 105; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 129; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 152; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250" MOD_RES 19; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC14F5.11c; CHAIN 1..586; /note="Sorting nexin-41"; /id="PRO_0000213832" MDFFEDNNPFSGSDNRSASSAVNVEPKVEPSQHQGSSSVKENAISQPNESFQSRNMFFQKDVDSVVDSALDPNGIVITGAMKAESGSHIVYIIKLQDSEIHHRYSEFASLRVQLSRLYPTCLVPPLPDKHKIMDYLINVTKNQRMSRMLEERKRLLQLFLRRVAQHPILGLSEVFRKFLSRHVSWKEVLHSPPISCLPKDLLKAPPADPSSKENAELYKELPIPSKTLVPRDNYDDVGKNFLMLEDTLQQYSIVAQEESNLFNQIVLSNSKYCLAHSTLGAMFNALSLSESGKLLTALEKVGQANDHTCLASIDFMHNFVIAVIEPLQELSKDAKNMRHIFIFRKMKFIQQVMVEELLTRKKSFLHLLERRERHAARLQQAIGEVDGDVILNRESEATLGVNNAQTSRSTIPEEDPLFNDEESKEPSVPLMGTDQPLENYHDGNGEQTEECLRDLRHNQSQDFETVSQDTSLTSVTVLPRTIRDVFDRIRFVLNGLTDNNVEVSRHNNIGRTAESVTHLTDMLLITTKDVAFVTDRVNFEFQRYQDTHRQDLNRILNRLTDSHIDWANRNLRIWNSVQESLKTYVS O60124 RRP42_SCHPO SPBC16G5.10; CHAIN 1..299; /note="Exosome complex component rrp42"; /id="PRO_0000139965" MQLSLPELSYTHKSITEFEPAIRNDGRSIDQLRPLSGQVDVLPGTNGSARVKWASSVEIVIGVKAEVGDATPEGGKYVASVEISPSVSIQNRETDEIPSFLTSALQDLLNALAVDYLKFTPSKAWIIHVDAVVILSSSPYENILSALSLAAYLALQTTRLPKISTPNVTDITIGSTKYEPSEEYDVDSEWENALPLQGLELMSVIILVSSIDQVIIVDPTIEESSVAQVTYAIGVQASGAISYTRVVGTGGGYASTGRAITVERYIELLETASTVGTKLLNASSDILSFKGLGFFDILP O60135 LCF1_SCHPO BINDING 246..257; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P69451" CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPBC18H10.02; CHAIN 1..676; /note="Long-chain-fatty-acid--CoA ligase 1"; /id="PRO_0000193118" MKVQSKAISKPKEHESAIYRNANFPDHLVETYSDDVHTLFDVFRHSVKQFGNKKAMGYRNLVKEHVETKMVTKVVDGEKKEVPKSWSYFELSDYNYLSFNDIYDKALRYAGALRKLGLNKGDKFELYAPTSAFWLLTAEACLSQSMTIVTAYDTLGEEGLLHSLRESGVRGMYTEGHLLKTLVNPLKEIESLEVIIYRNDAKEEDIKTIQEIRPNLKLIKFADFEKMSPPVEPDPPSPEEICCIMYTSGSTGLPKGVILSHKNMVAIVTAIVKHVPEVTSKDYLLAYLPLAHILEFAFENICLAWGGTIGYANVRTLVDTNCRNCKGDINTFRPTIMVGVPAVWEMVRKGIMSKLNAASAVKRSVFWTAYYTKAKLMRHNLPGSCVLDTAVFNKIRSMGTGGRLRYTLSGGSALSPDTKRFLSIVLCPMLIGYGLTEISAAAMVQNPACFNLDDSAGSLLPCTEMKLVDCEEGNYNSHGHPPRGEIWLRGPSLTRGYLNRDKENKESFTPDGWFRTGDVGELTPEGLLRIIDRKKNLVKTQNGEYIALEKLESRYRTSSLVSNICVYADQTKVKPLAIIVPNEPVVRKLATEQAGLSPDASWEEVCHNKKVRQLVYDDLIRIGRSHHFANIELIQNVVLVPIEFTPENGLVTAAQKLQRRKILDRFKKEIDAAYAE O60139 UBP4_SCHPO ACT_SITE 236; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 530; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 338; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 343; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC18H10.08c; CHAIN 1..593; /note="Probable ubiquitin carboxyl-terminal hydrolase 4"; /id="PRO_0000080605" MSDDYFDRLFELAFVYINEDETIQSCSFRGQRWLEEAQTLEQKNSLLKAYYYYLKALKLAYEIPCRFEISVKSTHYGEFKQFQKLAIQAVSKAFTIKSKLAVKHYLPVIQISDALSLSKKSSLKVLFLNFYSQESSKGYVFSKHTIAIPISCLQSMDSSKIYDFLKSAPFHPSMVICYSLERYFEDVSLAYKLYSMLRSLKLDPHFMELANPKKVDSSLSYENYQPIGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNASRSPIAPLTEDQLSAREELPLSHFSHIEWNLHLRSNKSIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVMGRKKIDTPLGLSLQIPSKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLENGHYISDVLFNNEWCHIDDSIVRTVGGITDLREDFSSSYILFYKRSSLLEEFEDKCPKMTLKRNVK O60143 RL7C_SCHPO MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 245; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC18H10.12c; CHAIN 1..251; /note="Large ribosomal subunit protein uL30C"; /id="PRO_0000104649" MAVASSTVPSKEQIFAPESLLKKKKTQEQSREQRVAAAAEKKAAQQKKRELIAKRAESYDAEYRKAEREQIELGRKARAEGNYYVPDETKLVFVIRIRGINNIPPKARKIMQLLRLIQINNGVFVKFNKATKEMLQVVEPYVTYGIPNLKTVRELLYKRGFGKVNKQRIALSDNAIIEAALGKYSILSIEDLIHEIYTVGPNFKQAANFIWPFQLSSPLGGWRDRKFKHFIEGGDAGKRDEHINSLVRKML O60145 PPK23_SCHPO ACT_SITE 198; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 80..88; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 103; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC18H10.15; CHAIN 1..398; /note="Serine/threonine-protein kinase ppk23"; /id="PRO_0000256822" MAGSKWETEETNQFAIENQKLEEEWRKKRRLEKKRKRKILEEEEKAEERNIDACRLYLMGNTPELKSCNSIDDYEILEKIEEGSYGIVYRGLDKSTNTLVALKKIKFDPNGIGFPITSLREIESLSSIRHDNIVELEKVVVGKDLKDVYLVMEFMEHDLKTLLDNMPEDFLQSEVKTLMLQLLAATAFMHHHWYLHRDLKPSNLLMNNTGEIKLADFGLARPVSEPKSSLTRLVVTLWYRAPELLLGAPSYGKEIDMWSIGCIFAEMITRTPLFSGKSELDQLYKIFNLLGYPTREEWPQYFLLPYANKIKHPTVPTHSKIRTSIPNLTGNAYDLLNRLLSLNPAKRISAKEALEHPYFYESPRPKDPKFFPTFPSKAKGESKEKNVFQSFRSASPKK O60152 UBR1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; SPBC19C7.02; CHAIN 1..1958; /note="E3 ubiquitin-protein ligase ubr1"; /id="PRO_0000056134" MLQDESSRSLPRSALIRRRLSLFLQSHALMYSFLWSESAKKSLLNEVFSALLGYDHTLWNTLLPERPTIDASFLLRRAQGHSEGDEYRHGTCESKCGHIFRKGEVFYRCKTCSVDSNSALCVKCFRATSHKDHETSFTVSAGSGGCCDCGNAAAWIGDVSCKIHSHEEDATISNDMIDEIPEKLENSIQTTIDCVLDFVLDVFSCSPENLKKMPTLESILQDEKTSRLSENKYGDIDDSCNMYSLVLWNDEKHSFKQFYEQITTALELPNNVFGKKMANIINDIGRACIVTETNIKELLKIGQKLAQINLAVSIRSMRDIFREESCAVLLEWLADIAGSSICGKRNYFSSVICKELVRPWNCGLHNSDLTFRLSLRSLALPEIVAIDSPDIFLNEDHINSSGPSDTSSHMLETDESSIHSRHWYPSNSLPDVLSYASRVRFDYFFLYDLKLWKSLRYKLQELYLGYFITQPGFKEIMGARIAISYRRLAELFLLLDREPEHSVIFFSMQIFTVADVAKLLVTEYDFLTTINATLYTFFTYKKLNTPNYVDQHAMIRTDSAAFHSRRYIHIFHHIQFMLSIPCVAEIVREDLKFLKQYADFFNLFQGMCPYTRAVSQHVEWENDSWMYVLNVSLQVAKLCRHVGNVFMELNTNKLANAINYLISLILYPKARNESWTNTESLTTGITVDERGNSKLIEYDIALQPVSFHHPLHWLLVYLLSFYVERDNYKLLWTQLDLLAVTDHPLRVCAWLSQMRAKLWIRNGTTLRDQAHHYRNLSFHEYTFDLDVLLLQLTLTYGDPDAILPSFISRFQLEDQMYGRFFVPHKHYDVSQVTIMMEEFLLLLISIVCNTAVLDHWDITRRIEYGIAHILCFRPLPYSEITKRTCEHLLEHKQFESTLKKVATFRNAEGINDSGSFTLKDEYFDYVDPFNIHYSRNQREEAENILRRRYSKQHSKHLESVVYEEYHPILHSNITIPILQSDSFVGILWHTIVYAYIYPYDQGKLEGLVNTALHACLLVLMSEKGSEPIFSKKICENRFPVVEGLQEYCNSPDVTLFSVLCQMKNHRNFVYVKEKISLIMKILKSEVPLLYEPVYAETLSISSSKIVQSLSDAEQQEQHLAKVRMAKERQARIMEQFRMQQNKFLENHALFEASDCEMDEADEFSVTSSVSTKLFLDPPIDTCLLCQEELKDKRPYGTLVFVLRSSVLRLFPADDANYVSEVLDIPDSLDHEIQERPFGLAGKRKKVLDSTEAYDYDNYYYEKKGNELHQLKDSFNGFPPDQLDRGLHATGCGHFMHIDCFKNHIATVTLATRANPYRNHPHNLSMKEFLCPLCKALCNTIFPILWRPKEEINFQEAGVLTAPLKNWLVSKTFSFNKDLNQQLLDIETSPSEHTQSYNLNLLDVLQHTLRDSLKDIYTLNTGADNSSDNVEENADNLFQSSVLDHVHFKSVVNNEVPADERLAISDDIFELYRRLDDVIDLNSSLYSDDFIPVNGKLHNVVKLFSYSLCQVEASTRGHIKCSSIPADIWVHNLGKNQQVFLRILSESIKTYTLLCAHDSQKRIGGSIQEFEFISFCQQKRIFGRLLPSLDSPVTKSITDDRVEPLLVKDTFREFAEASVSGLLSCDESFHYLTQLYYTADIVRNLWILLSQRNSLLKCMESVEFEAFDYEQLKGFEHLVIQIWKSLRVDGAGLINFDCCTEDDLNNPHLLFTLYKLLERFSLIFLRKCALLWYCRYGVSFETQPNLNFQNSELSRLQTKMHIPGVIELSNHLCLTASSTEWSLIKHWCNFFTETGPLCDFPRAYYPGIYELVSLPYELDKVFELLLARRCSKCLTEPMEPAICLFCGKLLCFQSHCCSFNGIGECNLHMQQCASDIGIFLIVKKCAILYLNPPVGSFSVAPFLDAYGETDLGLRRGRSQYLSQKRYDETVRTMWLNGSIPSYIARQLDANPDTGGWETL O60157 TYW4_SCHPO BINDING 66; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 92; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 119; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 165..166; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 193; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543, ChEBI:CHEBI:74275; EC=2.1.1.290; CATALYTIC ACTIVITY: Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119, Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231; SPBC19C7.08c; CHAIN 1..681; /note="tRNA wybutosine-synthesizing protein 4"; /id="PRO_0000226144" MSNKNQRKTKSKDREVRKTNDSSILSKASVEKCGYPGFTVGHSYYQPFIQKSPRRSPSVNRGYWTRCMAIRFAVYQFLKNKTGKRKAIVNLGAGYDPLAFQLLSSHEYNTDDVVFYDVDYPETIENRVQMIRSDSFLSSIVLEDKEFDLDGTEIHTKNYHSFGCNLNLLNQLESCLEKYGIDYCNDAILFISEVAAVYMPRQASEKLIRWMSKFPDAHSCFFEQIAPATFDHPFANVMVKHFKEWGTPLHGLYAYPTIESLKSRWVKNGWEYVEILDVCTFWNFLMDSKLKHLCEMVEPFDEWEEFYFFLQHYSIQHASSKLVGKYDLVESPDPCMQYIRYVKSEIIFNNSPLTLRNSIYSLKRTDLPACLKELPSLRLPAVCDLDDSVIVQGGLSTAGRSKDAYLISEKDDGSIMKITTDSLTSCMGQSVVSIDKKTCMFIGGRESPKKILSSCIYFADGNWSDFPSLPYASHRASSVSIKHNGSSYVVLLAGKPFGGCLIWSDSKRKWNTLKCKDPLFYSRWGACLHWSSKLKKGILCGGMNELNEPVREVLEWEMVLRDDDHFEIVTRVLNFDVQVEILLSRIGSKVVFFGDDSKPIIVGGAAVFRTILWEEESVCINMNDYSVTGVCIEETEKRPVFTMFGISGMGNHLQIFGGGCICFSFGSCLNENATFYKLVSA O60159 YHYB_SCHPO SPBC19C7.11; CHAIN 1..766; /note="Putative anion/proton exchange transporter C19C7.11"; /id="PRO_0000310340" MSSQKRADSSSSFDQAERRSLDENERKKKYFFNREGSGIDNFETDDRVNEIINEQNEENVIDQSRWSKLWRIWNVGYSWFILSIIGTTVGFAAYMLDIVTSWLSDIRRGYCTSHWYYNEKFCCWYSETMGSSCTAWKPWTYKFSLNYLIYTAFALLFVLCAAIMVRDVAPLAAGSGISEIKCIISGFLRDSFLSFRVMLVKCVGLPLAIASGLSVGKEGPSVHLATTIGHNISKIFKYAREGSIRYRDICVASAASGVAVAFGSPIGGVLFGIEEMSGGYDPKMIVYSFFCCLSAVGVLHMLNPFRTGQVVLFEVRYSGSWHFFELLFFCFLGIFGGLYGEFVMRLFFLIQKLRKKYLSRWGVLDAAFVTVITSLVSFLNPWLRLDMTLGMELLFQECKSSSSPELINLCDPSLRTKNTILLLIATFARTIFVTFSYGAKVPAGIFVPSMAVGASFGYMIGLIAEMIYQRFPNSVLFLACHGSESCITPGTYALLGAAASLSGIMHLTVTIVVIMFELTGALNFILPTVLVVALANSIGNMLGKTGIADRSIEINGLPLLEPEKSINSSNTINIPITEVMASNLITIPSIGFTWRKLLGMMEGYDFSGYPVVLDSRSNYLIGYLKKSSLKSSFEAAKLEPSFTFDQQLCFGKVDSVGDSKSSKFGESDRIDLSAYMDVNPISVLHTQSIANVAVLFEVLSPSVIFIEKDGNLVGLISKKDLLLASKYYQEDNDLVNPANRHRAVSTERINDSYENIELKPLKLNIE O60160 OMH1_SCHPO ACT_SITE 279; /note="Nucleophile"; /evidence="ECO:0000255" SPBC19C7.12c; CHAIN 1..390; /note="O-glycoside alpha-1,2-mannosyltransferase omh1"; /id="PRO_0000316587" MVRLPRKFKRVLLLVVLLTLVVFVRFKKQYIPTISVFEGSLIDNRDTLSYFNISNLEPSERSEWLPNKRVNAAFVTLARNEDLNDLLKSIRKLEKTFNHKYHYGWVFLNNEEFSDEFKEHVIEAVSGKCEFGLVPQEQWSIPEYIDQDKMHENWKKLQELGILYADKESYRHMCRFESGFFYRHPLVQKYEYYWRVEPSVDFFCDLDFDPFAYMKENNKAYAFTITVTEYSETIPSLWPSTKEFIKMHPNALHPNNALNFISNDDGETYNGCHFWTNFEIAKVDFWESEVYSKYFDYLDKSGNFFYERWGDAPVHSIAVSLFADRDNIHFFNEIGYWHPGSGHCPLDDATRAKCDCDPYESIDYNGWSCLDKFYTAFEMPFPENWSFYSH O60163 AK_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; MOD_RES 326; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 328; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19F5.04; CHAIN 1..519; /note="Probable aspartokinase"; /id="PRO_0000066689" MSIAKNIENDPSKGWVVQKFGGTSVGKFPIKIAVDVAKEYLSTKRVALVCSARSTDTKAEGTTTRLIRATEAALRPAVGSVHDLVRIIETDHVQAARDFIQDVGIQDELIDAFHADCVELEQYLNAIRVLSEVSPRTRDLVIGMGERLSCRFMAAVLKDQGIDSEFIDMSHIIDEQREWRNLDASFYAYLASQLASKVTAVGNKVPVVTGFFGMVPGGLLSQIGRGYTDFCAALLAVGLNADELQIWKEVDGIFTADPRKVPTARLLPLITPEEAAELTYYGSEVIHPFTMSQVVHARIPIRIKNVGNPRGKGTVIFPDTISRHGSATPPHPPKIMPDDISASLANKGATAVTIKDTIMVINIQSNRKISAHGFLASIFAILDKYKLAVDLITTSEVHVSMALYEESDDGNMHEAFVELRRLGTLDILHGLAILSLVGKHMRNTTGYAGRMFCKLAEAQINIEMISQGASEINISCVIDEKMAVKALNVIHKELLEPLALHEVPSQASMLVEKPWLYSA O60164 PESC_SCHPO SPBC19F5.05c; STRAND 16..18; /evidence="ECO:0007829|PDB:8EV3"; STRAND 63..65; /evidence="ECO:0007829|PDB:8EV3"; STRAND 150..152; /evidence="ECO:0007829|PDB:8EV3"; STRAND 177..182; /evidence="ECO:0007829|PDB:8EV3"; STRAND 184..193; /evidence="ECO:0007829|PDB:8EV3"; STRAND 196..203; /evidence="ECO:0007829|PDB:8EV3"; STRAND 357..360; /evidence="ECO:0007829|PDB:8EV3"; STRAND 379..382; /evidence="ECO:0007829|PDB:8EV3"; STRAND 400..403; /evidence="ECO:0007829|PDB:8EV3"; STRAND 414..416; /evidence="ECO:0007829|PDB:8ETG" HELIX 12..15; /evidence="ECO:0007829|PDB:8EV3"; HELIX 19..26; /evidence="ECO:0007829|PDB:8EV3"; HELIX 30..39; /evidence="ECO:0007829|PDB:8EV3"; HELIX 50..53; /evidence="ECO:0007829|PDB:8EV3"; HELIX 66..73; /evidence="ECO:0007829|PDB:8EV3"; HELIX 76..97; /evidence="ECO:0007829|PDB:8EV3"; HELIX 100..108; /evidence="ECO:0007829|PDB:8EV3"; HELIX 116..122; /evidence="ECO:0007829|PDB:8EV3"; HELIX 126..131; /evidence="ECO:0007829|PDB:8EV3"; HELIX 133..145; /evidence="ECO:0007829|PDB:8EV3"; HELIX 154..174; /evidence="ECO:0007829|PDB:8EV3"; HELIX 216..241; /evidence="ECO:0007829|PDB:8EV3"; HELIX 251..255; /evidence="ECO:0007829|PDB:8EV3"; HELIX 259..261; /evidence="ECO:0007829|PDB:8EV3"; HELIX 366..375; /evidence="ECO:0007829|PDB:8EV3"; HELIX 421..430; /evidence="ECO:0007829|PDB:8EV3"; HELIX 554..557; /evidence="ECO:0007829|PDB:8ETG"; HELIX 571..597; /evidence="ECO:0007829|PDB:8ETG" TURN 54..56; /evidence="ECO:0007829|PDB:8ETG"; TURN 350..355; /evidence="ECO:0007829|PDB:8EV3"; TURN 384..386; /evidence="ECO:0007829|PDB:8EV3"; TURN 436..439; /evidence="ECO:0007829|PDB:8EV3"; TURN 561..563; /evidence="ECO:0007829|PDB:8ETG" CHAIN 1..607; /note="Pescadillo homolog"; /id="PRO_0000186191" MARVKQKGKAGAARIYITRNQALKKLQLTLADFRRICILKGVYPREPKNKKKANKGSTAPVTFYYTKDIQYLLHEPIVQKFREYKVFARKLSKALGKGELETAKRLEARKPTYSLDHIIKERYPTFHDALKDIDDALSMLFLFSTMPVTDKIGAATVANCERLCAEFQHYVIRSNSLRKAFLSIKGIYYQAEIFGEQITWIVPYKFAQSVPTDVDFRIMHTFLEFYQALMGFVNFKLYNTLGLRYPPKIDVAKSESAAGLAAYELEESSSLPAIVHGNNKNARKNIATLKSKIRDIVNSDANVVEQSEKTTEDADEEPETEENLDEFKPADGADNEDSKSLVSHISSSNTSLFSNFTFFLSREVPRFSLEFVIRAFGGKVGWDPILGSGSPFSESDPVITHHICDRPHISQKYEGRIYIQPQWVYDSINKGILERTDLYACGATLPPHLSPFVKVGENDYDPEAELSAEENDDVSEALDDNISGEAVPISKKNDEPENVEQIDDAEEEDLEHQRELEAEAGGVAYSEYVKQNSKSAKKTKKRQRDTLTAEEKEEKEAKELSKMMMSNKQRKLYSKLKNENSKNENYNNALRNRKRDIEKRKKLKVEN O60174 SFC6_SCHPO SPBC21H7.05; CHAIN 1..582; /note="Transcription factor tau subunit sfc6"; /id="PRO_0000307796" MGPKSKEYENPSSYKNDEDNDDDGDFVLENVMSEEDIEIETPSRNRKRVSTTRRTPSKPIRSQPLTPSSSKGAGNEPKSQNSSTTRGSAKKQSSKGLEEKLINSYGTHVESLNKGRRLIEIWKYYETAPGQSSFEGQTSSDSKLQTLLNLDGQQLLSYSENPFYLFEVKNLSISFHFESPQQVEPCQPVNPFKENPQKSGFVVNTGIPLSSVSWLPTNKETQFLAVGGMLKFSETTESVFMRTSGRNQIQLWKLENKTNFKSEFILYHDWGSVLQLEWCPTISVEDSILGFLAVVCSDGKLRVLRVPRSPVKFHVFVEQADFTFGFNDSLISCCTWVSPEHGDIHQILVGCSNGYLALWDILSSQECPLFYIPYHDSYIHNVVQCLDDFPWLFLTTAFDCYTRIFDIRDPIIDNRPLSHKRDICYTITWNNMLQSIISCSESQSVVIESLRGTSTQLLDERNGSIISLSNSKFHPFVACAASDGIVTIVNPFRLLGFSHKQKANVHRIFQLEYSEKQDSYRMLDGFRPRLPKAKKLDMYIYPWQIQVNKVEWNGNKGYAGWLASGMACGILRVEDLSAVERR O60177 YG42_SCHPO BINDING 416..423; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPBC23E6.02; CHAIN 1..1040; /note="Uncharacterized ATP-dependent helicase C23E6.02"; /id="PRO_0000310787" MRNNTAFEQFTLNPCEQIPLDDKHNIGFNKNNTPDYSSSASSDQLLKNDINRHEMERRIAFLNRKQALFNAFMHDSSSSLNTMESNIEKVNGLFPNDNSVIALKPNEEKLNSSLSVENNDSTYTDATLIAPKIGLDRPNINAITIDVDGHSLQNEISSSTDKLSPSQSDALFEQKQDSLFWNDNAVIVVSDSESDDNNVRTKSSLNDHDKVNMKEKRNLELAFMNSKRKKLELPSLPVLSTAGPSYTNSLALPPFHHHNNYKMFNTTHTLEDDKFLQGKGTSNNPISLSDEEDNEINFQNKRYGSDSVILPGGLLHDSKLPEPGKHLFHLQWYHDRFHNIEGFNLSDSNNQKVQDDQQQQLEELFKDLDEQLVNDPTIREGTPAGLIPTLMEHQKEGLMWLKRLEESSKKGGILADDMGLGKTVQALALLVTRPPESKSVKTTLIITPVSLLQQWHNEILTKIAPSHRPTVYIHHGSSKKHKIAEQLMSYDIVLTTYNVIAYEFKNKMAYDKSIEDNAPIKKFEHLPFFEAEWYRVILDEAQTIKNRNTLAARGCCLLESTYRWCLSGTPMQNGVEEFYSLIKFLRIKPYSDWSSFSKDFTIPLSSNINTSAPMKRFRGLLKAVLLRRTKNTKIDGKPILTLPPKTAVKSETDLSSSEMEFYNTLQSGAQIQMRKYLQEGTITTHYGSLLVLLLRLRQACCHPWLIVAREAAVDDNDSFQAKNRAIYNQIYPEAVNRLKLIETLQCSLCMDVVAELLIIVPCGHFLCRECLTHVITSSEDMAKQTSNENISPKCSVCEEYIDTERLLSYALFRRYSGMAPIVDADNKLRTENISELLPKQYSNILENRQMGMKIFTDPKHWTTSTKIEKALNAVKEIIKKQPTDKILIFSQFVSFLELFTVPFRQEGIKYLMYTGGLSTAERNQALINFEVDPNVRVLLISLKAGNVGLNLTCANHVIILDPFWNPYIEEQAVDRAHRIGQDKPVNILRIVTNNTIEERVLALQDRKRELIDSALGEKGLREISRLNTKELSFLFGMSSR O60187 SID4_SCHPO SPBC244.01c; CHAIN 1..660; /note="Septation initiation protein sid4"; /id="PRO_0000097755" MDEAFGDSLSTDYRWLGHSHFDSHPSAGDSIYFDSLDEDADPSRTARIDRIAELLDGLNDEQISELVNGVNSTTIKENTKKEISNPNDSTRLPLEQIPGSNNLFLDPRHQLGDNSQNAQRHHEPSFNSEKASYTSTPYKNVAPKVIDSPSARHMHSNSPSFPPSQSHTSSYDQSPKGQLRDNISVPNQQDGLDPEVFNQQSKETKKSLQVPPSRNVPPPVTRPNQYNPEPNFSLSSGYPQQHFSQPELQNRNVHLETVPESYPVPPSGYPLTSSTCVSSISQPIQSTDCQKAQENLSNNKQMSSNDQDIDPFKQAITDLPPSFVNIVLEMNATIQSLSNQCQQRDKQIENITKQLLMNQQDYCPTTMSTTVSTPLCPPKRFPKSTKDFKEQKPDTKQVRSATISNDFNLKGNGRYNEKSQIAVPSEIRVQLSTLDAILLQFEHLRKELTQARKEIQILRHTSQNGDQESNESSKNAITTKTTDKGNNKENTMLNDGSTAPAKNDIRNVINTNNLDAKLSDESELMIEKNKSYSTPASSTIPTFHTSQPLTSLNMPDSRFNLAKEKQLYYRLGLQHIDQQCSVETANMLKTVLVQLNIPFAIFPSTIGQVRRQLQQGRRLYQWARNIHYLIYEENMRDGLVSKQCLADMLKKIRELKKRSL O60198 METK_SCHPO BINDING 10; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P13444"; BINDING 16; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q00266"; BINDING 44; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 57; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 100; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 166..168; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q00266"; BINDING 234..237; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q00266"; BINDING 245; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q00266"; BINDING 245; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 251..252; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 268; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 272; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P0A817"; BINDING 276; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P13444"; BINDING 276; /ligand="L-methionine"; /ligand_id="ChEBI:CHEBI:57844"; /ligand_note="ligand shared between two neighboring subunits"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A817" CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000269|PubMed:10620770}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P13444}; Note=Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate. {ECO:0000250|UniProtKB:P13444}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13444}; Note=Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate. {ECO:0000250|UniProtKB:P13444}; SPBC14F5.05c; CHAIN 1..382; /note="S-adenosylmethionine synthase"; /id="PRO_0000174450" MAQTFLFTSESVGEGHPDKICDQISDAILDACLKDDPFSKVACETASKTGMVMVFGEITTRSQIDYQKVIRNTIKSIGYDDSEKGFDYKTCNVLVAIEQQSPDIAQGLHYEKALEELGAGDQGIMFGYATDETPEKLPLTILLAHKLNAAMSVARRDGSLPWLRPDTKTQVTIEYEEENGAVIPRRVDTIVVSAQHADSISTEDLRSEILEKIIKPTVPAHLLDEKTVYHIQPSGRFVVGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYSKVDRSAAYAARWIAKSLVAAGLARRCLVQLSYAIGVAEPLSIFVNTYGTSSKTSAELVEIIRKNFDLRPGVLVKSLKLQTPFYLSTASYGHFTDQSKPWEQPKELKF O74215 DAK2_SCHPO ACT_SITE 223; /note="Tele-hemiaminal-histidine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00814" BINDING 58..61; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 109; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 114; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 413..416; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 459..460; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 511..512; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 572..574; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216; EC=2.7.1.29; CATALYTIC ACTIVITY: Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378, ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216; EC=2.7.1.28; SPAC977.16c; CHAIN 1..591; /note="Dihydroxyacetone kinase 2"; /id="PRO_0000121521" MSVKQFVSDGHIVRPYLLGLARSNPGLTVIEHDRVIYRTASAPGSGDLPKVTLVSGGGSGHEPTHAGFVGDGALDAVACGDIFASPSTKQIYSALKAVASPKGTLIIVKNYTGDIIHFGLAAERAKAAGMNVELVAVGDDVSVGKKRGALVGRRGLGATVLVHKIAGSAAALGLDLHQVAQVAQSVIDNAATIAASLDHCAVPGRKFETNLGPDEYEIGMGIHNEPGTFKSSPLPSIPELVTEMLSILFGEKNPDNSFVEFSSKDDVILLVNNMGGMSNLELGYATEVVSEQLAKRGIIPKRTMSGTFVTALNGPGFGITLVNASKATPDIFKYFDLPTTASGWNVSYHNAKDWEVLADGKVPTAPALEHTRNEKHSGVKADPKMFTKILKAAVDAINEFEPKTTWYDTIAGDGDCGTTLVNGGEAITKAINDKSIRLDDGVNGIDDLAYIVEDSMGGTSGGLYSIYLSALAKGVHESGDSELSVHTFAFASKYALDALFKYTRARKGFRTLIDAIQPFVETLNEGKGLDAAAKAATEGSEQTRKMDAVVGRASYVAKEELHKLDSEGGLPDPGAFALAAILNAIVEASEH O74311 NAA30_SCHPO CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]; Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256; Evidence={ECO:0000250|UniProtKB:Q147X3}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256; Evidence={ECO:0000250|UniProtKB:Q147X3}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256; Evidence={ECO:0000250|UniProtKB:Q147X3}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256; Evidence={ECO:0000250|UniProtKB:Q147X3}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein]; Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256; Evidence={ECO:0000250|UniProtKB:Q147X3}; SPBC15D4.06; STRAND 3..5; /evidence="ECO:0007829|PDB:7L1K"; STRAND 22..25; /evidence="ECO:0007829|PDB:7L1K"; STRAND 44..51; /evidence="ECO:0007829|PDB:7L1K"; STRAND 55..62; /evidence="ECO:0007829|PDB:7L1K"; STRAND 64..66; /evidence="ECO:0007829|PDB:7L1K"; STRAND 68..76; /evidence="ECO:0007829|PDB:7L1K"; STRAND 88..91; /evidence="ECO:0007829|PDB:7L1K"; STRAND 104..113; /evidence="ECO:0007829|PDB:7L1K"; STRAND 119..121; /evidence="ECO:0007829|PDB:7L1K"; STRAND 127..132; /evidence="ECO:0007829|PDB:7L1K"; STRAND 142..147; /evidence="ECO:0007829|PDB:7L1K" HELIX 9..11; /evidence="ECO:0007829|PDB:7L1K"; HELIX 12..19; /evidence="ECO:0007829|PDB:7L1K"; HELIX 29..36; /evidence="ECO:0007829|PDB:7L1K"; HELIX 79..81; /evidence="ECO:0007829|PDB:7L1K"; HELIX 92..100; /evidence="ECO:0007829|PDB:7L1K"; HELIX 122..124; /evidence="ECO:0007829|PDB:7L1K" TURN 116..118; /evidence="ECO:0007829|PDB:7L1K" CHAIN 1..150; /note="N-alpha-acetyltransferase 30"; /id="PRO_0000310302" MVTIVPYSHQYLKDICQLIQKDLSEPYSKYVYRYFVHQWPEFSFVALDNDRFIGAVICKQDVHRGTTLRGYIAMLAIVKEYRGQGIATKLTQASLDVMKNRGAQEIVLETEVDNEAAMSFYERLGFCRYKRLYRYYLNGTDAFRYILYPN O74331 RLP1_SCHPO SPBC1685.11; CHAIN 1..363; /note="DNA repair protein rlp1"; /id="PRO_0000122947" MNAAEWVAELKRKSQIESFKEQKGLVYDDHIEKVLYSGSVNGTLLVIEGNSCSGKTELLYHLASNVLLRSSQELVLIVSSEWDWSIKRLTFILHERLISSRGVSQTCKCNCAVKLENESTVHLQNAAREDGTDEDINSNSVNDVSLSSGETMLQFPEHEEQHECNREMEQLYESASSTVYPCSFWEDAERKIDAQCAILWPMEFSGVVESIPQSTKDLLRIWKEAKIQMHEDFRCNKTEFNEACFDASSSRLGCILMDGLSTFYWQLRLERGYTQVYADLQNRLCTSSKLFGCPVVCTNWLLNNKQHLPIQCKRFRSERRANARFYLENCVSKLGETFYLSVKGVQTKTEMASPYSQQEMEKV O74333 NCE2_SCHPO SPBC1685.13; CHAIN 1..183; /note="Non-classical export protein 2 homolog"; /id="PRO_0000350998" MVGIRQYGVFTWVFRTFQLAIDTIVLALASALVNQQTSGGSPGKINFSVAVGSFAILTFFLTAVGRFLPTILGNPWLIAFYDFVNWVFALTGGCCIAVAIRVHACDNQKYLDRNHYTQGSMRRCQELKALCFFLWFMFGLYVASFIVQIFIAKNDTPNYTFRGRGRGKGSGPAVAPRPVMSAV O74335 RGA5_SCHPO SPBC17F3.01c; CHAIN 1..361; /note="Rho-GTPase-activating protein 5"; /id="PRO_0000097313" MTVVVGVLQIDDMGKKSSFASWWKQLRVKKSDDNKLFGLSLTRALEVSKVAIFLTRRDGEKVFYGYIPAVVAKCGFFLKQNATQVKGIFRVNGSSKRIQILQKAFSTGPDYGRSFDWEGYTVHDAANVFRRFINLMPEHVIPLEYYERFREPMTIPNLTDNERVEMYRRRIDELPIPNRQLLLYLLDLLSVFAMNSSKNLMTADNLAAIFQPGILSHPDHEVYSKDYQISQTALLFLINHQGSFIKTIPLSSLPPLVAAPTSPNTSSTLITQSAAPTPIASTSIRINSFNPRNGSIKRWRSFSRHSSATYSNSPSSNFSNMKSSEVDPGSPPRIKSRSYSLSRSSSMKLFHTLDRRRENRM O74338 BLT1_SCHPO MOD_RES 636; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1A4.05; CHAIN 1..700; /note="Mitosis inducer protein blt1"; /id="PRO_0000116767" MSKSAFTSKSQLKGIDGSFNDPFRQPSMNLPTPPHDDGLPSIPRSTALPNLSNRLSPYSHRNYLPIPEADSRNLEVLNSISLTTGSVVNQINKLYQRSCDNANYLQDLRSLILQTPTAEANATQVTESLNQIQKILQEASSKDREQIVQVIKELNKGNSLEVRRELGNCLAHLKKGTLNIDNALQASLQKYWKELQYFNVSKDKLLSLEESIKLLSARLEETDTPSSTHWIEINAGFKEVGDELSENFQRKQEILSGLQNNVILRTNNRKPVGSDGSNSNFNGGEEQMDSKDQEEIQDYLNSLLSVHEKDGVLLQKFHNSYVQYQKLAVALSKYENFDADKLFQQMNLAKQSNETLLQTLTEQTDQLLSFKETMDSFKFILGPSMENQALQQGILAEQQDLVAQLRDIVLRSETLAENPSNMPGSCLPGASSNTADEFTEQLNLLKNEVARLSAICPSPNSGINASVLTNADNLEKENLLLVNNNAFKVDDRSVSSVALDDHNRQLQMNVEELEGKKADLTSKINRLDKDFVKLNTTYSLLTDQVKTKQLALQEIESRVIRLEERLNMLQKLSMQPAISSSSEFVPIESHPSSSAVVPIEEPKNSIIEKKRVPHNAARNSVNLEVTLPNSKKRFSSFSGSSSKLPVRPSTALTDKRKPSWSRRLAAAIGFSSGSPEKKHVITSSDAGHQRSKSRSFSSKM O74339 TAM41_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230; Evidence={ECO:0000250|UniProtKB:P53230}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P53230}; SPBC1A4.06c; STRAND 73..79; /evidence="ECO:0007829|PDB:6IG4"; STRAND 96..103; /evidence="ECO:0007829|PDB:6IG4"; STRAND 139..141; /evidence="ECO:0007829|PDB:6IG4"; STRAND 143..150; /evidence="ECO:0007829|PDB:6IG4"; STRAND 153..161; /evidence="ECO:0007829|PDB:6IG4"; STRAND 186..190; /evidence="ECO:0007829|PDB:6IG4"; STRAND 215..218; /evidence="ECO:0007829|PDB:6IG4"; STRAND 272..274; /evidence="ECO:0007829|PDB:6IG4"; STRAND 294..297; /evidence="ECO:0007829|PDB:6IG4" HELIX 35..39; /evidence="ECO:0007829|PDB:6IG4"; HELIX 43..45; /evidence="ECO:0007829|PDB:6IG4"; HELIX 47..49; /evidence="ECO:0007829|PDB:6IG4"; HELIX 55..67; /evidence="ECO:0007829|PDB:6IG4"; HELIX 105..115; /evidence="ECO:0007829|PDB:6IG4"; HELIX 117..119; /evidence="ECO:0007829|PDB:6IG4"; HELIX 134..138; /evidence="ECO:0007829|PDB:6IG4"; HELIX 162..171; /evidence="ECO:0007829|PDB:6IG4"; HELIX 176..180; /evidence="ECO:0007829|PDB:6IG4"; HELIX 191..212; /evidence="ECO:0007829|PDB:6IG4"; HELIX 219..236; /evidence="ECO:0007829|PDB:6IG4"; HELIX 247..253; /evidence="ECO:0007829|PDB:6IG4"; HELIX 255..268; /evidence="ECO:0007829|PDB:6IG4"; HELIX 278..282; /evidence="ECO:0007829|PDB:6IG4"; HELIX 301..309; /evidence="ECO:0007829|PDB:6IG4"; HELIX 312..314; /evidence="ECO:0007829|PDB:6IG4" TURN 80..82; /evidence="ECO:0007829|PDB:6IG4" CHAIN 1..393; /note="Phosphatidate cytidylyltransferase, mitochondrial"; /id="PRO_0000248361" MIFGKTHFLSYNILRYSTKRWMNRHSYSHHAKCTVAQLLKQNLLTFENQRIQPEEELKENLTKVVNYFQAPIDVAVGYGSGVFRQAGYSQKENPMIDFIFQVEDPVKWHKINLQQNPSHYSFVKNFGPGFVSTLQESFGTGVYYNTHVEVEGNIIKYGVTSKKDVYEDLKNWNTMYLAGRFQKPVVILKGEDEFYKENSYNLSSALHVGLLMLADRFTEFDLYKTIVSLSYLGDIRMSFFAENPRKVENIVSKQIAFFRKLYLPLLYAEPGVHFIESSEVLKSMDPSDNSRYLSFHQNITKDSISRLLNGLPLNLVKILGLKPDTSSFEKCAELMLTNQISTRSLLISKSIKKLTSFSILTQSIKGIFTAGVIRSFVYVYAKLKKGLLSKWGR O74343 PUS7_SCHPO ACT_SITE 277; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q57261" CATALYTIC ACTIVITY: Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA; Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q08647}; CATALYTIC ACTIVITY: Reaction=uridine in snRNA = pseudouridine in snRNA; Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q08647}; CATALYTIC ACTIVITY: Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA; Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.27; Evidence={ECO:0000250|UniProtKB:Q08647}; CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q08647}; SPBC1A4.09; CHAIN 1..680; /note="Multisubstrate pseudouridine synthase 7"; /id="PRO_0000152560" MSQENHVDVPRKRIRIDQSESSRNLERNGLEDEANAPSDLSGQKFYMTESDVGIDAFLNPNLPSIDGIIKARFTDFAVFEVDTDGNIVHLTDMEAHDPILSKATGDKETEDAKDSSNQDISNDQKAPSFKEQEPATLPILPNDLQSIIPKGIGNEFIQSLHKLSVGEITDPISLILPENTPPMDKGQRTILHQFIRNNFSGLESSTKGNGTFTVSKTTRKNQPRSRRDPRLSWKALGGEYCHFHLYKENRDSMDCLGKIARLLKVPTRTLSIAGTKDRRGVTCQRVAIHHVRASRLAQLNSGSLKNSTYGFLLGNYSYKNSNLRLGDLKGNEFHIVVRNVITPKEKVVEALNSLKEHGFINYFGLQRFGTSSVGTHTIGVRLLQSDWKGAVDLILSPRPEHTGSVKEAIDLWHSTHDAEASLRILPRRMIAESSILETWSRSGNQTDYLGAFQRIPRHLRSIYPHAYQSYVWNRVASWRIKNLGDRPVVGDLVYSTESNGLSQKSPIVDPEAPDLLEDLPVSSKLSARPIEEDEVNNFSIYDIVLPLPGRNVIYPKNETFDIYKSVMNEASLDPLNMSRKDRELSLPGDYRKLLVRPENMEFNFIKYDNMEQQLILTDKDRLENRSISVSSEVGKHTAVTLKFVLPSSAYATMALREALRTATASGDQRMLMPAVLKDSI O74349 LTN1_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q04781}; SPBC21D10.09c; CHAIN 1..1610; /note="E3 ubiquitin-protein ligase listerin"; /id="PRO_0000310490" MKKKSTDLYGRKNPGMQSMSGSFSSLQIALDESSSNFSTIYEPPDLSGLDAEMIVIVKNLQKRDIVTKCRALQDLIQWNDPSQFDNEQFLNALAVLFPRLSIEVERHVRLKIFVFMSVLSSALQKKLAPWLKFYITPWVMGFFDSDRAVSVSAKDSFKNLLSEEKWPHVWLKFGSTIAPIVTDVFLHEDKESLTDLRFFSNEEAESKVTRVKSSCLLTLSFLFKQTADLENLETDKKIDKQTFKSSLYENLSTLFKSDEFWSLVSSPQDGVTVSLSDLLLIILKYDKPFVTQYKEKYFKRVSRMISRLTSLTCVPMLRLLSNMISNFPNEVHQFANDSKRPLSKLFSNLITKRISLPNSGFYTSLLNLFKSIGAMQLVPSIESVDELCDAFLETANQEQRFLSTEVYDCLLNFLSFVYTDSSDPQIKDHVRDRLRTIFTRYFKGEFVLRCSTSDFDHCLQSVFDKNSDFASLWNEVLFGFFNDESMDIETIPFDSLSRNLSLTVQTVLYLKNRNFQTGNEVMSILGPCLSFLMKLSTHKNERIACLSASQLITVCHIFSDTTLIKPVKELFQKYLVNDLPSSILKLGPQSPAFTLLRDILLLLKDYADLSEPWENVANQFTVSFDELENIRVLNSLPSLFADGKLRGKISLVKTLVEYYDTAVFAIMQNPGNDWDMIRACIGSKEILVPEETIKNILFTTLEYFLTNDWVDNHLIILCASLHSLKAHLPTIFDENKSLYSLLPVILFSKPEDDGHVAAHFESIFSLLKEKALEDSGFSLKLCSEVQEWSLNKVLNGSINEKLAADKCVLVFNSFGKLPSNFFTFPASFWDAKISSCIPFFSNKLFIDQDFILGFLDLVASEPINVDMTDVGTQFVHIFHASLYTLYYVETTGCDGDALFNLTFAYLLIRIYLQNGIQSIIDVPIRDAGIFVESFECYFKGEVVKFMRDKDALTVLNELLIDDIDGKMPVLFKRFKNLSSAENTTSFSIFAAQGLTDFLIVVSNLLEMDEKHVDVVLGKLGLSSSKSPIFVSSILEGLKPLEVDSEIIQRIRFKAVNDLTGKLHSANEVSKSLLILNAATTQQITEKPLLPITRCRLFLENITNWCSESGIKSLELLPVCCFLRFMYYFLPTVFSLSGSYWNSIFDYIKYAMKMSVVDAPIVKSFELFALRLYNALSKNYEMNSDIKDCIVESNESMNYLLLKRFLFTHESTLRNSVTARMCNQYLVKLLENCPGKVVRSFQYQEFFPSLCNSNDLQMESVCMKFLREKLSHELKELTVYYMVESDYEPDVSLCPELLSLAIDFPGDPFVMVSKMEKYEHALRVYLLVWDLIFYHFEETTYNIKLSIINQLHAMDLLRPLLNTLVEILNLSYDRPINVDKYPKIDYNLMDYSSATDRIRCLAIHIYYQCLRHLSSSVRSYWSEVKNRAFTSTVESFTGYNVSPLLISASLDDVERSIESEDFQSVGDVNVKVNRNTREISFIYNVDEHKLEMAIKIPSVYPLQNVQVEGIERVGVNERQWRSWILASQSILSSQNGSITDALLVLKKNISMHFEGVEECAICYSVLSVERTLPNKRCGTCRHKFHASCLYKWFKSSNSSRCPLCRSSFTFV O74351 NFS1_SCHPO ACT_SITE 425; /note="Cysteine persulfide intermediate"; /evidence="ECO:0000250|UniProtKB:P0A6B7" BINDING 172..173; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P0A6B9"; BINDING 252; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:O29689"; BINDING 280; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P0A6B9"; BINDING 300..302; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P0A6B9"; BINDING 340; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P0A6B9"; BINDING 425; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /note="via persulfide group"; /evidence="ECO:0000250|UniProtKB:O29689" CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000250|UniProtKB:P25374}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P0A6B9}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 303; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P0A6B9" SPBC21D10.11c; CHAIN ?..501; /note="Probable cysteine desulfurase, mitochondrial"; /id="PRO_0000001303" MSKMGSLMLSRARCLLELRSALFFVKRESQDINNVRQSLGVYGRSFMTSSRMDKPSMSNKPREQMYGLGNMTAVQEPIPENSLKTVTLDQAQTAASTVTGLHPIYMDFQATSPLDYRVLDSMLPFFTGIYGNPHSRTHAYGWEAEKAVENARQEIASVINADPREIIFTSGATESNNAILKGVARFYKSRKKHLVSVQTEHKCVLDSLRALQEEGFEVTFLPVQTNGLINLDELRDAIRPDTVCVSVMAVNNEIGVCQPLEEIGKICRQKKVFFHSDAAQGYGKIDIDVNRMNIDLMSISAHKIYGPKGIGAAYVRRRPRVRLEPLISGGGQERGLRSGTLAPSQVVGFGTAARICKEEMKYDYAHISKLSQRLIDGLLAIPYTSLNGDPKSRYPGCVNISFNYVEGESLLMGLKNIALSSGSACTSASLEPSYVLRAIGQSDENAHSSIRFGIGRFTTEAEIDYAIENVSRQVSFLRNMSPLWDLVQEGVDLSTIEWSQH O74368 MMM1_SCHPO SPBC27B12.01c; CHAIN 1..313; /note="Maintenance of mitochondrial morphology protein 1"; /id="PRO_0000372306" MIHLPQGSFTQGLIVGQLLTLAIIYVFLRFFLFCSPIPKSVANSPKQTGNETPDETPSTPLSNNKKRYKKPLTILEPHILNLLYDVNEHEPESLDWFNVLIAQALIQFRYDACSNDVALRKLETVLNKGAQDKSMVDHIYVRDLSLGDGFPVFSHCRVLPHQHNSSQLRAEMLVSLTDNINCTVDTKLLLNFPKPAFATLPLSITVRICKFVGKIMIYFSPSNGAGQPAYMNLSFDPNFVISLQVSSLVGARSKLQDIPKITQLIESRIRQWFTNRCVSPQFQQIAIPNLWPTSAKEGHARSHAPQEESSNED O74370 ISY1_SCHPO SPBC32F12.05c; CHAIN 1..217; /note="Pre-mRNA-splicing factor cwf12"; /id="PRO_0000192973" MSSAKYVVGSKPTEKRPKDIKSIKSVPICEKHRASVVKDISRKISRIQSATLPEYQIRDLNDAINRLMREKHEWEVQIRDLGGINYLYNKAKLFEDEGEQISDIDDYRYYGRARELPGVKELFEADMSFIPERQRKQEMQKRRLDAWYFGYIPPAQESLLEDFEAKIEEQQHKHLENLGDEVEQDWKPLVIEQIPTRDDVEAILLERRKNALLSRIS O74374 PGM_SCHPO ACT_SITE 113; /note="Phosphoserine intermediate"; /evidence="ECO:0000250|UniProtKB:P00949" BINDING 21; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 113; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 113; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /note="via phosphate group"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 278; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 280; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 282; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 282; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 283; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 346; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 365; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 367; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 378; /ligand="alpha-D-glucose 1,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58392"; /evidence="ECO:0000250|UniProtKB:P00949" CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:P37012}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]; Xref=Rhea:RHEA:68748, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58392, ChEBI:CHEBI:58601, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P37012}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = alpha-D-glucose 6-phosphate + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:68752, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58225, ChEBI:CHEBI:58392, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P37012}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00949}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949}; MOD_RES 111; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 113; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC32F12.10; CHAIN 1..554; /note="Phosphoglucomutase"; /id="PRO_0000147795" MIETIPTKPYEGQRPGTSGLRKKVTVFEQPNYVENFVQATMDVVEPSAKGAHLVVGGDGRYFNFHAIQVIAAIAAGNGVEKIIVGTNGYLSTPAASHIIRKYKLTGGIILTASHNAGGPKNDFGIKYNLGNGGPAPESVTEKIYSITKTISEYKMVKIPPLDLTTTGVRRYGPLTVEVIDPVKDYVQLMKEIFDFDLIRSFLSKNPDFTFVFDALHGITGPYGEALFCKELGMPSSVCQNCKPLPDFGGGHPDPNLTYAKSLVARVDRDNIVMGAASDGDGDRNMIYGANAFVTPSDSVAIIAHHAELIPYFRDGGVHGFARSMPTSGAIDRVGKYKGKNVYEVPTGWKFFCNLFDAKRLSICGEESFGTGSDHIREKDGVWGILCWLNILAGLNAQNPKIKTLIDVKKDFYNIYGRTFYSRYDYEELENEAAGKVMDRMRAIADDKSKVGEAVLPGFVVSEAGDFEYHDPIDGSESKHQGLYIKFENGSRIVTRLSGTGSSGATLRLYMEKHESDSSKFDLDAQVALKPVVHAALEILALEELTGRKEPTVIT O74386 TR141_SCHPO BINDING 23; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 27; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 63; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 86; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 112; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 133; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7" CATALYTIC ACTIVITY: Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:27354703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50957; Evidence={ECO:0000269|PubMed:27354703}; SPBC3H7.11; CHAIN 1..248; /note="tRNA N(3)-methylcytidine methyltransferase trm141"; /id="PRO_0000339157" MSGISKLSDFWVEKYKKESKKSWDKFYKRNETRFFKDRHWLDREFDCYFGLPDKLPLTILEVGCGVGNLVYPLLEVQPNLKIYCCDFSPRAIDFVKKHSCYNENRVFPFVNDITEDSLLEVLGSACIDTLTAIFVLSAIPREKQLRSIKNLASVIKPGGHLVFRDYCDGDFAQEKFMTSGDPSMIDEQTFVRQDGTLSLFFREEDIAEWMKSAGFGLVTLDRVNRTVDNRKRNLNMKRTFLQGVWKKL O74387 RAV2_SCHPO SPBC3H7.12; CHAIN 1..287; /note="Regulator of V-ATPase in vacuolar membrane protein 2"; /id="PRO_0000116863" MQTEIDASVIVKEKEWLETNVLPEFWESMSEGLKEALNLISSDDPTVLVFTSPKTDAVKGIVSRSSSNVVRVNVTAKVGRTTHVLKLKDSAIIHLDQILNLSNYMHYALYCLPRLRHNTERAIKELQEILHAIVCLLHSIMQEESEKEEIPSNASSISLKSQNSIVSRTSNPFSCLNHSPRQIHKTVRNHLFSPPLPSNLALSFSISNASVCLHLFRLSGPNEVLESFAKNSVDIEMLKPFVSQRIDAFSQDPILLAVTAKLSALQKKVNDVSYRFKTISSSLYGAK O74388 YNVD_SCHPO MOD_RES 204; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 231; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3H7.13; CHAIN 1..301; /note="Uncharacterized protein C3H7.13"; /id="PRO_0000116864" MSAVITLTPLNESFQTKKLVISPSTIYKIGRHTNKSTSPSPSNLFFNSKVLSRQHAELWLDKDTLSVYIRDVKSSNGTFVNETRLSPENKPSAPCKLNSGDIVDFGVDIYNEDEIVHQKVSAQVRIVVRGATFATTPARSLDSEVMLDSIMRQMVFQYQRCVELNENLESLENGVEEVSKSLSWLETGKTRDNRNNHHYSRKSSPHISSLAVPSTKHLDGERDRNLKRSTSPLSSSPFVTEAALNEAELAKTNLEAWKARAFTAEARLSSKNKSWQEKKYLVLSPFFIAVAGIIVYMGYWR O74393 MAK5_SCHPO BINDING 166..173; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 566; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 567; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4F6.07c; CHAIN 1..648; /note="ATP-dependent RNA helicase mak5"; /id="PRO_0000232239" MPKKAALDELKWKEVKLPDHLDDFDGFMGLEEIEGVDIKYQPKGAMKEVIYELPEVHEKKDKKPEKRKKDQKEASEKKKKGKRTSPTIEMTSLGSKVTSKNYNEFSTLEEEDEHNSHGVDVSAWAHFSLSPEMLGSLSKAGFSKPMPIQSLVIPEASIGFDIIGKADTGSGKTLAFGIPILEHCLRNVDAKYVQALVVAPTRELAHQICQHFELIKPSPNIRVMSITGGLAVQKQQRLLNKHPHVVVATPGRLWSVINENNLTGNFKKIKCLVLDEADRLLQKSHFEELSKLLEILGNPMHTQRQTFIFSATFDEGLQQRLKKNMKGNITEKYNSPMENMLKEVRFFGKPKFLDANPQSAVASRVLEGLIECAPAEKDLYLYYLIMRYPGKTMVFANGIEDIKRITPFLNELKVPSYPLHAQLDQKKRLQSLEKFKNNPKGVLVCTDVAARGIDIPSVTHVIHYHVPHTADMYVHRSGRTARANEDGVSILMCGPKELSQLKRLCYRLKKKIETFINFPVDMSILDILKTRVVLAHKIVNLTRKDGRVGREEAWLKSMAQELGVESSDDEDPDLPKKSESSKNKKQIAHLRSELAPLLHEKIRTGFSGRYLTSGLVNMAEKLANEEVHDNIIGMDSISALEVLQKRKK O74398 YOCC_SCHPO MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 96; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4F6.12; CHAIN 1..438; /note="LIM domain-containing protein C4F6.12"; /id="PRO_0000315960" MHSPIPELPRFERRLTGPRAAPSSPVSTNGSPLNNLVRSRLSDGALNFTGGRIATPLPQPSLKTPESPLSKRNPTIKQNRVRFDLPDDELSRSNVSSPEKTLLTSASTSTFDSLKKELLPELPSLAYSDDDEFPSSPEELNSHVNYPDVRNVYDCHTGLQPLVDHDCIEDRQKTFASKQLPTLPLQKSSKLSNRRPALHSFHSAPANSLYPLPTPTSQLPSNLSSNNLFQSDSLKPSMVSSHTSTKPVLYRGNSEKSCHSCGGSLRAGRIISASGKKLHPQCFKCDTCSQNLEHVGFYYREGKFYCHLDYHEQFSPRCKHCKTPIEDQAVHINNDWFHENHHFCAGCSEVFNVNIPCIYRDDLYWCQTCYDNKYAVKCKKCRKPILGISVKGSDGEYHSQCWTCGACNALLGDEGYFMIENTPICRPCKAISVKFNLD O74399 ERB1_SCHPO MOD_RES 434; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4F6.13c; STRAND 205..209; /evidence="ECO:0007829|PDB:8EUY"; STRAND 299..301; /evidence="ECO:0007829|PDB:8ETG"; STRAND 345..348; /evidence="ECO:0007829|PDB:8ETG"; STRAND 386..391; /evidence="ECO:0007829|PDB:8ETG"; STRAND 393..402; /evidence="ECO:0007829|PDB:8ETG"; STRAND 408..411; /evidence="ECO:0007829|PDB:8ETG"; STRAND 452..457; /evidence="ECO:0007829|PDB:8ETG"; STRAND 466..470; /evidence="ECO:0007829|PDB:8ETG"; STRAND 473..477; /evidence="ECO:0007829|PDB:8ETG"; STRAND 505..507; /evidence="ECO:0007829|PDB:8ETG"; STRAND 521..526; /evidence="ECO:0007829|PDB:8ETG"; STRAND 533..536; /evidence="ECO:0007829|PDB:8ETG"; STRAND 538..546; /evidence="ECO:0007829|PDB:8ETG"; STRAND 551..559; /evidence="ECO:0007829|PDB:8ETG"; STRAND 564..566; /evidence="ECO:0007829|PDB:8ETG"; STRAND 576..581; /evidence="ECO:0007829|PDB:8ETG"; STRAND 583..600; /evidence="ECO:0007829|PDB:8ETG"; STRAND 605..611; /evidence="ECO:0007829|PDB:8ETG"; STRAND 614..622; /evidence="ECO:0007829|PDB:8ETG"; STRAND 626..633; /evidence="ECO:0007829|PDB:8ETG"; STRAND 638..642; /evidence="ECO:0007829|PDB:8ETG"; STRAND 650..653; /evidence="ECO:0007829|PDB:8ETG"; STRAND 662..665; /evidence="ECO:0007829|PDB:8ETG"; STRAND 667..675; /evidence="ECO:0007829|PDB:8ETG"; STRAND 681..687; /evidence="ECO:0007829|PDB:8ETG"; STRAND 690..693; /evidence="ECO:0007829|PDB:8ETG"; STRAND 697..704; /evidence="ECO:0007829|PDB:8ETG"; STRAND 715..720; /evidence="ECO:0007829|PDB:8ETG"; STRAND 722..725; /evidence="ECO:0007829|PDB:8ETG"; STRAND 727..731; /evidence="ECO:0007829|PDB:8ETG"; STRAND 736..739; /evidence="ECO:0007829|PDB:8ETG" HELIX 178..186; /evidence="ECO:0007829|PDB:8ETG"; HELIX 222..225; /evidence="ECO:0007829|PDB:8EUY"; HELIX 229..243; /evidence="ECO:0007829|PDB:8EUY"; HELIX 250..255; /evidence="ECO:0007829|PDB:8EUY"; HELIX 329..342; /evidence="ECO:0007829|PDB:8ETG"; HELIX 484..494; /evidence="ECO:0007829|PDB:8ETG" TURN 187..189; /evidence="ECO:0007829|PDB:8ETG"; TURN 320..322; /evidence="ECO:0007829|PDB:8ETG"; TURN 412..414; /evidence="ECO:0007829|PDB:8ETG"; TURN 560..563; /evidence="ECO:0007829|PDB:8ETG"; TURN 601..604; /evidence="ECO:0007829|PDB:8ETG"; TURN 643..645; /evidence="ECO:0007829|PDB:8ETG" CHAIN 1..740; /note="Ribosome biogenesis protein erb1"; /id="PRO_0000316569" METGMNRKRSRSKRANSNVGVEKDKEKEKSKGVSNVPNEVETESSSHEPSFKKDVDEEIPSLTAELSEEEEGEYSSESGRSTPELSPDDFEDADDEEEFEEIDAGYSSDSSTEDVAPGLYESPYDENLYINYDIDGKKITRPATPAALDSLIASIDKDKGWTGIVDPMTGKPVNLTTEELGLLKRLAQSEIPDENFDPYPDYDDFFTNTVRETPLSSAPEPKRRFAPSKHEQKRILQLAYAIRKGRILTSEQRAERERESQSNYADHDLWADDDQATVNQRKLDYAPAPKLPPPSHEESYNPPEEYLKQSSDFPKKYKSLRVVPAYSNLIKEKFERCLDLYLAPRVRRTKLNIDPESLLPKLPTPSELRPFPTRCTNVFIGHKGRVRCLSVHVSGNWLASGGDDGVLRIWEVMTGRCVWKCSLDSFGNAHNIDSDEDAVNESLSHSTKSSIIQSLAWGPLSDSPVLAVAVDETVYFITPPIFSDEQIEASKELFTSAPYQESSAIWRRGAKQSLQLHGGIVHATVSTPSSIKSLSWHRRGDYLATSSPTSSSQAVLIHQLSRGASQSPFSKSKGSVQAVTFHPTMPYLLVATQRYVRIYNLVKQELVKTLLTGVKWVSSLSVHSSGDHVIIGSYDKRLCWFDLDFSSKPYKNLRYHSRALRDVSYHPSLPLFCSGSDDGDVQVFHGRVYSDLLANPLIVPLKILRNHKVVDNVGVLSTCWHPKEAWLFSAGAGGEIRMWT O74401 ERO11_SCHPO ACT_SITE 358; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q03103"; ACT_SITE 361; /evidence="ECO:0000250|UniProtKB:Q03103" BINDING 147; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 149; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 160; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 223; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 226; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 255; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q03103}; SIGNAL 1..26; /evidence="ECO:0000255" PTM: N-glycosylated. {ECO:0000269|PubMed:15449306}. SPBC4F6.16c; CHAIN 27..467; /note="ERO1-like protein 1"; /id="PRO_0000008428" CARBOHYD 110; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 129; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 286; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 421; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 68..355; /evidence="ECO:0000250|UniProtKB:Q03103"; DISULFID 78..83; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:Q03103"; DISULFID 114..296; /evidence="ECO:0000250|UniProtKB:Q03103"; DISULFID 358..361; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:Q03103" MIGITKLISIWNAIWNFLLLPEIIISQTDTSSTGIYQMQSKVRSLVPVLTERSDYFSYYRVNLYRSSCPLWENDNAMCSNQGCAVKSLNEIEIPKVWKKLSDFEPHSKKNDTKCNWKYNPDLDYCYLDNSTSPDEYVYVSLVQNPERFTGYAGDHSAAIWRSIYEQNCFVVDDDDNPSEQPKSNALFRPNQIPLNLFTENHDDTSLSPSVACLEKRMFNRIISGFHASISTHVCQNYYDVEEQRWTQNLDWWRAKVGSFPDRIENIFFNYALLHQALVQIATQMKNITSDSSFTFCPTDKDVDWRTHTAFEQLVYHAYQDRHVINREQFFADEEAKRFKDSFRKHFRDISRIMDCVGCDKCRLWGKVQITGYGTALKLLLEPETQLSDLRPEEVVALVNTFDRISHSVEATFWFSLKAKTNDTLDAIKALIYKTYRSPSKEILAFFIDQTWYLFYALFFICNVPRVI O74405 SET11_SCHPO BINDING 223; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" SPCC1223.04c; CHAIN 1..381; /note="Ribosomal lysine N-methyltransferase set11"; /id="PRO_0000116804" MSNKQNIESEVSWVKSKGAFVHPSLEFSVIPDAGSCVLANNDINENTVLLKLPPNILINKRTCSRYSFRDKLTSFQFLSWLISEDVHSNLEISPYYTKALPQGFSFHPVTLTSDHPLWSILPDEVRNSLLERKNVMAFDYEQVKKFVSVDQPTFQWGWLCVNTRCLYYDTGSKNTEDHLTLAPIFEYFNHSPEAQTALINTRGTITIKSTRRIDKGEQIFLCYGPHGNDKLFTEYGFCLSNNPNISIQLDRFIEFDKWQQSFLQDHGYWNDYTCSLHGASFRTLVGVRTLLVSPSEKLNDASYDQTRRVLQYINGFSDGSRDRQDVEDYLKKVLQELLCEAEECKEKVKGISDGSYVFICAEQLWKDRIMCCQYLMEHSFE O74409 URIC_SCHPO ACT_SITE 14; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:D0VWQ1"; ACT_SITE 61; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:D0VWQ1"; ACT_SITE 258; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:D0VWQ1" BINDING 61; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511"; BINDING 62; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511"; BINDING 163; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511"; BINDING 180; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511"; BINDING 229; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511"; BINDING 230; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511"; BINDING 256; /ligand="urate"; /ligand_id="ChEBI:CHEBI:17775"; /evidence="ECO:0000250|UniProtKB:Q00511" CATALYTIC ACTIVITY: Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2; Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3; Evidence={ECO:0000269|PubMed:4020341}; SPCC1223.09; CHAIN 1..296; /note="Uricase"; /id="PRO_0000165998" MSETTYVKQCAYGKTLVRFMKKDICPKTKTHTVYEMDVQSLLTGELEESYTKADNSIVVPTDTQKNTIYVFAKNNDVSVPEVFAAKLAKHFVDKYKHIHGAALDITITPWTRMEVQGKPHSHSFIRNPGETRKTHVVFSEGKGFDVVSSLKDVLVLKSTGSGFTNFHKCEFTTLPEVTDRIFSTSIDCNYTFKHFDTFEELAGFDFNSIYEKVKEITLETFALDDSESVQATMYKMADTIINTYPAINEVYYALPNKHYFEINLAPFNIDNLGSNCSLYQPQAYPSGYITCTVARK O74411 MEU10_SCHPO SIGNAL 1..29; /evidence="ECO:0000255" SPCC1223.12c; PROPEP ?..416; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000021683" CHAIN 30..?; /note="Meiotic expression up-regulated protein 10"; /id="PRO_0000021682" CARBOHYD 51; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 57; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 160; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 234; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 244; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 304; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 373; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 381; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRLSSRFYLFTSFTAWSVVIAGATPAVCGAPEYIIETQNDLDVLSNCQVVNGSIIMNTSSATSLNFNRIETITGDLIIRNNNYLASVALTSISSVGGELRFEKLTRLASVYAPQLANVGQLTMRILPNLQGIRFDKGIKKAHKLTIEDTQLSTLAGISLNTTDTMVIVNNNYLREVDMPYLESVESKFYVSYNAREISVTLPRLKTVGDMTIQRVAHLQLSNLEEVKGFLGFLNSTLQDISCPNITRIGQSLFFIGNQELTSLNFKQLESIGGTFMIANSAALAQIKGYDKLKTVAGSIDFTGNFSSVELPKLRDVKGGLNIQTTSSDFTCPFRQSDGIIKGKSFVCRGSVDNPRQSKESSFDDDDFDELLGNGTIKGSKNSTSPVKQSGAAKVDSRPFRLVTFFLVLVSGFAHLL O74412 CBF12_SCHPO SPCC1223.13; CHAIN 1..963; /note="Transcription factor cbf12"; /id="PRO_0000363404" MSPNVQKRPSSEDIKTQEFYDSTRNIRRVATAIGSINANLESPQLYSLAKSTSLQEPVRIYGDSVSPAISSSKAHSTSSVSPYYSEKNESQALNADGTAFANPSFHSFGLPQEDSQDNTQTYSTPYTTMNPSNEMHPYPPATFENNYSVLPDHSSQPNAYSFTGSNILPTQSPSLNQMQDYQNLQQNGSSNTTIPSFSSQHDLSQGLTHQPVPNHDEYAFSYPYELQRKPLIPAHPVPSFRPTSALKVNMNSNVPSSDSVRNSSPNQYYASTSKQSIPSQSQNLQPPQKASVLGTVNNYRQYQNSFISLNDYQAAQSNISSPSSRFPTPYSPSVPFGTYQEKEKSYSQDHAELSYYQQSPSMMPPYDRSSVYFQQPLSRTDVPNQSFQQYPTTVDGGSMIPNLYPTSAEQMGLYPQDSQNKDTYPKSLVNRPSSAVCEPARNDSIPMMVYSQPVTIEQRIQYVLSNCHCLSAFYLCMPSLCQKSYGTERRYLCPPIVLYLLGTTWLNNVTDNLKISAQTLEDKDNPKFAKNIFYYNADGALISPETDIAKSTYQLTNYNENTNFDSFPVWGNALLKTIYYTGQGKNDGFGRSTFLQLSVQSKTKYFKLENLRLGVISKPSQKRALMKVSDMSIRHGDCVCLFNRYRAQHNNALFLGTSNVQRAISKVSLNMKYNSNYFPTTDAPNDAENEGAGLAMANNLWEPFYIFSVDELNKGNNSNPSDSRSKVLCSNMVIILVSKITGVQSPPLILKKHDNWKVSLSSRAPSEAINCLSKLAFQCHETKRFLYIDEKQSSEISFTSGELEYSDPNDPTKATHSVLPWSAMWSIISTQSVRTMFYNEPIHQNAFHVVPSMPFVKFIRLDENSMFHIYGTGFANDVQIWMAYTRCEVKSINAFKPDTTLPPDIISDSRFSSRVYACTANLIELICEIPVCMFEPTVELSPILLFQYETLFHSGYKWPLESH O74421 COQ3_SCHPO BINDING 65; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03190"; BINDING 88; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03190"; BINDING 109; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03190"; BINDING 154; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03190" CATALYTIC ACTIVITY: Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694, ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000255|HAMAP-Rule:MF_03190}; CATALYTIC ACTIVITY: Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378, ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000255|HAMAP-Rule:MF_03190}; TRANSIT 1..30; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03190" SPCC162.05; CHAIN 31..274; /note="Ubiquinone biosynthesis O-methyltransferase, mitochondrial"; /id="PRO_0000035931" MNSMNILNKVKNVKSYTRLVRQGFLSQQRNHSVSVNEVDHFNELAKTWWDWDGGSRLLHLMNSTRLDFMTEVFRERNCFSGKKILDIGCGGGILSESMARLGASVTAVDASPMAIEVAKKHASLDPVLNGRLEYIHGSVEGSQLPTTFDVVTCMEVLEHVEQPRDFLFSLMEKVKPNGRLVLSTISRTLLARLLTITLAEHVLRIVPVGTHTFEKFIRADELSNFLKEQNWIINDIRGVCYNPLKQQWTLDKPGSSGLGLSCNYFLSAQKPMSA O74424 NU211_SCHPO MOD_RES 650; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1558; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1560; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1563; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC162.08c; CHAIN 1..1837; /note="Nucleoporin nup211"; /id="PRO_0000290673" MHDSSWTEADILGVCSFLDIPKTKIDPLLQVDAFTSILIPLISKSKDYESIKNDRIVTEVNYEQQLRNSEKKLLQSNERYDLLEDERKLLENELSQIKEYLREKSSSYDTVLHDCSSLKSVNEALKQAQDQNLKQTAQLQNLLSDKEKEVEKKITIIKDLKDALASSTHQVLELQHTQQEKASLQTNYEFELQKLTQKNSILENNNTWLSRELQGVNDKLLSLHQEASLEKSQLSSQLSDAVLEKDALQRKVSSLSQQFTESNLRYQNIVAELSEMRKQYEFSQVSFEKEISSQKQISELWMEKCEDCSLRLKELQNSNGELEKLLEAAQSSFEEQLESHKEAEASLKSQINFLEKEVSSLESQLKLANERLRHYDEIEISDMSELKYSNLLNNSMKGFKGQSSVSDLYSERLYYKQKYEQTCQEVERLQRSYNHVMEEANLQHPLVKEQFKRFAHMQREIVAMSEQYQKSLEDCQKAKSRYEQLETLFKDKCTENKHYEQETKDLARQVQVLLHELDLCENGIVLGVDSRKKINSYVEKSLTEDETDTDQIISSRLVVFRNIRELQQQNQNLLSAVHELADRMEKDEKPDLDGAEIQEETLIKANETIDQLTKMLEEVSDQLRYSLKERDFFRSLVQENEKLLDMAPATPNSKLNTNLIEQTSYQRSLIRLEQLTNELESLKSISRNKEKKFEEAISSLQLEKSNIQLQLTSLTSERSLALEKLNDLEKSLVLSERSKDELDESYKSLQEQLASKKIEVQNVSSQLSICNSQLEQSNHIVDNLKSENLLLTSVKDKLKADLSNLESKLSSLQQDNFHMKAQIESSNQEYTATVDSMNSRILELSNDLRVANSKLSECSDDVRRLTLQNSFDLREHQTLVLQLQSNITELKQDITLQRTVRNQLEIQTTELKERLKFMEERQENLQSKLIAANKDTTQNPDNVEVEAISIELERTKEKLRMAELEKSNIQQKYLASEKTLEMMNETHEQFKHLVESEISTREEKITSLRSELLDLNKRVEVLKEEKESSSKELAKQLEDAVREKDSALSFKKDYEKIRSDADRVITSLKEDIEKERSLMKECHSNYESEIVSHGRTTQKLRDLRTEFDEVNTKYLKLKANFEQQHSGLSGAEKDWNIQRKAMEDEISSLKDYILGLENQNKLLHSQFDSLSQQITVLQQNSSENLNISANLEAVQDNDLRELVSYLRHEKEIMDNKYELTILDNRGLNQQVKSLQSTVDSLQLELNRLQSLPVSNDQTDTPIISGSQEVQLLYESNSVLRKDNDAKLGKIQELEKEVEKLNASLNPLQTEINELKAEIGAKTASLNLMKEYNSRWKLRFQSVLNKYERVDPTQLEELKKNCEALEKEKQELETKLQETAKETDTFKQQVNSLNEEVENLKKEVEQANTKNTRLAAAWNEKCENLKKSSLTRFAHLKQELTNKNKELTSKNAENEAMQKEIESLKDSNHQLQESASSDAEQITKEQFEQLKSEKERTEKELADSKNELEHLQSEAVDADGKTEISNLEKEIHELRSDKEGLVQQVQNLSAELAALREHSPTQGSLENADEIARLRSQLESTKQYYEKEKETEILAARSELVAEKEKTKEELENQLNEKSQRIKELEEQAQKNSSENTHDNIDDMIKQQVEEKLKENSANFDVKLKKVVAETEFRSKAKISVYEKKTRDLQNKITQLEETIENLNKQLSNPEKTDESTSSVTETKPVTSKPTASKADVGQNATEASSAKREPSGKSLSARLQGTGKQKGVQRPAVSRPVPMKPDSGKLSITGASKRIATSKNAAQNAKELSSTAKSGSLKRQRDDANKGGSSSNQKKAK O74427 URK1_SCHPO BINDING 28..35; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48; CATALYTIC ACTIVITY: Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674, ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48; SPCC162.11c; CHAIN 1..454; /note="Uridine kinase"; /id="PRO_0000311758" MPEAFERYSSNPTYEPPWRKVRFIGIAGPSGSGKTSVAQLIVKALNLPHVVILSLDSFYKSLNAEQKKRAFNNDYDFDSPEAIDWDLLFVKLLELKQGRKVDIPIYSFNEHNRLPETNTLFGASIIILEGIFALYDEKIRSLLDVSVFLDTDSDVCLSRRLNRDINYRGRDIVGVLEQYNKFVKPSYENFVRRQLSYTDLIVPRGRDNKLAIDMVINFIRRTLSIQSETHVKNIDSLQQIVPTIPHLPLNLVQLKITPEISAIRTILINKNTHPDDLQFFLSRIGTMLMNLAGDSLAYEKKTITLHNGNQWEGLQMAKELCGVSVLRSGGTLETALCRQFPTVCLGKILVQINKVTQEPTLHYHKLPRGIATMNVVLMASHLTTHADVLMATQILVDFGVPEENIIIVVYVCYSESIKALAYIFPKVTIVTAFLESVAEPVVGRLDIEKVYYGC O74428 TCO89_SCHPO PTM: Either Thr-10, Ser-11, Ser-12, Ser-13 or Thr-14 and Ser-214 or Ser-215 and Ser-247 or Ser-249 are phosphorylated as well. {ECO:0000269|PubMed:18076573}. MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573" SPCC162.12; CHAIN 1..451; /note="Target of rapamycin complex 1 subunit tco89"; /id="PRO_0000304086" MERPSLSRRTSSSTVSTDGEGVYSRSTKERKRNFIVNSRLKRGGGHVRVNRSGRLGSVTMRPSALTRAHSQNPNSSLVNNSSAVSHLTKQRSLNDLHELNGPKHVAKNGLIPLTQRKPNCVWDDAPVDNDSTAGNLDSDSALPTPSVTTNEAADSSRASSPVTRVVAVHDNKKKIINSNISNAPPFNNTDVQASARPPAAGQDDSAADASTTKSSPVHNEVMAEPLPHSNNREVTQATNQPKWQIHSGSDIASEPPTLSRGNSLSLLANRKVPSTNVKKSQAELYDLGSSTSRTQQKLLIQRASSKFDIVEDDMDTNPSKRFSNPHTKHIMDLVRTQYRNVLRTRELIPEFLEKIRSSYSNNQNFDSQNAFNTSAAGTAGTREETISNGQNGIVASAETSKKDDGVQSASLNASMSARSHARQRSIHVPKTRKDTDYESIHQKLLQLWSQG O74430 TGCE1_SCHPO ACT_SITE 222; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 389; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P80035"; ACT_SITE 415; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P80035" MOD_RES 66; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1672.09; CHAIN 1..467; /note="Probable lipase C1672.09"; /id="PRO_0000312659" CARBOHYD 311; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 316; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIQLPFIQRLKWEEYMALFLGFFFVIFEKLLSCLAFMIHNTLGLFYRSVVRNEIKKRSKKRSRSRSVSLQRAKAIHDAADIREMCKISGYYVEDHLVRTEDDYILCIHRISKDSPGRIGSPHPKKLPVVYCHHGLLMNSEVWVCNVDPRNCLVFDLVNKGYDVWLGNNRGNKYSRQHLRFDSTDKEFWDFSIDDFAQYDIPDTIDYILKTSGQTKLTYIGFSQGTAQAFASLSIHPLLNDKINSLIALAPAISPKGLHNRVVDAFVKARPSILFFLFGRKSILPSAGFWQSFLAPKFFDAVLAYCLSQLFNWSCQNISSYQRLVSFAHLYSYTSVKCLVHWFQIMRSAEFRMYDNDQLGHDYFLKYYKAAKFPTNNIRTPIYLIWGGSDSLVDIQAMLNALPAEVEHVKVDSYEHLDMIWADTVKDYVIPPVLRRLRDIHHPPEHEENDKENREIQKNHIAPRNKPI O74442 UBP16_SCHPO ACT_SITE 134; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 388; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 61; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 64; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1682.12c; CHAIN 1..457; /note="Probable ubiquitin carboxyl-terminal hydrolase 16"; /id="PRO_0000248399" MSLATLQGQSLDFAVKHSLDDLLKNPVRFRPAVVSSPSVPEGTYTVLNNPKQSTVSRKSFSAPTSPTRNKRSGSSSQEYKKSSGTRGDGANDFVDEDPAFIPPARILFPEEKLSMEWDNIMPNAPGLVNLGNTCFMNSVLQLMTQTPPLVQYLLSGQHSLSCRMNACVLCRMEQHVARAYPNKGTKRASAFKPSGIQSMLKVISSHFRPYRQEDAHEFMRYLVDAWQKSCLQNHKNLDHPSRETSVVHRIFGGYLRQQILCSVCKKPSNTYQALLDLSVDAKGSSLADSLKHFVHAEKLTKQNKYRCENCKQLVDASKQMTIYRAPNILTIHFKRFTFNGFQSSKISKQISYPESFNLGPYMSDPNCSCWYELIGVLVHAGGSTRSGHYYSFCKSSNGVWLKFDDDFVSNSSIDRVLNQQAYILQYKRKSTSSSKHKLNTENTVTKTSNKKRRKISF O74443 LAF2_SCHPO MOD_RES 130; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 135; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1682.13; CHAIN 1..272; /note="SWIRM domain-containing protein laf2"; /id="PRO_0000303945" MQILKDQENLNPDGGSFVLITPPLSPPKQKSLSYTNISRRHGMRACMKGIVYEVYKNQPKLWLQQELIWLRRKRIHPIPKARRNNHVGRWANRHSNVSSSSGSRGRSSVSSRDSSPSYSGALRSAERSISSSPSTIEARRRKSARGNGLNGAIDVANLPFEELPNFCPDMSVLDNRTHPRTLKAEWKGPPLDLSDDPYRDLLHPAELHLASTLRLPCLIYLDNKKRIFAEWHHRRQQGLTFRKTDAQRASRVDVNKASRLWKAFHEVGFFDD O74448 PIN1_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPCC16C4.03; CHAIN 1..175; /note="Peptidyl-prolyl cis-trans isomerase pin1"; /id="PRO_0000193443" MSNTGLPKPWIVKISRSRNRPYFFNTETHESLWEPPAATDMAALKKFIANELQESVTPTEASNSPKIRASHLLVKHRESRRPSSWKEEHITRSKEEARKLAEHYEQLLKSGSVSMHDLAMKESDCSSARRGGELGEFGRDEMQKPFEDAAFALKPGEISGVVETSSGFHIIQRHA O74453 SKB15_SCHPO SPCC16C4.08c; CHAIN 1..341; /note="Shk1 kinase-binding protein 15"; /id="PRO_0000051217" MLRFVVGTYTHLIYGVDADIERKKCKPLWLFEAHEGALTALAVDGIYLASTSSDETIKIFDHTRNVQIADVSVPTDIANACIRDMCFTKNHLLACHDNGQISMWSKGSWLLVHTLKSSSHKGITGIAVHPSEKLALTVGGDGKLRLWDLVRGKGGKVLPLSTIPESILFLNESSFVIMSRRGIDAFKLDLTSLFSFSSKSQLNALCLYQSKLIVGRDNGTVLVLDTSDGKILHEFTAHKKRVKSVYPVDDYLITASSDGSVCIWDKDWNLVIEHNIPEGNRITCMVAMLADSNSEPKNVEDEAAKRQSLDSETSETSSESESESEYYSTSKQPPVKRTKHA O74454 STS5_SCHPO MOD_RES 157; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 262; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 264; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 377; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16C4.09; CHAIN 1..1066; /note="Protein sts5"; /id="PRO_0000166422" MDEEFENDFPYKVMLNQQQDPSDAQSSPTFVPSANPSLTTPWLQTTPSANRPTWLPLQQHMHQLRHTGLLPAVESSFVHGHRRSASAGVGMGNFSNQATIPSNSPAVSNMQPPTQGGQPLYPTNFFTTSVSASSDSFPNSPTVPSKFSLNPSVATSTNISPRRHAKSHSVASVSSPNSHNAVPFTPHAFVPPVNNASPLPALNTLPQLLRPRNLDAQWRPSSLSQTNSPTHAANPSFPGTIVTHNTSNFRPEGGGHRHRRSTGSLSVGSSGSGFSSGGSGNPRKNLFSPYLPQSSIPALLAERRLVTGILIVSKKNRSDAFVSVDGLDAEVFICGSKDRNRALEGDVVAIELLDVDEVWAGKLEKEENRRRKDPISTRGSFDNLRIDAVPFEVPQRSAIKARDDEQVEGQTLFLLDQKQLGADEKPKYAGHVVAVLQRAPGQVFSGTLGILRPSSAANKERQTSSGNQGSSNNSGNDKPKIVWFKPSDKRVPLIAIPTEQAPTDFLGNDQAYAQRLFLASIKRWPVTSLHPFGMLVGELGSMDSMSAQVSALLHDTGVHSEPWEGSAATSAVTALNALSDNFLNVAGCADYRSEDVFLFVKNDVSKAAVSEVKQHESNINSSSATDFVSSAFHIRPTSTGYHVGIHVTDVSRVIEPGSPLDRELQRRSIAVNLCQKSVPLFPTTLGEALSLREDKDCYTMSLLLDVSSTGKIRGTWIGWAVIRPRKAYTMKEADELLQTDARLRLFHTVSSRLRTHHLGTDVPLSRYCRLVRRWDEESCSFDPNETNLFISSAVEVLRETLLDAANRAVASHLRQEFRENAFLRTQRLPSRENCRILQSMAIQMGCVLDLSSTKSLLRSLSLIEDDTVRNILQLYYYKVTPRAVYEMQKYKGNLASQMMSLGIEDESDDLTHFTAPLERYGDIVVHYQLQLLLRGELASEKRLRVWSQAANDASRRLVISKFAQETSIHIKIFSDWAESQVWQDGLVCFVAPSYFDVFFPSLGMEKRVHLDLLNLTHVRFEEDQGILSLYDESGAVTVVKLLTSVKVKLFVQLSTPPLINVSNVEF O74458 SFC4_SCHPO PTM: Phosphorylated. {ECO:0000250|UniProtKB:P33339}. SPCC16C4.14c; CHAIN 1..1006; /note="Transcription factor tau subunit sfc4"; /id="PRO_0000307795" MIQNGGNSYVDSNMNETQNDTTDNFDAEMQDLNGYISEIVDEARNVSEVDAKFLGDTSALQAEGLWSDEESDYEGSDDESNFSKTASRTEDDIANEEWEENLKAVAGFRKVRKGHKGRGRVSRADMLPSVEVQQMLSLANHLFAQEGNFDEAQKLAEEIVRIDNNVIAAWKMLGECHRQRGNGRVNIEKCLIAWMAAAHLKPKDHELWFTCAKLSESLEFWDQADYCYNRAVSAKPPNKSELKKYIWNRSVLNKEHGSLKKAAEGFKFLLQSSPYNASILKNLAEIYIKIHAPREILKQFEIAWKYFYQYPAPPIGNDIFDLPTLNLYAELLLLDHQWSNLIRLINRGVRWFRGRKSESFWDEFDDDREWDVDERRREFPNASEEHTNKEAYLLPHLFRTKLGIARLKTGELPEAELHFSVIKNLPPDYAWGMLYDIAKAYMDIERLDLALEYFVLICNHEPAQNIGLWYNMGVCYLELKEYEHAQQCMEAILIVDNSNTNALIKLAEINELQDNRDAALEIVTNIFEQRRNINELEREQSQNEDHEKNVGSQLFVGNQKVPQDKWEKRARISRSKEEARQFTIWKTEETQRRFHKLDILRQSLKKEENVSESLNEWLAIASELIDEFVSIKAFFPSEKKARARAGLLTRRTRYASLNDQLTSMINRLNDSLTRTKYGDLDLDTILRTGYFRNVSIDAWYQLFVEFSLRLTKVGSVQQAYDVLTTAMGAILFDQDTIKRQNLRWCMLACSMYARDPQGALTPLRWVFTTFQFRQDTYRLFSAVLSQGYECSRAFVDSANQKFLLRLIKLMDQLMSNSLVSGAATLVKNDDGLATVPTSYDPVLVLLYGHIMARNRSWIPAINYYSRAFAINPDCPITNLSLGLAYLHRAMQRLSDNRHYQILQGFTFLYRYYDLRVNEGLGEKQEALYNLGKAYHFIGLEHYAVKYYEAVLGLSPMSQGDKMTSSESTVSTTYDFGFEAAYNLRLIYICSGNIKLAFQISSKYLIF O74462 TAF6_SCHPO SPCC16C4.18c; CHAIN 1..452; /note="Transcription initiation factor TFIID subunit 6"; /id="PRO_0000361054" MSLTVWNIESIKDVAEMLGIGNLADEPAAAIAMDLEYRIHQVVQEATKFMVHSKRTVLTSADISSALRTLNVEPLYGFNNSRPLEFHEAAVGAGQNSLYYLDDEEVDFEKIINAPLPKVPRNISYSAHWLAIEGVQPAIPQNPTPSDHTVGEWASKGTSGVMPGASTAAKEARNGVTSMDNVEIKPLVRHVLSKELQLYFERITSALLDETNVELRDAALSSLRDDPGLHQLLPYFIMFLSDSVTRNLGNLVVLTTLMHMAWALLDNPNLFVEPYVQQLMPSILTCLVAKRLGSDPNNHEHYALRDLAAFLLGIVCDRFGNVYYTLKPRVTRTALKAFLDNTKPYSTHYGAIKGLKTMGKEAIRVLVVPNIKVYEVLVRKTLEKGNEEEIYEANKCMDALYDALLLLRDDQLPNQRTLPPNASGLLEKNVGSLMAEKIMKENDTSLLLGLLE O74467 SET5_SCHPO CATALYTIC ACTIVITY: Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000305|PubMed:15550243, ECO:0000305|PubMed:37731000}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10025; Evidence={ECO:0000305|PubMed:15550243}; MOD_RES 316; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 318; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1739.05; CHAIN 1..319; /note="Histone-lysine N-methyltransferase set5"; /id="PRO_0000317700" MNPYETEIYKVVPIPNKGMGMIAKVKIPVGTRIFAETPLIRTKSDAKEIEEALSTKTKEEQEAFHRLFNAHPDTMGPFLGPFYSNALTIDETKGGMFLLGSRMNHDCSPNVKHTWNPRLDQVTVHAVRDIEAGEEILTTYIDLHKSHTERQKILLEHFGFKCYCSVCSVEERKIRKISDLRRKQLAYYDRTMAKMCIVNPRGALRALRHRIHIAHEELLFGRLDIIALLDAFRLCVIHGDFERASIFAKKGTKAISLYEGTDSEKYLKISKYVENPRSHALAEGVPALPLFLEEDDELSDLEDNLWGCKLEEDVYSDTD O74472 MUG33_SCHPO SPCC1739.10; CHAIN 1..336; /note="Meiotically up-regulated gene 33 protein"; /id="PRO_0000278497" MRIRSATPSLILLVIAIVFFVLAICTPPLANNLTLGKYGDVRFGVFGYCLNSNCSKPLVGYNSDYLDEHAKDGFRTSVIVRQRASYGLVIVPVSACICLISTIMTIFAHIGAIARSPGFFNVIGTITFFNIFITAIAFVICVITFVPHIQWPSWLVLANVGIQLIVLLLLLVARRQATRLQAKHLRRATSGSLGYNPYSLQNSSNIFSTSSRKGDLPKFSDYSAEKPMYDTISEDDGLKRGGSVSKLKPTFSNDSRSLSSYAPTVREPVPVPKSNSGFRFPFMRNKPAEQAPENPFRDPENPFKDPASAPAPNPWSINDVQANNDKKPSRFSWGRS O74478 PGM3_SCHPO ACT_SITE 149; /note="Phosphoserine intermediate"; /evidence="ECO:0000250|UniProtKB:P00949" BINDING 49; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 53; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 149..150; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 149; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /note="via phosphate group"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 306; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 308; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 310..311; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 310; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 380; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 404..406; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949"; BINDING 418; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00949" CATALYTIC ACTIVITY: Reaction=alpha-D-ribose 1-phosphate = D-ribose 5-phosphate; Xref=Rhea:RHEA:18793, ChEBI:CHEBI:57720, ChEBI:CHEBI:78346; EC=5.4.2.7; Evidence={ECO:0000250|UniProtKB:Q03262}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00949}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949}; MOD_RES 149; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1840.05c; CHAIN 1..587; /note="Probable phosphoribomutase"; /id="PRO_0000315630" MDPILQELVDEWFKLDQDETTRNEVSQLIKAEDYATLKQIMHPRIGFGTSGLRAEIGAGFARMNCLTVIQASQGFAEYLLQTVPSAAKLGVVIGHDHRHKSNTFARLTAAVFLQKGFKTYFFDHLVHTPLVPFAVKTLGTAAGVMITASHNPAAYNGYKVYWGNGCAIIPPHDKGIAACIEKNLTPITWDKNLVENHKLADRDFAVGLLKNYWSQLHEFHSENNFSLEMKSLKFVYTPIHGVGLPFVTSALHLFGEQGDMISVPLQDSPNPDFPTVKFPNPEEEGALDLAYEQADANGISYVLATDPDADRFAFAEKINGAWRRFTGDEVGCILAYFIFQEYKNVGKPIDDFYVLSTTVSSAMVKSMAKVEGFHHVETLTGFKWLGNKALELEKQGKFIGLAYEEALGYMVGSIVRDKDGVNALITFLHLLKRLQLQNLSITEVFEQMSKKYGYYTTQNSYFLSRDTPKLRALVDALRHYDTKSGYPATLGSKKITNVRDLTTGYDSSSTDGKATLPVSKSSDNVTFELENGEVIMTIRTSGTEPKLKFYICARGHSLEDSIKNATEVKQAIKSEWFHPQQNGLEEP O74483 LSM8_SCHPO SPCC1840.10; STRAND 9..15; /evidence="ECO:0007829|PDB:6PPN"; STRAND 20..28; /evidence="ECO:0007829|PDB:6PPN"; STRAND 34..43; /evidence="ECO:0007829|PDB:6PPN"; STRAND 46..48; /evidence="ECO:0007829|PDB:6PPN"; STRAND 51..60; /evidence="ECO:0007829|PDB:6PPN"; STRAND 65..71; /evidence="ECO:0007829|PDB:6PPN" HELIX 2..6; /evidence="ECO:0007829|PDB:6PPN"; HELIX 62..64; /evidence="ECO:0007829|PDB:6PPN"; HELIX 73..78; /evidence="ECO:0007829|PDB:6PPN"; HELIX 81..83; /evidence="ECO:0007829|PDB:6PPN" CHAIN 1..94; /note="U6 snRNA-associated Sm-like protein LSm8"; /id="PRO_0000125584" MSLADFMEQRVQVITNDGRVVLGSLKGFDHTTNLILSDSFERIISMDQDMETIPLGVYLLRGENVAMVGLVNEELDSEIEWTKIRGEAIPDVVH O74486 WTF19_SCHPO SPCC1906.03; CHAIN 1..393; /note="Meiotic driver wtf19"; /id="PRO_0000193231" MKNKYYPLRSSMDELSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSENINLKDPKQMGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFAVWCASCLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVTSISLAKCVKLTAVFLAQCVKVTAVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILEGAGRAIRGANDNNDIPLGEMEVESEV O74500 NUP60_SCHPO MOD_RES 157; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC285.13c; CHAIN 1..736; /note="Nucleoporin nup60"; /id="PRO_0000350997" MSSGPIRTLHKGKAARNRTPYDRIAASKDGNHSNGPQTPSKSIFQRAKEWLTPSSWKKAISIFSSPVVNKHEDSFDSKTDEEYLQNVSTTTEDVSMLINTPVTEKYEQEHRDTSAQATPSIVEQSPNQMLANFFSKKGKTPLNEIEKEGIISILNKSASPSSSVISPAASLNRFQTPRAAAISKRESGVSSEPRARTSSLTPGNTPNSAKQWSAFRSTFSPLREQDQLSTISPNSLLPAQRLSYYGPTLSTPYNRRLRHKRHSTTPISLSNSIAPSLSFQPKKARYESANVSFNDTSFTNVPTSSPLHQSTTANHPEKTPSRAAASLLSILDSKEKNTPSITAKAGSPQSAPSKASYISPYARPGITTSRRRHDQIRPSSEKSEPEKKEPSAFETLEKSSNVQTYKPSLMPEFLEKASTHGSFAKQKEGEQTSLSEKTALSEPENKTPVFSFKAPSATTDKPSPPVSSIFSFNAPSAASTKPSPAVSSTFSFNAPTTTPSATSFSIINKEKPARSPNETIDVDLEEEGSGISAEVEVANEGEDLQKNATEVKASTSEKPVFRFEAVTDEKNSEVSSSNQASSSTMISQPNTGFSFGSFNKPAGQEEKPQQRSLFSASFTTQKPELPAAKIEPEVQMTNVAIDQRSFEQAEKSPISVSESTSLVEVEKPSAEGTNEHKQDATMTLEKTDKQGSLEEEPFPKFSFTVLPKENGENLSTMESTQELPKFSFSVLKEEKN O74502 MSH6_SCHPO BINDING 1024..1031; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 205; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 299; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 307; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 309; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC285.16c; CHAIN 1..1254; /note="DNA mismatch repair protein msh6"; /id="PRO_0000115212" MSVGNVGKQREKTKDSSAKTKQKTLFGFFSKIPNVKQEKSDSTLSSSSNHDSNHDTPADVDNSSNVNKNSSSPERELPTSPSHHANTEIDSSSSMLPPPSSDPFSSPLSSSLHRSSPKRPHDSLGEESPGKLLRTSVKQEPDSEEEIDSPTKKKSFKSLDTSIFQAEDQFRHPVSSKLENSELSEVDKPFIASRRSRKPVSYAESDEDEDFDDAPTKGSRHKRIVSDDESDDYVEPDHISEASSEASLPIDEVESMDEDVDGYSDHSVSVAAPIPKKESRKESSNSLYESYRLGSQIASPSPSVSGSASPTKSNKNGVLNREEKRRQRMEAFKKENNERYEWLLDVRDADQNRVGDPNYDPRTLYIPPSAWATFKPFEKQFWKIKKDLMDTVVFFQKGKFYELYENDAAIGHQVFSLKLTDRVNMKMVGIPEASFDYWASQFIAKGYRIARVDQLETALGKEIKDRQRTQKEEKVVQRGLTQVLTSGTLVDEAMLTSDLSTYCMAIKESLQSDNEEPSFGICFIDTSTGGFHMCEFTDDIHRTKLDTLLTQVRPKELILEKSKISQKSIRAIKYCVSSSSIWNFIKPYTEFWDNERVEREIIAGDYFKNGLEGAPKILKSYLSEKPLAISAFGALFWYLRQLKLDKDMCSMGNFDEYDASQQSTSLLMNGQTLKNLEIFSNSFDGGSEGTLFHLLCRCVTPFGKRLFHTWLCHPLRSGTAINARLDVVELIADNPVIRDTIWGFLHKLPDLERLISRVHAGRSKPADFVRVLEGFQRINSAFDQLREEFMEVAEGTLLGEIIQSAPNMKEELEAWTRAFNWQKASEEGVFEPEIGFEAEYDTSQKYQSELKNELYALLEQYKKQLRCSSLNFKNIGKEVYQVEVPSDVKVPVNWCKMSGTKKTNRYYNDELRKKIKKLLEAEELHLAIMSRMQEKFYIRFDSNYEQWLALIKYTASIDCFFSLSQAAAALGEPYCRPEIIEQKDGHLYFEELRHPCINASAASTFVPNDVVLGGESPNMIVLTGPNMAGKSTLLRQVCIAVIMAQLGCWVPAKRASITPMTSIYTRLGANDDIMSARSTFMVELSETKKILDECGPKSLVILDELGRGTSTYDGHAIAYAVLHHLVSNIGCLGFFSTHYQSLCVDFMHHRQVRLMQMAAAVDEKIRRVTFLYKLEDGICPKSYGMNVASMAGLPEKVIDAAEEKASELEQASASFINASDDIALMSDFLQVLRISKSIEPLTAVNIPLILDSFE O74503 UAF30_SCHPO SPCC285.17; CHAIN 1..233; /note="Upstream activation factor subunit spp27"; /id="PRO_0000290654" MEEYETDIKQILGTVDRQTVSAKQVRQLLEERRKVDLSAHKKDLNALILKCFDETAAPSEKESLEKQAPARKTKGKRATENGTEEGKKPAKRTRKRKEDGEEGGKRKRNQDPANNPLNKPMKLSPKLAEFLGLEQLSRPQTVKKLWEYIKAHDLQDPNDKRTILCDDKLKSVFEVDTLHMFTMNKYLTNLMTKIPDDQLPKPQPKNEEPAAPNDLPKQEEKELVEPPTAESTA O74508 SPP1_SCHPO SPCC594.05c; CHAIN 1..424; /note="Set1 complex component spp1"; /id="PRO_0000059337" MELTQENTEENEKTHVESIVKFEDSNRGTITDFHIETANNEEEKDANVILNKSVKMEVEEVNGHVDSSSTETDIEMQVIQQPTIPKKPPVSAHRRGPRKHRGNANSQLNLSTADHQRPLYCICQKPDDGSWMLGCDGCEDWFHGTCVNIPESYNDLTVQYFCPKCTEEGKGITTWKRKCRLRECSNPTRPNSNYCSDKHGVDFFREKVKLSTVEPSAIKNLVLFAKKREEFQNLGTVGPTLPSQVPPEVVYNFEIEEANRLNAEIVQLNKEKEVASNKKIFLQLIKDSSRRAVLAYKEREGIKKDLCGFDSRLLFNQQQMNELWEKVSNGAPLSLDMSIDPSPESTCFTEKRRCAKHTSWQVIFTEDFELQESNILQKLNMKQTAKDVMLEHQKQRCLPGIQYDGYARFCHEQLSPEKMANLLK O74509 VAM7_SCHPO SPCC594.06c; CHAIN 1..341; /note="Vacuolar morphogenesis protein 7 homolog"; /id="PRO_0000339882" MALKIKIPETSQSSDEYSRWTVYHIEVAFPNGGKHVVFRRFNEFVALDAQIRPNDYNSRLCKLPSKSWVSSTVTNEKLRESRRLALQAYVQCLSETPWIKMPVVKKFLNIKDESEDETQGQFLGPTDWIQVFQDCKRNLHMYRVDLMSGKSITIGVQTKNVYAIKSLMDNLSESLDKLELANALGPGEILRRKDMLEQLGSEFLSFKRLVKNANSPVAPPSASSQLNSSNPSSPFRPLSASTDKQSNTSLNRVLGKNRMPETQTTKKLDNVGLYNMQNQTMEDQDMQAESLLPIIQRQKELSKMINQEVVEQNSMLDELSNEAYANQKKLHRTRAGLRKLG O74515 ASF1_SCHPO SPCC663.05c; STRAND 3..13; /evidence="ECO:0007829|PDB:2CU9"; STRAND 15..17; /evidence="ECO:0007829|PDB:2CU9"; STRAND 22..30; /evidence="ECO:0007829|PDB:2CU9"; STRAND 38..47; /evidence="ECO:0007829|PDB:2CU9"; STRAND 54..62; /evidence="ECO:0007829|PDB:2CU9"; STRAND 67..76; /evidence="ECO:0007829|PDB:2CU9"; STRAND 84..86; /evidence="ECO:0007829|PDB:2Z3F"; STRAND 91..102; /evidence="ECO:0007829|PDB:2CU9"; STRAND 105..118; /evidence="ECO:0007829|PDB:2CU9"; STRAND 141..145; /evidence="ECO:0007829|PDB:2CU9"; STRAND 151..154; /evidence="ECO:0007829|PDB:2CU9" HELIX 51..53; /evidence="ECO:0007829|PDB:2Z3F"; HELIX 81..83; /evidence="ECO:0007829|PDB:2CU9"; HELIX 87..90; /evidence="ECO:0007829|PDB:2CU9"; HELIX 123..125; /evidence="ECO:0007829|PDB:2CU9"; HELIX 128..131; /evidence="ECO:0007829|PDB:2CU9"; HELIX 138..140; /evidence="ECO:0007829|PDB:2CU9" CHAIN 1..262; /note="Histone chaperone cia1"; /id="PRO_0000089743" MSIVNILSVNVLNNPAKFSDPYKFEITFECLEPLKSDLEWKLTYVGSATSQSYDQILDTLLVGPIPIGINKFVFEADPPNIDLLPQLSDVLGVTVILLSCAYEDNEFVRVGYYVNNEMEGLNLQEMDDAEIKKVKVDISKVWRSILAEKPRVTRFNIQWDNPDFDDAPPVQPDADEEEEEEEADEMEEEFDEEGEGDEEEEEEDDGDGDGEGDGDGEGENDGKGSEEEEEEEIDIEEEEEESALANASAAEEKPEEKPETSQ O74526 KJ45_SCHPO ACT_SITE 584; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 452..460; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 480; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 94; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC70.05c; CHAIN 1..781; /note="Probable serine/threonine-protein kinase C70.05c"; /id="PRO_0000086137" MPSDKPVFDIGSQAPERSDSESPSSRSIGSGTPAPVRKGLSKFKNSFLSRKNSSQIKSPSDYKSSAHEQRVNHTTDSMAHVPGNNSPLQTPQKSPPRQKHTAPATPIPVSASRHHKPHHSGLKNLLEKAMHPGHKSNANSPTSESPSKGFGSFINNHILHKNTSSHPSSPVNGKSSDIHKSQSYQHLKNSPPNSRTARKPVPRRANSASHNLGSTKSPNGNAKESLSRSAELPSKAKPMEINNGYRKKPSPLSPNSSIRNREGGNGSYFDGPLTASPTPSSPTGTPNSMSKSPSLSSLASTGASYRPGPSKPLVSRVRDNYANTSYESWPHSTEFDMFTYAVSGSLKLTPQGTGFDCINPANPFSPGYSGKSSMKSDDNVGSSANTAPNSPTSANSSEGNQGNGPTTYPIKPPTNISEIPRKLKSGFIPPYAKRVVPRLSAKYKLVDETKDMGSGATAVIRIVTLKNPKENEKNLRFAVKAYRRKADDETDGQYIAKLASEWLVQCRMEHPNVVKSYDLCIDSHIFPLYSDTWCAVMDFCPRGDLLSLIEDRHDRLGKKDFECMIKQILRGLNYIHSQGIAHRDIKPENILISEYGVLRITDFGACDVLCNPGDDITAVESKSMGIFGSDPYMAPEILTPGSYNAFFADMWSTAIVLHCLYFRTYPFRKASQNDQLYAKYCKAWREYNLICDVQNIRISKTLPYFKPVNDLPMHMQRLFFCLANPTAEQRITAQEALNLPFVQEIECCSVDDCTCTHDAPEECLEWANPPVQKLSTPHNHL O74540 FADH2_SCHPO BINDING 50; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 51; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 72; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 73; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 102; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 105; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 108; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 116; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 179; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 204..209; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 228; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 297..299; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533" CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P32771}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P32771}; CATALYTIC ACTIVITY: Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378, ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000250|UniProtKB:P32771}; CATALYTIC ACTIVITY: Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000250|UniProtKB:P06525}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + S-nitrosoglutathione = NAD(+) + S-(hydroxysulfenamide)glutathione; Xref=Rhea:RHEA:78371, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:145544, ChEBI:CHEBI:229723; Evidence={ECO:0000250|UniProtKB:P32771}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P06525}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525}; SPCC13B11.04c; CHAIN 1..380; /note="Putative S-(hydroxymethyl)glutathione dehydrogenase 2"; /id="PRO_0000160784" MQQSPTAGKIINCKAAVAWQPAAPLSIENVQVFPPRVHEVRIKIVNSGVCHTDAYTLSGKDPEGLFPVILGHEGAGIVESVGPQVTTVQVGDPVIALYTPECKTCKFCKSGKTNLCGRIRTTQGKGLMPDGTSRFSCNGNTLLHFMGCSTFSEYTVVADISVVAIERLAPLDSVCLLGCGITTGYGAATITADIKEGDSVAVFGLGSVGLAVIQGAVKKRAGRIFGIDVNPEKKNWAMSFGATDFINPNDLQSPIQDVLIHETDGGLDWTFDCTGNVHVMRSALEACHKGWGQSIVIGVAAAGQEISTRPFQLVTGRVWRGCAFGGVKGRSQLPDLVKEYLDHKLEIDKYITHRRPLKEINEAFTDMHNGNCIKTVLSIP O74544 RAGCD_SCHPO BINDING 17; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P53290"; BINDING 18; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P53290"; BINDING 37; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P53290"; BINDING 118; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P53290"; BINDING 121; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P53290" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q7L523}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:Q7L523}; SPCC777.05; STRAND 5..10; /evidence="ECO:0007829|PDB:8FW5"; STRAND 54..56; /evidence="ECO:0007829|PDB:8FW5"; STRAND 59..61; /evidence="ECO:0007829|PDB:8FW5"; STRAND 76..88; /evidence="ECO:0007829|PDB:8FW5"; STRAND 112..118; /evidence="ECO:0007829|PDB:8FW5"; STRAND 121..123; /evidence="ECO:0007829|PDB:8FW5"; STRAND 153..157; /evidence="ECO:0007829|PDB:8FW5"; STRAND 197..203; /evidence="ECO:0007829|PDB:8FW5"; STRAND 208..212; /evidence="ECO:0007829|PDB:8FW5"; STRAND 242..245; /evidence="ECO:0007829|PDB:8FW5"; STRAND 258..263; /evidence="ECO:0007829|PDB:8FW5"; STRAND 266..273; /evidence="ECO:0007829|PDB:8FW5"; STRAND 275..285; /evidence="ECO:0007829|PDB:8FW5" HELIX 16..22; /evidence="ECO:0007829|PDB:8FW5"; HELIX 70..75; /evidence="ECO:0007829|PDB:8FW5"; HELIX 91..107; /evidence="ECO:0007829|PDB:8FW5"; HELIX 125..146; /evidence="ECO:0007829|PDB:8FW5"; HELIX 164..176; /evidence="ECO:0007829|PDB:8FW5"; HELIX 180..194; /evidence="ECO:0007829|PDB:8FW5"; HELIX 219..239; /evidence="ECO:0007829|PDB:8FW5"; HELIX 292..309; /evidence="ECO:0007829|PDB:8FW5" TURN 23..25; /evidence="ECO:0007829|PDB:8FW5"; TURN 204..207; /evidence="ECO:0007829|PDB:8FW5"; TURN 286..291; /evidence="ECO:0007829|PDB:8FW5" CHAIN 1..314; /note="GTP-binding protein gtr2"; /id="PRO_0000372338" MKPRKIILMGLRRSGKSSIQKVVFYKMPPNETLFLESTSKLTQDHISSFIDFSVWDFPGQVDVFDAAFDFESIFTQVGALIFVIDAQDDYLDALARLHVTVARVVTINPNICIEVFIHKVDGLSDEFKIDTQRDIQQRTQDELADIGLENVPISFHLTSIFDHSIFEAFSRVIQKLIPQLPTLENLLNIFCSNSLVEKAYLFDVLSKIYVATDSSPVDVQSYEICSDFIDVILDIGSIYGRSSQLKPGHSPEILDETSSVIRLSNDLVLFLREMNQYLALICIVRADNFEKSGLIEYNVQCLQTAIQSIFSPRT O74547 BIT61_SCHPO PTM: Either Thr-23, Thr-25 or Ser-26 and Ser-78 or Ser-79 are phosphorylated as well. {ECO:0000269|PubMed:18076573}. MOD_RES 109; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18076573"; MOD_RES 201; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC777.08c; CHAIN 1..422; /note="Target of rapamycin complex 2 subunit bit61"; /id="PRO_0000352803" MVGRGSFSSTSSASSINWIPKNTKTSIESVSNTISLSENGQNQDLETVTTKESNVGDSDTTENIKSPFNGQWPFSRRSSQSSSHPVFEETHWSKHSKRPGKLNVLTPTSPSNVNAEVQSISTKTQLSLLNLSPHKHKKPKDGLDLSALQKTLNGSRNFLRGRRDAGGIFGASIPQSLVTNQIINGFGAASLAFAKLGKVRSPLEGRFNLVPISADETWLIVESEVCSLYSGEALHYSLEDLNGILILHLQALIRDTKMNEFVGHLETLFRKATKCLSDSLSPVPEELFLNRIIETWLFFFSSVLPYVQGVFLPIKTKLFDEQEKTQLPYEVNEFCSTNREKLNVHRLALMTFRDYMVLPIANRIQICIGRAESAENALDNAGEVFARLFQILSLLASVRTNDSKEQEITNLATKVRCLLIAS O74548 ARGD_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 294; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPCC777.09c; CHAIN ?..441; /note="Probable acetylornithine aminotransferase, mitochondrial"; /id="PRO_0000002081" MFQRRSLLSVRSSGSQIAFRRFVSLTHKDPTPDTTSCNIIKKEGANIISVYARYPVVAAKGEGSYLFDKEGRKYIDFTSGVAVTSLGHAHPEVARLAADQCSKLVHSSNLFYNEPAIELSNVINNSLAKNSGIAGPTKIFFANCGTEANETALKFARKAAFEKYGEGKSQIVYFNNSFHGRSLGSLSITANPKYKRGFQPLLPDVVQAVYNDPASIEQFVNDKTAAVIVEPVQGEGGICPAKPEFLIALRKACDKVGASLIYDEIQCGLGRSGDLWAHSIVKDVASPDIITVAKPLANGLPIGATIVSSKIAAEIHPGEHGSTFGGNPVACRVGTFCVNELGSSKILQNVRKQHKALTSRFDDFVAKYPNLIRGYAGRGLLLGLQFTEPPAKFIELARQQGLLLLPGGNNNTRVLPSLNVKDEVIAKGLDIMESTLKALSK O74552 VPS35_SCHPO MOD_RES 316; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 783; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC777.13; CHAIN 1..836; /note="Vacuolar protein sorting-associated protein 35"; /id="PRO_0000065898" MNGINTANEEITRSLEESLNICKQSSRLMQRNLQTGRLMDAFRNCSISLVEMRNSALTPKQYYELYMFNMESLRLLGGTLLETHLNGTHNLMDLYELVQYAGSIVPRLYLMITVGSAYLETPNALVREIMNDLLDMCRGVQHPLRGLFLRHYLLTQTRKGLPLGSEDEEDASRKGTVLDSVKFLVINFTEMNKLWVRIQHLGPIKEFSKRTQERNELKVLVGLNLVRLSQLNLDIDTYRDHVLPAIIEQIIECRDSLAQEYLVEVICQAFSDNMHLQTLDTYFGTVIKLSPSVNVTQLVVAMLNRLTDYVQREYESDSSNEDESETVTEKLGDIKINEEVQQKDEQECPGDKVIPPEYAIQEVLWSHVVEVIQSRSGLPLDCIVSILSSILNFFLRCYPYKPQYADRVFQYINEHIINQPSLRSALHERPLQKSLCAILLLPLTYFPSFSYCLELQNFLPVFNAQDPNLRYDIARMIVQKIIEKGHSLSELTEAQELLGFVSVIIEKKGVDSLDDLQNVALMVHYLNNDDPQIQIEILRSLKDTFIKAGENVKYLLPVVVNRCIFLARNFRIFKCMDWAEKVRLLWEFVNTCINVLYKNGDSLELCLALYLSAAEMADQENYPDFAYEFFTQAFSIYEESVLDSELQYQQLLMIIGKLQKTRNFSVDDYDTLITKCTLYASKLLKKPDQCCGIYLASHLWWQVASGEDSRPFQDPKRVLECLQKSLKIADACMDQLTSLKLFINILERYFYYYDQHCESIIAKHISGLIDLTEQNMRSILISSPADLIASDPRAYASSIWEVANVSVIDSLKNHLERATAYAEKRSEDERWSSIFQ O74553 DUS4_SCHPO ACT_SITE 108; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" BINDING 26..28; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 79; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 149; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 177; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 208..210; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 232..233; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH + uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535, Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90; Evidence={ECO:0000250|UniProtKB:Q06063}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53346; Evidence={ECO:0000250|UniProtKB:Q06063}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH + uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535, Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90; Evidence={ECO:0000250|UniProtKB:Q06063}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53350; Evidence={ECO:0000250|UniProtKB:Q06063}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(20b) in tRNA + NAD(+) = H(+) + NADH + uridine(20b) in tRNA; Xref=Rhea:RHEA:53352, Rhea:RHEA-COMP:13537, Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90; Evidence={ECO:0000250|UniProtKB:Q06063}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53354; Evidence={ECO:0000250|UniProtKB:Q06063}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(20b) in tRNA + NADP(+) = H(+) + NADPH + uridine(20b) in tRNA; Xref=Rhea:RHEA:53356, Rhea:RHEA-COMP:13537, Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90; Evidence={ECO:0000250|UniProtKB:Q06063}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53358; Evidence={ECO:0000250|UniProtKB:Q06063}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853; Evidence={ECO:0000269|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857; Evidence={ECO:0000269|PubMed:34798057}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q5SMC7}; SPCC777.15; CHAIN 1..326; /note="tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]"; /id="PRO_0000316228" MRDRLKDPVKIFEINKGKRPVHIAAPMVRYSKLPFRQLVRDYNTDIVYTPMILAKEFLHPKGRYFDFSTNDADASLILQFGVDDPVILEKAAQLVGPYVDGIGINCGCPQTWAIQEGIGSALLDEPEKVHKLVRAVKSTLGESFCTEVKIRIAKDLNKTRHLMQVIEKSGADIITVHGRTRQDRSSFPVNLDAIREVRPCVQIPVVANGDVKSLRKGLEIAKYTETQGIMSARGLLENPALFAGYEETPWGCVERFLWYSTSYSLNFHLFYHHLTTMMGQMTTKRERMTIPKDSFASVMDWLDEHFVVRRPDEPMFGESVLPCRRY O74557 NCB5R_SCHPO BINDING 142..157; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 168..199; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; Evidence={ECO:0000250|UniProtKB:P38626}; CATALYTIC ACTIVITY: Reaction=2 Fe(3+)-[Dph3] + NADH = 2 Fe(2+)-[Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71231, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228; Evidence={ECO:0000250|UniProtKB:P38626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71232; Evidence={ECO:0000250|UniProtKB:P38626}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255}; SPCC970.03; CHAIN 1..301; /note="NADH-cytochrome b5 reductase 1"; /id="PRO_0000310844" MAKQTLLSTPLHGVYIPVFLIIFGTYIVKREWVGYAIVVAFSLGFHKFWRGRVRKVLSDKIQQFELSDKAVLNHNTAIYRFRLPRANDVLGLPIGQHLKVFVDVDGKEYSRSYTPLSSDADKGYFDLLVKSYPNGKVSKKFSELKIGDTIGVRGPKGNWKHRTGLARHFGMIAGGTGITPMLQIIRAVLSNFEDPTEITLLYANVSEGDIVLRDEIDALAKKDPRFTVHYVLNNPPENWKGSVGFVTQELIKAHFPAPSPETKVLICGPTPMVNSLREATVALGYEKSRAISKLEDQVFVF O74635 RPB9_SCHPO BINDING 7; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 10; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 29; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 32; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 75; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 78; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 103; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 106; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472" SPAPYUG7.04c; CHAIN 1..113; /note="DNA-directed RNA polymerase II subunit RPB9"; /id="PRO_0000121473" MSNFQYCIECNNMLYPREDKVDRVLRLACRNCDYSEIAATSKVYRHELQSSNVENTTVSHDASTDPTLPRSDKECPRCHQHEAVFYQTHSRRGDTMMTLIYVCVHCGFAFEEQ O74731 DUS2_SCHPO ACT_SITE 116; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" BINDING 14..16; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 87; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 159; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 187; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 221..223; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7"; BINDING 245..246; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q5SMC7" CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH + uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533, Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91; Evidence={ECO:0000305|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53338; Evidence={ECO:0000305|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533, Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91; Evidence={ECO:0000305|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53342; Evidence={ECO:0000305|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853; Evidence={ECO:0000305|PubMed:34798057}; CATALYTIC ACTIVITY: Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; Evidence={ECO:0000269|PubMed:34798057}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857; Evidence={ECO:0000305|PubMed:34798057}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q5SMC7}; SPBC1709.06; CHAIN 1..479; /note="tRNA-dihydrouridine(20) synthase [NAD(P)+]"; /id="PRO_0000316226" MGLLNYSNKVCLAPMVRIGELPMRLLALRYGANLVWGPEIVDKALLSGTPVERVVNDRINCIDFVKPPSNKVLFRVHPLEANRLIFQLGSASPELAVEAAKLVANDVAGIDLNCGCPKHFSVHAGMGAGLLKNQDRLVSILDALVNEIGKPYKISISCKIRLLETKEDTLKLVERICDTGVRAITVHCRTTPMRNTEPADRSYLSEIVGVCRNKDVSILVNGDVLSYNDGLDVIEKYGVDGVLIARAAERNVSCFRIEGPLSSFKVAEEFLKMALEVDNNFGNTKYCLNQIMQGSFRKNVRQLAQTAKTYEDLKKAFEIEYKHSDASSVCPTLEKEKSLVISFVDLPSFLESLLASNILKQLSRLHFTKIFAVSEEEDICKQLDDIHEKFLCHGIALSLISADNLASAIASAHLVICMEKDESIMNEAVCDQKITIRLPINSNTNEAVVECENKSMQSKHALDIIQERIKDLEEKAQVV O74739 PNG1_SCHPO ACT_SITE 163; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 190; /evidence="ECO:0000250"; ACT_SITE 207; /evidence="ECO:0000250" BINDING 105; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 108; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 137; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 140; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 210; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.; EC=3.5.1.52; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC1709.14; CHAIN 1..333; /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase"; /id="PRO_0000248994" MDFHAISQRFIDMMRSKNSQNASQPPETYPFYHEVRQMSQHPWMYEDPELQDYALSILPLDKLFQDASELEKEGDGSWGYQDYVIQALLKWFKREFFVWVNQPPCEKCGGETHMTGNGPPNEEEKWNGVRNVELYQCNVCGHNQRFPRYNRIRALLDSRKGRCGEWANCFTFLCRALGSRARWIWNAEDHVWTEVYSNKQQRWVHVDSGEESFDEPLIYEQGWGKKMSYCLGFGIDSVRDVSHRYIRHPENGLPRDRCPESVLQQALHEINIEFRSRLTDSERKALEEEDKREKDELDGYMRPVSQATPTNTDLPARQTGNVEWKEKRGEAGK O74742 FOLE_SCHPO BINDING 89..92; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 121; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 190; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 218; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 332; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 346; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P08192" CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738, Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005, ChEBI:CHEBI:456216; EC=6.3.2.17; COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000250}; Note=A monovalent cation. {ECO:0000250}; SPBC1709.17; CHAIN 1..505; /note="Probable folylpolyglutamate synthase"; /id="PRO_0000168311" MHTAKPVKRYFNLKSSRIGMNPQTKTFEGAINRLNSLQSNAKVLEVLRKRGKIPNDQSMVEMRHWLRCIGYQPSDLNRLNVIHVAGTKGKGSTCAFTSSILQQIQKSGERSIPKCIGMYTSPHLRSVCERIQLNGKPISQELFTKYFFDVWERLENAVGSDSEKPMYFRFLTLMAWHVFISENVDAAIIEVGIGGEYDSTNLIEKPYATAVTSLGLDHTSLLGNTIAEIAWQKAGIYKESAIALTCEQAPEAMNVLKNRAAERNTSLKVVIPPAELTPDMIGLSGVHQLGNTSLAVSLVQEFYEKAGCPFDRDPYQDPAILDGLKYVKWPGRCQIEEINNIKWCFDGAHTKESLEATGLWLASKKNLYEDADARILLFNQQSRDDPIALLRSFLKGLESSGTGISFTHVIFSTNVTWKDAGYNPELLSINTITDNKPVLHVQEDLCKWWKESKGTTSEATVAPTIQEAIETVMSIKQKSRNTFVCVTGSLHLTGGVFVVLDQAVF O74745 ANP1_SCHPO SPBC1734.04; CHAIN 1..430; /note="Mannan polymerase II complex anp1 subunit"; /id="PRO_0000193673" CARBOHYD 122; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKANRDFGRDGGPFSITPNRFQPKSSGNPIFRQKTIRTVGIIALTLVLFLFFHRSFFSSFGEFPSFSSTANAPNSDVQEYDLRKVMNAKFTGDYSPKEKVLICAPLRNAAEHLNMFFGHMNNLTYPHELIDLAFLISDTDDNTLEVLKQHLDAIQNDEDESKHFNNVLIMLKDFGAIFGQEFSDRHGFAAQGPRRKLMARARNWLLSAAIQPYHSWVYWRDVDVETAPNTILEDLMRHDKDIIVPNVYRPLPDWLGNEQPYDLNSWAESETALQLADTLGEDDVIVEGYAEYATWRPHLAYLRDPNGDPSVEMPLDGIGGVSIMSKAKVHLEGCEFPAFSFEKHAETEGFGKMAKRMGFSVYGLPHYVIWHIYEPSDDDKRIMAEMERERKEREAAELEEAKKYQTAGFTQPDDQGAEEGPLAHADDHVD O74747 RAD18_SCHPO BINDING 159; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 162; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 174; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 178; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; SPBC1734.06; CHAIN 1..387; /note="Postreplication repair E3 ubiquitin-protein ligase rad18"; /id="PRO_0000056159" MNELDATDPSDWNQTKIPSLKGLDSSLRCLICHEYFRAPLITSCSHTFCSFCIRDYLREHPMCPACRAPEQESRLRKNTILEEILESFKVIRPTLFEFLKVENVPKPVLQAPETVIAQDSASGDEEWEDDLASNSSPASIAKKTSRDSKKRKREDLVHCPACSNLVPHNQINQHLDSCLNSPSSPSSSSSPYKNKDNSKSNSLLSFKTDDDSITKRRLRSFNSADELPLKDRVRLPKLTYALLSESKIRSKLSEMGLPTDGHKQLLQRRHAKWVTLYNSNLDQKQPVSKRNLIRQLIDWERVQSKSIGVEKEKLGGGDWEKAYAEDFADLINRAKQSTTNKNDSLRNTAVESSTEPSTSNGFPATSVSPPLTIDLTNSQTGSDGPQS O74749 HSE1_SCHPO SPBC1734.08; CHAIN 1..373; /note="Class E vacuolar protein-sorting machinery protein hse1"; /id="PRO_0000292503" MFRGKPNSIETLILQATDEKNTKEKWDVIMDACDQLSSTSGDVGRNSIKFLNKRLDTANANIQLLALTLTDAIVKNCKTSIVREISSRTFTDSLLKIASDSTTHNRVRSRIAVLVNEWAEIMKKDPNMSLMQDICEKIRKLDIVDLRAPKKPEKEAMNELELKREEEELQYALALSLSESTAQSNKVENPQSTKDEPLQKTNQRQESNLATSPASTVSRVRALYDFAATEQGELSFKKGDIILVLESVYKDWWKGSCKNAVGIFPVNYVQRVVEPTIEQQRQSAHMEQQVFDALPQIDELLDTLSTTSPDAADDDALQGKYHAMIALRPKLVRLIEKYASQKEELMDLNERLLVARRDYEKLYEQSMSEMRNF O74756 CHS2_SCHPO SPBC1709.01; CHAIN 1..926; /note="Chitin synthase-like protein 2"; /id="PRO_0000193717" MSFQNPSYINAKHRSFLQPKDTQDSQDLRNWVSHSSVDEETAYSSSTLSSSSSKSFPCYDEYDEIKSPDDQKVEYMKTLRTLEEDAFSYTDSVYDFEERSFDEHEPPIPPLHKTGVFSVPLQPTHTVNSNSDDGYENSSKNEYLDFNSEISASPVNEPMTHSQSYTSIDRLNSSSSHYSKDVPLLCGSLTIDCPTPIDLRGMLGPFMQKNPDEASFLRYSAITCQPEDMNNNGLQLRTWSTGRDIQIAVCLTLSDEDLASFAISLSSIMNNLKHLCSRSKSRVWGNESWEKVLVCVVIDGRNTVHQNVLDLLASIGVYQPHIAKGRVNGKRTLSHMYEFTSTINVDEKLNLTTATGDGNVPMQMLLCVKDRRLGTYNSHRWFLNGIASLARPKVCLFVRNGARLGPTSIYHAWKAFDVDSTIGGMCGKTSIDTGKFGFRLLNPFIASQHFDQMIHNNLRLPYDSCMGYISNALNAIYGFRYVALQDSYPNPGPLADYFEQDQYEIPRRGILQSNAFLAQEQLLFWKVITRKDAKWHLQYVPEACATIEAPNSMAGILESKKSEINSSFSLAVYVIVDFFSLWTTRHKFFRFLLLTVQSLVFAIEKLVNFFSMANFFLAFYFVCNATSYSSLNPYGNWARPLFLVFEYILICLIFSQFMLAMGNRPRSCRVLLFISTALFSIIMIYFVFCVFYISLIPLHNSDNSEIVLGNNYFTTLIFSSLLILACYAFVSLICMDPFFIFTCIVQYILLMPTRIYTEQIYALCHLDDASISKDDNQQEFNFDTGITHCSMNDEGYTTISIPKANVLNSVYNSSLKNFSSSNDTSVYHDVQDHCYRKPQSYEDHYQDIRTRYVLVWAVSNLILAIVLIQVFDGMRFINNGYMKYIFWSIVAFTAWKTMGAVTFIATKIISRIANCVKSKLYIFNDP O74761 PRI2_SCHPO BINDING 291; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 369; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 386; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 428; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P49643}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P49643}; SPBC17D11.06; CHAIN 1..459; /note="DNA primase large subunit"; /id="PRO_0000046775" MFRTTKSRVVEKNQNFSSASFESLSYPTRLNFYKKPPVSEISIEEFETWAIDRLVVLGEIESAMLRNKTKNELNGIIKKILDKRLPMSSNMARTVKGNSLDEERRKDHYSHFILRLAFSRSDELRIRFLRAESTLFRFRFVNEETRERQAFIDSLDFQWESVSQEEKDVFYEKLQASSQRNIENESFFKVPFFKVPDLVERRAVFVHKGYAYVPFSEQVSLVVEEFEENLKKALESTAKSLPRLDEDDRLLPILNHLSKGFVAPESSIVAPKSGAITAGQVDSFVSHFPLCAKHLHEVLKRDKHLRHFGRLQYGLFLKDIGLSVDEALVFWRKSFTNVTEDKFNKEYRYNIRHTYGLEGNRKNYKGYNCQQILTGPQLGPGDAHGCPYRTYSVNNLVSALASMGIAPDSAGCREVVEAVKARHYHIACTRVFELTHPNVGSLEESIHHPLQYFQLSLES O74771 DIP1_SCHPO SPBC24C6.10c; CHAIN 1..374; /note="Protein dip1"; /id="PRO_0000372346" MEFTDVFYNLENEKQFLAEIDELLTIPYEKNELEIGVSKFLSFINKYGEPYLITEFQLQRCMEKFLNSPLYQLDENAVLSIFYDCFFFLKEQQTLKFIIIVFQSEIQENEYCLRLLASTGFIPVLIKAMKQFKDRSENVAFTSFRYALFLVYYICRSRRLSPTDLVAIDEYFLVNLFKTSEEAWNDEDMDSFGMCVLTLLSINEQFMLVRLASKGSFEIANGIMDLLSSSKVDNGIYSEGLVFTLNREKDPRSRMLILKQLFLLFTTPATYEIFYTNDLNVLIDIFIREINNIPDELSDLRYAYLQVLIPLLENTQVRHPPHYKTKCIVDAVNNVLISHSKSSNMEDARTTDVAIRVLEVPWLQQEMKSLGTAQ O74773 MSH2_SCHPO BINDING 721..728; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC19G7.01c; CHAIN 1..982; /note="DNA mismatch repair protein msh2"; /id="PRO_0000115190" MSSRNASIANERTDEARMFNFYEKMPKDTNTVRVFDRGEFYVAIGEDASFVAQNAYHTTSVLKHHNVSNTSYCNLSPSLFIKFAEDVLSNLAKRVEIWGANSAKTGFELLKQASPGNMQMLEDLLVSENYQESTAISDSSVSSVLLAVTTRVKQDQRIIGVAFIDPILKKLGVSEFVDSDAYTNFEALIVQVGAKECIISQSGHESTNGNSAVSINTAEINRLRNIIEGCGALVTTIRSSEFSARDVELELSKVLDSPVTHALVPELGLQLAMASCNALLRYLGPALLNPDMEDDRENTSRKLHLYHHNLEQYMRLDIAAVRSLNLLPPPNGNAHKTMSLYGLLNHCRTAMGARNLRRWIVQPLLDAKSIERRHDLVSALVEDAEARQLLLDDDHLLRSIPDIPKLCRRLTRGSASLEDVVRIYQMAKALPKIVTVLDSLTSEHKDLVDKVYTNVLNNHCKNLEKLIELVETTIDLEALDSHQYIIRAEFDEELLDLRQRLDELQHSIFEEHKRVGSDLHQDTEKKLHLEQHHLYGWCLRLTRTEAGCLRGRSSHYTELSTQKNGVYFTTKRLHSLNNSYMDHQKSYRYHQNGLAREVIKIAATYGPPLEAIGQVIAHLDVILSFAHASTVAVIPYVRPNIVDSSIAQEKHGQSSNILDIVSLEDTPNFEEIRRTLENNHCARLYLKQARHPCLEAQDDVKFIPNDVNLEHGSSELLIITGPNMGGKSTYIRQVGVITVMAQIGCPVPCEVADLDIIDAILARVGASDSQLKGISTFMAEMLETATILRAATPRSLIIIDELGRGTSTTDGFGLAWAITEHIVTQIGCFCLFATHYHEMTKLSEEITTVKNLHVTAYVGDSESKDVALLYNVCEGASDRSFGIHVAKLAHFPPKIIEMASNKAAELEAEDSGAQGDTQEVKSKKEGMAIVRDIMRQWRSNVKPEMTQQQMMDQFQKVIGSFAQQINSNNWLQSRVSTNEVSS O74786 SEC9_SCHPO MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC26H8.02c; CHAIN 1..419; /note="Protein transport protein sec9"; /id="PRO_0000213611" MKKLFKKKKGVSPHMYMLPEESNSNTATNAPSYSVGGTTANSYSSNSYNDNNNSNSTYGSSNNYGNYGSSNNYGSYGASNTYGSNGSSNNYGNYGATNSNGDAGYSITPIRNDPYARKDMPPMKSSAAVTERPSMHRSAPSQDTLDLKKQELFAGARIQNDDESTTDTIPHNDDGTEGDEYGEGYRDGYEEDQEVEAIKQKIQFVKQDSLSSTRNALLMAGNAEQMGLATLANLGEQTEKIATAEKELDISKIHAKRAEEQARELKTLNRSMFAIHVPKPWGKAKRVAAEEARLAAKRDAERQDEMLNRQFAYRSQKRIDQAMKDNMKSNKKKGDSKGVSILERSHYQFEPDAEDDAMEKEIDGNLDQIGALATRLKGLAYATGQEIDSQNARLGSIHDKSDRLDTDVYLNVERLRHIH O74787 CHO2_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_03217}; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC26H8.03; CHAIN 1..905; /note="Phosphatidylethanolamine N-methyltransferase"; /id="PRO_0000089647" MTNQIPSASSAADFGSSKSTSVDAVPNMDKSSSVRRKNIDSNGLQQTNQIEQAESSLNAEADHSEPERYGCTPSGKVFLLPKEQENRRSILETVDPRFSKTPWDWIVISSILAQVLLFFMTTGAVRRYSMMLCFFFWRISYDAGIGFLLHMQSNHRKVVTWISDFGFFDKENHPKLYDLTKKQLISKMDSSYNYDTSPLEFNSWLVFRHFVDLILMCDFCSYILMGLAWTCWPKVNIILQFLRIFGGIALIVFNYWVKMDAHRVVRDYAWYWGDFFFLLRSSLVFNGVFELAPHPMYSVGYAGYYGMSLLTGSYAVLFASILAHAAQFGFLLFVENPHIERTYGTDINHARLSPRGEDNEFELPPEHDLVGFVNFDFTRISDVALLIIALYSIFIILLSSNSHYSQFWAIFQAFVWRFLHSIIHAFILFYQSKSKAWTKHFIRNGESAAYAWSQWKGLYNLTLNMSYISFVMAAWKLYHLPSNWTYGLVSLRHALGFGLIALHIYTSVSIYEDLGQYGWFYGDFFLPSRSPKLVYQGIYRYVNNPERFLGCSAYWGLALISSSAWIFLIAILAQLSNLAIIRLVEQPHMQKVYGNTLRKEAGISKLIKQATSEKGNILPKTVETHMKALTTSVDKVLDQTAEALEEFVNTAPPKVQELLKGTESNLRKNAQLAILKLFAPQLSSSTHFDYKLEIKGIDNNQVLLGHPITVCWTASPNHEINDWIGLYKLSDNASDLYTQTSSEGRWSAIDANGYTSHCSSIKSLSNDKNSGEVEFSGDLLFWETGTFEFRYHYGGKHLVMAKTEPFVITATSMNTTDVDEVSAYLLKSIKFCDPNITPHDGDASLCDISEGSARKLTSIIKYSFGIDLSYRVVQVDGSCSALSRRIVNSLKILQSFDGPSGAKDD O74789 YOU5_SCHPO ACT_SITE 114; /note="Proton donor"; /evidence="ECO:0000250" BINDING 53; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 55; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 81; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 81; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 113; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 163; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 237; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; MOD_RES 272; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 348; /note="Leucine methyl ester"; /evidence="ECO:0000250" SPBC26H8.05c; CHAIN 1..348; /note="Putative serine/threonine-protein phosphatase C26H8.05c"; /id="PRO_0000310805" MTDLDLDWQLEELENGRLIPESNVVELCQRVRDILIEESNIQWISSPVTICGDIHGQLHDLLELFRIGGSCPGTKYLFLGDFVDRGFYSVETFLLLLTLKCKYPKEMTLIRGNHESRQITQVYGFYDECVRKYGSANVWRYCCEIFDYLSLGALVDGKVFCVHGGLSPSISSIDQIRLLDRKQEVPHEGAMCDLLWSDPEDISGWGLSPRGAGFLFGADVSEVFNRANDLSFIARAHQLVMEGYKIHFSDKDKQYPKFTNEEDSELDSDSASPVDDSPAPGDIITIPEKDKGSVVTVWSAPNYCYRCGNVASILQLDENQTQSFKIFGTASQERSGIPTKRPIADYFL O74790 GLRX4_SCHPO BINDING 164; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250"; BINDING 172; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 201..205; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250"; BINDING 226..227; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250" SPBC26H8.06; CHAIN 1..244; /note="Monothiol glutaredoxin-4"; /id="PRO_0000102253" MSVEITFVEQFQEILQNGKEQIILLNFYAPWAAPCKQMNQVFDQFAKDTKNAVFLKIEAEKFSDIAESFDVNAVPLFVLIHGAKVLARISGANPQKLKAAIDEYIQPLISQISSTNASVETQVNSVQTTNTTSNTSKAPNGLDSELNERLSTLTNAHNVMLFLKGTPSEPACGFSRKLVGLLREQNVQYGFFNILADDSVRQGLKVFSDWPTFPQLYIKGEFVGGLDIVSEMIENGELQEMLPN O74796 ORC6_SCHPO SPBC2A9.12; CHAIN 1..264; /note="Origin recognition complex subunit 6"; /id="PRO_0000127101" MERQQIIESLRRIIPTESTEYNERLISLGESFLEWSKYKHNLKATEELCRPYMAAHLACELLSNDLNLEINLLATPIPKKKYYKLFTYFQEILSPLTKSLAAKDDLMETITYLCTKLGGSTAIPYVKQLVKAVVTNDMRIEHKRGIIIAAYLLVSAKAFGKDELHINHTERRKAQSVLQDTSSALQIQYWMHVLSESWQYKEIPLNGIEGYESQKQRIKPWSGIASMIQIDYEKRLQNYPIWKACIEERIQYYKSQLEKDGTAS O74799 EXG3_SCHPO CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; SPBC2D10.05; CHAIN 1..464; /note="Glucan 1,3-beta-glucosidase 3"; /id="PRO_0000184054" MGLNKQDLYIYRKQYGVNLGAWFCAERWINDFLFTGEGSSELEAVSGNVKAHGIDKARENFEAHWKSWIGIEDFSYMKQHLVNSVRIPLGYWSLGNDELVKGTPFEPYAEVYRNSLHILCEKIQEAGSLSIGVLLDFHGVYGGGNCDGHSGTSSGKAEFYEKQEYQDRTVEAVKFLSSKIGQFENVIGIQVINEPIWGQYDVLANFYQKARSVVPSYLPVYIGDGWDKDHWVNWVNDHESEGFYVVDHHSYFCFGGELCHAPPKLITRRLDTGEEYGKTKLSNIVIGEWSCTLSQESWSQTKLHDKRRRDFGEAQLNQYLNYCGGCFFWTYKFLHGKGGDWDFRSVVEDKVINYPPPPPTENKAMPALLEQSRDQNFGGHCYYWDQKQHDHPYEHDLYVKGWNQAWEDYIEFLQHGAMIGFPRAWTQKRMTSISSASAWEYRDGMNAAWLHLERMGFLNPFRHP O74804 EST1_SCHPO SPBC2D10.13; CHAIN 1..490; /note="Telomere elongation protein est1"; /id="PRO_0000087071" MSQQLSSNEICEEQGKLVKALCEAAQGGFKHDLYEKIIAIEIEVEKKLLNRLKSIQTNTFERPDIIWSCCHYKIIQHFRSRFREIHPRHVVEKKKTKKVFFKFLKTCAIFYQTCISELISKFQLDSYRPFFCKWTSSATVSSTISNDEMSSIPEASYSRNHMEALECVYNCFIYLGDMARYSSTCLKKRGAYDRALGFYDLAHRTLPGNGMHRNQIAVVWASDECIVESIYWFSSALCSEDPPKSALLNLLKQLIAFYRRCFAVHFEFVSPMMILLFIISDCCIHSLKEIQPFKCPSIMVKDLENSLLQSNIRNVGYEKKNLYYISSAFSNLLHCRYFNCNDRLRSFYYRFSSWLFHQTLACAKEVESERAPTSYLTSCLPSIKVILARVLESSPAFGFIERNELEQLSYHFRICEKFFKESSENKMLNLFEDYNEFGLCKSFICLFKRLNEDIIGPKLNINPPDYTTHPFSESIKRFYQISKILNLLLS O74824 RAGAB_SCHPO BINDING 11; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 14; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 15; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 16; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 17; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 31; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 37; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 60; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 122; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 125; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582"; BINDING 159; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q00582" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q7L523}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:Q7L523}; SPBC337.13c; STRAND 2..10; /evidence="ECO:0007829|PDB:8FW5"; STRAND 39..46; /evidence="ECO:0007829|PDB:8FW5"; STRAND 52..58; /evidence="ECO:0007829|PDB:8FW5"; STRAND 81..88; /evidence="ECO:0007829|PDB:8FW5"; STRAND 116..122; /evidence="ECO:0007829|PDB:8FW5"; STRAND 149..156; /evidence="ECO:0007829|PDB:8FW5"; STRAND 196..205; /evidence="ECO:0007829|PDB:8FW5"; STRAND 208..213; /evidence="ECO:0007829|PDB:8FW5"; STRAND 246..252; /evidence="ECO:0007829|PDB:8FW5"; STRAND 257..262; /evidence="ECO:0007829|PDB:8FW5"; STRAND 264..274; /evidence="ECO:0007829|PDB:8FW5" HELIX 15..22; /evidence="ECO:0007829|PDB:8FW5"; HELIX 29..33; /evidence="ECO:0007829|PDB:8FW5"; HELIX 62..68; /evidence="ECO:0007829|PDB:8FW5"; HELIX 73..76; /evidence="ECO:0007829|PDB:8FW5"; HELIX 94..111; /evidence="ECO:0007829|PDB:8FW5"; HELIX 124..126; /evidence="ECO:0007829|PDB:8FW5"; HELIX 129..131; /evidence="ECO:0007829|PDB:8FW5"; HELIX 136..146; /evidence="ECO:0007829|PDB:8FW5"; HELIX 163..175; /evidence="ECO:0007829|PDB:8FW5"; HELIX 179..192; /evidence="ECO:0007829|PDB:8FW5"; HELIX 224..241; /evidence="ECO:0007829|PDB:8FW5"; HELIX 280..300; /evidence="ECO:0007829|PDB:8FW5" TURN 69..71; /evidence="ECO:0007829|PDB:8FW5"; TURN 132..135; /evidence="ECO:0007829|PDB:8FW5" CHAIN 1..308; /note="GTP-binding protein gtr1"; /id="PRO_0000372337" MRKKVLLMGRSGSGKSSMRSIVFSNYVAKDTRRLGATIDIEHSHVRFLGNLVLNLWDCGGQEAFMENYLSAQRDHIFRNVQVLIYVFDVESREFERDLVTFRNCLEATVANSPQARVFCLIHKMDLVQEDLRDLVFEERKAILLETSKDLETTCLATSIWDETLFKAWSAIVYTLIPNTPTLESHLREFAKAAEAAEVILFERTTFLVISSYSSESNPATDAHRFEKISNIVKQFKLSCSKMQAQFTTFELRGGNFSAFIVPYTEDTYILVVIADPEIESAVTLMNIQSARRFIEASKSASDGIQLQP O74826 COQ7_SCHPO BINDING 54; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 86; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 86; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 89; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 138; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 176; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 176; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194"; BINDING 179; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194" CATALYTIC ACTIVITY: Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908, Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60; Evidence={ECO:0000255|HAMAP-Rule:MF_03194}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|HAMAP-Rule:MF_03194}; Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03194}; TRANSIT 1..27; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03194" SPBC337.15c; CHAIN 28..216; /note="5-demethoxyubiquinone hydroxylase, mitochondrial"; /id="PRO_0000315897" MLSRRQLIPIATKSVSPFLRSSITCRRISMGRKELSEKDSNILDSVIRVDQAGELGANQIYKGQHFILQFTDPKVAPTIQHMWDQEKYHLATFDNYVLKNRVRPTFLRPFWDIAGFALGAGTALLGTKAAMACTEAVETVIGGHYNDQLRETAHLENKAPEFKEIRSHLAEFRDDELEHLNTAVEGWNAKEAPAHALLTNAIQMGCKAAIWMCKRF O74827 PLMT_SCHPO BINDING 119..121; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03216"; BINDING 201..202; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03216" CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305|PubMed:9755189}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; EC=2.1.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305|PubMed:9755189}; SPBC337.16; CHAIN 1..221; /note="Phosphatidyl-N-methylethanolamine N-methyltransferase"; /id="PRO_0000193923" MSLILYPKPTSYLYQPFIKAYFSLNMAIFEINNSFLICAVSIALNPLLWNIAARSEYNHKTLTKLANGDSKKACYMLAACIFVAGIVRDLIYQNALKQQPTLGIFMNPLVQGIAKLIFCFGSVLVLSSMYKLGLVGTYLGDYFGFLLPERVSGFPFNVNDNPMYNGSTLCFLSTALRYGKVAGLLLTLEVFFVYRIALKFEEPFTAKIYAARDSKQAKKSE O74834 UNG_SCHPO ACT_SITE 142; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03166" CATALYTIC ACTIVITY: Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27; Evidence={ECO:0000255|HAMAP-Rule:MF_03166}; SPCC1183.06; CHAIN 1..322; /note="Uracil-DNA glycosylase"; /id="PRO_0000176171" MTVLNTTDKRKADDTVNKLDGKLKQPRLDNFFKTNTSSPALKDTQVLDNKENNSVSKFNKEKWAENLTPAQRKLLQLEIDTLESSWFDALKDEFLKPYFLNLKEFLMKEWQSQRVFPPKEDIYSWSHHTPLHKTKVILLGQDPYHNIGQAHGLCFSVRPGIPCPPSLVNIYKAIKIDYPDFVIPKTGYLVPWADQGILMLNASLTVRAHQAASHSGKGWETFTSAVLQVALNRNRKGLVILAWGTPAAKRLQGLPLKAHYVLRSVHPSPLSAHRGFFECHHFKKTNEWLEEQYGPEKCINWSAVSEQKAKIKSSELESSSTE O74842 FFT2_SCHPO BINDING 575..582; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; MOD_RES 323; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 383; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1235.05c; CHAIN 1..1284; /note="ATP-dependent helicase fft2"; /id="PRO_0000310748" MLPYNSNYLSDNGKRKFSDENPQSEVYGSSQTGLPSSYGNPQSYGTPPVQQSSAMYGVNNSMGGGMYNTSENTQFMNTDYSQTSSYASTPMSNAYSRDAPAAINNNFGYSYVGQSSQPVPSYNPLPSYNTASLPNAGIPAAMPGMPSGYPGTVPIPQGGYNAHYSSPYNNGYPIGAVNPTSAIPAQPPAQPVNNVLPSYVRSNSRSSARSTARSAPRSTQRSRSSSANPVTTPPVNNTLLTPPAPPVELPPVTTTSPNAIIRSVQWIRSFVPQAPIHQVINTLAQTKWDETAALSILSQKYLSCDLGIPIQEHKRFKQSPVASNMPTYGSSNRTVQSQKRSIRDKYIQMPNDSTQASLMPSYTRKTSNASKKLTTEEDEFYDSEEEPEAIVHRDTSALERTVLNFINSSTAKELSDTASCPLSHSKLLLEHRPFQTLAEACIIKHPDDVPSKPGRRGRRREKNPMGQKIVNACMETMEGYYAIDNLIAKCEFLGNRISKGMASWGIKLEMSNGELNIVDMESVPTEAADNSDFPKFVTEQPKTLASDVQLKSYQLVGVNWLHLLYQQKLSGILADEMGLGKTCQVVAFFALLLEQGHHGPHLVVVPSSTLENWLRELARFCPSLRVEPYYGSQQERANIREAIEENEIKYDILVTTYQLATNNKEDRSFLKHQNFDVCVYDEGHYLKNRMSERYKHLMNLNANFRLLLTGTPLQNNLKELVSLLAFILPNMFDSDMDDLDVIFKAKPTADADIEQALLSKQRISRAKTMMTPFVLRRRKNQVLNDLPKKTQIIEHCKLSENQLEIYNRYAALQKNQQLRRDDKRNKRSKNDEESDGKSLSAGHVLMQLRKAANHALLFRKFYDDEKLKQMAKDIMQEEQYKNANEQYIYEDMEVMSDFELHRLCRSFPTLQSYTLKDDPWMDSGKIRVLKELLPKMKEEGSRILLFSQFTQMLDILEQVLDTLKISYVRLDGSTQVEVRQDIIDQFHKEEDVTVFLLSTKAGGFGINLACANVVILYDCSYNPFDDLQAEDRAHRVGQVREVTVIRLITDNTIEEYIQKLANTKLALDMSLSSDGKDREEIGERLVQDMLDEENNGNNTKPEITGNESDGEFKVSSSNNSKQTDAEETNTGVPLEGSQPNSVEKTDLADGDEKANIKTEMKSETVEGDNKELRETMKGENVQTDSNAAVPSSKSSTEEPNESVLSGHLDLDTEASPVVSTIEKTTKGDVSVTEEQQSANIDGQLEKPEIEESKKPDVLNQVSLSIEEEKPKNKESEVDNNAAKD O74843 SIF1_SCHPO MOD_RES 35; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 134; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1235.06; CHAIN 1..257; /note="Sad1-interacting factor 1"; /id="PRO_0000097757" MSTASEQARLRRERRLNKIKQGGASRINQILGQNSDDSQSDVRATASEEAVHSETATPVTPMSSGFMEKRDDTFNADQVEYLPSQDYHNLESSPFKLQCDSPYNVPPENMFNQNPDFANFFQAMLQSAKEGSDTNFQGENEQIPQATAPLKNLVEKYAHLLAISIVVIVCYFKHLPLLPWTFTVEACLFSIQFVLDRNNGPSYSLLASLASQLPPPYGAMIRHTTSYVPYFTQLITDACMTIFALGLCCYFYPSLVY O74845 HIF2_SCHPO MOD_RES 137; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1235.09; CHAIN 1..564; /note="Set3 complex subunit hif2"; /id="PRO_0000303899" MDTNQVNYIIWRYLKECGYSHTKFAFERETGIQNLDKQWGSTCQVGALVEILQKGLQYVELEKHYVDNHSSNEEASKTSIDGESLVNENPCKLPFYLTVPHICETTLTKADSTNGFCEHNNSNDHQLKILQDKGSGSPSSPVMPFKDKIEKRDIDITMADESNVEKDPARPIAVYNSSPVTEITEIKQVTFTGGEDIKSDFFKVIPTKHPVTCADWRPLLQENYHVYEFSIGMTNATLASVSICEEQNDFKAKTDYCLQSSFDNQDITGVAWNNSGSFLAYAFFSGVIEIYDSHGSQILSFHNNKGPVLSLKWSGTDTYLAAGSADGTITLFDQLKQTQYSIDTLASSVLDIEWISFDEFVTSDVEGSLRVYKVDGKAPVSTVSHAHDNSIVALRYNLRISLLLTASSDTTVKLWSRGDAGAFECLHVFSFSSPVNCIDWNLREGTPILAVASNSIVSMYNAISLQQLAVFMRHTAPVSALSFSHNGRYLATGDTSGGVCIWSCKTAKLFKELGSDNSELIAVTNVLPEEQVNFLRWSFDDKDLLIGKQKKEIICCCDFLHDSL O74849 GHT6_SCHPO SPCC1235.13; CHAIN 1..535; /note="High-affinity fructose transporter ght6"; /id="PRO_0000050414" CARBOHYD 359; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAKILTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRYADRYDPVTDTYSYSSARQGLLVGMVNTGTTVGCLLSSPLGDRFGKRKCIMGWTLVYITGVIVQLTTIPSWVQMMVAKIWTGLGIGALSVIAPGYQSESSPPHIRGAIVTTYQLFITLGIFIAACINMGTHKYTTHPEAQWRVPIGINLLWGILMFFGMLFLPESPRYLAVKGRNEECMKILTRNAGLPADHPIMQKEYNAIQADVEAELAGGPCSWPQIFSNEIRYRTLLGMGVMAFQQLTGNNYFFYYGTQVFRGTGLNSPFLAALILDAVNFGCTFGAIFVLEYFGRRGPLIVGGVWQSICFFIYASVGDRALTRPNGTSNHRAGAVMIVFSCLFIFSFAQTWAPAAYVIVGESYPIRYRSKCAAVATASNWFWNFMISFFTPFISNSIGFKYGYVFAACNLCAAIIIFLFAKETKGLTLEEINQLYLSNIKPWNTGAYQRDREDIKQSDSEKERGPTSKLHEYVEHAPNSYASTHSTESENYPQQVTNPVGL O74853 FAP1H_SCHPO MOD_RES 33; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC18.03; CHAIN 1..1077; /note="FKBP12-associated protein 1 homolog"; /id="PRO_0000317322" METSKNPSDLPKKPANVKKNRRRFQKSQKKSISPSSGSELPNFKTTISQNNEEVKTSLKEDSSKFHPSASAPIFVPTSSVQLNVSKNNGHKASDIVDAVSSKDEELRKHAKGEGKRSKNRKRSSKHSEKQAVDLKSSNSSQETSSSKGSVNNKSERSREAKSRMPKNSKEIKKGLDLSKLDMTSRMIVELKNRLYECSVCTDTINPSTSIWSCGTCYHVFHLSCIRKWCKNSIEQRNEDAWRCPYCQSNQTETSLHYLCWCGKQEKPEFVKNLVPHSCGDPCGKTRGQDCEHPCPLLCHPGPCPPCTATVEKFCLCGKESIHARCSNISKVNTEPFRCENVCDELLPCGEHTCKKRCHSGLCGACFEPINAKCYCGLHSKTYPCSSLPSPSISKKDENGSVKEWFGYYSCNNPCTLFFDCGLHKCSKTCHPISETRAHCPFATDVLTKCPCGKEDISFLLKGHERKSCSDPIPTCENICGKLLSCGHRCKYKCHLGSCGTCSETLTIPCRCTANEVQVTCEQLQNGFIPTCERLCTILLSCGRHQCNKKCCSGYSKAQTRLARRPKGAKLRYHLLTEEFEEEHICFRPCNKKLSCGNHFCQHMCHRGPCPRCLEASFEELPCTCGRTRLYPPVACGTPIPDCPYLCVLPKSCHHPQVKHNCHPTSEPCPPCPYFVKKRCLCGKHILENQPCYRENVRCGELCNKLLSCKTHFCEKLCHPDGECESSCKKECGKRRMYCEHVCQSPCHAGHPCDERIPCKAPLEVSCECGRIRKKVTCDASYDNPDPQHKVSCTLECSQQQRNKLFAEALNIKTDRRSNDVAQYTKSLLVFYGKHSDFADEVESLLRNFVNNKASSFRFPSMRREQRAFVHMFAKLLGLESVSFDPEPKRNVMVYNKGEAKLPNMLLKEANLYHLQHPEIPLKPDSLLGPEEENATASHIDGSSNASDSGYNAFVLKELLKEVNDESAIFSVLDDIVDFNHLTWSILFGENYIILKPLNTDLIVNKTGKLVALRPLVNRRLADAGIASRCEICEINDKNEIVKTRSQRIHSKKKAFLSLVPDKSIGVINRYKELATEL O74861 SDC1_SCHPO SPCC18.11c; CHAIN 1..109; /note="Set1 complex component sdc1"; /id="PRO_0000114685" MSNSAPARQYLNEKVTPVLLEGMKILARDRPENPLQFLGQFLLDANANQQKQKEIVNQPEPQQETPKADADMSTPTMAEQVQTSFSNPASTPLTQTSSPSSNPGKNSAS O74878 ALG11_SCHPO CATALYTIC ACTIVITY: Reaction=an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + 2 GDP-alpha-D-mannose = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523, Rhea:RHEA-COMP:19515, Rhea:RHEA-COMP:19516, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511, ChEBI:CHEBI:132515; EC=2.4.1.131; Evidence={ECO:0000269|PubMed:11015724}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29524; Evidence={ECO:0000269|PubMed:11015724}; SPCC330.08; CHAIN 1..471; /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase"; /id="PRO_0000080278" MITTLAIALFIAVVAIHSHIRRKICKEIGIRLIKKIAPVKASLYKQVGVEPKLARTVGFFHPYCNAGGGGERVLWTAVKSVQTEFPNVISVVYTGDNVSKAEILRRVKNTFEIDLDSSKIVFVYLKLRFLVSATTWHRFTLLGQSLGSMILGFEAIYRFAPDIFIDTMGYAFTFCVVKSFQNIPVGAYVHYPTISTDMLKSLKQVSLLAKVKMAYWRWFAQLYSDAGSHADYVMTNSSWTRNHIASLWGKDIQLSVVFPPCNTSELEKIDINRKREPTLLYLAQYRPEKNHENVLRSFALYFEQHPDSPAKLLLVGSVRGEEDMCFVNHLKTLATELNLQSKVKFVVDAPWPKVVEYLGTCSIGVNYMWNEHFGIGVVEYMAAGLIPVVNNSGGPKFDIVIPWIGKPTGFHASTISEYAEAYHKALTLSPQEQLEMRINARSACARFGEHVFMRDFGNVFAKLLREDYSRT O74885 XANA_SCHPO BINDING 183; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P37610"; BINDING 185; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P37610"; BINDING 228; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250|UniProtKB:P37610"; BINDING 362; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250|UniProtKB:P37610"; BINDING 377; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P37610"; BINDING 389; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250|UniProtKB:P37610" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + xanthine = CO2 + succinate + urate; Xref=Rhea:RHEA:43120, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:30031; EC=1.14.11.48; Evidence={ECO:0000269|PubMed:15948966}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43121; Evidence={ECO:0000269|PubMed:15948966}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P37610}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610}; SPCC576.01c; CHAIN 1..413; /note="Alpha-ketoglutarate-dependent xanthine dioxygenase xan1"; /id="PRO_0000194021" MSATATTTVVEPPTTTLTGATEPPFTAYTTSQGLRVSPVPLPEHNTDVGFGALIENVDLNNLSDEQFEDIRKALFEHQVVCFPNQHNLPPETQYAITHRFDPESSTYGHGNRTNQQNNSILHPDLHTLPGVPQVQLIGHGVVKDHYGLEEVRLKHPHHRTFHRDPISEEEEKEKQVTRFYRWHIDAALYDYNPPVVTTLLAVNAPQGTQTLRYDDKSGHEMPVPLGSTAFASGYRMYELLTDEEKKVAARTRVQYFPHAYVTINKARALPNGLGMYSEGLELDKSELPPWEESRVKTFPLLWKNPVTGKLALQTHGCCAEKILIDNEDGTTTVIDDLPKVREILYNYQRPGINPERVYCHDWKNGDFVIFHNRGVTHCITGAYRDDQTRIFHQCNLAASHPPAGPSEEDIAAM O74890 SYYM_SCHPO BINDING 33; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 37; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 77; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 184; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 188; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 191; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 210; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"; BINDING 248; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P83453" CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; Evidence={ECO:0000250|UniProtKB:Q9Y2Z4}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:P48527, ECO:0000255" SPCC576.06c; CHAIN ?..445; /note="Tyrosine--tRNA ligase, mitochondrial"; /id="PRO_0000314632" MSRLLACLKQLQARSLIHNTTLLQPSCNVNSVYLGADPTAASLHVGNLVALMPLVHFFLNGFPVFTVIGDATAQLGDPSGRSTSRKQMAETTRTANSNSIHNQLKDLSSSILSYAQDCNYPFSQMPSSSQWSIVRNSSWYENLKLLKFLSSVGPHVRVSQMLARDSVTTRLQSPSGLSFAELTYQLLQAYDYSYLYENHSVNLQIGGSDQWGNITAGTDLVRRTHPNANVYALTTPLLTSSSGQKLGKSAGNAIWLDPKLTDSYSLYQYFISAPDDLACKCLDMLTLLPLEQLEQIKAEHEKDPSQRIVHKYLASNVVRMVHGKKALELAQIQTKLLHGAHQAPFGFYSEAPQQGDSFPSLPEIRALFKDCKFYRTIDSSIKDQPFSRLLRTLQIYTSRKEATEHILSGAVSLGHKPILDSNYKFPDNSLFVLRAGKRTFVLDSL O74895 RL15A_SCHPO SPCC576.11; STRAND 14..16; /evidence="ECO:0007829|PDB:8EUP"; STRAND 35..41; /evidence="ECO:0007829|PDB:8EUY"; STRAND 59..67; /evidence="ECO:0007829|PDB:8EUY"; STRAND 113..123; /evidence="ECO:0007829|PDB:8EUY"; STRAND 125..135; /evidence="ECO:0007829|PDB:8EUY"; STRAND 176..178; /evidence="ECO:0007829|PDB:8EUY"; STRAND 194..197; /evidence="ECO:0007829|PDB:8EUY" HELIX 4..10; /evidence="ECO:0007829|PDB:8EUY"; HELIX 17..32; /evidence="ECO:0007829|PDB:8EUY"; HELIX 45..50; /evidence="ECO:0007829|PDB:8EUY"; HELIX 98..109; /evidence="ECO:0007829|PDB:8EUY"; HELIX 140..143; /evidence="ECO:0007829|PDB:8EUY"; HELIX 149..152; /evidence="ECO:0007829|PDB:8EUY"; HELIX 154..156; /evidence="ECO:0007829|PDB:8EUY"; HELIX 159..161; /evidence="ECO:0007829|PDB:8EUY"; HELIX 166..171; /evidence="ECO:0007829|PDB:8EUY"; HELIX 190..193; /evidence="ECO:0007829|PDB:8EUY" TURN 110..112; /evidence="ECO:0007829|PDB:8EUY"; TURN 146..148; /evidence="ECO:0007829|PDB:8EUY" CHAIN 2..201; /note="Large ribosomal subunit protein eL15A"; /id="PRO_0000127564" MGAYKYLEELAKKKQSDVNLFLSRVRAWEYRQMNVIHRASRPSRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGQTYGKPVHQGVNHLKYQRSARCTAEERVGRYCSNLRVLNSYWVNQDATYKFFEVILVDPSHKAIRRDPRINWIVNPVHKHRESRGLTSIGKKSRGIGKGHRFNNSPQHATWLRHNTLSLRRYR O74896 CENPX_SCHPO SPCC576.12c; CHAIN 1..89; /note="Inner kinetochore subunit mhf2"; /id="PRO_0000372347" MEQESELLSLNTLARILTLYFSSEKGTKITPSALELITQYLRIYSKEAVCRAYEEKKNSIMSSSENEDIVLELEDLENGIAAQLALDFS O74914 HSP31_SCHPO ACT_SITE 139; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 140; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 173; /evidence="ECO:0000250|UniProtKB:Q04432" CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000269|PubMed:24758716}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for methylglyoxal {ECO:0000269|PubMed:24758716}; Note=kcat is 31.1 min(-1) with methylglyoxal as substrate. {ECO:0000269|PubMed:24758716}; SPCC757.03c; CHAIN 1..244; /note="Glutathione-independent glyoxalase hsp3101"; /id="PRO_0000317306" MASEGKVLLVASSYYGPFYPDGMNTGVHFAELLIPYQVFREAGYEVQLTSETGKCKFDDHSIKKSALGEVERDAFDNKDNEFWYALKDIKPADKINYKEFCIMFIAGGHAAMFDLPHATNLQTLAQQIYASNGVLAAVCHGPVMLPFVDDTKSPEGRSVVYGKKVTAFNSTGELVMGVSSALRERNMQDLNSLFREAGAEFVDPPTPMSDFTQVDGRIVTGVNPMSAKSTAEAAIKVSQSLRKT O74918 RRP45_SCHPO SPCC757.08; CHAIN 1..291; /note="Exosome complex component rrp45"; /id="PRO_0000139973" MSRHLETSLNNKEFVLNSLEKGLRLDGRQLSDFRSLEIQFGKEYGQVDVSFGHTRVMARITTEITKPYTDRPFDGIFSITTELTPLAYSAFEAGRVSDQEIVISRLIEKAVRRSNALDTESLCIISGQKCWHVRASVHFINHDGNLVDAACIAVIAALCHFRRPELTVVGEEVTVHPVEERVPVPLSILHMPICVTFSFFNNGELAIVDATLEEEDLCNGSMTITLNKNREVCQIYKAGGIIIDPSKIISCAKTAFDIAVSVCSVIQQALDEDLRKKETQYLGGSAENERS O74922 AMY1_SCHPO ACT_SITE 229; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P56271"; ACT_SITE 253; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P56271" BINDING 105; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 143; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 185; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P56271"; BINDING 198; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P56271"; BINDING 227; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 229; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 232..233; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 253; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 322; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 370; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3" CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P0C1B3}; Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. {ECO:0000250|UniProtKB:P0C1B3}; SIGNAL 1..22; /evidence="ECO:0000255" SPCC757.12; PROPEP 604..625; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000374016" CHAIN 23..603; /note="Alpha-amylase 1"; /id="PRO_0000374015" CARBOHYD 153; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 163; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 180; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 241; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 260; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 286; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 331; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 440; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 461; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 51..59; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 172..187; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 263..306; /evidence="ECO:0000250|UniProtKB:P56271" LIPID 603; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MGFSKIALFSLFALFGLPTSLAKSSEEWRDRIIYQVITDRFAVDSDNTPDCSFDDSSYCGGTWSGIRSKLDYIQGMGFNAIWISPVEKNLEGSYGSDGEAYHGYWNTDFTQLNEHFGSEDDLIDLITDMHNRDMWIMFDALANSMAIPGPTDNISYSNLVPFNDSSYFHPYCWIDYGSNNNTDIEDCWTGDDNVILADLDIESTNVADYLHEHIHDMVERYQIDGIRIDAVKQMNPEFFPNYTSAAGVFAIGEMFSYDPNVSCSVRNYLDSITSYPIRQGIEFAFNYTGAAFEYLQEIDTQFQQACEGQDMSVIGNFLENHDLPRYTSITNDTSQDIGAIVFLLLHTGIPIIYYGEEQRLPGGSDTPENRAALWNYGYDTDANYYQTIRTAIALRKQAISDSDSWTTDSHSYLDYDLRHAVVRKGDVLGVYTNYESSSDNVTYDVSSNFDDGTVLREVLSNTTTTVGSSGALHVTVVSGLPQVYYPEASLTSFGNFLGTATSYSSASASYPSTSMSASLSSVHTSSATSSSKSSSSSSSRSGSSSSSSSRSGSTSSSGSSHTITSTSQSVHTSGSSTSTSSVAVTSTAYSSSSSSSSSSSIESSANAVRVSILGVAAFIAIVLFI O74925 PEP3_SCHPO SPCC790.02; CHAIN 1..900; /note="Vacuolar membrane protein pep3"; /id="PRO_0000055992" MSLAEDWIDPNSSEDSDIQEDAELEYTADNPEKEQRGVFSLEKVQLQFPVSIRCLAVENNILVMALTSDKLMIVDLERPEDIIDIELPKKVLALGLTYKIFLDPSGHYIFVTTTAGDNCLFTPSHQGRVLTKLKGHTVEAVQWNLNGGNILELLIASKSGVLLELVLTLDSANLKRIEKSINTLYSFPFMESPMGILKNIQDDSMTIVTNKRILRFEPKTSRGKDQLYFSPAFQGSMKEILSFSEEETAQCFSYSPFPKNLAEPYTLALKTSKRIIYLDIMNPVNPDIQDYEFNESPKLSVPTVEMNMILTSFHLAFLDLDTLYIVNRVNGKESYQQRVNLSPHEEILGLCCDHEKNTYWLYTTDSLHELVVNNETREASLVFLEKGDFEKALECANTAKVRNTVLVGYAEFLMEHEEYERAATLYAETLKSVEEVALKFIELNQKDVLRLYLWKKLRSYKSTMKIQKSLLVNWLLELMLAKLNSLDEKERLELFPENVMQQRQQVQREFSTLLNQYKDEINREAAYNLANNYGKEEQLLQIATVMKDQSYIMHYWVQRENYEKALETLNEGVSQETLIQHATALLTHRPNETVSIWERQTDLDVHALIPSLLSYNQRSHVPVEENAAIRYLRYVTGVLGCVDPSIHNTLFCIYACHSSSNESYLMNYIEQQGNHPLYDMDLGIRLCLQFNCRRSAVKILVLMKLYSQGVELALEADDCELAATIANIPEEDVVLKKTLWQTIAKYMFSKKSGIKETLRFLENSEVLQLPELIRLLPEDIKLDDLSDNVCDELDHCMKRIEQLDFEIGQASEVAHEIQTNAENMRNRYIVLEPNESCWHCNQPLFSEPFVLFPCQHAFHRSCMLEKTYKLASEKNILKECQLCGPSYAVRLINEPFSTDF O74927 MTHR2_SCHPO ACT_SITE 20; /note="Proton donor/acceptor"; /evidence="ECO:0000250" BINDING 20..25; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 52..53; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 52..53; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 81; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 111..113; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 113; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 153; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 172; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 179; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 190; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.53; Evidence={ECO:0000250|UniProtKB:P53128}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; SPAC343.10; CHAIN 1..641; /note="Methylenetetrahydrofolate reductase 2"; /id="PRO_0000190254" MKIVDLIDKIPNGNAFYSFEYFPPKTTVGLENLSSRITRMSRNMMPLFSSVTWGTAGSTAEVSIYLAKMLEQHHKIPACLHLTCTNVDKAIIDKALETAKEYGIRNILALRGDPPLNSDHWEGKVSEFEHAVDLVRYIREKYGDYFCIGVAAYPEGHVDSNVPELSKDPLRDIPFLIEKVEAGADFIITQIFYEPEAFIKFENFVRNHSSNALRNIPIIPAIMPIQSYGSLKRMTRLCGCSVPSSLMQRLNAAKPDDEAIKNIGVEHIVDMIKKIMDNVQGRVHGFHFCTLNLERSVALILKNSGLLTKRWKQVESEMEDEKLLRTTRKRLSLDEPAELHNQVVVPSQQPVADKSSNLFVTSKQSSVSGHKDNLTEEAPFSVSEGSGVLGRQANWDDFTNGRFGDPRSPAYGEIDGYGPTLHFPPSEALKLWGYPVDESDITSLFQKHIMSDISAIPWIDEPVEVETKTIAKYLLKLNGNSWWTVGSQPAVNGAPSADPVFGWGPKGGRVFQKAFVECFVNGKDLKDFITKWHDNPQVTYYAGNNKSEFLTNAPKDGASAVTWGVYPGREIIQSTIIAEVSFKAWLSESFQVWGEWANLYSKNTPSRKLLENCINDRWLVTVIHHDFMDKNGLWKVLEIDF O74928 PUR9_SCHPO ACT_SITE 133; /note="Proton donor/acceptor; for FAICAR cyclization activity"; /evidence="ECO:0000250|UniProtKB:P31939"; ACT_SITE 260; /note="Proton acceptor; for AICAR formyltransferase activity"; /evidence="ECO:0000250|UniProtKB:P31939" BINDING 30..33; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 60..63; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 97..98; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 121..122; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 200..201; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 260; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 308; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 331; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 423; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 443; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 444; /ligand="(6R)-10-formyltetrahydrofolate"; /ligand_id="ChEBI:CHEBI:195366"; /evidence="ECO:0000250|UniProtKB:P31335"; BINDING 534; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P31939"; BINDING 539; /ligand="(6R)-10-formyltetrahydrofolate"; /ligand_id="ChEBI:CHEBI:195366"; /evidence="ECO:0000250|UniProtKB:P31335"; BINDING 558..559; /ligand="(6R)-10-formyltetrahydrofolate"; /ligand_id="ChEBI:CHEBI:195366"; /evidence="ECO:0000250|UniProtKB:P31335"; BINDING 581; /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide"; /ligand_id="ChEBI:CHEBI:58475"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P31939" CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; Evidence={ECO:0000250|UniProtKB:P54113}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; Evidence={ECO:0000250|UniProtKB:P54113}; SPCPB16A4.03c; CHAIN 1..585; /note="Bifunctional purine biosynthesis protein ade10"; /id="PRO_0000192158" MYALLSVYDKTGLLELAKALTSKGVKLLGSGGTAKMIRESGMEVADVSSITNAPEILGGRVKTLHPAVHGGILARDIPSDEKDLVEQSIEKIDIVVCNLYPFRETIAKPNVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPADYATFTDKFLSDKLTQDDRNTYALKAFASTASYDAAITDYFRKQYAAGVDQLTLRYGANPHQSPAQAFMEQGPLPFKVLCGSPGYINLMDALNSWPLVKELRENIGIPAAASFKHVSPAGAAVGLPLSDVEKKVYFVSDITEFTPLACAYARARGADRMSSFGDFIALSDTVDVCTARIISREVSDGVIAPGYEPEALELLKKKKGGKYCVLQMDPKYVPAEIETRQVYGISLQQHRNHAKIDFSLFEKVVSKNKDLPKSALIDLVIATTALKYTQSNSVCYAKNGMVVGLGAGQQSRIHCNRLAGDKADNWWLRHHPKVLGMQFKKSAKRPEKSNAIDLYVLDAVPAEGSEREQWESAFETIPEPLTKKEREEFLATCKDVVCASDAFFPFPDNIYRLAQSGVKYVAAPGGSVMDQAVRDTANEFNMVFSEIPLRLFHH O74946 DPOA2_SCHPO PTM: Phosphorylated in a cell cycle-dependent manner. {ECO:0000250}. SPCC553.09c; CHAIN 1..574; /note="DNA polymerase alpha subunit B"; /id="PRO_0000194040" MEFPIDDEELLDERNKLLQICNMDEQTMFYKWESWCLQRGNTPKLDLDTFKAFAKDMKFQMERQVKATLKQNPERKSIKQIPGMNIDSILGLPVKTTASGDSLMQESKPSTETFELNSSDAGRVLEVLNKELKIVTSKPSAPSKLVIVANFDLKAFNYRIMYQKLYDSSEVLDDRIELFSALTCRKYNISDEDLANPSELTQEPVVVVGRIVVESTNLGGRLNQNSILLESSRRLGAGVRVRLKVDDLPSYSIFPGQIVSVKGSNPSGNMFIAKEILPIPPLPFPSSSKQEHATFVANTNNQPISIYIASGPWSLRDDLSFSPLKSMISYVNKNPVDLVILCGPFLDINHILIRTGNITGTSATSLEELFKERVTPILSQLTCPCILIPHINDAASDHPAWPQDAFNRVALGLPSNFKCFPNPCMFSINDVVFGVSTNDILLHTSREELFRLPSHGNLFARLVSHVLHQRHFYPLFPGGSLEKCNPSNLDIAHLKLGEFLNTMPDILILPSDLRYFVKNVENVVSLNPGKATKGINLGTFAKLTIAPLELGDNGSSNHYSHRVWLRTKAEILKL O74960 PIL1_SCHPO PTM: Phosphorylated by ksg1 and ppk21. Phosphorylation is regulated by sphingolipid long chain bases (LCBs) (By similarity). {ECO:0000250|UniProtKB:P53252, ECO:0000305}. MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 15; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 39; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P53252"; MOD_RES 230; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 233; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC736.15; CHAIN 1..351; /note="Probable sphingolipid long chain base-responsive protein pil1"; /id="PRO_0000308182" MMNRAYSLRNSRAPTASQLLNPPPPSSSTRSGRLFAPLSHTMRINHAATFTPDLAKRLAVLVKMEKNVMRSMEVTIRGRRDCARQLSYWGEDCDDDISDVTDKLGVLFYEMAELENYLIDRYDQYRMTLKSIRNIESSVQPSREKKQKLLDQIYALKHKDPESPRLVTMEQELVREEAACLVAEAQLSNTTREKFKQAMTFNLDALHEHAEKLNLIATYGRHLLNLIDDTPVTPGEARPAYDGYETSRQIVMDAEHALSSWVPSQPAVNFVKPQIEDDAQSDARSWNEYEAQGEPVPVEQVTHLQDDVQSDTSEIIENEPGMHPHVHAERMSRIASESSDAVPQQTAVQVA O74962 PANK_SCHPO CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33; Evidence={ECO:0000250|UniProtKB:Q8K4K6}; MOD_RES 80; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 84; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4B4.01c; CHAIN 1..403; /note="Pantothenate kinase"; /id="PRO_0000316854" MSETECGRFSTISRETISNVERQLSQPPSVWLNLTGARIIENEGQFDKDIALPNNKSHVTHIAVDIGGSLAKVMYYVCESSSPSSSSSSISEAENYTGGRLSFMIFETAKIEDCIQFMANLIDNHVKNCNKKKITLIATGGGAYKFYDRMSKQLDIKVIREDEMECLIMGLNYFVSCIPREVFVLDLDTCELTFQNHLNCYHYPHMLVNIGSGVSILKVTGPSQFERIGGSSLGGGTLWGLLSLLTPANSFDEMLELSKGGDNTSVDMLVGDIYGKDIGYERFGLKSTTIASSFGKVFRERKPLEEFAPQDISRSLLLAISNNIGQIAYLHAQKHNVQNIYFGGSFIRNHVQTMHTLTYAIQYWSNHTMNAYFLRHEGYLGVFGAFMKYATSQPSNVPVPSIS O74964 RSC1_SCHPO MOD_RES 168; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 331; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4B4.03; CHAIN 1..803; /note="Chromatin structure-remodeling complex subunit rsc1"; /id="PRO_0000211210" MSSKIRPSADDKKLQRVLYFFLERVRAAKDVSGQLLSPLIDNASVDTASVSPSSNGRPTTLKSIQSKIDEFQYHDFSEFVSDLAYLFINVKALYEGTQTYSFVQALEEFCIQQLRTFQQQGYIPVITWPNTDSPSATTSSPISRNPEYSVSPPNGSKFVKNEDEAYDSDLYVEEEDSDVKGRSMVGRDGRYKSEDLKRRKLQPSSKPLSSLEARAKVIMRQVRRYRDGSGRQLFAPFERLPDPRMFPEYYQAIEQPMALEVIQKKLSKHRYETIEQFVDDFNLMFDNAKSFNDPSSQVYRDADFLKNYLADVLRLEAGKLDSEFFNYETDSRASPQLPKNDIQPAVSIDGTLLNVGDWVLIRNPADSSKPIVSQIYRIWKSDDDINYVTVCWYLRPEQTVHRADAVFYENEVFKTSLYRDHPVSEIVGRCFVMYITRYIRGRPKGIRSTPVFVCESRYNDDTKQFSKIKSWKACMPQEVSGSEYEMILFDRPITLTKVASPLLHLLASKSQGLPSPATTDSNTHMLPSQGSLLPPSSISETKSFSTKASTPLSTDDIATPLSSAPNPPSVMPTYARKTSSHSERSSHSSYHNSSHVPTAAFNSPIMRTSTKSTSPIPARPFYAQSGSLQSLNTTQHSHQISGGHSGRMNVPYAKLSYTSHNGRHGGSNGNISGAKTPMTNYTINSMPSLPVFPPAFIVPGTHQKLDESSPVPGIDDVTVINTETAKMLDKDEHQNVLWYTVPPLDPIPLENRNGSLTHSVEYVLYKKSKGSQVITEKARSNELSREAKFENLVASLSDALIPP O74969 GHT2_SCHPO MOD_RES 507; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 515; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 519; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 520; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 523; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4B4.08; CHAIN 1..531; /note="High-affinity glucose transporter ght2"; /id="PRO_0000050410" CARBOHYD 361; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGFKRGKNFTLVMLIFVSMAGWMFGADTGSIGGVTSMRDFRERYADRYDPITDQYSLSSARQGLLTGMVNVGSLFGCIISSPIADRFGKRLSIIGFCAVYIIGIIVQVTAVPSWVQIMVAKIWTGIGIGALSVLAPGYQSETAPPSIRGTVVVTYQLFVTGGIFIAACINMGTHKLHKTAQWRVSIGINLLWGIITMIGILFLPESPRYLIQVGKDEEAVRVLSESAELFPDSEEVQNEYHRLKSSIDEEFAGGPCSWASIFGKDIRYRTFLGMFVMSLQQLTGNNYFFYYGFSVMQGAGINSPYLSAMILDAVNFGCTFGGMYVLERFGRRNPLIIGGIWQSICFFIYSAVGSRALYHKNGTSNTRAGAVMIVMACLFIFGFAQTWAPAAYVIVGESYPVRYRSKCAAVATASNWLWNFLISFFTPFIQASIGFKYGYVFASCNLTGAIVIFLFAKETKGLTLEEINELYMSVIKPWESGNFKLNYSEQKKVEKEKSRKGGARGESVEYVERASNTDSSPQYSSHEEDYA O74976 FAT2_SCHPO BINDING 168..179; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P69451" CATALYTIC ACTIVITY: Reaction=ATP + CoA + oxalate = AMP + diphosphate + oxalyl-CoA; Xref=Rhea:RHEA:18293, ChEBI:CHEBI:30616, ChEBI:CHEBI:30623, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57388, ChEBI:CHEBI:456215; EC=6.2.1.8; Evidence={ECO:0000250|UniProtKB:P38137}; MOD_RES 283; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 284; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1827.03c; CHAIN 1..512; /note="Oxalate--CoA ligase"; /id="PRO_0000193183" MSFTTLYSAIQGDASARALVAPSLNAELSFSELRIAIMDLQRQIASLGIKVGDPVNIAIPNGLEFVVAFYAVSWQRAICGPLNSNYKQSEFEFYIDDLKSKLVIVPEGSVAANTPAVRAAKKLSVAVAELAWCPKSRLVRIVHFEGAKINAPQPLGLPQPDDVMLVLHTSGTTGRPKVVPLTHKNLCRSIHNITTSYRLDPRDTSYVVMPLFHVHGLLCGLLSTLASGGCAVVPPKFSAHSFWKEFIQYGATWYTAVPTIHQILLRTPPPKPLPRIRFIRSCSSPLAPPVLSKLEATFRAPVLEAYAMTEASHQMTTNPLPPLVHKPHSVGKPFGVELKILDQKGNEMPQGKEGEICVRGINVTKGYLNNPAANKSSFTKDRFFRTGDEGKLDKDGYVFITGRIKELVNRGGEKISPAEIDAVLMQHPDVSEAVCFAVPDEKYGQDIQAAINPVAGKTVTPKQLHDYLEQKVAAFKIPKKFYFTDRIPKTATGKVQRRLVCDAFFNHSKAKL O74977 VMS1_SCHPO ACT_SITE 249; /evidence="ECO:0000255|PROSITE-ProRule:PRU01389" MOD_RES 38; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1827.04; CHAIN 1..600; /note="tRNA endonuclease vms1"; /id="PRO_0000310323" MGDISKHNIFSLPEDILAKLELREEYSVEEKTDSANLSNQGDIVDSTQKNISSCVNCQIDNLHTLDERKSHIKSDWHRFNTKRKITKLPPVSQDEFESIIEDLPESLSGSESETNSESEEDNFQIEKAFKQSLNIGKVDSADENNNQRTNSPLTWFQLSNASAEVPTYIGVYKHMFSGNNHITKDLLVQQQNHNRQKPLQLAMFMVGGGHFAAMIASNEFNPRDPHVPKVLAQKTIHRYTTRRKQGGSQGAADNTKGNIHSAGSGLRRYNEQALIKDIQQVFKDWGKLLETCDLIFVRAIGSSNRSIFFSQPGALISPKDPKLRVFPFTTKRATHSELLRCYKELVTPKISHVDSISIKAQEEERKRQAEIEKEIRQSRLQEEERKKKKLAKYTEVIISNLKASNIEAFLEYLRSNDLSINFQFYPKNVHLHTSTPLHYAVTQKNAKLVAKLLRNGADPAMLNGNGKTPFEISTGNKEVKDEFLIARHELGESFFDWEAAKVGAPQSREQIQKQRQKAKTKLENQRRDKERQEELRRKEAMQKIEEQSKRDYDKLHGEGHSLGINNVRKVDELQSLSPEMRMRIEREKRAAAAMKRMQTK O74995 TFH47_SCHPO MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1682.07; CHAIN 1..421; /note="General transcription and DNA repair factor IIH subunit ssl1"; /id="PRO_0000046856" MNENQKSFDSDKSESEDEQKNGRVKVRSRKTDDNEGYTWEGEYQRSWDIVQEDAEGSLVGVIAGLIQSGKRKRLLRDTTPLQRGIIRHMVLVLDLSNSMEERDFHHKRFDLQIKYASEFVLEFFEQNPISQLSIIGVMDGIAHRITDLHGNPQSHIQKLKSLRDCSGNFSLQNALEMARASLSHIASHGTREVLIIFGSILSSDPGDIFKTIDALVHDSIRVRIVGLAAEVAICKEICNKTNSSTKNAYGVVISEQHFRELLLESTIPPATDSAKTTDASLVMMGFPSKVVEQLPSLCACHSIPSRGGFHCPRCKAKVCTLPIECPSCSLVLILSTHLARSYHHLFPLKNWSEIPWSANPKSTHCFACQLPFPKPPVSPFDESTSSMRYACPSCKNHFCLDCDVFAHEQLHECYGCQCSGN O75004 CDC24_SCHPO SPAC8F11.07c; CHAIN 1..501; /note="Cell division control protein 24"; /id="PRO_0000089445" MDFPGLIKKIKEDLENRLVEKSKQPAFTDYWLINKTISLLKEYPSGFSYPILINEIELACSERNKLDNVFSSLEWLTKSDAVIYLEDQFHFHCYDYYYTPIPSLKLKDSEENTCEMILHSSFYLLFHEPFNILKGSTLRFSQSRIHQKWYLRKQIRFLPTTSFVPVLQYAASKSFVKSMVESTEHEFFQIRDITISKSDQGVKRITVELGRIISLDKKGAFLIDNNTNFIHFSGTYHDFPKLLDKQQYLLIPFWSTVWEGSTNWQDGMIGILVILSENDFEEKKCDSWQVGRLAAVNSNFLVLDNNGQRVKILYSNSQKHYFKDTYIGDLLCISPINHSSDNLSDYSCVSDTTTEILSNLENPLSSNFLRNDLCKFSNLFSGVSGHLKIQPLTLVITGFVANLTRQSDLNTSLVLPEVNPLTAKMEVIDCLRNSFWAALRPNCVSYFASMISGFKELFQKEMEFPIYLDLKSYKLGFHWCDIYVDSEHNCHIQKINSLPCE O94247 HCS1_SCHPO BINDING 232..239; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPCC737.07c; CHAIN 1..660; /note="DNA polymerase alpha-associated DNA helicase A"; /id="PRO_0000353816" MSSSNEQICLDEDWIQKFGDREIEFVDEAQKSEVDETEKSIKRFPLSVLQRKGLALINLRIGVVKTGFGGKTIIDFEKDPAFSNGEELPANSFSPGDVVSIRQDFQSSKKKRPNETDISVEGVVTRVHERHISVALKSEEDIPSSVTRLSVVKLVNRVTYERMRHTMLEFKRSIPEYRNSLFYTLIGRKKADVSIDQKLIGDIKYFNKELNASQKKAVKFSIAVKELSLIHGPPGTGKTHTLVEIIQQLVLRNKRILVCGASNLAVDNIVDRLSSSGIPMVRLGHPARLLPSILDHSLDVLSRTGDNGDVIRGISEDIDVCLSKITKTKNGRERREIYKNIRELRKDYRKYEAKTVANIVSASKVVFCTLHGAGSRQLKGQRFDAVIIDEASQALEPQCWIPLLGMNKVILAGDHMQLSPNVQSKRPYISMFERLVKSQGDLVKCFLNIQYRMHELISKFPSDTFYDSKLVPAEEVKKRLLMDLENVEETELTDSPIYFYDTLGNYQEDDRSEDMQNFYQDSKSNHWEAQIVSYHISGLLEAGLEAKDIAVVTPYNAQVALIRQLLKEKGIEVEMGSVDKVQGREKEAIIFSLVRSNDVREVGFLAEKRRLNVAITRPKRHLCVIGDSNTVKWASEFFHQWVDFLEENAIVMDIDATMFE O94248 MDN1_SCHPO BINDING 159..166; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 474..481; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 901..908; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 1193..1200; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 1566..1573; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 1876..1883; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 593; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC737.08; CHAIN 1..4717; /note="Midasin"; /id="PRO_0000363386" MDVLIEWVAIYPQIYDILEHINYVPSNTLQRLRLHQPWSKIDYDVWFLYASDEIRETCKVKYYGETKTYGEVFVLENERISQLHRLFVSWTVSERAEHLKNLLFDAGLSNLPLVELGGNVFFNSHVPLPCSLVLTKSTQENLNRITPYLVQKRPILLAGPEGIGKKFLITQIAAKLGQQIIRIHLSDSTDPKMLIGTYTSPKPGEFEWQPGVLTQAVITGKWILFTNIEHAPSEVLSVLLPLLEKRQLVIPSRGETIYAKGSFQMFATSSMKTKILGQRLWQILDLTYQPDECVEVVSTLYPVLSIICPTLYSVYKDIFDLFSQRSFLATSKIYRRLCLRDFYKFIKRVAFLYHKFMIPSDHVVISQELQDAVFKEAIDMFGAFIPSRDGFDLVVRNVAIELNIPPEKALQLRYSIPVFQNLEHNINIGRCSLKKLSTIRSCSTNSYAFTSSSLGLLEQLAAGVQTNEPLLLVGETGTGKTTTIQLLAGLLGQKVTVINMSQQTESSDMLGGYKPINASTLGLPLHERFIDIFEQTFSSKKNAKFISMASTSARRFRWKTCLKIWKEACKLSKTVLDGQQPLPNPQKRQKRLSNQVELRNQWAKFEKEVEDFEKVLTGGSNGFMFSFVEGALVKAVRSGHWVLLDEINLASLETLEPIGQLLSSYESGILLSERGDITPITPHKNFRLFGCMNPSTDVGKRELEPSFRSRFTEIYVHSPDQNLDDLLSIIQKYIGSLCIGNEHVIREVAELYQVAKSLSLDGSLVDGAGQRPHYTVRTLSRTLSYVTEIAPIYGLRRSLYEGFCMSFLTLLDHTSESLLYNHVVRFTLGELNRDQQNAILKQIPKVPDHSSYIAFCHYWLRRGSFPVEEQEHYIITPFVQKNLLNIARACSTRMFPILIQGPTSSGKTSMIEYVAKKTGHKFVRINNHEHTDLQEYIGTYVTDDNGSLSFREGVLVEALRNGYWIVLDELNLAPTDVLEALNRLLDDNRELFIPETQVLVKPHPEFMLFATQNPPGVYAGRKHLSRAFRNRFLEIHFDDIPENELETILHKRCKIAPSYAAKIVQVFRELSLRRQTTRIFEQKNSFATLRDLFRWAFREAVGYQQLAENGYMLLAERARDQKDKLAVQEVIEKVMKVKIDTDGIYNLDSMEIFQDMSLKEGPLSKVVWTRPMIRLFCLVWRCLLAKEPVLLVGDTGCGKTTVCQILAECLHKELHIINAHQDTENGDIIGAQRPVRNRSAVNYSLHSQLCEKFNVQESLDSIDDLIEKFEKLSSSEKNDNLSNLIERQIIKYRSLFEWHDGALVTAMKQGDFFLLDEISLADDSVLERLNSVLELSRTLTLVEHSNAAVSLTAKDGFAFFATMNPGGDYGKKELSPALRNRFTEIWVPPMVDTEDILKIVEGKLHNNKIELARPLVEYAKWHANEYLYTDVISIRDVLSAVEFINACEILDLNLVLFNAVSMVFIDALGSFTTFSLSNNLASLHAERQRCFAKLNELAGSNIMASKSADISIKFSDSSFFIGDFGIPLGDSVESDSTYSLHTDTTLMNASKVLRALQVLKPILLEGSPGVGKTSLITALARETGHQLVRINLSDQTDLMDLFGSDVPVEGGEGGQFAWRDAPFLAAMRNGHWVLLDELNLASQSVLEGLNACLDHRNEAYIPELDKVFKAHPNFRVFAAQNPQHQGGGRKGLPRSFINRFSVVYVEALKEKDMIEIAACNYHQVNEDWRLKIIKFMFRLQDNIEKDISFGSFGSPWEFNLRDTLRWLQLLNDAPKYTCVSPADYLEVMVLHRMRTVEDRVRTCELFKEVFDIDYEPRTIGFSLSSQCFKVGHSLLVRDVERQKTLLDSQNILQSQLPVLESVITCINKKWPCILVGDTATGKTCILRLLAAIAGAKIKEMAVNSDTDTMDLIGEYEQIDISRKASELFTDLSQQLLNIVIKYRNFDNIFRETSLYTLTTTSFKTHSQAFTLLQKVVDQLDQLKIHETLVHSLGDIHEKARKLLAEFSASPAGRFEWFDGYLLKAVEEGHWFVLDNANLCSPAVLDRLNSLLEHKGVLIVNEKTTEDGHPKTIKPHPNFRLFLTVNPVYGELSRAMRNRGVEIFLLKEALTEIDKKQMSLLEPAPISSAVDTLASNISYIKYVFETMGKIEIDGNYMYIAHAIILALFSPRQLKLLRKVLLTNPQFSLSIKADAELLLTLKNLVQKIYCADYFNHMDLKASRFMDIYEYPVQLREVVGLIQTINDFQSVILTSHLELPETYASGLLFVSAHEILDLTEEVNRLAVSTSNSTYLLKSASAVYHNVSSFKGSTPSLWNLLNQFSKFLIEIASANSNIVYKLSYDVIRHFLKLVVLWKNIYVWTNVPDCDISRFYCYTKMLGEWMFTLTEKTKLLESFLPKDSLEKFSELQNLSTGLHMQAIWDKWHAFVPRTYDQWSLWNTVDKLLTQYVNANIPSISMETTACEVVGTSLSLLNKVLVENEVGDIYSYLKILGKGVNELKSSKQVILPENLVNLFNCLASLDLLHIFIKYTTSSFFLTDDFVRFIRVCFHSRISGNLLTLLHGISFDSTKAVAPVLTYFDFCSLTTGNILGRIALAFTSIDENANLESANIFEHARLALLQHFMDHSSLLAEDSSTKMNLILLQRYAVIISIFLDQGKCEKANDLITKLSLPYEELAENFVSILEACKAFLVANSEFISYTYTERFIHSLRFLKDSWLSSNQQKMLKNQGMAYIYFASGMLLVYVPDKPFDPALLPLLTVESLRHYLESLYKESQILEIAESLNSGKVNSVMRRLVSTEISNTPNIDSSFSTVYRSLNESIVPLYSELEFFMKSVVLNQYIFELAMRLSKESNIAVVEEAKSFVTKWKAYIERIREAYPQFVDVYELILSFISFMIYGIELLMFEAKRRLDERSQILSTLILTLVDPSSFARSLSFDDVSNLIEQIKVLDLNDSIRFEIYLFLASRLCSEKQHSSDTHSLANSFVLLANEFYIHNAKIKQKELEEIEEKNRLYRQREFNFDKNDYLKVFINYDDEVEPEVEPEVVIERKRFLQLQFAFWSLYNEIYSEKMNVIPLEQLMNTGSYLAKKIKVKNPDMIASSGFDIVSVVLMMGVKSTNERQYWTPPVYNFYSDPNPSKAIEVRDLIKIVESRAISLIKNWPENFVLRGLKDAIDAILNLSPFSPIAEYLSKLERVFHLLSEWEKLASREYSLANEMDLIKKKIIDWRKFELSNWNNLLKLEEYKLSERVYPRLYSILQFIILKPFFENSKFTKQNLCESASIIVQFITDLTVGEFQLCLKCLLSFSQHAASLRICHGIDAMLLNIYHYFEQFLSKVSEAIHTQKQSLENSIKERILLMSWKDTNVYALKESAKKSHAELFKVLHRYREVLRQPVSSYLSQKHDWDSLLDTENNSAMWVAKKVNLSPSYIEKMDTEIMKLVPVRFSNTPTTLRLMWTLFANVEKPGSTFTNMVSNLITDARELMKLTPETINDDNLSEIKHLKSRKHLLLTETFKTLKAFGLQYRVKAGIEENLSNLRNLLAVIPTFPVTSLSIEKVDRSLMKSLDFIPKFQTLAGHQHNDLSVPEVQKGVGLFNSMLSLQLGERAQLVEFTNELLALKNVYSEVGVNGSPLESFNNSSFNEVSSLGYDHDFENRAQAVSMLCQIYAIVIQKHSSISPTASFQSIGHELSRFADLLSNKLFPSSIPLYASADKVSSIRDQQKGINDLIEYCRKKRTELPELSYCFKHLVSLQSLKSISRTQVDLTNDEFLNLMNFVLNLFDSLLSSIETATKNMRTFKELAETSSFIEMSSCFSKVLRAFNLKFQSMKLSSLKEKLRSSSVDKMSCQLLMLFLPVCEQFINLAESVLDYFINVHNSNLDSLSKISTLFFMVANNGFCSPDLPQEGKSNSGELESGTGLGSGVGAEDITNTLNEDDDLEELANEEDTANQSDLDESEARELESDMNGVTKDSVVSENENSDSEEENQDLDEEVNDIPEDLSNSLNEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDHLDLPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFEDPLEENNTLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNHPKMDAKSTFASAEADEENTDKGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREWQQANRIHEWEDLTESQSQAFDDSEFMHVKEDEEEDLQALGNAEKDQIKSIDRDESANQNPDSMNSTNIAEDEADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEKVFELSEDEDIEDELPDYNVKITNLPAAMPIDEARDLWNKHEDSTKQLSIELCEQLRLILEPTLATKMQGDFRTGKRLNMKRIIPYIASQFKKDKIWMRRVKPSKRTYQVMISIDDSKSMSESGSTVLALETLALVTKALSLLEVGQIAVMKFGEQPELLHPFDKQFSSESGVQMFSHFTFEQSNTNVLALADASMKCFNYANTASHHRSNSDIRQLEIIISDGICEDHDSIRKLLRRAQEEKVMIVFVILDNVNTQKKSSILDIKKVYYDTKEDGTMDLKIQPYIDEFAFDYYLVVRNIEELPQLLSSALRQWFQQMSNT O94251 POP7_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; SPBP8B7.01c; CHAIN 1..102; /note="Ribonucleases P/MRP protein subunit POP7"; /id="PRO_0000304053" MSVERIKRAPAFRKGIIIRRKTHLIAMIRRMRKKLDIDGSILYQATGMAIPHLVELSDKYKRQGYNISMDTATVEFMDEIVDEVSIQNKNRLGNVLLLRVSR O94258 XPOT_SCHPO SPBP8B7.09c; STRAND 36..38; /evidence="ECO:0007829|PDB:3ICQ"; STRAND 161..163; /evidence="ECO:0007829|PDB:3ICQ"; STRAND 393..395; /evidence="ECO:0007829|PDB:3ICQ"; STRAND 401..404; /evidence="ECO:0007829|PDB:3IBV"; STRAND 481..483; /evidence="ECO:0007829|PDB:3IBV"; STRAND 571..573; /evidence="ECO:0007829|PDB:3IBV" HELIX 2..14; /evidence="ECO:0007829|PDB:3IBV"; HELIX 20..35; /evidence="ECO:0007829|PDB:3IBV"; HELIX 39..46; /evidence="ECO:0007829|PDB:3IBV"; HELIX 55..71; /evidence="ECO:0007829|PDB:3IBV"; HELIX 78..94; /evidence="ECO:0007829|PDB:3IBV"; HELIX 103..119; /evidence="ECO:0007829|PDB:3IBV"; HELIX 127..138; /evidence="ECO:0007829|PDB:3IBV"; HELIX 141..158; /evidence="ECO:0007829|PDB:3IBV"; HELIX 167..183; /evidence="ECO:0007829|PDB:3IBV"; HELIX 185..201; /evidence="ECO:0007829|PDB:3IBV"; HELIX 205..218; /evidence="ECO:0007829|PDB:3IBV"; HELIX 224..228; /evidence="ECO:0007829|PDB:3IBV"; HELIX 230..239; /evidence="ECO:0007829|PDB:3IBV"; HELIX 243..258; /evidence="ECO:0007829|PDB:3IBV"; HELIX 263..279; /evidence="ECO:0007829|PDB:3IBV"; HELIX 289..310; /evidence="ECO:0007829|PDB:3IBV"; HELIX 318..330; /evidence="ECO:0007829|PDB:3IBV"; HELIX 332..339; /evidence="ECO:0007829|PDB:3IBV"; HELIX 344..348; /evidence="ECO:0007829|PDB:3IBV"; HELIX 351..364; /evidence="ECO:0007829|PDB:3IBV"; HELIX 372..387; /evidence="ECO:0007829|PDB:3IBV"; HELIX 406..426; /evidence="ECO:0007829|PDB:3IBV"; HELIX 428..446; /evidence="ECO:0007829|PDB:3IBV"; HELIX 451..467; /evidence="ECO:0007829|PDB:3IBV"; HELIX 475..477; /evidence="ECO:0007829|PDB:3IBV"; HELIX 488..498; /evidence="ECO:0007829|PDB:3IBV"; HELIX 507..519; /evidence="ECO:0007829|PDB:3IBV"; HELIX 521..525; /evidence="ECO:0007829|PDB:3IBV"; HELIX 528..530; /evidence="ECO:0007829|PDB:3ICQ"; HELIX 531..538; /evidence="ECO:0007829|PDB:3IBV"; HELIX 552..565; /evidence="ECO:0007829|PDB:3IBV"; HELIX 574..580; /evidence="ECO:0007829|PDB:3IBV"; HELIX 581..585; /evidence="ECO:0007829|PDB:3IBV"; HELIX 602..607; /evidence="ECO:0007829|PDB:3IBV"; HELIX 611..627; /evidence="ECO:0007829|PDB:3IBV"; HELIX 632..654; /evidence="ECO:0007829|PDB:3IBV"; HELIX 663..679; /evidence="ECO:0007829|PDB:3IBV"; HELIX 691..708; /evidence="ECO:0007829|PDB:3IBV"; HELIX 713..726; /evidence="ECO:0007829|PDB:3IBV"; HELIX 731..734; /evidence="ECO:0007829|PDB:3IBV"; HELIX 738..748; /evidence="ECO:0007829|PDB:3IBV"; HELIX 754..767; /evidence="ECO:0007829|PDB:3IBV"; HELIX 773..790; /evidence="ECO:0007829|PDB:3IBV"; HELIX 800..820; /evidence="ECO:0007829|PDB:3IBV"; HELIX 825..828; /evidence="ECO:0007829|PDB:3IBV"; HELIX 830..833; /evidence="ECO:0007829|PDB:3IBV"; HELIX 836..846; /evidence="ECO:0007829|PDB:3IBV"; HELIX 854..868; /evidence="ECO:0007829|PDB:3IBV"; HELIX 879..892; /evidence="ECO:0007829|PDB:3IBV"; HELIX 893..895; /evidence="ECO:0007829|PDB:3IBV"; HELIX 908..934; /evidence="ECO:0007829|PDB:3IBV"; HELIX 946..952; /evidence="ECO:0007829|PDB:3IBV"; HELIX 971..974; /evidence="ECO:0007829|PDB:3IBV" TURN 50..52; /evidence="ECO:0007829|PDB:3IBV"; TURN 74..76; /evidence="ECO:0007829|PDB:3IBV"; TURN 120..123; /evidence="ECO:0007829|PDB:3IBV"; TURN 219..221; /evidence="ECO:0007829|PDB:3IBV"; TURN 365..367; /evidence="ECO:0007829|PDB:3ICQ"; TURN 468..471; /evidence="ECO:0007829|PDB:3IBV"; TURN 501..503; /evidence="ECO:0007829|PDB:3IBV"; TURN 541..545; /evidence="ECO:0007829|PDB:3IBV"; TURN 549..551; /evidence="ECO:0007829|PDB:3IBV"; TURN 566..569; /evidence="ECO:0007829|PDB:3IBV"; TURN 608..610; /evidence="ECO:0007829|PDB:3IBV"; TURN 727..730; /evidence="ECO:0007829|PDB:3IBV"; TURN 735..737; /evidence="ECO:0007829|PDB:3IBV"; TURN 751..753; /evidence="ECO:0007829|PDB:3IBV"; TURN 768..771; /evidence="ECO:0007829|PDB:3IBV"; TURN 873..875; /evidence="ECO:0007829|PDB:3ICQ"; TURN 935..938; /evidence="ECO:0007829|PDB:3IBV" CHAIN 1..978; /note="Exportin-T"; /id="PRO_0000343105" MSAQDVENAVEAALDPSVGPIIKQQATDFIGSLRSSSTGWKICHEIFSEKTKYKPSTRLICLQTLSEKVREWNNESNLLELQMIRDSVWSYIKELSFLDEPAYISNAVQHLLTLLFLQLYPSNWNDFFASLQGVIAASSQSEFSNFYLKVLLSIGDEIADSLVLKTDVQIQKDNLVKDAIRANDMSDIVSFVYEMMLAYSNAKNYGTVGLCLQVYAQWVSWININLIVNEPCMNLLYSFLQIEELRCAACETMTEIVNKKMKPLEKLNLLNILNLNLFFSKSQEQSTDPNFDEHVAKLINAQGVELVAIKSDPSELSPELKENCSFQLYNLFPYLIRYLSDDYDETSTAVFPFLSDLLVSLRKESSSKELSASLKEFLKSLLEAIIKKMKYDESQEWDDDPDSEEEAEFQEMRKKLKIFQDTINSIDSSLFSSYMYSAITSSLSTAATLSPENSWQLIEFALYETYIFGEGLRGPDAFFNEVDKSPTVLSQILALVTTSQVCRHPHPLVQLLYMEILVRYASFFDYESAAIPALIEYFVGPRGIHNTNERVRPRAWYLFYRFVKSIKKQVVNYTESSLAMLGDLLNISVSPVTDMDAPVPTLNSSIRNSDFNSQLYLFETVGVLISSGNLTPEEQALYCDSLINALIGKANAALSSDLSALENIISVYCSLMAIGNFAKGFPARGSEEVAWLASFNKASDEIFLILDRMGFNEDIRGAVRFTSGRIINVVGPDMLPKVPQLISILLNSIDMNELVDVLSFISQLIHIYKDNMMEITNRMLPTLLMRIFSSLSAAPQGTDDAVKQNDLRKSYISFILQLLNKGFGSILFTEENQVYFDPLINSILHFANLVGEPATQKSSIALVSKMVSLWGGKDGIAGFENFTLSLTPLCFEMPVNPNFNTRDGQSLVVLGELAGLQKIILEKLGDIYKSYLVTVYFPTVNFPDVMASEYLQALSNLDSRSFKQFFQKFIQALKSGNV O94261 CENPH_SCHPO SPBP8B7.12c; CHAIN 1..220; /note="Inner kinetochore subunit fta3"; /id="PRO_0000290639" MDNNDQISNLCLGALQLLADQPISVISNEPSEEQRNEHVLKKWENNVLRHWKILFSLFMQTCGDSVQGNAAFSILNFMTTNSLVGQLYQRLYDESNSLGFISSPLNETEHLSEENLKIESSITFTSEEIEKEKENIKSVLLPSVQSISSSLELYASKESDYRSSIEGVLADLKLARARWEIVRNVTQILLLESGISFLENKKLAYIMDLCGDREDNYSSY O94263 DPB2_SCHPO SPBP8B7.14c; CHAIN 1..594; /note="DNA polymerase epsilon subunit B"; /id="PRO_0000071571" MNNSITDSVEKKPEQVSFEVQPNALRPVAFHVFTRKYDLNINRDSLQELASFVSKKCGSQWRSQCEPLLDEIAKTWKRVHETQPIVTRPLLIPVLANLNVPHEVRVSSLARVQTLETTGSFLNSSNSEIRETIKNEKYFRVLDAFKMPKFKYDSSRKVFVLSKQSPTLMASASACTDMLNRRFNVVYSRILRNESFQTPSFSGSFSQTGTYQLTPIRNLLGRAGNTFLLFGLLTIAPDGTLWLEDLDSQVQLDVSQAEQGFGLFCPGCLVLVNGQFLSSGLFLVFELGHPPIERRDASLKALNNLDILGLNMDAKQLALLRHAEQAYQSQAFVCISEVHLDNHQTFYALEKIFQKYESSEAVPFCIILCGSFMSSAFHNSGSSIQYKEGFNKLAASLEKFPKICEKTKFIFVPGPNDPWTTNGISLMPKHSIPLHFVNRIQRVCKHTIFASNPCRIIFFSQEVLIYRDDISGRFQRNSLKFGKTPQGTSNINSIPLAEQQVHQQRKLVKTVLDQSHLSPFPSRTRPILWDFDYALSVFPLPSCMGLIDSESSAFDVHYGGCPTFNPGALLLGVHYNWQEVFPVKKEIITHKERI O94265 THI21_SCHPO BINDING 43; /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"; /ligand_id="ChEBI:CHEBI:16892"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+); Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:Q08224}; CATALYTIC ACTIVITY: Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP; Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7; Evidence={ECO:0000250|UniProtKB:Q08224}; SPBP8B7.17c; CHAIN 1..506; /note="Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1"; /id="PRO_0000315972" MISTCITVAGSDCSGGAGVQADLKVFTAHSVYGMSAVTAITSQNTIGVNGVHLIPASYVEQQISACLLDVHCEVMKTGMLFNQQILKVIVESIDRFKIKKVVVDPLIATRKGALLVMPDYLELFVKELIPRAEVLIPNIAEALIILKHMTNEFVEIHHLEDVKAVGKKLIKAGCKNVVIRCDDIPFASDFFCSRETNMPPTWYLYVLCTSEGEVLLPQKWLASKTARGTSCALSSAVASNLAIGLDLVTATQNAVSYTQRALEMSFHLGRGANSLDYASALTRLPYEKGEFINFVRYHPSITPKWLSIVNHPFVEQLKAGTLSRLPFQKYLVLKYHMLINNAQAAGMMAFSSSSISAIEHSAKIIQAIKEENVTHLRICEQYGLSASQITKSKPEIVKSHSLFIHDTAQQDGLRGIQIAMLPFVFMIQEVVSQISASDGYPYVAWVEHCKDKSATSHIETLLESLETNSQIISLSKVQHLLGILEKSLDFERLVLDTSSSNESSVF O94268 NOP2_SCHPO ACT_SITE 473; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" BINDING 347..353; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 371; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 398; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 416; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" CATALYTIC ACTIVITY: Reaction=a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:47780, Rhea:RHEA-COMP:11911, Rhea:RHEA-COMP:11912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000250|UniProtKB:P40991}; MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP8B7.20c; CHAIN 1..608; /note="25S rRNA (cytosine-C(5))-methyltransferase nop2"; /id="PRO_0000317149" MGRKQKSKQGIPPTLEENHNSSHKVTENAKKRKHSKEKPQNSRKRQLAEEKKSLFENSDSENEKDLIDADEFEEAETLSDLEHDEEPQTFADEFIDDEAKECEGEEEDSVFDSDEEHEVKPMFSDDSGDEEDLELANMEAMSRKLDEEAELEEKEAEEELHTNIHPEAPTVLPPIDGFTDSQPISTLPQDLSQIQLRIQEIVRVLNDFKNLCEPGRNRSEYVDQLLNDICAYYGYSRFLAEKLFELFSVSEAVEFFEANEMPRPVTIRTNTLKTQRRELAQALINRGVNLEPIGKWSKVGLQVFESQVPIGATPEYLAGHYILQAASSFLPVMALAPQPNERILDMSSAPGGKVTYVAALQKNTGIIFANDSNKARTKALSANIHRLGVRNAIVCNYDGRKFPNEVIGGFDRVLLDAPCSGTGVIYKDQSVKTNKSERDFDTLSHLQRQLLLSAIDSVNADSKTGGFIVYSTCSITVDEDEAVIQYALKKRPNVKLVSTGLEFGREGFTRFREKRFHPSLKLTRRYYPHVHNIDGFFVAKLKKISDKIPTVNVADDMKDGTNNDVEIEKNSTEIDNITFNDEADKEIIEQNRRKWLKSKGYKVAKKKD O94269 UBP3_SCHPO ACT_SITE 142; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 453; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPBP8B7.21; CHAIN 1..512; /note="Probable ubiquitin carboxyl-terminal hydrolase 3"; /id="PRO_0000080604" MRDLTSATDSASLESDSSRNQFIINSLLPWYSCSEHEFPHRKARKRRSPKNLDWSVSVQMPLVTSKTKESEKSPKSWSAIAKKHVQGDSPVKKSHSVPVPSDRSEKKSFNSSLGELIETYSPSLDAPRPIQPRGFINTGNICFMNSILQALMYCVPFYNLLKQINRMVPYNFERTTPLIESLTMLSRDFREYSEKFDLQGDSILPEVVYSATKGNPRFEMLQTGEQEDAEEFLNLFLDELHEEFVRERRHYLLKNDERNPKSDIKISNGIKSGLDSFDDQSSVEASGWTEVGKNKKPVIARSATVERSPISQIFGGQLRSTLRVPSARDSVLLEPFQPLQLDIQAEDIHSVIDALEHMTAPEILPEWHSSKGNVTATKQMYIESLPPVLILHLKRFFYEASGGTQKNYKPIAYPARLSIPQNVFSPSVRGSIHPEYDLNAVVYHHGTSASGGHYTVDVQQLDKSGWFRIDDTHIHRVPIHDVENSELSADPSLSKLGHGDRVAYLLFYTRRS O94273 PPIB_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SIGNAL 1..19; /evidence="ECO:0000255" SPBP8B7.25; CHAIN 20..201; /note="Peptidyl-prolyl cis-trans isomerase B"; /id="PRO_0000233050" CARBOHYD 131; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKLFYFSLLFTLFFGLISANRGPKVTDTVYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGEKGFGYEGSIFHRVIPNFMIQGGDITKGDGTGGKSIYGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKIIKSGQLSQENVEDDGTDEL O94275 MUG30_SCHPO ACT_SITE 775; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; SPBP8B7.27; CHAIN 1..807; /note="Probable E3 ubiquitin-protein ligase mug30"; /id="PRO_0000300502" MSRPIEIANVSSGNRRTLPALHGSSFSSRSELDNNTNSKISRRLRELVCQRMGENPLRLRQSFHETISNDSYGNSEKLVIRPCICCNSVLRYPAQAMCFRCSLCMTVNDVYFCLSGSQIKTKASTDGSQFISVEHFVETIHQTRSALQLAKQRTGNVQAIVAAGLPLRELISLVFGSPPILNKLFSVKNGCSIQSSGLNYKLIYQLYHDITNLDILITNELLRAIESLLRRPMLYCHDPADYQYLLILLENPLLNSKSKNIVNKSSSILKRILGVLSNLNEKTHHFFISCFKKQPYNNPKFFRRKVDLINKFIGQRLMETYSRNKRKHYYNNDWQIKSAAITMALLYSANSQMRLIDRSSFYCIMADFINLYHDFELWEQKINCFCFCQYPFLLSMGAKISILQLDARRKMEIKAREAFFSSILSKMNVEPYLMIRVRRDRLLEDSLRQINDRNKDFRKALKVEFLGEEGIDAGGLKREWLLLLTRKVFSPEFGLFVNCEESSNYLWFNYSHRSKEIDYYHMSGILMGIAIHNSINLDVQMPRAFYKKLLQLPLSFNDLDDFQPSLYRGLKELLLFEGDVKNTYGLNFTINLKAVEGFRTVELKEGGSELSVDNENRKEYVLRYVDYLLNTTVKKQFSAFFDGFMKVCGGNAISLFQDNEISKLIRGSEEVIDWELLKNVCVYDFYDQNAISNSISESEPSMTASKYLCHSFVSKRKIILWFWDLISHYSLKMQKLFLIFVTGSDRIPATGAHNFQLRISVLGPDSDQLPISHTCFNHLCIWEYSSREKLKKKLDTALLETNGFNIR O94277 ADCS_SCHPO ACT_SITE 88; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 177; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 179; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85; SPBP8B7.29; CHAIN 1..718; /note="Putative aminodeoxychorismate synthase"; /id="PRO_0000310363" MSEISNRLQILLIDCYDSYTFNLYDLLYKASENACVIVVHWDKMSPDLWEDILQFDAIVVGPGPGHPAEYSSILNRIWQLNIPVMGICLGFQSLALYHGATIERMPNLPWHGRVSSVTTSKTFIFDGISAVKGMRYHSLYANKIPIDSLQILAQSDEDNIVMSIKATKFPHFGILYHPESVGSSKSLKIFKNFLSLADTPNIQCVNSFSKSANGFSHNLNRYDISPAAFILKSGSPSLQIHSVEIPWVEPLALADCIQKSGNPICFLDSAKKPGRYSILGILTGPLARIIHYEKATNTTEIRICKDNSFVRINNDLWSTVADFMNQHKAIKPDTNLPFYGGIMGIIGYECSDLSTKSVSNASFPLDFQQTTVDAELAFVDRSFVFDLEIKKLFVQTLTPLNETCSEWWGELLASTCNTKLDNLSCLHSFDGKQNFGLVQSFPKKEVYCESVKACQEHLLAGDSYEMCLTDTTFVSAPPELSDFEMYMRARSLNPATFAGFVRLNHFTLLCCSPERFLQFRDDRCLFSPIKGTLKREGHMSLEEARKKLLNEKDMGELNMIIDLIRNDLHQLAKKNSVHVPELYSVEEHSNVYSLLSNIYGRIESPITAWDVLSKSFPPGSMTGAPKLRSVRMLEPLEQHGRGIYSGTLGYWDVTGSAEFNVIIRSAFKYKADDYWRIGAGGAVTILSSPEGEYEEMVLKANSILPAFVNLKNKKRSCK O94283 ERV41_SCHPO MOD_RES 317; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 319; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2G5.04c; CHAIN 1..333; /note="ER-derived vesicles protein 41"; /id="PRO_0000337254" CARBOHYD 187; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLRSRVPANIRAFDAFPKFSKEYRRQSSSRGGFFTILLSVLIVVLVFSQCVQYIRGIREQELFIYDSVSELMDLNIDITIAMPCSNLRIDVVDRTKDLVLATEALTLEEAFIKDMPTSSTIYKNDRYAGLRWARTEKFRKKNNAEPGSGTACRIYGQLVVNRVNGQLHITAPGWGYGRSNIPFHSLNFTHYIEELSFGEYYPALVNALDGHYGHANDHPFAFQYYLSVLPTSYKSSFRSFETNQYSLTENSVVRQLGFGSLPPGIFIDYDLEPLAVRVVDKHPNVASTLLRILAISGGLITVASWIERVYSSRAHRSTSEADMLGLLGKSETE O94285 RPC8_SCHPO SPBC2G5.07c; STRAND 2..13; /evidence="ECO:0007829|PDB:3AYH"; STRAND 37..39; /evidence="ECO:0007829|PDB:3AYH"; STRAND 43..54; /evidence="ECO:0007829|PDB:3AYH"; STRAND 66..77; /evidence="ECO:0007829|PDB:3AYH"; STRAND 84..93; /evidence="ECO:0007829|PDB:3AYH"; STRAND 96..100; /evidence="ECO:0007829|PDB:3AYH"; STRAND 107..110; /evidence="ECO:0007829|PDB:3AYH"; STRAND 118..121; /evidence="ECO:0007829|PDB:3AYH"; STRAND 126..131; /evidence="ECO:0007829|PDB:3AYH"; STRAND 140..143; /evidence="ECO:0007829|PDB:3AYH"; STRAND 149..159; /evidence="ECO:0007829|PDB:3AYH"; STRAND 184..191; /evidence="ECO:0007829|PDB:3AYH" HELIX 15..17; /evidence="ECO:0007829|PDB:3AYH"; HELIX 22..34; /evidence="ECO:0007829|PDB:3AYH"; HELIX 111..113; /evidence="ECO:0007829|PDB:3AYH"; HELIX 122..124; /evidence="ECO:0007829|PDB:3AYH"; HELIX 199..202; /evidence="ECO:0007829|PDB:3AYH" TURN 40..42; /evidence="ECO:0007829|PDB:3AYH"; TURN 61..63; /evidence="ECO:0007829|PDB:3AYH" CHAIN 1..203; /note="DNA-directed RNA polymerase III subunit rpc8"; /id="PRO_0000362999" MFLLSRFSDIISIHPSNFWKPTKEALAEEIHKKYANKVIQNIGLAICVYDFLKIGEGIIKYGDGSSYMNVVFRLIIFRPFRGEVMLGKIKSCSEEGIRVTISFFDDIFIPKDMLFDPCVFRPDERAWVWKIEGEDGSEGTELYFDIDEEIRFQIESEDFVDISPKRNKNATAITGTEALESVSPYTLIASCSRDGLGIPAWWK O94286 MTND_SCHPO BINDING 82; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /ligand_note="for iron-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 82; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_note="for nickel-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 84; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /ligand_note="for iron-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 84; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_note="for nickel-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 88; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /ligand_note="for iron-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 88; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_note="for nickel-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 127; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /ligand_note="for iron-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154"; BINDING 127; /ligand="Ni(2+)"; /ligand_id="ChEBI:CHEBI:49786"; /ligand_note="for nickel-dependent acireductone dioxygenase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03154" CATALYTIC ACTIVITY: Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+); Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252; EC=1.13.11.54; Evidence={ECO:0000255|HAMAP-Rule:MF_03154}; CATALYTIC ACTIVITY: Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+); Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016, ChEBI:CHEBI:49252; EC=1.13.11.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03154}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03154}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000255|HAMAP-Rule:MF_03154}; Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate. {ECO:0000255|HAMAP-Rule:MF_03154}; MOD_RES 157; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC887.01; CHAIN 1..178; /note="Acireductone dioxygenase"; /id="PRO_0000315971" MRAYIFQDEGDQRKPNDSKIEVSAEDLEAAKVSYRHHDGDLHTFADGLMKEYGFKNRDEVVVSRKGLGDRYDNMVKKFFEEHLHEDEEIRLILDGNGYFDVRSVDDRWVRIFVEKGDLIILPPGIYHRFTTTTDDYIHAMRLFHENPKWIALSRTDSTSEELDARKSYLNSIKKSVYV O94289 LUB1_SCHPO SPBC887.04c; CHAIN 1..718; /note="Ubiquitin homeostasis protein lub1"; /id="PRO_0000051070" MTSYELSRELGGHKQDVRGVCSISNELIGSASRDGTYSVWEQINGEWTPHFYENHEGFVNCVCYVPAIDKNSRGYIFSGGQDKCGILQEVGTNSPSYYLFGHESNICSASALNSETIITGSWDSTARVWALGQCKYVLKGHQSSVWAVLALGEDIFITGSADKLIKIWNGEKLVKSILAHNDCVRSLCQIPGGFASCSNDGVIKLWTSDGEFLYELHGHTSFVYSLTYIHNQQLIASCGEDRTIRIWKGKECLQCITLPTTSVWSVSSLPNGDLVCGSSDGFVRIFTVDKVRVAPTEVLKNFEERVSQFAISSQEVGDIKKGSLPGLEILSKPGKADGDVVMVRVNNDVEAYQWSQKENEWKKIGQVVDAVGNNRKQLFEGKEYDYVFDVDVADGQAPLKLPYNATENPYQAANRFLELNQLPLSYTDEVVKFIEKNTQGHSLESKKEPNLESQSSNKIKTTIFPVSQLLFSNANVPAMCQRLRSLNNTKSNPLPAKSIDSLERALSSKKITDTEKNELLETCLSILDSWSLAERFPALDALRLLAINSSSDLAPIFLEVFSRVVKSVPSSGNFESINVMLALRGLSNVVPNITDAEGVSKLMDCLTSTVPQASSAKDFKIAFATLAMNLSILLIQLNLENTGIELLSILFSFLDDPSPDNEAFYRALMALGTLCTVPDIALAASQIYHAQSIVHGIAERFSQEMRFVDAEKQILSLF O94290 IST3_SCHPO MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC887.05c; CHAIN 1..217; /note="U2 snRNP component ist3"; /id="PRO_0000342366" MNSIRQIERLNEQELDKPFSSSWHQDYSDSAYIYIGNLDFDLNEDDILCVFSEFGEPVDINLVRDKETGKSKGFAFLKYEDQRSTVLAVDNMTNVKLLDRLVRVDHVASYKVPQKEKEPANLVPLGESGSSLSVSTINTSNLPDHDYKTIIQNEVEQTLSPKDEKDLLDPMRDYIHREKRRKLKHESSDRSDKSDSNRHSRHHRRHSRSRRHRDLDG O94294 SOG2_SCHPO MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 464; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC887.09c; CHAIN 1..886; /note="Leucine-rich repeat-containing protein sog2"; /id="PRO_0000312230" MSAHEVSSTKNSEIERIIKEAEDAGPENALTLDLSHLNLRELPYEQLERIQGRIARLALGHNFIKSIGPEILKFTRLRYLNIRSNVLREFPESLCRLESLEILDISRNKIKQLPESFGALMNLKVLSISKNRLFELPTYIAHMPNLEILKIENNHIVFPPPHIANNDLQDSDMQLFIANIKGYLSRNESVFRTRSESTVSAALSASANLSHSEENDSSVVDSYLFSAPSDTSHAVSPGMLTFVTPSPHSHSPAGHQQSTPKSTLSKTNENSEGTLYDSNVAHGCTHPPSLNQLNKFHLDASPRQARPRRSVSLATGLNSPSVSKPPSSATGPLYHSPQSSLTNSSVASADVQERTHNTNGASPIQDQISEFTDQHQNPSNNDAASTQSILKTAPTQLSASAKTSAISLPEVAKKERNRSNSTNDDYSSTRLPSSVLHRLEALKEARKLSEQLPNRIFAQDPHPSPRLKKEETHENGSNLTNDSVNSYFSNIGGSEVEMKHSAFEKTLESSRGILFSLSQVQQALRQQLLFCSNPVVLDSMRHVLHTANVQIKRLILCFEDTQQSNDGTANINSIVNASLSCISSFRKLIEVTKKFLNELTSRADVRYVRLLLLILFDAAKELQNALVPLSPSQPHSGNNIFADQVRQSPTSMIRTASGLTNRIVSVEKPASVMNPEIDKQIQDQVALATNSAMSVLTLLIDAVPKNNQPDLVNENIAPNLISKLRELGSLSAAACDVTRKLKHRLLTFQTNPEELEWQLFLDDTQAFVKSIIAVANLAKALSSEYTFQKSVLAGLSAATRSTKDLTILLSSSARHYTESSLATPVPLMSPIARVPATPLSAALGSAAQSITSPLIMSPAAIPASAYSTNKIDYFTDADGNVEGLQR O94297 OXSM_SCHPO ACT_SITE 170; /note="For beta-ketoacyl synthase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"; ACT_SITE 311; /note="For beta-ketoacyl synthase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"; ACT_SITE 351; /note="For beta-ketoacyl synthase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; CATALYTIC ACTIVITY: Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; CATALYTIC ACTIVITY: Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000250|UniProtKB:Q9NWU1}; TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC887.13c; CHAIN 19..426; /note="Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial"; /id="PRO_0000310303" MKRVVITGLGAVTPLGNGVKTNWRNLIQGKSGIVSLKGFPEYEQIPSKVAGVIPRGKEKEEWNVLDYVDQGKLREVATFTQLALTSAAEALKDARWIDIDEQEKLATGVCFGTGIGNLDDALNENGVLNKAGIRKVSPRVISKILINMPAGYISQRYGFTALNHTTTTACAAGCHAIGDAFNFIKLGHADVIIAGGSESCINPLTVAGFSKARSLSTKFNDNPKAASRPFDANRDGFVIGEGSAALVLEELEHAKNRNAHIYAEIVGYGLASDSYHITAPNPNGDAAYYAMKRSLKQAGLSASQLDYINAHATSTKLGDVAESIAITRLLCDVNRNPEAFPVSSSKGSIGHLLGAAGAIESVYTVLTVQKGVLPPTLNFEYSDIPQQFQCDYVPNVAKESRINVALSNSFGFGGTNASLCFKKFLQ O94298 SUR2_SCHPO SPBC887.15c; CHAIN 1..293; /note="Sphingolipid C4-hydroxylase sur2"; /id="PRO_0000317336" MVTTVEMLTTWNPVTVSLVSPVIIYWVASAFFGFLHYIELPVFEKYRIHPPEEIARRNRVPQMAVVKAVLFQQLCEVVVGIALAMFEGYPEPIDEAKQMLRYEAFFSKNLPALLQVAPFAPKLAYNFIVPAFQYFFAFFIIDSWQYFWHRYLHYNKKLYNMIHAHHHRLQVPYAMGALYNHPFEGLILDTFGAGVAYLAAGLSPQQAVIFFTLSTLKTVDDHCGYVFPYDPLQMFFANNARYHDLHHQPYGFQKNFSQPFFTFWDHVLGTYMPPKSETPYEKKQKAKNAKKVN O94303 HIS5_SCHPO ACT_SITE 80; /note="For GATase activity"; /evidence="ECO:0000250"; ACT_SITE 189; /note="For GATase activity"; /evidence="ECO:0000250"; ACT_SITE 191; /note="For GATase activity"; /evidence="ECO:0000250"; ACT_SITE 237; /evidence="ECO:0000255"; ACT_SITE 396; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate; Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475, ChEBI:CHEBI:58525; EC=4.3.2.10; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; SPBC418.01c; CHAIN 1..541; /note="Imidazole glycerol phosphate synthase hisHF"; /id="PRO_0000152475" MIVSIVDYGSGNVRSLINAVRYLGFETQWIRNPHDIEKAECLIFPGVGNFGFVCDSLAKQGFLEPLRRYALSGKPFMAVCVGIQALFEGSVEAPHSKGLGVFPGLVQRFDNDDKTVPHIGWNSCAVRSDTSKEFFGMRPHDKFYFVHSYMIPEKGLILPPEFKIATTKYGNETFVGAIVKNNFLATQFHPEKSGSAGLRCLKAFLTGNYEQPISGEASKLIENSFGGLTKRIIACLDVRSNDAGDLVVTKGDQYDVREKSSGSEVRNLGKPVELCQRYFQEGADEVVFLNITSFRNCPMADAPMLQVLEKAAQTVFVPLTVGGGIRDVSDPDGTFHPAVEVAGIYFRSGADKVSIGSDAVYAAEKYYENGKKLSGKTAIETISKAYGNQAVVISVDPKRQYVKVPEDTKHHVVKTSRLGPNGEAYCWYQCTVKGGREYRDIDVVELTRACEAMGAGEVLLNCMDQDGSNAGYDIELVRLVKNSVNIPVIASSGAGIPQHFEEVFKETDCDAALAAGIFHRQTCRIEDVKEYLAIHDVLVRT O94305 MGLL_SCHPO ACT_SITE 99; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P28321"; ACT_SITE 219; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P28321"; ACT_SITE 249; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P28321" CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:P28321}; MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC5E4.05c; CHAIN 1..378; /note="Putative monoglyceride lipase"; /id="PRO_0000312656" MADLYTKDWTDVKDKPVARVVFIHGFGEHVNAYPEFFEALNERNIEVYTFDQRGFGHSRKGGPKKQGCTGGWSLVFPDLDYQILRASDTELPLFLWGHSMGGGLALRYGISGTHRHKLAGVIAQAPMLRCHPDTEPNFLLRKALTLVSKVHPNFLFDSDVQSQHITRDEAVNQRLQDDPLVSSVGSLQVFSDMLNRGTKTIELAPQFFLPLLITHGTDDNVTCSDSSKEFYENAGTKDKTYQSYPGFYHSLHIEKKPEVYEYLDKVAAWIYEHSKPSETVKSEQETAVEHPKPTATTSAPSASPTGVPVEEESHKATSDAVPPAEAKPEPVPASAAERAPTSESTTVPETIVASTTKVISEPAPRVTTAATADIVTNK O94307 PFD5_SCHPO SPBC215.02; CHAIN 1..154; /note="Probable prefoldin subunit 5"; /id="PRO_0000153667" MAEGNKAVDLTSLSLEQLSEVIKQLDSELEYLSTSYGQLGRAQLKFRECLANVNDAVRAENDGKEVLVPLTSSLYVPGKLNLGNSKLLVDIGTGYYVEKSAGEATEYYKRKCEYLASSIENLNNAIDAKSVQIRAVQNIMQQKATATTAATKSS O94308 CSN1_SCHPO SPBC215.03c; CHAIN 1..422; /note="COP9 signalosome complex subunit 1"; /id="PRO_0000120967" MSLNLLVNQEELKRYLDEYGVWSKIFRALFVARNSKPLRSFCVHYAIKELKEKTYNLELYQSLFEEFQDCFENEQLDVEWVESVTFHRKQNLEQLRRELKAYKNNLIRESIRAAQLDLASFFADVGQFDSALRSYAKVREYCTNAGQIAHLSLELMRISIWIGNYSHVLAFGSRAKSTVSAAMELTSPIYAYCGLANFCLGDYEEALAHFLKVETDTSDGIITKTDISVYISLCALACWDHKRLIQELERNEEFNALSDLDPSLRRCLQAKCNRKYSLLLDTLQQNAQDYSLDMYLAPQLTNLFSLIRERSLLDYLIPYSALPFSKIAVDFHIDENFIEKNLLEIIEAKKLNGKVDSLQKRVYIEPSSEPENFEDIKNIAQTSLLYSKALYLQTLAAMNTENTDDEAPVIAQTNITAEDSQN O94318 VPS20_SCHPO SPBC215.14c; CHAIN 2..226; /note="Vacuolar protein sorting-associated protein 20"; /id="PRO_0000362998" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000250" MGVNSSKINDKDRSILSIKEQRDKLLRYSKRLEKIEQLEIDIARKCLRDSDKRGALRALKAKKLYSGLITQTYGQLGNIEQLLSTIEFTLIQKDVMFGLQEGTNLIRQLQADMPLERVGRICNDRDEAMSYVDEVNDMLQGRMSRDQEDEIQEELDSLIREQEDEKVKDLEKPGFTPSTGVDVLPSVPLKNAIPSLDESFPKAASVSNTSSAVVIDEELRKDPVLG O94319 SEC13_SCHPO MOD_RES 29; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC215.15; CHAIN 1..297; /note="Protein transport protein sec13"; /id="PRO_0000295423" MTTVDTQHDDMIHDAILDYYGKRLATCSSDQTIKVFSIENNQQTLLETLRGHSGPVWQLGWAHPKFGTILASASYDGHVIVWRETGGVWSELMDHTAHQASVNAVSWAPHEYGALLACASSDGKVSVLEFKDDGSCDTRIFTAHEPGCNAVCWSPPSLSGSVVGQSPAAGPKKLATAGCDNLVKIWAFDAGVNNWILEDTLAGHVDWTRDVAWAPSVGLTKTYLASASQDKNVFIWTKEGDGPWQKTPLTEEKFPDIAWRVSWSLSGNILAVSCGDNKVYLFKESQNKWQLLNELSN O94320 AATM_SCHPO BINDING 72; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 167; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 220; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 413; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:Q01802}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:Q01802}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:Q01802, ECO:0000305" MOD_RES 284; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPBC725.01; CHAIN ?..437; /note="Aspartate aminotransferase, mitochondrial"; /id="PRO_0000309452" MLARNLRCLHPNTFASLKTNVSYHGVKCLASQSKRGFKVWADVPMGPPDPIFGITEAYKKDGDVKKMNLGAGTYRDDAGKPYVLPSVRQAETELLSQKLDKEYAPITGIPSFRVQATKLAYGDVYESIKDRLVSAQSISGTGALCIAANFLASFYPSKTIYVSDPTWGNHKNVFSRAGLTVKSYKYYDPATRGLDIKGMLSDLTSAPDGSIILLHACAHNPTGVDPTKAQWDDILKTMQKKNHFALLDMAYQGFASGDFARDAYATRLFASSNVPMLLCQSFAKNMGLYGERAGCFSILANDAEEAARIESQTKILIRALYSNPPVNGARIANHILSNPALREQWAGEVVGMSERLKSMRKALRNILEKDLKNKHSWKHITDQIGMFCYTGLNPQQVDVLAKQYHIYLTKNGRISISGLNTSNVRYFAEAINAVTSN O94321 MPR1_SCHPO MOD_RES 221; /note="Phosphohistidine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00110" SPBC725.02; CHAIN 1..295; /note="Multistep phosphorelay regulator 1"; /id="PRO_0000096558" MSVYRDNMYMKYDRNFENRVARRNGQARNASLAKTLHDSGIAERARSPSGSAIPHAYRVMNGSGANDTSLPLTSNPAYVALTSRISSSKSENNQQLAANETAGAPEGTEETVDISNSISDDHANAKNLPAASVKALVGAGVLSDELSVIAYDMSFEDELIQDKQLIDHSVFDQLLEMDDDDEHEFSKSIVWNYFEQAETTIADLQKALEAKDLKKLSSLGHFLKGSSAVLGLTKMRKVCERIQNYGSLRSRDGVMKLPSEEIALDLISKSLSVVNDFYKDARAYLLDFYEKNSST O94324 PPK31_SCHPO ACT_SITE 652; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 534..542; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 557; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC725.06c; CHAIN 1..1032; /note="Serine/threonine-protein kinase ppk31"; /id="PRO_0000256828" MTNPEQLKRILSHEVLLKIEMSKNGIVEYANPAFFELIGYEGDLFQCSFYEYLQSDDEHLMKKATDNLFRKSISVAHVFAFLRCNPIRSPNYYIQQAKAPFEGKTYIRMLFRGILVDSLYGKDTRVLWAGKYLYPQRSVINEMDFILFNTLGIGAFILHDHLLGIIKYNYIHVPPPSGKLCSLCEDNLPEWYFEVHSDFCLVWNDLVRRVFAVQQLINCKKLEIEDIVNKLPTGSNHMVEETFLSLPVITVFNGKKNRKQRFRIRSWRSSLNFLVKELDKSIKNFAYLEHRTFLTISNSAAKDMKREIYEKSLVNWEYDFLVPSKIQDYFYDVHSLLLKNLSSKIKLCNHILMYQATFNEVKNFLQTYSLNMLSIEMENIEGSLYFGNAQLSNLICVNQYLSEQRPVFFNRLLALGNVENNNSIYDDIQKRTERISTIKRHKKYFEIGERLTEKDLIVSKTFKTTRIDYFKAVKGSIEDLDVRPLKNRQKFVNKFYASIVHFLTESMQFPSHNDRRFGDNTPHSLDEFILLKEINRGAYGRVYLAKKRSSGKYFALKMIPKSSLDSLKKIKGLLLEKRNMHIQRYGPNTVKLYYAFDSGDYLCLVMDYFNGGDCETLIQKLGPLPEQWVCQYAAELLNAIELLHQDGIIHHDIKPANMLVDETGHIRLTDFGLSENVEEKKEVYKLTKRMSFEQKHGNLYEQLQPKKFEFVRYVRNYRGNIDELEKAESPQQNSDYANDSVQHLLDFDINNMDETAIHMLMNQLEKKENRTFIKKDISGTPNYMAPEILMGVDTQMGDIWAMGCVIFEMLTGTRPFEANTVKAIWARIERNDIGWTKRVKESCSKEAVDLITKLMDPDCNKRLGSNGYQEIKKHPFFRTIKWDNLNSGPGPFVPQTENVEDLTYFEKNISGSDNINKNNCQTSATLILNGIFAFHPPPKATPADSGTETSNSAAFSASEEETTNLTDQKRKDLFSLITKAFKGIDLKALNYNNKATLLRMYDEVDFPKNQQRNKEKFRIQKRPNKKYRYHLF O94325 PEX5_SCHPO PTM: Monoubiquitinated at Cys-7 by PEX2 during PEX5 passage through the retrotranslocation channel: monoubiquitination acts as a signal for PEX5 extraction and is required for proper export from peroxisomes and recycling. When PEX5 recycling is compromised, polyubiquitinated by PEX10 during its passage through the retrotranslocation channel, leading to its degradation. {ECO:0000250|UniProtKB:P35056}. MOD_RES 66; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC725.07; CHAIN 1..598; /note="Peroxisomal targeting signal receptor"; /id="PRO_0000106314" MSVEAGCSTLSNPLKKLTSTAVVNNSTPSAQYRKHLTKSQSRTYAPLQTLSEDQFTSFKNLQGNNSPLGNVVKNPVSLKTGNHTGTTTRGGSKENWVHSFSSLQQQNSKSAWTSEFSEVFLNSSENDRFRNLNQPLKQSFFGSAGLNLSSNTEIPLQSSLAIDETELAKKFEEASQISNKLEKEKDATGSKSIEELWEEHQKQLKNAGLEPASLEEYQKQWEDFLKSNNISDDPYTSSVNSFANDNLAHNKNIDPQIFQHSDTDNVVENSLQTEDVYSQNQDESSEVVKELNGIDPFVEAMNLIKNGGSISKAAVLLEQSVKENPQHFEAWKWLGRIHTLLGNESRVVEALLEAVKLDSTNLDLMMDLAVSYVNQSLNVQALVCLEDWIVNSFPQYRNRFAKINERFEEKDSANDLLKMQMYFLDVAYELSLAKKRSSKVQAGLGIIMYMLKEYERSADCFRQALQDEPSNEILWNKLGAALTNAEKNTEAVSSYNRAVSLQPQYVRVRSNMAVSNINLGYFEDAAKHLLAAIDIIQNSSTSMESCESNEELWEMLRKVFLIGFQSTDLASQSYPGANTSYIRAQLSDLQGWPGVELE O94329 PSF2_SCHPO SPBC725.13c; CHAIN 1..183; /note="DNA replication complex GINS protein psf2"; /id="PRO_0000194821" MALPRELEISFSPEEMEFLAGNEYINIVPSETMDQLPLVSATIPIMKPPKKCRVPLWLALELKKQNLARIVPPEWMEIGKLENIRDDELENETFSELPFRWLETAHLLLNFCADDIEDVEDIRRILLDIREARQSKARTGLEAINEVQLTLDNLGAMEINEIRPIFREVMDRMRKIVQVSQEE O94335 STT3_SCHPO BINDING 55; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:B9KDD4"; BINDING 173; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:B9KDD4"; BINDING 175; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:B9KDD4"; BINDING 411; /ligand="dolichyl diphosphooligosaccharide"; /ligand_id="ChEBI:CHEBI:57570"; /evidence="ECO:0000250|UniProtKB:B9KDD4"; BINDING 555; /ligand="dolichyl diphosphooligosaccharide"; /ligand_id="ChEBI:CHEBI:57570"; /evidence="ECO:0000250|UniProtKB:B9KDD4" CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a di-trans,poly-cis-dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805, Rhea:RHEA-COMP:19506, Rhea:RHEA-COMP:19509, ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497, ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18; Evidence={ECO:0000250|UniProtKB:P39007}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:B9KDD4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B9KDD4}; SPBC1271.02; CHAIN 1..752; /note="Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3"; /id="PRO_0000072292" CARBOHYD 569; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 573; /note="N-linked (GlcNAc...) (high mannose) asparagine"; /evidence="ECO:0000250|UniProtKB:P39007" MANSATITSKKGVKSHQKDWKIPLKVLILICIAVASVSSRLFSVIRYESIIHEFDPWFNFRASKILVEQGFYNFLNWFDERSWYPLGRVAGGTLYPGLMVTSGIIFKVLHLLRINVNIRDVCVLLAPAFSGITAIATYYLARELKSDACGLLAAAFMGIAPGYTSRSVAGSYDNEAIAITLLMSTFALWIKAVKSGSSFWGACTGLLYFYMVTAWGGYVFITNMIPLHVFVLLLMGRYTSKLYIAYTTYYVIGTLASMQVPFVGFQPVSTSEHMSALGVFGLLQLFAFYNYVKGLVSSKQFQILIRFALVCLVGLATVVLFALSSTGVIAPWTGRFYSLWDTNYAKIHIPIIASVSEHQPPTWSSLFFDLQFLIWLLPVGVYLCFKELRNEHVFIIIYSVLGTYFCGVMVRLVLTLTPCVCIAAAVAISTLLDTYMGPEVEEDKVSEEAASAKSKNKKGIFSILSFFTSGSKNIGIYSLLSRVLVISSTAYFLIMFVYHSSWVTSNAYSSPTVVLSTVLNDGSLMYIDDFREAYDWLRRNTPYDTKVMSWWDYGYQIAGMADRITLVDNNTWNNTHIATVGKAMSSPEEKAYPILRKHDVDYILIIYGGTLGYSSDDMNKFLWMIRISQGLWPDEIVERNFFTPNGEYRTDDAATPTMRESLLYKMSYHGAWKLFPPNQGYDRARNQKLPSKDPQLFTIEEAFTTVHHLVRLYKVKKPDTLGRDLKQVTLFEEGKRKKLRRPAKTNEIPLRV O94346 ARGJ_SCHPO ACT_SITE 226; /note="Nucleophile"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124" BINDING 189; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; BINDING 215; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; BINDING 226; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; BINDING 312; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; BINDING 440; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; BINDING 445; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124" CATALYTIC ACTIVITY: Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_03124}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03124}; PTM: The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion. {ECO:0000255|HAMAP-Rule:MF_03124}. SPBC1271.14; CHAIN 1..225; /note="Arginine biosynthesis bifunctional protein ArgJ alpha chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; /id="PRO_0000310325"; CHAIN 226..445; /note="Arginine biosynthesis bifunctional protein ArgJ beta chain"; /evidence="ECO:0000255|HAMAP-Rule:MF_03124"; /id="PRO_0000397971" MQTKIFARLAGIGRARFVGTMPDKTKFISKSGTYPQGFSLNGIASGVKANGKKDLAILFSSRPCNAAAVFTKNAFQAAPVQVSRQTLNGCGGKDIHCVVFNSGCANAVTGEGGLMDAQLITAEADNLTRPHWTSWTENSEEFPSSLVMSTGVIGQRLKLDKIQSGLEHAVEDLGSTHEYWMRAAEAICTTDTFPKLVSRELSIAGKVYRIAGFAKGAGMINPNLATLLGLFVTDAPISVDAVRSILRHAINNSFNSISIDGDTSTNDTIAFLANGAAGGSEITKSSPAYKEIRDAVTDIAQQLAKLVVRDGEGATKFVTVQVRGARSEKDAALVASTISNSALVKTAFFGEDANWGRILCAVGYSGAAVNPPATTVSFIPADGTEPLKLLVNGEPQNVDETRASEILSQDELTVDVDLGCGPYAKTNWTCDFSYDYVRINADYRS O94353 APQ12_SCHPO SPBC428.04; CHAIN 1..115; /note="Nuclear membrane organization protein apq12"; /id="PRO_0000304062" MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNKTTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF O94354 ASSY_SCHPO BINDING 11..19; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 37; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 88; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 93; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 116..124; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 120; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 124; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 124; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 125; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 128; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 181; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 190; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 269; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250"; BINDING 281; /ligand="L-citrulline"; /ligand_id="ChEBI:CHEBI:57743"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000305|PubMed:15704224}; SPBC428.05c; CHAIN 1..410; /note="Argininosuccinate synthase"; /id="PRO_0000148558" MPQEVKRCVLAYSGGLDTSCILAWLIEEGWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIYENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPVFFERFAGRKDLLEYAAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLECKDGTFSGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQFVTFNLAKILYNGQFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAHLYDEKLSSMDELGGFDPTWTSGFIQIESMRLRNSDEGKHWM O94364 WAPL_SCHPO SPBC428.17c; CHAIN 1..602; /note="Wings apart-like protein homolog 1"; /id="PRO_0000116778" MKRGKCKEKDNGLKRISSESEVWNFLDVTVSELNKQKRSPGQTVSKRLHKKQRVVSNPDLSLPSSPVKQILRNGLQNSKYGSHKTGLERSASCSSIDASANHSSTTYREQRSYLMEEGLDTQPIVPREVSSGRELDSTNHTIGTERAFLIEEDVSEDDEIQMKSIHELRFAGEQQRIVDEIEYLVDGVTFSGNSSASRYLSLIGIAEKMFDNSFRLCLKSIRDVFLRIFEEIDPKDTLHTFLQIYIFATMANEMDCMSSLLDAYSNNVKLLLQTAITLEPQVPVSILAKSLPKSVKGAVQEFVIKAELTFSFSNESLASSDSISLAAIALMKTSSGVFAESELFTELINLLIEKSYPILKENDGSNNFLLHALCSSLEKFTDFQGSEKIQKVSQILSSKLQILIDEHNETNSPKIDDTVVHACSEKLLRTLIQTVNSNSDHALAVSKSEVPLFAYKILQKFSNFSSDDETTRELIILILGLLLGLVEESHEFIQTITHVEVSFGASALDVLISFYQKNESIVEISGYVVMILSHCFLNDPKAFAQLKPLISQFYESLHKFKNFHLKLKEELMMMGSNGLAIVSIIDELHKSLQDYLRSDLVK O94376 MED21_SCHPO SPBC1604.10; STRAND 35..37; /evidence="ECO:0007829|PDB:5N9J" HELIX 4..28; /evidence="ECO:0007829|PDB:5N9J"; HELIX 43..46; /evidence="ECO:0007829|PDB:5N9J"; HELIX 51..78; /evidence="ECO:0007829|PDB:5N9J"; HELIX 87..136; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..138; /note="Mediator of RNA polymerase II transcription subunit 21"; /id="PRO_0000096376" MACRCTQLQDTIDEVATQFYSSIHYLSSHHDFVPLPGQEKVSDSKVNPISAEELQFAQRDLAKDLVTKFMQIDTLINQLPGISTAPKHQLEKIKKLQNSIEEKQLERKSLESENEDLKLQLAKRIETFGRLSCVLFQP O94387 YGSA_SCHPO BINDING 1293..1300; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" SPBC29A10.10c; CHAIN 1..1944; /note="Uncharacterized ATP-dependent helicase C29A10.10c"; /id="PRO_0000350747" MENDEAFDRLIRKIQENQKHPSFEGSNKVLHLALSYLNTNRQNPHWVCDPKLQVAVRECLFLFSFQNDNEYLVWFKKHLNERLQLCPKCIVKYHQSLDDFKSLCLNIFHFDPNTLEIVMEKIYSWDIFRLQEVLKTVPKIDTSSASKPILCAFYEILYSPRILHNKEIFPLFRNRFLESGFLRLSKNLVPGVISLLFSRDDELRRWACSILSDVKTISDNEFKILEGPLLQEIRSLDQKKENENEMQIFLKGLSLLLKHVDHLYFRGLTGKNFNVADFILSGLQSDHTNLCPSFLVCLHSLLYCYGRNFWTPEISPSEVIDKIFNGNAYKRWTEENTSNFSNDQKAENPFEWATSLLKTISIIDEVELINKILINYTMQYKKELEVGFKNVQLLQSLADIFSVLFSEYFMIFPHSDQSLQNKVFELHSTLAIKFDELFRLLNLENEESVEWRLIKKVFEYRLNLDLYILKQFYCHYLDRNRKPPLNIKSVSESFKNFWVYLQNVFREEKFFMVRIVFRACSTVCLIDKLPPKKVDIPFKSDFENALNGFVATFSEMLIQTQCWHLSAQTQLVSNPLTFRGIFSLVFSPILEISTGSISIIKSISLSDSVVDTIGELLRSQFSNTLNSSCYVLLQWLKVRNFGGAKHIVYFNKLIINTIFDSVDGLTSKDATFAKQVEKKESLKNFWESLWKFFTHFFIVLPTWPVHDKDNLVDLMRDTLDFCDMLINIFEEVNGFIFGLSDNDIKIVSANDKGSALAMCIADSLVTVSYWLKLTDSSLLTSVVKVICKMLKICKKLECPISQNVIDIIHRASITSDEQTILTFTEREDLFISLTPYLSEDVLNHSPFNDTNTLETKLQSDDRGLLSKDQTIGIAKKLPESNISTSNHFLLPPKAISASKAINRNAQKSQNLNFLKSKQETTQRIRESAKVPRTSAGNHLSEKLNSDNHIPKALQKLDSADPIRKPSLLHTSKSYSNPDDKNTSTSDEDTSESEEESSNGLFSLAREANSHASKSLPQRRQIQFLDFDSLKTKNVVHPTQLRRNTQQSAQLARLRLNPDVQEFYKVILGWNPLADSFSASNVEMQCVQAKFTYNDSNAYEKVFKPMLFHECWAQVKSAVEEKQYPPIDLILNTRSTVDNFVDIYFTSCSPTEVSFLSDTDICLLSKSQSSGDTNNPKSFQLCKIQSISRKKESLELCLRMNIESIDLQEYAPNIRFTAQKLFNATTSLREFAALKSLRHLPLSQRILDANVTRLPSNFTDDKKQKIMKSYGVNEPQAYAIYASSVNDGFTLIQGPPGTGKTKTILGMIGAVLTSSSQGLQFNVPGQTRKTSKNKILICAPSNAAIDEILLRIKAGVYDHEGIKFFPKVIRVGFGDSISVHAKEFTLEEQMIKQMELTNLKKDQEANNSSDTRKKYDSIIKKRDSLREDLEKFRSTGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDVLKKQIQNQLLQEADIVCATLSASGHELLLNAGLTFRTVIIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMSAVTSRPWHEDPQLGIYRFFNVHGTEAFSNSKSLYNVEEASFILLLYERLIQCYLNIDFEGKIGVVTPYRSQVQQLRSQFQRKYGSIIFKHLDIHTVDGFQGQEKDIIIFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSKPLMQEDIFYSLIEDAKTRGVWRDLSANQFKNSKSISNVSTHLASNNLNLASRDTPIKSPSVGICEEKQEAHKVKKRHNIDSANLSRGTERDEDIPNKRAKNKVSTDQTAADNKVTKPRLDESSSSKQDVLNKIDESEIEQASSKKPGYVEKNKDKGHMKKSKKPKSKLALAAMAHGFAPPKVEHFKRK O94389 CC124_SCHPO SPBC29A10.12; CHAIN 1..207; /note="Coiled-coil domain-containing protein 124 homolog"; /id="PRO_0000339130" MGNPKKRAEKAEAAKSRKQDEEKKKKDAEEDEKWSKGVKTNKKEQEAEKRKAALERKAERERLEKEEMESLPSKGGKGSKKAAKKNSSLDAFLNETPQTASYSARNIDDALDLLSLNNSSSKDKIDRHPERRFKAALTEYKQSRLPELRKEQPGLRLNQYEDIMYKEFQKHPDNPFNKMNVSYNTSQDEVEQLRKARKAELEARLRE O94397 SGF73_SCHPO SPCC126.04c; CHAIN 1..344; /note="SAGA-associated factor 73"; /id="PRO_0000343136" MLTEQQTLELFPENWERNEQVLLKYPDGLPKDVLADQRVDNTESQVKDEITSNITNQTQILLPADSFPQYGSYPNNSELDYVVCTKCDRPFLSEYIEDHHSSCNGIKPPKPQFEPVANSQVLNKDVNNGNNAPIKNGVKSTAKGSAGNHEKNSVNGQKNPEMPPKRRKTEENKKPTKSALPKKEASKKKNPKVKGPVDVEKQCGVLLPNGQMCARSLTCKTHSMSSKRAVPGRSQPYDVLLAACQKKNQVKIQRQILETAKESEDNQHQAPVDSDEEVSFIMNVLQKSGNQPLEQKVFLPVKRRHSYFRTRELIAAAFRHGEQGMQVTGTILGRVIPFSARQPL O94399 TWF1_SCHPO MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC126.06; CHAIN 1..328; /note="Twinfilin"; /id="PRO_0000214952" MSASVELKPTEKFSKFLEEYSSVPVRAAIISISNENSFDVKTMVEKSESIESDFKKVRECLLGSEEPAFVLVYDDSKKNLLQLISYVPENANVRRKMLYASSRAAFVRCVTLAKLDESYFASTPEELDYQQIMKSLSKQEDQSPLRQDELERKEYNESMQSSVTHKRPLVTRGVAMSIDDKALKALSDLKSSTENNLVILSIDKEVISLSQEKQNIPPSDVKSFFSSTEPNFAFYSLPKDGSSKILFIYICPMQATVKHRMVYSSSKLGLLDSIKAELGIVIDGKIESNDAADITEKEILHAAGISSPQAETSTTKTGFSRPRPPRRR O94408 LSM2_SCHPO SPCC1620.01c; STRAND 13..19; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 24..32; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 38..45; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 59..62; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 67..72; /evidence="ECO:0007829|PDB:6PPQ" HELIX 2..8; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 48..50; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 52..54; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 64..66; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 76..92; /evidence="ECO:0007829|PDB:6PPQ" TURN 9..12; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..96; /note="U6 snRNA-associated Sm-like protein LSm2"; /id="PRO_0000125558" MLFYSFFKTLIDTEVTVELKNDMSIRGILKSVDQFLNVKLENISVVDASKYPHMAAVKDLFIRGSVVRYVHMSSAYVDTILLADACRRDLANNKRQ O94412 PGTA_SCHPO CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.60; SPCC1620.05; CHAIN 1..344; /note="Geranylgeranyl transferase type-2 subunit alpha"; /id="PRO_0000314652" MHGILRVKLSEEQRKLKAEKERAKIEEYRGLVSRFQEARKRKDYSEGNLKLTTELLDWNPETYSVWNYRREILLNDVFPKISLNEKQDLLDNELKYVLSKMKVFPKVYWIFNHRRWCLENAPYPNWNYEMMITEKLLSADARNFHGWHYRRYVVSQIERAGNCSLAKKEMEYTTSAIATNFSNFSALHNRTKLIETILNLEADPNSQKALAKQILEQELDMIHQAVFTDPDDSSVWIYHRWLMGHCNPNSMTPLISMITIEERIQYLQKEIELIQELHEMEPENRWCCESLVNYEALCKTLEKQKPTEADIKRWTLLVDKMIKVDPQRRGRYRTLQEKINNLNK O94413 KPR2_SCHPO BINDING 130; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P38689, ECO:0000255"; BINDING 132; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P38689, ECO:0000255"; BINDING 145; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P38689, ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000250|UniProtKB:P38689}; MOD_RES 172; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1620.06c; CHAIN 1..321; /note="Ribose-phosphate pyrophosphokinase 2"; /id="PRO_0000309463" MASNSIKIFAGNSHPELAEKVARRIGLSLGKVAVVQYSNRETSVTIGESVRDEDVFILQTGCGSINDHLMELLIMINACRSASARRITAIIPCFPYARQDKKDKSRAPITARLVANMLQTAGCNHIITMDLHASQIQGFFNVPVDNLYAEPSVLRYIRENIDTTVNPTVIVSPDAGGAKRATALADRLDLDFALIHKERQKANEVSRMVLVGDVRDKLAILVDDMADTCGTLGLAAKTLKDNGAKAVYAIVTHGILSGKAIKVINESALEKVIVTNTIPHDDKRSLCSKIETIDISGVLAECIRRIHHGESVSVLFSVAPA O94414 LNP_SCHPO MOD_RES 284; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1620.07c; CHAIN 1..334; /note="Endoplasmic reticulum junction formation protein lunapark"; /id="PRO_0000374042" MGWFFQKKKEFDFGGELDRLEMKLEEAQYNIDNIQSQKKKILFRYTVCSLAIYTIGMAVWASRSSILFQHPLFSKLFRISLYILGVFSLYMFRWAIAWFCEKRLSRARMNLHKLNAEKRKILDALKSRKEYFETQALLEKYGEQPTLAQKKLSNAAAAKSVPGSSSSSSDPMHPQHWYDRVLEGLVGANENSENNREALICSHCFHHNGLASYGEKASDVRYVCLFCKAWNGPPIDKSLPSSEMDSNLQTNPSSISKGKKNNSNNTTQKGPNIISSPQVINASSPVRKAGKKKSKKALPTSPLSSSSPDASYNSVSDSFHTVAASVPESLTPTK O94416 T2FA_SCHPO MOD_RES 259; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 399; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1620.09c; CHAIN 1..540; /note="Transcription initiation factor IIF subunit alpha"; /id="PRO_0000238604" MDSQETKVFENVKQENPDEKKPKVEEPDSQNNASTQSQQKFLDFQLSWCPESERKTTKYHLLKFHSNKAIDPSKSFVPPIKMQRRDPNAPSSSNGEQNAEQGSSSNVNIASIAPYGGAQNMKQNAFKRKTRQVVKVDPQARRLQEEELSPWIMEDFEGKNTWVSTMEGGQSSAYVLFMFSENGFKVIPTDRFYRFNQRNNFQTLSIDEAEAKMNKKTPIPRWFMKKESEENLAEAGSASPMYKLKTVPNARPVTGPRASGSDDELDYDEEFADDEEAPIMEGNEEDNKKLKDKIKKEMLTANLFGEADQDVDLEEENDRQMSREGKKLQRYLKLLEKNLAYESDEEDEDPYASSHDASSEEEVLQEEEELQKREEKLKSRFSANASKTNTPRPLERTPSSVSPVKASSQLQSPNTSIQIRPQEQLINKPGYIILRLSSEKLSRFANDFPRMVPSMGSTETSVGDQVEVVGDTTNVPIDDSNLITEAEVMKALRAGPISIKDLVHLFQRKIRADNRNRLGIQKIIRKVARFENKLLVLKNY O94423 MFR1_SCHPO SPBC1198.12; CHAIN 1..421; /note="Meiotic fizzy-related protein 1"; /id="PRO_0000051077" MGDRFIPIRNVSNEFNFSFQSFKECVLSHGSNLRRKTSGTIQRQFMELLSMELFGSQASRSRAFYYGEDKRKIEKKMLDTPDRKSYSLSPISPQSQDMLRQPQKPKRAFPKTPYKILDAPYLKNDFYLNLLDWGQSNVLAVGLASSIYLWSAASGKVVQLHDFGATNHVTSVLWTGKGTQLAVGTDSGVIYIWDIESTKSVRSLKGHSERVAALAWNDNTLTSGGKDEVILHHDLRAPGCCAEMMKVHEQEICGLQWDRSLGQLASGGNDNNLFVWDYRSSRPLHKFEEHTAAVKAIGWSPHQRGILASGGGTIDRCLTIHNTLTGRLQNKLDTGSQVCNMAWSKTSNEIVTTHGFAKNQVSLWKYPSLKNIANLTAHTNRVLYLSMSPDGQSIVTGAGDETLRFWKLFNKKPKEESTLIR O94431 EGT2_SCHPO CATALYTIC ACTIVITY: Reaction=AH2 + H(+) + S-(hercyn-2-yl)-L-cysteine S-oxide = A + ergothioneine + NH4(+) + pyruvate; Xref=Rhea:RHEA:42688, ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:82706, ChEBI:CHEBI:134344; Evidence={ECO:0000250|UniProtKB:A7UX13}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P23721}; MOD_RES 219; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P23721" SPBC660.12c; CHAIN 1..392; /note="Hercynylcysteine sulfoxide lyase"; /id="PRO_0000310318" MAENNVYGHEMKKHFMLDPDYVNVNNGSCGTESLAVYNKHVQLLKEAQSKPDFMCNAYMPMYMEATRNEVAKLIGADSSNIVFCNSATDGISTVLLTFPWEQNDEILMLNVAYPTCTYAADFAKNQHNLRLDVIDVGVEIDEDLFLKEVEQRFLQSKPRAFICDILSSMPVILFPWEKVVKLCKKYNIVSIIDGAHAIGHIPMNLANVDPDFLFTNAHKWLNSPAACTVLYVSAKNHNLIEALPLSYGYGLREKESIAVDTLTNRFVNSFKQDLPKFIAVGEAIKFRKSIGGEEKIQQYCHEIALKGAEIISKELGTSFIKPPYPVAMVNVEVPLRNIPSIETQKVFWPKYNTFLRFMEFKGKFYTRLSGAVYLEESDFYYIAKVIKDFCSL O94439 FSC1_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC22H12.05c; CHAIN 22..728; /note="FAS1 domain-containing protein fsc1"; /id="PRO_0000356245" CARBOHYD 89; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 404; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 501; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNLQFRLYLLFILLFISFANGKNEYEDKSTSIIDLLSSKSQFSKLIRRLQRNRLVPYLNRNKGLTLFAPLNEAFPDDSIEPNLLYYIVNTTELDRSVLRTQLKSSDGQQIALKIHYKAETGRAYDKVNNAQIVQSNWRADSGVVQVIDNIIDLPPPALEILSSEKDFSIFHRLSVAWVGEYSSVTMLVPDSSAFLNVYTNTELAYLYSMYAAEDVKTLIHQHILVNQRVYAEDVIEPKTFHYKNGISISMKFDKDQKKLFINDVSTTKYDLLTFSGAIHTVSSLINPEIISFTPAKYLIGIGAAWFSEKLSRERKSISVDKTSKRAILAPTNWAYREIIDIDYHIIENFDLPAPNKYALYVTNIKSGNSVGEDTNALVRIATGSAGEMYVNVETRSIQSENIGNVSLYVLDKDIEPPQPLLSQLILVDEISFSVRYLASLGLGDYTKVTWFLVKNSAWTQLGLVHLVLQQNLELLESVMLDYAFEGIAFYGSSDEAWASGNYTTLSNKEFLIEGVYEDSNSRNKRDLLRINNEIYEVQTRDLLVKDGVVHLVDKVKLPFSVSQKDMIIAGGRKEFLELLDKFEMLDMLDSGYPVVVPSLTGSDVNTKDSSFAERHIIDPEKRNFVISGSRLSVDSSPWISIQDYGYSELGNVYFVQNAIPTKRQNRWRITFISISGLLLSVGICVLCYKIYFKFFRNRFMNQGEREPLLAPADSDTMAGRRNSSSLSV O94444 RPN10_SCHPO SPAC637.10c; STRAND 4..10; /evidence="ECO:0007829|PDB:2X5N"; STRAND 21..23; /evidence="ECO:0007829|PDB:2X5N"; STRAND 48..53; /evidence="ECO:0007829|PDB:2X5N"; STRAND 61..67; /evidence="ECO:0007829|PDB:2X5N"; STRAND 106..114; /evidence="ECO:0007829|PDB:2X5N"; STRAND 137..145; /evidence="ECO:0007829|PDB:2X5N"; STRAND 167..171; /evidence="ECO:0007829|PDB:2X5N" HELIX 14..17; /evidence="ECO:0007829|PDB:2X5N"; HELIX 25..43; /evidence="ECO:0007829|PDB:2X5N"; HELIX 69..76; /evidence="ECO:0007829|PDB:2X5N"; HELIX 87..99; /evidence="ECO:0007829|PDB:2X5N"; HELIX 122..134; /evidence="ECO:0007829|PDB:2X5N"; HELIX 152..160; /evidence="ECO:0007829|PDB:2X5N"; HELIX 178..183; /evidence="ECO:0007829|PDB:2X5N" CHAIN 1..243; /note="26S proteasome regulatory subunit rpn10"; /id="PRO_0000173833" MVLEATMILIDNSEWMINGDYIPTRFEAQKDTVHMIFNQKINDNPENMCGLMTIGDNSPQVLSTLTRDYGKFLSAMHDLPVRGNAKFGDGIQIAQLALKHRENKIQRQRIVAFVGSPIVEDEKNLIRLAKRMKKNNVAIDIIHIGELQNESALQHFIDAANSSDSCHLVSIPPSPQLLSDLVNQSPIGQGVVASQNQFEYGVDPNLDVELALALELSMAEERARQEVAAQKSSEETEDKKMQE O94447 SLM1_SCHPO MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 312; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC637.13c; CHAIN 1..498; /note="Cytoskeletal signaling protein slm1"; /id="PRO_0000310807" MELSGKSEFPTRTEIPNQASNGDAVPNTDAYMGLCNSLTYRFEGWRHLVENLIAFFKQLESTSKNNAKEYMKLSKVIVHPYKDANVFEEHGIQDIFAALRDQTAAIASDSEQISIQLPGTIINILELLREDLREHCKKIAAEGTKGVKVVEKQRAETQKYLSLLDRALLPWRASSPPTVNIKNDPFIVDRQVLNCLARQVQEENNHSVAVAQLQEFSFRFEQNLIAKIKDTVKQFEGMMNQTHVKAINHLQEVVRVSEAQTLAGEWTGYAKREPEFIHGSVPPRSVDAIKYPGKNDQPTVPIMAGYLIRKTSFLKKKQRGFYAFTHSGYLYEFKSSDSLQDPEPEFALYIPDCLIGRPSEKKPKFKITGKDATKKIFGARNDYAFRASNNTELMRWWEALNTHIANVNYIQPLSNANGPSAVSDSDDDDDDPNDFRPAVERQSSTMNTRMSQPSSAVNTNRSYGSEQIPSYADSQGNSGANNNFIYNASATGHNAWNV O94454 CSN5_SCHPO BINDING 118; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 120; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"; BINDING 131; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01182" SPAC1687.13c; CHAIN 1..299; /note="COP9 signalosome complex subunit 5"; /id="PRO_0000194856" MNNQLENVFRFDEEKERAKIRESPWKHDPEFFRSVKISAVALLKMLRHVSQGMPLEVMGYVQGKVEGASLIILDSFALPVEGTETRVNAHEEAQEYSVQYHTLCKSVYRHENVIGWYHSHPNYGCWLSGVDVETQRQNQKYQDPFVAVVLDPKRSLESPYVNIGAFRTYPVGNDGSIRTKSRHHPSVLFKNLPSSKIEDAGAHAEAYYSLPITYFHSKAEKKVTEFLRNRNWSRSITECSILQNNEFLHDSEKLIDHLIHETGNNELPVASAYEQSKACCNELSTFLSQIDVQDKLFKE O94460 TGT_SCHPO ACT_SITE 98; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; ACT_SITE 272; /note="Nucleophile"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218" BINDING 98..102; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 152; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 195; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 222; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 310; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 312; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 315; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218"; BINDING 347; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03218" CATALYTIC ACTIVITY: Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:18571, ChEBI:CHEBI:16235, ChEBI:CHEBI:17433, ChEBI:CHEBI:74269, ChEBI:CHEBI:194431; EC=2.4.2.64; Evidence={ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000305|PubMed:24911101}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03218}; SPAC1687.19c; CHAIN 1..404; /note="Queuine tRNA-ribosyltransferase catalytic subunit"; /id="PRO_0000135569" MASSFPALQFKVVARCSTTRARVTDIQLPHGLVESPVFMPVGTQASLKGVLPEQLDALGCKIMLNNTYHLGLKPGQEVLDTVGGAHRFQSWNKNILTDSGGFQMVSLLKLATITEDGVTFLSPRDGTPMLLTPEHSISLQNSIGSDIMMQLDDVVHTLTESKRMEEAMYRSIRWLDRCIQAHKRPETQNLFCIIQGGLDKRLREICCREMVKRNTPGIAVGGLSGGEEKHAFCETVYTCTSILPDNKPRYLMGVGYAEDLVVCVALGMDMFDCVYPTRTARFGNALTRKGVINLRNQKFRNDIGPLEEGCSCPCCKTELEGGWGITRAYFNSLVSKETVGANLMTIHNVHFQLQLMRDMRESIIKDEFPSFVKNFFHEWNHGDKSNYPSWAVDALRMVNIDLLA O94462 PUF3_SCHPO SPAC1687.22c; CHAIN 1..732; /note="mRNA-binding protein puf3"; /id="PRO_0000372691" MFTAVNSNPNASESISGNSAFNFPSAPVSSLDTNNYGQRRPSLLSGTSPTSSFFNSSMISSNYTFPHGSNKQASLESPVSYSNPIPSLTWLSLDGDSPDSLVSTPTAPSANHHGNPFPNGKQSIKAMPSLVNLQEDSVISKFPNSLEVPFRKRSESTSSSLSGLHSDLRPLKTELYGQLNSECGARFPQTLKSPLTPIGGDSARTVSASTARTSDKFFPRHTRAHSDFWIPATSKPSRHASHSSIGDLTTITQSSISSGSGSFKPSWDGSFDSSLMAHQSYGTSPAFANGNSPTLKNDSSFFGSASVRPTVSPIGTSFRQSLPDISAFGIPKTETNPSEVVAPGTIPISVLPTSNFSAATPANPSLINQNGQEFLQQSRVLYLFHANKQRHFELSDILGNVVLFSTDQHGSRFIQQKLATATEEEREAVFQEIASTSCLQLMMDIFGNYVVQKYFEFGNEKQKQILLSQIKGHVFSLSLQMYGCRVVQKAIEYISPEHQVQLIQELDGHVLDCVCDQNGNHVIQKAIECIDTGHLQFILRALRPQIHVLSAHPYGCRVIQRAIEHCHSERKLIIEELLPHILKLTQDQYGNYVVQHILRTGSESDKKYIFDLMIDHLLFLSCHKFASNVVERCISYISDVDRRRILNKIISEKAENCSILMLMMKDKYANYVIQKLLDASPEEERDLLISYIYPHISVLKKFTYGKHLIMSVERFRQKSISAVPKLASKECK O94464 NVJ2_SCHPO MOD_RES 473; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23G7.06c; CHAIN 1..779; /note="Nucleus-vacuole junction protein 2"; /id="PRO_0000350757" CARBOHYD 233; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 489; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 536; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 640; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 660; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFFAFLITYLLGGVTFLPFILFIYLLTRPTHKSEELRIIEPNNDCLTKLDKDIRIQGWIRVTTKFLQGKSGSVKVQEIPQDQLPKSSSDNAVTDRKTISPSGINNQYVIRNPKDVYYATVQAGKLHLFDPVKTSELLHVINLHEYLVVFYPGTVTENELFSNRNAIFLKYPAVSHKKESSTKSLLNKDLYVYGRTPSNKEDWYYALLSYSKISPAIKPLEAPIDFDYASVHHNLTALSSPDTDWLNAFIGRIFLGIHKTEGFKSLVVEKLTKKLSRIKTPGIMTDVKVIDVDVGEAIPTVNGLKFESLSNGGELIVSADIWYEGDCSFKAETTANIKFGSHFPSKTVPLALVIRLTHVSGKVRLLIKPPPSNRVWYAFYEKPRLHLIVEPMVARKQLTNNYLINFITQKLVELVHETIVMPNMNDLAFFIDNEAPIKGGLWDIELFRAPTIQKPAEKDAKAERKKSGLSSSTSEESLNRHISKRSSNSNDTAPSSHIIADKNLEPTSNIQLKKNPDGNLVETSELSDSDENSVLSNKSSTLSKKVVENTSPLKYTHSASKSFIGEVQDSLQALKTKAHKPRSIGGDSSQTTLSETTKKYGSVAKKSFFQGVSDAKSFVKKIKSTYIDDSSSNSPSDIESNYSADDNEISKSKAQNAIDFNVTNTHSPSRSISSEKSYKAAERGQQDKHNDVLVDLNPNVEAEKSNPHSNSQKTSKNDMSRNQRNKYAKEIMTGQPTLHPQGQLPIQNVEQRATHKPLPRPPVQVETREPVRPVPPIPKL O94468 MAG2_SCHPO BINDING 53; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 54; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23273506"; BINDING 61; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23273506"; BINDING 91; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 94; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23273506"; BINDING 96; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23273506"; BINDING 97; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 99; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23273506"; BINDING 102; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23273506"; BINDING 137; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 138; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 140; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 143; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 163; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506"; BINDING 164; /ligand="DNA"; /ligand_id="ChEBI:CHEBI:16991"; /ligand_note="abasic DNA"; /evidence="ECO:0000269|PubMed:23245849" SPBC23G7.11; STRAND 72..75; /evidence="ECO:0007829|PDB:4B21" HELIX 3..14; /evidence="ECO:0007829|PDB:4B21"; HELIX 19..28; /evidence="ECO:0007829|PDB:4B21"; HELIX 41..50; /evidence="ECO:0007829|PDB:4B21"; HELIX 56..70; /evidence="ECO:0007829|PDB:4B21"; HELIX 79..83; /evidence="ECO:0007829|PDB:4B21"; HELIX 87..91; /evidence="ECO:0007829|PDB:4B21"; HELIX 97..111; /evidence="ECO:0007829|PDB:4B21"; HELIX 118..123; /evidence="ECO:0007829|PDB:4B21"; HELIX 126..133; /evidence="ECO:0007829|PDB:4B21"; HELIX 141..150; /evidence="ECO:0007829|PDB:4B21"; HELIX 163..172; /evidence="ECO:0007829|PDB:4B21"; HELIX 181..187; /evidence="ECO:0007829|PDB:4B21"; HELIX 189..191; /evidence="ECO:0007829|PDB:4B21"; HELIX 195..203; /evidence="ECO:0007829|PDB:4B21"; HELIX 204..207; /evidence="ECO:0007829|PDB:4B21" TURN 15..17; /evidence="ECO:0007829|PDB:4B21"; TURN 51..53; /evidence="ECO:0007829|PDB:4B21"; TURN 92..94; /evidence="ECO:0007829|PDB:4B21" CHAIN 1..213; /note="Alkylbase DNA glycosidase-like protein mag2"; /id="PRO_0000194882" MSKDSDYKRAEKHLSSIDNKWSSLVKKVGPCTLTPHPEHAPYEGIIRAITSQKLSDAATNSIINKFCTQCSDNDEFPTPKQIMETDVETLHECGFSKLKSQEIHIVAEAALNKQIPSKSEIEKMSEEELMESLSKIKGVKRWTIEMYSIFTLGRLDIMPADDSTLKNEAKEFFGLSSKPQTEEVEKLTKPCKPYRTIAAWYLWQIPKLHRKGQ O94476 IF6_SCHPO PTM: Phosphorylation at Ser-174 and Ser-175 promotes nuclear export. {ECO:0000255|HAMAP-Rule:MF_03132}. MOD_RES 174; /note="Phosphoserine; by CK1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03132"; MOD_RES 175; /note="Phosphoserine; by CK1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03132" SPCC1919.09; STRAND 3..5; /evidence="ECO:0007829|PDB:8ETC"; STRAND 17..19; /evidence="ECO:0007829|PDB:8ETC"; STRAND 24..26; /evidence="ECO:0007829|PDB:8ETC"; STRAND 28..30; /evidence="ECO:0007829|PDB:8ETC"; STRAND 48..50; /evidence="ECO:0007829|PDB:8ETC"; STRAND 53..55; /evidence="ECO:0007829|PDB:8ETC"; STRAND 64..66; /evidence="ECO:0007829|PDB:8EV3"; STRAND 71..73; /evidence="ECO:0007829|PDB:8EUY"; STRAND 74..76; /evidence="ECO:0007829|PDB:8EUP"; STRAND 95..97; /evidence="ECO:0007829|PDB:8EUY"; STRAND 100..103; /evidence="ECO:0007829|PDB:8EUP"; STRAND 108..110; /evidence="ECO:0007829|PDB:8ETC"; STRAND 112..114; /evidence="ECO:0007829|PDB:8EUY"; STRAND 119..121; /evidence="ECO:0007829|PDB:8EV3"; STRAND 135..139; /evidence="ECO:0007829|PDB:8EV3"; STRAND 152..154; /evidence="ECO:0007829|PDB:8ETG"; STRAND 159..161; /evidence="ECO:0007829|PDB:8ETC"; STRAND 163..165; /evidence="ECO:0007829|PDB:8ETC"; STRAND 181..183; /evidence="ECO:0007829|PDB:8ETC"; STRAND 197..199; /evidence="ECO:0007829|PDB:8EV3"; STRAND 204..206; /evidence="ECO:0007829|PDB:8EV3"; STRAND 208..210; /evidence="ECO:0007829|PDB:8EV3" HELIX 13..16; /evidence="ECO:0007829|PDB:8EUY"; HELIX 32..41; /evidence="ECO:0007829|PDB:8EUY"; HELIX 59..62; /evidence="ECO:0007829|PDB:8EUY"; HELIX 78..87; /evidence="ECO:0007829|PDB:8EUY"; HELIX 104..107; /evidence="ECO:0007829|PDB:8EUY"; HELIX 123..133; /evidence="ECO:0007829|PDB:8EUY"; HELIX 148..151; /evidence="ECO:0007829|PDB:8EUY"; HELIX 167..177; /evidence="ECO:0007829|PDB:8ETC"; HELIX 186..189; /evidence="ECO:0007829|PDB:8EUY"; HELIX 193..196; /evidence="ECO:0007829|PDB:8EUY"; HELIX 212..221; /evidence="ECO:0007829|PDB:8EUY" TURN 42..45; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..244; /note="Eukaryotic translation initiation factor 6"; /id="PRO_0000153741" MALRAQFENSNEIGVFSNLTNSYALVALGGSENFYSVFEAELGDVVPVVHTTIGGTRIIGRLTCGNRKGLLVPSSTTDNELQHLRNSLPDPVKIQRVDERLSALGNIVACNDYVALVHPDIERETEEIIADVLDVEVFRQTVAGNVLTGSYCALSNQGALVHPRTSIQEQDELSSLLQVPLVAGTINRGSDVIGAGLVVNDWCAFAGLDTTATELAVCESIFKLQDAQPSAIISNRDTLVESYT O94483 HSK3_SCHPO SPCC417.02; CHAIN 1..94; /note="DASH complex subunit DAD5"; /id="PRO_0000084029" MRRSTIVPTSRTSSSSPSPSQMKSFQMNRLVDQLSKLQSNMSHLENHLHVTAIQAEAIRRLGALQASLLMASGRVMSEARIQKSSDAVEEDVPM O94494 CENPK_SCHPO SPBC18E5.03c; CHAIN 1..277; /note="Inner kinetochore subunit sim4"; /id="PRO_0000097761" MNSENASLFRNILNDTENLVQPLTQDESRLALFESLVQSDQLLVEKIEKWEKKVSKFTENSKSEKRKLQLELFQEIIDLKKCIAFKPIIGKNAIDNNISDLKKNLHSNKKLEAVLKEELHQIKKFSSDLQSLKSSMGERQKQQAAMSRRGKKSIIHSAIIQEKERYEKESQELFTFLDGFLDEHAPSLLEGAQASIDKNRPGKNQPSLNFENISKKDLTEEFKQVIENLMNNSIIPGSPYIEVKNERIVSFLVLASLCTVDPQDPSKVKLIPFSDEI O94508 CWF11_SCHPO SPBC646.02; CHAIN 1..1284; /note="Pre-mRNA-splicing factor cwf11"; /id="PRO_0000079611" MVLYKNKKKQIINYANSNWGQNEGVEFQETMLQCILEAVIVSKDAKQVLSLLHELKLFENFLWQRVNTEMSLNHINLTCMLLLYKSKYEYITWDLIDENRFQLFFEKVIEVSLSLNLSEVVYMIQFITLCFQFSNIEKLRKLVYQLTNISILNSLDNLDKVKYLLHDSSSLTKAFDSYKEKRPSIVEKFPLHNLLSRWIHSLLIKSISYAQTEKQEAKVTPLLAIINMSLVLLSAFPTRRFAHPVIEDSCFYTALRMSLYYDSNELFKKMTDDLNYVLKFPFDNTRGNEYEKEQKIRNDELVYYHLQLTLFSDFQKELGDLVFCTQTSLQQRQKLEEITSFLSFNSLKSLCSKCYLRTSFPEKYAIKVDFEFLKNVFINTYDRTRLVNDYDEIINFTLKDVLGERSVMDQENSLTNYFLLQNTAIQYLSISFFMRQQSKAYKKLLLRSLYAELLNFSEQYRRLSIKNATKNLTKDNFFSLNNFKVTSVAPPQIGQVLPQFVKCQMGLSRPGPFHSALRDLKNSIKSPFLCLIYISKDMEYKLLHGNALDPLEGVTDFTIATICNDDVGMFQSDMQSDSDNKSINVYLSPFYYHSLAGLGEYRPKQLKFNFALVLSPEANKYWLDLNILVSLLNRAKEFPKWFEDLFLGFGTPDICAFPNAGLNSIYARNLFNTVEQLQSVLPNCHVPSNLSTESLLIKFYTNQNKISADVTASDRHFLLPSNRLYTYNDKQLESILRGSQPGLTMVNGPTRCGKHVLVCKLLEVLQDTSPNDRTVVLSDSNFSMNTLFTLLEKARCFHQGHLLYLSDEGKDETLERYGTLSSWISKLPGLLREIGRLAASIQAPGSHDASPDTALYFRDAYIKRLWEKYLNTVDDKDSVDAYNRFPFHSYFGDKSKRPIETYNKDNFFDYATKLYGELEYMFQQLEEIRPFGLLRYYEDQELYALCQQSRIIGCTWTSLSTRLGTLKEKGFCFNNLIVMNSQNISESSITSILLSNCEPTGFDRLVLLGNQYLTSGNQDINNTSNGSLFKRLRYLKSRIIDLNTQYNVRESISSLCSSIYPLDIKTVDSSPNKRLDYGNSGFAHEVQFINVGAFKGSQETEPVSGYKQNLGEAEYAVALFQYMRMLGYPTNEIVICTLYESQVSLLNEIISVRCSHNSFFGQPAFVGTVEKLPSDKRVNFVIFTTVESKEASDHWNPKTFYKAFSACSYGLYVLCNRDLFRSTRGLEKLWNEIEKTPDKLLLTTGEIYPSSHKIGSSVETFEIENLLHLSNYVVEMTKKRLNTN O94518 DIC1_SCHPO SPBC646.17c; CHAIN 1..544; /note="Dynein intermediate chain 1"; /id="PRO_0000297693" MDKNIKREIEIKRAKLLLLKNKENCTDAVSSSNKEGPKQISEDQLSNFLCKILKPTNLTPQTYSLESKSSNLVSDCELKISSVYQSYSSTFNVSNHVPSISKTVNIRETSKHLKHSTKAPKCSLPTSALEIDHLNNFLHSSAKILDRALCDQSNQLFTDYTVKKKSKKNKSQLEENGLNHLFTFQDEKITLNSVVNSISYSSFFEELLITSYAKPKEALRTRGLAIVWNQRWKNSPESVLKARSEITVCKPSPFHPQLIAGGAYNGQVFLWDLRQGQYPVSFTTIISGGHLEPVTDITYINNPPSNNIVTCSTDGLVHIWEPDMFSRPSETICLSSQVDSSSQCIPATCLSFIPENNMEFLVGAEDGKLQRGYRSDYSETKAVQPSNVSYEGHNVFISGIDVMTSNSQNVFLEKNKDFALTSSFDWTVRLWQCSPSRNQHELVPSNDLDEQVIINSCKTFTHKAMVFDVKWCVSEPCCFASVDALGNLNLWDLQKDVEAPVTSDIPDGKPLNKIAWQPEKRNLACGGLNGNVHIYKHLSPNLAN O94522 RSC7_SCHPO MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1281.05; CHAIN 1..390; /note="Chromatin structure-remodeling complex subunit rsc7"; /id="PRO_0000373988" MDSTAGSDASTPTNHTVSSKKRRGRPPKGSYAAYGSSDDDDEEYSGRTRRRNRNTRPRVSAPSSSSTVVPKDLYSHRATLEDDELNFGVVDPEGEKKVNELGYLNGGREYRCRTFTCLGRGNRLYMLSTEPARAMGYRDSYLLFLKHRSLHKIIVDDSEKWDLIERNIIPHSYKGRAVGIVAARSIFREFGARIIVGGRRIVDDYWEGEFRARGFVEGELADPDDKLPPPGMPYNRNQYVAWHGASAVYHPQPSLEAQLPAAARKRKKEPPKDATWLFQHAKATAAYNNDITKYLVQKQDIGYFEPHTNLLHVPLNTQPTKTHWIQAKTGTECPAPKLDILVALNSDVAPQVSIANIPPSVYASCPLHVQEAIRKRQEQEIRSIRLNSMY O94523 ACO1_SCHPO BINDING 110; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 115; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 147; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 150; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 151; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 255; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 284; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 287; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 288; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P13516"; BINDING 390; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"; BINDING 416; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387, ChEBI:CHEBI:57394; EC=1.14.19.1; Evidence={ECO:0000250|UniProtKB:P21147}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P13516}; Note=Expected to bind 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P13516}; SPCC1281.06c; CHAIN 1..479; /note="Probable acyl-CoA desaturase"; /id="PRO_0000185405" MTAPSATAFSSATTQPTTEGNASMRKRTIPVVPSVPERKWDPKAPKHIQEQPWTMQNWWRHLNWLHCMLIFGLPMIAIYGVFTTPLQTKTLIFAIIYYAYSGLGITAGYHRLWSHRAYKAKKPLEYFLAAGGAAAFEGSIRWWSRDHRAHHRYTDTDKDPYNVKKGFWYAHVGWMIILQNPRRIGRSDVSDLNSDPFVMFNHRHFLPIASFMAFIFPSLFCGLLWGDYRGGYFYAGVCRLVFVHHATFCVNSLAHLIGSQPFDDTNSARNHFITALVTLGEGNHNYHHAFPNDYRNGLRWYEYDPTKIFIYIASLFGLAYNLNTFPDNEIQKGIVQQKQKVLDRWRAKLNWGIPLEQLPVMEFEDFLEQSKTRPLVLINGVVHDMTGFEHPGGQGLLRSAFGKDATAAFNGGVYDHTNGAHNLLSTYRVAVVRGGMEVEVWKSGAGAQLPMKDTQGQKIVRVGEQITRIQPPIEAAAAN O94524 GTO2_SCHPO ACT_SITE 49; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; CATALYTIC ACTIVITY: Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide + L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1; SPCC1281.07c; CHAIN 1..313; /note="Glutathione S-transferase omega-like 2"; /id="PRO_0000343153" MSNTHITDWSSKDGEFRRQVSSFRERISPEHKYFQPEKDRYHLYVSYACPWAHRTLIVRKLKGLENVIPVHVVGWLMGPNGWNFDKENDSTGDPLYNSPYLRNLYFRADPNYNMRFTVPVLWDSKYNTIVNNESAEIIRMFNDAFNEVIEDEEKRVVDLYPSSLRTKIDELNDYFYDTVNNGVYKTGFATTAEAYEKNVRVVFQGLDRLEQVLKESKGPFLLGDHLTETDVRLYTTIVRFDPVYVQHFKCNIGTIRHNYPHINQWLKRLYWKHPAFHETTDFKHIKCHYTQSHTQINPLGITPLGPIPNVEYF O94530 SUA5_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87; SPCC895.03c; CHAIN 1..408; /note="Threonylcarbamoyl-AMP synthase"; /id="PRO_0000315950" METKIQTVDTRLISFEKPSNDSEHPFEHTRVSIPPSETRSALENAANILRNTDYPVAFPTETVYGLGADARRTEAVLSIYKAKNRPADNPLIVHVASLDQLRRLLLSAYPKAKSEVKNQAHDSEEIIPKVYLPLIKKFWPGPLSILLPVVDEANPPVSPIVTAGQKTFAVRMPQHPVALALISISDSPLAAPSANASTRPSPTLAKHVYNDLQGKIPLILDGGACGVGVESTVVNGLCDPPVILRPGGISLEEIQSSGGAWERTKVFVAKKSDMETDFIPQTPGMKYRHYSPTAKVLLFVNYTESDAYGVFEKYLSEQGITKEKQKIGVLCSKRWNEESFPSHCPFVFLHMGRDGHEITKNLFAQLRDLDLQGVDFVLVEGVSEENEGLAIMNRLGKAASVVFEGPSH O94538 SNU66_SCHPO SPAC167.03c; CHAIN 1..649; /note="U4/U6.U5 tri-snRNP-associated protein snu66"; /id="PRO_0000290651" MSGNSGASESISIEETNRIRISLGLKPLDISEEKPQKELSDASVKSSYVDQEQQAYENWKKQEQEEINRKKEEELKSKFEKLRQKNERRRRTQGKTLAETLAEEDDQIDANDTRAWILKMRNSSLNKNGNGLNFEAKNDAPRRSTLHSQNAGPNVNSSLEGMKIAHGFQDLNKNDGLVLTLKDADILDEDNHDLLENVEMVQRKTKNERKEDNPYKPYEDENDFLQQSEADQPSEDTFTTIGPQNSLTVNSTIEKHKSDNKKTFGTLVSFVEPTITGSEQSDYRQIKIKKSKKKKSKSDRRKRLVELDAENENENDPSDFVLPNGQSNSDLSVEQDSAIFKEQKKMKIQKRMRELETQSFADDDDLQQSIAMQRRLAQKRAKILKPEDVAEQLQNAEEVTDMTDSDTASGLIFDDTRAFVNSIKETENREALGSINEQAFEDSKDLNDTNSITGSSPTEESNALVEDTSVDISATLEEANTQQENAEDEPLVSDNVGAVLSLLRNKGVIKVSDEAKEKIQKEEEYNKWFARKQQARVELEEQRRKKKEQDRLSGKFEKMTQKEREQYAKKENERWDKKIAEIELEQFHDYKPQVDIKYVDEFGVELGPKEAYKYLLSHQFHGKGSGKAKTEKRLRRIVEKEREERKPIF O94552 FUMH_SCHPO ACT_SITE 243; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P05042"; ACT_SITE 373; /evidence="ECO:0000250|UniProtKB:P9WN93" BINDING 153..155; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P05042"; BINDING 184..187; /ligand="substrate"; /note="in site B"; /evidence="ECO:0000250|UniProtKB:P05042"; BINDING 194..196; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P05042"; BINDING 242; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P9WN93"; BINDING 374; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P9WN93"; BINDING 379..381; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P9WN93" CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000250|UniProtKB:P08417}; TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC18.18c; CHAIN 40..520; /note="Fumarate hydratase, mitochondrial"; /id="PRO_0000010332" MASVAHISTAKAIFRAGGLPCRRLITPTLTGLPLKTHRMNSTTPTYHLIPKGGKHGEFRQESDTFGPIQVPAEKYWGAQTQRSLQNFRIGGEKERLPLPLVRAFGVLKRAAASVNREFGLDPKLADAIEQAAQEVIDGRLDDNFPLVVFQTGSGTQSNMNSNEVIANRAIEILGGTLGSKKPVHPNDHVNMSQSSNDTFPTVMHIASVLQIHTHLLPAMKHLHRALKGKEEEFKNIIKIGRTHMQDATPLSLGQEFSGYVTQVGYGIERINNALPRLCLLAQGGTAVGTGLNTFEGFDVKVAEKVSKLTNIEFKTAPNKFEALAAHDAIVEMSGALNVIACSLMKIANDIRQLGSGPRCGLGELILPANEPGSSIMPGKVNPTQCEALTMVCAQVMGNHATITVAGASGHCELNVFKPLLAKNILSSIRLLGDACESFTDHCVVGIEPNYEGIARHLRDSLMLVTALNPHIGYDNCAKIAKTALKNKSTLKHEFVTLGFGTPEQFDEWVRPELMISAKKV O94556 APC8_SCHPO SPAC6F12.14; STRAND 150..152; /evidence="ECO:0007829|PDB:5FTP" HELIX 20..36; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 40..51; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 79..86; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 88..99; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 103..109; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 116..134; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 155..168; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 173..185; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 189..202; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 207..215; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 220..227; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 235..248; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 253..265; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 270..283; /evidence="ECO:0007829|PDB:3ZN3"; HELIX 296..298; /evidence="ECO:0007829|PDB:3ZN3" TURN 110..112; /evidence="ECO:0007829|PDB:3ZN3" CHAIN 1..565; /note="Anaphase-promoting complex subunit 8"; /id="PRO_0000106282" MTVSLNTMMGVDGLEDQEQLREIRNCLLKCISECSERGLVYAVRWAAEMLNGMNPIEMEHIPFSSTPTGEFDLDPDMANEKLLEVEEKNIYLLAKSYFDCKEFERAAYTLQNCKSSKSIFLRLYSKYLAGEKKSEEENETLLNTNLTLSSTNREFYYISEVLESLHYQGNKDPYLLYLSGVVYRKRKQDSKAIDFLKSCVLKAPFFWSAWLELSLSIDSLETLTTVVSQLPSTHIMTKIFYVYASHELHQVNSSAYEKLAEAEIIFPNSRYLKTQRALLTYDSRDFDEAESLFENILTNDPYRLDDMDTYSNVLFVLENKSKLGFLAQVASSIDKFRPETCSIIGNYYSLLSEHEKAVTYFKRALQLNRNYLSAWTLMGHEYVELKNTHAAIESYRLAVDVNRKDYRAWYGLGQTYEVLDMHFYALYYFQRATALRPYDQRMWQALGNCYEKIDRPQEAIKSYKRALLGSQTNSSILVRLGNLYEELQDLNSAASMYKQCIKTEETEISPETIKARIWLARWELGKKNYREAELYLSEVLNGDLELEEAKALLRELRSRMEHSYD O94587 COX18_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1442.15c; CHAIN ?..202; /note="Cytochrome c oxidase assembly protein cox18, mitochondrial"; /id="PRO_0000020360" MLQTLIGVHSYMPWCYEIPAMAIFLRSTITLPIAIASLKTARRFVQVQPLIKEAKKRCRTNTDFRTVRKKLYKRFNCHPLMIYALPITQLPLFAFASYQLRQAVDVCPESMSTEGMLWFTDLTLPDPHGVLPAVLAVTYLTNMSILKRPSDSRLLKIFNTAGIMSAFFVSFMAFKTSTALSLYWTTSAIYSLVQNVALRKLL O94616 RPAC1_SCHPO SPBC1289.07c; CHAIN 1..348; /note="DNA-directed RNA polymerases I and III subunit RPAC1"; /id="PRO_0000132741" MAAVDRSRTEISVLSDRVTDVGSVDFPGYYFDEDNIWDLDKFKKNLKVSITSLDQETMVFEISGIDASIANAFRRILIAEIPTLAFEFVYIINNTSIIQDEVLSHRIGLVPISADPDMFKWFQHPLPGQEATHTDYDTVVFSLNKKCEFNKNAATDEKDPKRLYVNSEVYSGDLIWKPQGRQEERFADNPIRVVNPDIVVAKLRPGQEIDLEAHAILGIGQDHAKFSPVATASYRLLPTIHILSPIEGEDAVKFQKCFPKGVIELEEGPDGKKQARVADVRKDTVSRECLRHPEFADKVQLGRVRDHYLFSVESTGIMKPDVLFIKSIAVLKSKCLAVKSSLQNISSD O94620 CWF17_SCHPO SPBC1289.11; CHAIN 1..340; /note="Pre-mRNA-splicing factor cwf17"; /id="PRO_0000050951" MDKRKESESATNGHLVKRIRIQDSSLITEGSVLQRTSDLNVPNLQMFGHTAEVLVARFDPSGSYFASGGMDRQILLWNVFGDVKNYGVLNGCKGAITDLQWSRDSRVVYCSSSDTHLMSWDAVSGQKIRKHKGHAGVVNALDVLKVGSELLTSVSDDCTMKVWDSRSKDCIKTIEEKYPLTAVAIAQQGTQVFIGGIDGAIKIWDLRNNHCSHVLKGHKDIITSLAISKDGSSLLSNSMDNTVRIFDVKPFASAQRQLQIFEGAIHGQEHNLLGVAWSRNSRFVGAGSSDKNVYVWSATGDLRYVLPGHEGSVNHVDFHPHQDIILSCSSDRTIFLGELN O94634 THDH_SCHPO CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; Evidence={ECO:0000250|UniProtKB:P00927}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P00927}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:P00927, ECO:0000255" MOD_RES 144; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPBC1677.03c; CHAIN ?..600; /note="Threonine dehydratase, mitochondrial"; /id="PRO_0000314633" MTGTSFYTSVLRLGRLAQQGLKFQSVKHIRPSCFSSFGLQAKRWNSTQQNDSSIDCLEPKLQGIIEDNISPSTAQKEISDIKFNIPKEMLLPDGTPDYLRLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDLRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNAAQVCILSGANMDFDRLRFIAERADLGLNKEVFLSVTIPERPGSFEALHNIITPRSITEFSYRYDNDDYANIYTSFVVKDRATELPLILQQISEQNMVAEDISDNELAKTHARYLIGGKSSVSKERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQVEKLHSVLEEIGYNWVDETNNPVYLRYLRK O94637 KAE1_SCHPO BINDING 117; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 121; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 138..142; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 138; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 170; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 185; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 277; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180"; BINDING 305; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03180" CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence={ECO:0000255|HAMAP-Rule:MF_03180}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03180}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03180}; SPBC16D10.03; CHAIN 1..346; /note="tRNA N6-adenosine threonylcarbamoyltransferase"; /id="PRO_0000255600" MGKPLIALGLEGSANKLGVGIILHDTNGSAKILANVRHTYITPPGQGFLPSDTAKHHRAWIIPLIKQAFAEAKISFKDIDCICFTKGPGIGAPLNSVALCARMLSLIHKKPLVAVNHCIGHIEMGREITGAQNPVVLYVSGGNTQVIAYSEKKYRIFGETLDIAIGNCLDRFARIIGLSNAPSPGYNIMQEAKKGKRFIELPYTVKGMDCSFSGLLSGVEAAATELLDPKNPSSVTKQDLCYSLQETGFAMLVEITERAMAHIRADSVLIVGGVGCNERLQQMMAEMSSDRGADVFSTDERFCIDNGIMIAQAGLLAYKTGDRCAVAESTITQRYRTDDVYISWRD O94639 ZRT1_SCHPO MOD_RES 234; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 237; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16D10.06; CHAIN 1..408; /note="Zinc-regulated transporter 1"; /id="PRO_0000316574" MSLNNLSNSYNQYLAQESHQILRHLFLNKQYSPLVKRDDDSSATVTCGGDANEFNEYGHLGYRIGAIFVILATSLIGMNLPLVLSKITKNRPNVYIEYLYLFARYFGSGVILATAFIHLLAPACNKLYDPCLDDLFGGYDWAPGICLISCWFILLLEVLLNRYVEWRFGMEIGDHHGPTLGAKQHSHSHEDGAHGVHEHPVYDIEECADGVEHECVKDDLEEVKLEPYTNTDSTDLTTKEEARSFLLKQQLTAFIILESSIILHSVIIGLTTAVSGEEFKTLFPVIIFHQAFEGCGLGSRLAGMAWGPKTAWVPWVLGVIYSLVTPIGMAAGLGVREHWDPLAHGSYAAQGVLDAISSGILVYAGLVELLAHDFLFSPERERNWYKLIYLLACSMAGTGVMALLGKWA O94642 TAD2_SCHPO ACT_SITE 268; /note="Proton donor"; /evidence="ECO:0000250" BINDING 266; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 296; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 299; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O67050}; SPBC16D10.10; STRAND 8..15; /evidence="ECO:0007829|PDB:7EEY"; STRAND 39..45; /evidence="ECO:0007829|PDB:7EEY"; STRAND 80..83; /evidence="ECO:0007829|PDB:7EEY"; STRAND 89..91; /evidence="ECO:0007829|PDB:7EEY"; STRAND 94..96; /evidence="ECO:0007829|PDB:7EEY"; STRAND 98..104; /evidence="ECO:0007829|PDB:7EEY"; STRAND 117..123; /evidence="ECO:0007829|PDB:7EEY"; STRAND 171..176; /evidence="ECO:0007829|PDB:7EEY" HELIX 21..35; /evidence="ECO:0007829|PDB:7EEY"; HELIX 46..49; /evidence="ECO:0007829|PDB:7EEY"; HELIX 60..62; /evidence="ECO:0007829|PDB:7EEY"; HELIX 65..76; /evidence="ECO:0007829|PDB:7EEY"; HELIX 110..115; /evidence="ECO:0007829|PDB:7EEY"; HELIX 126..137; /evidence="ECO:0007829|PDB:7EEY"; HELIX 145..154; /evidence="ECO:0007829|PDB:7EEY"; HELIX 156..163; /evidence="ECO:0007829|PDB:7EEY"; HELIX 165..170; /evidence="ECO:0007829|PDB:7EEY"; HELIX 183..199; /evidence="ECO:0007829|PDB:7EEY" TURN 105..108; /evidence="ECO:0007829|PDB:7EEY"; TURN 138..141; /evidence="ECO:0007829|PDB:7EEY" CHAIN 1..389; /note="tRNA-specific adenosine deaminase subunit tad2"; /id="PRO_0000310823" MAGDSVKSAIIGIAGGPFSGKTQLCEQLLERLKSSAPSTFSKLIHLTSFLYPNSVDRYALSSYDIEAFKKVLSLISQGAEKICLPDGSCIKLPVDQNRIILIEGYYLLLPELLPYYTSKIFVYEDADTRLERCVLQRVKAEKGDLTKVLNDFVTLSKPAYDSSIHPTRENADIILPQKENIDTALLFVSQHLQDILAEMNKTSSSNTVKYDTQHETYMKLAHEILNLGPYFVIQPRSPGSCVFVYKGEVIGRGFNETNCSLSGIRHAELIAIEKILEHYPASVFKETTLYVTVEPCLMCAAALKQLHIKAVYFGCGNDRFGGCGSVFSINKDQSIDPSYPVYPGLFYSEAVMLMREFYVQENVKAPVPQSKKQRVLKREVKSLDLSRFK O94643 CENPU_SCHPO SPBC21.01; CHAIN 1..441; /note="Inner kinetochore subunit mis17"; /id="PRO_0000116523" MENNSHNVDERRAARMRGAERYKIQNVEFSLDQNLLANLESSTSSSTRSSPASNQQNLEIVSQSEAYHKISDLDDSTSIFSISDQENILERRISEEVVRENSVSSIENVSSSAVARETQSSANILVKDNHFFSHKQKKIQRESIPFHKRDNIETSDAYSSSILENSPPNKVQRLSSLDSSQDSFQEEHPGNVTGTTFSSQAPEERIASPISTSSPESLTNQSSSLQSSLQTSSMAPRNLLDQSTEKDIVVGASDELVRIELTKLSKEAGGSKTLNELDAVQQFFQEFIKENEPLEPYVVKVKNAFVEQVSIRLLELIDLLDANRILSTACKKAANEKLAVQRDLSKLREDRLSVQRKKIQLRNEYIKLSHQQNFLDDIDDFFSQCETVKNELENVTTTPNSTEAFSEINEYASALSKNYGLESQLVELQSLLTQFYQKFLS O94646 MED8_SCHPO SPBC21.04; STRAND 74..78; /evidence="ECO:0007829|PDB:4H63"; STRAND 154..157; /evidence="ECO:0007829|PDB:5N9J" HELIX 4..37; /evidence="ECO:0007829|PDB:4H63"; HELIX 43..66; /evidence="ECO:0007829|PDB:4H63"; HELIX 68..72; /evidence="ECO:0007829|PDB:4H63"; HELIX 88..94; /evidence="ECO:0007829|PDB:4H63"; HELIX 101..117; /evidence="ECO:0007829|PDB:4H63"; HELIX 130..147; /evidence="ECO:0007829|PDB:4H63"; HELIX 148..150; /evidence="ECO:0007829|PDB:4H63"; HELIX 160..165; /evidence="ECO:0007829|PDB:5N9J"; HELIX 184..197; /evidence="ECO:0007829|PDB:3C0T" TURN 84..86; /evidence="ECO:0007829|PDB:4H63" CHAIN 1..200; /note="Mediator of RNA polymerase II transcription subunit 8"; /id="PRO_0000096396" MEDISTEKTVESLEAIRHRIAQIVQSLTHFLAILHQSESLSPWPTIHKNFNILLSQIHSLSNNLAAHSHTLQTTSIYPSLEFPVKEQEPLLTTLLRTKALPEVEEWEANTLQEYEASISSQPKKKEANDAYQKDQLWDQARIIFMEERENYSWFDFVTRRQESEGEFVSQRQLEIDRATEEQNANQMLTDILSFMKSGKR O94647 PPK24_SCHPO ACT_SITE 256; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 126..134; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 153; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC21.07c; CHAIN ?..461; /note="Serine/threonine-protein kinase ppk24, mitochondrial"; /id="PRO_0000256823" MTNYPFFRQGTIFVDNSAIQRNSENKNSLSIENIFGRFPKEFFQFFSINVSKSTTKKSSVVIKPSTITAPWLENEYLDSNTSLLSVHSIQPSFIGMSDFAIGLDPSLKRILPEIRFRLDFQHLKSIAKGATSTIKVVTHRDKITDAKIYYAAKVYRKTKTSHKKRLNTMVYFLREWSIQPKLDHPNILKVICPCVTLTSVFNKSAGFCLVQEYCPQGDLFKQIEEKVLTLEDKCCYLKQILQAVAYLQSQRIAHRDLKPENILIGRDGLLKLTDFGTSEIVGNPGDNESIRFVSGAVGSLAYLAPEAFHENEYCGLLADRWSCGILLKVLFTGYFPFKTSVKTDLYYSKYMSILTDTCGISSTDESSFQTEVIKQIPTLQPLRYIPEGAKKIILSLLNPDSQNRPSLDSILGTAWVRKLDCCSNFSTDHENKSLQEVDFDASKPITRKSLIPRIHNHQTLV O94650 HUB1_SCHPO SPBC31E1.03; CHAIN 1..73; /note="Ubiquitin-like modifier hub1"; /id="PRO_0000114878" MIEVLCNDRLGKKVRVKCMPDDTVGDFKKLVAAQTGTDPRRIVLKKWHSVFKDNITLADYEIHDGMSLEMYYS O94651 PEP12_SCHPO MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC31E1.04; CHAIN 1..263; /note="Syntaxin pep12"; /id="PRO_0000210270" MSFVDLEQGRHKIEQNGDFPALASSIAQEIHALRGNTAAIHRYLVNNLTKNLHEVLEQSRELSQKVRSDLVRLANIKDTKYGEEASSFALSKLTRDFNTVLAELQRVQQKCAQQESDSVAAAQAALNQDVGQHFIEEEERNVSLSNNSSGQRQPLTESKISNSQLEYQQRLINERQGEIENLTQGINELNEIFRDLSTIINEQGELVTNIEYNVGNTSTNTKNASRQLQIANEHSRKARKRSFCFLVILVVILGVILTALIMG O94653 BMS1_SCHPO BINDING 81..88; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 438; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 442; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 464; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 474; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 476; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 546; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC31E1.06; CHAIN 1..1121; /note="Ribosome biogenesis protein bms1"; /id="PRO_0000195005" MDEKKGHYAKHSGPKAEKKKLKKVSDGSASNNPKAFAVASAGRMARQAMRTADISQKKLHVPMVDRTPDEAPPPVIVAVMGPPGTGKSTLIKSLVRRYSKYTISQITGPITVVAGKKRRITFLECPNDLSSMIDVAKIADLVLLLIDANFGFEMETMEFLNILAPHGMPRIMGVLTHLDLFKKTSTLREAKKRLKHRFWTELYQGAKLFYLSGVLNGRYPDREILNLSRFISVMKFRPLRWRNQHPYLLADRMEDLTLPVDIEQNPKVGRKITLYGYLHGTNLPKHDASVHIPGVGDFVTSDVSSLEDPCPPPDADKVRRRRLSEKQKLIYGPMADIGGILFDKDRVYIEVPTSNFSKDENSEAGFGERMVMQLQEAQQPLGVDGNSGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGLINQELIKEDEGAFDDSDVNSADENEDVDFTGKIGAINNEDESDNEEVAFADSDSDLGGQFDDEDSNLRWKEGLASKAALAYSQSGKRRRNIQKIFYDESLSPKDAYAEYKGESAKSSESDLVVSDDEEDFFKVSKVANESISSNHEKLMESESDRLSKKWENPQLLAQLKSRFITGSLLDSIEGQEEVSQDDEEGDFEDLEDEENSSDNEMEESSGSSVTAENEESADEVDFQTEREENARKKEELRLRFEEEDRGDPEKKDVDWYTEEKEKIARQLVINREAFEDMDPESRAEIEGYRAGTYVRIVINDVPFEFVEHFDSRYPVVVGGLLPNEQRYGLVQVRIKRHRWHKKILKTNDPLIFSMGWRRFQSIPVYSISDSRTRNRMLKYTPEHMHCFGTFYGPFVAPNSGFCAVQSVANSFAKAGSFRIAATGSVLNIDQSTDIVKKLKLTGVPYKIFKNTAFIKKMFSSPLEVAKFEGANIRTVSGIRGQVKKAVDQEHGHFRATFEDKILMSDIVFLRAWYPVQVRKFCTMVTNLLETDKTEWNGMRLTGEVRHELGLKTPLRPNSQYQEIVRPSRHFNPLKVPASLQAQLPFNSRQKALRPRSKPTYMQKRTVLLNAEERKVRDLLQKVMTLHTDKEAKRKAKKAAEHERYHKRMQKEEQAYIEKKREEKAEWFAQHGKRLRQDGNSSGSGKRSKN O94656 ATG16_SCHPO SPBC405.05; CHAIN 1..143; /note="Autophagy protein 16"; /id="PRO_0000358934" MELIKKIQDRDAAEKAYYDVIEPYSELLEFSFHKEFVSEEKVTQRTASSDSLNTIASENNDENVINLEEFRQLKRNCDLYQRNLQKLQLLFKQQSQKNTLLEKQLSLQTELNQEKDKRVKILQDELWALQLEVAALERKSPNA O94659 NOG1_SCHPO BINDING 175..182; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 221..225; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 289..292; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" MOD_RES 468; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 471; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC651.01c; STRAND 166..168; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 170..173; /evidence="ECO:0007829|PDB:8ETC"; STRAND 197..199; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 206..212; /evidence="ECO:0007829|PDB:8ETC"; STRAND 215..221; /evidence="ECO:0007829|PDB:8ETC"; STRAND 248..251; /evidence="ECO:0007829|PDB:8ETC"; STRAND 254..258; /evidence="ECO:0007829|PDB:8ETC"; STRAND 287..289; /evidence="ECO:0007829|PDB:8ETC"; STRAND 314..317; /evidence="ECO:0007829|PDB:8ETC"; STRAND 318..320; /evidence="ECO:0007829|PDB:8ETG"; STRAND 393..395; /evidence="ECO:0007829|PDB:8ETC"; STRAND 422..424; /evidence="ECO:0007829|PDB:8EUP"; STRAND 436..438; /evidence="ECO:0007829|PDB:8EUP"; STRAND 439..441; /evidence="ECO:0007829|PDB:8EUY" HELIX 6..8; /evidence="ECO:0007829|PDB:8ETC"; HELIX 15..29; /evidence="ECO:0007829|PDB:8EUY"; HELIX 41..63; /evidence="ECO:0007829|PDB:8EUY"; HELIX 77..87; /evidence="ECO:0007829|PDB:8ETC"; HELIX 104..118; /evidence="ECO:0007829|PDB:8EUY"; HELIX 123..142; /evidence="ECO:0007829|PDB:8EUY"; HELIX 181..188; /evidence="ECO:0007829|PDB:8ETC"; HELIX 235..245; /evidence="ECO:0007829|PDB:8ETC"; HELIX 265..279; /evidence="ECO:0007829|PDB:8ETC"; HELIX 306..311; /evidence="ECO:0007829|PDB:8ETC"; HELIX 329..343; /evidence="ECO:0007829|PDB:8ETC"; HELIX 380..383; /evidence="ECO:0007829|PDB:8ETC"; HELIX 399..405; /evidence="ECO:0007829|PDB:8ETC"; HELIX 425..429; /evidence="ECO:0007829|PDB:8EUY"; HELIX 442..444; /evidence="ECO:0007829|PDB:8EUY"; HELIX 449..464; /evidence="ECO:0007829|PDB:8ETC" TURN 72..74; /evidence="ECO:0007829|PDB:8ETC"; TURN 157..160; /evidence="ECO:0007829|PDB:8EV3"; TURN 323..326; /evidence="ECO:0007829|PDB:8ETC"; TURN 409..411; /evidence="ECO:0007829|PDB:8ETC"; TURN 416..418; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..642; /note="Probable nucleolar GTP-binding protein 1"; /id="PRO_0000195034" MATAVFKNITPIPDVNTFLDVVLSRTQRKTPTVIRSGFKISRIRGFYGRKVKFTQDTITEKLDSILQEFPKLNDIHPFHADLLNILYDRDHLKIALSQLSTAKHLVENVARDYIRLLKYGDSLYRCKQLKRAALGRMATIIKRQKSSLEFLEQVRQHLSRLPAIDPNTRTLLVCGYPNVGKSSFMNKVTRAQVDVQPYAFTTKSLFVGHFDYKYLRWQVIDTPGILDHPLEQMNTIEMQSITAMAHLRSAVLYFMDLSEMCGYSVAAQVKLYHSIKPLFANKVTILVLNKIDAMRPEDLDQKNQELLQTIIDDGNVKVVQTSCVQDIGVMDVRTTACEALLAARVEQKLKGSRVNNVLNRIHLAEPAARDEVARPACIPDSVKTRRAYDANDPNRRILARDIEAANGGAGVYNVELRDKYILQDPSWKYDRMPELLDGKNVADFVDPEIEAKLLALDEEEERLEREGYYDSDQEIEDADEEEVLEKASRIREKNKLTMLAARQKKIKNRPVLPRTAGIRTLDELQSSLQSAGLPSDSIEERARSRARTAAANEMADGSGVDLLMNEGEEIRSKSIAPRSQSNRRESGVHAEGARSYADRLARVKQIHRNRMARASESDRHVIAAKPKHLLSGKRGNGKTQRR O94663 SNF8_SCHPO SPBC651.05c; CHAIN 1..252; /note="Vacuolar-sorting protein dot2"; /id="PRO_0000362144" MRKRIGIGALNDDEYLKQYEEVGNELIEQQSDEIASQLSTFQEALKTFAREHATEIKQNSQFRNTFVKLALKIGLDPFVSGSDESAWAAVGMNEFYYQVAVRVIEVCYATQMENGGLLSVSQVCRFLNEENEAFGHEWLRETDVVRAVDSLAPLGPGFVLEKIAGKQYIRSLPLELNTDQNVVLEAVEILGYVTISILRDNYAWERSRCIQVLNDLVSKSLLWIDSQGVEMAYWGASNLIDDQAQRFLYENF O94667 RTF1_SCHPO MOD_RES 197; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 502; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 506; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC651.09c; CHAIN 1..560; /note="RNA polymerase-associated protein C651.09c"; /id="PRO_0000315631" MADFQDELLALAGIDDSDVASNRKRAHDDLDDVLSSSSDEDNNENVGQDYAEESGGEGNEKSEDEFEEKFKNPYRLEGKFKDEADRAKIMAMTEIERESILFEREEEISKLMERRELAIRLHQQNAQYMAQSTRRSTRDKPLTSAAAGKRDKLTELKKRRQERSARSVSERTRKRSPVSDYEEQNESEKSEEEEGYSPSYAEEKVEQVSKDNASANLYDLNAIRLGRKHVAEYMYHPIFESTVTGCFVRVKIGERDGQGVYRLCQVKGILESRKPYRVDGVLTKVSLECFHGRSKRVFDVNVLSNEPFSDHDFQRWHHQMMEDKLSMPSKNFVQRKLNDLRDMSKYVLSEKEVSDIINRKKELSRVPSNIAAEKTRLRQRRQAAYVAGNAELVKEIDDQLNTLEELSMGSNQNSNSAMDQLAKVNERNRRRNHTEIRLAEQRMNEERRRLSAAATATPMSAPTSVLTGTSPQPSPSLSTSIMSTPKLNPSESVVVASEKASSPDLSPKLLPSESQIFDEGIAVTQTPNTLEDKDFKLHEKAVHGIDDIIATVDFGIDINI O94668 NSE5_SCHPO SPBC651.10; CHAIN 1..388; /note="Non-structural maintenance of chromosome element 5"; /id="PRO_0000116527" MNSALKAIIELCIEEDLLPKSLDVLEYLLSTTSIPIPACYIRMCITLLVHPEYPTSSNIQESCNWILQQVVENRSKINFDAWSFENDLSDNDMPKENYLKIFSNQCLFTQDVDYWDLIAYMSSRPPDLERWMSLMDIWLRILEIDAEENGSALMKKYMGEDLCELQDAIRICFSCFTLPQQTMESPFATSMSKAPAKTESRGSNSFEGTSRLANLGAKLLCLIWAMLPKGRFFVVHLTDAFHFLSKLDERFSKLNAKQQDLFFGNLGASNLRYCLSQYILMKGIGIGINIRHTRCEFTKQLTQLLPTSLPKNKIRQKLHLRAWVSFLGSALRESDRNFDKELFYTTLKQLYTMYQQTELVGIDRPMAILKDMLVLLDISKKLSLDKIV O94671 DHOM_SCHPO ACT_SITE 231; /note="Proton donor"; /evidence="ECO:0000255|PIRSR:PIRSR036497-1" BINDING 17; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 18; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 18; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 18; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:O58802"; BINDING 67; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:O58802"; BINDING 99; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 99; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 99; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:O58802"; BINDING 123; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 123; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:O58802"; BINDING 150; /ligand="Na(+)"; /ligand_id="ChEBI:CHEBI:29101"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 153; /ligand="Na(+)"; /ligand_id="ChEBI:CHEBI:29101"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 155; /ligand="Na(+)"; /ligand_id="ChEBI:CHEBI:29101"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 157; /ligand="Na(+)"; /ligand_id="ChEBI:CHEBI:29101"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 213; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 216; /ligand="L-homoserine"; /ligand_id="ChEBI:CHEBI:57476"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 216; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 227; /ligand="L-homoserine"; /ligand_id="ChEBI:CHEBI:57476"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 349; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P31116"; BINDING 349; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:F9VNG5"; BINDING 349; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:O58802" CATALYTIC ACTIVITY: Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3; Evidence={ECO:0000250|UniProtKB:P31116}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15763; Evidence={ECO:0000250|UniProtKB:P31116}; CATALYTIC ACTIVITY: Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3; Evidence={ECO:0000250|UniProtKB:P31116}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15759; Evidence={ECO:0000250|UniProtKB:P31116}; COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000250|UniProtKB:P31116}; Note=A sodium ion is seen in the structure; a metal ion may subtly affect the relative position of the nucleotide-binding region to influence enzyme activity, and could increase the stability of the enzyme. {ECO:0000250|UniProtKB:P31116}; MOD_RES 201; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC776.03; CHAIN 1..376; /note="Homoserine dehydrogenase"; /id="PRO_0000066706" MSASRTNVNVAIVGTGNIGGELLNQIKGFNENASTNGTTSFNVVAISSMEGHYVSKDYQPINLSEWKNLTSQNQGAYSLDALVDFLAKSPLPAILVDNTASEAIAQSYPKFLSKKINIATPNKKAFSASNDVYQNIIKASKESGALLMHEASVGAGLPIISTLKELIATGDEIIKIEGIFSGTLSYIFNVWSPNGKKGTASFSDIVKIAKQNGYTEPDPRDDLNGMDVARKVTILSRIAGVHVESASSFPVKSLIPEPLKSAVNAEEFLAGLPNFDSEFASMREEAEKEGKVVRFVGEADVANKTTLVKLEKYDASHPFANLQSSDNIISFTTKRYHTRPLVVIGAGAGAAVTAAGVLGDMIKIMSQVRASDAPSA O94672 SC232_SCHPO BINDING 56; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 60; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" MOD_RES 565; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 566; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC776.04; CHAIN 1..765; /note="Protein transport protein sec23-2"; /id="PRO_0000295472" MNFEDIEDQDGIRLSWNTFSATPAENARAVIPIAAMYTPLHENERMTIEQYDPVACRAPCRAVLNPYCHVDLRARFWICPFCFQRNPLPAQYSDISSNSLPLELLSQSTTMEYVLSKPVKSPPVFLFVMDTAVDESELTALKDAVIVSLSLLPPDAIVGLITYGSLIQVHEIGFEAMPKSYVFQPAADYSTMKLQQLLALSGNQIRSSSSKAKISGTGITLNLGAASRFLMPVQKCEMHLLNILEQLQPDCLEVPAGQRQLRCTGAAVKIASDLLGIAFPKCGSRIELFCGGPCTVGLGQVVSTELKEPMRSHSEIANDKAKHFKKSKKFYSSLAERLSNQGHALDLFAGCLDQVGIMEMENLVNNTGGAIVLSDSFTTSIFKQSFQRLFSVDASGYLKMGFMANLEVLTSKGLTICGMIGNGVGENKKGTNISDTQIGISKTNSWKMAAISPKSSYALYFDLGKEMGNPNSQRPTQAFIQFLTYYQHSSGTYRLRVTTISRSFITGNAKSISESFDQEAAAAIVARMALFKCQTEDEMSVTRWIDRNLIRLCQHFADYRKEDPSSFRLLPNFTLYPQFIFHLRRSPFLHIFNNSPDETSFYRHMLNVADVNDSLIMIQPTLQSYSFNEPEGVPVLLDSVSIKPDVILLLDTYFHILIFHGSTIAQWRNAGYQEQPEYVNLKELLLAPRLEVTELLADRFPIPRFIVCDQGGSQARFLLSRINPSVSFNKSSQFSPMSKDSETVLTDDVNLQKFMDHLRKMAVIS O94673 GPC1_SCHPO CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycerol 3-phosphocholine = a 1-acyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:58476, ChEBI:CHEBI:16870, ChEBI:CHEBI:57287, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; Evidence={ECO:0000250|UniProtKB:P48236}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycero-3-phosphoethanolamine = a monoacyl-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:62108, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:67274, ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:P48236}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + sn-glycero-3-phosphoethanolamine = (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:62104, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:143890, ChEBI:CHEBI:145434; Evidence={ECO:0000250|UniProtKB:P48236}; SPBC776.05; CHAIN 1..403; /note="Glycerophosphocholine acyltransferase 1"; /id="PRO_0000343219" CARBOHYD 240; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MDHLEFDENTDSEYSIFEEDNDYGLHGLDDSVGFTDLFDAPNIYRVYSWLHKHYNQKKGQLKHGVSRQKNKLQPIHKQINYETDKLKERLGKSIDKFQEQWNSGKVVRFRDKLSFALGVSTCILTALLVGMAPESMHLWYTIQLFVYLPLRYYTYQRKGYEYFIADFCYWGNILLLVYIWIFPESRRLFILSYSISYGTLAWSVVAWRNSLLFHSIDKITSLFIHFFPPLVLHTIVHLTNKSYLKDRFPAVLKVKKIDLLSSVEIASFFYALWQIWYYFFIQVGKQKQIQEGRPTSFTWLSKAYSKTKLGRAVAKLPQNLQPFVFMIIQYLYSITTMLPCSLWYNNKLYSTAFLALIFGWSVWNGASYYIDVFGRRFQKELEALRQQLAETPTNSGSSSALSR O94681 ODO2_SCHPO ACT_SITE 424; /evidence="ECO:0000250"; ACT_SITE 428; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 1 lipoyl cofactor covalently.; TRANSIT 1..?; /note="Mitochondrion" MOD_RES 83; /note="N6-lipoyllysine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" SPBC776.15c; CHAIN ?..452; /note="Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial"; /id="PRO_0000020477" MTSYGNGFRMMAKCLLSLRSGYSVTAPVSKSMANVLWARYASTRIKTPPFPESITEGTLAQWLKQPGEYVNKDEEIASVETDKIDAPVTAPDAGVLKEQLVKEGDTITIDQDIAVIDTSAAPPEGGSAGPKKDEVKTADADAAKDLSTPQDSSKPIEEKPMPDLGAEQKESAPSSTKPAPDAKEPEFSSPKPKPAKSEPVKQSKPKATETARPSSFSRNEDRVKMNRMRLRIAERLKESQNRAASLTTFNECDMSAVVALRKKYKDEILKETGVKIGFMSFFSKACTQAMKQIPAINGSIEGEGKGDTLVYRDFCDLSIAVATPKGLVTPVIRNAESMSLLEIESAIATLGSKARAGKLAIEDMASGTFTISNGGIFGSLYGTPIINLPQTAVLGLHAIKERPVVINGQVVPRPMMYLALTYDHRMVDGREAVTFLRLVKEYIEDPAKMLLV O94682 MIS20_SCHPO SPBC776.16; CHAIN 1..253; /note="CENP-A recruiting complex protein mis20"; /id="PRO_0000304095" MLEQSESHAFINNAPKEDRIQVKFEQLFESLPLPLRAEEALSKLRHDSARLMILKTSDPTLNMSTYSIEDSPMGFECLKYNLSDNNKLLSQNNYRLPDYLEEDEIVSYTFSKTGPTTSKNKHPSHSNTIRSPPYKVKKESCHTEINNVSNVSTESINVIDASRGYSPYTSVDSLSVSKNRSFISLEESASNQYDAAEAFYFNADSSSPLRKLSPIELPVTPIRRKTPTINPNSELKRLQTFGKLILHKGSRRR O94688 APC15_SCHPO SPBC83.04; CHAIN 1..136; /note="Anaphase-promoting complex subunit 15"; /id="PRO_0000237685" MSFMSLMANTAHQLWYPTSFPSMKELEKEEVRLETQELAIKQFGFRTIRPIGLNRSMQEQLDLEEQEREEANQDTELDEEELGSGSFPEEGEMDDMDGDNEEVEDHDIEEVDLDADITNADASEFYEDISEYGFQN O94692 RUVB2_SCHPO BINDING 72..79; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPBC83.08; CHAIN 1..465; /note="RuvB-like helicase 2"; /id="PRO_0000165672" MSISVTSHNDVSKLERIGAHSHIKGIGLNDNLEPKESSQGMVGQVKARRAAGVILKMIQEGRIAGRAILMAGPPSTGKTAIAMGMAQSLGSDTPFVTLSASEVYSLEMSKTEALLQALRKSIGVRIKEETEIIEGEVVEVQIDRSITGGNKQGKLTIRSTDMETVYDLGTKMIDSLTKEKVLAGDVISIDKSVGRVTKLGRSFSRARDYDAMGADTRFVQCPQGEIQKRKEVVHTVSLHDIDVINSRTQGFLALFSGDTGEIKPEVREQINTKVSEWREEGKAEIVPGVLFVDEVHMLDIECFSFFNRALEDDLAPIVIMASNRGITRIRGTNYRSPHGIPVDLLDRMLIISTLPYSHEEVKEILKIRCQEEDVDMEPSALDYLSTIGQETSLRYALLLISSSNQVALKRKSATIEESDIRRVYELFLDQKRSVEYLEEYGKNYITENEWSASGAQDNAVAMQED O94697 RFC5_SCHPO SPBC83.14c; CHAIN 1..358; /note="Replication factor C subunit 5"; /id="PRO_0000121764" MLWLDQYRPKTLASLDYHKQLSERLISLSSTNEFPHLLVYGPSGAGKKTRVVAILRELYGPGSEKLKIDQRTFLTPSSKKLQINIVSSLHHLEITPSDVGNYDRVIMQELLKDVAQSAQVDLQAKKIFKVVVINVADELTRDAQAALRRTMEKYSNNIRLILIANSTSKIIEPIRSRTLMVRVAAPTPEEIILVMSKILTAQGLEAPDSLLNNIANNCDRNLRKAILLLETVHAKSPGNKQLIDTGAQLPLPDWQTFIQQVGDSMLQEQSPARILAVRSMLYDLLSHCIPPTTILKELLSFFLSKVDTKLHPYLIQAAANYEHRTRMGNKSIFHLEAFVAYFMKVYAMLQLGMELPSY O94703 RPA12_SCHPO BINDING 10; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 13; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 30; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10145"; BINDING 80; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 83; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 108; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 111; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472" SPCC1259.03; CHAIN 1..119; /note="DNA-directed RNA polymerase I subunit RPA12"; /id="PRO_0000121464" MSAIGSLIFCSECGNLLESTTAQWTTCDQCQSVYPSEQFANLVVETKSSASAFPSALKLKHSIVQVESQKEEAATIEEKCPKCGNDHMTFHTLQLRSADEGSTVFYECPRCAYKFSTNN O94704 IEC3_SCHPO SPCC1259.04; CHAIN 1..168; /note="INO80 complex subunit 3"; /id="PRO_0000304000" MASVKSFKRKYLKLRKSFDSVVLETEEIEQKIAEISEVYRRILLENAHLNDLLIDMNSTVLPTPPASPPGSPYWEAKPVSHTVFLESPSDVFTLEKPIASTHRWLSKLTALSKSTNSTLSTPKSFHSPLQSRGISPSSAQSSAAVSSSRKQKRKRTSEGPSERRARKK O94716 NKP1_SCHPO MOD_RES 189; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 191; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1393.04; CHAIN 1..233; /note="Inner kinetochore subunit fta4"; /id="PRO_0000290640" MDIYEHKKSFMERQIRLLNRPMRPPKDWKLPLKSGQLSESVVETVFQRLQLRIQKHAKLNYSHQATQHVAAQIRKLYEQNSAIEDITFLNPLFYGEIDLSNLDSVKSLPHPWPFQKESRPVEKDEEQEKFNRLTGELLGLLTTLSELEQERSELEQIEKMLEPFEDGPSSIHTNMWKKNPELISTLNSTNTMVAKINSLLRGVSFPSLNNDNQEASLEDEIRSQLFEKTISDD O94717 ERS1_SCHPO SPCC1393.05; CHAIN 1..956; /note="RNA-silencing factor ers1"; /id="PRO_0000303939" MGKVSANNQSGFFKFYIDTALLLNAEFISSFTNCINSEYNGKVKISYSSSSQQFKVIVYEEHKREAFSLFEEIVQKLKRESTVYKKPRLDIHPFGQLHYDFTTLLNFQRYLDLGYGIEDVKIKENEDIVKSKVGKKPTSSDFYIPCLIKPKIITPFEWEGNFKQVIYSPTVYNGSFKRLFYLPDNNDLLKEFAHATNTKYKASLKDNKIVVLANNDQDINAMLEKMKHIENLVSQKVYEYPEETLVYAGKIAPCQLKFLKLKFENEILYTAMHTTSIFKSVFNILGSFYTMRLLRNKHDGDSYELVPVFAKNPSKTPPCNDNFKIFSDDIKLIGCKIFAGVSLNFSSPKPAHRFYELNKTSSNLSIPVLQKPSNFHSSSTELSDNSIHQGRRAVDPVVNQNNPSNFEEMIMNKLNKLPTIDKQILGTSSLTHFQDKTTAIEHSINKSNSKQPPRFKFQLPPRPTSNTLPLEPEEELVTRYSVSSDGNTVDEAITKQSQTFQLVNSNEFNEVNANDVHKSLRQNCAKLDFDDSKSKNLLSVECLELDKGSDCSTPKSGSLTPSIDMKFLRLQDEKMDDLGDNYYTILMSSNPVSSYGVGSLYLFQPKIVCSEKYINHEEIDNMNLKSLHRWLSRSLHVLQSFSGEIELNLEFGVILYPNISSDVSACSHGFMNIYKDLNLPRSYFADCITKSVSNIDSLLNTPVKILFGRTEYTYPLIEHEVLDSKNYFVFKGSLLFTDDKRNKTEDSTVFFSMICSSKLDQFAFYKDSKQSSTCTINFPLALWDSRLRIETKVPLNDAILTEFSKSIRFRNVNKDLLLVFGNMEDRVIIHSVTRINENSVPFNKNLLPHSLEFILKCSKVKSYDISPSSINSKEAFVCLDRSKESKPIESCFSLSIQSVYMQSQFKYNNSIRAGETAPWKLANKQFIGGAITENVSDLYTAAIIMVNQLGGIHPTI O94722 CTR4_SCHPO MOD_RES 279; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1393.10; CHAIN 1..289; /note="Copper transport protein ctr4"; /id="PRO_0000195048" MSFFSAAKQSLGNSLIKLGTSMAQNSQGPVDDSSLSQLENLLPPLQILTARAAMAAMNMSNDTSMSGMNMTNSTTPMSGMNMTNSTTSMSGMNMSNSTTSMSGMNMTNTTTTAKASSCKLSMYWNWYTIDACFITKHWHITSKHMFVGSIFGIIFMMMALELVRRGQREFDRWCVRRFSPASNSCCHSGAPVHSGPSMALRIFLHFLRSCFYLVQYIVAYIAMLLAMYYNGYVILFLFCGTFFGYFLFGADTISTKASSSVQTKTIVQVADEKHEHDSSQYSDTTPTTE O94725 ART1B_SCHPO BINDING 252..253; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 252; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 253; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 290; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 367..371; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 405; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371" CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate; Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721, ChEBI:CHEBI:43474, ChEBI:CHEBI:138881; Evidence={ECO:0000250|UniProtKB:Q04371}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; Evidence={ECO:0000250|UniProtKB:Q04371}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q04371}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250|UniProtKB:Q04371}; SPCC1393.13; STRAND 227..230; /evidence="ECO:0007829|PDB:7T7N"; STRAND 244..250; /evidence="ECO:0007829|PDB:7T7N"; STRAND 273..280; /evidence="ECO:0007829|PDB:7T7N"; STRAND 282..284; /evidence="ECO:0007829|PDB:7T7N"; STRAND 327..330; /evidence="ECO:0007829|PDB:7T7N"; STRAND 360..366; /evidence="ECO:0007829|PDB:7T7N"; STRAND 398..403; /evidence="ECO:0007829|PDB:7T7N"; STRAND 433..439; /evidence="ECO:0007829|PDB:7T7N" HELIX 21..27; /evidence="ECO:0007829|PDB:7T7N"; HELIX 29..50; /evidence="ECO:0007829|PDB:7T7N"; HELIX 58..78; /evidence="ECO:0007829|PDB:7T7N"; HELIX 93..103; /evidence="ECO:0007829|PDB:7T7N"; HELIX 108..110; /evidence="ECO:0007829|PDB:7T7N"; HELIX 113..129; /evidence="ECO:0007829|PDB:7T7N"; HELIX 141..149; /evidence="ECO:0007829|PDB:7T7N"; HELIX 152..162; /evidence="ECO:0007829|PDB:7T7N"; HELIX 165..175; /evidence="ECO:0007829|PDB:7T7N"; HELIX 178..194; /evidence="ECO:0007829|PDB:7T7N"; HELIX 201..204; /evidence="ECO:0007829|PDB:7T7N"; HELIX 208..211; /evidence="ECO:0007829|PDB:7T7N"; HELIX 214..223; /evidence="ECO:0007829|PDB:7T7N"; HELIX 232..239; /evidence="ECO:0007829|PDB:7T7N"; HELIX 256..270; /evidence="ECO:0007829|PDB:7T7N"; HELIX 295..306; /evidence="ECO:0007829|PDB:7T7N"; HELIX 310..324; /evidence="ECO:0007829|PDB:7T7N"; HELIX 334..337; /evidence="ECO:0007829|PDB:7T7N"; HELIX 342..344; /evidence="ECO:0007829|PDB:7T7N"; HELIX 345..348; /evidence="ECO:0007829|PDB:7T7N"; HELIX 350..356; /evidence="ECO:0007829|PDB:7T7N"; HELIX 367..373; /evidence="ECO:0007829|PDB:7T7N"; HELIX 385..388; /evidence="ECO:0007829|PDB:7T7N"; HELIX 390..392; /evidence="ECO:0007829|PDB:7T7N"; HELIX 416..421; /evidence="ECO:0007829|PDB:7T7N"; HELIX 427..429; /evidence="ECO:0007829|PDB:7T7N" TURN 132..136; /evidence="ECO:0007829|PDB:7T7N"; TURN 224..226; /evidence="ECO:0007829|PDB:7T7N"; TURN 287..289; /evidence="ECO:0007829|PDB:7T7N"; TURN 374..376; /evidence="ECO:0007829|PDB:7T7N"; TURN 393..395; /evidence="ECO:0007829|PDB:7T7N" CHAIN 1..442; /note="Damage-control phosphatase SPCC1393.13"; /id="PRO_0000230802" MGLKLLHPPKPYAMTSDPESYASVCVMKKWPIIATNVIDEVSRNISKALEAGMSDKAAYVTQGKEIISLLNQLKYDLQHNRPLKPLVGQGPDIDDYNEELEQVGPLTWGDAPWLYAGCYFYRIMSLFFQARSEWNRHDPFFEQKDFTLRSSKSAIEEFAKRYVHLNSELASIQENKDDKAAYMIFVEMAEISLWGNAIDLGLLVNATYEQLQSLQGQKAVEESQKNILVNDFPKIWSKLSKVRHGRIDFVLDNAGFELFVDLLFATYLLKTEIAETIILHPKDVPWFVSDVLVNDIPHLFNSLTSYFSGEGVQKLASDLAEFHAEGKIVIRPNPFWTTAHYFGRLPDVAPKLLSDLEQSDMVIFKGDLNFRKLTGDCEWPHTTPFAEALGPIAGKFNILALRTIKADVVVGLGKGVYEEIAKDNPHWERTGKYAVVEFCPKD O94727 FRP2_SCHPO BINDING 150; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="1"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 164; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="2"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 218; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="1"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 232; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="2"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 310..316; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255"; BINDING 419..427; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9; Evidence={ECO:0000250|UniProtKB:P32791}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P32791}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P32791}; SPBC947.05c; CHAIN 1..564; /note="Ferric/cupric reductase transmembrane component 2"; /id="PRO_0000337260" CARBOHYD 106; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 261; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 350; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 442; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 496; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 548; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MILARDDKWTLGSIALIFVLLIGFALLFLLERFRVKEKSRTFKDCVNVYQCPSKGERVYLALRHWFIFLATHKAQMTLILSPLVMLVTIPFTGKETKNSIASYDWNLTGVAARLGYLSCGLFFVSYFFSLKNNPFCLMLFSSHEKMNYLHRWLSVYAVLISVLHGILFMIFSAQSYKPLLYDKISIYGYFITVVLFLMTVASLPSVRRKFFEWFFVLHHTCSVLIIFLIWLHHPRTIVYMKACIIIYAFDRGCRLFRSIWNRSNFRIYLLNEDMIYMVGRKPKRSFFALPWAAGSHVYINIPSLSYWQVHPFTLASAPFDDFIELFVAVHSGFTERLANRLYSMPHEYPNFSLAPGTPESLSNTYRELNSFKSYAVEIENTAQGHTYEPEDLYLETTVFMDGPYGTTSNVFKEYSYVLLIAGGVGFSYTLPILRDLILKECNVTSITFIWSCRSLSLLKVASKSLNSLLHQSNVRLKIINHFTGSISCKESSEFSNQTTENSEMEFFDDRPDLDMYIQKFFDYVGYQTAALAACGSQSFLKRIKNSVNKSISSTTDIYQHYEEL O94730 CHMP7_SCHPO SPBC1604.18c; CHAIN 1..449; /note="Charged multivesicular body protein 7"; /id="PRO_0000303922" MGKKEKVNALEFSVNKGIFTKTRLKSLYSDFTSLFIKNPEGFLANVNTWREAIETSAWSGKLNSRIILVFDETFESAFSSPALGRPLSLGAVAAYWIQQGVWLRKQDFLNDCKKGNLVREDGFSIFSILRWSFQKLGFQNQASSILSNRSPSGQYVIRKNIEKLACLVHNEAMRRCSSYTSAIYTWDFFQDTFGSLYWEEGKLNKDEMECLLNWMCYQKHVLIFDSKIIKFLPNSQIDAQLASIDKSIDGSVADLIQARASIAQRSEFLNEELEQLSQVLNQAVKKGEKTIAITYLRRKKILSKDLERKVSSRLQLDTIISNIDNAVDNKILLIAMSSGSEALDAILAQMGGTEKVEDVLENVNDTLARSEEIDATIQTYNPQNIDLEDEAVEKEWQDLVAEEQKVEDIVSTLGNVSLKTPSDTFTLTNTDSDKKTSKPEKIQAELVEQ O94752 EDC3_SCHPO SPBC18E5.11c; STRAND 10..15; /evidence="ECO:0007829|PDB:4A53"; STRAND 20..29; /evidence="ECO:0007829|PDB:4A53"; STRAND 34..39; /evidence="ECO:0007829|PDB:4A53"; STRAND 43..48; /evidence="ECO:0007829|PDB:4A53"; STRAND 52..57; /evidence="ECO:0007829|PDB:4A53"; STRAND 63..65; /evidence="ECO:0007829|PDB:4A54"; STRAND 68..70; /evidence="ECO:0007829|PDB:4A53"; STRAND 88..90; /evidence="ECO:0007829|PDB:4A53"; STRAND 93..97; /evidence="ECO:0007829|PDB:4A53" HELIX 3..6; /evidence="ECO:0007829|PDB:4A53"; HELIX 49..51; /evidence="ECO:0007829|PDB:4A53" TURN 30..33; /evidence="ECO:0007829|PDB:4A53"; TURN 40..42; /evidence="ECO:0007829|PDB:4A53" CHAIN 1..454; /note="Enhancer of mRNA-decapping protein 3"; /id="PRO_0000119063" MSVADFYGSNVEVLLNNDSKARGVITNFDSSNSILQLRLANDSTKSIVTKDIKDLRILPKNEIMPKNGTKSPSTNSTKLKSAETYSSKNKWSMDCDEEFDFAANLEKFDKKQVFAEFREKDKKDPAKLLVSHNKSPNRNYHHKQNVLGPSVKDEFVDLPSAGSQINGIDAVLSSSSNGHVTPGSKKGSRETLKKKPFVDENIPAELHTTTGDILKPITPEQLSQGIALAIAKTSTDIVVENAAQLLSQFVFSVLGGHKRLSSRNHNSQPLVCILVGSHDHASAAVAAGRRLCAIGIKVVLRLLTPFNVDNRQLLMFQAAGGYIPTENFDQFLNKLTSPIELVVDVLTGFHPSIDKNSHALIQWANDLNVLILSVDIPSGYTVQKKNTAILPKWTLALGAVTTTLAQAALVKQAAGVSVFVGNLGTGSQTWAELGILESQVTGQYLAQISCTSTN O94756 MEU14_SCHPO SPBC1347.03; CHAIN 1..335; /note="Meiotic expression up-regulated protein 14"; /id="PRO_0000096448" MPKSSNLKMQRKGSLRENGLVKGLNKNKFSISKLKELSHADDSRKSHRIIRSGKSSGEAYKQAGKGLMNLGNHLSDWGAKSSNLSLNDISDKIGVLVSELGETEIEFVKAFNENRIKFKAIRAMEDSIAPSRAHRQRLISSIEREEERDPLSPKLTDLQNQLVRTEAENLVGEMQLDNTSREVFKSSFQGLMDAFQLRAQKQMTLSYYASQLAELINDEVAYPGDNPAAYSQKYATQIMHQCVESMARLLAPVTSETTEHVGSDCEFTRKSSSSVEFSDHSQDSGDPSQQNILQVKNVQAVLSIPEAESYKAQLLSSIAEEQKKKELQAKSTVFL P00046 CYC_SCHPO BINDING 19; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /note="covalent"; BINDING 22; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /note="covalent"; BINDING 23; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; BINDING 85; /ligand="heme c"; /ligand_id="ChEBI:CHEBI:61717"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue" PTM: Binds 1 heme c group covalently per subunit. MOD_RES 77; /note="N6,N6,N6-trimethyllysine"; /evidence="ECO:0000269|PubMed:207525" SPCC191.07; CHAIN 2..109; /note="Cytochrome c"; /id="PRO_0000108333" MPYAPGDEKKGASLFKTRCAQCHTVEKGGANKVGPNLHGVFGRKTGQAEGFSYTEANRDKGITWDEETLFAYLENPKKYIPGTKMAFAGFKKPADRNNVITYLKKATSE P00332 ADH_SCHPO BINDING 46; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 47; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 48; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 51; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 100; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 103; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 106; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 114; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 156; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 183; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 184; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 185; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 204; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 209; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 224; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 271; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 273; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 296; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 298; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330"; BINDING 343; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P00330" CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000305|PubMed:6294096}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000305|PubMed:6294096}; CATALYTIC ACTIVITY: Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH; Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:3546317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291; Evidence={ECO:0000269|PubMed:3546317}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25292; Evidence={ECO:0000269|PubMed:3546317}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00330}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=160 uM for NAD(+) {ECO:0000269|PubMed:3546317}; KM=14 mM for ethanol {ECO:0000269|PubMed:3546317}; KM=1.6 mM for acetaldehyde {ECO:0000269|PubMed:3546317}; KM=100 uM for NADH {ECO:0000269|PubMed:3546317}; MOD_RES 205; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 250; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC13B11.01; CHAIN 1..350; /note="Alcohol dehydrogenase"; /id="PRO_0000160729" MTIPDKQLAAVFHTHGGPENVKFEEVPVAEPGQDEVLVNIKYTGVCHTDLHALQGDWPLPAKMPLIGGHEGAGVVVKVGAGVTRLKIGDRVGVKWMNSSCGNCEYCMKAEETICPHIQLSGYTVDGTFQHYCIANATHATIIPESVPLEVAAPIMCAGITCYRALKESKVGPGEWICIPGAGGGLGHLAVQYAKAMAMRVVAIDTGDDKAELVKSFGAEVFLDFKKEADMIEAVKAATNGGAHGTLVLSTSPKSYEQAAGFARPGSTMVTVSMPAGAKLGADIFWLTVKMLKICGSHVGNRIDSIEALEYVSRGLVKPYYKVQPFSTLPDVYRLMHENKIAGRIVLDLSK P05733 RL37B_SCHPO BINDING 19; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 22; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 34; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 37; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P51402}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P51402}; SPCC1223.05c; STRAND 15..18; /evidence="ECO:0007829|PDB:8ETC"; STRAND 24..28; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 41..43; /evidence="ECO:0007829|PDB:8EUY" HELIX 51..57; /evidence="ECO:0007829|PDB:8EUY"; HELIX 65..74; /evidence="ECO:0007829|PDB:8EUY" TURN 20..22; /evidence="ECO:0007829|PDB:8EUY"; TURN 29..32; /evidence="ECO:0007829|PDB:8EUY"; TURN 35..37; /evidence="ECO:0007829|PDB:8EUY"; TURN 75..77; /evidence="ECO:0007829|PDB:8EUY" CHAIN 2..91; /note="Large ribosomal subunit protein eL37B"; /id="PRO_0000139721" MTKGTQSFGMRHNKSHTICRRCGKRSFHIQKSTCACCGYPAAKTRSYNWGAKAKRRRTTGTGRMSYLKKVHRSFKNGFRSGKPAAAVAASA P05734 RL19A_SCHPO SPBC56F2.02; STRAND 22..24; /evidence="ECO:0007829|PDB:8ETC"; STRAND 49..52; /evidence="ECO:0007829|PDB:8ETC" HELIX 5..15; /evidence="ECO:0007829|PDB:8ETC"; HELIX 29..34; /evidence="ECO:0007829|PDB:8ETC"; HELIX 38..46; /evidence="ECO:0007829|PDB:8ETC"; HELIX 60..67; /evidence="ECO:0007829|PDB:8ETC"; HELIX 91..111; /evidence="ECO:0007829|PDB:8ETC"; HELIX 117..128; /evidence="ECO:0007829|PDB:8ETC"; HELIX 135..144; /evidence="ECO:0007829|PDB:8ETC" TURN 19..21; /evidence="ECO:0007829|PDB:8ETC" CHAIN 2..193; /note="Large ribosomal subunit protein eL19A"; /id="PRO_0000131183" MANLRTQKRLAASVLKCGKRKVWMDPNEISEISNANSRQNVRKLIKDGLVIRKPNLMHSRFRIRKTHAAKRLGRHTGYGKRKGTAEARMPSAVVWMRRQRVLRRLLRKYRESGKIDKHLYHTLYLEAKGNTFKHKRALIEHIQRAKAEANRTKLIQEQQDARRARAKAARQRRAKAVEEKREQLYTAAEKIEE P07657 COX1_SCHPO BINDING 45; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 48; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 50; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 68; /ligand="Fe(II)-heme a"; /ligand_id="ChEBI:CHEBI:61715"; /ligand_note="low-spin"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 247; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="B"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 251; /ligand="O2"; /ligand_id="ChEBI:CHEBI:15379"; /evidence="ECO:0000250|UniProtKB:P00396"; BINDING 296; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="B"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 297; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="B"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 375; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="ligand shared with subunit 2"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 376; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="ligand shared with subunit 2"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 383; /ligand="heme a3"; /ligand_id="ChEBI:CHEBI:83282"; /ligand_note="high-spin"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 385; /ligand="Fe(II)-heme a"; /ligand_id="ChEBI:CHEBI:61715"; /ligand_note="low-spin"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P00401"; BINDING 447; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P00401" CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00401}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P00401}; Note=Binds 2 heme A groups non-covalently per subunit. {ECO:0000250|UniProtKB:P00401}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00401}; Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401}; SPMIT.01; CHAIN 1..537; /note="Cytochrome c oxidase subunit 1"; /id="PRO_0000183414" MNSWWTYVNRWIFSTNAKDIAILYLLFGLVSGIIGSVFSFIIRMELSAPGSQFLSGNGQLYNVAISAHGILMIFFFIIPALFGAFGNYLVPLMIGAPDVAYPRVNNFTFWLLPPALMLLLISALTEEGPGGGWTVYPPLSSITSHSGPAIDLAILSLQLTGISSTLGSVNLIATMINMRAPGLSLYQMPLFAWAIMITSILLLLTLPVLAGGLFMLFSDRNLNTSFYAPEGGGDPVLYQHLFWFFGHPEVYILIMPAFGVVSHIIPSLAHKPIFGKEGMLWAMLSIALLGLMVWSHHLFTVGLDVDTRAYFSAATMVIAIPTGIKIFSWLATLTGGAIQWSRVPMLYAIGFLILFTIGGLTGVILSNSVLDIAFHDTYFVVAHFHYVLSMGALFGLCGAYYWSPKMFGLMYNETLASIQFWILFIGVNIVFGPQHFLGLNGMPRRIPDYPEAFVGWNFVSSIGSVISILSLFLFMYVMYDQFTSNRVVKTNPYLIPSYFDDNVIFVNEKLGVAQSIEWLLHSPVHEHAFNTLPTKSI P08091 PPA1_SCHPO ACT_SITE 69; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 331; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; SIGNAL 1..18 SPBP4G3.02; CHAIN 19..453; /note="Acid phosphatase"; /id="PRO_0000023951" CARBOHYD 95; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 151; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 183; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 193; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 243; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 319; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 410; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 429; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 443; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFLQNLFLGFLAVVCANAQFAEFTAFDGKFDFKEHLTSRSPYHKPYFYGPSIDFPTTCKIKQVHTLQRHGSRNPTGGNAAFDAVGIANFQQRLLNGSVPIDYSVSGNPLSFVPTWTPVIEAANADALSSSGRVELFDMGRQFYERYHELFNASTYNIYTAAQQRVVDSALWYGYGMFGEDVHNFTNYILVSENATAGSNSLSSYNACPASDADDFTTPALEAWRNVYMPPIRQRLNPYFSNYNLTNDDILNLYGICSYEIALQDYSEFCKLFNSVDFLNFEYEGDLSFSYGMGNSVKWGSIFGGAYANSLANSLRSVENNTQQVFFAFTHDANIIPVETALGFFTDNTPENPLPTSYQVHSHSMKASEFVPFAGNLITELFQCEDSKYYVRHLVNEEVFPLSDCGFGPSNTSDGMCELYAYLNSPVRVNGTSNGIQNFDTLCNASAVAAVYPY P08094 RLA2_SCHPO MOD_RES 100; /note="Phosphoserine"; /evidence="ECO:0000250" SPBP8B7.06; CHAIN 1..110; /note="Large ribosomal subunit protein P2A"; /id="PRO_0000157683" MKYLAAYLLLTVGGKDSPSASDIESVLSTVGIEAESERIETLINELNGKDIDELIAAGNEKLATVPTGGAASAAPAAAAGGAAPAAEEAAKEEAKEEEESDEDMGFGLFD P09202 F16P_SCHPO BINDING 19..23; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 44..48; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 85; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 114; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 114; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 127..128; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 133; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 133; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 135; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 136..139; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 136; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 155; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 227..230; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 258..263; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 279; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 288..290; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00636"; BINDING 294; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:P00636" CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00636}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P00636}; SPBC1198.14c; CHAIN 1..347; /note="Fructose-1,6-bisphosphatase"; /id="PRO_0000200510" MKKDLDEIDTDIVTLSSFILQEQRRYNQKHKNEEGKPCIIQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSNGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISDVLRPGKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTPDKKPYSARYIGSMVADMHRTILYGGLFAYPCSKGNNGKLRLLYECFPMAFLVEQAGGIAVNDKGDRILDLVPKTLHGKSSIWLGSKHEVEEYINFIK P09322 H4_SCHPO PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. {ECO:0000250|UniProtKB:P02309}. MOD_RES 6; /note="N6-acetyl-N6-methyllysine; alternate"; /evidence="ECO:0000305|PubMed:37731000"; MOD_RES 6; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02309"; MOD_RES 9; /note="N6-(2-hydroxyisobutyryl)lysine"; /evidence="ECO:0000269|PubMed:29192674"; MOD_RES 9; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02309"; MOD_RES 13; /note="N6-acetyl-N6-methyllysine; alternate"; /evidence="ECO:0000305|PubMed:37731000"; MOD_RES 13; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02309"; MOD_RES 48; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 92; /note="N6-glutaryllysine"; /evidence="ECO:0000250|UniProtKB:P02309" SPAC1834.03c;SPBC8D2.03c;SPBC1105.12; HELIX 32..40; /evidence="ECO:0007829|PDB:6S1R" TURN 41..43; /evidence="ECO:0007829|PDB:6S1R" CHAIN 2..103; /note="Histone H4"; /id="PRO_0000158357" MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALVYEETRAVLKLFLENVIRDAVTYTEHAKRKTVTSLDVVYSLKRQGRTIYGFGG P0C016 RS27A_SCHPO SPAC6G10.11c; CHAIN 1..76; /note="Ubiquitin"; /id="PRO_0000396486"; CHAIN 77..150; /note="Small ribosomal subunit protein eS31A"; /id="PRO_0000137687" MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKTYTTPKKIKHKHKKVELAVLKYYKVEDDGSVKRLRRECPNCGASTFMANHKDRLYCGRCHLTLKLEN P0C8R3 RS27B_SCHPO SPAC589.10c; CHAIN 1..76; /note="Ubiquitin"; /id="PRO_0000396488"; CHAIN 77..150; /note="Small ribosomal subunit protein eS31B"; /id="PRO_0000363372" MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKTYTTPKKIKHKHKKVELAVLKYYKVEDDGSVKRLRRECPNCGASTFMANHKDRLYCGRCHLTLKLEA P0CG72 UBI4P_SCHPO SPBC337.08c; PROPEP 381..382; /id="PRO_0000396305" CHAIN 1..76; /note="Ubiquitin"; /id="PRO_0000396300"; CHAIN 77..152; /note="Ubiquitin"; /id="PRO_0000396301"; CHAIN 153..228; /note="Ubiquitin"; /id="PRO_0000396302"; CHAIN 229..304; /note="Ubiquitin"; /id="PRO_0000396303"; CHAIN 305..380; /note="Ubiquitin"; /id="PRO_0000396304" MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGLF P0CH06 RL401_SCHPO SPAC11G7.04; CHAIN 1..76; /note="Ubiquitin"; /id="PRO_0000114860"; CHAIN 77..128; /note="Large ribosomal subunit protein eL40A"; /id="PRO_0000138774" MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCEKQICRKCYARLPPRATNCRKKKCGHTNQLRPKKKLK P0CH07 RL402_SCHPO SPAC1805.12c; STRAND 1..7; /evidence="ECO:0007829|PDB:4II2"; STRAND 12..18; /evidence="ECO:0007829|PDB:4II2"; STRAND 42..45; /evidence="ECO:0007829|PDB:4II2"; STRAND 66..70; /evidence="ECO:0007829|PDB:4II2" HELIX 23..34; /evidence="ECO:0007829|PDB:4II2"; HELIX 38..40; /evidence="ECO:0007829|PDB:4II2"; HELIX 56..59; /evidence="ECO:0007829|PDB:4II2" CHAIN 1..76; /note="Ubiquitin"; /id="PRO_0000396452"; CHAIN 77..128; /note="Large ribosomal subunit protein eL40B"; /id="PRO_0000396453" MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCEKQICRKCYARLPPRATNCRKKKCGHTNQLRPKKKLK P0CT53 EF1A1_SCHPO BINDING 14..21; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 91..95; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 153..156; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 2; /note="N,N,N-trimethylglycine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 3; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 3; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 30; /note="N6-methyllysine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 79; /note="N6,N6,N6-trimethyllysine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 316; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 316; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 390; /note="N6-methyllysine"; /evidence="ECO:0000250|UniProtKB:P02994" SPCC794.09c; CHAIN 2..460; /note="Elongation factor 1-alpha-A"; /id="PRO_0000090968" MGKEKGHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEATELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAVLIIGGGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAVNKMDTTGWSQARFEEIVKETSNFIKKVGFNPKTVPFVPVSGFQGDNMIEPTTNMPWYQGWQKETKAGVVKGKTLLEAIDSIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMIVTFAPAGVTTEVKSVEMHHESLDAGLPGDNVGFNVKNVSVKDIRRGNVCGDSKNDPPMGCASFTAQVIILNHPGQISAGYSPVLDCHTAHIACKFAELIEKIDRRSGKKIEESPKFVKSGDACIAKMVPSKPMCVEAFTDYAPLGRFAVRDMRQTVAVGVIKAVEKVAPGAAKVTKAAVKAGAKK P0CT54 EF1A2_SCHPO BINDING 14..21; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 91..95; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 153..156; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 2; /note="N,N,N-trimethylglycine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 3; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 3; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 30; /note="N6-methyllysine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 79; /note="N6,N6,N6-trimethyllysine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 316; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 316; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 390; /note="N6-methyllysine"; /evidence="ECO:0000250|UniProtKB:P02994" SPAC23A1.10; CHAIN 2..460; /note="Elongation factor 1-alpha-B"; /id="PRO_0000090969" MGKEKGHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEATELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAILIIGGGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAVNKMDTTGWSQARFEEIVKETSNFIKKVGFNPKTVPFVPVSGFQGDNMIEPTTNMPWYQGWQKETKAGVVKGKTLLEAIDSIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMIVTFAPAGVTTEVKSVEMHHESLDAGLPGDNVGFNVKNVSVKDIRRGNVCGDSKNDPPMGCASFTAQVIILNHPGQISAGYSPVLDCHTAHIACKFAELIEKIDRRSGKKIEESPKFVKSGDACIAKMVPSKPMCVEAFTDYAPLGRFAVRDMRQTVAVGVIKAVEKVAPGAAKVTKAAVKAGAKK P0CT55 EF1A3_SCHPO BINDING 14..21; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 91..95; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 153..156; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 2; /note="N,N,N-trimethylglycine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 3; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 3; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 30; /note="N6-methyllysine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 79; /note="N6,N6,N6-trimethyllysine"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 316; /note="N6,N6-dimethyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 316; /note="N6-methyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P02994"; MOD_RES 390; /note="N6-methyllysine"; /evidence="ECO:0000250|UniProtKB:P02994" SPBC839.15c; CHAIN 2..460; /note="Elongation factor 1-alpha-B/C"; /id="PRO_0000433409" MGKEKGHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEATELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAILIIGGGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAVNKMDTTGWSQARFEEIVKETSNFIKKVGFNPKTVPFVPVSGFQGDNMIEPTTNMPWYQGWQKETKAGVVKGKTLLEAIDSIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMIVTFAPAGVTTEVKSVEMHHESLDAGLPGDNVGFNVKNVSVKDIRRGNVCGDSKNDPPMGCASFTAQVIILNHPGQISAGYSPVLDCHTAHIACKFAELIEKIDRRSGKKIEESPKFVKSGDACIAKMVPSKPMCVEAFTDYAPLGRFAVRDMRQTVAVGVIKAVEKVAPGAAKVTKAAVKAGAKK P0CT75 RS23A_SCHPO PTM: Hydroxylation at Pro-62 affects translation termination efficiency. {ECO:0000305|PubMed:24550462}. MOD_RES 62; /note="3,4-dihydroxyproline"; /evidence="ECO:0000269|PubMed:24550462" SPAC23C11.02c; CHAIN 1..143; /note="Small ribosomal subunit protein uS12A"; /id="PRO_0000146479" MGKPAGLNAARKLRNHRREERWADAHYKKRLLGTAYKSSPFGGSSHAKGIVVEKIGVEAKQPNSAIRKCVRVQLIKNGKKVTAFVPHDGCLNFVDENDEVLLSGFGRKGKAKGDIPGVRFKVVKVAGVGLSALFHEKKEKPRA P0CT76 RS23B_SCHPO PTM: Hydroxylation at Pro-62 affects translation termination efficiency. {ECO:0000305|PubMed:24550462}. MOD_RES 62; /note="3,4-dihydroxyproline"; /evidence="ECO:0000269|PubMed:24550462" SPBP4H10.13; CHAIN 1..143; /note="Small ribosomal subunit protein uS12B"; /id="PRO_0000433413" MGKPAGLNAARKLRNHRREERWADAHYKKRLLGTAYKSSPFGGSSHAKGIVVEKIGVEAKQPNSAIRKCVRVQLIKNGKKVTAFVPHDGCLNFVDENDEVLLSGFGRKGKAKGDIPGVRFKVVKVAGVGLSALFHEKKEKPRA P0CU08 GEMI2_SCHPO MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 118; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19B12.12c; CHAIN 1..235; /note="SMN complex subunit yip11/gem2"; /id="PRO_0000237700" MPSKRKRNPLQYQTSGSLDEETNQRSAFPQIDNNSASESLEYDIPLDGLDYLATVREEARKLVPFVAARREPETRETIPLRKLEIEAGKKSFDPFLRYLLNIIDKEGERLEQYMESSSLDASILPKNLQQWRVYIEHKAPCWAILAVVDLATVLEILESLSSWLEKDAIDLQSQWIFCFCYKLPELLNGEDISTLRSVLKSLRSTHTSFPALQMSASALQAVLVYRYGQKDLFQT P0CU17 RPN51_SCHPO MOD_RES 209; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1420.03; CHAIN 1..443; /note="26S proteasome regulatory subunit rpn501"; /id="PRO_0000173864" MEQKPEVDYSEKFAELQKSLNNLNTIDIDANLEKLLIFEKQVRQASDTSTNTKVLIYIADLLFRAGDFQGLNEQLVSLFKKHGQLKQSMTSLVQHVMTYLPGIDDLKTKINLIETLRTITDGKIYVEVERARLTQLLSQIKEEQGDIKSAQEILCNEPVETYGSFDLKEKVAFILDQVRLFLLRSDYYMASTYTKKINVKFFEKEDVQSLKLKYYEQKIRIGLHDDAYLDVCKYYRAVYDTAVVQEDPEKWKEILENVVCFALLTPYDNEQADLLHRINADHKLNSLPLLQQLVKCFIVNELMRWPKIAEIYGSALRSNPVFAENDEKGEKRWSELRKRVIEHNIRVVANYYSRIHCSRLGVLLDMSPSETEQFLCDLIAKHHFYAKIDRPAQVISFKKSQNVQEQLNEWGSNITELLGKLEKVRQLIIKEEMMNSIQQAVAK P0CU18 RPN52_SCHPO MOD_RES 209; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB8E5.02c; CHAIN 1..443; /note="26S proteasome regulatory subunit rpn502"; /id="PRO_0000437236" MEQKPEVDYSEKFAELQKSLNNLNTIDIDANLEKLLIFEKQVRQASDTSTNTKVLIYIADLLFRAGDFQGLNEQLVSLFKKHGQLKQSMTSLVQHVMTYLPGIDDLKTKINLIETLRTITDGKIYVEVERARLTQLLSQIKEEQGDIKSAQEILCNEPVETYGSFDLKEKVAFILDQVRLFLLRSDYYMASTYTKKINVKFFEKEDVQSLKLKYYEQKIRIGLHDDAYLDVCKYYRAVYDTAVVQEDPEKWKEILENVVCFALLTPYDNEQADLLHRINADHKLNSLPLLQQLVKCFIVNELMRWPKIAEIYGSALRSNPVFAENDEKGEKRWSELRKRVIEHNIRVVANYYSRIHCSRLGVLLDMSPSETEQFLCDLIAKHHFYAKIDRPAQVISFKKSQNVQEQLNEWGSNITELLGKLEKVRQLIIKEEMMNSIQQAVAK P0CY15 MATMI_SCHPO SPBC23G7.17c; CHAIN 1..42; /note="Mating-type M-specific polypeptide Mi"; /id="PRO_0000410972" MSAEDLFTIQILCDQIELKLASIVINSNIKLQLKRKKKTQQL P15398 RPA1_SCHPO BINDING 63; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 73; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 643; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 645; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 647; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; MOD_RES 159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1438; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1441; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4C3.05c; CHAIN 1..1689; /note="DNA-directed RNA polymerase I subunit rpa1"; /id="PRO_0000073929" MNIAQPVSSEIKSVKFGIYDVDDVEKISVKQIVNPVLLDNLNHPTNGGLYDLALGPYLKNSVCATCHLDERYCPGHFGHIVLPIPAYHPLFFSQMYNLLRSTCLYCHHFKLSKVKVHLFFCRLKLLDYGLLNESEMVENVSLTEAIIKNSNGTPLEDGSDSEDSGLGHDDIAKDAATLMRIRDEFVAKSIADSRQNAHIDAQLTTLLLHERKKVVRAFYHAISSRKQCDNCQSFSPNFRKEGFAKIFEIPLSGKNLQFMEQTGKIRSDVLRDTSKKHHEDEGYDGDSDSSNESEVEGIDLFEEDPNPLKNKSKSPIAHGAKYMTSTEVRNHLRRLFVKENVVLSRLYAHKRGKPASADMFFLQNIAVPPTRFRPASKMGDEVHENIQNELLTRILQSSIQIASLSKDSTVEVNPDEKEGLERRSRAFELLINAFVQLQHDVNSLIDSNRNPSSGGQSRTVPPGIKQILEKKEGLFRKHMMGKRVNYAARSVISPDPNIETNEIGVPPVFATKLTYPEPVTLYNFNEMRNAVINGPHKWPGASHIQNEDGTLISLMPLTIEQRTALANQLLTPQSNLISSPYSYSRLINTNKKVYRHVRNGDMLILNRQPTLHKPSMMAHKARILPGEKTIRMHYANCNSYNADFDGDEMNMHFPQSTNARSEAQFIANTDSQYLVPTSGDPLRGLIQDHVVMGVWLTCKDTFYTRDEYQQLLFQALKPDETGMYGRIKTLPPAIQRPGIYWTGKQIISSVLLNLKPSDRPGLNLKSKAKVPGKYWSPDSEEGSVLFDDGELLCGILDKSSFGASAFGLVHSVHELYGPDIAGRLLSVLSRLFTAYAQMRGFTCRMDDLRLDEQGDNWRRQLLENGKSFGLEAASEYVGLSTDSPIALLNANLEEVYRDDEKLQGLDAAMKGKMNGLTSSIINKCIPDGLLTKFPYNHMQTMTVSGAKGSNVNVSQISCLLGQQELEGRRVPLMVSGKSLPSFVPYETSAKSGGFIASRFLTGIAPQEYYFHCMAGREGLIDTAVKTSRSGYLQRCLMKHLEGLCVQYDHTVRDSDGSIVQFHYGEDSLDVTKQKHLTQFEFSAKNYKSLIQKYKVKSVLSAVDSETASSYAKKALKKPYKYDPVLDKYPPSRYLGSVSEKFQRAVDEYTQKNPDKLIASKKESKLDDSLLNESKFKALMQLRYQQSLVDPGESVGVLASQSIGEPSTQMTLNTFHFAGFGAKNVTLGIPRLREIIMTASANIQTPTMTLRLNDGVSDKRASAFCKEVNKLVLSEVVRQVRVTEKISGQGSDEQSKTYAIRLDLYSRDEYQDEYGVLQEEIESTFSNRFLKILNRIIKSYLAKSKQRKSGGKDDTVPEVGQALKPLEDIDEAPIEGRAQEALEDEDNDATNEKMVSRSKQHASYEGPDEADKVALRQLKGSNKVEDVNMDEEEDEGFKSDESVSDFKERKLLEKQNTVSISERRELQLKTAKEILSNCKHLDFDYVNGEWATVELVFPINTEKLLMVSLVEKACSETVIHEIPGITRCFSKPPDSALDTVPKVITEGVNLKAIWEFYNEISMNDIYTNDIAAILRIYGVEAARNAIVHEVSSVFGVYGIAVDPRHLSLIADYMTFEGGYKAFNRMGIEYNTSPFAKMSFETTCHFLTEAALRGDVDDLSNPSSRLVVGRVGNFGTGSFDIFTPVVDSPAN P17609 YPT2_SCHPO BINDING 16..23; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 64..68; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 122..125; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC9E9.07c; CHAIN 1..200; /note="GTP-binding protein ypt2"; /id="PRO_0000121309" LIPID 199; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"; LIPID 200; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MSTKSYDYLIKLLLIGDSGVGKSCLLLRFSEDSFTPSFITTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGILLLYDVTDKKSFDNVRTWFSNVEQHASENVYKILIGNKCDCEDQRQVSFEQGQALADELGVKFLEASAKTNVNVDEAFFTLAREIKKQKIDAENEFSNQANNVDLGNDRTVKRCC P18253 CYPH_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPBC28F2.03; CHAIN 1..162; /note="Peptidyl-prolyl cis-trans isomerase"; /id="PRO_0000064130" MSNCFFDVIANGQPLGRIVFKLFDDVVPKTAANFRALCTGEKGYGYAGSTFHRVIPQFMLQGGDFTRGNGTGGKSIYGEKFPDENFALKHNKPGLLSMANAGPNTNGSQFFITTVVTPWLDGKHVVFGEVTEGMDVVKKVESLGSNSGATRARIVIDKCGTV P18869 LEU3_SCHPO BINDING 78..89; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 96; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 106; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 135; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 224; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 224; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 249; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 253; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 290..302; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000305|PubMed:3063400}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32272; Evidence={ECO:0000305|PubMed:3063400}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; MOD_RES 55; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1A4.02c; CHAIN 1..371; /note="3-isopropylmalate dehydrogenase"; /id="PRO_0000083618" MCAKKIVVLPGDHIGPEIVASALEVLKVVEKKRPELKLEFEEHKIGGASIDAYGTPLTDETVKACLEADGVLLGAVGGPEWTNPNCRPEQGLLKLRKSMGVWANLRPCNFASKSLVKYSPLKPEIVEGVDFCVVRELTGGCYFGERTEDNGSGYAMDTWPYSLEEVSRIARLAAWLAETSNPPAPVTLLDKANVLATSRLWRKTVAKIFKEEYPHLTLKNQLIDSAAMLLVKSPRTLNGVVLTDNLFGDIISDEASVIPGSLGLLPSASLSGVVGKSEEKVHCLVEPIHGSAPDIAGKGIVNPVGTILSASLLLRYGLNAPKEAEAIEAAVRKVLDDTSIGGRGLYTRDLGGEASTADITKAVVEELEKIL P21534 COX2_SCHPO BINDING 182; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A1"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 217; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A1"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 217; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A2"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 219; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A2"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 219; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="ligand shared with subunit 1"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 221; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A1"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 221; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A2"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 225; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A2"; /evidence="ECO:0000250|UniProtKB:P00410"; BINDING 228; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="A1"; /evidence="ECO:0000250|UniProtKB:P00410" CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00410}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00410}; Note=Binds a dinuclear copper A center per subunit. {ECO:0000250|UniProtKB:P00410}; SPMIT.11; CHAIN 1..248; /note="Cytochrome c oxidase subunit 2"; /id="PRO_0000183686" MLFFNSILNDAPSSWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILILVALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTNENEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS P21696 GPD1_SCHPO ACT_SITE 232; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 29..34; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 121; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 144; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 144; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 177; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 296..297; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 296; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 325; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000305|PubMed:8825100}; MOD_RES 376; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 382; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC215.05; CHAIN 1..385; /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1"; /id="PRO_0000138095" MSGYGQQGVSAANIDSIRPKKRLSIGVVGSGNWGTAIAKICGENARAHGHHFRSKVRMWVFEEEIEYKGEKRKLTEVFNEAHENVKYLPGIECPPNVIAVPDVREVARRADILVFVVPHQFIERVCDQMVGLIRPGAVGISCIKGVAVSKEGVRLYSEVISEKLGIYCGVLSGANVANEVAREQFCETTIGFNPPNEVDIPREQIAAVFDRPYFSVVSVDDVAGVALGGALKNVVAMAVGFADGLEWGGNTKAAIMRRGLLEMQKFATTFFDSDPRTMVEQSCGIADLVTSCLGGRNNRCAEAFVKTGKSLETLEKELLGGQLLQGAATSKDVHEFLLTKDMVKDFPLFTAVYNISYEDMDPKDLIIVLQPLKEDSENEGGTETE P21911 SDHB_SCHPO BINDING 98; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"; BINDING 103; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"; BINDING 106; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"; BINDING 118; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"; BINDING 188; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 191; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 194; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 198; /ligand="[3Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:21137"; /evidence="ECO:0000250"; BINDING 203; /ligand="a ubiquinone"; /ligand_id="ChEBI:CHEBI:16389"; /ligand_note="ligand shared with DHSD"; /evidence="ECO:0000250"; BINDING 245; /ligand="[3Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:21137"; /evidence="ECO:0000250"; BINDING 251; /ligand="[3Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:21137"; /evidence="ECO:0000250"; BINDING 255; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; TRANSIT 1..24; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC140.01; CHAIN 25..275; /note="Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial"; /id="PRO_0000010350" MFSRRIQVLSPFLKHFVNRNARMMATEANISATSANPQSQGENLKTFEIYRWNPEKPEVKPKLQKYTVDLTKCGPMVLDALIKIKNEQDPTLTFRRSCREGICGSCAMNINGSNTLACICNIKKDNKPTKIYPLPHCFIVKDLVPDLTYFYKQYKSIEPWLQNDNIPKDKEFYQSRADRAKLDGLYECILCACCSTSCPSYWWNSEEYLGPAVLMQAYRWIIDSRDQATAKRLDVMQNSMSVYRCHTIMNCARTCPKGLNPGLAIAKVKALMATA P23635 PP2A1_SCHPO ACT_SITE 118; /note="Proton donor"; /evidence="ECO:0000250" BINDING 57; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 59; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 85; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 85; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 117; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 167; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 241; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; MOD_RES 309; /note="Leucine methyl ester"; /evidence="ECO:0000250" SPAC823.15; CHAIN 1..309; /note="Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit"; /id="PRO_0000058871" MSVSGKIGEVDRWIEQLSRCEPLSEEDVIQMCDLAKEVLSVESNVQSVRCPVTVCGDIHGQFHDLMELFNIGGPSPDTNYLFMGDYVDRGYHSVETVSLLIAFKIRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWQYFTDLFDYLPLTALIEDRIFCLHGGLSPSIDTLDHVRILDRVQEVPHEGPICDLLWSDPDDRPGWGISPRGAGYTFGPDIAEAFNHNNGLDLIARAHQLVMEGYNWTTNHNVVTIFSAPNYCYRCGNQAAIMGIDDHINYAFIQYDTAPRKEELHVTRRTPDYFL P24782 DBP2_SCHPO BINDING 166..173; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBP8B7.16c; CHAIN 1..550; /note="ATP-dependent RNA helicase dbp2"; /id="PRO_0000054998" MSYRDNEYSGNYNGKEDGYNSRGRYGGGYRNNYSRGGGRGGFNDGASYGYDQRGQGRNFYESDGPGANLVKKDWKNETLIPFQKDFYKEHENVRNRSDAEVTEYRKEKEIVVHGLNVPKPVTTFEEAGFPNYVLKEVKQLGFEAPTPIQQQAWPMAMSGRDMVGISATGSGKTLSYCLPAIVHINAQPLLSPGDGPIVLVLAPTRELAVQIQQECTKFGKSSRIRNTCVYGGVPRGPQIRDLIRGVEICIATPGRLLDMLDSNKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTVMFSATWPKEVQRLARDYLNDYIQVTVGSLDLAASHNIKQIVEVVDNADKRARLGKDIEEVLKDRDNKVLIFTGTKRVADDITRFLRQDGWPALAIHGDKAQDERDWVLNEFRTGKSPIMVATDVASRGIDVKGITHVFNYDFPGNTEDYVHRIGRTGRAGAKGTAYTYFTSDNAKQARELVSILSEAKQDIDPKLEEMARYSSGGRGGNYRRGGYGRGGFRRGGGYGNRNRGFTGSNSAPLARSRW P24865 CG21_SCHPO MOD_RES 96; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4E9.02; CHAIN 1..415; /note="G2/mitotic-specific cyclin cig1"; /id="PRO_0000080400" MDVSTQTRHATYFQDENQLQKDHIYVKKKSHIKLNTGVRAPFKAVDNINQQDEPTLIEGNNESSISSSTGDTFEEDFAYQDKVEIEERSIRSTPKSIGDDDLENREGSFDAPEGILTHGKHRLPTIPEWTKEDLAALSEAAARLQANPSPEDIETDPSMVPDYDPEIFHYMQSLERKLAPPPNYMSVQQEIDWVTRHMLVDWIVQVQIHFRLLPETLFLAVNLIDRFLSIKVVSLQKVQLVGLSALLIACKYEEIHPPSIYNFAHVVQGIFTVDEIIRAERYMLMLLDFDISWPGPMSFLRRISRADSYDHDIRMLAKYLQEVTLMDEIFIGAHISFIAATAYYLSMQMLGHLDWTPCHVYYSGYTARQLKPCAIIIMECLVDAPNHHNAIYRKYSENRMKRVSAFAHNWVLSVI P25009 PUC1_SCHPO SPBC19F5.01c; CHAIN 1..359; /note="Cyclin puc1"; /id="PRO_0000080418" MLVSSNEEQLTAHTPTSSSSIEPKILAACSYSLSVGPCSLAVSPKGVNSKSPSLKNETAFVVDSVSTLSAESSALLYNTQSSLLTGLSMNGYLGEYQEDIIHHLITREKNFLLNVHLSNQQPELRWSMRPALVNFIVEIHNGFDLSIDTLPLSISLMDSYVSRRVVYCKHIQLVACVCLWIASKFHETEDRVPLLQELKLACKNIYAEDLFIRMERHILDTLDWDISIPTPASYIPVLDPIFFLVLDASMFVPNLFKFPASKIACSVMNIVNEHVGSFLLTHPSMESYRKDDNFLWPEDLDTVTSYMENMSKRYANEECTDLLFSSLGRISSILAKKYPEQCAMAAWCNMTEKDTERTL P28706 RAD13_SCHPO BINDING 30; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 77; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 777; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 779; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 798; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 800; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 849; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000250}; SPBC3E7.08c; CHAIN 1..1112; /note="DNA repair protein rad13"; /id="PRO_0000154036" MGVSGLWDILEPVKRPVKLETLVNKRLAIDASIWIYQFLKAVRDKEGNQLKSSHVVGFFRRICKLLFFGIKPVFVFDGGAPSLKRQTIQKRQARRLDREENATVTANKLLALQMRHQAMLLEENNKKATALANASVQNERQMPSSMTLDNSEIKPVLNQRKNYLKPDPYQLPEMDVSFDKLGSSYDPRIMSQDELTQYVSSFTKIEDINLFDFSNIDFDSELFQSLPDTDKYSILSAARLRSRLRMGLSSEQLSEMFPNRMDFSRFQIERLKERNDLTQRLMDFTGMNEFGPSRVVSEKNREYILVKNEGAEGGWALGVISGSTNNEPIIIDDEATKLSSNLIDEDEDEAFYDVPLPSRSHSMNPRELVAAKLKEIKENSFSENQQSDEADYNVTDDLILQLATQQSLEENKKSKELFSLSASEFDKLNSEKKTFEILSTDIPAEDSMNSLLNDEENLKLEHVGDVSNDSLAFAEKKHPENGTSIFMDALPSASREKKTNDLIDPLPFQPMDWGKSIFFEKLKKPTETFMDSKTDIPSEAPDNSKLVEDTNLHTINATVNIESDLDAAKPGIENPIISPLLPVKDDEKDLDLRELNPLEPFENMKEQADDGTVTNPLNVSSDKAMSVYLLSSENAKDTGDIKSESIDAVLPTLETSSPSLSIPTDFQKEASPNKGAAALSSKVEPEVVEKLLDEEEEEMIIRMAEEEKEYDRFVSELNQRHETEEWNQEAFEKRLKELKNQKRSEKRDADEVTQVMIKECQELLRLFGLPYIVAPQEAEAQCSKLLELKLVDGIVTDDSDVFLFGGTRVYRNMFNQNKFVELYLMDDMKREFNVNQMDLIKLAHLLGSDYTMGLSRVGPVLALEILHEFPGDTGLFEFKKWFQRLSTGHASKNDVNTPVKKRINKLVGKIILPSEFPNPLVDEAYLHPAVDDSKQSFQWGIPDLDELRQFLMATVGWSKQRTNEVLLPVIQDMHKKQFVGTQSNLTQFFEGGNTNVYAPRVAYHFKSKRLENALSSFKNQISNQSPMSEEIQADADAFGESKGSDELQSRILRRKKMMASKNSSDSDSDSEDNFLASLTPKTNSSSISIENLPRKTKLSTSLLKKPSKRRRK P28748 SPI1_SCHPO BINDING 17..24; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62825"; BINDING 67; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62825"; BINDING 121..124; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62825"; BINDING 149..151; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P62825" MOD_RES 20; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1289.03c; CHAIN 1..216; /note="GTP-binding nuclear protein spi1"; /id="PRO_0000208735" MAQPQNVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATLGVEVHPLHFHTNFGEICFNVWDTAGQEKLGGLRDGYYIQGQCGIIMFDVTSRITYKNVPHWWRDLVRVCENIPIVLCGNKVDVKERKVKAKAITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLVGNPNLEFVASPALAPPEVQVDQQLLAQYQQEMNEAAAMPLPDEDDADL P28758 SODC_SCHPO BINDING 47; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 49; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 64; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 64; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 72; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 81; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 84; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 121; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P00445"; BINDING 144; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00445" CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000250|UniProtKB:P85978}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445}; SPAC821.10c; CHAIN 2..154; /note="Superoxide dismutase [Cu-Zn]"; /id="PRO_0000164127" DISULFID 58..147; /evidence="ECO:0000250|UniProtKB:P00445" MVRAVAVLRGDSKVSGVVTFEQVDQNSQVSVIVDLVGNDANAKRGFHIHQFGDNTNGCTSAGPHFNPEGKTHGDRTAAVRHVGDLGNLESDAQGNIKTTFSDSVISLFGANSIIGRTIVIHAGEDDLGKGTSEESLKTGNAGARNACGVIGIAV P28876 PMA2_SCHPO ACT_SITE 464; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250" BINDING 720; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 724; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate; Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1; Evidence={ECO:0000305|PubMed:1833395}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20853; Evidence={ECO:0000305|PubMed:1833395}; PTM: In addition to transient phosphorylation of the active site Asp residue, this protein, but not the product of the pma1 locus, is phosphorylated efficiently in isolated plasma membrane. SPCC1020.01c; CHAIN 1..1010; /note="Plasma membrane ATPase 2"; /id="PRO_0000046270" MQRNNGEGRPEGMHRISRFLHGNPFKNNASPQDDSTTRTEVYEEGGVEDSAVDYDNASGNAAPRLTAAPNTHAQQANLQSGNTSITHETQSTSRGQEATTSPSLSASHEKPARPQTGEGSDNEDEDEDIDALIEDLYSQDQEEEQVEEEESPGPAGAAKVVPEELLETDPKYGLTESEVEERKKKYGLNQMKEEKTNNIKKFLSFFVGPIQFVMELAAALAAGLRDWVDFGVICALLLLNATVGFVQEYQAGSIVDELKKTMALKASVLRDGRVKEIEASEIVPGDILHLDEGTICPADGRLITKDCFLQVDQSAITGESLAVDKHQNDTMYSSSTVKRGEAFMVVTATADSTFVGRAASLVGAAGQSQGHFTEVLNGIGTILLVLVILTLLCIYTAAFYRSVRLAALLEYTLAITIIGVPVGLPAVVTTTMAVGAAYLAKKKAIVQKLSAIESLAGVEILCSDKTGTLTKNRLSLGEPYCVEGVSPDDLMLTACLASSRKKKGLDAIDKAFLKALRNYPKAKDQLSKYKVLDFHPFDPVSKKITAYVEAPDGQRITCVKGAPLWVFKTVQDDHEVPEAITDAYREQVNDMASRGFRSLGVARKADGKQWEILGIMPCSDPPRHDTARTIHEAIGLGLRIKMLTGDAVGIAKETARQLGMGTNVYNAERLGLSGGGDMPGSEVNDFVEAADGFAEVFPQHKYAVVDILQQRGYLVAMTGDGVNDAPSLKKADAGIAVEGASDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYAYVVYRIALSLHLEIFLGLWLIIRNQLLNLELIVFIAIFADVATLAIAYDNAPYAMKPVKWNLPRLWGLATIVGILLAIGTWIVNTTMIAQGQNRGIVQNFGVQDEVLFLQISLTENWLIFITRCSGPFWSSFPSWQLSGAVLVVDILATLFCIFGWFKGGHQTSIVAVIRIWMYSFGIFCLIAGVYYILSESSSFDRWMHGKHKERGTTRKLEDFVMQLQRTSTHHEAEGKVTS P30655 PSB5_SCHPO ACT_SITE 62; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; SPAC4A8.13c; PROPEP 1..61; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000026609" CHAIN 62..272; /note="Probable proteasome subunit beta type-5"; /id="PRO_0000026610" MNSIVSKYTQSTNNDDPKKIIEEEGFTNRFDVVPVPQSSLYLRNLTDETKNKHCLIKMNHGTTTLAFRYQHGIVVCVDSRASAGPLIASQTVKKVIEINPYLLGTLAGGAADCQFWETVLGMECRLHQLRNKELISVSAASKILSNITYSYKGYGLSMGTMLAGTGKGGTALYYIDSDGTRLKGDLFSVGSGSTFAYGVLDSGYRWDLSKQEALYLAQRSIVAATHRDAYSGGSVNLYHIDENGWVFHGNFDVDSLIWEAKDNENSFAHIPR P30821 P25_SCHPO MOD_RES 181; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3C7.14c; CHAIN 1..202; /note="P25 protein"; /id="PRO_0000200766" MSTANTVAIVIYSTYGHVVKLAEAEKAGIEKAGGKAVIYQFPETLSPEILEKMHAAPKPNYPVVTLDVLTQYDAFLFGYPTRYGTPPAQFRTFWDSTGGLWVQGALHGKYFGQFFSTGTLGGGQESTALTAMTSFVHHGMIFVPLGYKNTFSLMANVESIHGGSSWGAGSYAGADGSRNVSDDELEIARIQGETFFKTVFRK P31406 VATA_SCHPO BINDING 258..265; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00499" CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000250|UniProtKB:P17255}; SPAC343.05; CHAIN 1..619; /note="V-type proton ATPase catalytic subunit A"; /id="PRO_0000144590" MAGGIELAKKAIRSLKNYDEHENRYGSIFSVSGPVVVAANMLGCSMYELVRVGHEELVGEVIRIHQDKCTIQVYEETSGLTVGDPVQRTGKPLSVELGPGLAETIYDGIQRPLKQIFDKSQSIYIPRGINTESLNREHKWDFTPNKDLRIGDHVSGGDVFGSVFENSLFNDHKIMLPPRARGTVTYIAEAGSYHVDEKLLEVEFNGKKHSFSMLHTWPVRAARPVADNLTANQPLLTGQRVLDALYPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDLIVYVGCGERGNEMAEVLMDFPELTIDINGKPEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYYRDQGKNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGAKLASFYERAGRARCLGSPDREGTVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINTSLSYSKYINALQPWYEERVPGFNTLRDQIKQIIQQEDSMLEIIQLVGKSALSETDKVTLDIAGIIKNDFLQQNGYSDYDRCCPLYKTYHMMRNMIAYYTKAKSAVETGSVPWSKIKESTSDIFYELTSMKFENPNEGEKEIVEHYETLHKKIEDKFHTLTE P31411 VATB_SCHPO BINDING 378; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P21281" MOD_RES 491; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 492; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 502; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC637.05c; CHAIN 1..503; /note="V-type proton ATPase subunit B"; /id="PRO_0000144647" MASLFDINAAAAVKDYSIKPRLSYNTVNSITGPLVILDNIRRPQYNEIVNLNLPDGSVRSGQVLEVAGHKAIVQVFEGTSGVDVRKTTIDFTGHSMRIPVSEDMLGRVFNGSGLPIDKGPNLLAEDYLDINGSPINPYARIYPEEMIQTGISSIDGLNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKRPTKDVHDGHEDNFSIVFAAMGVNLETARFFQRDFEENGSFERVTLFLNLANDPTIERIITPRLALSASEFLAYQTEKHVLTILTDMTSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNNAIYPPINVLPSLSRLMKSAIGEGMTRNDHGDVSNQLYAMYAIGRDAASMKSVVGEEALSQEDRLALEFLGKFEKTFISQGAYENRTIFETLDLAWSLLRIFPREMLTRIPKKILDQYYSRSSAYTESSKDVIDNTPESS P32434 PGTB1_SCHPO BINDING 195..197; /ligand="geranylgeranyl diphosphate"; /ligand_id="ChEBI:CHEBI:57533"; /evidence="ECO:0000250|UniProtKB:P53610"; BINDING 254..257; /ligand="geranylgeranyl diphosphate"; /ligand_id="ChEBI:CHEBI:57533"; /evidence="ECO:0000250|UniProtKB:P53610"; BINDING 260; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P53610"; BINDING 262; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P53610"; BINDING 263..266; /ligand="geranylgeranyl diphosphate"; /ligand_id="ChEBI:CHEBI:57533"; /evidence="ECO:0000250|UniProtKB:P53610"; BINDING 312; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P53610" CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.59; Evidence={ECO:0000269|PubMed:9781874}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21241; Evidence={ECO:0000269|PubMed:9781874}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P53610}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P18898}; SPAC2E1P5.04c; CHAIN 1..355; /note="Geranylgeranyl transferase type-1 subunit beta"; /id="PRO_0000119778" MELTRAKHIAFFKRHLILFPTPYEEHDCERTVLAFFCLLGLDLLNALNTIDDDDKKSWIEWIYKNYVTKESKGIKYSGFQAYRTGIQPISFEQEPQLAGTVFSICCLLFLGDNLSRIDRDLIKNFVELCKTSQGHFRSIAVPSCSDQDMRQLYMATTIASLLDFSLSDPLCSIQYIKSCQRYEGGFSLLPYGEAHAGATFCALASWSLILKMIPNSSLNTSNQSYNLMDCVPKVERLIRWLASRQLSSGGLNGRTNKDVDTCYAYWVLSSLKLLDALPFIDGGELEKYLLLHAQHALGGFSKTPGEFPDVLHSALGLYAMAYQDDKSFPKVNADIHMTSKYINICRDCIQAAKGK P32586 PYP2_SCHPO ACT_SITE 630; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; SPAC19D5.01; CHAIN 1..711; /note="Tyrosine-protein phosphatase 2"; /id="PRO_0000094859" MLHLLSKDEFNSTLKSFEEQTESVSWIIDLRLHSKYAVSHIKNAINVSLPTALLRRPSFDIGKVFACIKCNVKVSLDEINAIFLYDSSMAGMNRIYDLVQKFRRGGYSKKIYLLSNGFEAFASSHPDAIVSTEMVKESVPYKIDINENCKLDILHLSDPSAVSTPISPDYSFPLRVPINIPPPLCTPSVVSDTFSEFASHAEYPGFSGLTPFSIHSPTASSVRSCQSIYGSPLSPPNSAFQAEMPYFPISPAISCASSCPSTPDEQKNFFIVGNAPQQTPARPSLRSVPSYPSSNNQRRPSASRVRSFSNYVKSSNVVNPSLSQASLEIIPRKSMKRDSNAQNDGTSTMTSKLKPSVGLSNTRDAPKPGGLRRANKPCFNKETKGSIFSKENKGPFTCNPWGAKKVSPPPCEVLADLNTASIFYKFKRLEEMEMTRSLAFNDSKSDWCCLASSRSTSISRKNRYTDIVPYDKTRVRLAVPKGCSDYINASHIDVGNKKYIACQAPKPGTLLDFWEMVWHNSGTNGVIVMLTNLYEAGSEKCSQYWPDNKDHALCLEGGLRISVQKYETFEDLKVNTHLFRLDKPNGPPKYIHHFWVHTWFDKTHPDIESITGIIRCIDKVPNDGPMFVHCSAGVGRTGTFIAVDQILQVPKNILPKTTNLEDSKDFIFNCVNSLRSQRMKMVQNFEQFKFLYDVVDYLNSGVNQASKPLMT P32587 PYP3_SCHPO ACT_SITE 227; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; SPAC11E3.09; CHAIN 1..303; /note="Tyrosine-protein phosphatase 3"; /id="PRO_0000094860" MSFKEVSTENGVLTPLITIKEKAYMIIEGLNEEEIELLNTRLPKLSKKALARNRYSNIVPYENTRVRLDPMWKEACDYINASIVKIPSGKTFIATQGPTSNSIDVFWKMVWQSVPKSGIIVMLTKLRERHRLKCDIYWPVELFETLNIGDLSVILVKVYTLTSLNEVQVREFELNKDGVKKKILHFYYNGWPDFGAPHTFSLLSLTRYIKSLSYSPDFETAPIIVHCSAGCGRTGTFMALFEILSQTDDSTSTSKFEVDNIANIVSSLRSQRMQSVQSVDQLVFLYTVSQELLQGKEFLLPQL P34068 MFM1_SCHPO MOD_RES 39; /note="Cysteine methyl ester"; /evidence="ECO:0000269|PubMed:1547790" SPAPB8E5.05; PROPEP 1..30; /evidence="ECO:0000269|PubMed:1547790"; /id="PRO_0000021707"; PROPEP 40..42; /note="Removed in mature form"; /id="PRO_0000021709" LIPID 39; /note="S-farnesyl cysteine"; /evidence="ECO:0000269|PubMed:1547790" MDSMANSVSSSSVVNAGNKPAETLNKTVKNYTPKVPYMCVIA P34069 MFM2_SCHPO MOD_RES 41; /note="Cysteine methyl ester"; /evidence="ECO:0000269|PubMed:1547790" SPAC513.03; PROPEP 1..32; /evidence="ECO:0000269|PubMed:1547790"; /id="PRO_0000021710"; PROPEP 42..44; /note="Removed in mature form"; /id="PRO_0000021712" LIPID 41; /note="S-farnesyl cysteine"; /evidence="ECO:0000269|PubMed:1547790" MDSIATNTHSSSIVNAYNNNPTDVVKTQNIKNYTPKVPYMCVIA P36209 ERG4_SCHPO BINDING 333; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 337; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 373; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 385..386; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 425; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 429..433; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 440; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86" CATALYTIC ACTIVITY: Reaction=ergosterol + NADP(+) = ergosta-5,7,22,24(28)-tetraen-3beta-ol + H(+) + NADPH; Xref=Rhea:RHEA:18501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16933, ChEBI:CHEBI:18249, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.71; Evidence={ECO:0000305|PubMed:8125337}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18503; Evidence={ECO:0000305|PubMed:8125337}; SPAC20G4.07c; CHAIN 1..453; /note="Delta(24(24(1)))-sterol reductase"; /id="PRO_0000207492" MKSTVKKSAPREFGGAKGALAIMTGFPCLMYYLWACSKFNDSQFIKPESFTIAGFQNFFRTLGHYIYVGAYPTRYAFLVFWSFCIVQAVMYLTLPGVRTQGLPLKHRNNERLPYLCNAIWSFYTTIVILAVLHVTHVFPITTFIDMFGPLMSVAIITAFVCTFVLYTGTLLFGDRLFDKPHRLSGNPIYDAFMGACLNPRLGKLLDFKMFFEVRIPWFILFFISVGAAVRQYETYGTVSPQVLFVCLGHYLYANACSKGEQLIVPTWDMAYEKFGFMLIFWNMAGVPFTYSHCTLYLFSHDPSVYNWSTQYTTGIYVLLLCCYYIFDTCNGQKNHFRNQIYGTEVHRKTFPQLPWLIIKNPTFIRCANGGTLLTSGWYRYARKIHYTADFFQSLSWALITGFQSPLPYFYPCFFFVVLVHRVSRDIKKCKAKYGADFDEYCRICPYLFIPYIF P36580 ALF_SCHPO ACT_SITE 108; /note="Proton donor"; /evidence="ECO:0000250" BINDING 61; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 109; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 143; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 225; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 226; /ligand="dihydroxyacetone phosphate"; /ligand_id="ChEBI:CHEBI:57642"; /evidence="ECO:0000250"; BINDING 264; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 265..267; /ligand="dihydroxyacetone phosphate"; /ligand_id="ChEBI:CHEBI:57642"; /evidence="ECO:0000250"; BINDING 286..289; /ligand="dihydroxyacetone phosphate"; /ligand_id="ChEBI:CHEBI:57642"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. {ECO:0000250}; MOD_RES 289; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 312; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 340; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 342; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19C2.07; CHAIN 1..358; /note="Fructose-bisphosphate aldolase"; /id="PRO_0000178761" MGILDIVPTGVITGDNVLKLFTYAREHGFAIPAINVTSSSTAIAALEAAREARSPIILQTSNGGAHFFAGKESSNEGQKASIAGSIAAAHYIRSIAPFFGVPVVMHSDHCAKKLLPWMDGMFEADEAYFKIHGEPLFSSHMLDLSEEPKKENIAQVKEYCKRAVPMKIWIEMEIGITGGEEDGVDNSHVSHTELYTQPEDIWDVYRELSSVTPYFSIAAAFGNVHGVYKPGNVKLQPALLGQHQAYVKEQLKTTNDKPVFFVFHGGSGSSVNEFRTGIKCGVVKVNIDTDTQFAYVEGVRDYVLKYKDYLMTPVGNPEGADKPNKKKFDPRVWIHEGEKTMTKRVLTALEDFYTVNTL P36586 YPT5_SCHPO BINDING 21..28; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 70..74; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 128..131; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 211; /note="Cysteine methyl ester"; /evidence="ECO:0000269|PubMed:8226998" SPAC6F6.15; CHAIN 1..211; /note="GTP-binding protein ypt5"; /id="PRO_0000121312" LIPID 209; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:8226998"; LIPID 211; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:8226998" MASNTAPKNVVTINQKLVLLGDSAVGKSSLVLRFVKDQFDDYRESTIGAAFLTQTLPIDENTSVKLEIWDTAGQERYKSLAPMYYRNANCAIVVYDITQAASLEKAKSWIKELQRQAPEGIVIALAGNKLDLAQERRAVEKADAEAYAAEANLLFFETSAKTAENVNELFTAIAKKLPLEDKLNQARGAVNRGVNLSEARPAAQPSGSCSC P36587 NCPR_SCHPO BINDING 59..64; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 110..113; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 156..165; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 191; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 285; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 441..444; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 459..461; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 476..479; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 540; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 602..603; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 608..612; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 644; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"; BINDING 678; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212" CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; SPBC29A10.01; CHAIN 1..678; /note="NADPH--cytochrome P450 reductase"; /id="PRO_0000167609" MKTYEYVLLVIILILSLCYFIYNNFLNKPKAPERRVVATDSIVELMEAEKLTAAVFFGSQTGTAEDFAYRFSTEAKANFNLTNMVFDLENYDLTDLDNFDRSKLLVFFLATYGEGEPTDNAEAFLQLLEGDDTVFSSGKGIEDTPFEGIRYAIFGLGNHTYEYYNAMAKKVDAAMTRLGATRVGNLGLGDDAAGMLEEDYLQWKDDTLPEIGKLFHLQEVHKEYNPMFEVIEKPEISNTSSTVFLGEPSRQQLKGNVASKAPRSQANPFFSSPVRSLELFKSGSRNCLHLELDIADSGMRYQTGDYASICPMNPSQAVDDLLEVLGLKEKRDTVIIVKPIDTLDKAPVLSPTTYDTVFRYYYEICGIVSRQLLSFIAPFAPTPESKQELEKLGNDYDYFKKNVVDLHLNLAQVLRRVSPDAPFTKLPFSMLLENMAHMKPRYYSISSSSVVHPDKVHVTAVVDKKEWTDKNHIFYGLTTNYLLAHCRHMHGEKIPHPNGLEYTLEGPRKNWTGKIPMFVKKSTFRLAPPDVPIIMVGPGTGVAPFRGFVMERANLASKGVKVAKTLLFYGCQYSDKDFLYKEEWQQYKDVLKDSFELITAFSREQDHKIYVQHRLLEHSDTIAKLVEEGAAFYICGDADHMAKDVVNALASILTTVDVDGMKAVKALRDDNRFFEDTW P36590 KTHY_SCHPO BINDING 14..21; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000269|PubMed:1327149}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13518; Evidence={ECO:0000305|PubMed:1327149}; SPCC70.07c; CHAIN 1..210; /note="Thymidylate kinase"; /id="PRO_0000155213" MSKQNRGRLIVIEGLDRSGKSTQCQLLVDKLISQHEKAELFKFPDRTTAIGKKIDDYLKESVQLNDQVIHLLFSANRWETIQYIYEQINKGVTCILDRYAFSGIAFSAAKGLDWEWCKSPDRGLPRPDLVIFLNVDPRIAATRGQYGEERYEKIEMQEKVLKNFQRLQKEFREEGLEFITLDASSSLEDVHSQIVDLVSNVNIHETLDVL P36591 DYR_SCHPO BINDING 239; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 246..252; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 260..265; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 292..294; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 308; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 314..316; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 365..372; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660}; SPCC1223.08c; CHAIN 1..461; /note="Dihydrofolate reductase"; /id="PRO_0000186377" MSKPLKVLCLHGWIQSGPVFSKKMGSVQKYLSKYAELHFPTGPVVADEEADPNDEEEKKRLAALGGEQNGGKFGWFEVEDFKNTYGSWDESLECINQYMQEKGPFDGLIGFSQGAGIGAMLAQMLQPGQPPNPYVQHPPFKFVVFVGGFRAEKPEFDHFYNPKLTTPSLHIAGTSDTLVPLARSKQLVERCENAHVLLHPGQHIVPQQAVYKTGIRDFMFSAPTKEPTKHPRDLTMIVAVSSPNLGIGKKNSMPWHIKQEMAYFANVTSSTESSGQLEEGKSKIMNVVIMGRSCYDSLPKKNRPLKDRINIVITRNSNYNFGLTKKEKMPENLYAADCIDSALDLVAEKYGADSDIQVGKVFIIGGSFLYGSALYHPLTKNLLFTRIHKEYPCDSFFPFEPAESSDWVRKAHPELEKFVGIPVEEGRLKAASSNKEEVEIEFELYGKNDDVNVALEKLSIC P36595 RPAB2_SCHPO PTM: Phosphorylated. SPCC1020.04c; CHAIN 1..142; /note="DNA-directed RNA polymerases I, II, and III subunit RPABC2"; /id="PRO_0000133796" MSDYEEDEAFGMDGAVMEEEVDELEMIDENGQSQQGVSHPGEPSTTVITEDVASSKTAQSGKAVAKEDRTTTPYMTKYERARILGTRALQISMNAPVLVDLEGETDPLQIAMKELAQKKIPLLVRRYLPDGSYEDWSVAELI P36598 THI1_SCHPO MOD_RES 208; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1486.10; CHAIN 1..775; /note="Thiamine repressible genes regulatory protein thi1"; /id="PRO_0000114983" MNEEIGFLKNQLFADVKDLERKKKRRVPPEQRRRVFRACKHCRQKKIKCNGGQPCISCKTLNIECVYAQKSQNKTLSREYLEELSERQLCLEYIFSRMCPNFNLETKNLISISKKLSENENLPVSKIAEVTNELDTLVRINDQLSRNHISGTTEEMQSSSSLIAGEVQPGISFRDQLKVGKLEDTLYLGPTTSEAFIERLQNELELESISEDDLYSKRLSPSVSYSEFDEQLLLHARSLIPSKAVVEFLINSFFINVQTNLFVYHPHFFKCRLEIFLAMENQIDAGFLCILLMVLAFGNQYTAEQQEDVSKSNFHASNIGNRLFSAALSIFPLVLLQSDVSAVQSSLLIGLYLQSTIYEKSSFAYFGLAIKFAVALGLHKNSDDPSLTQNSKELRNRLLWSVFCIDRFVSMTTGRRPSIPLECISIPYPVILPDLEIPGSQSIVENMRAVINLAKLTNEICDSLYWNPSPSFESQVNSVRRIYARLELWKSDLHSSVVFDESAVQHPLFRSNAHVQMIYDNAIMLTTRVIMVKKLKDKDLTAENRRYIQLCVESATRVINIAHLLLTHKCLSSLSFFGLHVPFASAPILLLSLHYENSQDIQAVVTKLWQVLEFLSSRCEFARESLNYLKSFNKQLSRRNAPDINNPIADFQNSFQNWQSWVGDMSHGDMLSTFKLTGESSNGSNSTPNEAFQPFDQTSSLYNVPGLNKSYVSNQPSLLTPETFLPDPVLNLEVDKQWTAPTFLSWTELLGPTNVSEQSSHTAEQTSNLTLEKNG P36612 PRS4_SCHPO BINDING 232..239; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC4.07c; CHAIN 1..448; /note="26S proteasome regulatory subunit 4 homolog"; /id="PRO_0000084684" MGQAQSGNFSNFGDGANGDNKKDQKKDKPKYEPPVPTRTGRRKKKAQSGPDASAKLPTVIPTTRCRLRLLKMQRIHDHLLMEEEYVQNQERLKPQDERTQEERNRVDEIRGTPMSVGTLEEIIDDDHAIVSTAGPEYYVSIMSFVDKDMLEPGCSVLLHHKAMSIVGLLLDDTDPMINVMKLDKAPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPRLVRQLFNAAEEHSPSIVFIDEIDAIGTKRYDAQSGAEREIQRTMLELLNQLDGFDTSQRDIKVIMATNRISDLDPALIRPGRIDRKILFENPDEATKRKIFTIHTSKMNLGEDVNLEELIQCKDDLSGAEIKAIVSEAGLLALRERRMRVVMDDFRQAREKVLKTKDEGGPAGGLYI P36618 CDC16_SCHPO SPAC6F6.08c; CHAIN 1..299; /note="Cell division control protein 16"; /id="PRO_0000208009" MPSIDCKRLQKLAPKSPENQSKCISRLRYMVMLDQVESDEGGNSSTRPYVWAVLLNAPPRNADEYIRYVRQGPSPMAQKIQNDVSRTLVVESQFHSRVSQSSLSRLLNAYVWKRGALYVQGMNVLASPFLYACKSENQAFQFFDRLLQNECPLYVLPNIDGVHRGAKLLDKCLEVLDHRLYTYLLSKGLTAKIYALPSILTLSACTAPLSEALTIWDFLFAYGIHLNILCVIAQMFIFREQLIDHPSPMTLLRTFPPLNAKNIMKITILLISKLPPELYNLLARHAWDSEAGVLIDRLT P36619 PMD1_SCHPO BINDING 455..462; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 1154..1161; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPCC663.03; CHAIN 1..1362; /note="Leptomycin B resistance protein pmd1"; /id="PRO_0000093452" MSLHSKKSTSTVKDNEHSLDLSIKSIPSNEKNFSTEKSENEASESHVVDVVKDPFEQYTPEEQEILYKQINDTPAKLSGYPRILSYADKWDIMLQLAGTITGIGAGLGMPLMSLVSGQLAQAFTDLASGKGASSFQHTVDHFCLYFIYIAIGVFGCSYIYTVTFIIAGERIARRIRQDYLHAILSQNIGYFDRLGAGEITTRITTDTNFIQDGLGEKVGLVFFAIATFVSGFVIAFIRHWKFTLILSSMFPAICGGIGLGVPFITKNTKGQIAVVAESSTFVEEVFSNIRNAFAFGTQDILAKLYNKYLITAQRFGINKAIAMGLMVGWMFFVAYGVYGLAFWEGGRLLHAGDLDVSKLIGCFFAVLIASYSLANISPKMQSFVSCASAAKKIFDTIDRVSPINAFTPTGDVVKDIKGEIELKNIRFVYPTRPEVLVLDNFSLVCPSGKITALVGASGSGKSTIIGLVERFYDPIGGQVFLDGKDLRTLNVASLRNQISLVQQEPVLFATTVFENITYGLPDTIKGTLSKEELERRVYDAAKLANAYDFIMTLPEQFSTNVGQRGFLMSGGQKQRIAIARAVISDPKILLLDEATSALDSKSEVLVQKALDNASRSRTTIVIAHRLSTIRNADNIVVVNAGKIVEQGSHNELLDLNGAYARLVEAQKLSGGEKDQEMVEEELEDAPREIPITSFGDDDEDNDMASLEAPMMSHNTDTDTLNNKLNEKDNVVFEDKTLQHVASEIVPNLPPADVGELNEEPKKSKKSKKNNHEINSLTALWFIHSFVRTMIEIICLLIGILASMICGAAYPVQAAVFARFLNIFTDLSSTDFLHKVNVFAVYWLILAIVQFFAYAISNFAMTYAMEAVLQRIRYHLFRTLLRQDVEFFDRSENTVGAITTSLSTKIQSLEGLSGPTLGTFFQILTNIISVTILSLATGWKLGLVTLSTSPVIITAGYYRVRALDQVQEKLSAAYKESAAFACESTSAIRTVASLNREENVFAEYCDSLIKPGRESAIASLKSGLFFSAAQGVTFLINALTFWYGSTLMRKGEYNIVQFYTCFIAIVFGIQQAGQFFGYSADVTKAKAAAGEIKYLSESKPKIDTWSTEGKKVESLQSAAIEFRQVEFSYPTRRHIKVLRGLNLTVKPGQFVAFVGSSGCGKSTTIGLIERFYDCDNGAVLVDGVNVRDYNINDYRKQIALVSQEPTLYQGTVRENIVLGASKDVSEEEMIEACKKANIHEFILGLPNGYNTLCGQKGSSLSGGQKQRIAIARALIRNPKILLLDEATSALDSHSEKVVQEALNAASQGRTTVAIAHRLSSIQDADCIFVFDGGVIAEAGTHAELVKQRGRYYELVVEQGLNKA P36620 ILVB_SCHPO BINDING 134; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 236; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 351..372; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 403..422; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 548; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 575; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; TRANSIT 1..140; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP35G2.07; CHAIN 141..669; /note="Acetolactate synthase, mitochondrial"; /id="PRO_0000035663" MTVLAPLRRLHTRAAFSSYGREIALQKRFLNLNSCSAVRRYGTGFSNNLRIKKLKNAFGVVRANSTKSTSTVTTASPIKYDSSFVGKTGGEIFHDMMLKHNVKHVFGYPGGAILPVFDAIYRSPHFEFILPRHEQAAGHAAQAYSRVTKKPGVVLVTSGPGATNVITPIADALADGTPLVVFSGQVATSAIGSDAFQEADMVGISRSCTKWNVMVKDVADLPRRIDEAFEIATSGRPGPVLVDLPKDVTASVLKEPIPILSSVPSMNRRMKEVLEEGSKNVTAKIDRVANLLKLAKKPVIFCGHGVLANPECPTLLRKFSERLQIPVTTSLLGLGAVDERSDLSLHMLGMHGSGYANMAMQEADLILALGVRFDDRVTGNVSLFAPQARLAAAEERGGIIHFDISPKNIGKVVQPTEAIEGDVYESLKLLDSATKNIKIPSRFDWLSQIQTWKERFPFTFTRSAPGELVKPQEVIQELDKQTSDIKDKVTITTGVGAHQMWAATFYRWTKPSSLVTSGGLGTMGFGLPAAIGASVAAPKDIVIDIDGDASFSMTGMELATVRQFDIPVKILILNNEEQGMVTQWQNLFYEKRYSHTHQKNPNFVKLADAMGIKALRVEKREDLAKKMKEFLSTKGPVLMEVLVAQKEHVYPFVPGGKALHQFILHESLS P36632 RAD26_SCHPO SPAC9E9.08; CHAIN 1..614; /note="DNA repair protein rad26"; /id="PRO_0000097152" MMADESFDLESLGSDEIFEGVNLDELEQQAQTQVQAQSSQVVVPSEKQKQNLNLPNSYTNSSQKVRESTVNSQASLSSNDLRTELLIKSGENAILRANLLKQSEANNAALESLNNSIKQKQDEYQRKLEELKKEIEYAKTKSLFHEREAQDAIETMKKMKRDVKNSPIMKKSHEEDGDNKLLSSSDQLAKSTKHAAKNSPSKKKRKTSVATAEDASTDSVSSSIAISDASLSLSLMKDLLSLQKREDLYFSSRTLAYVFGGCMHSLETIEGEEEGECLFNNLKALIYSPDLSMDSSNYVQSVVQTSSSILNYSMKKLLYNASFAITSLFNALLILDPKSSTFIFQENVVSLISGFLLKEYEKSNFLDSKFYVLIDFLYLYLSIARESADDFANITKAVDPSLFESCIRVQNAPSLIKCGVCLIISSTTPSFCASVNLLNADDKSQESLMQLFTTMAHILVVTTRERINFPELNEWITLHRFVISFFTVFIQMSGNIGKEILKVCNPLIVCIGLAITWYHQQLLSSMYPQNECVEILVSLVRLLYILSSEDLSSKFMLAENALQPRFVYAIACCAFGDTEQKAFGNLGEEMYFLTTELLEVCVSPEELEQLYTNF P37382 RPB3_SCHPO SPCC1442.10c; CHAIN 1..297; /note="DNA-directed RNA polymerase II subunit RPB3"; /id="PRO_0000132747" MDSETHITIRNISKNSVDFVLTNTSLAVANSLRRVVLAEIPTVAIDLVEINVNTSVMPDEFLAHRLGMIPLDSSNIDEPPPVGLEYTRNCDCDQYCPKCSVELFLNAKCTGEGTMEIYARDLVVSSNSSLGHPILADPKSRGPLICKLRKEQEISLRCIAKKGIAKEHAKWSPTSAVAFEYDPWNKLQHTDYWFENDADAEWPKSKNADWEEPPREGEPFNFQEEPRRFYMDVESVGSIPPNEIMVQGLRILQEKLAVLVRDLDEEQPTQLSANELNMEENAEMNWSPYQNGEENTW P37818 ARGI1_SCHPO BINDING 119; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 142; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 142; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 144..148; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 144; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 146; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 155..157; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 198; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 247; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 247; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 249; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 261; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 292; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608" CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742}; SPBP26C9.02c; CHAIN 1..323; /note="Arginase"; /id="PRO_0000173709" MSPHKIPEVHRHIMSSRYMEGNAVSIINMPFSGGQPKDGAELAPEMIEAAGLPEDLERLGYSVNVVQNPKFKSRPLKEGPNQALMKNPLYVSNVTRQVRNIVQQELEKQRIAVNIGGDHSLAIGTVEGVQAVYDDACVLWIDAHADINTPDSSPSKNLHGCPLSFSLGYAEPLPEEFAWTRRVIEERRLAFIGLRDLDPMERAFLRERSITAYTMHDVDKYGIARVVEMALEHINPGRRRPIHLSFDVDACDPIVAPATGTRVPGGLTFREAMYICESVAETGSLVAVDVMEVNPLLGNKEEAKTTVDLARSIVRTCLGQTLL P38938 CEK1_SCHPO ACT_SITE 713; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 595..603; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 618; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 525; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 748; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1450.11c; CHAIN 1..1338; /note="Serine/threonine-protein kinase cek1"; /id="PRO_0000085847" MKHIKNEREEVFLEDDQAQHSQAELLSSKDENLQPSIPLSPVAFELDFSGNFQFISDNSSELLDIPKDKIIGHSVAEVLGTDGYNAFMRAVNCLLKDDSHSYHVRFQHSINANHANQNYYTAKGDLPSDEKITKPFDAIGILIRHPGSAIPAHTMWVVNPATNSLGSVSPLVTKLLDVIGFGASLLDKYLCDLRTSYHKHNSLDALPLPTPEFCQICEREIQSWFFELHSKFCLSTSTYESVVQAAQDSLLYFRSTLLEIQEGMQKDSSLVPVYKNEPLIVDADDYFFTDENKQTLSLCSFLSQVMYYLEVAIDITIPPVKIIVNFDKVDSLRVQSPRSEKATIELDNYNPSLENCSSAVIALWEDIKTAVDTKITGVLRLRNAIYYSERIRLEIDHHVQEIIDDVVSNLVTNHSSTSLGHLESKLAPSITFPDACDALEAEECITRPGSATNTPQSDRSLDINDLSRSSSYSRHLSHVSLSNPDFAIGSPMSQDSSNYSSPLHRRKASDSNFSDPRFDDLKYLSPNSSPRFVASDGPNRPASNGRSSLFSRGRASNLGDVGLRLPSPSPRIHTIVPNSAPEHPSINDYKILKPISKGAFGSVYLAQKRTTGDYFAIKILKKSNMIAKNQVINVRAERAILMSQGESPFVAKLYYTFQSKDYLYLVMEYLNGGDCGSLLKTMGVLDLDWIRTYIAETVLCLGDLHDRGIIHRDIKPENLLISQNGHLKLTDFGLSRVGYMKRHRRKQSSSIPVLDLRDRSSAISDLSLSTASSVLEAQSLITPERPKRPSLNEKLLSLDGTSIRLAGQSFNYENSAEDSPTATNTPTSQVDESNIFRSTDSPRVQPFFENKDPSKRFIGTPDYIAPEVILGNPGIKASDWWSLGCVVFEFLFGYPPFNAETPDQVFQNILARRINWPAEVFTAESSVALDLIDRLLCMNPANRLGANGVEEIKAHPFFKSVNWDTILEEDPPFVPKPFSPEDTVYFDSRGLKGFDFSEYYNQPTVTEAQKLEEERPASSIPQHVSGNRKGRLRSNTISTPEFGSFTYRNLDFLNKANRNTIQKLRKEHMAVKSAKTSVDDTFSQYMSRFKAKLSTSQSVGPVKSSRRASMADYEASTTTRVQDITTDSIDSIDDFDSLKEGRMLSFFDNLALEDHKGVSSTMSASQSQSSMHTALPDVTEGTSSDEHTTIQKGRIDNLQAQSLTHKRNAISYPGLFQLDRLQMIIPKDEIELAEILKKIFPKLTLVLIDDPWSILKKLLQNEQFNVVFLHFGNDKVSSSRLMYSVRTSATINSRVPFVYICEDETCIPTDLQSDGVLLKPITCENIESCLRKLDVWHS P40232 CSK2B_SCHPO PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}. SPAC1851.03; CHAIN 1..231; /note="Casein kinase II subunit beta"; /id="PRO_0000068255" MQLYSSESESDDSQYWVDWFLGLKGNEFFCEVDEDFIQDRFNLTGLSHEVPHYSQSLDLILDVLDPDLPEEVQDEVEASARHLYGLIHARYILTAQGLYKMLEKYKKCDFGHCPRVLCNGQPMLPVGLSDIAHTKSVKLYCPRCEDVYTPKSQRHASIDGAYFGTSFPHMLFQVYPELAVPKSQERYIPRIFGFKVHSYSATFKKQDVYKEKQKKRLQGAEAESKNKLAIT P40370 ENO11_SCHPO ACT_SITE 211; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 345; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 159; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 168; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 246; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 295; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 295; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 320; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 320; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 372..375; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 396; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Mg(2+) is required for catalysis and for stabilizing the dimer. {ECO:0000250}; MOD_RES 85; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 249; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 250; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 253; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 351; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 353; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 421; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1815.01; CHAIN 1..439; /note="Enolase 1-1"; /id="PRO_0000134058" MAIQKVFARQIYDSRGNPTVEVDLTTETGIHRAIVPSGASTGIWEALEMRDGDKTKWGGKGVLKAVGNVNNIIAPAVVKANLDVTDQKAADEFLLKLDGTENKSKLGANAILGVSMAICRAGAAQKKLPLWKYIAENFGTKGPYVLPVPSFNVLNGGSHAGGDLAFQEFMILPTGAPSFSEAMRWGAETYHTLKSIAKKRYGSSAGNVGDEGGIAPDLQTPQEALDLIVEAINKAGYEGKIKIGLDVASSEFYVDGKYDLDIKAAKPKPENKLTYQQLTDLYVELSKKYPIVSIEDPFDQDDWSAWTHMKAETDFQIVGDDLTVTNVKRLRTAIDKKCANALLLKVNQIGSVTESLNAVRMSYEAGWGVMVSHRSGETADTFISHLTVGIGAGQLKSGAPCRSERLAKYNELLRIEEELGSEGVYAGAHAGKYIKAAKF P40372 RL3A_SCHPO MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 140; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 207; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 372; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A5.03; STRAND 37..39; /evidence="ECO:0007829|PDB:8EV3"; STRAND 41..43; /evidence="ECO:0007829|PDB:8EUY"; STRAND 45..52; /evidence="ECO:0007829|PDB:8EUY"; STRAND 56..59; /evidence="ECO:0007829|PDB:8EUY"; STRAND 71..74; /evidence="ECO:0007829|PDB:8EUY"; STRAND 76..80; /evidence="ECO:0007829|PDB:8EUY"; STRAND 84..95; /evidence="ECO:0007829|PDB:8EUY"; STRAND 98..106; /evidence="ECO:0007829|PDB:8EUY"; STRAND 120..122; /evidence="ECO:0007829|PDB:8EUY"; STRAND 156..163; /evidence="ECO:0007829|PDB:8EUY"; STRAND 178..186; /evidence="ECO:0007829|PDB:8EUY"; STRAND 201..203; /evidence="ECO:0007829|PDB:8EUY"; STRAND 211..215; /evidence="ECO:0007829|PDB:8EUY"; STRAND 218..220; /evidence="ECO:0007829|PDB:8EUY"; STRAND 223..227; /evidence="ECO:0007829|PDB:8ETC"; STRAND 268..271; /evidence="ECO:0007829|PDB:8ETC"; STRAND 274..276; /evidence="ECO:0007829|PDB:8EUY"; STRAND 281..284; /evidence="ECO:0007829|PDB:8EUY"; STRAND 297..299; /evidence="ECO:0007829|PDB:8EV3"; STRAND 321..326; /evidence="ECO:0007829|PDB:8EUY"; STRAND 335..340; /evidence="ECO:0007829|PDB:8EUY"; STRAND 355..358; /evidence="ECO:0007829|PDB:8EUY"; STRAND 364..366; /evidence="ECO:0007829|PDB:8EUY"; STRAND 369..371; /evidence="ECO:0007829|PDB:8EUY" HELIX 112..118; /evidence="ECO:0007829|PDB:8EUY"; HELIX 131..139; /evidence="ECO:0007829|PDB:8EUY"; HELIX 141..153; /evidence="ECO:0007829|PDB:8EUY"; HELIX 188..197; /evidence="ECO:0007829|PDB:8EUY"; HELIX 205..208; /evidence="ECO:0007829|PDB:8EUY"; HELIX 229..233; /evidence="ECO:0007829|PDB:8ETC"; HELIX 348..351; /evidence="ECO:0007829|PDB:8EUY"; HELIX 373..379; /evidence="ECO:0007829|PDB:8EUY" TURN 14..16; /evidence="ECO:0007829|PDB:8EV3"; TURN 66..69; /evidence="ECO:0007829|PDB:8EUY"; TURN 166..170; /evidence="ECO:0007829|PDB:8EUY"; TURN 198..200; /evidence="ECO:0007829|PDB:8EUY"; TURN 291..294; /evidence="ECO:0007829|PDB:8EV3"; TURN 312..314; /evidence="ECO:0007829|PDB:8EUY" CHAIN 2..388; /note="Large ribosomal subunit protein uL3A"; /id="PRO_0000077249" MSHCKFEQPRHGSLGFLPRKRASRQRGKVKAFPKDDASKPVHLTAFLGYKAGMTHIVRDLDRPGSKMHKREILEAVTVIETPPMVVVGVVGYVETPRGLRSLTTVWAEHLSEEVKRRFYKNWFKSKKKAFTKYAKKYAESTQSINRELERIKKYCSVVRVLAHTQIRKTPLAQKKAHLMEIQVNGGSVADKVEWAREHFEKTVDIKSTFEQNEMIDVIGVTRGKGNEGTTARWGTKRLPRKTHRGLRKVACIGAWHPANVQWTVARAGNAGYMHRTQLNSKIYRIGAGDDAKNASTDFDATEKRITPMGGFVRYGVVENDFVMLNGATPGPVKRVLTLRKSLLTHTSRKALEPVSLKWIDTASKFGHGRFQTPAEAKQFLGTLKKDVA P40375 MAOX_SCHPO ACT_SITE 103; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 177; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 248; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 249; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 272; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 272; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 419; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate; Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38; CATALYTIC ACTIVITY: Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526; EC=1.1.1.38; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Divalent metal cations. Prefers magnesium or manganese. {ECO:0000250}; MOD_RES 445; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC794.12c; CHAIN 1..565; /note="NAD-dependent malic enzyme"; /id="PRO_0000160205" MPAGTKEQIECPLKGVTLLNSPRYNKDTAFTPEERQKFEISSRLPPIVETLQQQVDRCYDQYKAIGDEPLQKNLYLSQLSVTNQTLFYALISQHLIEMIPIIYTPTEGDAIKQFSDIYRYPEGCYLDIDHNDLSYIKQQLSEFGKSDSVEYIIITDSEGILGIGDQGVGGVLISVAKGHLMTLCAGLDPNRFLPIVLDVGTNNETHRKNHQYMGLRKDRVRGEQYDSFLDNVIKAIREVFPEAFIHFEDFGLANAKRILDHYRPDIACFNDDIQGTGAVALAAIIGALHVTKSPLTEQRIMIFGAGTAGVGIANQIVAGMVTDGLSLDKARGNLFMIDRCGLLLERHAKIATDGQKPFLKKDSDFKEVPSGDINLESAIALVKPTILLGCSGQPGKFTEKAIREMSKHVERPIIFPISNPTTLMEAKPDQIDKWSDGKALIATGSPLPPLNRNGKKYVISQCNNALLYPALGVACVLSRCKLLSDGMLKAASDALATVPRSLFAADEALLPDLNNAREISRHIVFAVLKQAVSEGMSTVDLPKDDAKLKEWIIEREWNPEYKPFV P40382 CDT1_SCHPO PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation. {ECO:0000269|PubMed:17039252}. SPBC428.18; CHAIN 1..444; /note="Cell division cycle protein cdt1"; /id="PRO_0000089459" MKCRALYSHDNNILIFGFCVQIMSAGSQTKLNFSVRKTRSSSKRSNAAIIEPPKNPEDSQIIPAVKRLKENLDTESLEQNEVLPPVKNESVLFLEKVFNAVDICVKFHLSINTKPTFVLLENKVSGLTKISLKITHLAQILTVWPESFAITPCFTIHQGKRVATYELSYPRNANLPEAFSRSIEFKRRLEKWLLEHCSETEIPAQQLQALPSLSKNTVNESSLVRKLNLEKSTSRELRIPTQTLEPKFTTNTAKYANELVSCSMLDSSSTLSKSVNSKINLKSHQSSSSVQNSSRKLTSSQLTLRQSSLFDRVRKKQKAMEAKKAEEFKNNLVVHTLAKEKVSFVRIIDLIFVQLSTWPTKRSFSMSEIVTSMQMSISSSLSPDQCAKAIELLSKALPAWCTINLLGNIQVVTFSRIVNGKPYLRSQLIEELQTKASITILSNS P40386 THI6_SCHPO ACT_SITE 433; /note="Proton acceptor; for hydroxyethylthiazole kinase activity"; /evidence="ECO:0000250" BINDING 40..44; /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"; /ligand_id="ChEBI:CHEBI:57841"; /evidence="ECO:0000250"; BINDING 72; /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"; /ligand_id="ChEBI:CHEBI:57841"; /evidence="ECO:0000250"; BINDING 73; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 92; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 111; /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"; /ligand_id="ChEBI:CHEBI:57841"; /evidence="ECO:0000250"; BINDING 137..139; /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate"; /ligand_id="ChEBI:CHEBI:62899"; /evidence="ECO:0000250"; BINDING 140; /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"; /ligand_id="ChEBI:CHEBI:57841"; /evidence="ECO:0000250"; BINDING 173; /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate"; /ligand_id="ChEBI:CHEBI:62899"; /evidence="ECO:0000250"; BINDING 199..200; /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate"; /ligand_id="ChEBI:CHEBI:62899"; /evidence="ECO:0000250"; BINDING 281; /ligand="5-(2-hydroxyethyl)-4-methylthiazole"; /ligand_id="ChEBI:CHEBI:17957"; /evidence="ECO:0000250"; BINDING 355; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 403; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 430; /ligand="5-(2-hydroxyethyl)-4-methylthiazole"; /ligand_id="ChEBI:CHEBI:17957"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3; CATALYTIC ACTIVITY: Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3; CATALYTIC ACTIVITY: Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:58296; EC=2.5.1.3; CATALYTIC ACTIVITY: Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212, ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616, ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; SPAC23H4.10c; CHAIN 1..518; /note="Probable thiamine biosynthetic bifunctional enzyme"; /id="PRO_0000157089" MKRQIDYSLYLVTSSSLIAPGSTIERQVEEGILGGVTLVQHREKDISTKCFVERAKRLSEICKKYDVPFLINDRIDVALAVGADGVHIGQDDMDCALARKILGDDAIIGVSTNNIEEIEKAAADGADYVGIGSIYETNTKDVKDRLIGITGLRKILEHVSKMHCQLGTVAIAGLNSSNIQRVIYLSEANGKRIDGIALVSAIMCSITPRETAKELRNLIATPPCFAQARSSLTTPKDLLNQIPAALQKLKDFTPLIHHLTNAVAKNFSANVTLAAYGSPTMGESYDEVADFAKAPGALVLNIGILENTKTYIHAAQVNNDLARPVILDPVAVGATTARSKVINTLLNYAYYDIIKGNEGEIMNLAGEQGLMRGVDSISQHTLAARITAVHRLAVERRCVVAMSGAVDVISDGNSTYVIKNGNPLLGQITASGCSLGSVMGVTASICQNDKLLAAITATLLYNIASELAVEAKNSCGDLLVQGPGTFIPIFVDKLHQLINETIKGNVDWIERAKLEKAE P40849 MFM3_SCHPO MOD_RES 38; /note="Cysteine methyl ester"; /evidence="ECO:0000269|PubMed:1547790" SPBPJ4664.03; PROPEP 1..29; /evidence="ECO:0000269|PubMed:1547790"; /id="PRO_0000021713"; PROPEP 39..41; /note="Removed in mature form"; /id="PRO_0000021715" LIPID 38; /note="S-farnesyl cysteine"; /evidence="ECO:0000269|PubMed:1547790, ECO:0000269|PubMed:8196631" MDSMANTVSSSVVNTGNKPSETLNKTVKNYTPKVPYMCVIA P40899 ISP3_SCHPO PTM: Palmitoylated by the erf2-erf4 complex. {ECO:0000269|PubMed:23843742}. SPAC1F8.05; CHAIN 1..182; /note="Spore wall structural constituent isp3"; /id="PRO_0000084260" MGLGNLCSYKQDDSLDILQKKVLIDAFNKVTIDGKPNVQHQQPTYWYPPPPPRHHKEHKKSHHHWEYSSDDDSSDDEESCEKKKPKCCEKKKPKCCESEQNNGCGRRNQLARRLAFLGSFGDGDCDGCNEAFTVTGPITYFRTCPDPLTGITPAVAAAAATPAAAATPATPAAAATPAAPAA P40903 ISP6_SCHPO ACT_SITE 221; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 253; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 409; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240" SPAC4A8.04; CHAIN 1..467; /note="Sexual differentiation process putative subtilase-type proteinase isp6"; /id="PRO_0000076410" MRIPYSNLFSAAAGLALFASTACAAPVMPATDSDIAHAGIRPELDNAFYDSHGEAATPKHKPHAGPNAAPLLSASNADTTGLDSHYIIVLQPDLSEQEFQAHTNWVSEMHQMDIASQEDEYYDTSDSNYMFGLKHVYDFGEDSFKGYSGQFSSNIVEQIRLHPHVIAVERDQVVSIKKLETQSGAPWGLARISHKSVKYDDIGKYVYDSSAGDNITAYVVDTGVSIHHVEFEGRASWGATIPSGDVDEDNNGHGTHVAGTIASRAYGVAKKAEIVAVKVLRSSGSGTMADVIAGVEWTVRHHKSSGKKTSVGNMSLGGGNSFVLDMAVDSAVTNGVIYAVAAGNEYDDACYSSPAASKKAITVGASTINDQMAYFSNYGSCVDIFAPGLNILSTWIGSNTSTNTISGTSMATPHVAGLSAYYLGLHPAASASEVKDAIIKMGIHDVLLSIPVGSSTINLLAFNGAQE P40923 YOX1_SCHPO PTM: Phosphorylated in response to hydroxyurea. Phosphorylation inhibits the repressor activity and is dependent on rad3. However, the regulation of yox1 by rad3 is probably indirect. {ECO:0000269|PubMed:21304269}. SPBC21B10.13c; CHAIN 1..201; /note="MBF complex negative regulatory component yox1"; /id="PRO_0000049411" MSLSDSPSKSGNTGKDLISNNEAKNHEDEETHQKKRRRRTTDAEATLLEQYFLKTPKPSLIERQELSKKLKSSMTPRELQIWFQNKRQSLRRSNCLSRNRLEGTGENSLLRRKSTLTLCETSTGQAELFFQSWPLHSQSVVGEMIHHEQDDYNKENKQQKVVDTTKDISRGSNGNEDSAAHQELEECARSLVELQQQCNDH P40976 LYS2_SCHPO CATALYTIC ACTIVITY: Reaction=(S)-2-amino-6-oxohexanoate + H2O + NADP(+) = 2 H(+) + L-2-aminoadipate + NADPH; Xref=Rhea:RHEA:12304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349, ChEBI:CHEBI:58672; EC=1.2.1.31; Evidence={ECO:0000250|UniProtKB:P07702}; CATALYTIC ACTIVITY: Reaction=(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-aminoadipate + NADH; Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31; Evidence={ECO:0000250|UniProtKB:P07702}; CATALYTIC ACTIVITY: Reaction=(S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP(+) = ATP + H(+) + L-2-aminoadipate + NADPH; Xref=Rhea:RHEA:46936, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349, ChEBI:CHEBI:58672, ChEBI:CHEBI:456215; EC=1.2.1.95; Evidence={ECO:0000250|UniProtKB:P07702}; COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000250|UniProtKB:P07702}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000250|UniProtKB:P07702}; MOD_RES 916; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" SPAP7G5.04c; CHAIN 1..1419; /note="L-2-aminoadipate reductase"; /id="PRO_0000193152" MSQTAPSDTEYNQRLERWSERLKSQTISHLPTDYSRPVPSRLVEAVFERTLPEDAKTALIKVYVAAQAKGILVTPFNILLTIFIILVSRMTGDEDISIGTSSENAIPFVLRTFIQPSDSFLDLLAKVCDLEKEGSSDAVDFSDLINFLNAKLSKKDDPRKTLVHLRFYNAPDAPSENFLSTTGLDVDLTVLVSVKKPSDQLTSLRSQFTFPDLQLKLIYNQLLFSESRVNIVADQLLKLVVSASKDVTGPIGALDLMTPTQMNVLPDPTVDLDWSGYRGAIQDIFASNAAKFPDRECIVVTPSVTIDAPVTSYTYRQIDESSNILAHHLVKNGIERGDVVMVYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQIIYLSVAKPRALVVLEDAGVLSPTVVEYVEKSLELKTYVPALKLAKDGSLTGGSVSKGADDILQHVLHLKSEQTGVVVGPDSTPTLSFTSGSEGIPKGVKGRHFSLAYYFDWMAQEFNLSESDRFTMLSGIAHDPIQRDIFTPLFLGASLIVPTAEDIGTPGQLAQWANKYKVTVTHLTPAMGQLLAAQADEPIPSLHHAFFVGDILTKRDCLRLQVLANNVNVVNMYGTTETQRSVSYFVVPARSQDQTFLESQKDVIPAGRGMKNVQLLVINRFDTNKICGIGEVGEIYLRAGGLAEGYLGNDELTSKKFLKSWFADPSKFVDRTPENAPWKPYWFGIRDRMYRSGDLGRYLPTGNVECSGRADDQIKIRGFRIELGEINTHLSRHPNVRENITLVRRDKDEEPTLVAYIVPQGLNKDDFDSATESEDIVVNGLKKYRKLIHDIREYLKTKLPSYAIPSVIVPLHKMPLNPNGKIDKPALPFPDTSQLAAASRSHSKHGVDETLTATERDIRDIWLRIIPHATDVNKKASFFDIGGHSILATRLIFELRKKFAVNVPLGLVFSEPTIEGLAKEIERMKSGEMISVMDIGKEETREPEIEYGKDALDLVDLIPKEFPTSKDLGIDEPKTVFLTGANGYLGVFILRDLMTRSSNLKVIALVRASSEEHGLKRLKDSCTAYGVWDESWAQKISVVNGDLALENWGIEERKWNKLTEVVDYVIHNGALVHWVYPYSKLRGPNVMGTITALKLCSLGKGKSLSFVSSTSTVDTEYYVNLSNEITSKGGNGIPESDPLQGSSKDLHTGYGQSKWVSEYLVRQAGLRGLRGVVVRPGYILGDSKSGAINTDDFLVRMVKGCIELGLYPNINNTVNMVPADHVARVVTASAFHPEQGVIVAHVTSHPRLRFNQFLGTLSTFGFNTKLSEYVNWRIALERFVINESHDSALYPLLHFVLDNLPANTKAPELDDTNTREILKRDASWTNVDVSNGAAILEHEMGLYLSYLVAIGFLPKPTLEGKKLPEVKINEATLEKLASAGGRGGAPTH P40977 PLC1_SCHPO ACT_SITE 456; /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"; ACT_SITE 500; /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" BINDING 343; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 345; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 347; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 349; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 354; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 582; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 584; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 666; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 693; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; MOD_RES 83; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22F8.11; CHAIN 1..899; /note="1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1"; /id="PRO_0000088513" MNCEMVTSPESVNLGDSNRAVSPFCLPDCSENAVAQTRSKTLDNAALDLPYVGNRKKSEQDFFKMLSSRDRDAHSTLRKRSNSLSSFLSTKSTSASENKFHGGLNWLSLKLNLLLRLQGRMNSARTNTSMNPYSCDSNENLSTLSSVNQNFNSRQLLATIVPESIQNGCSLLRITKKKVRQRKVSLDPISGYLMLDKNTGKAYKKLCVDDIKEIRQGRDARNYREQYKISSENEKRWFTIIYCADNKLKAMHMISPTLDAHNQWIMALEGLKTYRLNEFIIGLNLVCHQGEKMIDYSENLNPWEKLEKEQSAQLDLGDVHRMCQMLHLNASMEFLEETFQKADADHSGKLSFEEFQHFVSLLKTRSEIVDIFKEYTSGSDKMSLEQFRHFLSTSQKARLDSDSIRTLYVSFCSNDDSKMGLIEFTSFLLSPHNSPVVPVIQDMSRPLNEYLISSSHNTYLLGKQFGGESSIEGYIRSLQRGCKCIEIDCWDGPNGPVVCHGHTFTSMIKFNDVIDAIRKYAFVVSPYPLFISLEIHCCPDQQRQMVSYMKQAFGDTLVMKPVTANESVLPSPEDLLNKILLKVKCSATPLHQFSTDILKVGITDSSTDTTESSELENSELTGLRKGKRRMKNIIVQELQQLAPYARSLKFRNFSLPESKTYSHIFSFSERTIKKHGKAMVPRLSKHNLRYLCRVYPGPLRVGSTNFNPQVYWRLGVQMVALNWQTYDTGLQINDALFIADPPTGYLLKPPCQRIIGTTVGEEGLPRKIKLTIDVISGQQLRRARELSNSETLSPYVEIQVHSMEESPFRWCSKVVHENGFRPFWGETMVYESIISDDFYSMIRFLVHHRGSNGNDSIFANFTCPIDRLQQGYRHIRLLDMQGENLLFSSLFLKIKKEDI P40997 MCE1_SCHPO ACT_SITE 67; /note="N6-GMP-lysine intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000250|UniProtKB:Q01159}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013; Evidence={ECO:0000250|UniProtKB:Q01159}; SPBC2F12.08c; STRAND 14..17; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 38..40; /evidence="ECO:0007829|PDB:4PZ8"; STRAND 43..48; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 62..65; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 70..79; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 81..85; /evidence="ECO:0007829|PDB:4PZ8"; STRAND 86..92; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 98..101; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 112..114; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 120..131; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 137..149; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 189..194; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 197..199; /evidence="ECO:0007829|PDB:4PZ6"; STRAND 221..228; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 232..241; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 249..256; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 261..263; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 272..280; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 283..290; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 308..316; /evidence="ECO:0007829|PDB:4PZ7"; STRAND 322..327; /evidence="ECO:0007829|PDB:4PZ7" HELIX 5..7; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 20..34; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 53..59; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 133..135; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 154..156; /evidence="ECO:0007829|PDB:4PZ8"; HELIX 159..169; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 171..179; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 182..185; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 203..208; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 211..213; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 244..246; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 294..303; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 337..348; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 353..358; /evidence="ECO:0007829|PDB:4PZ7"; HELIX 360..370; /evidence="ECO:0007829|PDB:4PZ7" CHAIN 1..402; /note="mRNA-capping enzyme subunit alpha"; /id="PRO_0000210104" MAPSEKDIEEVSVPGVLAPRDDVRVLKTRIAKLLGTSPDTFPGSQPVSFSKKHLQALKEKNYFVCEKSDGIRCLLYMTEHPRYENRPSVYLFDRKMNFYHVEKIFYPVENDKSGKKYHVDTLLDGELVLDIYPGGKKQLRYLVFDCLACDGIVYMSRLLDKRLGIFAKSIQKPLDEYTKTHMRETAIFPFLTSLKKMELGHGILKLFNEVIPRLRHGNDGLIFTCTETPYVSGTDQSLLKWKPKEMNTIDFMLKLEFAQPEEGDIDYSAMPEFQLGVWEGRNMYSFFAFMYVDEKEWEKLKSFNVPLSERIVECYLDDENRWRFLRFRDDKRDANHISTVKSVLQSIEDGVSKEDLLKEMPIIREAYYNRKKPSVTKRKLDETSNDDAPAIKKVAKESEKEI P40998 THI4_SCHPO BINDING 87; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 108..109; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 116; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 181; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 217; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 232; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 284; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158"; BINDING 294..296; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158" CATALYTIC ACTIVITY: Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708, Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, ChEBI:CHEBI:139151; EC=2.4.2.60; Evidence={ECO:0000255|HAMAP-Rule:MF_03158}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|HAMAP-Rule:MF_03158}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03158}; PTM: During the catalytic reaction, a sulfide is transferred from Cys-215 to a reaction intermediate, generating a dehydroalanine residue. {ECO:0000255|HAMAP-Rule:MF_03158}. MOD_RES 215; /note="2,3-didehydroalanine (Cys)"; /evidence="ECO:0000255|HAMAP-Rule:MF_03158" SPBC26H8.01; CHAIN 1..328; /note="Thiamine thiazole synthase"; /id="PRO_0000034056" MAPATAVVTPQTAFKTDLPVEKTAHNTVVKSEMGALSKAYPTYSLDESFSFAPIRESTVSRAMTRRYFSDLDKYAESDIVIVGAGSAGLTAAYYIGTRRPDLKIAIIEASVAPGGGAWLGGQLFSAMVVRKPADLFLNEIGVPYEDEGDYVVVKHAALFTSTVMARTLALPNVKLFNATAVEDLIVKEGKDGKQRIAGVVTNWTLVSLNHGLQSCMDPNTINAHLVVSATGHDGPFGAFCVKRLASAQLVSNLHDMRPLDMNRAEDLIVKGTREVFPGMIVGGMELSEFDGANRMGPTFGGMMFSGIKAAQEALAIFDERKAVNEKYL P41005 MES1_SCHPO SPAC5D6.08c; CHAIN 1..101; /note="Protein mes1"; /id="PRO_0000096438" MVNTDNKENEPPNMEKAHMDSSNALYRVQRPLQRRPLQELSIELVKPSQTITVKKSKKSTNSSSYFAQLHAASGQNPPPSVHSSHKQPSKARSPNPLLSMR P41390 PUR1_SCHPO ACT_SITE 2; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" BINDING 383; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 384; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; MOD_RES 506; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4D7.08c; CHAIN 2..533; /note="Amidophosphoribosyltransferase"; /id="PRO_0000139646" MCGILALMLADPHQQACPEIYEGLYSLQHRGQDAAGIVTAGNKGRLYQCKGSGMVADVFSQHQLRQLVGSMGIGHLRYPTAGSCAHSEAQPFYVNSPYGLVLGHNGNLINGPELRRFLDTEAHRHVNTGSDSELLLNIFAYELQRLDKFRINENDIFEALRNVYDRVNGGYACVAMIAGLGVLGFRDPNGIRPLVIGERDTPEGKDYMLASESVVLTQFGYRTFRDIRPGECVFIRRSNREDILAGFRGPRLFSRQILPCLRFTPDIFEYVYFARPDSVIDGLSVYQSRLNMGEKLAHTIMKRFGPDYMEKIDAVIPVPDSARTSALALAQTAQLPYVEAFIKNRYIGRTFIMPGQQIRRKSVRRKLNVQPQEFFDKNVLIVDDSIVRGTTSREIVQMARESGAKNVYLASCAPMITHPHVYGIDLADCKDLIAYGKTEDEVAEAISADGVIYQTLEDLLDSCRTAELTEFEVGLFTGEYTTGASKEYLVHLEQMRIANNRARKHSFAEDEEREAPEDISLHNTHSDVTFDFV P41820 BFR1_SCHPO BINDING 918..925; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" MOD_RES 486; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 489; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 491; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1186; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC18B5.01c; CHAIN 1..1530; /note="Brefeldin A resistance protein"; /id="PRO_0000093451" CARBOHYD 28; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 67; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 273; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 334; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 450; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1159; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1175; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1449; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1460; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNQNSDTTHGQALGSTLNHTTEVTRISNSSDHFEDSSSNVDESLDSSNPSSNEKASHTNEEYRSKGNQSYVPSSSNEPSPESSSNSDSSSSDDSSVDRLAGDPFELGENFNLKHYLRAYKDSLQRDDIITRSSGVCMRDHSVYGVGSGYEFLKTFPDIFLQPYRAITEKQVVEKAILSHCHALANAGELVMVLGQPGSGCSTFLRSVTSDTVHYKRVEGTTHYDGIDKADMKKFFPGDLLYSGENDVHFPSLTTAETLDFAAKCRTPNNRPCNLTRQEYVSRERHLIATAFGLTHTFNTKVGNDFVRGVSGGERKRVTISEGFATRPTIACWDNSTRGLDSSTAFEFVNVLRTCANELKMTSFVTAYQASEKIYKLFDRICVLYAGRQIYYGPADKAKQYFLDMGFDCHPRETTPDFLTAISDPKARFPRKGFENRVPRTPDEFEQMWRNSSVYADLMAEMESYDKRWTETTPASSEAPEKDNFGSDISATTKHELYRQSAVAEKSKRVKDTSPYTVTFSQQLWYCLARSWERYINDPAYIGSMAFAFLFQSLIIGSIFYDMKLNTVDVFSRGGVLFFSILFCALQSLSEIANMFSQRPIIAKHRASALYHPAADVISSLIVDLPFRFINISVFSIVLYFLTNLKRTAGGFWTYFLFLFIGATCMSAFFRSLAGIMPNVESASALGGIGVLAIAIYTGYAIPNIDVGWWFRWIAYLDPLQFGFESLMINEFKARQFECSQLIPYGSGYDNYPVANKICPVTSAEPGTDYVDGSTYLYISFNYKTRQLWRNLAIIIGYYAFLVFVNIVASETLNFNDLKGEYLVFRRGHAPDAVKAAVNEGGKPLDLETGQDTQGGDVVKESPDNEEELNKEYEGIEKGHDIFSWRNLNYDIQIKGEHRRLLNGVQGFVVPGKLTALMGESGAGKTTLLNVLAQRVDTGVVTGDMLVNGRGLDSTFQRRTGYVQQQDVHIGESTVREALRFSAALRQPASVPLSEKYEYVESVIKLLEMESYAEAIIGTPGSGLNVEQRKRATIGVELAAKPALLLFLDEPTSGLDSQSAWSIVCFLRKLADAGQAILCTIHQPSAVLFDQFDRLLLLQKGGKTVYFGDIGEHSKTLLNYFESHGAVHCPDDGNPAEYILDVIGAGATATTNRDWHEVWNNSEERKAISAELDKINASFSNSEDKKTLSKEDRSTYAMPLWFQVKMVMTRNFQSYWREPSILMSKLALDIFAGLFIGFTFYNQGLGVQNIQNKLFAVFMATVLAVPLINGLQPKFIELRNVFEVREKPSNIYSWVAFVFSAIIVEIPFNLVFGTLFFLCWFYPIKFYKHIHHPGDKTGYAWLLYMFFQMYFSTFGQAVASACPNAQTASVVNSLLFTFVITFNGVLQPNSNLVGFWHWMHSLTPFTYLIEGLLSDLVHGLPVECKSHEMLTINPPSGQTCGEYMSAFLTNNTAAGNLLNPNATTSCSYCPYQTADQFLERFSMRYTHRWRNLGIFVGYVFFNIFAVLLLFYVFRVMKLRSTWLGKKITGTG P41831 KPR1_SCHPO BINDING 128; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255"; BINDING 130; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255"; BINDING 143; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0000250" SPAC4A8.14; CHAIN 1..409; /note="Ribose-phosphate pyrophosphokinase 1"; /id="PRO_0000141091" MKSATIIGGGSHPELLHLISNRLGITPCDVSLKRFANGETSVEIRESVRDKDVFILQSGSSTVNDSLMELLIIISACKGGSAKRITAVMPYFPYSKQSKMRKYRDAITARMVANLLTVAGVDHIITLDLHASQMQGFFTRPVDNLYAEPNIAEWIRRNVDDWEEAVVVSKNPGGAKRVTSLADTLNLDFALINTDRQRSSHFSQNFEDSIMDETEATETHVTNCSVYLDRPRIHTAKYLLGHIIDDEEIITTPASVCSEDYAQEVNLYSQGGCPSDDDEEENIMSASIYAERMITLVGDVNGKTALLIDDTIENPTAFIVASEHLVKRCGAKRVIVIGTHGIFQNKCLKDLQSCEYIEQIVVTNTYPIKPQAVLECDKLTVIDISGVLAEAIRRTHNGESISFLFKKAF P41838 RAE1_SCHPO SPBC16A3.05c; CHAIN 1..352; /note="Poly(A)+ RNA export protein"; /id="PRO_0000051182" MSLFGQATTSTVSNATGDLKKDVEVAQPPEDSISDLAFSPQAEYLAASSWDSKVRIYEVQATGQSIGKALYEHQGPVLSVNWSRDGTKVASGSVDKSAKVFDIQTGQNQQVAAHDDAVRCVRFVEAMGTSPILATGSWDKTLKYWDLRQSTPIATVSLPERVYAMDCVHPLLTVATAERNICVINLSEPTKIFKLAMSPLKFQTRSLACFIKGDGYAIGSVEGRCAIQNIDEKNASQNFSFRCHRNQAGNSADVYSVNSIAFHPQYGTFSTAGSDGTFSFWDKDSHQRLKSYPNVGGTISCSTFNRTGDIFAYAISYDWSKGYTFNNAQLPNKIMLHPVPQDEIKPRPKKGR P41888 TNR3_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + thiamine = AMP + H(+) + thiamine diphosphate; Xref=Rhea:RHEA:11576, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385, ChEBI:CHEBI:30616, ChEBI:CHEBI:58937, ChEBI:CHEBI:456215; EC=2.7.6.2; Evidence={ECO:0000269|PubMed:7499352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11577; Evidence={ECO:0000269|PubMed:7499352}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6 uM for thiamine {ECO:0000269|PubMed:7499352}; KM=1.9 mM for ATP {ECO:0000269|PubMed:7499352}; SPAC6F12.05c; CHAIN 1..569; /note="Thiamine pyrophosphokinase"; /id="PRO_0000072610" MAMSSITSAKQLNAEELLDECDSFNGEFVPGTIPFRANGAAIGYVTPLVLEILIKADNFKFNWVYVPGEYIEINASTFEKRTDILAKVLEHWRHNNTFGIADQWRNELYTVYGKSKKPVLAVERGGFWLFGFLSTGVHCTMYIPATKEHPLRIWVPRRSPTKQTWPNYLDNSVAGGIAHGDSVIGTMIKEFSEEANLDVSSMNLIPCGTVSYIKMEKRHWIQPELQYVFDLPVDDLVIPRINDGEVAGFSLLPLNQVLHELELKSFKPNCALVLLDFLIRHGIITPQHPQYLQTLERIHRPLPVPVGKYERGDSFEDTSKKAETCVPAKPQKATHQLAPCKAWLRDYDTDQKFAVLLLNQPIDIPDDRFRTLWKRASIRVCADGGANQLRNYDSSLKPDYVVGDFDSLTDETKAYYKEMGVNIVFDPCQNTTDFMKCHKIIKEHGIDTIFVLCGMGGRVDHAIGNLNHLFWAASISEKNEVFLLTELNVSTLLQPGINHVDCHDNIGLHCGLLPVGQSVYVKKTSGLEWNIEDRICQFGGLVSSCNVVTKATVTIEVNNFIVWTMETRL P41891 GAR2_SCHPO MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 144; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 146; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC140.02; CHAIN 1..500; /note="Protein gar2"; /id="PRO_0000081595" MAKKDKTSVKKSVKETASKKGAIEKPSKSKKITKEAAKEIAKQSSKTDVSPKKSKKEAKRASSPEPSKKSVKKQKKSKKKEESSSESESESSSSESESSSSESESSSSESESSSSESSSSESEEEVIVKTEEKKESSSESSSSSESEEEEEAVVKIEEKKESSSDSSSESSSSESESESSSSESEEEEEVVEKTEEKKEGSSESSSDSESSSDSSSESGDSDSSSDSESESSSEDEKKRKAEPASEERPAKITKPSQDSNETCTVFVGRLSWNVDDQWLGQEFEEYGTIVGARVIMDGQSGRSKGYGYVDFETPEAAKAAVAANGTKEIDGRMVNLDLSNPRPANPQPYAQQRAGNFGDQLSEPSDTVFVGNLSFNATEDDLSTAFGGCGDIQSIRLPTDPQSGRLKGFGYVTFSDIDSAKKCVEMNGHFIAGRPCRLDFSTPRTGGGSRGGRGGFGGRGGFGGRGGFGGGRGRGRGGARSGNPNRGSVAPFSGNKVTFD P41893 PPAL_SCHPO ACT_SITE 11; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P11064"; ACT_SITE 17; /evidence="ECO:0000250|UniProtKB:P11064"; ACT_SITE 128; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P11064" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; SPAC1071.12c; CHAIN 1..156; /note="Low molecular weight phosphotyrosine protein phosphatase"; /id="PRO_0000046564" MTKNIQVLFVCLGNICRSPMAEAVFRNEVEKAGLEARFDTIDSCGTGAWHVGNRPDPRTLEVLKKNGIHTKHLARKLSTSDFKNFDYIFAMDSSNLRNINRVKPQGSRAKVMLFGEYASPGVSKIVDDPYYGGSDGFGDCYIQLVDFSQNFLKSIA P42657 RAD25_SCHPO MOD_RES 234; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A2.13c; CHAIN 1..270; /note="Checkpoint signal transducer rad25"; /id="PRO_0000058718" MSNSRENSVYLAKLAEQAERYEEMVENMKKVACSNDKLSVEERNLLSVAYKNIIGARRASWRIISSIEQKEESRGNTRQAALIKEYRKKIEDELSDICHDVLSVLEKHLIPAATTGESKVFYYKMKGDYYRYLAEFTVGEVCKEAADSSLEAYKAASDIAVAELPPTDPMRLGLALNFSVFYYEILDSPESACHLAKQVFDEAISELDSLSEESYKDSTLIMQLLRDNLTLWTSDAEYNQSAKEEAPAAAAASENEHPEPKESTTDTVKA P46960 PGTB2_SCHPO BINDING 176..178; /ligand="geranylgeranyl diphosphate"; /ligand_id="ChEBI:CHEBI:57533"; /evidence="ECO:0000250"; BINDING 218..230; /ligand="geranylgeranyl diphosphate"; /ligand_id="ChEBI:CHEBI:57533"; /evidence="ECO:0000250"; BINDING 224; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 226; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 276; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.60; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPAC167.02; CHAIN 1..311; /note="Geranylgeranyl transferase type-2 subunit beta"; /id="PRO_0000119779" MAVLLRDKHISYLHDIGNRTDELDFWLKEHLHVSAIYWSCMSFWLLKKKDQIDKERIVSFLLSCLTESGGFACYPGHDDHITNTVYAVQVLAMLDSLHVVDKDKVASYIIGLQNEDGSMKGDRWGEIDARFLYSGINCLAILGKLDYLNKNTAVDWLMKCYNFDGGFGLCPGAESHGAMVFTCVAALKILNKLDLIDEELLGWWISERQVKGGGLNGRPEKLPDSCYGWWDLSPLAIIGKLDWIDRNQLIDFLLGTQDADSGGFADRKEDATDVYHTCFSLAGLSLLQFPNIEPVDPRFCLPLEVTQKMKL P47943 IF4A_SCHPO BINDING 63..70; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1006.07; CHAIN 1..392; /note="ATP-dependent RNA helicase eIF4A"; /id="PRO_0000054966" MVDQLEDSVIETNYDEVIDTFDDMNLKPELLRGIYAYGFERPSAIQQRAIMPILGERDVLAQAQSGTGKTATFSISVLQKIDTSLKQCQALILAPTRELAQQIQKVVVALGDLMNVECHACIGGTLVRDDMAALQAGVHVVVGTPGRVHDMIQRRALPTDAVQMFVLDEADEMLSRGFKDQIYDIFQLLPPTAQVVLLSATMPQDVLEVTTKFMRDPIRILVKKDELTLEGIKQFYVAVEKEEWKLDTLCDLYETVTVTQAVIFCNTRRKVDWLTEQLTERDFTVSSMHGDMDQAQRDTLMHEFRTGSSRILITTDLLARGIDVQQVSLVINYDLPANRENYIHRIGRGGRFGRKGVSINFVTNDDVRMMREIEQFYNTHIEEMPMNIADLI P47946 TRK1_SCHPO SPAC3F10.02c; CHAIN 1..841; /note="Potassium transport protein 1"; /id="PRO_0000070461" CARBOHYD 116; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 164; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 215; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 401; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 771; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVLNYIQRWFKWVIPTFGFLAIHYIYIISLTIIASILLFTGGTTTKIKYIDALFLASSATTQTGLNSVDLNSLSIWQQFILYGFTAITVPIWMHGSISFIRLYWFRRKFKDVVRQNRTRKFQRKLRKSLMKKSEDDEEQGVRGRKIRVMLPYLHSLRSPTSLKNFSRFDTHDSTNNPYFPDNPPSPKADISKDEYFGKYLPKKSDTLDMDLESHNMTFHDYEPSIENKNYDFGSSHSASMQMYEMDDLHPRLRRQSSFISSVNPLEADDTRETLSEGALVQESLPMAYSYSDTNLVVSRDSFTLTGDDNLFPEGGLRPANTIDGIVRSSLSSSSLSKDTEPSTVDMHIAFTGLNKPTIERERNLKLRKKSRFYKKSLRSRFSRGLHRPIRWTKSFTSNRRNLTLERVLSSAFAKKREPSISSRHTTMSLPYLSYNPTVDRNSAFVALSKEQRDELGGIEYRALKCVCSMVTLYFIIFNIAAFVTFIVFAYTAVGSREVIDSYDLRRGWWALFSSASSFNDLGFSLIPSSFVPMNRNIFLLLISSLFIIAGNTGFPCFFRTFIWTTYKLYPFSFEKKEAMAFLLDHPRRCFTLLFPSGATWVLFFVLLLLNVIDLVLFMVLDTGSKAVASLPKGIRVVNAIFQSVCTRTAGFTSVSISELHPAVLVSYMVMMYISVYPVAINMRNTNVYEERSLGVYRTEDDEGKSFLKDHLTEQLSYDLWYIFLGLFIICICEGGKISNPLDTDFSIFTVLFEVVSAYGTVGLSTGLSSSNCSLSARFTTISKLVIIALELRGRHRGLPRAVDRAILLPSEKNNLKEEEDYQRRHGFSIDNARGSIAVSRD P48383 SAK1_SCHPO MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 224; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 227; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G9.14; CHAIN 1..766; /note="Protein sak1"; /id="PRO_0000215293" MNPSDLPGQIPLSRSDMNVQDQLDPVQRFDTHFMLPQEENFLNRPSITSESAHPRGSDLEQETELKRLALEHEHYSLESLAEKLRMDHVSANSEKFRQVFGICWLKRACEEQQDAAVQRNQIYAHYVEICNSLHIKPLNSASFGKLVRLLFPSIKTRRLGMRGHSKYHYCGIKLRGQDSFRRLRTFSDSSLSPVSCSSFPKPIPNHFENDVSSIQNTNQRVESSPASVNAAAIVRKSAVTPSSDPYNSPPPSIPLLGSQTNLQLAPSFAAPQAHPLPSHLSQSNVPPQLSHSSVPSPAPPRSVSQPTYFSQPMPQFSSSFVPGTSSIVPTLHPASAQEDFNLQHSLFFKLKLKFLPPHKLPWIPSLDVSSFSLPPIDYYLNGPYDNVEAKSALMNIYSSHCITLIESVRYMHLKQFLSEISNFPNSLSPSLLALLSSPYFTKWIERSDTVMYREILKLLFPMTLQVVPPPVLVLLRHLAENLVNHISSIYASHSSCLLQVKSETAAIFSNLLSRLLRVNDTAHAAARFLANPADRHLICNDWERFVSTRFIVHRELMCNDKEAVAALDEWYSILSTCSNPSELLDPLKDKHEASDTSMNRVELRQIDGVLDRMADFFLELPSRFPSCSPRMFLLCLGALQTSVLREITVSGGEAFGALWVIRCWVDEYMTWVAEIGGYLDDSYDELEQHHANFHNKAGISQSNIPPHLQEHRQSQQHFQQDIEALQSQQQQQATKNSLMEAAYQNAQKQKEDDYISIVFDTNGACS P49373 TFS2_SCHPO BINDING 255; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 258; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 283; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"; BINDING 286; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00472" SPAC20H4.03c; CHAIN 1..293; /note="Transcription elongation factor S-II"; /id="PRO_0000121442" MDSADIRSAKAALEKAIQGKNIETIINIMTRLKNEVVATEELLKETRLGLVVGKLRSHPNEKVGEQAREIVKKWKADVSKGRPLKTTTTTSSTPSKHADVGSQAQKQVQKQSSSGQRTFKSDNVNVNVTDDKIRNNCIGLMYNALVIDSDESSSLIIAKAKEIDAQVLARAAGKTGSEYRNRMRSLYMNLKDKNNPKLRASVLRNEITPQRLSTMTSAELASEDRRKEDAKLEQENLFHAQGAKPQKAVTDLFTCGKCKQKKVSYYQMQTRSADEPMTTFCECTVCGNRWKFS P49740 NDK_SCHPO ACT_SITE 117; /note="Pros-phosphohistidine intermediate"; /evidence="ECO:0000250" BINDING 11; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 59; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 87; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 104; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 114; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC806.07; CHAIN 1..151; /note="Nucleoside diphosphate kinase"; /id="PRO_0000137152" MSTEQTFIAVKPDAVQRGLIGYIISKFELKGYKLRALKFLVPSRDLVEEHYAEHKGKPFYEKLVGFMASGPVCAMIWEGKQAVKTGRLMLGASNPLDSAPGTIRGDYGIDLGRNVCHGSDSIESANREIKLWFQPSEIQVYDRTIEPWIYE P49776 APH1_SCHPO ACT_SITE 97; /note="Tele-AMP-histidine intermediate"; /evidence="ECO:0000250" BINDING 28; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 84; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 90..93; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 99; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP + 2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; EC=3.6.1.17; SPCC4G3.02; CHAIN 2..182; /note="Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]"; /id="PRO_0000109788" MPKQLYFSKFPVGSQVFYRTKLSAAFVNLKPILPGHVLVIPQRAVPRLKDLTPSELTDLFTSVRKVQQVIEKVFSASASNIGIQDGVDAGQTVPHVHVHIIPRKKADFSENDLVYSELEKNEGNLASLYLTGNERYAGDERPPTSMRQAIPKDEDRKPRTLEEMEKEAQWLKGYFSEEQEKE P50525 APN1_SCHPO BINDING 61; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 136; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 136; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 170; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 207; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 220; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 222; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 252; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 3 Zn(2+) ions. {ECO:0000250}; SPCC622.17; CHAIN 1..342; /note="Apurinic-apyrimidinic endonuclease 1"; /id="PRO_0000190897" MCAINKAYLLTKFYISANSCAFFVKSQRKWTSPDLSEDVAQKFLETASEMKFDASKQVLVHGSYLINMANADEQKREQAFNCFVDDLKRCERLGVGLYNFHPGSTASCTKEEGINNLAECINRAHEETKSVIIVTENMAGQGNCLGGTFDDFAALKSKIKNLDRWRVCLDTCHTFAAGYDIRTEESYKKVIDEFDEKVGAKYVSGWHLNDSKAPLGSNRDLHENIGLGFLGLEPFRLIMNDSRWDGIPLVLETPAKSPEQWKKEVELLRFMVGKSSDDVELMKESARLSNLGAASRKEHLNKFEKKEAKKDRKKKSKDGDQTTLLLRKKQKLGNAEVKSLDE P53694 RTN1_SCHPO SPBC31A8.01c; CHAIN 1..308; /note="Reticulon-like protein 1"; /id="PRO_0000079619" CARBOHYD 65; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 113; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 135; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 303; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSEQHSLNPFESGSVTASDVAAAKSGAEDLVNTLTAHTVHPSTELPSATSFPSALPNSENPVIQNISSSSSEPHHTSQSTPGETSSPVCPVSGAHGGADKKCPALEAGCPFTNTTKQNVDPEISNALWSVLTWKNTSCSFSTLMSILALVYVPSWINLPRLFFRTFRYVFLITSIIEFGGLFASNGKRGVLSHFRSSYITCDSKALDRIVNSIVDIFNVMLIQFQRILFAESPILTFTASVAAFIEFFLSGFLSYKSLFVWNVLFAFILPRLYVCNERSIKHLVASLERSGDKLKKQATETINTTVNK P55306 CATA_SCHPO ACT_SITE 60; /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"; ACT_SITE 133; /evidence="ECO:0000255|PROSITE-ProRule:PRU10013" BINDING 344; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P04040" CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P15202}; MOD_RES 363; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC757.07c; CHAIN 1..512; /note="Catalase"; /id="PRO_0000084927" MNSKDSNTVPVYTTNTGCPIFNPMAAARVGKGGPVLLQDSHLIDVFQHFDRERIPERVVHAKGSGAFGEFECTDDITKYTKHTMFSKVGKKTPMVARFSTVGGERGTPDTARDPRGFALKFYTDEGIFDMVGNNTPVFFLRDPAKFPLFIHTQKRNPQNDMKDATMFWDYLSQNAESIHQVMILFSDLGGTPYSYRFMDGFSSHTYKFVNDKGEFYYCKWHFITNQGTKGLTNEEAAALDGSNPDHARQDLFEAIERGDYPSWTLYVQVMTPQEAEKYRYNIFDLTKVWPHKDVPMQRVGRFTLNQNPTNFFADIEQAGFSPSHMVPGIEVSADPVLQVRTFSYPDTHRHRLGANFEQIPVNSPKCPVFNYSRDGPMNVNGNQGNWPNYPSSIRPLAKVQYEPDEGHEKWVGQVTYHMDEITDVDFEQPRAFWQNVLGKKPGQQDNFVKNVAGHLSGAISPVRERQYGVFTRVDSELGRRIREATEAEVKKMEEKAPKPINKGEPHMFQGSS P56286 IF2A_SCHPO MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 179; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 273; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 305; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3G9.09c; CHAIN 1..306; /note="Eukaryotic translation initiation factor 2 subunit alpha"; /id="PRO_0000137388" MSTTSCRMYENRFPEVDELVVVNVRQIQEMGAYVKLLEYDNIEGMVLLSELSRRRIRSVQKHIRVGRNEVVVVLRVDKEKGYIDLSKRRVSPEDVVKCEERFNKSKAVHSIMRHIAEKHNVPLETMYTTIGWPLYRKYGHAYDAFKLAISNPDHVFEGLEPPKSGVINDLLAQISRRLTPQPIKIRADVEVTCFGYEGINAIKAALKAAEDVHTEEVPIKVKLVAPPLYVLLTNALDKSLGLKKLEEAIGAIEKSITASNGTCTVKMKPKAVSETDELELADLMKKFEKENAEISGDEEDDQSGSE P56287 EI2BE_SCHPO MOD_RES 172; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 500; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 506; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC8C9.15c; STRAND 19..23; /evidence="ECO:0007829|PDB:5B04"; STRAND 29..31; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 36..38; /evidence="ECO:0007829|PDB:5B04"; STRAND 43..49; /evidence="ECO:0007829|PDB:5B04"; STRAND 65..70; /evidence="ECO:0007829|PDB:5B04"; STRAND 92..99; /evidence="ECO:0007829|PDB:5B04"; STRAND 123..128; /evidence="ECO:0007829|PDB:5B04"; STRAND 130..132; /evidence="ECO:0007829|PDB:5B04"; STRAND 153..161; /evidence="ECO:0007829|PDB:5B04"; STRAND 174..179; /evidence="ECO:0007829|PDB:5B04"; STRAND 185..191; /evidence="ECO:0007829|PDB:5B04"; STRAND 198..200; /evidence="ECO:0007829|PDB:5B04"; STRAND 212..226; /evidence="ECO:0007829|PDB:5B04"; STRAND 260..266; /evidence="ECO:0007829|PDB:5B04"; STRAND 271..273; /evidence="ECO:0007829|PDB:5B04"; STRAND 307..309; /evidence="ECO:0007829|PDB:5B04"; STRAND 313..315; /evidence="ECO:0007829|PDB:5B04"; STRAND 329..333; /evidence="ECO:0007829|PDB:6JLY"; STRAND 344..347; /evidence="ECO:0007829|PDB:5B04"; STRAND 361..364; /evidence="ECO:0007829|PDB:5B04"; STRAND 378..381; /evidence="ECO:0007829|PDB:5B04"; STRAND 422..428; /evidence="ECO:0007829|PDB:5B04"; STRAND 432..434; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 436..438; /evidence="ECO:0007829|PDB:5B04" HELIX 15..17; /evidence="ECO:0007829|PDB:6JLZ"; HELIX 40..42; /evidence="ECO:0007829|PDB:5B04"; HELIX 50..61; /evidence="ECO:0007829|PDB:5B04"; HELIX 74..83; /evidence="ECO:0007829|PDB:5B04"; HELIX 85..87; /evidence="ECO:0007829|PDB:5B04"; HELIX 108..115; /evidence="ECO:0007829|PDB:5B04"; HELIX 137..147; /evidence="ECO:0007829|PDB:5B04"; HELIX 204..209; /evidence="ECO:0007829|PDB:5B04"; HELIX 229..236; /evidence="ECO:0007829|PDB:5B04"; HELIX 247..252; /evidence="ECO:0007829|PDB:5B04"; HELIX 277..288; /evidence="ECO:0007829|PDB:5B04"; HELIX 290..292; /evidence="ECO:0007829|PDB:5B04"; HELIX 297..299; /evidence="ECO:0007829|PDB:5B04" TURN 32..35; /evidence="ECO:0007829|PDB:5B04"; TURN 171..173; /evidence="ECO:0007829|PDB:5B04"; TURN 181..183; /evidence="ECO:0007829|PDB:5B04"; TURN 237..239; /evidence="ECO:0007829|PDB:6JLZ"; TURN 243..246; /evidence="ECO:0007829|PDB:5B04"; TURN 310..312; /evidence="ECO:0007829|PDB:5B04" CHAIN 1..678; /note="Translation initiation factor eIF2B subunit epsilon"; /id="PRO_0000156077" MPPSKGLNGKLEKPKHALQAIVLSDSYNYRFRPLTLDKPRCLLPLANTPLIEYTFEFLALAGVQEVYVFCCAHAGQIREYIEKSKWNLPSSPFSVNTIVSRESLSVGDALRELDSKQLITSDFILVSGDVVSNVPLNEVLKEHRKRREDDKNAIMTMVVREASPFHRTRARTESSVFVIDKKTSQCVHYQANERGKHYVSMDPEIFNEHEELEVRNDLIDCQIDICSNDVPALFTENFDYQDIRKDFVYGVLTSDLLGKKIHCHVAKENYAARVRSLQTYDAISKDVLSRWVYPFVPDSNLLNQTFSYQRHQIYKEEDVVLARSCIIKARTLIGAYTKVGDASVVANTIIGRNCTIGSNCSIDSAFLWEDVVIGDNCRIGKAILANSVKIGNNCSIEDGAIVAAGVVIGDNTIIEKNKRLTTFESHSQGTLNDPSLVGIGGRGQEYHAEEDSDDEGEFMEASGLIESTNELHLSDSESSETSSSSEEDMEFIPFSARRDSANTINSEDFDEGDFNKEAQQSLERAFEENHQIDIAALELNTLRMAMNANYHEVRSAIVLALLRRIMHLDVSPKEALAKVMTRWGPLLAKLTFSHEEQVDNVLTLQKYCVRLSMTRHFLQLLGYFYQLEIAEENAIQEWYSDPRSSEGELAALRDAGGKQFVDWLNTAESESESEEGSE P56288 EI2BG_SCHPO MOD_RES 291; /note="Phosphoserine"; /evidence="ECO:0000250" SPAC4D7.09; STRAND 33..35; /evidence="ECO:0007829|PDB:5B04"; STRAND 39..45; /evidence="ECO:0007829|PDB:5B04"; STRAND 58..60; /evidence="ECO:0007829|PDB:5B04"; STRAND 66..71; /evidence="ECO:0007829|PDB:5B04"; STRAND 87..92; /evidence="ECO:0007829|PDB:5B04"; STRAND 112..117; /evidence="ECO:0007829|PDB:5B04"; STRAND 141..147; /evidence="ECO:0007829|PDB:5B04"; STRAND 169..176; /evidence="ECO:0007829|PDB:5B04"; STRAND 196..199; /evidence="ECO:0007829|PDB:5B04"; STRAND 204..207; /evidence="ECO:0007829|PDB:5B04"; STRAND 210..213; /evidence="ECO:0007829|PDB:5B04"; STRAND 216..221; /evidence="ECO:0007829|PDB:5B04"; STRAND 230..245; /evidence="ECO:0007829|PDB:5B04"; STRAND 253..256; /evidence="ECO:0007829|PDB:5B04"; STRAND 315..319; /evidence="ECO:0007829|PDB:5B04"; STRAND 321..323; /evidence="ECO:0007829|PDB:5B04"; STRAND 353..360; /evidence="ECO:0007829|PDB:5B04"; STRAND 373..376; /evidence="ECO:0007829|PDB:5B04"; STRAND 390..393; /evidence="ECO:0007829|PDB:5B04"; STRAND 407..410; /evidence="ECO:0007829|PDB:5B04"; STRAND 424..427; /evidence="ECO:0007829|PDB:5B04"; STRAND 435..438; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 441..443; /evidence="ECO:0007829|PDB:5B04" HELIX 62..64; /evidence="ECO:0007829|PDB:5B04"; HELIX 74..82; /evidence="ECO:0007829|PDB:5B04"; HELIX 94..96; /evidence="ECO:0007829|PDB:6JLZ"; HELIX 97..105; /evidence="ECO:0007829|PDB:5B04"; HELIX 128..134; /evidence="ECO:0007829|PDB:5B04"; HELIX 136..138; /evidence="ECO:0007829|PDB:5B04"; HELIX 156..166; /evidence="ECO:0007829|PDB:5B04"; HELIX 247..249; /evidence="ECO:0007829|PDB:5B04"; HELIX 332..338; /evidence="ECO:0007829|PDB:5B04" TURN 52..54; /evidence="ECO:0007829|PDB:5B04"; TURN 200..203; /evidence="ECO:0007829|PDB:5B04"; TURN 222..226; /evidence="ECO:0007829|PDB:5B04"; TURN 250..252; /evidence="ECO:0007829|PDB:5B04"; TURN 261..266; /evidence="ECO:0007829|PDB:5B04"; TURN 277..279; /evidence="ECO:0007829|PDB:6JLY"; TURN 284..289; /evidence="ECO:0007829|PDB:6JLZ" CHAIN 1..458; /note="Translation initiation factor eIF2B subunit gamma"; /id="PRO_0000156082" MSLYEHAALPLASSPSILGPISGGRNRGNIQLQSIPIEFQAVVFAGFGNSLYPLTGSDALPKALLPIGNKPMLHYPLYWLEAAGFTSAILICMEEAEAHINAWLRSGYEGHMRIHVEAPTILDDSKSSADALRAVSHLIKNDFVCLSCDSIVGLPPIYGLDKFRLDNPSALAVYSPVLKYEHITSQSKEIDAKQLIGIEEKTSRLLYAKSSADVGSDFTFRMSLLWKHPRVTLNTNLSDAHIFVFKHWVIDLIREKESISSIRGDLIPYLVKCQYQKSFTVRENIQRFLSSPNNIDNYDGGLSSQEIKINALIAKDGIICSRANNLPNYFELNKCIAKLTPEQRLVDVTVSERALVGADCMVNEGTTIKDNSNIKKSIIGKNCVIGKGVVVSNSILMDNIVVEDGVRLESCIVASGAQIGAKSKLRECEIGVDHRVEAGRIARGERLVDMEKIETDMD P57728 RL28B_SCHPO MOD_RES 108; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC776.11; CHAIN 1..148; /note="Large ribosomal subunit protein uL15B"; /id="PRO_0000104903" MPTHTSKTRKLRGHVSAGHGRIGKHRKHPGGRGKAGGLQHLRSHFDKYHPGYFGKVGMRRFHLMKNPLWRPTVNLDRLWTLVPNETREKYLGKNTEVAPVINVLQSGYGKVLGKGRLPDTPVIIQTRYVSRRAEEKIKQAGGVVELIA P59289 RL37A_SCHPO BINDING 19; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 22; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 34; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 37; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P49166}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49166}; SPAPB17E12.05; CHAIN 2..89; /note="Large ribosomal subunit protein eL37A"; /id="PRO_0000139720" MTKGTQSFGMRHNKSHTICRRCGKRSFHIQKSTCACCGYPAAKTRSYNWGAKAKRRRTTGTGRMSYLKKVHRSFKNGFRAGKPTSAATA P62505 DAD3_SCHPO SPAC14C4.16; CHAIN 1..86; /note="DASH complex subunit dad3"; /id="PRO_0000175950" MSLEEKRALQNQILAEYANLASNLETLVKVLQDMVYNPSNNILDSLRDLEKEVGLVYTLYKASVWAILADLENNQEGKSGMFQDES P78759 2AD2_SCHPO SPAC6F12.12; CHAIN 1..627; /note="Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 2 isoform"; /id="PRO_0000071470" MKGLRSKFVKALSLKDEQGSHKNGHSKSHYISKNGSYVETDDVKHTDTHHSSKHELKKLKSHFLKDTLKHKRNHHANSNNEKHENSDKKIHTTVLASGHEDSDYSTFLPVIETSKVKDANHFPPNYPEPKNDSVSSNIDEFPNDSISSASFLSVPQSTPPYLVSQPTPLNKFLAGAENVDIPHSLRPVPRREHSSQFQVSEKRTLVRLPSFDDVHTSEREELFIKKLEQCNIIFDFNDPSSDLASKEIKREALLQMIDYVSENRGISSASLFPYVVNTFSLNVFRPISPALNDYSSDMFALDDEPFLEPAWPHLEEVYLLFIKFLESPDFRASKAKSLVDRRFFNRLLALFDTEDPRERELLKTTLHRIYGKFLNLRSYIRKSMNNVFLQFIYEREKFHGIAELLEILGSIINGFAVPLKEEHKIFLSKVLIPLHQTKSVFLYHPQLTYCIVQFIDKDPSLTKAVLTGILKYWPRINSFKELLFLNEIEDIFEVLEPSEFVNIMSPLFQQLARSISSMHFQVAERALCLWSNEYFTSLVSQNVVTLLPIIYPSLYKTANEHWNSTIQAIACNVLQIFVDMDADFFNGLVEDYKQAIIKQEEVMIIRKQQWCQIEALAAENKPTDYLR P78768 VTI1_SCHPO SPBC3B9.10; CHAIN 1..214; /note="Vesicle transport v-SNARE protein vti1"; /id="PRO_0000218231" METYEQEYRLLRADIEEKLNDLSKSGENSVIQSCQRLLNEIDEVIGQMEIEITGIPTSERGLVNGRIRSYRSTLEEWRRHLKEEIGKSDRKALFGNRDETSGDYIASDQDYDQRTRLLQGTNRLEQSSQRLLESQRIANETEGIGASILRDLHGQRNQLEHSLEMLGDTSGHLDRSLRTLKTMARRLAMNRFFTTAIIAILVILILLVLYSKFR P78780 DHAS_SCHPO ACT_SITE 151; /note="Acyl-thioester intermediate"; /evidence="ECO:0000250"; ACT_SITE 247; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 12..15; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 39..40; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 111; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250"; BINDING 179; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 182..183; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 205; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 208; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250"; BINDING 240; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 335..336; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; MOD_RES 323; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1827.06c; CHAIN 1..357; /note="Probable aspartate-semialdehyde dehydrogenase"; /id="PRO_0000141399" MAIKKVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQENKLDRGCIITNSNCSTAAVVVPLKALQDAFGPIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTISGYELTDNVVSAQCNRVPVIDGHLMCISVKFAKTSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDSTPDRPQPRLDRNNENGYAVSVGRIRSDSIFDIKFVSLVHNTVLGAAGAGILNAEVAVKKGLM P78789 AAKB_SCHPO BINDING 250..252; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /ligand_note="ligand shared with subunit gamma"; /evidence="ECO:0007744|PDB:2QR1, ECO:0007744|PDB:2QRC, ECO:0007744|PDB:2QRD" SPCC1919.03c; STRAND 209..211; /evidence="ECO:0007829|PDB:2QRD"; STRAND 217..219; /evidence="ECO:0007829|PDB:2OOX"; STRAND 220..223; /evidence="ECO:0007829|PDB:2QR1"; STRAND 251..253; /evidence="ECO:0007829|PDB:2OOX"; STRAND 266..268; /evidence="ECO:0007829|PDB:2QRD"; STRAND 271..283; /evidence="ECO:0007829|PDB:2QRD"; STRAND 286..294; /evidence="ECO:0007829|PDB:2QRD" HELIX 214..216; /evidence="ECO:0007829|PDB:2QRD"; HELIX 234..236; /evidence="ECO:0007829|PDB:2QRD"; HELIX 240..242; /evidence="ECO:0007829|PDB:2QRD"; HELIX 247..250; /evidence="ECO:0007829|PDB:2QRD"; HELIX 259..261; /evidence="ECO:0007829|PDB:2QRD" CHAIN 1..298; /note="5'-AMP-activated protein kinase subunit beta"; /id="PRO_0000339125" MGNVQSQEGETRAHAVPSQDATTTPDNANNVPKEPRAQSMISIAADDLNQEGEMSDDNQQEGGNNRTSQNGTSGSSGHTKRRSQTSGKKTHQPYSGPCVPTIIRWRGGGEVVYVTGSFSRWKKKIQLLKSEDYTVLLQLRPGTQRFKFLVDGIWCCSSDFPTATDAEGNLYNYLEVEANEKLGASIDERLSQVHTDLPMEEKSESEQYSTEIPAFLTSNTLQELKLPKPPSLPPHLEKCILNSNTAYKEDQSVLPNPNHVLLNHLAAANTQLGVLALSATTRYHRKYVTTAMFKNFDV P78794 CWC15_SCHPO SPBC337.06c; CHAIN 1..265; /note="Pre-mRNA-splicing factor cwf15"; /id="PRO_0000218242" MTTAHRPQFDPARGHSEMAPTRITSSRALPAHLKLKYRQESQGTEEEVRKQDLREALLRAEAAHFATQEHGASSEEVSQNSKLIEGFTSPSTDDKPNNDVEVDYQELLRQTLEADEDASDSDDSVDSSNKNSEVSIKRRKTESNSQESVDSSNSESSDEESDSEDETQQLLRELENIKQERKREQMLQEEKNRALEQEKREREIAFGNELLNKASSGSFQVKRRWDEDVVFRNTHKGVDDTPRPGFVNDMLRSEFHKKFLARFVD P78811 UGPA1_SCHPO ACT_SITE 394; /evidence="ECO:0000250" BINDING 115..118; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 117..118; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16851"; BINDING 129; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 129; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 192; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 221; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 222; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16851"; BINDING 250..252; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16851"; BINDING 252; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 252; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 394; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3" CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885; EC=2.7.7.9; Evidence={ECO:0000269|PubMed:21862693}; MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1322.04; CHAIN 1..506; /note="Probable UTP--glucose-1-phosphate uridylyltransferase"; /id="PRO_0000185763" MDLAPRPLGRQHSKSQSAFAFDNTATSIAASTMKNELNHLASTVKDPLAKKAFQKEMDNFFSLFSRYLQEDARGSEINWDLVESPKPEQVVEYDTITEAGGLSRDYLNKLAVLKLNGGLGTTMGCVGPKSIIEVRDGNSFLDLSVRQIEHLNRKYNVNVPFVLMNSFNTDEATAKVIKKYEAHKIDILTFNQSRYPRVHKETLLPVPHTADSAIDEWYPPGHGDVFEALTNSGIIDTLIAQGKEYLFVSNIDNLGAVVDLNILNHMVETNAEYLMELTNKTKADVKGGTLIDYDGNVRLLEIAQVPPQHVEEFKSIKKFKYFNTNNLWFHLPSVKRVVNNHELSMEIIPNKKTIKHKGENINIIQLETAAGAAIRHFKNAHGVNVPRRRFLPVKTCSDLLLVKSDLYSINHGQVEMNPRRFGGTAPLVKLGAHFKKVADFSAHIPSIPKILELDHLTITGDVNIGRNVTLKGTVIIVASDANRIDIPNGSVLENCVITGNLNILEH P78812 6PGD_SCHPO ACT_SITE 187; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 194; /note="Proton donor"; /evidence="ECO:0000250" BINDING 13..18; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 36..38; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 78..80; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 106; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 106; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 132..134; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 190..191; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 195; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 264; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 291; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 449; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 455; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44; MOD_RES 107; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 215; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC660.16; CHAIN 1..492; /note="6-phosphogluconate dehydrogenase, decarboxylating"; /id="PRO_0000090074" MSQKEVADFGLIGLAVMGQNLILNGADKGFTVCCYNRTTSRVDEFLANEAKGKSIVGAHSLEEFVSKLKKPRVCILLVKAGKPVDYLIEGLAPLLEKGDIIVDGGNSHYPDTTRRCEELAKKGILFVGSGVSGGEEGARYGPSLMPGGNPAAWPRIKPIFQTLAAKAGNNEPCCDWVGEQGAGHYVKMVHNGIEYGDMQLICETYDIMKRGLGMSCDEIADVFEKWNTGKLDSFLIEITRDVLRYKADDGKPLVEKILDAAGQKGTGKWTAQNALEMGTPVSLITEAVFARCLSSLKSERVRASKKLTGPNTKFTGDKKQLIDDLEDALYASKIISYAQGFMLMREAAKEYGWKLNNAGIALMWRGGCIIRSVFLKDITEAFREDPNLESILFHPFFTNGVEKAQAGWRRVVAQAAMLGIPVPATSTGLSFYDGYRSAVLPANLLQAQRDYFGAHTFRVLPEAADKSLPADKDIHINWTGHGGNISATTYDA P78813 YCTB_SCHPO MOD_RES 173; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 228; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 235; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 243; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 244; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 459; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC794.11c; CHAIN 1..476; /note="ENTH domain-containing protein C794.11c"; /id="PRO_0000116555" MESIQSTMKNINLYDIKAAVRKAQNVVMNYTSMEARVREATNNEPWGASTSLMMEIAQGTHNYSQLNEILPMIYRRFTEKTAEEWRQIYKALQLLEFLVKNGSERVVDDARAHQATIKMLRNFHYIDHRQKDQGLNVRTRAKELVELLNDSERIRKERKRARQNRGKFIGVGSDGDSRISTSSKSRFPSFGSSRGSYRTRVYGDGGGFTDYGNGYHDSSSMSDSRDASDNDVEEYNEDGDGGSSDAATANSTRGSRRTTTKQSDKAPEQPKQESAMIDLLGLDNEPSPAQPQTNTSAPLAFEDDGFGDFQSSAAAPASSTLNNASLFMGSQTASTAAKNDDDAFDDFQSAPSAKPASNTAAFSSISFGGFNSLNQLPTSSSAFTPQPTTFNTGYTSAFGMSSGLSNTSSQAGLGLTSQQPTAAKSSGSNGDAFGSLWSSAVNKVHQENSTRERVVSSSSEPVSKTQNFLDNDNLLL P78827 ILV5_SCHPO ACT_SITE 178; /evidence="ECO:0000255" BINDING 91..100; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255"; BINDING 115..120; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 153..157; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 262; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"; BINDING 262; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"; BINDING 266; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"; BINDING 298; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"; BINDING 302; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"; BINDING 324; /ligand="substrate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01198" CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC56F2.12; CHAIN ?..404; /note="Probable ketol-acid reductoisomerase, mitochondrial"; /id="PRO_0000015633" MSFRNSSRMAMKALRTMGSRRLATRSMSVMARTIAAPSMRFAPRMTAPLMQTRGMRVMDFAGTKENVWERSDWPREKLVDYFKNDTLAIIGYGSQGHGQGLNARDQGLNVIVGVRKDGASWKQAIEDGWVPGKTLFPVEEAIKKGSIIMNLLSDAAQTETWPKIAPLITKGKTLYFSHGFSVIFKDQTKIHPPKDVDVILVAPKGSGRTVRTLFKEGRGINSSFAVYQDVTGKAQEKAIGLAVAVGSGFIYQTTFKKEVISDLVGERGCLMGGINGLFLAQYQVLRERGHSPAEAFNETVEEATQSLYPLIGKYGLDYMFAACSTTARRGAIDWTPRFLEANKKVLNELYDNVENGNEAKRSLEYNSAPNYRELYDKELEEIRNLEIWKAGEVVRSLRPEHNKH P78854 PLB1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SIGNAL 1..21; /evidence="ECO:0000255" SPAC1A6.04c; CHAIN 22..613; /note="Lysophospholipase 1"; /id="PRO_0000024640" CARBOHYD 142; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 173; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 220; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 244; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 281; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 319; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 348; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 365; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 494; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 499; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 523; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 551; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 572; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLFRGLSLWMLFLASCLSALALPAAEDDGSVKVFKRAKKHSTKQEGPSYAPYYVDCPSDNIVESLSSNEIPSAESEYLSTRSTITNTAMKDFLRNANLPGLNADTLSGSEGPSIGIALSGGGLRAMILGSGALSAMDARHDNHTVLTGLLQASDYLVGTDGSAWTVGGIALNNFSTINDFSKLWAFNHPLMYPKSAIVFNAHFYSSIMNEVAEKANAGFNISLSDYWGRVISRTLGDTTYGFPNVSLSSITSQEWYRNANFPYPIITFATQNYGEDISNVNTTFFEASPNVFGTFDHGINSFIPTEYLGTTLNNGASSNGSCVINYDNFGFMMGASSTYFNKIMRNFNDSSTKNGRIIQQYLKGNFSENGQQIISIPNPFQGVESANSDAANNLGSSSSLNLVDTFLTGEKIPLWPLLQKGRDVDVIVAVDNGDDSEWLWPNGNSLVQTYERVVAAQAAGNTNVKGFPYVPSQQSFVSLHFNDRPVFFGCDGRNTTAGNHTVTRDTPPLVIYLPNVPYNYFTNISTDRTYYTEDMIQQLLTNGLISSTVDNDTYFGQCFACAVVKRTLERNNITASPECQQCYYNYCWSGLYDDSAANDDIVYNPTCRLGEGI P78859 ISA1_SCHPO BINDING 116; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P0AAC8"; BINDING 180; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P0AAC8"; BINDING 182; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P0AAC8" SPCC645.03c; CHAIN 1..190; /note="Iron-sulfur assembly protein 1"; /id="PRO_0000077036" MLSCLSKPALRCRSVNRLQFLRKLSLQEIQTLKTQHQYLGRTRLDVETPSLKPSAAGSGSTAPKPVTEREIASTRFMPRKNVIKLTPLAVEHLKKMQSSASMKGKMLRIGVKQKGCAGQAYSLEYIEKPDKFDEIVKQDGISIIVARRALLQIIGSVMDYRDDDLQSRFIFSNPNVKSTCGCGESFSTLK P78870 FADH1_SCHPO BINDING 47; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 48; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 70; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 99; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 102; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 105; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 113; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 176; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 201..206; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 225; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 293..295; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533"; BINDING 318..320; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96533" CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P32771}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P32771}; CATALYTIC ACTIVITY: Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378, ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000250|UniProtKB:P32771}; CATALYTIC ACTIVITY: Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000250|UniProtKB:P06525}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + S-nitrosoglutathione = NAD(+) + S-(hydroxysulfenamide)glutathione; Xref=Rhea:RHEA:78371, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:145544, ChEBI:CHEBI:229723; Evidence={ECO:0000250|UniProtKB:P32771}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P06525}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525}; SPBC1539.07c; CHAIN 1..378; /note="Probable S-(hydroxymethyl)glutathione dehydrogenase 1"; /id="PRO_0000160783" MSFEGKTITCKAAVAWGAKEPLSIEDIQVAPPKAHEVRVKVDWSAVCHTDAYTLSGVDPEGAFPIVLGHEGAGIVESIGEGVINVRPGDHVILLYTPECKECKFCRSGKTNLCSKIRETQGRGLMPDGTSRFSCRDKTLLHYMGCSSFSQYTVVADISLVAISHSAPLRSICLLGCGVTTGFGAVTHSAKVESGSTVAVVGCGCVGLAAMQGAVAAGASRIIAIDINADKEVYAKKFGATDFIDSSKVKDLVQYVIDVTDGGVDYAFDCTGNVTVMQQELQFCHKGWGKLCVIGVAAAGKTLDFRPFLVVTGRQVLGSAFGGVKGRSELPNFVDEYMQGHFKVDEYITNEEPLKNINKAFDHMHEGKCIRCVVDMNKP P78917 G6PI_SCHPO ACT_SITE 363; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P06744"; ACT_SITE 394; /evidence="ECO:0000250|UniProtKB:P06744"; ACT_SITE 516; /evidence="ECO:0000250|UniProtKB:P06744" BINDING 164..165; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P06745"; BINDING 215..220; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P06745"; BINDING 359; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P06745"; BINDING 363; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P06745"; BINDING 394; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P06745"; BINDING 516; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P06745" CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000250|UniProtKB:P06744}; MOD_RES 455; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1604.05; CHAIN 1..550; /note="Glucose-6-phosphate isomerase"; /id="PRO_0000180577" MSFSLASTLPAWQAVQTHYESVGKHLVLKELFAKDSSRFEKFSFTFNGLKEEDGPILFDFSKNLITEETVELLVKLAKEANVEGLRDALFAGEHINFTEDRAVFHPALRNVSEKPMKVNGQDVMPGVRKVLRHMKEFSDAVRSGAWKGYTGKPIKSIVNVGIGGSDLGPVMVTEALKPYGQENLELHFVSNIDGTHLAEALKKCDPETTLFLIASKTFTTAETCTNAKSAKDWFLASAKDPSHVAKHFVALSTNEKEVTAFGISAQNMFEFSDWVGGRYSVWSAIGLSVALYIGYENFEAFLSGAHAMDEYFCSTPLEKNIPALAALISIWYSDFFGAQTHLVAPYDQYLHRFPAYLQQLSMESNGKAITRSGDMVNYTTGKILWGEPGTNSQHSFFQLIHQGTKLIPADFLIPIESHNPIDNNKHHRMLFSNFAAQTEALMLGKTPAEVKAEGTPDEIVPHKTFVGNRPSNSIIAKKITPASLGALIAFYEWVTFTEGAVWNINSFDQFGVELGKKLAKNVLAQLETKGDVENHDSSTNGLINLFKNGF P78926 PMAP1_SCHPO SPAC11E3.06; CHAIN 1..398; /note="Pheromone receptor transcription activator"; /id="PRO_0000199442" MMDERKLSNFQIDGEKAYTGSSQGNSYLEDRQKRQNTFTKRKAGIFKKANELALLTGSEVMVLVVSETGLVHTFSTPKLENVVKSPEGQKLITESLINATTDQNESQASQAKQSSAQLSDSESGYPLDHEEMRISEENGPSHIENLNFFSDIDNFSKTSAEEIASKLFSSVSPTHETLQFDHGLQNLEGFQANEHPEMFADHSIDFYNSNNVDIPALSMLTSQTSSSSTLNLPPEPASREVKIFPKQGKRIFSPSTGIDYETTGQHSVNSPPSTYKHRRSLNKSFATRSEPQTPRKNKIRDSLQSSPLNFPPRDRPPLIPISRIAVPSTIETEERQYRGNQKIINFYAKIFEPNSGLGTSSEGASSSFPDVDPNLAQNGVPYYSLPDIDHNQFDHLRR P78954 IF4E1_SCHPO SPAC16E8.15; CHAIN 1..218; /note="Eukaryotic translation initiation factor 4E-1"; /id="PRO_0000193651" MQTEQPPKESQTENTVSEPQEKALRTVFDDKINFNLKHPLARPWTLWFLMPPTPGLEWNELQKNIITFNSVEEFWGIHNNINPASSLPIKSDYSFFREGVRPEWEDVHNKTGGKWAFQNKGRGGNALDEMWLTTVLAAIGETLDPTGQEVMGVVINMRKGFYRLAVWTKSCNNREVLMEIGTRFKQVLNLPRSETIEFSAHEDSSKSGSTRAKTRMSV P78970 LAG1_SCHPO CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine + CoA + H(+); Xref=Rhea:RHEA:23768, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756, ChEBI:CHEBI:77636; EC=2.3.1.24; MOD_RES 372; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 374; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1A6.09c; CHAIN 1..390; /note="Sphingosine N-acyltransferase lag1"; /id="PRO_0000185526" CARBOHYD 26; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSNRKADEKHHMSSSSLTNDRSYIRNLSNRKTSISRKVPITRTLEDPSNFVAKDGTKLVQAPLFLLVWQKEICLSIIAICFACLLSPSLRPYAEPFIFLSYKQPDGSYGKGPKDACFPIFWVIVFTAFRVIVMDYVFRPFVLNWGVRNRKVIIRFCEQGYSFFYYLCFWFLGLYIYRSSNYWSNEEKLFEDYPQYYMSPLFKAYYLIQLGFWLQQILVLHLEQRRADHWQMFAHHIVTCALIILSYGFNFLRVGNAILYIFDLSDYILSGGKMLKYLGFGKICDYLFGIFVASWVYSRHYLFSKILRVVVTNAPEIIGGFHLDVPNGYIFNKPIYIAFIILLFTLQLLIYIWFGMIVKVAYRVFSGEEATDSRSDDEGEDEEASSTNEDK P79007 HAP5_SCHPO SPBC3B8.02; CHAIN 1..415; /note="Transcriptional activator hap5"; /id="PRO_0000218261" MNSIPDSYSLKQGFPEGLGEYVDPSGNPNSQVRIGYGQDSVSRFQQPVPDVDPTAVNHYNASAPIEVASPFDNVTQGLVGSDAQALAEYWQKTIDTLEHDDQAVKTLHLPLARIKKVMKTDDDVKNKMISAEAPFLFAKGSEIFIAELTMRAWLHAKKNQRRTLQRSDIANAVSKSEMYDFLIDIISKDNNNSRASSSQAHMSATQVAAMGGMNGLQPFPTQAGLPNQGFPMPTGSQLPFSNQQSSQPSMQYSSHPSRMQQMQDIDQSMYKQQRLGSEYPQLQMSDNSGNVNQMNMQRPVMVAPYMAEHLYRYPPTHLESGSSAFRLQSSPMGYQMPQFQGNMRPNMQQSQMFDPSAYGMSRRPGSPRQFDQQQRLYSQPNAMMYQTQQGRQGNPMHQQFSQQQNPLSRYSQQPQ P79015 RL32A_SCHPO MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H5.10; STRAND 23..25; /evidence="ECO:0007829|PDB:8EUY"; STRAND 44..46; /evidence="ECO:0007829|PDB:8EUY"; STRAND 69..73; /evidence="ECO:0007829|PDB:8EUY"; STRAND 89..93; /evidence="ECO:0007829|PDB:8EUY"; STRAND 123..126; /evidence="ECO:0007829|PDB:8EUY" HELIX 38..41; /evidence="ECO:0007829|PDB:8EUY"; HELIX 52..54; /evidence="ECO:0007829|PDB:8EUY"; HELIX 76..80; /evidence="ECO:0007829|PDB:8EUY"; HELIX 81..83; /evidence="ECO:0007829|PDB:8EUY"; HELIX 99..112; /evidence="ECO:0007829|PDB:8EUY" TURN 17..21; /evidence="ECO:0007829|PDB:8EUY"; TURN 58..62; /evidence="ECO:0007829|PDB:8EUY"; TURN 86..88; /evidence="ECO:0007829|PDB:8EUY"; TURN 117..122; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..127; /note="Large ribosomal subunit protein eL32A"; /id="PRO_0000131143" MAAVNIIKKRTKPFKRHQSDRFKRVGESWRKPRGIDSCVRRRFRGTISMPKIGYGNNKKTRYCMPNGLKAFLVRNVSDVELLLMHNKTYAAEIAGNVSARKRVEIVEKARALGVKVTNAGAKVRSQE P79058 IGO1_SCHPO SPAC10F6.16; CHAIN 1..139; /note="mRNA stability protein mug134"; /id="PRO_0000116735" MVRTRKWMLSTTIIAMSSSNSEQKVDVAKLSPEEQKLFRLYGRLPQRKDLLVQKLQQGRKYFDSGDYALNKAGKASDSGITCIGKEIPSPDTIPHRVVSAGSPNKEPSLHTKRPSESSPSGASSRRESVTRHDLESNEN P79071 RL6_SCHPO MOD_RES 105; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 115; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC622.18; STRAND 53..55; /evidence="ECO:0007829|PDB:8EUP"; STRAND 57..60; /evidence="ECO:0007829|PDB:8EUY"; STRAND 68..75; /evidence="ECO:0007829|PDB:8EUY"; STRAND 77..83; /evidence="ECO:0007829|PDB:8EUY"; STRAND 93..97; /evidence="ECO:0007829|PDB:8EUY"; STRAND 101..103; /evidence="ECO:0007829|PDB:8EUY"; STRAND 112..114; /evidence="ECO:0007829|PDB:8EUY"; STRAND 130..132; /evidence="ECO:0007829|PDB:8ETJ" HELIX 50..52; /evidence="ECO:0007829|PDB:8EUP"; HELIX 98..100; /evidence="ECO:0007829|PDB:8EUY"; HELIX 121..124; /evidence="ECO:0007829|PDB:8EUY"; HELIX 139..141; /evidence="ECO:0007829|PDB:8EUY"; HELIX 151..170; /evidence="ECO:0007829|PDB:8EUY"; HELIX 175..179; /evidence="ECO:0007829|PDB:8EUY" TURN 64..67; /evidence="ECO:0007829|PDB:8EUY"; TURN 86..88; /evidence="ECO:0007829|PDB:8EUY"; TURN 135..138; /evidence="ECO:0007829|PDB:8EUY"; TURN 144..148; /evidence="ECO:0007829|PDB:8ETC"; TURN 190..192; /evidence="ECO:0007829|PDB:8EUY" CHAIN 2..195; /note="Large ribosomal subunit protein eL6"; /id="PRO_0000171016" MSTVKVNGAKNGGERMVLPAGEAAAKYYPAYRENVPKKARKAVRPTKLRASLAPGTVCILLAGRFRGKRVVVLSQLEDTLVVTGPYKVNGVPIRRVNHRYVIATSAPKIDVSGVSVEKFTKAYFAKQKRSGPVKKDEAFFAENAPKNALPAERIADQKAVDAKLLPAIKAIPNMKEYLAASFALSNGDRPHLMKF P87014 MAM4_SCHPO BINDING 155..158; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TMG0"; BINDING 163; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TMG0"; BINDING 168..171; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TMG0"; BINDING 205; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:D6WJ77"; BINDING 209; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TMG0" CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21672, Rhea:RHEA-COMP:12125, Rhea:RHEA-COMP:12126, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90510, ChEBI:CHEBI:90511; EC=2.1.1.100; Evidence={ECO:0000269|PubMed:9032282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21673; Evidence={ECO:0000269|PubMed:9032282}; SPAC10F6.12c; CHAIN 1..236; /note="Protein-S-isoprenylcysteine O-methyltransferase"; /id="PRO_0000209898" MGNLHTSIAVASICLTSAFLGCVFGLGFFVWIIYGYSIGGFFAFLSLFHLLEFYITARFQGSQLSWDSFILNNGKAYWLAMLVGLLECLLSGGKSFAKVINCLRFPSFLINFIFSVYQTSALGFLCLGQYLRSSAMVQAGQSFSHIVASKRNKDHLLVTDGIYAYVRHPSYVGFFIWALGTQMLLGNFVSTLLFSLVLWKFFSQRITTEEAYLVSFFGDSYEQYRKKVPSGIPLIP P87049 CGP1_SCHPO SPAC19E9.03; CHAIN 1..411; /note="G1/S-specific cyclin pas1"; /id="PRO_0000080506" MSKVNMRALLESFSTVILSIYPLAKSTNQQSHSHSLSLTQFLYETIRRSRVDYTTLLLALYYFIRFRDAASSKPTNYIPLLCGRRLFLVCLMAATKFLQDRSFSNRAWSRLSGLPVDKLLVLEYMFYQCIDYRLVVPKHIFARWSLLVGECCAHATARYDSTDPNVASFGSVAQYWVSLFSNVQSSLDDLFSIACLTKIAHRRMNANAALKNQATRKPSSSPQTTQDSSPILTMAPSTPVSVGSTPPSTPSVLPIAKQLAPMNVCKAHIQASNQSRTLTTASPPEQIPLMEPQVYVNPQVLPGRLSSLSKPVSLPPTPSSPKVGVYRPMTSKSNGGVAYCYNAQKLNNATGPVTFNMPFASVLPLAVSVSCDLGTASAYVASLPQPCSQKRHLEEDYSCLTEHSAKRRSYF P87051 PPIL1_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPAC57A10.03; CHAIN 1..155; /note="Peptidyl-prolyl cis-trans isomerase ppi1"; /id="PRO_0000064176" MANVELQTSLGKILIELYTEHAPKTCQNFYTLAKEGYYDGVIFHRVIPDFVIQGGDPTGTGRGGTSIYGDKFDDEIHSDLHHTGAGILSMANAGPNTNSSQFFITLAPTPWLDGKHTIFGRVVSGLSVCKRMGLIRTDSSDRPIEPLKIIKAVAL P87059 MIA40_SCHPO COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Cu(2+) or Zn(2+). {ECO:0000250}; TRANSIT 1..61; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC57A10.11c; CHAIN 62..313; /note="Mitochondrial intermembrane space import and assembly protein 40"; /id="PRO_0000116636" DISULFID 199..201; /note="Redox-active"; /evidence="ECO:0000250"; DISULFID 210..243; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 220..233; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MFAKNLLFRFPKCIRINGYNNMRRSLLQRNGFQAGICRKFGTATKTDVWKGRFLPIVSGVAAASLTAGYLLGKNTSNASSSQDNDHPVVGEHVHTETQSYNEPYMQRHRIEDAIEKKMTSETQPSTDEKGRKVSATENSAPKKTDKEKSSGETAGNILREQIATGKDDDEYARKFEEVEEESSEESAFNPDTGEINWDCPCLGGMAHGPCGEEFKAAFSCFVYSKSEPKGMECLDKFQAMQACFQKHPEIYQDMVGESEEEDAETNEKPSTTSDENNQPQSPPSDNASNPEEDVMNMEKEIVNLTPMSVIKEI P87113 ERG2_SCHPO CATALYTIC ACTIVITY: Reaction=fecosterol = episterol; Xref=Rhea:RHEA:33435, ChEBI:CHEBI:17038, ChEBI:CHEBI:23929; Evidence={ECO:0000305|PubMed:18310029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33436; Evidence={ECO:0000305|PubMed:18310029}; SPAC20G8.07c; CHAIN 1..219; /note="C-8 sterol isomerase erg2"; /id="PRO_0000087019" MKLTKFLTVFIPFIAGLIYYIQKYHLRSFYQFDPAKLQELSKQSIALYANDTKALLYDLSDRLVAEYGDLITPVNQDEWVHNNAGGAMGTMFILHASFSEYLIFFGTPIGTEGHSGVHMADDYFTILRGRQLAASANDLEARVYLPGDQHVHPWGHTAQYSMPSGEPCFALELAQGWIVSMLPFGFMDGLFSTIDFGTLYKTVYFTAGRMLKSVLMGKF P87114 FFT1_SCHPO BINDING 439..446; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPAC20G8.08c; CHAIN 1..944; /note="ATP-dependent helicase fft1"; /id="PRO_0000310747" MKRKDNKELICIPSSSPPSTPIREENYYLLTSSPIECSPIQQLDLSGSFKNYSTTSSRANGKKFGQLAMQSRIFFDTTDHKKYVESSYAAYDPHDQPPERDVSLKESSNKINPSNFFDSEQITKINAVKKRFPALDSEMIIATLEKFNWRENITIHKLTFQKLLGRGNSTINKSAQKLNNQPIEKSSVDKENAKRKRYVEEGTKQGQKKKPLRVIELSDEETNEDDLLGQSPTACTTDANIDNSIPENSDKIEEVSIESSGPSEVEDEMSEYDVRVLNFLNESTLQEIVEVSGCESKVVEYFISKRPFPSLEKAEALCQRNAHAATGKRKKSDGRNVGRKLVNSTYEVLQGFDAVDSLIAKCERYGAMISNTMRSWHNLFDDKKMEQFLNTSTGSISYEYNSQQPSSIASGITLKSYQIVGLNWLCLMYKAKLSGILADEMGLGKTCQVISFLASLKEKGIQNRHLVVVPSSTLGNWLREFEKFCPSLRVESYSGTQSERINKRYYLMDTDFDVLVTTYQLASGSRDDRSFLRKQRFDISIFDEGHYLKNRMSERYKHLMNIPANFRLLITGTPLQNNLKELISLLAFMLPKVFDNNMQGLDIIYKIKTTSDGDIERAYLSQERISRAKTIMNPFILRRRKENVLSDLPPKIQHVEYCHMEETQLSLYLSVLELKNLVNANRENILMQLRKAALHQLLFRSQYNLETLSLMSKRILREDAYLDANPQYIFEDMEVMSDFELHKLADQYRHLHPFALKGKPWMDSAKVKKLCSLLKKSRPNERILIFSQFTQVLDILEYVLNTLDLEFLRLDGSTPVETRQQLIDDFHTNENYKVFLLSTKSGGFGINLTCANIVILFDCSFNPFDDMQAEDRAHRVGQTRPVHVYRLITKNTIEENIRRLANTKLTLESSLTTDSEKIQKEISGELMKSLQMDGRVDTMDGSVV P87131 CYSKL_SCHPO BINDING 228..232; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P16703"; BINDING 335; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P16703" CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000250|UniProtKB:P0ABK5}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P0ABK5}; MOD_RES 83; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P16703" SPAC3A12.17c; CHAIN 1..395; /note="Cysteine synthase 2"; /id="PRO_0000167129" MAKKYQDLASGIAMGAVFMYLLRRLYESLRVKSSADSLEEDIVNGVEGLIGNTKMVRIKSLSQATGCDILAKAEFLNPGNSPKDRVALQMIRTAEENGDLVPYQSNAVYEGTAGSTGISIAMLCCSLGYDSRIYMPSDQSKEKSDILELLGAHVQRVTPAPIVDPNHFVNTARRNAANHTVDESIPGKGYFANQFENPANWQAHFNSTGPEIWRQCAGKLDAFIAGSGTGGTIAGISRYLKSKDPSITVCLADPPGSGLYHKVLHGVMFDLAEREGTRRRHQVDTIVEGVGINRMTRNFSIAEPLIDMAYRVTDEQAVAMSRYLVTHDGLFVGSSSAVNCVAAVRLAKKLGPGHRIVTLLCDPGSRHFSKLYNEEFLRKKNIVPQVPSSLDFVEA P87140 COPG_SCHPO MOD_RES 604; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A7.10c; CHAIN 1..905; /note="Probable coatomer subunit gamma"; /id="PRO_0000193860" MSYSKKDDDGDESIFANVNQVTVTQDARAFNSSSISPRKSRRLLSKIAYLIYTGEHFQEKQATELFFGITKLFQHKDPSLRQFVYIIIKELSVVAEDVIMITSSIMKDTATGRETIYRPNAIRSLIRVIDANTVPAIERILTTGIVDPISAVASAALVSAYHLYPVAKDIVSRWNNEVQDAVTSHNVGRKVASSPFFTSTLGYTPNASGISQYHALGLLYRIRRHDSIAMNKLLQLLVSNLGTVSNSHAFVMLIRYISSLMDQNTQFRDQMVPFLHGWLKSKGDMVNLEVARNMVRLKNISDDDLQPVVSVLKIFLSSHRSATRFSAIRTLNELAMTRPHLVHSCNLNIESLITDVNRSIATYAITTLLKTGNDESVDRLMKQIVTFMSDISDNFKIIVVDAIRSLCLKFPRKQDSMLTFLSNILCDEGGYEFKRAAVDAISDMIKYIPESKERALAELCEFIEDCEYPKIAVRILSILGEEGPKASEPTRFIRYIYNRIMLENAIVRSAAVSALTKFGLNAEDKFVQRSVKVILTRCLEDADDEVRDRAAFSVKALEDRDAFLPVVKSDKIPSLPALERSLVIYISERKFGQGFDIKSVPVLSQEEIDAENLRIKKATTEVEFTEVTPAEDQNALASSNIETEFLNALESVSEFNEYGPVLKSSPSPIELTEQETEFVVKVVKHVFKDHLVVQFQLHNTLSEVILENAVVVSTPSTDDLVEECVVPAAIVSGEPVSIFVSFKFNDSVPYPLTTLTNTLQFTTKEIDIHTGEPEEEGYEDEYKIDDLDVSAGDFISPAYESNFDGLFDSLEHEASEVYVLSLLDSFRSTCSRVAELLQMQPLEGTENPTDKPVHVMKLSGKLVNGEKVLALVKMAHSKDGEGITIKVIARGESDSSVELVVGGIA P87152 SPT7_SCHPO MOD_RES 475; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25H2.11c; CHAIN 1..992; /note="Transcriptional activator spt7"; /id="PRO_0000310328" METNFEDSKSLDEPVLHDIAIALLKNDYWSLYLSPEQKRKYISILNDTLLWNRFINVIEWDKLCDEKDSNGSNDDEEDDLDITTLFRCRCMIFDAKINPALFDLSSTSSGSIEHVDHQNISLEASLAEEEERKKGDAKKSEATGRQLFDDDDFDESDAEDSSKATITLDLQKDKSLRKSIIDLKSVDIDDMDTSGFAAIESNKALSNISFNYVYYTLENDSENINEVKKFEDEEDTSTPNTSSFQNNSSSLDLSDNLSLNSKFGSLTSSFKYLLQYLEGNRSKINATDADVKQLLSDVKKNKSKWANDQRIGQEELYEAAEKVVLELRSYTEHSLAFLTKVSKRDAPDYYTVIKEPMDLGTILRNLKNLHYNSKKEFVHDLMLIWSNCFLYNSHPDHPLRVHAQFMKDKSLELINLIPDIVIQSRKDYDDSLIEAELESDEESTAETSKHVTSKKTSSRGGQTQQAVEVHTDANSPEENNTPVTKKEVETSKPPAVSGSTPPVNEAAVIESSNTLEKEPLSDVATEYWKIKTKDIRESHILNNRRILKSLQFIETELPMIRKPTAMSAFIDREVAYGSIDCLPMDKGDFEPIMKLDTTPLLEYDVGSGVPMTAGSVLETESEEDLYFRDYSLFEINRNTPGVPSLMYKNIAKMQEIRKLCNKIQTVRQLQLPQPFYYEHHKSHVPFANNEPILLDIPQNYDNMSSFKPLAHDVLKKLCTIILFHAGFESFQMGALDALTEIAADYMAKMGAVMDQYLIYGKDKSQQEIVGQTLGELGVDDVNDLISYVYHDVERQSVKLLEIHQRLQRHFVELLRPALSERNDEEAIFNQNGESFVTGNFSYETGDDFFGLRELGLDRELGLDSLSVPLHLLQSRLRSNMSWQPEATIKGDQEYAPPPKYPPITAESISNEIGLIQGFLKKNLEEFGLDELLEDEDIRPRSKPPRPRLPPNGKITTGRKRIASSVFLNQSLRKKRCLKENEQGTEVTTLPEE P87157 YB0G_SCHPO MOD_RES 320; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25H2.16c; CHAIN 1..533; /note="Probable ADP-ribosylation factor-binding protein C25H2.16c"; /id="PRO_0000353801" MSSAKRRLYSLIQNATEPYAFEPDLAVNLDIADLINQTGGNLPREAAFAIVRKVNDRNPTVAYLALNLLDICVKNCGYAFRLQIASKEFLNELVRRFPERPPSRLNKIQVMILSLIEEWRKTICRVDRYKEDLGFIRDMHRLLSYKGYTFPEIDKENLAVLSQKSVLKTAEELEKEDREAMSAKLQELIRRGTPADLAEANKLMKVMAGYDTEQKQKYKEHVLVDLEKVKRKAALFGEMLNEVSESDKLASGDLYDELAYSLKAAQRKVDKILEEMSPEDDSYVTVSDLKSLIASLLTQYDHLLEGDFSSARTVAADNNSLLQATTESAKSNSKTSANASNTQSAMDLLIDLDIGSDAQSPSLPASSSQMPTSSFNMESLSQSLLGTVEAPAEVGAISLTESFNSPVSNSSPNVPINNFTSTCAFENSHLNFQITPKSKTRDQVVLLATYTNLSPYDTVENLQSFIAVPKKYNLVLQPQSGTNLSPLQKDGIYQEMIVTKLLDVTELPVRFKLTYKVNGRSQEYTGQSSIRLL P87159 NIF1_SCHPO MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 196; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23G7.04c; CHAIN 1..681; /note="Mitosis inhibitor nif1"; /id="PRO_0000096819" METMQSRTYAGLTKLNTTTALLNKKDGNDDDKAEHSKRSGYHGLSPLDALALKHRDLNRKLNLRAMMSKSEDNLQILKETTSGSSSDLLNIESPASPAEASSPFTVRTPTVHDPEHYFVAQKLSSVFGTPDLEDETDFFDYFSAAPDVHPNDIFDSYNSNNIAESFDDDNYYNSLLPPNAPYYHEIEPPRTASNTSPTPNSIKSAHPAEPPKRPAFTRSATSPDKILPTRIKSKDTVSSGDSTPLSGSSSSKGMLMSMSTSENHSLSSNPELSNSNLLAKNESPADVSNNESGNESSKEPDKEHSTPIHPTTPVSRCARPSSRQQTISILQAQSPFLKKSDKERANLNKTMVSINKSINIHQSIHEISCPHHSSSDNCLFILISLMDRLHSPVLKQLDVSLQSLTMTAIRYIDLNYVDVQYTNLRGGAYGNGNNSESSDNAQLKKEEHLNLAIHFHLLNDHDKCFWHTGMASSYEDYTATFIYGLYLRHGLACSPKTHVSFLFLLKTATQLLNKLVECLHSSDLGLNDTTPNEKLSTEYNQQRLLLALILYELGVCFMHGWGITRDRYLALHLIKLSGAWGDADAQFEAGLQMSLGAVSDKDSHMAAYYYRLAGFQGISPPSKCKWVYKSKYSLAANHKVPAASEVAYVSAIVENLESHSLKFSTKPKAKLRSLITSVRYL P87168 RNZ2_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.; EC=3.1.26.11; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; TRANSIT 1..37; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3D6.03c; CHAIN 38..678; /note="Ribonuclease Z 2, mitochondrial"; /id="PRO_0000315962" MKASLLVPRRALLFGQLLPPKYSWYSVKRWQSQLTFRNKSKRNTNRIMLSVVSSLNPDSLIAPLLCVSLDNRKYLIGSMGELTQMKFRSQASNYGGKSVSVFLMPPSLQSLNAWGITAGLFGYLQSSGIQNTWGLHAPKPVISIIKKSHHLFSGSPLRLDLNSFSSEDNADATNSFYLDEPEFCTIKGNIYSNWSFLSFNSKEAAGVFNADKALALGVPFGPSNGKLCAGEAVLSKDGTTWIYPHQVVGPPRKRQYFYVLGCSSLSALNQMSKHVDSFSDVYPTCIIHILEKGIWGPEYIKFLSHPKFSRAQHFISCIELASNNPVFQRNKGRNVLPACRDFAAFDIKPSTLDTQTQLPENTYVLKEETSMVLYDEQCKISESPSYSPVKLAKKFSSFNPLPFENEGYTLDVLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRQYGTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKANTNNSMHINIIGPKFLWQWLQRLKSPANLQALLNRIIFIIAKETVTTPLQLTSDLSISSVPSIHINDSYSCIISHTKYGKLVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRSYDADFLPPDWTIYPKSKTIYANDGLQWQQFQSKQRETI P87169 MAD1_SCHPO SPBC3D6.04c; CHAIN 1..689; /note="Spindle assembly checkpoint component mad1"; /id="PRO_0000213796" MSSKLTVYQATTSMADSPRDPFQSRSQLPRFLATSVKKPNLKKPSVNSANETKNPKLASLEFQLENLKNDLKRKELEFEREQIELQRKLAEEHEQKNSLQLRLTLVEKQLEEQSTSYQKEIEEVRNEKEATQVKIHELLDAKWKEIAELKTQIEKNDQALSEKNHEVMVSNQALQMKDTNLTNLEKLFADSREQLETKCKELAAAEQQLQELSVHNQQLEESIKQVSSSIELEKINAEQRLQISELEKLKAAQEERIEKLSSNNRNVEILKEEKNDLESKLYRFEEYRDKVATLELENEKIQTELNSWKSLITNELPTPEAVSNKLVFLQNTNANLGERVSSLESQLSNKPANQPLGANEKDAAHITELETKLKELHEQNRRLQRQKSLATQEIDLLRENLKSYDDEEAILSEKNTDMKKLERIEGLVKLVDEYKLKLESMPVSLDVDETSDEVSLQKRRRKNEHKDAGYVTELYRKNQHLLFQVKEKTNIEAFLREQIITLESSIATLRQELAQVTEINSCRVLQHRSNPTLKYERIKAAQLEMLNAENSALKALLEDKKVDCLPIQSFKIAERKALDLKKEVAEREKRIQRLKEIFSVKSLEFREAVFSLFGYKLDFMPNGSVRVTSTYSREDNTAFIFDGESSTMKLVGNPSGPEFERLIRFWCDERKTIPGMLAALTLELLDKND P87170 DGK1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + CTP = a 1,2-diacyl-sn-glycero-3-phosphate + CDP + H(+); Xref=Rhea:RHEA:25948, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069, ChEBI:CHEBI:58608; EC=2.7.1.174; Evidence={ECO:0000250|UniProtKB:Q12382}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q12382}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12382}; SPBC3D6.05; CHAIN 1..218; /note="CTP-dependent diacylglycerol kinase 1"; /id="PRO_0000371716" MSTKLTWSQWSKKHEIPRKALHTSIGFFALLLQGCGYHAAQIIPVIEIGFIPAFTGDVIRFNWPAFSRLYNRVIGPLMRESEKNAWNGVIFYMIGVWIVLKVFPEEIAVMSVLLLSWCDTTASTVGRKWGKYTPKIAKNKSLAGSLGAFVCGVFCCYVYWGLFRTGPDSLAAQSRIPFPWLCLINGFIGAFAEAMDVWGLDDNLVIPVVSACLLYLIM P87173 LSM1_SCHPO SPBC3D6.08c; STRAND 22..28; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 33..41; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 47..58; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 61..72; /evidence="ECO:0007829|PDB:6PPQ"; STRAND 77..82; /evidence="ECO:0007829|PDB:6PPQ" HELIX 16..19; /evidence="ECO:0007829|PDB:6PPQ"; HELIX 74..76; /evidence="ECO:0007829|PDB:6PPQ" CHAIN 1..140; /note="U6 snRNA-associated Sm-like protein LSm1"; /id="PRO_0000125590" MNQATQIIPFTTSGSLVDYVDRKVIVVLRDGKKLIGILRSFDQFANLMLQYTIERIYVDDMYGDIDRGVYIVRGENVVLLGELDLDKEYDAVKQLRRMPAEELYPLAKLHEEEKKKNIREKGKYLHSVGFSVDGGHDDLY P87179 WSC1_SCHPO SIGNAL 1..29; /evidence="ECO:0000255" PTM: O-mannosylated. {ECO:0000269|PubMed:15948957}. MOD_RES 354; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC30B4.01c; CHAIN 30..374; /note="Cell wall integrity and stress response component 1"; /id="PRO_0000041487" CARBOHYD 278; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 284; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVFLNSSPFKGRLLFFVYLLIISTRLVAADMNTQYGCYLVDSSLTEQGTFTYLDPAYCYNNICGGSDNIAFVAIRNNQCYCGSTLTATEVSSSLCTTPCPGYGSLMCGGDLYWSVYLTGNGVLQTTVSSSSVSSTTSSSSSSSPSSSSTTTTTSPSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSVPITSSTSSSHSSSSSSSSSSSSSSRPSSSSSFITTMSSSTFISTVTVTPSSSSSSTSSEVPSSTAALALNASKASNHTSLNAGAIVGIVIGCVAFAVVMALCIFLYFYFRRFKIRMSDSANEGKYPSYASELDSRLDPAMMNRKSSESLADSQDYSRKILRVTNLN P87228 SERA_SCHPO ACT_SITE 284; /evidence="ECO:0000250"; ACT_SITE 313; /evidence="ECO:0000250"; ACT_SITE 344; /note="Proton donor"; /evidence="ECO:0000250" BINDING 205..206; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0A9T0"; BINDING 225; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0A9T0"; BINDING 282..284; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0A9T0"; BINDING 308; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0A9T0"; BINDING 344..347; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0A9T0" CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.399; Evidence={ECO:0000250|UniProtKB:P40054}; MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 258; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC364.07; CHAIN 1..466; /note="Putative D-3-phosphoglycerate dehydrogenase"; /id="PRO_0000076017" MDIKGGRRGNVEDSLNKLSLSPPDNNSSFLSNHFQVRKSYSQAPARTLKPFASEDIKILLLENVNQSALSNLKDEGYQVEFLKTSMSEDDLVEKIKGVHAIGIRSKTRLTRRVLEAADSLIVIGCFCIGTNQVDLDFAAERGIAVFNSPYANSRSVAELVIGYIISLARQVGDRSLELHRGEWNKVSSGCWEIRGKTLGIIGYGHIGSQLSVLAEAMGLHVVYYDILPIMPLGSAKQLSSLPELLHRADFVSLHVPASPETKNMISSKEFAAMKEGSYLINASRGTVVDIPALVDASKSGKIAGAAIDVYPSEPAGNGKDKFVDSLNSWTSELTHCKNIILTPHIGGSTEEAQYNIGIEVSEALTRYINEGNSIGAVNFPEVSLRSLTEADRNAARVLFVHRNVPGVLRQVNELFIDHNIKSQFSDSRGDIAYLVADISDCTPGSLEALHQKLESLPCKINTRLLY P87233 PHF1_SCHPO SPCC4G3.07c; CHAIN 1..461; /note="SWM histone demethylase complex subunit phf1"; /id="PRO_0000363000" MSQKNFFDEGKSYGVNDYAGFHFENGADSSLPQVSAQGVVRETDSSNFDASPVASGSGISDVGPFGADFHQLQQHVQTPYGGMTMPASSSSGATSVPPEQDPSLSVSFNRLPKSASTKTKNGRIRSSRREDDNRIPFYDLDVAEGAEDDLQEDFHVEGMKTKSGRKIQRPVAYNPNATALKRKSRKVDMVTLCSVCQRGHSPLSNRIVFCDGCNSPYHQLCHHPPIDDATVQDVDAEWFCMKCQYRRAKQPLETGMTAQDLGLSESDKKMYLSSLPTPHLADLILFCEKSYPSLPIYNPRTRELLGEIRHQLLVSSERQQISLQERLHAKQDEAPSDEPAPVPYTASYVANSGTLYDYPTLIRLAIRNTLSPSKDEIFNWLAQNVPLLPTFHDSASEAIRWMVNKGQLVRSGSIYQIATVEEYPHLQPSLLPTFQRNRKVPKLVPVSFPTDDPQNLCATVL P87241 RIB2_SCHPO ACT_SITE 307; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q12178" BINDING 305; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 335; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 345; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+); Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26; Evidence={ECO:0000250|UniProtKB:O66534}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion. {ECO:0000250}; SPCC4G3.16; CHAIN 1..405; /note="Diaminohydroxyphosphoribosylamino-pyrimidine deaminase"; /id="PRO_0000310862" MQIPEKYLSSVDNVEEETQILFALSKQKDADLGMLDSKQEQIALTIGNKPIKVKQSLQSLHQSRGSTGSVLWKTSVKVVPWLLQQSWFMNSLTPKTSILELGSGISGLAGILLSPFVGNYVASDKQLYLKKIRENLDQNNASDVEVHELDWKSTPYPKDWTFDFLDYVLFFDCIYNPHLNAHLVSCLASLAERYPGMQCLFAQELRDQETLVDFLERVRPYFEVDLIKMEEINKTSVASSTNLPPANMSLFIMKPYNHEEYMLKALNEAKKCEPTDSAFCVGAVIVQNGKIVSTGYSRERPGNTHAEECAIEKFMLKNPTDSLEGAIMYSTMEPCSKRLSKKVSCTDLIVKQKFSTVVLGSLEPDIFVKCEGVDLLKKAGIVVIEKLTFQDDCLREAVRGHPPKH P87244 ALP16_SCHPO SPCC4G3.19; CHAIN 1..759; /note="Spindle pole body component alp16"; /id="PRO_0000064567" MDGIMKNDLLWFGNHVFDLTPNSFDSDFVEQLSKFEGKEGLKRKLFDSSEYFQNFSFQVNDDLLGKDVILDISNQQLTPAVPGCETSSNSKLISASKEITSERKRAKSSVSPSYLTDSSPSDLSVENKVLLTCPSWDGENFKNLEARSPFISEAPSRVYDYFLHNQDWSPKPLFSALQVYPLATIFNCVAGLPQGFESTVFPWNKTSSTFELDPTISVSGMSDECFASIVQKFSAIGGLIKKALNEFSLYKTNISFYLSNFIVNGVLQYRKEFQRWLRLYEFRRFGLIGLSNFVNSFSSFFELISHFLIKSAQNLKGDSLLDFLFDYARSCQNTISYPIALQCLIYCSNPYFKRLELALKVSCAYGHIDSSLFLSLPRFFPSELCVSIEQCIQFLSLIREQKEIFNKNNKEFINPLNIRFAYSFNDINQACVIEERCNFSSLSFGNLEQTSVNNDSEEFETLLAKMNMTPDFNDNLLQLKFTDDVRNVCPLNLNVCCCIAEPIQSFILSFLRSTYKVLKNDFQVFDLLNFFHSTFLFQNYEFSDNVISLLKSRRLDKSDRNELAEDLNSDDRYNFISRLKKFIFMEKEKNGLSRSLSKSITFTLDSASVSEFEDVYPDLQFQCQVIGALRILFTDNSLNYYSKTFSYVLHLFQAQSDFESSVELKDRSIVTKTTIMSWSKYQGTKESLFQFLSIYIPECMLPFTKLLKSIYSPDCPTNIQNSAIKNAASVHEQCTKAIYQKVKELFDTMKLWESSIKVS P87306 MED17_SCHPO SPBC31F10.04c; STRAND 46..48; /evidence="ECO:0007829|PDB:5N9J"; STRAND 154..158; /evidence="ECO:0007829|PDB:4H63"; STRAND 218..220; /evidence="ECO:0007829|PDB:4H63"; STRAND 226..229; /evidence="ECO:0007829|PDB:4H63"; STRAND 242..246; /evidence="ECO:0007829|PDB:4H63"; STRAND 253..256; /evidence="ECO:0007829|PDB:4H63"; STRAND 265..271; /evidence="ECO:0007829|PDB:4H63"; STRAND 277..282; /evidence="ECO:0007829|PDB:4H63"; STRAND 330..336; /evidence="ECO:0007829|PDB:4H63"; STRAND 342..348; /evidence="ECO:0007829|PDB:4H63"; STRAND 419..421; /evidence="ECO:0007829|PDB:5N9J"; STRAND 451..457; /evidence="ECO:0007829|PDB:4H63"; STRAND 473..475; /evidence="ECO:0007829|PDB:4H63"; STRAND 479..486; /evidence="ECO:0007829|PDB:4H63"; STRAND 487..490; /evidence="ECO:0007829|PDB:5N9J"; STRAND 493..497; /evidence="ECO:0007829|PDB:4H63"; STRAND 509..512; /evidence="ECO:0007829|PDB:4H63"; STRAND 517..522; /evidence="ECO:0007829|PDB:4H63" HELIX 34..45; /evidence="ECO:0007829|PDB:5N9J"; HELIX 53..65; /evidence="ECO:0007829|PDB:5N9J"; HELIX 101..130; /evidence="ECO:0007829|PDB:4H63"; HELIX 136..140; /evidence="ECO:0007829|PDB:4H63"; HELIX 143..148; /evidence="ECO:0007829|PDB:4H63"; HELIX 168..213; /evidence="ECO:0007829|PDB:4H63"; HELIX 293..320; /evidence="ECO:0007829|PDB:4H63"; HELIX 322..324; /evidence="ECO:0007829|PDB:5N9J"; HELIX 374..407; /evidence="ECO:0007829|PDB:4H63"; HELIX 425..447; /evidence="ECO:0007829|PDB:4H63"; HELIX 459..461; /evidence="ECO:0007829|PDB:4H63"; HELIX 466..472; /evidence="ECO:0007829|PDB:4H63"; HELIX 523..534; /evidence="ECO:0007829|PDB:4H63" TURN 131..133; /evidence="ECO:0007829|PDB:4H63"; TURN 222..224; /evidence="ECO:0007829|PDB:4H63"; TURN 248..250; /evidence="ECO:0007829|PDB:4H63"; TURN 338..340; /evidence="ECO:0007829|PDB:5N9J"; TURN 535..537; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..545; /note="Mediator of RNA polymerase II transcription subunit 17"; /id="PRO_0000096365" MAEEANKDADISSLSLSLDPEIIGGQNNFLENNLQQIFQKIIQERGPFRDLKEEDLQKELQKESIKDESSAKSSETENVLEFATLDSKRNVNDTEVESMDSQAYKKELIEQIMIAQTECSLALDMTSLLLSKFKENSIETISPFLKSTVPPSSLQFSRSQPPESKESDATLAKCWKEKSLTSSCKFLFEAKERLTSVVETEHEYYTELVKVKEASWPLFNSQGSNHLSVQYSCLGGISLGLGLIRMKPESKSFEVQSSLLYSQAALKISILNKDRDEIGSSTWSWPSQNCNSVLLKDIYKLQEILFEMDIWNSLLQEAQSCGNQGVNFTGDEILVPISDDHVVRITLETSSKNTESGFTEDKKSNEDTSTNFVTIKQEKELLKCLCDTLNAIAHILFLKHCRKSDRRSQQPELYMAIDANAPLILRPLIFYYNLNQESLEFQRWLKQRDISFKFMPNYPWEKAKDFLELENSLSINRLSISWRIMVSNFEPAIFIQHTPTLHGTDKSVWRCKDQYSSNQFSSLKNVCQYIEHHINSLSRRSKKTE P87310 MED10_SCHPO SPBC31F10.09c; STRAND 68..70; /evidence="ECO:0007829|PDB:5N9J" HELIX 9..33; /evidence="ECO:0007829|PDB:5N9J"; HELIX 43..65; /evidence="ECO:0007829|PDB:5N9J"; HELIX 71..78; /evidence="ECO:0007829|PDB:5N9J"; HELIX 83..122; /evidence="ECO:0007829|PDB:5N9J"; HELIX 124..126; /evidence="ECO:0007829|PDB:5N9J"; HELIX 127..137; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..144; /note="Mediator of RNA polymerase II transcription subunit 10"; /id="PRO_0000096356" MLPQDDMTDEMKSLASRLEDTTQAFYDLALIVYNLEDTTPSDAIPESLDTLIRDLKSLPDISRKVNNLIPQDVLEYIEQGRNPDVYARQFSELVQKDNQYVNGKLYAIEGFQKAFAEEIKQAYPEVSSVVDKILNEGKVESTVS P87312 CLF1_SCHPO SPBC31F10.11c; CHAIN 1..674; /note="Pre-mRNA-splicing factor cwf4"; /id="PRO_0000205750" MTSEAPRVKNKNPAPIQISAEQLLREAVERQDVAFVPPKINITDLEELQEFQGRKRKEFEDAIRRNRLAMGHWMRYGQWELDQKEFARARSVFERALDVDSTYIPLWLKYIECEMKNRNINHARNLFDRAVTQLPRVDKLWYKYVYMEEMLGNITGCRQVFERWLKWEPDENCWMSYIRMERRYHENERARGIYERFVVVHPEVTNWLRWARFEEECGNAANVRQVYLAAIDALGQEFLNERFFIAFAKFEIRQKEYERARTIFKYAIDFMPRSKSMELYKEYTHFEKQFGDHLGVESTVLDKRRLQYEKLLKDSPYDYDTWLDLLKLEESAGDINTIRETYEKAIAKVPEVVEKNAWRRYVYIWLNYCLFEEIDVKDVDRARKVYQEALKLIPHKKFTFAKLWLMYAMFELRQRKIDVARKTLGRALGMCPKPKLFRGYIEFEDAIKQFDRCRILYEKWILYDPEACAPWLGYAALETKLGDSDRARALYNLAVNQPILETPELVWKAYIDFEFEEMEYGKARSIYQQLLRTAPHVKVWISFANFEIAHLEDDDEEPPNEEVASPTAVVRARNVFENALAHLRQQGLKEERVVLLEAWKQFEAMHGTEDTRKHVSSLMPQVVKKRRRLEDGSFEEYLDYLFPDTATDQGDKMRKMLELSRKWKEEMAKKKLEA P87315 HIR3_SCHPO SPBC31F10.14c; CHAIN 1..1630; /note="Histone transcription regulator 3 homolog"; /id="PRO_0000256203" MATFTPLNAASEDLDKEKRTLEIRIEEAVQIYQNALSAQKQGDDNAATKYYDELLNVRILRELPFTVNSNYKKNNALLLLHYLTRKNHGLFLLSKLQSLLSLDPSTDPIPVYRDALLDFAIALACDYNDIELWSFVAELAEKLEMPRIQRFALESSFYTGYEPFDAERVFTNIDDLNPGKLISLQNLYNLLKKLGGIAEPLPQLDLSISSLYTLPSFFPQLPTPSFHRRSINLCPKIKKLQLSHDTLHGFLDLVLYALQINEKKTPTRGFPSTLIIHVHSLNLSTAESHDLESTDSELWSEISDAGPDTNTINTAAKLSEPVYAKDIVPPPSDNLPKPQLLKRPIDDSDVRISKRSRGRDLRTPSESNLFSLIASITSDINEQIQKRFPDATSPFSGESMFREYSSIFEDYHQLLVNFPSEGSIPDLDVSTDSAANGAFSKMILIDLAMHSANRLEHMQVPDGYLLQLLSEVNSLNMVPAELATFFVESMLRPRKLEPPFYLQQCWGKIFKKKFTTICERIESTLHELVKASLQTPEVFNISQSLFELFLDDYFLALKFSSNDQKDDNVSEIPTESLEYKKLRCLRWKSLTEQVVELQPSCKSSSQRHLIIRNSWARNLLLRLTGCSSEAIVENFKQLRCLLQENSDSLELLNSQCMADLSVQVVDFELSKLQTVEFFNTLFMNTKNLDFNAVIKNLEPVLSPENKFAEDPQAKFISQFLEKTSTEFQIHLWYLLYQAYSSAHRPYNSLLCAFQSLKIILIRLCSSSFSIQDAGRRQAELLGMLNFSSNLFRIIWQKLHEQPDILSPCNEMTVIDCIRIILIYLRTFAIYVGIDEDISDQRIPKPSNPEFDSYAQTVKDSLMSGWCIFYTLFAHLLHYDFIKADAQKLLPQILTAIHSQYSFRGYCSSSNQSFLELSQTECQRLDAWENENEILQCVCCRFNLIIGSEYYVPQSHQSDSVNLTSNDAIKIIPFILGFAVKRSHGWVMPRSDQKNALEIICKVIRFPGENNADVYFNKCAIKEFLERDISPQLTKMLLKSNDILGLREIGSKVVDDRVRGLYYAQSQVLFGYYRSRLKGSRCINDLLVIIKYFLLDLYLNPRRQDSWYTCSSVFSSLADEELGWSAEQICLADDVINEYRRKAILCNLMALSLPFTQDKLFKANVYFDFAMNLYASARPPLEMAAFLPSETRVFSGASGLYNLSMKPIEVSKVIALAADYFGMSAELSNDWRALYMLGKACRKCGDMENALVHFEAAAALAPTKSGSGSQQALLIEPHYALLSNLSKAAIEGSVEIVQILSYLRRIRHPPKDSGSLLEVKNEDVNIYKRNALLFILKALAEMRILDKQSWHHRPTYRIAKIMEHLGNVQQAKEEMETLFSYKTSGKSLLNIWRTPNERPGRHFYYGATYSRYLLSLFYKTNDKVNFLQFLKRFRRSSSTIYEHRQIWLDIMIKYLEDLRLQHSVKETQINDLPLVEFKYVYKEISLLDEQKLSLLHQVYEIRKLNNGLYPTIKVDDFLIDCFMSLYNEVKSSISPLDANIPNSPSTITAKPLNDEKAINNENSVKQKTVITRKDVVSKVLALFRPHRETYYRETQNKILQKLASTSSSLVRSFTEDSSQAGESPGIHEEIQ P87323 MCS4_SCHPO MOD_RES 412; /note="4-aspartylphosphate"; /evidence="ECO:0000305" SPBC887.10; CHAIN 1..522; /note="Response regulator mcs4"; /id="PRO_0000081407" MRIWFKKVPDGITSSVILSEDHLVDDLKDAIARKFPIRISQYYDAPELSIRVVAPPNASSELQSRELSPNESILFVMETYYPHGQDFNDALLVASPDTSVALRYRSSQLSSSTFESTPPVFSEYPPNIIPTPANETVPRIKQPSIALDSLESPVSAPSRHQSTYSYKGGPLNYNLRNASRTRSHQTLPSSNVNKTGVLLLPRSSRQQTLASRPSLPDLTSADKSQPSDEAESITRKNSIGMSTRSDESTAEKLAKAEVATPTNSRSISHSSLYTKQSGTAGVLPAVNADIDAANRMNPDISSQFPIADNKDPLNADTQAHLGFPSNQIDGIVGTSPVNVLTSPGIGAKAPFASLLEGVIPPINVLIVEDNIINQKILETFMKKRNISSEVAKDGLEALEKWKKKSFHLILMDIQLPTMSGIEVTQEIRRLERLNAIGVGAPKLTQPIPEKDQLNENKFQSPVIIVALTASSLMADRNEALAAGCNDFLTKPVSLVWLEKKITEWGCMQALIDWNGWCRFRGR Q00472 PNPP_SCHPO CATALYTIC ACTIVITY: Reaction=4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) + phosphate; Xref=Rhea:RHEA:21664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57917, ChEBI:CHEBI:61146; EC=3.1.3.41; PTM: The N-terminus is blocked. SPBC15D4.15; CHAIN 1..298; /note="4-nitrophenylphosphatase"; /id="PRO_0000058480" MAKKLSSPKEYKEFIDKFDVFLFDCDGVLWSGSKPIPGVTDTMKLLRSLGKQIIFVSNNSTKSRETYMNKINEHGIAAKLEEIYPSAYSSATYVKKVLKLPADKKVFVLGEAGIEDELDRVGVAHIGGTDPSLRRALASEDVEKIGPDPSVGAVLCGMDMHVTYLKYCMAFQYLQDPNCAFLLTNQDSTFPTNGKFLPGSGAISYPLIFSTGRQPKILGKPYDEMMEAIIANVNFDRKKACFVGDRLNTDIQFAKNSNLGGSLLVLTGVSKEEEILEKDAPVVPDYYVESLAKLAETA Q01682 PPA2_SCHPO ACT_SITE 69; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 341; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; SIGNAL 1..18; /evidence="ECO:0000269|PubMed:2249257" SPBC428.03c; CHAIN 19..463; /note="Thiamine-repressible acid phosphatase pho4"; /id="PRO_0000023952" CARBOHYD 98; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 186; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 251; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 328; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 433; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 439; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 458; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKLSGISLWLLAASIVHAGKSQFEAFENEFYFKDHLGTISVYHEPYFNGPTTSFPESCAIKQVHLLQRHGSRNPTGDDTATDVSSAQYIDIFQNKLLNGSIPVNFSYPENPLYFVKHWTPVIKAENADQLSSSGRIELFDLGRQVFERYYELFDTDVYDINTAAQERVVDSAEWFSYGMFGDDMQNKTNFIVLPEDDSAGANSLAMYYSCPVYEDNNIDENTTEAAHTSWRNVFLKPIANRLNKYFDSGYNLTVSDVRSLYYICVYEIALRDNSDFCSLFTPSEFLNFEYDSDLDYAYWGGPASEWASTLGGAYVNNLANNLRKGVNNASDRKVFLAFTHDSQIIPVEAALGFFPDITPEHPLPTDKNIFTYSLKTSSFVPFAGNLITELFLCSDNKYYVRHLVNQQVYPLTDCGYGPSGASDGLCELSAYLNSSVRVNSTSNGIANFNSQCQAHSTNVTVYY Q04635 ESC1_SCHPO SPAC56F8.16; CHAIN 1..413; /note="Protein esc1"; /id="PRO_0000127170" MSSYALPSMQPTPTSSIPLRQMSQPTTSAPSNSASSTPYSPQQVPLTHNSYPLSTPSSFQHGQTRLPPINCLAEPFNRPQPWHSNSAAPASSSPTSATLSTAAHPVHTNAAQVAGSSSSYVYSVPPTNSTTSQASAKHSAVPHRSSQFQSTTLTPSTTDSSSTDVSSSDSVSTSASSSNASNTVSVTSPASSSATPLPNQPSQQQFLVSKNDAFTTFVHSVHNTPMQQSMYVPQQQTSHSSGASYQNESANPPVQSPMQYSYSQGQPFSYPQHKNQSFSASPIDPSMSYVYRAPESFSSINANVPYGRNEYLRRVTSLVPNQPEYTGPYTRNPELRTSHKLAERKRRKEIKELFDDLKDALPLDKSTKSSKWGLLTRAIQYIEQLKSEQVALEAYVKSLEENMQSNKEVTKGT Q04800 FRP1_SCHPO BINDING 157; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="1"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 171; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="2"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 225; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="1"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 239; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_label="2"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P32791"; BINDING 317..323; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255"; BINDING 419..427; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9; Evidence={ECO:0000250|UniProtKB:P32791}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P32791}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P32791}; MOD_RES 362; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 381; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 383; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1683.09c; CHAIN 1..564; /note="Ferric reductase transmembrane component 1"; /id="PRO_0000210152" CARBOHYD 4; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 111; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 268; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 360; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 501; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAINSSDKWTVIAICLILGILLAFILMFWLERFRVIIKSNAHKHDPSDKRQIWLEKYYLFVRQIYTYLVTHKVILTLIAVPVVFAISIPFIGMQTPASSHGKQTTQVSTGNWSKNAVAARLGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVYVFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFTIASVPSDDFIELFVAVRAGFTKRLAKKVSSKSLSDVSDINISDEKIEKNGDVGIEVMERHSLSQEDLVFESSAAKVSVLMDGPYGPVSNPYKDYSYLFLFAGGVGVSYILPIILDTIKKQSRTVHITFVWSARSSALLNIVHKSLCEAVRYTEMNINIFCHLTNSYPVEEVSSLNSQSARNYSLQYLNGRPDVNDYFKDFLHATGTQTAALASCGSDKLLRHLKSCVNTHSPSTVDLYQHYEEI Q09130 IF2G_SCHPO BINDING 33..38; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32481"; BINDING 170..173; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32481"; BINDING 205..207; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:P32481" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; Evidence={ECO:0000250|UniProtKB:P32481}; SPBC17G9.09; CHAIN 1..446; /note="Eukaryotic translation initiation factor 2 subunit gamma"; /id="PRO_0000137447" MAENLDISELSPIHPAIISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKCSNEECPRPGCYRSYSSNKEDHPPCEICNSPMNLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMQLKHIIILQNKVDLIRESAAEEHYQSILKFIKGTVAENSPIVPISAQLKYNIDAILEYIVKKIPIPVRDFTTAPRLIVIRSFDVNKPGAEVDDLKGGVAGGSILTGVLRLNDEIEIRPGIVTKDDDGRIRCQPIFSRIISLFAEHNDLKIAVPGGLIGVGTTVDPTLCRADRLVGQVLGSKGNLPEVYTELEINYFLLRRLLGVKSGDKNTTKVQKLAKNEVLMVNIGSTSTGGRVMMVKADMAKILLTAPACTEIGEKVALSRRIEKHWRLIGWAKVVEGKTLKV Q09171 ODPB_SCHPO BINDING 94; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with alpha subunit"; /evidence="ECO:0000250|UniProtKB:P11177"; BINDING 147; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P11177"; BINDING 195; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P11177"; BINDING 196; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P11177"; BINDING 198; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P11177"; BINDING 200; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /ligand_note="structural"; /evidence="ECO:0000250|UniProtKB:P11177" CATALYTIC ACTIVITY: Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; Evidence={ECO:0000269|PubMed:7828917}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P11177}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC30D10.13c; CHAIN ?..366; /note="Pyruvate dehydrogenase E1 component subunit beta, mitochondrial"; /id="PRO_0000020460" MIRLQKFGEIVGTSRSWKLLSSTIAKRYSSSSNGVKEMTVRDALNSAMEEEMKRDDRVFLIGEEVAQYNGAYKISRGLLDKFGPKRVIDTPITEMGFTGLATGAAFAGLRPICEFMTFNFSMQAIDHIVNSAARTLYMSGGIQACPIVFRGPNGPAAAVAAQHSQHFAPWYGSIPGLKVVSPYSAEDARGLLKAAIRDPNPVVVLENEILYGKTFPISKEALSEDFVLPFGLAKVERPGKDITIVGESISVVTALEAADKLKADYGVEAEVINLRSIRPLDINTIAASVKKTNRIVTVDQAYSQHGIGSEIAAQIMESDAFDYLDAPVERVSMADVPMPYSHPVEAASVPNADVVVAAAKKCLYIK Q09172 PP2C2_SCHPO BINDING 63; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 63; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 64; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 233; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 282; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; SPCC1223.11; CHAIN 1..370; /note="Protein phosphatase 2C homolog 2"; /id="PRO_0000057771" MGQTLSEPVLDKHSSSGGDRWLHFGVSHMQGWRISMEDAHCALLNFTDSNSSNPPTSFFGVFDGHGGDRVAKYCRQHLPDIIKSQPSFWKGNYDEALKSGFLAADNALMQDRDMQEDPSGCTATTALIVDHQVIYCANAGDSRTVLGRKGTAEPLSFDHKPNNDVEKARITAAGGFIDFGRVNGSLALSRAIGDFEYKKDSSLPPEKQIVTAFPDVVIHNIDPDDEFLILACDGIWDCKSSQQVVEFVRRGIVARQSLEVICENLMDRCIASNSESCGIGCDNMTICIVAFLHGRGLEDWYNWITQRVNSGEGPCAPPSYAELRGPNTIADARNLQLEYDHIASHEYGSGDTYDSDSDDETIAYDRYYLH Q09174 GMA12_SCHPO PTM: O-glycosylated. SPCC736.04c; CHAIN 1..375; /note="Alpha-1,2-galactosyltransferase"; /id="PRO_0000215163" MRFAPYLISAVVITTIILGGAWWTSAMDTKLQTKMKEIIDQHTSTWTPVVSSVTSTQTDTLRVTISEVVSVTATLTETFTATPTVTSVVHALATTDPHPDNSKIVILMGSNFQNDANSPLHPFAQSIIKNRREYAERHGYKFEFLDADAYASRVTGHLMPWVKVPMLQDTMKKYPDAEWIWWLDHDALVMNKDLNVVDHVLKHDRLNTILTREAEYKSGAGIPADGFRTPKDQDAKDVHFIISQDFNGINAGSLFIRNSEVGRWIVDLWFEPLYLDHIQGYAEQQAFSHMVFYHPQVYKHVGVVPLKAINAYDFDDNIWGYDDGDLCIHFAGCNYFKNCPEKFLKYAQILSSKQGSDWMSAQEKDHIQNLLKPSS Q09177 RPAC2_SCHPO SPAC1687.01; CHAIN 1..125; /note="DNA-directed RNA polymerases I and III subunit RPAC2"; /id="PRO_0000149318" MAAMTDVTDPSSVAMESATEKIIILPGHSADLTSVTFQIQKEDHTLGNSLRYVIMKNPEVEFCGYSIPHPSEAKMNFRIQTAPSTTAVDVLRKGLDDLIDLCDAVTEKFTEQLPRDTSTTMEVDG Q09179 GLNA_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; MOD_RES 273; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 303; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 305; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23H4.06; CHAIN 1..359; /note="Glutamine synthetase"; /id="PRO_0000153162" MSQYDVEPLLSKAAILNKYADLPQNGKVMAEYIWIDGFNHLRSKTMTLDAKPSSIDQLRVWNFDGSSTGQAPGNNSDTLLKPVAMYNDPFRRGDNILVLAACYTADGSPNGFNHRDACAKLLEKHADKETWFGIEQEYTMLDYYDRPFGWPKGGFPGPQGPFYCGVGTGRVFARDIVEAHYKACLYAGINISGINAEVMPSQWEYQVGPCAGIEMGDQLWMSRFLLHRIAEDFGVKISFHPKPILGDWNGAGCHTNVSTKDTRAEGGIKAIESYLEKFAKRHKEHIAVYGDDNDLRLTGRHETGSIDKFTYGVADRGASVRIPRSVAMNGCGYFEDRRPASSIDPYLVTGIITETMFEH Q09181 DHH1_SCHPO BINDING 88..95; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC776.09; CHAIN 1..485; /note="Putative ATP-dependent RNA helicase ste13"; /id="PRO_0000055066" MAESLIQKLENANLNDRESFKGQMKAQPVDMRPKTEDVTKTRGTEFEDYYLKRELLMGIFEAGFERPSPIQEESIPIALSGRDILARAKNGTGKTAAFVIPSLEKVDTKKSKIQTLILVPTRELALQTSQVCKTLGKHMNVKVMVTTGGTTLRDDIIRLNDTVHIVVGTPGRVLDLAGKGVADFSECTTFVMDEADKLLSPEFTPIIEQLLSYFPKNRQISLYSATFPLIVKNFMDKHLNKPYEINLMDELTLRGVTQYYAFVDESQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKITELGYSCFYSHAKMLQSHRNRVFHNFRNGVCRNLVCSDLLTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHRGLAISFISWADRFNLYRIENELGTEIQPIPPSIDPSLYVFPNGDYQIPRPLTASADQVLAAQQAKGQEGYHNRPNNNRGGHPRGGGNRGGYRQSNRQPRYRGQQKAD Q09188 ADT_SCHPO BINDING 100; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /evidence="ECO:0000250|UniProtKB:P02722"; BINDING 112; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /evidence="ECO:0000250|UniProtKB:P02722"; BINDING 257; /ligand="ADP"; /ligand_id="ChEBI:CHEBI:456216"; /evidence="ECO:0000250|UniProtKB:P02722" CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:8675018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000305|PubMed:8675018}; SPBC530.10c; CHAIN 1..322; /note="ADP,ATP carrier protein"; /id="PRO_0000090592" MATSSAAAAASTPVNANTITETKNSTFFFDFMMGGVSAAVSKTAAAPIERVKLLIQNQDEMIRAGRLSHRYKGIGECFKRTAAEEGVISLWRGNTANVLRYFPTQALNFAFKDKFKKMFGYKKERDGYAKWFAGNLASGGAAGAASLLFVYSLDYARTRLANDAKSAKKGGERQFNGLVDVYRKTYRSDGLRGLYRGFGPSVVGIVVYRGLYFGMYDTLKPVVLVGPLEGNFLASFLLGWAVTTGSGVASYPLDTIRRRMMMTSGEAVKYSSSFECGRQILAKEGARSFFKGAGANILRGVAGAGVLSIYDQVQLLMFGKKF Q09195 ERG24_SCHPO BINDING 317; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 321; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 344; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 349; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 356..357; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 396; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 400..404; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86"; BINDING 411; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:G4SW86" CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH; Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813, ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70; Evidence={ECO:0000250|UniProtKB:P32462}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18563; Evidence={ECO:0000250|UniProtKB:P32462}; SPBC16G5.18; CHAIN 1..424; /note="Delta(14)-sterol reductase erg24"; /id="PRO_0000207493" MAKGAVKKEKFEYEFFGPIGALGVTVLTTVVSFGSFYICNEEGCPAKFSKISHIFKKTPLFDQKSLILYLLWFSTLTLLWKCTNGKWAKGTPIDDKGTRLLYKINGFNSACLILGVVCTSIYLLGASCMEFIWDNFLQLMFAAYVFSVVLCTFCYVQSFFGKQQLAKGGTSGNILFDWFIGRSLNPRIGNFDIKCFCELRPGLILWVVFDIAFACHQYLVLGGRITDSMVLVIIFHTWYVLDSLINESAVLTTMDITTDGFGYMLSFGDLVWVPFLYSLQARYLAFHPVDLGLVKTLAILCLQFLGYYIFRGANGQKNRFRSNPNDPKLKHLKFIQTKRGTKLLTSGWWGMARHINYFGDWIMAWAWCLPAGFGSPIPYFYVAYFGVLLVHRNARDDHKCRVKYGEDWEKYCKAVKYRIIPYVY Q09330 MLO3_SCHPO SPBC1D7.04; CHAIN 1..199; /note="mRNA export protein mlo3"; /id="PRO_0000081634" MSMELDQSLDAIIASKPKGGIRKRRARSNKPKPTKNAKPAVNTASALKSVISEESKIIVSNLPTDVTEAQVKELFVKSIGPCKRVSLAYGPNGRSKGIATIIFSRPGDATRAYEQYEGRLVDGTRKMKVEIILDPSRQLNSLAARVSPASNASATASKNGAKSSKRKTTRRRRTPNRPKKSAEELDKEMDDYFGSNEKE Q09669 ADH4_SCHPO BINDING 82; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 114; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 141; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 142; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 181; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 182; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 190; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 192; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 203; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 225; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 237; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 241; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 306; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 310; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 320; /ligand="Fe(2+)"; /ligand_id="ChEBI:CHEBI:29033"; /evidence="ECO:0000250|UniProtKB:P0DJA2"; BINDING 320; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P0DJA2" CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:15040954, ECO:0000269|PubMed:16999687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737; Evidence={ECO:0000269|PubMed:16999687}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000305|PubMed:15040954, ECO:0000305|PubMed:16999687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10741; Evidence={ECO:0000305|PubMed:16999687}; CATALYTIC ACTIVITY: Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH; Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:15040954, ECO:0000269|PubMed:16999687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291; Evidence={ECO:0000269|PubMed:16999687}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25292; Evidence={ECO:0000269|PubMed:15040954}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC5H10.06c; CHAIN 30..422; /note="Alcohol dehydrogenase 4"; /id="PRO_0000087818" MSILRSPFRLIRSPARFFPSLFHSSCNQSFTNGLKHQSTSSKAMPVSAFYIPSFNLFGKGCLAEAAKQIKMSGFKNTLIVTDPGIIKVGLYDKVKALLEEQSITVHLYDGVQPNPTVGNVNQGLEIVKKENCDSMVSIGGGSAHDCAKGIALLATNGGKIADYEGVDKSSKPQLPLIAINTTAGTASEMTRFAIITEETRHIKMAIIDKHTMPILSVNDPETMYGLPPSLTAATGMDALTHAVEAYVSTAANPITDACAVKCIELVNKYLKRAVDNGKDEEARDNMAYAEFLGGMAFNNASLGYVHAMAHQLGGFYGIPHGVCNAVLLAHVQKFNSRDPRANARLGDIAFHLGCEEHTAEAALDRISQLVLEVKIRPHLVDLGVKEKDFDVLVDHAMKDACGATNPIQPTHDEVKAIFKSAM Q09675 HSP32_SCHPO ACT_SITE 141; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 142; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 175; /evidence="ECO:0000250|UniProtKB:Q04432" CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000269|PubMed:24758716}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 mM for methylglyoxal {ECO:0000269|PubMed:24758716}; Note=kcat is 58.0 min(-1) with methylglyoxal as substrate. {ECO:0000269|PubMed:24758716}; SPAC5H10.02c; CHAIN 1..240; /note="Glutathione-independent glyoxalase hsp3102"; /id="PRO_0000157854" MSIAKGKNALLVASSYYGPFYPDGKNTGVHFSELLIPYNVFKKAGFNVQFVSENGSYKFDDHSIEESKLGDFERKVFNDKNDDFWTNLNNMKKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKNPQSVEGKTVVYHKHVTAFNKAGEEKMGVMDELKKRGMKSLNEIFAEAGATFIDPPNPNVNFTQIDGKIVTGVNPQSAKSTAEAAVSAL Q09687 AGM1_SCHPO ACT_SITE 51; /note="Phosphoserine intermediate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2" BINDING 51; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /note="via phosphate group"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 267; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 269; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 271; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 360..362; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 486..490; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 495; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2" CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513, ChEBI:CHEBI:57776; EC=5.4.2.3; Evidence={ECO:0000250|UniProtKB:P38628}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9P4V2}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2}; MOD_RES 49; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13C5.05c; CHAIN 1..518; /note="Phosphoacetylglucosamine mutase 1"; /id="PRO_0000148017" MTKNKKYSYGTAGFRTKASDLEAAVYSSGVAAALRSMELKGKTIGVMITASHNPVEDNGVKIIDADGGMLAMEWEDKCTQLANAPSKAEFDFLIKQFLTPTTCQPKVIIGYDTRPSSPRLAELLKVCLDEMSASYIDYGYITTPQLHWLVRLINKSTAASFLEEGPPITEYYDTLTSAFSKIDPSMQDSPTVSRVVVDCANGVGSQPLKTVAGLVKDSLSIELVNTDVRASELLNNGCGADFVKTKQSPPLALEGKIKPNQLYASIDGDADRLIFYYINQNRKFHLLDGDKISTALVGYLNILVKKSGMPFSLGVVQTAYANGASTEYLQDLGITTVFTPTGVKHLHKAAKEFDIGVYFEANGHGTVLFSDKALANLAHPFFTPSPVQAAAIEQLQSYSVLINQAIGDAISDLLATISVLNALHWDASAWSNTYKDLPNKLAKVKVSDRTIYKSTDAERRLVSPDGLQEKIDALVAKYEKGRSFVRASGTEDVVRVYAEASTKQAADELCEKVCQLVL Q09694 LYS1_SCHPO ACT_SITE 77; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P38998"; ACT_SITE 96; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P38998" BINDING 18; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 77; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 101; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 130; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 131; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 135; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 203..204; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 227; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 231; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 251; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 278; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 279..281; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:P38998"; BINDING 319..322; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:P38998" CATALYTIC ACTIVITY: Reaction=H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH; Xref=Rhea:RHEA:12440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57951; EC=1.5.1.7; Evidence={ECO:0000250|UniProtKB:P38998}; MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC227.18; CHAIN 1..368; /note="Saccharopine dehydrogenase [NAD(+), L-lysine-forming]"; /id="PRO_0000199014" DISULFID 205..249; /evidence="ECO:0000250|UniProtKB:P38998" MVAPHLWLRAETKPLEERSALTPRTAKILADAGFQITIERSSQRAFKDKEFERLGFPMVPEGSWRHAPKDAYIIGLKELPENDNSPLKHTHIQFAHCYKNQEGWREVLSRFPAGNGLLYDLEFLQDDNGRRVAAFGYHAGFAGSAISCLVWAHQLLHPNKQFPAIRPFPNEKSLVRHVARQVRLALKKNNNQYPRILVIGALGRCGTGACDLASKIGIPFDNILRWDINETKKGGPFTEITESDIFVNCIYLSMPIPKFCTVESLNVPNRKLRVVCDVSCDTTNPNNPIPIYNVNTTFDHPTVEVKGVTTPPPLEVISIDHLPTLLPRESSEAFSEALIPSLLALKDVDNAPVWVRAKKLYETMVQKL Q09701 AKR1_SCHPO ACT_SITE 430; /note="S-palmitoyl cysteine intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; SPAC2F7.10; CHAIN 1..642; /note="Palmitoyltransferase akr1"; /id="PRO_0000212931" MGSLFLAASQGELDTVKNLISSEKIDVNATDEGGATALHWAALNQQIPICKFLLEHGADVNAIGGDLQAAPIHWAAKRGSVKTVHYLVQHGADPLLKDKQGFNCLHLAVHAASPLLVVYLLHLDISVDLRDDQQHTPLMWASYHGNEPITNCLLRWGADVLATDEDKMTPLHWSIVGGNLKCMKLILKEGGIPCTAVTANLSGQLKTPWALASELRVSHLFKQALISNGLKVKETSEEPEKWVVVPSKFQFSQKTFIIFCFLSSFIITGVFFFIMSICPMVISLIIAPLWIYFTFKYITTCIHANIDIVHFYLETPFLAGIFSSIFFWVWCHSLLYIVPKTLPIKPLSSLLFVLISFTCIGLYVRTAFQNPGYVDKIGAVVQRREEISKLLDKDLFNQSHYCLKCFQVKPPRSYHCGACKRCINRYDHHCPWTGNCVGARNHRTFLLFVFTLSTLIPIYFYVAFYYLQNIPIQKKYESYRCLFISGTICQWSLKDMFVLVASLTLFVNWCWVVVLAFTQICQVAHNVTTAEFRLFKRYGTLVPPTKQNSSPKNGHGIHGSFLRTVCGILGLDQCILLIRESNCFVRCFPSRAELGSQNSTSLSRNLSTVNPYDEGSIIKNCKTFWKQNFLNDGRQDEATRHV Q09715 TUP11_SCHPO SPAC18B11.10; CHAIN 1..614; /note="Transcriptional repressor tup11"; /id="PRO_0000051310" MASVEDATKVQEMLDALKAEYNALAHHSFASKARGNDYESSMIQSQIQEIEAFRKTVDDMYEKQKSIRETYEKDINKLKRELEELGVEANTASYRNRGERSELAASNNQVTHIDQEHPSQTKSTSQPPSNHLPAFQQIPPIHQSAYPQNNVAEVLMPPIPPSVEASSGQNFNQGIASQNPAISTSNLPSTTPLYIPPVNYGANQVSQQPNPQLPGVSNYYNPSATSKPAVNVQPPRIPTKATPSAEPSMTASANAGSISQAGPDGEYQGREQIAPVSDTEAARKTTSQSWYVTYNPACKRVFNINLVHTLEHPSVVCCVKFSNNGKYLATGCNQAANVFDVQTGKKLFTLHEESPDPSRDLYVRTIAFSPDGKYLVTGTEDRQIKLWDLSTQKVRYVFSGHEQDIYSLDFSHNGRFIVSGSGDRTARLWDVETGQCILKLEIENGVTAIAISPNDQFIAVGSLDQIIRVWSVSGTLVERLEGHKESVYSIAFSPDSSILLSGSLDKTIKVWELQATRSVGLSAIKPEGICKATYTGHTDFVLSVAVSPDSRWGLSGSKDRSMQFWDLQTGQSYLTCQGHKNSVISVCFSPDGRQFASGSGDLRARIWSIDPASP Q09717 RANG_SCHPO MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1773.07c; CHAIN 1..215; /note="Ran-specific GTPase-activating protein 1"; /id="PRO_0000213669" MSAEQEKKTQGTTKEEQKSSFASEDVASKQTEEAKAVFGDGVAKQENKSGASTNDEKKPAEGDEDAEPASPEVHFEPIVKLSAVETKTNEEEETVEFKMRAKLFRFDKAASEWKERGTGDARLLKHKETGKTRLVMRRDKTLKVCANHLLMPEMKLTPNVGSDRSWVWTVAADVSEGEPTAETFAIRFANSENANLFKENFEKYQEENAKILKKN Q09718 AP2M_SCHPO MOD_RES 145; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 152; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 157; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31A2.09c; CHAIN 1..446; /note="AP-2 complex subunit mu"; /id="PRO_0000193779" MISGLFIFNLKGDTLICKTFRHDLKKSVTEIFRVAILTNTDYRHPIVSIGSSTYIYTKHEDLYVVAITKGNPNVMIVLEFLESLIQDLTHYFGKLNENTVKDNVSFIFELLDEMIDYGIIQTTEPDALARSVSITAVKKKGNALSLKRSHSSQLAHTTSSEIPGSVPWRRAGIKYRKNSIYIDIVERMNLLISSTGNVLRSDVSGVVKMRAMLSGMPECQFGLNDKLDFKLKQSESKSKSNNSRNPSSVNGGFVILEDCQFHQCVRLPEFENEHRITFIPPDGEVELMSYRSHENINIPFRIVPIVEQLSKQKIIYRISIRADYPHKLSSSLNFRIPVPTNVVKANPRVNRGKAGYEPSENIINWKIPRFLGETELIFYAEVELSNTTNQQIWAKPPISLDFNILMFTSSGLHVQYLRVSEPSNSKYKSIKWVRYSTRAGTCEIRI Q09719 DBP10_SCHPO BINDING 113..120; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 638; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 733; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 736; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31A2.07c; CHAIN 1..848; /note="ATP-dependent RNA helicase dbp10"; /id="PRO_0000055041" MSGFQTSDEVDISNSLKAFPVDIATDNQKDKHENVGENVSDEDDGNYIASKLLESNRRTKGKKGNGKASNFQSMGLNQTLLRAIFKKGFKAPTPIQRKTIPLLLEGRDVVGMARTGSGKTAAFVIPMIEHLKSTLANSNTRALILSPNRELALQTVKVVKDFSKGTDLRSVAIVGGVSLEEQFSLLSGKPDIVVATPGRFLHLKVEMKLELSSIEYVVFDEADRLFEMGFAAQLTEILHALPTSRQTLLFSATLPRTLVDFAKAGLQDPVLVRLDVESKVSADLQSAFFSVKTAEREAALLCILQDIIKLPLKDNVRPREIGNVNNPKKRKRALELALKGSESGSPDSTLVFVPTKHHVEYVSELLVQAGYSVSKIYGSLDQEARLNEINNFRLGKTNLLVVTDVASRGIDIPLLANVINYDFPPQPKVFVHRVGRTARAGRTGWAYSLVRAEDAGYLLDLQLFLNRPLVTSSKQVKTDSDCDFTKQIVLGSLPQELVAELLEWVQRIVSRDVELQQLSNVAARGEKLYFRTRATCSAESAKRAKELVDSKGWSSNNPLFGDVSVIEAEEKYAELLSKVSSYRPSETVFEIGQRGHLKTEAAEIMRKRRNKVKPKGIKSEVASDKITDSSPGNMSEASESELEEVFKNPKELSKKKTTDFKDKEYYMSHYAPKESIQETGYAINSGENFTTAARHAILDLTNDEGIEQSRKGGQRWDPKKKKFVNIINDEDGSKGSPKIIRGESGVKLPATYRSGRFDEWKASKAFGANDSPIRENKRYKHNKLQTPKPADKFRDNYHKQNKRNREAKERGIGIKVNSELKSAVEIRKARELKEKRLAKNNRPSKKHR Q09722 EIF3M_SCHPO SPAC1751.03; CHAIN 1..402; /note="Eukaryotic translation initiation factor 3 subunit M"; /id="PRO_0000121006" MEGSDFILVVDSSVEEQVEELAMYLDNLEANTDKNVLALCREYLASENVKEVLNLFLTRLPLLAQAPEKELEPILAVFINLIQESAAFEDHVSKFCQALEQIADQNNNLTPAILSVLSILFNTAVKERQHARLSILTSVVTLTTRYSLFSTLAPNLKYFPDWLKEAGVSVSDHRAFNIFVSKAIQSYDDEQSFAFLLEAVKMDNSTADEAVRELVQRAVNSPKYFFFDDIVTLPPVQQLEQSTLQLLGILSGGMTDDYVSWVAENHAHCQHQKFDEDAIARKMKLLTIASLATQAPNNTLSYGDVAKSLKIDENEVELWIIDVIRAGLVEGRMSQLTKTLSIHRSSYRVFGKHEWVALHEKLAKWGSSLRYMLQVMEQPLSSFTIASSKKGNRDGSAVTASE Q09731 BU107_SCHPO MOD_RES 717; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31A2.14; CHAIN 1..962; /note="UBP9-binding protein bun107"; /id="PRO_0000051487" MSVRKRYKVTYVLDSCNDQLGHRLDANCLVLGRYFSEQGSAPVTRALYSGGRDGQLFGWDIGYDYGKASQPLAKIQAHSAWVNDIALTHDSEGVISCSSDSTVKLWKPHVLNASCLSTIGEHTDYVKRVSIPKYSKSPLVASGGLDKRIIVWDYNVGQEVMRFEQLPDCSLVVGPRSGVYSLAANNNIIANGGLQKDIQLWDCVSKKRITDLVGHTDNVRDILISDDGRTILTASSDATIKLWSLRAQKCLFSFIAHSDSVWALYSEHPDLKVFYAGDRSGLITRTDIRNQPNNQSCTAICKQDAPVSDIVARQSFIWSTSRDGSILRWKDEPLFNQDVGAALSKHTSSHLSVSSDCPSRHSSDIRNHSCPTLYHDDAEDIYYDLHHTESYSNINLTKTPDYVIHGGIGLLKYRMLGDRRHVLTEDAVGNKCLWDILACKQAGEFDKSEDFEKIVQSLDTVQAIPRWASVNCLLGILAVTLDENHYMDAEIYADECPLLKVDSPSDKRINLGVWILKNLFREFIDAELHRDLKFRQNLDVVRSEAKKQIEAQREEARKGNVNMPSALSPLRIRSRPSPLSLPPEPLLSPTIDYSATPFPLEPPPESPGPSLQIPSNNPVYTNLTDTDSMMGAPDYFSIPARQNRNRKPHTEVVGSPTVVRTKEIIPPKVTREGSFMGRLKKLGRSKSSKSLQTDFMKASVERAASSRVFSTGTSVTSPQALSKTNNTVNNAANTENNTLAKDKQQTSEASSPGTPRELKTTGELIEDLHEQYVHFKDKDTVLSLMKPPNDDTFPMLNLSSQITVIISEESPEAGNSRDIYRSTLENMADDIDLLENIMPFWLGRLLLLNEFPSKTAPTVNFTLQPFPGSGLPLIVNENTRLSASAMLRAQKIMDYSYSKLSQQRKDVSSLQFRCKDVVVTPKMTLATVKARIWRSGDDVVFHYDVAPRSVSEIVDKTQSLNI Q09733 GEF2_SCHPO MOD_RES 736; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 977; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31A2.16; CHAIN 1..1101; /note="Rho guanine nucleotide exchange factor gef2"; /id="PRO_0000080989" MDVGTMGSRAELLAISIQFGGLWVFRDLLQMNPLFEQDHVFCTFNHPNMGLVLISFAKVDGHILAAYALSKLGPDTFSICYPFSSKLDAFAQTLDLEWQIASMHKEAAACVYEFLCVESVCLHTGENWRESVIEPEYASYIFDTINVFQSSSLTRELYSLGEPNGVREFVVDAIFDIKVDNSWWEDPSNSYWKTVIGSREMFEDSRKKTSSPSPSFASSKDAGTIPAIQKKKSLLIEMMETESTYVERLRHLVNDYALPLRDLAKSSKKLLGLYELNTLFPPCLNKLIQLNSAFLDEFEAIMSDLNFEDIDEKKFEEIDLRLACCFESHFFAFSQHYPRYLEQSNDFGNVLKMASKIPKFVEFHDQVKLNANMNVGLSQLIMEPVQRIPRYSLFLDQIILLTQEGECQHTYVRSVEIIKNIAEMPTVDAEERSRIFAGLQHIIPDLAPNMISNSRNFIDCIDVTREFLKNGQLHLIPYTLILFNDRICLVQRRSKSSIASTILDLRKQNPRNSYSKEKRAQYIGSNMNEAVELTRSMVEENTIFLISKYASSPSFFNEYPILKFRCDFENVRTMDRFYQSFQKALSMNKSQPSCLSFSKLNDFVVFFNNYSRFEYEKESKRSDIVCICTNDANVDKHKFLQDGNIVITFFQQDEDFHLSFDSWLGVSLPTEAVIAKEDLREACLNYLINIKRLLLCPFSNRNFSSLDLYSNLIQHLLSANSSPRKSRLSFGGRPGSPSKISLSLNRFYNQGGLSKSCATLPSQMYNLDHNNISQKSLKFNTHNTSKASAEKTVEHLEAFKGGFKYHTDLKNLLYPLSEKEKIEGDELYDNILKETFNEELLSHYPPNIIYATFQKYLSSFINRKFGVLLSSSFIQQLNTVENLNLSFNSTDAVYHLKKILQDLPESSLKILENIFSIASDLLLRLPLKDQCDFVTKQLAIALAPSMFGSNAVELVYYLAYHSDRIFGTVEELPTPVSPANSNNDKQLDESKFQAIAMKEMPERHPKEILPGQIEREAYEDLRRKYHLTLARLAQMTRLNEDSKKSIPLLYDRFNHDLKLIKQSVQASLIRKQCELDTAKWTLEEYESKLNAKEGCQTNIFI Q09738 UBP8_SCHPO ACT_SITE 154; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 395; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" BINDING 8; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 10; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 38; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 41; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 51; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 54; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 59; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 64; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 74; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 87; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 90; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPAC13A11.04c; CHAIN 1..449; /note="Probable ubiquitin carboxyl-terminal hydrolase 8"; /id="PRO_0000080609" MPGDVEGCQHLKLKPADVENYQKICTQIFSCHFVPRRCSTCKRINKRSIRCLSCHSVGCLWGHHGEEHAMEHTHMIGVDVKNGHTYCFGCQDYVYQTELETLRFKIKNIKAWQSDHKRLPEKYNQMVCLEAYRKYPPVCATAGLRGIQNLGATCFMSVILQSILHNPLVRNLFFSGFHTSTDCKRPTCMTCAIDDMFSSIYNSKNKSTFYGPTAVLNLMWKLSKSLCGYSQQDGHEFFVYLLDQMHTESGGGTSMPCTCPIHRIFSGSLKNVVTCLDCKKERVAVDPLMDISLDINEPTLQGCLERFVSKEKVQYSCHSCGSKNAIKQLVFDKLPPTICMQLKRFEQNNFAMSTKIDKQVSYPAFLRMRYNFNQDDVDYQLYSVVCHKGTLDTGHYIAYTYYQNQWFLLDDTTIVEVKESEVLNSQAYLLFYHERQILYSDEMTVKTEN Q09739 MCP7_SCHPO SPAC13A11.03; CHAIN 1..210; /note="Meiotic coiled-coil protein 7"; /id="PRO_0000096293" MPPKGLSLAEKRRRLEAIFHDSKDFFQLKEVEKLGSKKQIVLQTVKDVLQSLVDDNIVKTEKIGTSNYYWSFPSDAKRSRESVLGSLQAQLDDLKQKSKTLDENISFEKSKRDNEGTENDANQYTLELLHAKESELKLLKTQLSNLNHCNPETFELKNENTKKYMEAANLWTDQIHTLIAFCRDMGADTNQIREYCSIPEDLDDLQLPIL Q09746 BZZ1_SCHPO SPBC12C2.05c; CHAIN 1..642; /note="Protein BZZ1"; /id="PRO_0000116505" MSLETYKFSDELHDDFKVVDSWINNGAKWLEDIQLYYKERSSIEKEYAQKLASLSNKYGEKKSRKSSALSVGDTPAMSAGSLECASLTTWSKILDELTRSSKTHQKLSDDYSLDIAEKLKKLESHIEALRKVYDDLYKKFSSEKETLLNSVKRAKVSYHEACDDLESARQKNDKYREQKTQRNLKLSESDMLDKKNKYLLRMLVYNAHKQKFYNETLPTLLNHMQVLNEYRVSNLNEIWCNSFSIEKSLHDTLSQRTVEIQSEIAKNEPVLDSAMFGRHNSKNWALPADLHFEPSPIWHDTDALVVDGSCKNYLRNLLVHSKNDLGKQKGELVSLDSQLEGLRVDDPNSANQSFESKKASINLEGKELMVKARIEDLEVRINKITSVANNLEEGGRFHDFKHVSFKLPTSCSYCREIIWGLSKRGCVCKNCGFKCHARCELLVPANCKNGEPEVADDDAVDTSVTATDDFDASASSSNAYESYRNTYTDDMDSSSIYQTSLSNVKTEETTPAEPASKVDGVVLYDFTGEHEGVITASEGQEFTLLEPDDGSGWVRVKIDGTDGLIPASYVKLNDELNTSVTLDGDSSYVKALYAYTAQSDMELSIQEGDIIQVTNRNAGNGWSEGILNGVTGQFPANYVTDV Q09747 DBP5_SCHPO BINDING 160..167; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC12C2.06; STRAND 142..144; /evidence="ECO:0007829|PDB:3FHO"; STRAND 156..159; /evidence="ECO:0007829|PDB:3FHO"; STRAND 187..190; /evidence="ECO:0007829|PDB:3FHO"; STRAND 232..236; /evidence="ECO:0007829|PDB:3FHO"; STRAND 257..260; /evidence="ECO:0007829|PDB:3FHO"; STRAND 288..294; /evidence="ECO:0007829|PDB:3FHO"; STRAND 312..314; /evidence="ECO:0007829|PDB:3FHO"; STRAND 329..335; /evidence="ECO:0007829|PDB:3FHO"; STRAND 355..358; /evidence="ECO:0007829|PDB:3FHO"; STRAND 400..402; /evidence="ECO:0007829|PDB:3FHO"; STRAND 423..425; /evidence="ECO:0007829|PDB:3FHO"; STRAND 457..463; /evidence="ECO:0007829|PDB:3FHO"; STRAND 467..470; /evidence="ECO:0007829|PDB:3FHO" HELIX 145..149; /evidence="ECO:0007829|PDB:3FHO"; HELIX 167..177; /evidence="ECO:0007829|PDB:3FHO"; HELIX 194..207; /evidence="ECO:0007829|PDB:3FHO"; HELIX 238..246; /evidence="ECO:0007829|PDB:3FHO"; HELIX 263..266; /evidence="ECO:0007829|PDB:3FHO"; HELIX 273..282; /evidence="ECO:0007829|PDB:3FHO"; HELIX 299..307; /evidence="ECO:0007829|PDB:3FHO"; HELIX 337..347; /evidence="ECO:0007829|PDB:3FHO"; HELIX 367..372; /evidence="ECO:0007829|PDB:3FHO"; HELIX 392..394; /evidence="ECO:0007829|PDB:3FHO"; HELIX 396..399; /evidence="ECO:0007829|PDB:3FHO"; HELIX 440..444; /evidence="ECO:0007829|PDB:3FHO"; HELIX 471..477; /evidence="ECO:0007829|PDB:3FHO" TURN 362..366; /evidence="ECO:0007829|PDB:3FHO"; TURN 373..376; /evidence="ECO:0007829|PDB:3FHO"; TURN 464..466; /evidence="ECO:0007829|PDB:3FHO" CHAIN 1..503; /note="ATP-dependent RNA helicase dbp5"; /id="PRO_0000055020" MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQSENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGTVMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEELSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRVGTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQRPITRVPTDDYEELEKVVKNALKM Q09750 PST1_SCHPO MOD_RES 442; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 446; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1443; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC12C2.10c; CHAIN 1..1522; /note="Paired amphipathic helix protein pst1"; /id="PRO_0000121541" MAKDWQDARLGQCHRLEDYSNVAINYTGPYLTPSGTMAYHPGNAPLFTQAPPHTNPQGPPPFPLFNSISPVYDPATGRLLYRNVNTQVSHTAIPNPANGYAAVYGGPPSQLPPPPQPQSHPNVTVISASPARAIEQQPTILSSTDSNIPRPGTVKSSASPFVPNQNPSAPPPPPQEYRQLNVTDALSYLDLVKLQFHQEPEIYNEFLDIMKEFKSQAIETPEVITRVSKLFAGYPNLIQGFNTFLPPGYSIEISSADPGSLAGIHITTPQGPLMINDLGKTTAPPPPHGSTTPLPAAASYTSMNMKQSSASHPVLQPPAPSTLQFNPSPSPAAPSYPPVDASVKQAADLDQAINFVNNVKNRFSHKPEAYNSFLDILKSYQHDQRPIQLVYFQVSQLFAEAPDLLEEFKRFLPDVSVNAPAETQDKSTVVPQESATATPKRSPSATPTSALPPIGKFAPPTTAKAQPAPEKRRGEPAVQTRNHSKRTRTATSSVEETTPRAFNVPIAQNKNPSELEFLEHARQYLANESKYNEFIKLLELYSQEVFDKNALVERCYVFFGSNEHLMNWLKDLVKYNPANPIPVPRPRVDLTQCKSCGPSYRLLPKIELLLPCSGRDDLCWTILNDAWVSFPTLASEDSGFIAHRKNQFEENLHKLEEERYEYDRHIGANMRFIELLQIHADKMLKMSEVEKANWTLPSNLGGKSVSIYHKVIKKVYGKEHAQQIIENLQKNPSVTIPIVLERLKKKDREWRSLQNHWNELWHDIEEKNFYRSLDHQGVSFKSVDKKSTTPKFLISELRNLAQQQKVELSEGKVTPSHQFLFSYKDPNIITDIARLFGVFLIHGSTHSAEDNEKMSNFLRSFLSLFFDVPYDSFIPYLPTHFNEEESDIDSLSSSLIEKPRASSSPIHHANNNGLRLLKDVLKKTYRGARENRSSVKEDYVSESTERTPDASEIDEHISEHEENDDESSSVFSTGEVWVNCKFTDTDGSLLDDGTKLSDRSVYNLFGNMSLYCFFRLFHTLYSRLEEIKNLEQMAYSKQHDVKSNPVAVELGLVRHPSERLGFALPTADTVYEQAIQLCERLMEGEIDQNGFEDALRCLYGIHAFRLYTVEKLVTSIIKQLHSVTTNRRLAQVFMYYEKDRVQRRTSPRQQIMYRIQTETAFGPDENLCCIDWNSQTRQSAIRLMGREDLTMGTLKSDAEKWCYYIGSYIMSSPTEGILPEHVRIPFLRKCLPSDEGNEDDESSSVVKSANAIITSFLESGLALTIPINTVKIRYENGTEDVFARNSEQVYNGPYDKIRDYRQSKWREWLNSDEGWTQGLSKDKVRRIKPCTIESLFNESTLRSGKAERFSENAGVESIGKKGKNLLNESGNGKKLDKGLPPKVNGKSSVTRGNKTNLKARNGRNNDDSSNKINLSEKEKEKESIEDEEKNREGSMSPVAKHASDVEDDHDVAKSTAPDFETSSHRPERSSEKKSPSPVFTSVKQTAENDADNEDDKTDMDDQTEETLDADNTMEEEPSKDDL Q09752 FNX1_SCHPO SPBC12C2.13c; CHAIN 1..531; /note="Multidrug resistance protein fnx1"; /id="PRO_0000173421" MVDQVNLATEQTSLLYPEVSRKKEELSVNKWTILPALWVGGFLSALDMTIVASLYPVIGSEFKLMNNASYIVTAYLITNTAFQPLYGRLSDIFGRRPTVVFANAAFTLGTFWCGISRSLPELCMARALAGIGGGGLGTMSSIISSDIVSLRERGTWQGITNIVWGIGGSLGGPLGGLIAQRWGWRTAFHFQVPMGILSTILVAWRVRVKPTVRNSNASLLSRIDYLGSFLLVTGITALVVTFNMGGDAFPWVSPVIITLLVSSVLILFAFYWVEKNIAVEPIAPVEILSQPTPLNVCLGNFFNAFCSFVIVYELPLFFETTLLMPSSEAGVRIFPYVISTSVGSLCSGLYMKKTGRYRNLVIAGFFFMLMGIVSFAVLTSFGHRTPLILISLCLAMTGCSYGMNLTSTLIAIISSLAPEEQAVATGLSYLFRATGSVIGISLSQTTTLSILMKQLASNLKDDPDKDDLIRRLRESISIIPNLPKDIQKLVIKSYATAFTWTFALVAIIAFAGFWCSLRIKQFYLHTSVDRS Q09757 RS9A_SCHPO MOD_RES 50; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 164; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 179; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24H6.07; CHAIN 2..191; /note="Small ribosomal subunit protein uS4A"; /id="PRO_0000132701" MPSAPRKQSKTYKVPRRPFESARLDAELKLAGEYGLRNKHEIWRVALTLSKIRRAARELLTLDEKDPKRLFEGNAIIRRLVRLGILDETRMKLDYVLALRIEDFLERRLQTQVFKLGLAKSIHHARVLIFQRHIRVGKQIVNVPSFVVRLDTQKHIDFALSSPYGGGRPGRCKRKRLRSQEGGEGEEAEEE Q09760 CUL3_SCHPO PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}. SPAC24H6.03; CHAIN 1..785; /note="Cullin-3"; /id="PRO_0000119809" MQRSAKLKIRAPRKFSANQVDFATHWEVLQRAIGDIFQKSTSQLSFEELYRNAYILVLHKYGEKLYNHVQDVIRSRLKEETVPAIYKNYDASLLGNALLDIRKNDSYSTSWSRSLEAAHRFLSSLVNSWKDHIVSMQMISSVLKYLDKVYSKSADKVPVNENGIYIFREVVLLNSFEIGEKCVETILILVYLERKGNTINRPLINDCLDMLNSLPSENKKETLYDVLFAPKFLSYTRNFYEIESSTVIGVFGVVEYLKKAEKRFEEEKERSKNYLFTKIASPLLSVVEDELLSKHLDDLLENQSTGFFSMIDSSNFEGLQLVYESFSRVELGVKSLKKYLAKYVAHHGKLINETTSQALEGKMAVGRLSSNATMATLWVQKVLALWDRLNTIISTTMDADRSILNSLSDAFVTFVDGYTRAPEYISLFIDDNLKKDARKAIEGSIEATLQNSVTLFRFISEKDVFEKYYKTHLAKRLLNNRSISSDAELGMISRLKQEAGNVFTQKLEGMFNDMNLSQELLQEYKHNSALQSAKPALDLNVSILASTFWPIDLSPHKIKCNFPKVLLAQIDQFTDFYLSKHTGRKLLWYPSMGSADVRVNFKDRKYDLNVSTIASVILLLFQDLKENQCLIFEEILEKTNIEVGDLKRNLQSLACAKYKILLKDPKGREVNAGDKFYFNENFVSNLARIKISTVAQTRVEDDSERKRTLEKVDESRKHQADACIVRVMKDRKVCEHNQLMAEVTRQLNPRFHPSPMMIKRRIEALIEREYLQRQADNGRIYEYLA Q09761 SLD3_SCHPO PTM: Phosphorylated. {ECO:0000269|PubMed:12006645}. SPAC24H6.06; STRAND 631..633; /evidence="ECO:0007829|PDB:6HM3" CHAIN 1..699; /note="DNA replication regulator sld3"; /id="PRO_0000071953" MNNDHASKKSFCIKAPSNWEKSYLEVWPLVTVPRQCICLRWCISKEYHEFTCSSLQFIVIRPAGTSVLLGRVKSSKANQLVGIEHVEGSRYALIFLSEKLDFKSLKVIANHQLTKSSKSLSNVSNKPLGDQLFRSNSLMSPSLLKKELHRIQSDASQANERESQAPHSFVTHDLISSSKDGNSLTHEFANDSVTEMVQDYTPSCSRDVKSLLDHLYNSYFYQLLMTKTPVVFYVKQMVGKTRQLAVEVHNHVEEKALVDELLKFLDNLKSVDDRKSRLLQCFESHLNYKAWHLEFENEAHQYEIKGYRLWLQNILNRENCQITKLDFEREFSQLKLKEYEIRVLLYFEILYLFLKWDPEYARRRANDNSLLDSRDSGKRKSRKKNAKTLNPFETAQLKLEFTFDGLCIRRTIEQNATERSEDLLLKFCKETIVPYYSSKFPRITRNLLEKCNGLDLLPERSHKHRHSAPPRSKLISSKSEAGRALPGNTSGASISNTSSPHSEASISKDYEILKRRRSNSGVHSLTRSDSSFNGFERDTRRRSSDIARIKNREINLPSSSLSKQRNSMHDISTNFPRRNLSFTEKLTMASLQGQSEESVQPKTTSSLSRSKTLSILEGSVSKRSEPSMDSILVQATPRKSSSVITELPDTPIKMNSLDKASACTVENHIVTESPAHKSNKAQLFVCVPTTPVKKKSASP Q09764 VSB1_SCHPO SPAC24H6.11c; CHAIN 1..958; /note="Vacuolar basic amino acid transporter vsb1"; /id="PRO_0000116397" MPTHSLNQKRSLLYPSIDNGSVPDSSFLSQSFRDTNDIHLLSARLASVEVDPETLPSNSPETNDDVSNYDYMSISSYQRAHSLASTSRNDFNYRPSEINETRPLLPEREEHSSQLPPAQNQVLPFQSLNAPSKKLRGRISLSKIYQFFFDDKGPILFILNIPAVIIGLLLNILDALSYGLILFPISDPLFKNLGADGLAIYYVSCVVSQLVYSLGGSFFKGSVGSEMIEVIPFFHQIAFTILNRVGEDNPKSVIATTILAYCLSSILTGLVFFILGILRLGRLIEFFPRHILLGCIGGVGSFLVLTAVEVSSRLEGSVSFNWASLSALFQPMTFAKWSIPLFLSSALEFAQQRWPHPFLIPSFFVIAPAIFYVLVWAIPGMSLEYLRETGWVFSSTETNVPWYHFYSLFSLRDTDWSALLATVPEMCALTFFGILHVPINVPALAISLGLDFVDTDKELIAHGVSNTLSGAVGSIQNYMTYTNSLMFIRSGGNNRLAGIMLALATVALLVIGPGIIAYIPVWTVGCLIYLLGIELLKESLWDPIGITTKIEYFTICAIVFTMTVVDFVVGIVIGIIMACVFFVIQASSRSALRGIYSGGIVRSTVRRPMNQQRFLNEIGRQIQVCKLSGFLFFGTINGVEKNIAGLIEELNVSNNPLRFLIIDFSLVNGADFSVVQAFLRIRRMLATMNVQLCVCGLDETRSSFKTLTTMCFGGDDNCGCQVFEDVNSSLEYCENMLLDDYDVYRTKLLHKAGYSHTLAVPGKHKQNISMAETFSPSPRHDLLRQVAMSSVKAETKELSKFEKYAKYEQPFPLLMQVFGEITTKREDFWLGLCPFFKKAFLRKGDLLWRKGDTPSKLVILETGMVKASYQMDRESLSENITCLCVVGELPFFSKTCYNATVVAELDSAVWILDREGWETMLKSSDKAEVIENEMLYLTLKMTRDKFNVFTNFALNLYR Q09765 UBA3_SCHPO ACT_SITE 205; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10132" BINDING 54..78; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.; EC=6.2.1.64; SPAC24H6.12c; CHAIN 1..444; /note="NEDD8-activating enzyme E1 catalytic subunit"; /id="PRO_0000194949" MPSSDVCKAGSHRHSGWIQSLKKPGPFNLDAPENPEETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQDKTIEFYKEFKLIICGLDSVEARRWINSTLVAIAKTGDLIPLVDGGSEGLKGQARVIIPTITSCYECSLDMLTPKISYPICTLANTPRLPEHCVEWAYLLEWPRVFLNASVDSFSKQEVFEPLDGKNSNFEPDNIRHIDWLVKRSIERANKFQIPSSSINRFFVQGIVKRIIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVGEDGAYTYTFNLEKRSDCPVCGVLSEVYDISASSTVTLKDILNHYSKSYNLQNPSVSTAAGTPLYLASPPALQVATSKNLSQPILSITSVDVNLVITDKNLSTSLSVQLREC Q09768 GSH1_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000305|PubMed:8619315}; SPAC22F3.10c; CHAIN 1..669; /note="Glutamate--cysteine ligase"; /id="PRO_0000192571" MGLLVLGTPLDWPESKKYCDYVRENGIMQFLHMYDTYISKKQDVLLWGDEIECIVVSMDDKSKKARVSLRQEDILNALGKYEETFRHVDFGPVYAALRNETCPKKIDAILSEVAKNPADYVERIGGNSNKDTIEITSSTKPHAQNAVPTFHPEYGRYMLESTPGAPYGSTLKDFTFVEYNMRLRRKIIENHLLPNELPLTITNFFRLGTPGFTDPEVEANGAISRSFFLPDDVINTHVRFPTLTANIRQRRGRKVAMNVPIFFDKNTIKPFHDPTVPWDRNLFPEDANARDGAALDNHIYMDSMGFGMGCCCLQITFQAKSCDEARLLYDQLTPITPLMLALSAGTPAFRGYLADQDCRWNVIAGAVDDRTEEEMKTVPKSRYDSVDLYISNDKRNLPEYNDVPVVINQDCYDKLIKDCIDERLAKHMAHIFSRDPLVIFSDSILQDNSVSNAHFENLNSTNWQSMRFKPPPPGSDIGWRVEFRSMEIQITDFENAAYSIFVVMLSRAILSFNLNLYMPISLVDENMKAAHARDAIHRKKFWFRCNPFPDASTDDESGQFRQLTIDELFNGEHRENGFPGLITIVRSYLYSCNPDAKTICLIERYIRLISQRANGQCLTAASWIRNFITTHPSYKQDSVVNDEINYDLIRRIAKIVDGDYDDTLLGKCS Q09769 LONM_SCHPO ACT_SITE 946; /evidence="ECO:0000255|HAMAP-Rule:MF_03120"; ACT_SITE 989; /evidence="ECO:0000255|HAMAP-Rule:MF_03120" BINDING 578..585; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03120" CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03120}; TRANSIT 1..36; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03120" SPAC22F3.06c; CHAIN 37..1067; /note="Lon protease homolog, mitochondrial"; /id="PRO_0000026732" MITRLSGACLRRSGAKRNWPREHLVHRSLLASFSTTQRVLKCSVGPFRTSNVVFKSKEPKDNKPLDNKNDPKKTHNEDESHTNESLPSTDKKKKKDNDDFKQNLKSSSNKTEEKYSATQASKSKNDEFELGGEENEDEMPLNGEFNKNVPAKYSVPDVYPQLLALPIARRPLFPGFYKAIVTKNPSVSEAIKELIKKRQPYIGAFLLKDENTDTDVITNIDQVYPVGVFAQITSIFPAKSGSEPALTAVLYPHRRIRITELIPPKEDADSAASSDAAELETDKSSNLSSNGEVKSDLKQDNGKEEPEKEVESTPSILQNFKVSLVNVENVPNEPFKRQDPVIKAVTSEIMNVFKDIANVSPLFREQIANFSISQTSGNVFDEPAKLADFAAAVSAADHRELQEVLEATNIGDRLQKALYVLKKELLNAQLQHKINKEIEQKITQRHKEYLLTEQLKQIKRELGQELDSKEALVTEFKKRTESLSMPDHVKKVFNDELSKFQHLEPMAAEFNITRNYLDWITQLPWGKRSVENFDLDHAKEVLDRDHYGLKDVKDRVLELVAVGKLRGTMQGKIMCLVGPPGVGKTSVGKSIASALNREFFRFSVGGLTDVAEIKGHRRTYIGAMPGKIVQALKKVQTENPLILIDEIDKVGKSHQGDPASALLELLDSEQNSAFLDYYMDIPLDVSSVLFVCTANTIDTIPPPLLDRMEVIELSGYVSAEKVNIAKGYLIPQAKAACGLKDANVNISDDAIKGLISYYAHESGVRNLKKSIEKIFRKTSFSIVKEIDDELNSKEKSTGKSGKKTSPQSSEDAANKEASSVPLKVPDKVNIEIEEKDLTKYLGPPIYTSQRLYDTTPPGVVMGLGWTPMGGVSMYVETIVKNILSSNSTPSLERTGQLGDVMKESSEISYSFSKSFLSKHFPNNKFFEHARLHMHCPEGSISKDGPSAGITMATSLLSLALDTPVPATTAMTGELTLTGKILRIGGLREKTVAAKLSGMKEILFPKSNLADWEQLPDYVKEGLTGVPVAWYDDVFKRVFSNIDAEKCNNLWPNLIKSSSKQHQISPSH Q09770 AGM2_SCHPO ACT_SITE 77; /note="Phosphoserine intermediate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2" BINDING 77; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /note="via phosphate group"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 292; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 294; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 296; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 385..387; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 510..514; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2"; BINDING 519; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9P4V2" CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513, ChEBI:CHEBI:57776; EC=5.4.2.3; Evidence={ECO:0000250|UniProtKB:P38628}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9P4V2}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2}; MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1296.01c; CHAIN 1..542; /note="Phosphoacetylglucosamine mutase 2"; /id="PRO_0000148018" MSDAEDSDSIVNEFVTAIVRESDKFAKVHSYPMQYGTGGYRADAELLSSVAFRTGVIASFLSAKLHGQPVGLMVTASHNASSENGLKIVNILSSLDSSKWEAYLDQVVNADSADELTVCLTSILKKAKIIPGSEARVFVGYDSRSTSEILAQAVIDGIVVCKAKYENFGLLTTPQLHYMVKASQTYGTPDAIGEPTERGYFEKLSKAYQSLMTGKKIKGTVLIDAANGVGAAKIKELAKYIDPKLFPIEIVNDNIDNPELLNNSCGADFVRTQQKPPNGISAPKHARCASFDGDADRIVYFAFGSHSFHLLDGDKICALFAQFLIDLIRSTGLDLQVGIVQTAYANGASTAFFQKTLKVPVLCVSPGLKHLYHAAQAYDVGVFFEANGHGTILVSHAALSKIISHEVLSPAQFNALKTLKTVFELINQTDGDAITNLLLVEVILAHKNCTLKEWNQLYSEIPSRLIRCEVEDRSIYTTTDAEQKLVTPEGLQEKIDALVAKYTGGRAFVRSSGTEDAVRVYAEASSRGESEDLALRIVELLH Q09775 ROK1_SCHPO BINDING 90..97; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC22F3.08c; CHAIN 1..481; /note="ATP-dependent RNA helicase rok1"; /id="PRO_0000055085" MDALKLLTTNVKFKNKVPQPSIKEKEAKKLQGITKGKAKVTGNNPVDPIEEFPEGILCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTGLSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNICKSLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFVGSDTSKIVILRQMISNGELKPRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFFTKEDGEYIKLIAGVMRSSGCEVPNWVMALPKPSKEMKKKLKKSPPKRKRITTRASYDRQKEQRKKEYIKKVKKEASIKKHNEATGDSGQ Q09777 RGS1_SCHPO SPAC22F3.12c; CHAIN 1..481; /note="Regulator of G-protein signaling 1"; /id="PRO_0000204242" MPALHNPSSPPPSYEAVTSYRNGNSIDSGDKRQQCSRLMKITSNGRPYSKDFLELFSTMVISTNFSRNRYRFSYVENSCTLLQLLSTLENLQLSQVNRIKSRCGSKVLKSTTKFTIPKTAAKCLCNTFLNARLLQIVNNPSARKFSNEKCLLQLTRKGYSVVSEFLQHNGHNSQAELYASKWNHSAPVIVSISRFSSTDQILKDSSFCEMLLVRMLGSVHEIGKSKNPLLVPVYSVSSPSPKDSLSKVTKYQMFGIDIAEWLMCNTMLLDWSEMETVASDLLIHSYIAYENNSETPLKFSYAKGVSYFLTGKGIATLGWTKNVSNNKLINKINEVEKGSTNKEILETILRKPNLQTYFFEFLKKNFCDENQRFYSEVCEFNDYFSHANETNDHEAIRESFAHACGIYNCFLSSNAPNAVNLPSDLYEKITNHMALAMEVEPLNEWLQLIHILLLEAQTAVLDLMAGDSLLKFLELNGGLGI Q09778 TSC1_SCHPO SPAC22F3.13; STRAND 63..65; /evidence="ECO:0007829|PDB:4KK0" HELIX 2..14; /evidence="ECO:0007829|PDB:4KK0"; HELIX 26..38; /evidence="ECO:0007829|PDB:4KK0"; HELIX 44..60; /evidence="ECO:0007829|PDB:4KK0"; HELIX 66..79; /evidence="ECO:0007829|PDB:4KK0"; HELIX 80..82; /evidence="ECO:0007829|PDB:4KK0"; HELIX 87..96; /evidence="ECO:0007829|PDB:4KK0"; HELIX 98..103; /evidence="ECO:0007829|PDB:4KK0"; HELIX 109..123; /evidence="ECO:0007829|PDB:4KK0"; HELIX 135..154; /evidence="ECO:0007829|PDB:4KK0"; HELIX 165..185; /evidence="ECO:0007829|PDB:4KK0"; HELIX 187..198; /evidence="ECO:0007829|PDB:4KK0"; HELIX 201..203; /evidence="ECO:0007829|PDB:4KK0"; HELIX 204..216; /evidence="ECO:0007829|PDB:4KK0"; HELIX 222..228; /evidence="ECO:0007829|PDB:4KK0"; HELIX 230..240; /evidence="ECO:0007829|PDB:4KK0"; HELIX 244..258; /evidence="ECO:0007829|PDB:4KK0"; HELIX 269..280; /evidence="ECO:0007829|PDB:4KK0"; HELIX 332..334; /evidence="ECO:0007829|PDB:4KK0"; HELIX 339..349; /evidence="ECO:0007829|PDB:4KK0"; HELIX 351..357; /evidence="ECO:0007829|PDB:4KK0"; HELIX 361..366; /evidence="ECO:0007829|PDB:4KK0"; HELIX 378..389; /evidence="ECO:0007829|PDB:4KK0"; HELIX 396..399; /evidence="ECO:0007829|PDB:4KK0"; HELIX 403..407; /evidence="ECO:0007829|PDB:4KK0"; HELIX 412..427; /evidence="ECO:0007829|PDB:4KK0" TURN 128..131; /evidence="ECO:0007829|PDB:4KK0"; TURN 259..261; /evidence="ECO:0007829|PDB:4KK0"; TURN 264..268; /evidence="ECO:0007829|PDB:4KK0"; TURN 284..286; /evidence="ECO:0007829|PDB:4KK0"; TURN 367..369; /evidence="ECO:0007829|PDB:4KK0" CHAIN 1..899; /note="Tuberous sclerosis 1 protein homolog"; /id="PRO_0000065653" MPLQSLVKALWNVLHEEESEGYPDLTELIAEVESYQQRYPKQNPTNSQKIRHILDEIYEKTPFNNTRRRILWLAVLKTVIPLLILDRQAVGEWWDQIFFPFLNSPTQLKPVFSDLKSILFYILIFHDEDEWGGDLRRECAEETITRLVDLYVSKAIENLGDVESQEQRNQTIECLVNVLVHYGIQRPKELSSCFCHHFLNPPTRIPILSVMVEVIRRQGPRLYEIPQTGFYDLVLKCAEFDTSPILLSYALSFILMILSHICNSLDDSLYRLFCIYLRFSMIDPTSGFPSSTASGNWEVFHDFMSTYASTTTSQTDSSYNDVHDIVGSSQPDYLESLDYSQLFSILYALYPINFLEFLRDPKLYASKHNFQIRYSFNQELLSTKSDGLLGRHLAHSNFLKYTAETELTDKSRWTRLDSIAVVALCNSLNAVGIAESVMDPFGGKLPTTYEETSSATGLLAYPNESHDIASEPFSISWPQNPSISGSVHSATTFDKAQLSNTEDSYDNISHGTSYSEGVSSIHMVKGERGSNNLELTSESLSSTNDTIRRLQRDLLFLQNELRFEKFVRQQHLQNIGKLHREHILDMAVESERQKLLLTNKRYKAQIELLNSEIDKHRSESQAALNRRVKWENDFNNKIKALREEKKAWKSEESELKSSIESLISQLESIRNSQIDIAFSKNQLELKLQLYETKLKEYEQHLSCVNISKKQVSSSSDTSFGNTKMDSSMILSNSEAVSDEQERELIESEKHRMKLESENLHLQANIELLKKDLEAINVVYEAKIFDLEKRLSSEANAPELHNPVNLNYDAQLSKISEIKENYDELLTRYRELEGKFLESQAEVEELKNFQKPLVDTGSSIHSSPGLQQSKFIIRNDSLHPKVGPPRRQSTDTSRSTFRQY Q09780 ERG12_SCHPO ACT_SITE 195; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q03426" BINDING 12; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17256"; BINDING 130; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17256"; BINDING 135..141; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P17256"; BINDING 141; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P17256"; BINDING 184; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P17256" CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+); Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.1.36; Evidence={ECO:0000250|UniProtKB:P07277}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17066; Evidence={ECO:0000250|UniProtKB:P07277}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P17256}; SPAC13G6.11c; CHAIN 1..404; /note="Mevalonate kinase"; /id="PRO_0000156661" MSKSLIVSSPGKTILFGEHAVVYGATALAAAVSLRSYCKLQTTNNNEIVIVMSDIGTERRWNLQSLPWQHVTVENVQHPASSPNLDLLQGLGELLKNEENGLIHSAMLCTLYLFTSLSSPSQGCTLTISSQVPLGAGLGSSATISVVVATSLLLAFGNIEPPSSNSLQNNKALALIEAWSFLGECCIHGTPSGIDNAVATNGGLIAFRKATAHQSAMKEFLKPKDTLSVMITDTKQPKSTKKLVQGVFELKERLPTVIDSIIDAIDGISKSAVLALTSESDKNSSAKKLGEFIVLNQKLLECLGVSHYSIDRVLQATKSIGWTKLTGAGGGGCTITLLTPECKEEEFKLCKESLLAHKNSIYDVQLGGPGVSVVTDSDSFFPQYESDFDFKKLNLLSKFNKYYI Q09785 GCSP_SCHPO CATALYTIC ACTIVITY: Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304, Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099, ChEBI:CHEBI:83143; EC=1.4.4.2; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; TRANSIT 1..49; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 783; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC13G6.06c; CHAIN 50..1031; /note="Putative glycine dehydrogenase (decarboxylating), mitochondrial"; /id="PRO_0000010751" MFDSFMKRNQLALIMFRACSKLQYHGVNTSLSRHLFLAKRNLSISSACLEAKNSQKFPALDTFEPRHIGPSKTDQQYQLESLGYKDFDSFLKDVIPDSVRTPESQLMAFGSVNPNEKNPPVNYSESEFTTLANNVANQNKLIKSFIGMGYYNVKLPAAIQRNVLENPEWYTQYTPYQAEISQGRLESMMNYQTMIADLTGLSISNASLLDEGTAAGEAMVMLMANDKKKRKTFLVDKNIYPNTLSVLRTRASGFGIKIELDNITPELITKSAKHVFGIFVQYPAADGSIFDYGHLAATARSFNMHVVAATDLLALTILKSPGEWGADVAVGSTQRFGLPMGYGGPHAGFFACSEEFKRKIPGRLIGLSKDRLENPAYRLALQTREQHIRREKATSNICTAQALLANMSAFYAIYHGPNGLQEIANRIYASTSFLKSALESSGYKIVNKSHFFDTLTIEVESADKVLAKALDHGYNLRKVDDSHVGLSLDETVCDKDIQALFSIFNINKSVDQYYMEIATSEPNGNSASTVDNLSICSLPENFRRTTLYLQHPVFNRYHSETELMRYIHHLQSKDLSLAHAMTPLGSCTMKLNAVTEMMPITNPLFANIHPYVPEEQAKGYRHVIEDLQLMLTTITGFDAACFQPNSGAAGEYTGLSVIRAYQRSIGQGHRNICLIPVSAHGTNPASAAMAGFTVIPVKCLNNGYLDMQDLKEKASKHADKLAAFMVTYPSTFGIFEPDVKEALEVIHEHGGQVYFDGANMNAMVGLCKAGDIGADVCHLNLHKTFCIPHGGGGPGVGPICVKKHLADFLPSHPVVSCGGKNGITSVSSSPFGSAGILPISWAYMRMMGLAGLRDASKAALLNANYMAKRLSSHYKLVYTNKNNLCAHEFILDAREFKATAGVDATDIAKRLQDYSFHAPTLSWPIANTLMIEPTESESMYEMDRFCDALISIRQEIREIEEGLQPKDNNLLVNAPHPQKDIASEKWDRPYTRERAVYPVPLLKERKFWPSVARLDDAYGDKNLFCTCSPVV Q09793 NUP45_SCHPO MOD_RES 289; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 290; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22G7.09c; CHAIN 1..425; /note="Nucleoporin nup45"; /id="PRO_0000204863" MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPGLNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTTGGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNANTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISSRILDVFKTPGATYPFASNDPLMNYFEQFTENAKKRTDLYAATIGELEQHLEQVETTPQNNSPEALLKTIKEEHKLFMALSNRFAQVHDEVKRLQVNTSTSLPFIS Q09798 PAN2_SCHPO BINDING 863; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03182"; BINDING 865; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03182"; BINDING 972; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03182"; BINDING 1025; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03182" CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182}; SPAC22G7.04; CHAIN 1..1088; /note="PAN2-PAN3 deadenylation complex catalytic subunit pan2"; /id="PRO_0000116406" MDAWKEITKTTENDGVSTCSLSSIAFDPYSELVWTGHKNGQIKSSFGPSLTSYTQFIGHEGPVHQVLPQERGVFSLSSKSLRLSNRKGTIRWRYQDSDCIDYRAMFYQSRNNPEVVIGGYHQKLTVVNAERGISIHKDKNVSDIFIMRRNRLLCCGSTNGEIILRDPNSFQPVNKVVAHTGTISDIDTSGNLLLSCGYSLRHGTYMLDPFVKVWDLRNLSSLVPIPFPAGPTIIRMHPKLSTTAVVCSCSGQFHIVDTGNPLDAKLMQIPLTSYLTGMDIASTGDAMVFTDVEDNIHLWSPLENPSFSDLKLPIQLPNTSTETVQLENNDPLNSIGLPYYKDELLSSWSKYLIFDVGKPILDSNLLIAKQISENSHPVPQEIKSFHRNQIIEVPWLNRKLISEGATPKFHSERQKDIMSGNDIEGSASYFEEIEDTISGPDSIPKFYQRPVIKYSKFGIEDFDFGFYNKTKYAGLETDITNSYCNSVLQLLSYVPSFSKAAISHSLGPCDLMECLLCELGFLFAMLKESTGRNCQATNFLRAFSNSSFAQSLGIVFDDYSDGTFPDSFVIQKFTKFMLTEISRIADYEDKKDGTSFPVSFLLKSFCIPEMQTYRCGICGITSQKIKSSLYIIDLHYPSQQLESILSFEWLFKMSLDRRVDLPPGWCEYCLAHQPFLLRSFIRSLPDCLFINTQVKHHEHWKLWARKNWLPKKLHLRRVNDTMQCVSQKISNLDKDQQSLSVYVLRGIIYEIRQNGEEPHFVSTIRVSDNTSSDNPDDNRWYIFNDFLVKEVTEEEALTVHGPWKIPIIVYYEKLDTKIPQWDEVSDYTLLYQPYSLNKNPPINKIQPLTTDEMLYPKMLVGIDSEFVALQQEETEVRSDGTKSTIKPSKLSLARVSVLRGEGPNKGLPFIDDYVATDDKVTDYLTEYSGIHPGDLDPDRSPYNVVPLKVAYKKLRLLVNAGCIFVGHGLQKDFRIINLLVPPEQVVDTVDLFFLSSRQRKLSLKFLAWYLLDEEIQLTEHDSIEDALTALKLYDCYDKLKSQGKLEETLDNIYEVGRRFKFRPPSVASMSLEDRNSYGDESVISNQTN Q09805 VPS45_SCHPO SPAC2G11.03c; CHAIN 1..558; /note="Vacuolar protein sorting-associated protein 45"; /id="PRO_0000206317" MDLVSASQSYFKRIFQEVSDLKILLLEEDTTKIVSSCITQSNLLEQQIYLTVLLGNKREKLRHLKCVAFLRPTPTTLRLLCEELRDPKYAEYHLYFTNVIPKSFLERLAESDDFEAVKSIQEFFLDYLVVNNDLASFNIPHIIEDSPDNWQDGAFHRTHQGIISLLLSLKKKPVIRYDNNSLLCLKLAEEVSYTIQHESQLFNFRKPDTAPILLLLDRKNDPITPLLTQWTYQAMVHELFGIDNGRVSFSNSTSDNEKSTEIVLNPTLDPFYKETRFDNFGDLGVKIKDYVSHLQTKSTKKASEIESIADMKQFLEAYPEYRRLSGNVSKHVSLVSEISQVVQRENLLEVGEVEQSLVCNEPQSTDFNDIQRLLFSNISENTKLRLAALYSLRFERIDPAKVSALQQMLIAGGVNPLKVSVIPTLLHVAGYSFRQGDVFPPSNLFSRARSGLKGLRGVENVYIQHNPFLKSILLDLIQGRLKETTHPFLNSETRAQTSNEKPQDIIVVIVGGATYEEAHFVSEFNATQPGVRIILAGTTILNSTAYIDDIMYMSTRIK Q09810 UBA4_SCHPO ACT_SITE 198; /note="Glycyl thioester intermediate; for adenylyltransferase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; ACT_SITE 358; /note="Cysteine persulfide intermediate; for sulfurtransferase activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049" BINDING 53; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 74; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 81..85; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 98; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 142..143; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 183; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 186; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 261; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049"; BINDING 264; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03049" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; SPAC2G11.10c; CHAIN 1..401; /note="Adenylyltransferase and sulfurtransferase uba4"; /id="PRO_0000120581" MNPQEKIICSSNGLELSLDEYSRYGRQMLLSEIGLPGQLSLKRSSVLVIGAGGLGCPAMQYLVAAGIGTLGIMDGDVVDKSNLHRQIIHSTSKQGMHKAISAKQFLEDLNPNVIINTYLEFASASNLFSIIEQYDVVLDCTDNQYTRYLISDTCVLLGRPLVSASALKLEGQLCIYNYCNGPCYRCMFPNPTPVVASCAKSGILGPVVGTMGTMQALETVKLILHINGIKKDQFDPYMLLFHAFKVPQWKHIRIRPRQQSCKACGPNKMLSREFMESSPKEYTTICDYVPTLSKQLAPIRRISALDLKNLIETSPHITFLDVREPVQFGICRLPLFKNIPLSEVDSLQNLSGKVCVICRSGNTSQTAVRKLQELNPQADIFDVVAGLKGWSTEVDPNFPLY Q09818 YAC4_SCHPO SPAC16C9.04c; CHAIN 1..489; /note="Putative general negative regulator of transcription C16C9.04c"; /id="PRO_0000081682" MLKTQEIYSSEDEDDMCCPLCMEEIDISDKNFKPCQCGYRVCRFCWHHIKEDLNGRCPACRRLYTEENVQWRPVTAEEWKMDLHRKNERKKREKERKEVELSNRKHLANIRVVQKNLAYVNGLSPKVANEENINVLKGPEYFGQYGKIIKIAINKKAAANSANGHVGVYITYQRKEDAARAIAAIDGSVSDGRHLRASYGTTKYCTSYLRNQQCPNPSCMYLHEPGDEVDSYTKEDLASLQHTRPLSTKPNVVNGATHSPSPSLPFKTPLLPVTKTPLEEANSSPAAQNQHITTVDHVHPQVSMTPSLSTNNTATSVPAPYSSAASVNVVPGHATTILHHEESSALPPTAAWAKLSPSVLQERLRAAVNQQPLDALKSSSTQTSIPKIQKLKAAKLPSEEENTTKWLNKAINDLVSSLSKINFSTEGTEFDKKQIEMIQNLPPLFVFNARSVIDKEVVPEQEKSAENQPPTSLGINNGNPVMPPPGFQS Q09831 PPK14_SCHPO ACT_SITE 320; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 201..209; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 224; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 379; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 381; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 385; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4G8.05; CHAIN 1..566; /note="Serine/threonine-protein kinase ppk14"; /id="PRO_0000086043" MNELHDGESSEEGRINVEDHLEEAKKDDTGHWKHSGTAKPSKFRAFIRLHFKDSRKFAFSRKKEKELTSEDSDAANQSPSGAPESQTEEESDRKIDGTGSSAEGGDGSGTDSISVIKKSFFKSGRKKKDVPKSRNVSRSNGADTSVQREKLKDIFSPHGKEKELAHIKKTVATRARTYSSNSIKICDVEVGPSSFEKVFLLGKGDVGRVYLVREKKSGKFYAMKVLSKQEMIKRNKSKRAFAEQHILATSNHPFIVTLYHSFQSDEYLYLCMEYCMGGEFFRALQRRPGRCLSENEAKFYIAEVTAALEYLHLMGFIYRDLKPENILLHESGHIMLSDFDLSKQSNSAGAPTVIQARNAPSAQNAYALDTKSCIADFRTNSFVGTEEYIAPEVIKGCGHTSAVDWWTLGILFYEMLYATTPFKGKNRNMTFSNILHKDVIFPEYADAPSISSLCKNLIRKLLVKDENDRLGSQAGAADVKLHPFFKNVQWALLRHTEPPIIPKLAPIDEKGNPNISHLKESKSLDITHSPQNTQTVEVPLSNLSGADHGDDPFESFNSVTVHHEWD Q09845 GPD2_SCHPO ACT_SITE 236; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 31..36; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 123; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 146; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 146; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 179; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 300..301; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 300; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 329; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23D3.04c; CHAIN 1..373; /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 2"; /id="PRO_0000138096" MTVAALNKLSALSGSIQKSFSPKLISVGIIGSGNWGTAIAKICGENAKAHPDIFHPQVHMWMYEEKIQHEGKECNLTEVFNTTHENVKYLKGIKCPSNVFANPDIRDVGSRSDILVWVLPHQFVVRICNQLKGCLKKDAVAISCIKGVSVTKDRVRLFSDIIEENTGMYCGVLSGANIASEVAQEKFCETTIGYLPNSSVNPRYTPKTIQALFNRPYFRVNIVEDVPGVALGGALKNIVAVAAGIIDGLELGDNTKSAVMRIGLLEMQKFGRMFFDCKPLTMSEESCGIADLITTCLGGRNHKCAVAFVKTGKPMHVVEQELLDGQKLQGAATAKEVYEFLDNQNKVSEFPLFTAVYRIVYEGLPPNKLLEAI Q09847 NU146_SCHPO MOD_RES 899; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 946; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1041; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1043; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1044; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23D3.06c; CHAIN 1..1325; /note="Nucleoporin nup146"; /id="PRO_0000116418" MNAENTFSILNTNEPNAGGSQVTESEIEEEDIEFLSFAALKIGATSSLSNSSLGLPEYSNLFAINNLKSLFVAGVPNYLIIGSTLDLQKSLIDADENVDANVLKDSASIRHVSLPDAKFSMVSFSSNGEFVIAYDFVSFELSVYETDALLKNSATSIYKAVFPDLVQVLPNPEINNLVILRNLKLEVFLLSLSKFQVESPLAKDATCAAWSRRGKQCVIGFNNGTMSQYTPAGEIKLRIPRPPSLENYFVECISWIENREFVVFYSPLTSLSNESDEPPHESECFVISVGMNGHFNFGKAGDPTPPFGAVNRRDHHYIASLHAWKPDLRSLVVVANTASADLGVLALSMEKNQWSILNIVDETKRASLPYSNKKDSDSSPTALVMDFTATDRISKPLDPTEAPADCSPLPIVWVFNDEFQLVAYRIFYADAISKSIDYPEMNVIKDKNKDSTVRASNNENIPTPDKQASPFVKNLSSTSSPFSQSSAFGNFKFGQATSFDKGLSTDASSGAKSNTPVFGQPSTFGQAPVFGQPSAFGQAPVFGQPSAFGQSSFSFGTSNMNQKLDFGTFKSPLSGAATGEAKTNLEKAVTSASGKASFTGFAPSQSTTSGLNFDSIPKDNEAASIFGSSQVSTKNTSGFQFSNNTLLADNVDEDIESDHDTKIEELANSDVEPSTEQNIGGDVSWGASTFQSKPQPSFSFGLTLDDKSNTPGKNFSIFGKTAETQVEQKKPENNVLTKPFSFAPSDKSMFAANIPSAGEGLDQQKTSKALPSTGITKLSENDNEKAEESNETKGFNTTIAKQNDKSSKSEGKASVANMSALNKSTNNETSDSKPSLKSPLFNFSADAPTFTFNKPSETPPFSFNKPLVEKESKQDVSDTSDRSPFSFKAFGIDSKKSPTPEPTEMAESNISEESEGWKLIEQPNVESEIEDQDEESSDLNGKRRSTPPKIHEVGVNKMLDVVPKEKRDLNSFFPKQPLVVQSTDKNKKEPQESLEDEILSAEGFSEVEAANKISRFEPFSSPKLKLATSDNAPEKYVFEESESSDLEEGPVPLRNLESLADLPEAESNEKLPMVNTFERLYLQFKNELDLVWQNINIIAEYIEGQTSTPSAVSEQATMAMLSQNTEELEDLLDTVTSFSAFCSDYSKQIDYLEACLVRINAKRIQVTRLLKALTNPAFEKQMELRQLGPEALRRQKELRLKMEKVLKSLSTLEQQAVDARMSDTRRFKKPTLGSIEVAYSRIATLLGQRLKQLYKLEKDIKRMATKKKMITKKSMSSDMMTQFRALGISQSSTKQVSAHYLREFERQDAFRNGVFKRLTSLKKAD Q09856 PRP3_SCHPO SPAC29E6.02; CHAIN 1..542; /note="U4/U5/U6 small nuclear ribonucleoprotein prp3"; /id="PRO_0000116420" MDRNKRRLESSQLRESSSPNSQNKPNAMEEIKRRRLQLEQRLAQQAQVPWEKRSENGNNAGMETIQNRISELKEKTAKRFNANIPKSEGLFRDDSNGAKGGLKVGIHPVLLDGNIQNTILTPENRKRTASFSTKGVSLSQHQLLKPPAITEQNPFLDTAPTPRLEDSPFYDPRTKESRKTRGSRNLHLNESGKFIEEANQARRQARLEDLKKRIALHSHKAGIEDELDITSKSIGRDTIPNIEWWDLPFIKDYNDYGDENNWLIDGPQSIINSAIQHPIPVLPPYAKNQPSSHSVFLTKKEQKKIRRQTRAEARKEKQDRQLLGIEPPEPPKVKLSNLMHVLGDDAIKDPTKIEAEVRKQVEERRLRHERENEERKLTPEERKEKAFRKKDEDSAAGLRCLVFRIKYLAHRPHRLKIDLNAKQWGATGVCILNANFNLVIFEAGQKAIKKLKRLMLERIDWTDTSRNSIIAQGNKLVDTEGRELNYTENTCNLVWEGEIGRRAFRYWSFRSCPSENDAKSYLEEQGGAEHFWMLAKSWSENV Q09857 USO1_SCHPO SPAC29E6.03c; CHAIN 1..1067; /note="Intracellular protein transport protein uso1"; /id="PRO_0000116421" MDIFHKSYNVILSPPKVQQADETISKLCDRLEHATLFEDRKAAALGIKSFAREFKELVAAHGLKGIIQSLHRDYDDPELLKVTLETCLILTRHDDDSRASDTGLWIADQFILNQDNIQCLLQSISHKDFYVRLYSVELFSAILSCRPTELKDCLQTFPSAISSIMVPLRDSIEPVRNADLYFLSELVKDCTSIQKLVVFENAFETLFSLLENEGGVDGGIIALEALKFLNVLLKDNISNQNYFRESNHIPSLLKLLSVDTFVDGTWDTSRVQCVIEALYALQSLVPIGLSSSIANQNAVVSNHGIDVLLTLATHPDLLFFDVQKISWITLAHVVYSNARAQNSFVDSTFFDIKNTDVLTCLFDYLFLSSISPSHRYSVAFFLRSLTSENDELSSKFLKQIIHAYTHKQDNRLNIIQGYLDLVHLSDQDQYDNWFTSTILTYLVIDNDQRKYLLCSIPLFQDMDNDEDSESEDKVTFIQCVSTKLIATLRHENALQNCVGYLTLLIALVYGNPDSVKDFLSESSILQTFLTALMDESSSANSVIQGMIAVFLSLVYYYCPIESPVSKSDVYNAITSAVKRDVFINRLQRLRRMNLYEITFLSMKQKMHAIDDAADAFNTKIGEINTLDAFDEAQKQLKSLREEIDNTKEALDLSVKERSIQEEKLNESLKTSKTNLEEQTQLAEKYHEELLDNQQKLYDLRIELDYTKSNCKQMEEEMQVLREGHESEIKDFIEEHSKLTKQLDDIKNQFGIISSKNRDLLSELEKSKSLNNSLAALESKNKKLENDLNLLTEKLNKKNADTESFKNTIREAELSKKALNDNLGNKENIISDLKNKLSEESTRLQELQSQLNQDKNQIETLNERISAAADELSSMESINKNQANELKLAKQKCSNLQEKINFGNKLAKEHTEKISSLEKDLEAATKTASTLSKELKTVKSENDSLKSVSNDDQNKEKSVNNEKFKEVSQALAEANEKLNARDEEIERLKVDIIGLQNASLNMQSLKDSDNRTISDLESKNKELEKKLKEADEYWLLIVEELESKRTKDKELLRQCGQAVSEDEQSEEE Q09858 NNF1_SCHPO SPAC29E6.04; HELIX 4..21; /evidence="ECO:0007829|PDB:5WWL"; HELIX 25..30; /evidence="ECO:0007829|PDB:5WWL"; HELIX 38..66; /evidence="ECO:0007829|PDB:5WWL"; HELIX 69..88; /evidence="ECO:0007829|PDB:5WWL"; HELIX 107..140; /evidence="ECO:0007829|PDB:5WWL" CHAIN 1..205; /note="Kinetochore protein nnf1"; /id="PRO_0000116422" MTSRKEQLDAFLSRTLSETIAHIPLEKFAQCFPSMKKGKVIAVIHQQLIEFFEKSCKQEYANLIKERDLNKKLDMLDECIHDAEFRKLHGESEVDISNKQPQEILKAHLYSHKRELLDKLNQDLLDIDKENEGLSTQIAAEEKATEDCISRMQSLIQKLEKTVYGMNEKNLAKEAHDTLNDLLPYIQNPSSTWTNALNEQGNIER Q09859 MSRA_SCHPO CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120, ChEBI:CHEBI:50058; EC=1.8.4.11; CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, ChEBI:CHEBI:58772; EC=1.8.4.11; SPAC29E6.05c; CHAIN 1..170; /note="Probable peptide methionine sulfoxide reductase"; /id="PRO_0000138631" MQIAIIAAGCFWGVQEVYLRKFIPAAAILKTSVGYTGGITADPTYKEVCTNTTNHAEALKIEFDEKLTSYDKIIEFFFAMHDPTTSNQQGNDIGTQYRSAIFTTNPEQATIAKRVMNEVQAKHYPNKKIVTQILPAGKWWDAEDYHQLYLEKNPDGYRCSSHFLRWNVFE Q09869 TAF9_SCHPO MOD_RES 159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12G12.05c; CHAIN 1..163; /note="Transcription initiation factor TFIID subunit 9"; /id="PRO_0000118895" MSSPGISDESIKGPKDVRLIHLILSSLGVPSYSQTVPLQLLTFAHRYTQQLIQDSQVYAEHSRGQNAPISVEDVRLAVASQINHSFTGPPPKEFLLELAMERNRKPLPQIQPSYGFRLPPEKYCLTQPNWIVSNETQQNQPKEENSSDSRMEEDKLDFSVKSE Q09904 NU124_SCHPO MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 380; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 465; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 546; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC30D11.04c; CHAIN 1..1159; /note="Nucleoporin nup124"; /id="PRO_0000204837" MPPVSKNTRTSSKTVKKPYDPPQGSSRPFFTVLKRAFSSVLHPFTSGLDEKASGTASKDRKSGRAGTKSLLTPELTPHYLGKSPRIIRVSNRSHVRTIDGIEEKVHTNTFEPRKPKQKQDYTNSPTLFKRHDELSLKSLNSLHPSSALSKKLGSTSQHQIATPKSSASLLNILRSLHDEQKNTLNISSVKQDRITEANPTCEKRKPSRSPSPMLSKKKSVARASENEPSAKQNKSFSGNDSHKSLTDIRDKENGETEVSAKNHVPHRSSRRRRRHQRLIPIIYETLEQMDLRKPVLVNAEVQTDSNPGNTMFIDKQDIYHRLSTPTSRKRQTLEKGHIKAFSAVDEDLDEIFACEDDVHYTALPKQNPKSERILEPIIASPKDNTSDKGLLTKSAPTFEELQASITPKPVKTSPNDTALTLANAEDNKTFEHQPLSKDTEAPKSQFSSSPTKESTTRKSEVEPPSPSKEIKSSHFSVPEFKFEPKTEATTDKKLNVPKFEFKPTATADVQTNRLKENEPKPTFFAQLPSKTQETPSITENKPSFFSQLSPKREETEKKDNAPSAPASTSGFSFGGFAPKTLEEKEETKAPTFNFSLNNASSTQDTTKPTLQFNFGSSFGKPTSNIFNDKKTSENGLASSTVASESKPSAPESKPSSGFGNTAGSSPFSFNLTKESKEVPPTNSFSFAKKGKDEANDSLSAKASTPFSFAKPNTENVTTTAPQFSFNFTKPNTDAKTNLLPEKTFNEEAVKQKETEKEVPPTGPKASEIKDSVSSNNAVPSSTFNFVSPFAAVSEKTNENNIPNDTTKTNGNATKRTLEQTEDAKPFAFSFGSTTEQANKKASTSNETTKPQLDTSSKTDGVTANAPFSFASAFNAPKPSTNTADGKDSASNLTTPSPAFSFGNNSGVKASSNNNPSTNSSTAPFSFGTSNKPAFSFGSATSKTTSEGTAPAASASAPAPTTSAFSFGASNSSMNKEENTPMAKDAGDTAPASGFKSGFSFGANNSPQPASMFGTSTPAPSSAFAFGNQSGTNPAAPAGFGGITNTATNNPPSTGFTFTPSNAGSTAAPMFGAGNTPNPSGSINNASQAFAFGSGEPSNPASNPPSTGFSFGAATPSAFNASASQSPAPNGIQFNLGSSNSQTNAPPGRKIAVPRSRRKR Q09908 PHF2_SCHPO SPAC30D11.08c; CHAIN 1..538; /note="SWM histone demethylase complex subunit phf2"; /id="PRO_0000116437" MPNSSYYDDDGGSFEAASYPFQFDGSRRFPNDLHPTMFEGEESNQNGGSVLIDQAFQDIQNPNVNSNMHLENQFQHFHEPNKESGAFGSYKNDDVAKEIESSKNQETDAKSEQAPFTEDASSSNYAHHRSADSQTKSALPPNVPASSSPLPPMSIAMNIARKRSWPASLAIERDNTADALFSTEDGREEQFNLEGVKTKSGRKVHRPNHFDPLVKLPTRRRGPGRRPVVALAMKCSVCQRLQSPPKNRIVFCDGCNTPFHQLCHEPYISDELLDSPNGEWFCDDCIRRKKQAPLVTGTTARELNLSSEEKKSYLLSLPISQLVDILLFCEQLHPDIPFYSPKTSTIVQELQSKRSAFTATMNEPVTGDQYLSLNNGTESQSKTTKHSTSLPSTEPVEVDKQYMESEKIPTIDEYLQEYSNEDEIVLQVLESFPAAVSFSTITNTIQAKYSNRKIKNSNITRSLNRLVRKNRVLRDARGSSYELNRTFDADRPSVRPDISITGPIPIDWMLYTPHTEDLTENFCTYYMFDETPIVLSSI Q09909 CWF19_SCHPO SPAC30D11.09; CHAIN 1..639; /note="Pre-mRNA-splicing factor cwf19"; /id="PRO_0000079614" MEKEKLTNRTSTHKFNETDRETNHSRRHRHHHSRHRESKHGRHDRSERPSSREAGDRSRHERFSKEPLEVKKLPVENEYFDSKFASASSMPSSKDNPQNNDFTNSLQGLDFGTFGSRIQREPIDRKSNKPGEIFVGATLQNESSTSTEHKDIEQLETEINESGINYKIGDNGSRWRMMKLKRVFDMAQDQRRPVEEVALERYGSLKEFDFALEERDELELRKRTRKVQKEVPTGELYEKRCADEFKTRKDSGNGATYYKVIPDPSVNKDTPTESDLNRLKADLLRAQLKKDPNYESLEREYQKACDDFENSLHPSENSNSQATIPSKKRNFDDPTIDEMVQEEKLLNKQRKYGQNYEYAKQIAKDKTYSNNLDYLDENAGKLSNRMKRGDVSLAQISSGGDLKKINHVLDTCPLCLNYETQPLAPVISLSHRAYVSLPTQPELAKYHCLIVPTGHRINTLSCDEDEWDEIRNFMKCIALMFDSMNLGVIFYENAPSPQRYMHTAIECIPVSKRILSLAPAYFREALSTSDEEWSQHRKIIDTLEGSKKYGKWAFRKMMVKELGYFHVWFSIDGGYGHVVEDEKAWGRHDQVPRQVFASMLNLPPEVIRRKGSWTGKKDPREDMFRSRFEKFDWTKGLID Q09915 SPT6_SCHPO MOD_RES 137; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 454; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F7.01c; CHAIN 1..1365; /note="Transcription elongation factor spt6"; /id="PRO_0000116440" MSENEVVGSPTTNGDKNEDGYPAENGEGTNVDDNNNEEEKDGIPLDNDNDENDSSEESATDEEAERQVREGFIVEDEEDEVPQEIRRKKKRKKHAESTADQDMLDEEDLELVMENTGQGSRFSKLRRLKRGRDQEETLENIFSEEEEEEENEVDDEAPNRTQGHRAGVIDEFADFIEQDEFEDEERQEEKYETGPPIESVRPEALGISDDDYIQIYEVFGDGTDYAFALEDEDAEDELEESVSLKTIFEPSELKDKMLTEEDEIIRITDEPERMQLYMKRNIDCSEDEFREQVAWIIDYLLKNRRDIDAELYEPFQTAVRYVVHFFIRDSLEVPFIWQHRRDYIVHNNRERNTITPLLSQNDLWNIFFLCTKFWSLHSKKQDILKLYSDLGINDDLVVPFCEAASSLDAIDDLNDYIHFTYSEQIRDRALLMGTGLRRPQGSKYSFFEKFRKSSLYNLVKEFGMSAKDFSFNVAQGARLRFVEDNTLSPEELSRTYVTNELSSPEQVLQKARRVLAEEIIHDPQFRKSFRDKLYNAGVVTVLATQKGVRKIGSEHPYYEFKYLKRKPLGSFELEPILFLKMLKAEEEGLIQLSIEFEDPDDVFKGLLELFVSDNFSENAMQWNAQRELVLKEVFKRFSALAPDAIRETLRSRYLDELGMRCRNQLFSRLDQAPYEPSTKNFDRGTIPSVLAVSNGKGESSDAIICVFVDDVGEPTDSLKLADLRDLANQAMFAEFVEKVKPDVIGVSGMSVSAHKIRQHVQDSLTSHEPVDLIMVNDEVARLYQNSTRAVDEFPTLPTISCYCVALARYVQNPLFEYAAMGRDLMSLSFDPWQHLLPPDVLWKYLETALVDISSLVGIDINEAVTNKYEANILPYIAGLGPRKADYVLKKIAATGGRIDNRSDLISKQIMSRKVFINCSSFFIIPNDEYPNMDILDSTRIHNEDYELARKMASDALELDEEDIEELETNRGVVYHLLEENETGKLDELVLEEYADQLEREFHQKKRNTLEKIRLELKDPYGEQRNVFHKLTPSEIFLMLTGENPEELQADAIVPVNVRRVTNRFVAVKLDCGIDGNIKADEVSDDFIPPPQLLQVGQTVEGVIISLDEANFMVDLSLRNSVLQSANSKRQTSSHRTSYWDTEAEKRDTERMQAETQAEQRVARVIKHPLFKDLNASQAEAYLSKMQVGDLVIRPSSKGSDHIVVTWKVAEGSYQHIDVLELEKENEFTIGQKLLVKGRFEKMTYQYSDLDELIVLHIKAIAKKIDEMCIHDKFRKGTQAETEKWLESYSEANPKRSCYAFCFDHQHPGYFILCFKASVNSPVTAWPVKVIPNAFFLQGNVYGDMTALCNGFKLLYAARTKNFRRM Q09916 HAS1_SCHPO BINDING 133..140; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F7.02c; STRAND 129..131; /evidence="ECO:0007829|PDB:8EUY"; STRAND 164..167; /evidence="ECO:0007829|PDB:8EUY"; STRAND 188..190; /evidence="ECO:0007829|PDB:8EUP"; STRAND 192..194; /evidence="ECO:0007829|PDB:8EUY"; STRAND 213..217; /evidence="ECO:0007829|PDB:8EUY"; STRAND 239..242; /evidence="ECO:0007829|PDB:8EUY"; STRAND 270..274; /evidence="ECO:0007829|PDB:8EUY"; STRAND 314..317; /evidence="ECO:0007829|PDB:8EUY"; STRAND 337..344; /evidence="ECO:0007829|PDB:8EUY"; STRAND 364..366; /evidence="ECO:0007829|PDB:8EUY"; STRAND 385..393; /evidence="ECO:0007829|PDB:8EUY"; STRAND 406..410; /evidence="ECO:0007829|PDB:8EUY"; STRAND 436..441; /evidence="ECO:0007829|PDB:8EUY"; STRAND 460..462; /evidence="ECO:0007829|PDB:8EUY" HELIX 99..107; /evidence="ECO:0007829|PDB:8EUY"; HELIX 114..117; /evidence="ECO:0007829|PDB:8EUY"; HELIX 120..124; /evidence="ECO:0007829|PDB:8EUY"; HELIX 140..154; /evidence="ECO:0007829|PDB:8EUY"; HELIX 158..160; /evidence="ECO:0007829|PDB:8EUY"; HELIX 171..184; /evidence="ECO:0007829|PDB:8EUY"; HELIX 201..210; /evidence="ECO:0007829|PDB:8EUY"; HELIX 219..228; /evidence="ECO:0007829|PDB:8EUY"; HELIX 245..251; /evidence="ECO:0007829|PDB:8EUY"; HELIX 254..263; /evidence="ECO:0007829|PDB:8EUY"; HELIX 280..288; /evidence="ECO:0007829|PDB:8EUY"; HELIX 320..322; /evidence="ECO:0007829|PDB:8EUY"; HELIX 323..333; /evidence="ECO:0007829|PDB:8EUY"; HELIX 346..357; /evidence="ECO:0007829|PDB:8EUY"; HELIX 372..384; /evidence="ECO:0007829|PDB:8EUY"; HELIX 394..397; /evidence="ECO:0007829|PDB:8EUY"; HELIX 417..424; /evidence="ECO:0007829|PDB:8EUY"; HELIX 443..446; /evidence="ECO:0007829|PDB:8EUY"; HELIX 447..454; /evidence="ECO:0007829|PDB:8EUY"; HELIX 473..482; /evidence="ECO:0007829|PDB:8EUY"; HELIX 484..502; /evidence="ECO:0007829|PDB:8EUY"; HELIX 517..524; /evidence="ECO:0007829|PDB:8EUY" TURN 185..187; /evidence="ECO:0007829|PDB:8EUY"; TURN 334..336; /evidence="ECO:0007829|PDB:8EUY"; TURN 358..360; /evidence="ECO:0007829|PDB:8EUY"; TURN 368..370; /evidence="ECO:0007829|PDB:8EV3"; TURN 466..468; /evidence="ECO:0007829|PDB:8EUY"; TURN 507..509; /evidence="ECO:0007829|PDB:8EUY"; TURN 512..514; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..578; /note="ATP-dependent RNA helicase has1"; /id="PRO_0000055087" MAKSELKRKKHQSGNEEVKEKRQKPLKNDKKIAEELPQDEDDYEQEEENEDADQNTSVESESEELDNENEDERVQKSVNLNASSTSDIEKFSDLQLSENIQKAIKEMGFETMTEIQKRSIPPLLAGRDVLGAAKTGSGKTLAFLIPTIEMLYALKFKPRNGTGVIIISPTRELALQIFGVAKELLKYHHQTFGIVIGGANRRAEADKLVKGVNLLVATPGRLLDHLQNTKGFVFRNLRSLVIDEADRILEIGFEDEMRQIMKILPSENRQTLLFSATQTTKVEDLARISLKPGPLYVNVDSGKPTSTVEGLEQGYVVVDSDKRFLLLFSFLKRNLKKKVIVFMSSCASVKYMAELLNYIDLPVLDLHGKQKQQRRTNTFFEFCNAEKGILLCTNVAARGLDIPAVDWIVQYDPPDDPRDYIHRVGRTARGTKGTGKSLMFLAPSELGFLRYLKTAKVSLNEFEFPANKVANVQSQLEKLVSKNYYLQQSAKDGYRSYLQAYASYSLKSIFDINKLDLAKVAKSFGFAHPPNVNITIGASGRTDKKERRAGYNKKNHVDVYSKQRSSAISQDKERGWSR Q09919 FIP1_SCHPO MOD_RES 337; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 338; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 340; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 346; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 347; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 357; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 374; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 375; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 376; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F7.07c; CHAIN 1..397; /note="Plasma membrane iron permease"; /id="PRO_0000159651" MAKDVFSVAIFFIVLRETLEASIIVSVLMSFISQTLMDKDGNVTDPKLKRKFMLQVWIGSFTALFICLAIGGGFIGAFYALDKDIWSGSEEIWEGVFSLIAVVLITVMGFAMLRVSHLQEKWRKKLMKSIANRKAKGISNWGKKYSMFLLPFFTVLREGLEVVVFVGGVGLETPATAFPLPVICGLIVGCLIGYFIYRGGNVMNLQWFLIASTCILYLISAGLMSKATFYFEMNKWNHQTGGDAGELGDGPGSYPFKSAVWHVNYGNPEMNSNGGYMIFNAILGWNNTGTYGSILSYIIYWLFVAFIMFLMWYKERRAARLLIAKLGDKVVDLEAASSHTPVQSSSSEDEFKINSPTDDKGDKAIDIVTEVRESSSPVEEHKDDKTVDVINEIRESH Q09920 FIO1_SCHPO BINDING 85; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="1"; /note="type 2 copper site"; /evidence="ECO:0000250"; BINDING 87; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="2"; /note="type 3 copper site"; /evidence="ECO:0000250"; BINDING 129; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="2"; /note="type 3 copper site"; /evidence="ECO:0000250"; BINDING 131; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="3"; /note="type 3 copper site"; /evidence="ECO:0000250"; BINDING 417; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="4"; /note="type 1 copper site"; /evidence="ECO:0000250"; BINDING 420; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="1"; /note="type 2 copper site"; /evidence="ECO:0000250"; BINDING 422; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="3"; /note="type 3 copper site"; /evidence="ECO:0000250"; BINDING 480; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="3"; /note="type 3 copper site"; /evidence="ECO:0000250"; BINDING 481; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="4"; /note="type 1 copper site"; /evidence="ECO:0000250"; BINDING 482; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="2"; /note="type 3 copper site"; /evidence="ECO:0000250"; BINDING 486; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="4"; /note="type 1 copper site"; /evidence="ECO:0000250" COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 4 Cu cations per monomer. {ECO:0000250}; SIGNAL 1..22; /evidence="ECO:0000255" SPAC1F7.08; CHAIN 23..622; /note="Iron transport multicopper oxidase fio1"; /id="PRO_0000002965" CARBOHYD 30; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 79; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 117; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 123; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 198; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 202; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 234; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 269; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 296; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 338; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 360; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 376; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 532; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNKFFSFPILGLLLTCVRFVVAKERLFEWNVTDVYDVDPDGSGNSRWVIGVNNKWPIDPLVVDYGDQVIIKMTNSLANNRTTSLHSHGLFQKFTPYMDGVPQSTQCEIPPGATFYYNYTALQNGTYWVHSHDMSQYPDGLRTPFIINALEEPYDYDEEYIISMTDWYYTPFNILVPDEFKTWKNPTGAEPVPDTGLFNDTANATFAMEPGKTYRLRFINIGAFNNYDVMIEDHNMTIIEVDGEYTEPQEVSSIHLTVAQRYSVLVTAKNSTDRNYAITAYMDESLFDTIPDNYNPNVTAWLSYNSDASYDLGPDIDEIDSYDDAELNPLYSWDVTESNHSINIWFDFFTLGDGANYAEINDSSYVFPKVPSIMIANSTNVDGYNLEPVTYGPYTNAYIFEYGDVVDVIIDNHDTGKHPFHLHGHTFQVLERGEENAGLYSDQESHTYYDNPMRRDTVEIEPGSFIVIRFIADNPGAWVIHCHIEWHMESGLLATFIEAPEMIPSISSPDFVKEQCMLDGVPTIGNGAGNYKNISDLSGAPSPPGEMPAGWTSKAIGTMAACVISACIGMGSIIFYGASIHPVPTEELDENDDLQEAALENAAMFLDTDKAVEKVVEGKDEIK Q09924 EI2BD_SCHPO MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 19; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 23; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 27; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 28; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC21E11.06; STRAND 119..121; /evidence="ECO:0007829|PDB:6JLZ"; STRAND 182..184; /evidence="ECO:0007829|PDB:6JLY"; STRAND 269..275; /evidence="ECO:0007829|PDB:5B04"; STRAND 294..300; /evidence="ECO:0007829|PDB:5B04"; STRAND 302..304; /evidence="ECO:0007829|PDB:5B04"; STRAND 320..325; /evidence="ECO:0007829|PDB:5B04"; STRAND 337..342; /evidence="ECO:0007829|PDB:5B04"; STRAND 344..346; /evidence="ECO:0007829|PDB:5B04"; STRAND 352..355; /evidence="ECO:0007829|PDB:5B04"; STRAND 372..375; /evidence="ECO:0007829|PDB:5B04"; STRAND 387..392; /evidence="ECO:0007829|PDB:5B04"; STRAND 405..410; /evidence="ECO:0007829|PDB:5B04"; STRAND 425..430; /evidence="ECO:0007829|PDB:5B04"; STRAND 432..435; /evidence="ECO:0007829|PDB:5B04"; STRAND 442..445; /evidence="ECO:0007829|PDB:5B04"; STRAND 448..450; /evidence="ECO:0007829|PDB:5B04" HELIX 107..116; /evidence="ECO:0007829|PDB:6JLZ"; HELIX 143..154; /evidence="ECO:0007829|PDB:5B04"; HELIX 160..177; /evidence="ECO:0007829|PDB:5B04"; HELIX 186..204; /evidence="ECO:0007829|PDB:5B04"; HELIX 209..224; /evidence="ECO:0007829|PDB:5B04"; HELIX 231..248; /evidence="ECO:0007829|PDB:5B04"; HELIX 251..262; /evidence="ECO:0007829|PDB:5B04"; HELIX 278..289; /evidence="ECO:0007829|PDB:5B04"; HELIX 306..316; /evidence="ECO:0007829|PDB:5B04"; HELIX 326..328; /evidence="ECO:0007829|PDB:5B04"; HELIX 329..333; /evidence="ECO:0007829|PDB:5B04"; HELIX 358..367; /evidence="ECO:0007829|PDB:5B04"; HELIX 378..380; /evidence="ECO:0007829|PDB:5B04"; HELIX 398..401; /evidence="ECO:0007829|PDB:5B04"; HELIX 437..439; /evidence="ECO:0007829|PDB:5B04"; HELIX 452..454; /evidence="ECO:0007829|PDB:5B04"; HELIX 455..461; /evidence="ECO:0007829|PDB:5B04" TURN 122..125; /evidence="ECO:0007829|PDB:5B04"; TURN 415..421; /evidence="ECO:0007829|PDB:5B04" CHAIN 1..467; /note="Translation initiation factor eIF2B subunit delta"; /id="PRO_0000156071" MGFSAEQAKKDGKDQSPVSESSSVGGTSPATASSVVSPNEPKLSGKEAKALKKARKQASRRAKAEAAAANNPPGVSEEKKVAIPNKNSNQQKKASKQNPQNSPETDANLQEKKIFEEKQVSIFSHLDWRRRRTTENIPKDIHPAVIRLGLKLANYKIFGSNQRCIDLLKTFKIVIQDYQTPYGTTLSRHLTTHINSQIAYLVSTRPLSISMGNAIRFLKLEISVLDIDLTDDEGKELLLEKIDSYIRDRIIIAGQVIVQAATEKIQDGDVILTYLHSSTVNDVLIHAKNVGKKFRVVVVDSRPEFEGRVCLKLLTEHGIECTYVMISALSYIMQEVTKIFLGGHAMLSNGALYSRAGTSLISLLGHESNVPVIACCESYKFTERIQLDSLVYNELAPGDQLVNMGVDDFEEKPGVLANWKSVKNLKLLSLKYDVTPPRLITVCVCEMGLLPSTSVPAIINEFKQVYA Q09927 ACA1_SCHPO BINDING 118; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:E9P8D2"; BINDING 128..133; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:E9P8D2"; BINDING 155..156; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:E9P8D2" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-glutamate 5-semialdehyde = CoA + H(+) + N-acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:48232, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58066; EC=2.3.1.271; Evidence={ECO:0000250|UniProtKB:E9P8D2}; SPAC21E11.04; CHAIN 1..209; /note="N-acetyltransferase aca1"; /id="PRO_0000074604" MKDPNTIPPWRCTDFNAWCIAVDKSTNVKNKEELLSTLTYFINYEIEMGQTYPIDIKMTRNEAEDFFFKFCTVICVPVESETSPAPDLATASIDWKTSLLGAFYIKPNYPGRCSHICNGGFLVSPSHRSKGIGRNLANAYLYFAPRIGFKSSVFNLVFATNIKSIRLWERLNFTRAGIIKDAGRLKGHEGYVDAYIYQYHFPSLEDALK Q09928 PPIL2_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q13356}; SPAC21E11.05c; CHAIN 1..516; /note="Peptidyl-prolyl cis-trans isomerase cyp8"; /id="PRO_0000064179" MGKNTDKLYITQTEHSGVHGWHGGMSGIAQKNSTTSYKQLPFNYCSLSLQPFNHPCCLVDETKQAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLKFAKNSAEEYCDPVTMKSFTRFSHIVAIRSTGNCFSWDTIERLNIKPKHWRDLVNEEQFTRDDIITIQDPHNVENRDFSAIQKQKETARDEKITKAKIALQASRAKSTESTSSPELSHSLDSSKSIASDMPIHRASHTTGYAAASLTSTSFTPVTKNERAIIAEEDYMLNHTRIKHKGYARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKHDDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIIIFVDPFEEWKKDEREKEKRKRQEEEEENNLDRTSWTGRDLSASSTDHSLNASVGKYLKKEVSLEEKTFTSTVNPKKKKARTGFGNFDAW Q09948 RSC4_SCHPO MOD_RES 257; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 271; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 287; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 313; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1734.15; CHAIN 1..542; /note="Chromatin structure-remodeling complex subunit rsc4"; /id="PRO_0000211178" MVDDSHNAPFDKTKFDEVLEALVGLKDNEGNPFDDIFEELPSKRYFPDYYQIIQKPICYKMMRNKAKTGKYLSMGDFYDDIRLMVSNAQTYNMPGSLVYECSVLIANTANSLESKDGTLNEEENEEMESSINEEHKPGTNEIDVPKVIQNILDALHEEKDEQGRFLIDIFIDLPSKRLYPDYYEIIKSPMTIKMLEKRFKKGEYTTLESFVKDLNQMFINAKTYNAPGSFVYEDAEKLSQLSSSLISSFSEQPKEHSPATSKHEPEETPASPTPSVSASTSRERSTSVAPSFITSDQAATPDVLKSEEAHVESFSKESEKDQTPIPEDVPSPMDTLSQANYGAFALIKSFPSTPVPDFLNFSHKSVMGRSTFNMPNFPEPKFFEDIPNTERCILSAFICSPPQLPLPNPLRMYLPCPSLNSTEVSVITLAPQHSFLNIVINLNPALALKSYTIITLLNGKRLGAGVSTPPSTLYALEGIKHTEEPIRTVYEAKLSVGLNCLEFVLGSTEPVEPPSIEPGLPASAYSRTVERERFVLMAYVQP Q0E7J7 STN1_SCHPO SPBC409.12c; STRAND 40..42; /evidence="ECO:0007829|PDB:3KF6"; STRAND 45..47; /evidence="ECO:0007829|PDB:3KF6"; STRAND 49..62; /evidence="ECO:0007829|PDB:3KF6"; STRAND 65..71; /evidence="ECO:0007829|PDB:3KF6"; STRAND 73..75; /evidence="ECO:0007829|PDB:3KF6"; STRAND 77..83; /evidence="ECO:0007829|PDB:3KF6"; STRAND 102..110; /evidence="ECO:0007829|PDB:3KF6"; STRAND 112..115; /evidence="ECO:0007829|PDB:3KF6"; STRAND 117..126; /evidence="ECO:0007829|PDB:3KF6" HELIX 23..26; /evidence="ECO:0007829|PDB:3KF6"; HELIX 84..86; /evidence="ECO:0007829|PDB:3KF6"; HELIX 88..94; /evidence="ECO:0007829|PDB:3KF6"; HELIX 131..153; /evidence="ECO:0007829|PDB:3KF6" CHAIN 1..325; /note="Protein stn1"; /id="PRO_0000312637" MLENENQLTHQFPTLSRWNPMFISDVHKISFHPHLQRYIGFWMGFPIRWIQIVGYIAAIDIYEGKHVLTVDDCSGMVLRVVFIIQDDFSMSKRAISMSPGNVVCVFGKINSFRSEVELIAQSFEELRDPNDEWKAWQKRMRYKKNLTKISKNHHSIIRTPKKSYFPKDHAKELLKCIRQMCKLNVQAGFTIEELIIYLKAKELHLPLVHIFNVENEIVENCDGNHILALNFSLQTLLQHGRIVRKSNSVYMLVTSKDIIRFVIPLMASGLLEAHKVQSIVRDSNPMFITLPLSAIAKHICQFLLRTKGKWRQAKKYTWVRDNQFV Q10056 SHK2_SCHPO ACT_SITE 434; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 315..323; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 343; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC1F5.09c; CHAIN 1..589; /note="Serine/threonine-protein kinase shk2"; /id="PRO_0000086652" MLLSVRGVPVEIPSLKDTKKSKGIIRSGWVMLKEDKMKYLPWTKKWLVLSSNSLSIYKGSKSESAQVTLLLKDIQKVERSKSRTFCFKLRFKSSTKNFEIQACELSVADNMECYEWMDLISSRALASKVSSPMNPKHQVHVGIDNEGNYVGLPKEWILLLQSSSITKQECMEEPKAVIQALDFYSKQLDTTSETKDSFSFCKETLPRSSTTSYSIRDADKHHKLTTSGVTKMNITERCKPKTTIQTDKKHIIRPFIEDKSHVESIMTGKVTKVPVKADSKNTLSRRMTDRQALAMLKDSVTSHDPVEYFNVKHKLGQGASGSVYLAKVVGGKQLGIFDSVAIKSIDLQCQTRKELILNEITVMRESIHPNIVTYLDSFLVRERHLWVVMEYMNAGSLTDIIEKSKLTEAQIARICLETCKGIQHLHARNIIHRDIKSDNVLLDNSGNIKITDFGFCARLSNRTNKRVTMVGTPYWMAPEVVKQNEYGTKVDIWSLGIMIIEMIENEPPYLREDPIRALYLIAKNGTPTLKKPNLVSKNLKSFLNSCLTIDTIFRATAAELLTHSFLNQACPTEDLKSIIFSRKANTHIN Q10057 PDI1_SCHPO ACT_SITE 51; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 54; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 385; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 388; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; SIGNAL 1..22; /evidence="ECO:0000255" SPAC1F5.02; CHAIN 23..492; /note="Putative protein disulfide-isomerase C1F5.02"; /id="PRO_0000034216" CARBOHYD 161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 257; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 51..54; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"; DISULFID 385..388; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" MKISNLLAAFLAFSGGFFCASAEVPKVNKEGLNELITADKVLMVKFYAPWCGHCKALAPEYESAADELEKDGISLVEVDCTEEGDLCSEYSIRGYPTLNVFKNGKQISQYSGPRKHDALVKYMRKQLLPTVKPISKDTLENFVEKADDLAVVAFFKDQKLNDTYTEVAEVMKDDFVFAASDDKELAKSLGSNFPGIVAFTKDAAQDSDKLVYTGDWDPASIADFIGVSSIPLLDELNQMTFGKYQQSGLPLGIIFYNSTESRDELYDVFQPLAKKYQDTLRFAFLDAVRYGAVAKQMNVESDWPAFVIANLKSMLKYPFPTTELTAKAMTKFVGDFVDGKLQPKIKSQPIPESQEDLVVLVADNFDDIVMDETKDVLVEFYAPWCGHCKNLAPTYEKLAEEYSDDSNVVVAKIDATENDISVSISGFPTIMFFKANDKVNPVRYEGDRTLEDLSAFIDKHASFEPIKKEKESVPAPDLEDQVAVEDEMADEL Q10067 ORC3_SCHPO SPAC3H1.01c; CHAIN 1..690; /note="Origin recognition complex subunit 3"; /id="PRO_0000127085" MSAILQYDSVSKGTYSVKPKPTESLGNEFSEGLFVPLIGGKEPIEYVKLRENLCTKVLNELEEITTHTTYDSNARVLRQLCEHASEPVDETGLLRTAIVCDKSSNSMHLKFYEQLKDDMEKIGWKNFVVLNLKAHRDLKSCFRVIKGGSFGLGVLSYDIEKLDEKTVLVLEDVEDCDRRLLSSLVEALSSLVRHSKLQGCLYTIFNLKIPLEMFDTSLDSKFLSNVKTKVFNMKASTEILESLFTSIEESLSLKFGWRTRRFFRSMFYERSWSVERVIECIRYSILTHFYGNALSIIEHLIYQKDFHLISPLHLTTLRTVPSFQRHIEQRLEIGDLESINYVEKMLNDDTYFQEMVIQMCENLLYRERLLRTQAKIWHELEMAVKTTTRISFADYLETFLQGDWLSSPQYKSICQAILRMNSTKALACLDYLNENIFTGNQTMKCLEIHQELSELIRNSSTNYLEPVEVRMQNYSGTKHTRKVVESGFDKSIIDFSKILKKIVGLLDEEVQYGCLGTESIDMYPFYEVLFYDYCRPLNQAFASGHQRSVIHSSCMDPEYYVGDEKKIDSEFSNAEKDGKDLISWLPDLSILYKLYSESGALLNLYDWYIAFSEHLQAGKENLKEDDNHPRESPQGNLQRELNELDEDKRKLEEAKLQSRFLFGLEELRFLGLIKPTARKTDHVMKTIYHQ Q10075 PCS_SCHPO CATALYTIC ACTIVITY: Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA-COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:131728; EC=2.3.2.15; Evidence={ECO:0000255|PROSITE-ProRule:PRU00773}; SPAC3H1.10; CHAIN 1..414; /note="Glutathione gamma-glutamylcysteinyltransferase"; /id="PRO_0000116449" MNIVKRAVPELLRGMTNATPNIGLIKNKVVSFEAVGQLKKSFYKRQLPKQCLAFDSSLGKDVFLRALQEGRMENYFSLAQQMVTQNEPAFCGLGTLCMILNSLKVDPGRLWKGSWRWYDQYMLDCCRSLSDIEKDGVTLEEFSCLANCNGLRTITKCVKDVSFDEFRKDVISCSTIENKIMAISFCRKVLGQTGDGHFSPVGGFSESDNKILILDVARFKYPCYWVDLKLMYESMFPIDKASGQPRGYVLLEPMHIPLGVLTVGLNKYSWRNVSKHILQQAATVKNADNLAEILLSINQSSIPLIQERSNSSKSGDFEHFKECIRSTKTYHLFLKHTNTNVEYITMAFWAIFSLPMIQKALPKGVLEEIQSLLKEVEISEINTQLTALKKQLDSLTHCCKTDTGCCSSSCCKNT Q10078 PPK13_SCHPO ACT_SITE 192; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 38..46; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 61; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC3H1.13; CHAIN 1..344; /note="Serine/threonine-protein kinase ppk13"; /id="PRO_0000086045" MQNLWKNALDTLSPYISNLFDNDVVCINNERYRIQKLLGEGGFAFVYLVQNVSNEKLYALKKIKCSFGNKGIKKAMKEADYHRKFKSNYLLKSYTHQLVKEADGSEFVYILFPYFAKGSVAQVIRNCDIEGSYISEKRILVWCSCLCKALQYLHENVAGDSPKQPEVNDLIMFDEPQVPQNTSNNNLVSYIHGDIKPDNLLLHENSREIVLTDFGSICLVPIFASNNSEAIAIQDKASENCTMPFRAPELFHVKAGSTITEKADIWSFGCTLYTIMFHASPFEREVSQGGSLALAVCNAQYSFPRKHPYSTLLCEIVEACLQREPNKRPSARELLSKIDLQINQ Q10101 RS7_SCHPO MOD_RES 146; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 151; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 172; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 173; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC18G6.14c; CHAIN 1..195; /note="Small ribosomal subunit protein eS7"; /id="PRO_0000174211" MSALNKIVKRSSSQPTETDLLVAQCLYDLESSSKDMAKELRPLQITSAREVEVGGGKKAIVVFVPQPLLKAFHKCQARLTRELEKKFADRHVIFIAQRRILPKPGRKSRVTQKRPRSRTLTAVHNAILEDIVFPTEIIGKRTRQATDGRKTIKVFLDNRDANTVDYKLGSFSSVYHKLTGKNVTFEFPVATGEGL Q10107 NEP1_SCHPO BINDING 287; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q06287"; BINDING 314; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q06287"; BINDING 319..321; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q06287"; BINDING 334..339; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q06287" CATALYTIC ACTIVITY: Reaction=a pseudouridine in rRNA + S-adenosyl-L-methionine = an N(1)-methylpseudouridine in rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46696, Rhea:RHEA-COMP:11634, Rhea:RHEA-COMP:13933, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314, ChEBI:CHEBI:74890; Evidence={ECO:0000250|UniProtKB:Q06287}; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 33; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 100; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC18G6.07c; CHAIN 1..359; /note="Ribosomal RNA small subunit methyltransferase mra1"; /id="PRO_0000158613" MPTYSKRKSRGSLEVSEKTNQPKFIKRSQSSETITSGETASELMQDEKEQSNGAVGSIEDEELQRLRENQASVEALSKKPESIDRELGVEALEIDNVVKSDEEKEDPNGASSKTVKARPLPAGSVHRVTTHMAPIPARSIGSHDTTTQRLIVVLDQACLEIYKVGKAKDAKYQLLNCDDHQGILKKLNRNIAQARPDITHQCLLTLLDSPLNKAGRLQVYIHTAKKVLIEVNPSVRIPRTFKRFSGLMVQLLHKLSIRSVNGNEKLLKVIKNPVTDYLPPNCRKATLSFDAPTVPPRKYLETLQPNQSVCIAIGAMAHGPDDFSDGWVDEKISISDYPLSASIACSKFLHSMEDFLGIV Q10132 IDI1_SCHPO ACT_SITE 89; /evidence="ECO:0000250|UniProtKB:P15496"; ACT_SITE 154; /evidence="ECO:0000250|UniProtKB:P15496" BINDING 39; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q13907"; BINDING 43; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q46822"; BINDING 54; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q46822"; BINDING 72; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q13907"; BINDING 77; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q13907"; BINDING 90; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q13907"; BINDING 152; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q46822"; BINDING 154; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q46822" CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000305|PubMed:7744766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23285; Evidence={ECO:0000305|PubMed:7744766}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q46822}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q46822}; SPBC106.15; CHAIN 1..229; /note="Isopentenyl-diphosphate delta-isomerase"; /id="PRO_0000205230" MIMSSQQEKKDYDEEQLRLMEEVCIVVDENDVPLRYGTKKECHLMENINKGLLHRAFSMFIFDEQNRLLLQQRAEEKITFPSLWTNTCCSHPLDVAGERGNTLPEAVEGVKNAAQRKLFHELGIQAKYIPKDKFQFLTRIHYLAPSTGAWGEHEIDYILFFKGKVELDINPNEVQAYKYVTMEELKEMFSDPQYGFTPWFKLICEHFMFKWWQDVDHASKFQDTLIHRC Q10142 AUR1_SCHPO MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H8.06; CHAIN 1..422; /note="Inositol phosphorylceramide synthase catalytic subunit aur1"; /id="PRO_0000064765" CARBOHYD 132; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSALSTLKKRLAACNRASQYKLETSLNPMPTFRLLRNTKWSWTHLQYVFLAGNLIFACIVIESPGFWGKFGIACLLAIALTVPLTRQIFFPAIVIITWAILFYSCRFIPERWRPPIWVRVLPTLENILYGSNLSSLLSKTTHSILDILAWVPYGVMHYSAPFIISFILFIFAPPGTLPVWARTFGYMNLFGVLIQMAFPCSPPWYENMYGLEPATYAVRGSPGGLARIDALFGTSIYTDGFSNSPVVFGAFPSLHAGWAMLEALFLSHVFPRYRFCFYGYVLWLCWCTMYLTHHYFVDLVGGMCLAIICFVFAQKLRLPQLQTGKILRWEYEFVIHGHGLSEKTSNSLARTGSPYLLGRDSFTQNPNAVAFMSGLNNMELANTDHEWSVGSSSPEPLPSPAADLIDRPASTTSSIFDASHLP Q10148 TLS1_SCHPO SPAC1D4.01; CHAIN 1..254; /note="Splicing factor tls1"; /id="PRO_0000116466" MNSIHIKKKSNRSFRRRKVFGNEKEFDLEELDDNDIRLRQALEATKRRKIRNSIIGINAEKLLNQETKKEKQLNTANEPHEANDQTSAQSSKLIEAQLPTVEDRFAKQTNEVDINTHLLNFVEKKLKQERLAQNYSENGETNALNTKNESTVQNIKNSLHPNEHSFIRDAAALGAIREVDLGIISTDVDNLKNGRKRQKKRARMKEKLDSKALRTSEDAARDEFIEKMLKPISQDEESKGIYRRFRVYKDGTQD Q10155 RNZ1_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.; EC=3.1.26.11; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; SPAC1D4.10; CHAIN 1..809; /note="Ribonuclease Z 1"; /id="PRO_0000155836" MSKTVNFRATKNFYLQFVSVSSRDTSCIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSSISSPDTYDSSSSSSTTSVSDMLQLDDRDKVIVSERNSMCSTVNYPTWWDSCGGFPGFLLSLNDISEPGETGEASPFVLHGPSEVHQFLSSMRHFTYHTNVNLTVQGYTSAEAPVFVDENICVTPVVVSLVKNSFKKRKHENINRGTNARPLKEDRANTSPHWYSHVSNDTSFVVENAMYNTPAPLEPDKPELFISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIGPSIPGSSFFIIHCPNELVIDLVIENHKWTNAPKPVCVIHSVTPEVYKNPRYQSWISSFPSEVSHLIASTEVNEVINYPRSAVAIATLNLLDSKVFPLGFNCYEVKNVQKNNRIAFAKPKLRFAFGKKTGIDDSEVGVSIEELKDKILKEKPDYKSFVEEAQKYVSDKPKAPSFAGSDIQICTLGTGSAMPSLYRNVSSTYVRIPVDKKCMEDSAISMKNILLDCGEGTLGRLSRQYGDNLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKYSDGRSKLFITAPPQFEFWLLEYSRIDYLPLSNIVFISNSALRTDRKPSALESSRLSSLFKEFDLVSFRTVPAIHCPYSYCMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDIDISTEDLHIALAFDGMTLKISDISLFRYFGKPLAYLFNEENLKEESDPLKF Q10161 CLH_SCHPO MOD_RES 392; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 393; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26A3.05; CHAIN 1..1666; /note="Probable clathrin heavy chain"; /id="PRO_0000205784" MAQQLPIRFSEVLQLASVGIQPSSFGFANVTLESDKYVCVRDNPNGVNQVVIVDLEDPSNVLRRPISADSVILHPKKKIIALKAQRQLQVFDLEAKAKINSYVMNQDVVYWTWISDSVIGMVTDTSVFHWTVSGSDPVKMFDRHSSLNGTQIISYKSNYNEEWFTLIGISSRDNRIAGNLQLYSKKRKVSQPLESHASAFAVIQPEGVDHEVQVLALASRLPTGSKLSIVEVDRNPNNPAFATKTVDLFFPPEAVNDFPIAIEIGSTYNVAYVVTKYGFIHVYDLETAKCIYMNRVSGESIFVTTAHKSVNGLMAINRKGQVLSVSINPETIIPYILSNLNDPGLAVRMASHANLPGADNLYMQQFQQLMAQGNYSEAAKVAASSPRGILRTSQVIDQFKLIQAAPGQIAPILQYFGTLLDKGPLNEHETIELARPVLAQNRIQLLEKWYGENKLACTEALGDLVKPYNTPFALKIYETANVPNKVVMCLSELGDFGKLATYTSQQNITPDYVSLLQNLVRVNPDQAAEFATQMFNSNPSINLEKIVDIFMSQNLVQQATAFLLDALKDDNPEHSHLQTRLLEINLINAPQVADAILGNQMFTHFDRAVIASLCERAGLVQRALELYDKPADIKRVIVHSNLLNPEWLMNYFSRFSPDEVYDYLREMLRSNLRQNLQIVVQIATRYSDLVGAQRIIEMFEKFKTFEGLYYYLGSIVNITEDPEVVYKYIQAACLMNQFTEVERICRDNNVYNPEKVKNLLKEAKLADQLPLILVCDRYDFVNDLVFYLFRNNMFQFIEIYVQRINPSKTPQVVGALLDIDCDEELVQNLLMSVVGQVPVDELVEEVERRNRLKLLLPYLESLLQSGSQDRAIYDALAKIYIDSNNNPEVFLKENNFYDTLTVGKYCEKRDPYLAFIAYEKGGNDTEIINLCNENSMFKQLARYLLKRSDSNLWSEVLQDSAYRRPLLDQVIATAVPESSDPEAVSIVVKALMEVDLPSQLIELLEKIVLQPSSFSENANLQNLLFLTAIKADKSRVMEYIDKLDKYDVDEIAEIAIENGLYEEAFRIYKIHNKHEQAMKVLVEDIVSLDRAQDYAETVEQPEVWSRLAKAQLDGIRIPDAIESYLKADDPSNYSEVIELASRAGKYEELIKYLLMARSKMHEPDVDSALLIAYAKTNQLTEMETFLIGSNVADVKAVGDECFESKNYEAAKLMYSSISNWSMLATTLVYLGEYQGAVDCARKANSIKVWKQVGTACIDKREFRLAQICGLNLIVHAEELPGLIRLYEERGYFEEVISLMEAGLGLERAHMAFYTELAILYAKYKPERMMEHLKLFWGRLNMAKVIRACDQMHLWNEAVFLYVHDQSYDNAAAVMMEQPEAFDHQSFKDIIVHVANLELYYRALNFYLEQHPMLLTDLLAALTPRIDHPRVIRIFEKSENTPLILNFMVAIQHLNIQAVNHAYNDLLIEMEDYQSLQDSIENYDHFDAIALARRLEKHSLLEFRRIAAYIYRKNKRWTQSIELSKQDRFYKDAIITARDSDQTTIAEDLMKYFVEIGNYECFAAILYTCYHLLRNDLVMEISWRKGLQDYAYPYFINFQCEMFSKVLNLEKDLKDRQAVKSEEESASTIGAGILGNTLMLTQGPMANNNDQFDSFQQASPMPRLGNF Q10164 RGA2_SCHPO MOD_RES 388; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26A3.09c; CHAIN 1..1275; /note="Probable Rho-type GTPase-activating protein 2"; /id="PRO_0000097312" MVKMDVVRTTGFFLRSEPTTCRITTFAYSAEIIYFHAETTFLFEKIMKEGNELEKYSKIELNSEIWEDEEEEDNSGIVSQNERLMKLVNKQREIIYELHKDLEKVKKDNTSLRMRLSKYESTDSFPSSQPSRANSPQSDSYSSPYEKGKLFPKISLKSSKDVPTASAHISSSDHEKSSSVSLSALNNYNKTTDIKARSLDRLSDMTRPKLLLNTKRSHRSSEEPGASSPVTSPILKDSQKERIQALRNKAIKTYSVSTESAERIDSIRSDNLSPLSLNTSSFRRPITKPTPFNSDSNISIDPKDNNSNKQDHFAEIEDELRQQFLDIKVGRANASSPRRKSISIVKPHGISSPKHSTNNLSSKSGKFHSDFRVVSENVLLQARSETNSPIIENKEANNFLAPTSNVPAYSTPARPTESPPPPPISSSSTTPRPDDKPSLPPRGLSEDNDSLSLQKTGSSDTRRSSFSTLKIPDSDICFTRRRSDSNRTWTVIDPHHSQSFDNDILAEIPTSKLDNSSQKSPGKLSSKGLLNSFSPISPFSKSKSHNHHPSSQVEKSTSNSKGSMLPLDTLYNNKLSFRLDESLVRYLRFELMKTSLASLSPDFDCIGLQFVVGVSASSHLASQWKDEVWSFTRSIGECRSFATSFVLDIGAPPFPTLDWFTNDSSVIQNELLRRSVDTYFRYIFQTDLKLEQRIKLLEFLSSDTLREYLHDVFFLPPEHAQKEGVLLKYIENSGLVSRYFYLKDNILYFAENRNSPVLGTIHLKDAQVNRYNANLPIFSIIDPPHEFLTGENYQSAFVIQEKQTETRTGTATVHVLLARDVEDQKSWLRAILRQVPGSTSPLNASPFSVLSSDFPGSSRYRDQSSPIRFYGKADSRPVSQEAILSQDISSSPSPVLPPSENVASYADDSLVSNLTMSPKLRDSMEQVPLENHREFEISDRVSELSFDSSTGSVLEIADTRRNQDAPEKHVPVIEIQSSRPSLEKTDQSTPVELLIDSHSQNSQNEEKRSRMKFWAFPHHKAENYEQISDTNIPVIETNVMLSPSSTTSAEPLQKHIVRKSGIFGLPLNEAVNISTQFNDSGLPIVVYRCIEYLESCRAEKEEGIYRLSGSASTIKHLKEQFNEGVDYDLLSSDEEFDVHVIAGLLKLYLRNLPTNLLDTSMHKLFELLPNVPNDSAALGELCDVISKLPPENFALLDSLLHHLRRIIAFEKVNKMNIRNVCIVFSPTLNIPSDIFMMLILNYDHIFTDISRQTNGAQNESDSDVSDDNGEDNEFF Q10167 ATG44_SCHPO SPAC26A3.14c; STRAND 30..32; /evidence="ECO:0007829|PDB:7YDO"; STRAND 70..72; /evidence="ECO:0007829|PDB:7YDO" HELIX 3..28; /evidence="ECO:0007829|PDB:7YDO"; HELIX 34..36; /evidence="ECO:0007829|PDB:7YDO"; HELIX 40..65; /evidence="ECO:0007829|PDB:7YDO" CHAIN 1..73; /note="Mitofissin"; /id="PRO_0000116475" MPFLSRLFHYGVDLALVSTCVAGIRRSSGISFEVEKIHNEDVKTAVEKYLNFGEWAFDQSSAFLGSSTWFKKV Q10172 PAN1_SCHPO MOD_RES 152; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 706; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1221; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1406; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1409; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1412; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1414; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC25G10.09c; CHAIN 1..1794; /note="Actin cytoskeleton-regulatory complex protein pan1"; /id="PRO_0000116609" MSYPNQMNGSMYGYGANNGVQPGFDSYGMPINQGGMNYQQQTYPYQQPYQPDGYAGNTMLPFQQSQPATQFNNGFGYASQPTGSVADYGQQQQQMYGYNGMMPQTMNNTGFMQPQQTGAIPGFAPQPTGFVQPQPTGFMSQQPASFMQPQRTGGAGFIQPQRTGAMPAYQPQMNNFMQPQKTGGFAPQATGFMQTQPFGAAPSFAPQPTGFVQPQQTGVVMPPQPTGYLQAQPTGPFASFVQPQQTASFMPAAQPLKPQKTGQIHNSKAMDTRLSFVSAADQAKFEQLFKSAVGREEAMSSEIGKAILVRSKLPTVQLSKIWRLSDTTRSGRLLFPQFVLAMYLCNLGLTGKPIPDKVPDGILNEVNAMVDAISFSLDENYAKPTQPIPQAAAQQMAAQMFGGFQQAAGIPSQITGFQPQAMMPQRTGMQPQMTGFQQPMIPQRTGMQPQMTGFQQPMMPQRTGLQPQMTGFQQPMVPQRTGMQPQMTGFQQPMMPQRTGLQPQMTGFQQPMVPQRTGMQPMMPGLQQPMAPQRTGMQPMMPQRTGMQPQMTGFQQPMAPQRTGMQPMMPQRTGMQPQMPGMQQPMAPQRTGMQPMMPQRTGMQQPMAPQRTGMQPMMPQRTGMQPQMPGMQQPMAPQRTGMQPMMPQRTGMQPQMPGMQQPMAPQRTGMQPMAPQRTGMQPMMPQRTGMQPQMPGMQQPMAPQRTGMQPMMPQRTGMQPQMPGMQQPMAPQRTGMQPMAPQRTGMQPQMTGGPMLPQRTGGMAPQPTGMPGQWGFINTPLSNLPGIEALGQQMMPNAPSGGLNNTFQQKKDIPWAISKEEKRIYDQIFDAWDKERKGTLGGNAVLEIFGQSKLTRTELEHIWNLCDHGDKGSLDRDEFAVALHLIYRKLNGNEVPAVLPPELIPPSTRNFTESLNQVKNLIKNDTSNRKPFGAENQSKLKKNSFYDNPSETTEKDATLYRHNDSDASAYVSSARRRDFKEEKIESAPPIINDIDSEIASLKKRIHEKSLVVNALEDKKLAATPANDVQNDSLIYRIKSVQDEINRLSTSNKSPEVASMNVRLEELSTRVSKMLSDINEVDHTIASLSLKLFQAEDTKNSYDQTSPEATQERNRTISSKLAEMEKQKNESKAALEQMKNYVTNIENNIRAKLLPSAANDDAWLSQNVVDESVTRVVKELPVPAPAAPQTLNPPSVSTVQQSKPIESNTHTPEVKATSESPSASSNLEDRAARIKAEAQRRMNERLAALGIKPRQKGTPSPAPVNSATSTPVAAPTAQQIQPGKQASAVSSNVPAVSASISTPPAVVPTVQHPQPTKQIPTAAVKDPSTTSTSFNTAPIPQQAPLENQFSKMSLEPPVRPAVPTSPKPQIPDSSNVHAPPPPVQPMNAMPSHNAVNARPSAPERRDSFGSVSSGSNVSSIEDETSTMPLKASQPTNPGAPSNHAPQVVPPAPMHAVAPVQPKAPGMVTNAPAPSSAPAPPAPVSQLPPAVPNVPVPSMIPSVAQQPPSSVAPATAPSSTLPPSQSSFAHVPSPAPPAPQHPSAAALSSAPADNSMPHRSSPYAPQEPVQKPQAINNIAPATNLGTSQSFSPRMGPVNNSGSPLAMNAAGQPSLAVPAVPSAPSNHFNPFAKMQPPAPSPLQPSGHDSDNWSQHGDEEEEDSEDDIRSSKDAAALAAKLFGGMAPAHPVSTPPVRPQSAAPPQMSAPTPPPPPMSVPPPPSAPPMPAGPPSAPPPPLPASSAPSVPNPGDRSALLQQIHTGTRLKKTVTTDKSKPIAGRVLDASDGNSSAWYGNLS Q10175 FKBPH_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 177; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC27F1.06c; CHAIN 1..362; /note="Probable peptidyl-prolyl cis-trans isomerase C27F1.06c"; /id="PRO_0000075316" MSKEETLYSVKVDQERVPLFDEDFYKGFRSELSVRFTMAALDPRAKSNDAVTVNVITRLEHPEEDGEESDEELFQEEKFTLCTLKKGSVYQQPIDIIFSPGEEVFFERVGGDIPVYLSGTCIITNIPEEEDSSDLENDFLYGADEFSSDEEEMDDISVTSSEEEEEENGARIEELNSDEEDAEQAEEEILEKPVPKDEVAEKHSKDKLKKEEKEKKTAVDVSDSVNGKKRKTEPAGEGEQTEKKSKSTKTYPKQVLEGNVTVQDKVKGDGPAAKRKKRVSMRYIGRLTNGKVFDKNITGKPFTFNLGLEEVIKGWDVGIVGMQVGGERTIHIPAAMAYGSKRLPGIPANSDLVFDVKLLAVN Q10177 PDT1_SCHPO MOD_RES 42; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 43; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC27F1.08; CHAIN 1..521; /note="Manganese transporter pdt1"; /id="PRO_0000212608" MSSQSYYMNDLDDLRSLESSTLNKKDTAINELNPEQNDTRRSTDLLLEDKYGIQTGFSKYWKKCTYGIREYCKFIGPGFLIAVAYIDPGNYSTDLDAGSRFQYKLLFIVFLSNLFAVYLQSLCIRLGSVTGMDLARNCREHYNRYICWSFYVLAEIAIIATDIAEVIGTAVALKILMHIPLVAGVVITILDVLLVLIAWRPEGSMLSVRIFETAVALLVLVVAISFAVVLGRVHIGGAGTVFKGFLPSSTVFSREGLYSSIGILGATVMPHSLFLGSGLVQTRLRDLDVRRGNYTPVGDCSDYRPTHETIKHSLTYSIVEVALSLFTFALFTNSSILIVAGAVFYNTSGADTSDLFSIYDLLKEYVSISCGRLFAVALLFSGMSAGYVCTIAGQIVSEGYINWNLRPWLRRVITRAIAIIPCLVVSAAVGQSGLNQVLNASQVCLSILLPFLTFPLVMFTCSRKVMRVVSDSTNEETGQLIRETHDYSLGWTMTIVTWAIWLFLTALNLLLIVWLGMGVSF Q10182 ERFD_SCHPO SPAC3F10.07c; CHAIN 1..172; /note="Ras modification protein erf4"; /id="PRO_0000213986" MLVRIERDYSVSGDKYPQFPTDYPVPLRAYVNLEDWDVFIHTLNEKLREAFCPWSIGNLLDGILSVLTIYISEFVFGSIHRKRIGAIDLYILDFATQHNLYVASLRNMGFLSLVFHTKETNSKSSTLHSNPYCPEHHSIRTLPSAVTATTSNISTSSSHRSDLPNEWTNSTL Q10193 SRP1_SCHPO PTM: Extensively phosphorylated by prp4 on serine residues in the RS domain. {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9421507}. MOD_RES 115; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 119; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 127; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 129; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 154; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 156; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 159; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 170; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 172; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 181; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC11C11.08; CHAIN 1..275; /note="Pre-mRNA-splicing factor srp1"; /id="PRO_0000081962" MSRRSLRTLYVTGFRDGMRARELAYEFEPFGPLIRCDIPIPRTRTSRPFAFVEYEDSRDAEDAYYEVHGRRLERGGGVLRVEWAKQPPPSGPGSKRGGRRERGGRVHGDSGRLRSRSPSPHEARSRSPYNDERSDRRSMSPRYRSRSRSPDGRSRSPDYDRRSPKRNHRSPSPVSFAPQKSPVENETETNVDNGDTKISESNEKSGTEVEQQSAPNSNGNEEVNNLEPVGQNESKQEPPKEENSNVSQEQPEQAQPEVSAASEQPESNPTTTESQ Q10204 RRN9_SCHPO SPBC17D1.04; CHAIN 1..250; /note="RNA polymerase I-specific transcription initiation factor RRN9 homolog"; /id="PRO_0000116529" MNDSEEELEQQGSQEDISSSQDTSDEKEMRKQDALYAQLIEYREIVSELRRSEMKNLCIQLYCSYKAGITRRNELQSDLDGYERRIPPRLRAVWPTIHSIPDESFFDGTSASRFRQEAAYLAVRLASKKLHKLGRMASSEELPNPDGLRYLVERLQIKLERLFDSVDTFRQEQGSKSMQSRVKPMDWKILYGLARVTNGSFSSSQKADVLALGNGTRACQSLFKEMSLQPSIDIEKVSHSNPEISIEFED Q10205 RRP43_SCHPO SPBC17D1.03c; CHAIN 1..270; /note="Exosome complex component rrp43"; /id="PRO_0000139969" MKTVSGVKQLSFTPSIFKKITPEQYLSHLLNQDVRSDGRSVSEFREIVINDNCISTANGSAIIRAGENVFVCGIKAEIAEPFENSPNEGWIVPNLELSPLCSSKFKPGPPSDLAQVVSQELHQTLQQSNLINLQSLCIFEKKAAWVLYADIICLNYDGSAFDYAWAALFAALKTVKLPTAVWDEDLERVICASTLTRPVQLSTEVRSFSWSVFDDKLLADPTDEEEDLSTEFLTIMLNSSKNIVKIIKLGGTHIQPLLLKKCIEVARSKF Q10208 KPYK_SCHPO BINDING 56; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 58..61; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P14618"; BINDING 58; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250"; BINDING 60; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250"; BINDING 91; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250"; BINDING 92; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250"; BINDING 98; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P14618"; BINDING 184; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P14618"; BINDING 249; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255"; BINDING 272; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 273; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 273; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 305; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; MOD_RES 29; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 63; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 281; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 412; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4H3.10c; CHAIN 1..509; /note="Pyruvate kinase"; /id="PRO_0000112118" MSSSAVSPKQWVAGLNSELDIPAVNRRTSIICTIGPKSNNVETLCKLRDAGMNIVRMNFSHGSYEYHQSVIDNARKASATNPLFPLAIALDTKGPEIRTGLTVGGTDYPISSGHEMIFTTDDAYAEKCNDKVMYIDYKNITKVIQPGRIIYVDDGILSFTVIEKVDDKNLKVRVNNNGKISSKKGVNLPKTDVDLPALSEKDKADLRFGVKNGVDMIFASFIRRAEDVIHIREVLGEEGKNIKIICKIENQQGVNNFDSILDVTDGIMVARGDLGIEIPASQVFVAQKMMIAKCNIAGKPVACATQMLESMTYNPRPTRAEVSDVGNAVLDGADLVMLSGETTKGSYPVEAVTYMAETARVAEASIPYGSLYQEMFGLVRRPLECATETTAVAAIGASIESDAKAIVVLSTSGNTARLCSKYRPSIPIVMVTRCPQRARQSHLNRGVYPVIYEKEPLSDWQKDVDARVAYGCQQAYKMNILKKGDKIIVLQGAVGGKGHTSIFRLTVAE Q10210 SWC3_SCHPO SPAC4H3.02c; CHAIN 1..391; /note="SWR1 complex subunit swc3"; /id="PRO_0000116481" MSLNGTFSHNNGLPSGEREESETPGGSTSIISSSFLLQPRASDSRPDALEGKYDKNVLARALKKSRDSCLNGALFEKFLPEENYKLSGGTVFSHVRYIDTATLCVGPLRFEDTKFYFVHYSNSPIEPFAKPNISYVNPQWNELDYRPDSQKLSPGKEKNTLDLKHCLLPSPEYKAPPAKKPEDYEASPGEPVEPLITDASLQRLKSRANEDPTIFNILKRISKGLGTPEQCMLLHNELIGPSTFPLPKRAKKPPRKRITLSINQQDKDEFFDSLINNKKEVRRHFDIVMEFSDAPDTKWIFPRESVLSHVFNTDKKKLEALSLLFHVYRPTEDRNVIDVKTEIKIRDFTPTLRSAIELLTSGTHADRLLSEKRRRMSNLEPKYYMQFHEQT Q10213 SRS2_SCHPO BINDING 33..38; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"; BINDING 302; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; SPAC4H3.05; CHAIN 1..887; /note="ATP-dependent DNA helicase srs2"; /id="PRO_0000102083" METKSSYLKFLNEEQRISVQSPHKYTQILAGPGSGKTRVLTARVAYLLQKNHIAAEDLIIATFTNKAANEIKLRIEAILGNSEASKLISGTFHSIAYKYLVKYGKHIGLSSNWLIADRNDTQAIMKRLLDSLKKAKNPIASGIRGQELTPQNALNRITKLKSNGLLVKPGMDQLSLINGLEEPPKELQSHQSVELYRLYQTSLWKNNLADFDDLLLNFILLLQKQPDCVRNIKHILIDEFQDTSKIQYFLVKLLALQNSDITIVGDPDQSIYGFRSAEIRNLNQMSEDFEGTQVLHLERNYRSAKPILELALSIISQDKSRPKKGLKSNHISSLKPHYRLFETNNKESYWIAREIKRIVGSCPELIFYNDIAILVRSSSLTRSLEHALSELGVPYRMVGVNKFFDREEIRDLIAYLRVLANKDSTSLIRVINVPPRNIGKTKIDRIIFESERRGLTFWQTLNEVKNENILLSQRNDKSFLKSLKSFLCSISKLENRYLSNGHSATLSDLLLGILSEIKYYEYLVRKNKETVEEKWENVMELVQQSDNISCIFYELDYKISTIVLLQNFLTQIALVNEEQKEGESQKVTISTLHAAKGLEWPVVFLPCLCENIIPHSRSDDLDEERRLLYVGATRAQALLYLSSFKSVTGMFADMQNSDNVQDVSPFLKGEEMKRWVMESEIVFNEKIASEIGTILGRKSYGKITNLSGIGSNANHNGTKFENLGFQCCRVLAEAELKKRERVKSVNDYNKDETNFRKHNAKRSKTDIRSWFEKKQPIDSDVEISEPSRSASIMVANKDLNDRSFETVNRIVSTRASTTNASFMSSVRQNLGRGPSTKDQVINRTLREGHQDVVQHTDLNQSNTKVASARPAGSRKRLGVRLRVSRML Q10218 PPC89_SCHPO MOD_RES 157; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4H3.11c; CHAIN 1..783; /note="Spindle pole body protein ppc89"; /id="PRO_0000116485" MPSQFNDNFVATDDDVGTMARVGMALDRELNGDSFQDNLNFQPRSGKREDFEPFFQDTPNTKSLSKHFHDFTMNASLETLPSVEKPRGRNMNAFEETSWNRFRKNGSLFPLSSPPISEPDLRPQALNETPDYRNRFLGAFKKQGVLDDHGNLKLDASPSFLKKPAEYTPLANRQNQNLAFDSPTEALPPKPTTPWRRNGFRSKTTPNLNSGKETPSSYKASARLMEQLGLNHSEPSVDFNNQTSYRLPNLTNLSSLIRDDTIDENGNAKEHDRLPELNTIPVASTDEQLFNAHQLLEKKFEILKRERNECNAKIDELQDKLELLTDAYNREKRRARSLEERMSKEMLTKLGESNVDDGMAASRYDTVKREKERLSEHLKSLQEQYEHIQSVYKNVLLDRESYIMRLGNKISENNELLNENRVLKEKLQTYLDKKESNVTSKIKSTAENSSKPLSMNEADERKDGLNNLLFENKSGANTKEMSNGTETAKENCSPQQDSTSPTSGYQDLVKELAKEIEMRKSLELKLKLSQSNKAGPVKHRKRRPKSKRRITGKVVFDSPNVASGVESDEGSEEISLDSEYSDILSDDGDFEKEKQATLPRRRSSSSMKGNKLAEDSYLNEAGFDWNQGTFHNGSEFGTTGVPDEPNEEELPKHVLKQVEHIINESAAHGVGKCNACHARQEDLIRGEQKVSHSNCLYADQTLRPSQPPSEALKTVVNQLTNELMELKKRYEKLSDRYNSLTPGYHKHKRQEIKNKLIKLIECMESKSDQIYLLYDVNVGKDFS Q10225 BTB3_SCHPO PTM: Ubiquitinated and targeted for cul3-dependent degradation. {ECO:0000269|PubMed:14527422}. SPAC13D6.04c; CHAIN 1..523; /note="BTB/POZ domain-containing protein 3"; /id="PRO_0000067248" MASQDQNTGTTHVELQGGENSKKLFSKYDLWSKAMDEKKLSSSLFTVNDTQEFLELCEACRRGDLEVVKSLVENYNTPINQVDQFDYSPLVLASLCGHEPVVKFLLENGALCERDTFQGERCLYGALNDNIRRMLLSYDITKAIDESQPYASHITSLLSNSALHFTTDIVFAGQYGRVFAHKFYLAARSSYFKSKFSKLGPSEHEIEVKHFAKEFESILRYLYLDTNAVFTKQYNNALLSIGKKFQLNDFIALYEKDREQLHSRDWKKIQLAKTQNDLGEFLDYIISNYKVPIESLNQPSDQYSFHDAYLQSYTHRYPVHRAIMCRCEYFLDMLAGPFLESNQELPVLSLPFSSSVVEIVLKFLYTDKTDIAPELALDVVYVADMLSLDKDRSLKSLASIVITKQEEPIDSIYDILRTAWDTSTPRLEQYASEYMANHLEHLIDDPEFCELVKESADRILQRQETDTIELIDDIRYFLSKRFGIYHEDLCIDGVVDTLTPYESEYNQKMEMIDDLLDKLELQA Q10231 ERG7_SCHPO ACT_SITE 451; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P48449" CATALYTIC ACTIVITY: Reaction=(S)-2,3-epoxysqualene = lanosterol; Xref=Rhea:RHEA:14621, ChEBI:CHEBI:15441, ChEBI:CHEBI:16521; EC=5.4.99.7; Evidence={ECO:0000305|PubMed:8604986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14622; Evidence={ECO:0000305|PubMed:8604986}; SPAC13G7.01c; CHAIN 1..721; /note="Lanosterol synthase erg7"; /id="PRO_0000072656" MEACRVRPELSKTVEQIDKSLWRLNIDSAGGETWEYVTKEEAEKRPLTIAEKYFLGFDLDLPKRPPAKTPLESAEYGYEFFRRLQLPDGHWASPYEGPMFLICGAVFAFYISQTPFPKGWAPEIIQYLINHTNDDGGWGIHTEGVSTVFGTSMNYVVLRILGMDAGHPVATRARNRLHELGGAIGCPHWGKFWLATLNCYDWDGVNPIPPELWLLPDWIPFHPGKWWCHVRLVYLPMGYMYGERLKCPKDSLIMQLRKELYVENYDSINFADHRNTISDVDLYFPHTQILDRLNWILEKYFTYLRPSWLKKLGTRRAYELIKIEDQNTDYSCIGPVNAAMNTVCVYFHEGPSSKAFQKHIQRLHDFMWVQPEGMLMRGTNGLQVWETSFTLQALVESGLYEKEAFKPDIAKALEFLDRQQIRTQYEGSGYRYNSLGAWPFSNITQGYTVSDTTSEALRAVLLVQSLPDFEKLVDIPRLRLSVDVILGMQNENLGFASYEPARTGEWMELLNPAEVFGNIMVEYSYPECTTSVILALRAFTKYDPGYRRDEIENTIENALEYVVKMQRPDGSWYGSWAICFTYAAMFATGSLASAGRYYENCPVQKKACEFLLSKQRPDGGWSESYMACVTGVYTETESSLVTQTGWALDALINAKYPDRKPIEKGIKFLMASQKSDGSWQQKSMEGIFNKNVAIAYPNYKLYFSIYTLGKFAKQYGNYLTI Q10233 RPC2_SCHPO BINDING 1111; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1114; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1123; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 1126; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; SPAC4G9.08c; CHAIN 1..1165; /note="DNA-directed RNA polymerase III subunit RPC2"; /id="PRO_0000048095" MGVNTAGDPQKSQPKINKGGIGKDESFGALFKPVYKGKKLADPVPTIEDKWQLLPAFLKVKGLVKQHLDSYNYFVDVDLKKIVQANEKVTSDVEPWFYLKYLDIRVGAPVRTDADAIQASISPHECRLRDLTYGANIYVDIEYTRGKQVVRRRNVPIGRMPVMLRSNKCVLSGKNEMEMAALNECPLDPGGYFIVKGTEKVILVQEQLSKNRIIVEAEPKKGLWQASVTSSTHERKSKTYVITKNGKLYLKHNSVADDIPIVVVLKAMGLQSDQEIFELVAGAEASYQDLFAPSIEECAKLNIYTAQQALEYIGARVKVNRRAGANRLPPHEEALEVLAAVVLAHINVFNLEFRPKAVYIGIMARRVLMAMVDPLQVDDRDYVGNKRLELAGQLLALLFEDLFKKFNSDLKLNIDKVLKKPHRTQEFDAYNQLTVHSDHITQGMVRALSTGNWSLKRFKMERAGVTHVLSRLSYISALGMMTRITSQFEKTRKVSGPRSLQASQFGMLCTSDTPEGEACGLVKNLALMTHITTDEEEEPIIKLAYAFGIEDIHVISGRELHSHGTYLVYLNGAILGISRYPSLFVASFRKLRRSGKISPFIGIFINTHQRAVFISTDGGRICRPLIIVQNGLPKVESKHIRLLKEGKWGFEDFLKQGLVEYVDVNEENDSLISVYERDITPDTTHLEIEPFTILGAVAGLIPYPHHNQSPRNTYQCAMGKQAIGAIAYNQLQRIDTLLYLMVYPQQPMVKTKTIELIGYDKLPAGQNATVAIMSYSGYDIEDALVLNKSSIDRGFGRCQVFHKHSVIVRKYPNGTHDRIGDPQRDPETGEVVWKHGVVEDDGLAGVGCRVQPGQIYVNKQTPTNALDNSITLGHTQTVESGYKATPMTYKAPEPGYIDKVMLTTTDSDQTLIKVLMRQTRRPELGDKFSSRHGQKGVCGVIVQQEDMPFNDQGICPDIIMNPHGFPSRMTVGKMIELLSGKVGVLRGTLEYGTCFGGTKVEDASRILVEHGYNYSGKDMLTSGITGETLEAYIFMGPIYYQKLKHMVMDKMHARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIAYGASQLLLERLMISSDACDVDVCGQCGLLGYKGWCNSCQSTREVVKMTIPYAAKLLFQELLSMNIVPRLALEDEFKY Q10235 ALP11_SCHPO MOD_RES 213; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13D6.05; CHAIN 1..234; /note="Cell polarity protein alp11"; /id="PRO_0000083512" MNEITLFIKSSSANAERRINPQWTVSQLKTKLVPIVGTPEQYQKLTYEPASSTVPGHVFTSEEENLDLGEFKLQPLGTIVVEDTRPPHLRLDFDDLSQVDKYVMPREQYENRTDSVYAWKKRNQLGRFNPDFEASKASRQESLKRELVDLQKNLNSRCCAAGERYGTIRYIGLVPEINNDNLWVGVEFDEPVGKNDGTVSGKRYFNAKNKHGSFLRSSEVEVGDFPPEDILEGL Q10236 RNH2A_SCHPO BINDING 69; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 70; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 180; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. {ECO:0000250}; SPAC4G9.02; CHAIN 1..326; /note="Ribonuclease H2 subunit A"; /id="PRO_0000111717" MKDDHDAWEPEELVSDNNSSENELQEDQNSSITFLPPSVNKSNPAKSNYYHSTVTDDISKSQPYRLGVDEAGRGPVLGPMVYAVAYCPVDFDLTNYGFADSKTLASLKREELLKLICNKSNELGKNVGWSTMSISARELAAGMLRYRNKYNLNLQAHDTTIDLIKKVYESGINVTEIYVDTVGPPISYQEKLQAHFPQAKVTVTKKADSLFPIVSLASICAKVTRDIQLECARESIRTENWGSGYSSDARTTEWLKVNVDKIFGWKGDIVRYSWKTAKDLLELPSKSQSSIEIDWHEDDDTPTLNFTQKKKPNPASRSWFGSEFYF Q10241 CMB1_SCHPO SPAC4G9.11c; CHAIN 1..223; /note="Mismatch-binding protein cmb1"; /id="PRO_0000048805" MRLFDAMPPYLTYQAPLSLIIFHKMVFAIRIRQFHTTLVSAEKNGLQKLIPPRLKTIWNQMLVETKGAGNGPERFEMIRQKYKALTADEIQKYKNKLQEQFDAEKKRFMETLRSFTPTEIDSENRRRSKEAHSTGSRYYRLRHPDVPKKPSSAFILFYKELRNNPKLRQELGIPEAISTLVEETQNASKAWKELAEDKKKPFIDKSKALKEQYDKFMKEAGFR Q10251 IF2P_SCHPO BINDING 491..498; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; Evidence={ECO:0000250|UniProtKB:P39730}; COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000250|UniProtKB:G0S8G9}; Note=Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound 'on' state. May also act as a transition state stabilizer of the hydrolysis reaction. {ECO:0000250|UniProtKB:G0S8G9}; MOD_RES 73; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 127; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 364; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC56F8.03; CHAIN 1..1079; /note="Eukaryotic translation initiation factor 5B"; /id="PRO_0000137295" MGKKGKKSGYADWEDDLGEDISGQNEYLDNTSQDSPQNDELAEKSENLAVSSEKTTSKKKKGKKNKGNKNQVSDDESQELESPQGPKELTAVTELDDDEFDYKPKKGKKGKKSKKVEEDDEPQEIESPQGPKELTAVTELDDDEFDYKPKKGKKGKKAQNNNESEAAAPPEIPEVRVKTKKEKEREKKEREKLRKKQQQAKKKGSTGEDTLASSEVSSEVDISTPAENDSSAKGKQAAGSKRKGPNVTALQKMLEEKRAREEEEQRIREEEARIAEEEKRLAEVEEARKEEARLKKKEKERKKKEEMKAQGKYLSKKQKEQQALAQRRLQQMLESGVRVAGLSNGEKKQKPVYTNKKKSNRSGTSSISSSGILESSPATSISVDEPQKDSKDDSEKVEKETEVERKEENEAEAEAVFDDWEAALEEPEVAENNEVVTEKKETDIKSDAVEHSIKDKEDSKTDKVDDIPQAAPAESNVSESDLRSPICCILGHVDTGKTKLLDNLRRSNVQEGEAGGITQQIGATYFPIESIKQKTKVVNKKGKLQYNIPGLLIIDTPGHESFTNLRSRGTSLCNIAILVIDIMHGLEPQTIESIRLLRDQKTPFVVALNKVDRLYGWHSIKDNAIQDSLSKQKKAIQREFRDRVESIILQLNEQGLNAALYFENKNLGRYVSLVPTSAQSGEGVPDLVALLISLTQTRMSDRIKYITTLECTVLEVKVIEGLGATIDVILSNGVLHEGDRIVLCGMGGPIITTVRALLTPQPLKEMRVKSAYVHHKEIKAAMGVKICANDLEKAVAGSRLLVVGPDDDEEDLAEEIMEDLENLLGRIDTSGIGVSVQASTLGSLEALLEFLKQMKIPVASVNIGPVYKKDVMRCATMLEKAKEYALMLCFDVKVDRDAEDLAEQLGVKIFSANVIYHLFDAFTAHQKKILEQKREESSDVAVFPCVLKTVAAFNKRDPIILGVDVVEGVLRINTPIVAVKQLPNGEPQIIELGRVASLEMNHKPVDKVKKGQAGAGVAMKLESSGSQILFGRQVTESDALYSHITRQSIDSLKDPAFRDEVSRDEWQLIIQLKKLFGII Q10252 COQ2_SCHPO CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate; Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914, ChEBI:CHEBI:78396; EC=2.5.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_03189}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03189}; SPAC56F8.04c; CHAIN 1..360; /note="4-hydroxybenzoate polyprenyltransferase, mitochondrial"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; /id="PRO_0000035922" MEMALLPQPSPARYFLRTPSWSAVAIFQAVKIKPLQLRTNSSNSVTPNLISPSKKSWKDLFSKRWQYYAEISRAGSPTGTYLLYSPCTWSILMAAYAYDSSLVNVTKMLALFGVGSFLMRSAGCVINDLWDRELDAKVERSKSRPLASGKLSVRQAISLLSVQLTASLGILLQLNPYTIKLGVASLVPVCIYPAMKRITYYPQVVLGLTFGYGAVMGWPALAGEACMNWSVVAPLYLSTISWIVLYDTIYAHQDKRDDVKANIYSTALRFGDNTKPVLCGLAALQIATLATAGIMNGQGPVFYTLGVAGAAYRLSSMIYKVDLDDPKDCFRWFKRNSNTGYLVAAAIALDWLAKSFIYDS Q10268 MAC1_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" MOD_RES 438; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13G7.04c; CHAIN 25..756; /note="Membrane-anchored protein 1"; /id="PRO_0000021632" CARBOHYD 52; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 64; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 190; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 396; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 407; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 459; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 470; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 471; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 496; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 497; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 521; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 522; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 547; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 548; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 573; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 574; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 594; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 598; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 599; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 618; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 623; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 649; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 664; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 676; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 685; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 715; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIRNTLAFLAILFLLIPTALLIIGSVSVPSTRMTLAKVEGTEFGIFGTCTGNGTDCTETSFGYNASSSLIDDFYYKGDKRLVLSKVLITHIISAFLSFLSAIFVFFSIFLVNQAVNIINIIVVFITTLLTCLAFAIELVLFLPHNTWQSYVTAGAIGSDLIAILALCLRSVSISRIGQKSARLEHVDTMNSSYSSYKTDVKYPLALDDKLSSVPTLPKFHDALTSTSEFGPPSDSGDTVGTTQYPGDIKYATGYESTVASPVPSRVAKLSSRDTPSIIADYDEFRKSESSPSRSSVLSTSKPEVHETEGYCPHKTGNRPGFPSLNIPRTRPTTAGIANTQFDLEPYRNRQAGSISSEGTDSRFFDVENQVSVAQTPSVKPEMFPKTARPFAAIHANASSTQLRNTENITHPGIPNHFAKTTSSVFDEPPATRMPQTRSPVNDHSSFPSDLPIKGEMSTNMTGAPRVGSRNNSSNDLHAQAGMLKNVGNGPRNAPRNNSSNNLHAQGGMPMNMRGPRGAPRNNSSGDLHIQSGMPMNGRNGPRDTSRNNSSSDLYAQSGMHPNMNNGHRGAPRNNSSNDLHAHGGMPVNMRGPRNTSRNNSSSEFNAQIPMNLRNGPRNASRSNSSTDLFGQSGIPGNSRGMPTSPNSRNNSALDLSMHGIPLANNSRQFKRPSYGNMSRPSFELNGSRNPSHGSLNTAHAGMGYGPRSMMRDPQNLSNVPPVSNTLDQLSGNADFELPVRGNRNNRRGPGGNRMIR Q10269 AREH1_SCHPO ACT_SITE 474; /evidence="ECO:0000250|UniProtKB:P35610" SPAC13G7.05; CHAIN 1..537; /note="Probable sterol O-acyltransferase 1"; /id="PRO_0000207652" CARBOHYD 250; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTDTPRILITPSPLSDISTTINKPNVHPSMSLLKALPECRLVVKSKGDKNNANVVEFPLDRHKQLLIAGKVYHDYKFKPRKSIFDRVTDPNYFAKSEFRGFYVLFWLSMAAWVLQLYARSYWQRDTLLGLPLARQVFRQFFVLFSSDFLMICLSFFSYGLQVCIEKNMIRWANLGYTIQTLWQGFYMVLAVYWVKHRDFPIVQCVFFTLHCAVLIMKQFSYSHHMGYISEIRILHNEYEKLLKFVRECLNSTEKDEKYTFELTFPNKPAETISTLQAEEIVALTAKYLSRQMRSEVGNVVYPDNINFFNYVDYLLVPSLVYSMEFPRVAHFRWHYMAFKAGSTFGLLALTLALVDWYFVPSAVAVKDLDFIGKLRIAPLLMNKIMFPAIILYLIMFYLIFDCILNAFAEITKFADRGFYGAWWNTVTWDEFSREWNKPVHVFLMRHVYHSSISGFKLKKSHAVLLTFLISALVHEFVMLLATGKFRCYILTFQLLQIPLYDLQQMFAFKKRDILGNVFFWIGMFTGPSFLCILYIVF Q10270 MET16_SCHPO CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol; Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8; SPAC13G7.06; CHAIN 1..266; /note="Probable phosphoadenosine phosphosulfate reductase"; /id="PRO_0000100661" MSSIDTPANKLQAKTLFHPEHLEYINKQLSELSPQDILKWCRWTLPSLFQTSALGLSGLVIMDMLSKMDMNVPLIFINTLHHFPETLDLLEKVKTKYPNVPVHVYRCAEAANEKEFAQKFGEKLWETDESRYDFLVKVEPASRAYSDLNVLAVFTGRRRSQGGERGSLPIVQLDGPVLKINPLANWSFTEVHNYIITNNVPYNELLNKGYRSVGDWHSTQPVREGEDERAGRWRGREKTECGLHSHPQSKFAQYMAELKKKETADQ Q10272 IPI3_SCHPO SPAC13G7.08c; CHAIN 1..446; /note="Pre-rRNA-processing protein crb3/ipi3"; /id="PRO_0000050942" MELLLSGCEAIEGEPSNVLCHNLHTGTLVSTFRQSSPAKNATCTTLNHLLSAQHTRPQLNIHNFGKEILDQSIILPEILICVQSSPCGSWLAAGTEKGNLYIWSLKSGALIYFFRAHYQPLTILKFSNDGMVLFTASNDGDVFAWLISTLVDQNSTFETSNSSVKAISHFSGHKRSIVSMEIGPGPIVSGRLYTASEDNTIRIWDVSTGNLLTTIALPSTPSCMTVDPSERVVYVGNEKGIIWIPLYTGSSTFSNNVKEKKRVTSVDNTTIPNAIGGMGRVVDYNDSRESSIISCQSPITTLTVSFDASLLISGDKDGNVLVWDSVSRQVLRRLVQYYSPVSFLQCKVDKISFYSNSSLSFPVLKRMITNEYLNSDVRICIQDDGVEQLMQPENILKISSDIVTQGSESSWRAKAETSEMQLKEAKRLFYELKQIHQALWEKYLQK Q10279 FUR4_SCHPO MOD_RES 572; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1399.03; CHAIN 1..581; /note="Uracil permease"; /id="PRO_0000197924" MESVDNNSFFSRIRNSNAYRKVKDFVILDHRPGMTMAERMLTNKDLYPVPPSKRLWGPWNFISFWLADAVNINTWMISATAIELGLNWWEAWICVWVGYLICGILVATTGRPGAVYHISFPVLSRSSFGTWGSLWPILNRSVLACVWYGVQAWIGGECVVLMIRSIWPSFSHIPNTMAKSGTETYQWVGFFIFWLLSNIAIWFPVHQIRHLFTFKAIVAPPAAIAFLIWALVKAHGAGPVIHEPTKLGQYEHAWVVINGIVTCIDGFATLIVNNPDFARFATTPGAVHWPQIITVPLAFGVTSLIGVLVSSASKAIYGTTLWDPTQLLASFLDHSNAHGVRAGVFFIAFGLCIAQLGVNIAANSVSAGNDLSALLPTVINVRRGGYIASIIALCMCPWNLLSSNNNFTTYLSSYSVFLSSFAGVIIADYYFVRKGLIRVAPLYSSSSSSPYYFWKGINFRAFASYICGMLINIVGMAGSTGQKVPKVANTMFNLNYFLGITVACLSHIIICKIFPVTECGEKMLSEVPEEADDYLLTLASEDSIDKDSTSEIYIDGLPTEKEVEKDDVLSITSKKLSGCFP Q10290 CENPO_SCHPO SPAC25B8.14; CHAIN 1..303; /note="Inner kinetochore subunit mal2"; /id="PRO_0000084556" MDDEEGNATLIDEISVLEARRDVLLDELKSLDNATLSDLVQKPELSKNLSVNNEFLKETPLNQPALHYDRLSGISFFQPNDPEELSRKTLLVKNKKTGAIETAPSIPLLGVRFDIMLNPVNIGFTNLSENPISSASGMDEELEGGNRFDVPYYIIFRVFHDSFALYKYTIPSFLNIQEWADEYLTGKNPERFRIFLWKVDKLLTAYICRKNALLQINKSLTIDGTNISANLSCTHLVIQIPKVIQATLVCSSESTRVVKSRIYQYSDENWKRDHRLELSLLDNKRWVNILVSHLTAPESHASL Q10303 ALP21_SCHPO SPAC22H10.10; CHAIN 1..511; /note="Cell polarity protein alp21"; /id="PRO_0000064569" MHISTGMVRASISNTLVTLTIEGNNDRYQVILDKNVNAKQFVKTCWRNKKPLIVKEGKIFVDKGFPFDPCRTFLEALYEKYSYSSPLPSSVEFKSGKQVEFCGFEKIQSKQRDLKSLRVIILDNYRIEDIEIEYEYSKILPEVIDLDLSRNLFHEFFPILKLCSQLPSLRNLTLDSNLFSNFISSNTVLLIPHLTQLSVNGCGLNSKDVQWITETFPSLEVLYLEANEIILSKATSFKNLQFLQTLSLANNLNLYSADGYAVDVFQGINNLNLSSTSLADVAELPVHTLHKLTFLDISENNIRDIRSLDHLRTLENLKHLRITLSYFNKPTDIAKLLVIARIPSLVKLNDVNISPNERLDAELYYTSCIRKLVIDNEIKDVEELTKIEPFWEEIWKSHELPSIQFHLEASINDWTSGILKNRITKGIKISSINSGATMLLKLHYNWKLLDIKALISYHFAIPVHTSTFVFASSERDVSFSPKTVRDDQKRLFELPFTCTFIDVYAKESGNV Q10315 BUR6_SCHPO SPAC17G8.03c; CHAIN 1..199; /note="Transcription regulator complex subunit bur6"; /id="PRO_0000208348" MGDPTNNNDSETKPNPATYWKSRFPVARIKKIMQADQDVGKVAQVTPVIMSKALELFMQSIIQESCKQTRLHQAKRVTVSHLKHAVQSVEQFDFLQDIVEKVPDAPPIKAERKTKRPRARRAANEGEHNESVPAKKVKKNTVKEEEIEKDDESATTETPVKEEPTGEETEADHEEKASVDHGNFSDKTTSEASSASGDE Q10316 ARPC5_SCHPO SPAC17G8.04c; HELIX 3..5; /evidence="ECO:0007829|PDB:8UXW"; HELIX 9..12; /evidence="ECO:0007829|PDB:8UXW"; HELIX 18..21; /evidence="ECO:0007829|PDB:8UXW"; HELIX 29..48; /evidence="ECO:0007829|PDB:8UXW"; HELIX 52..59; /evidence="ECO:0007829|PDB:8UXW"; HELIX 70..86; /evidence="ECO:0007829|PDB:8UXW"; HELIX 92..96; /evidence="ECO:0007829|PDB:8UXW"; HELIX 101..115; /evidence="ECO:0007829|PDB:8UXW"; HELIX 123..137; /evidence="ECO:0007829|PDB:8UXW"; HELIX 140..147; /evidence="ECO:0007829|PDB:8UXW" TURN 89..91; /evidence="ECO:0007829|PDB:8UXW"; TURN 118..120; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..152; /note="Actin-related protein 2/3 complex subunit 5"; /id="PRO_0000124058" MTFRTLDVDSITEPVLTEQDIFPIRNETAEQVQAAVSQLIPQARSAIQTGNALQGLKTLLSYVPYGNDVQEVRTQYLNAFVDVLSNIRAADIPAFVKECSTEEIDNIVNFIYRGLANPQAYNSSVLLNWHEKVVEISGIGCIVRVLNSRPDL Q10318 ILV3_SCHPO ACT_SITE 511; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P9WKJ5" BINDING 84; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250|UniProtKB:P9WKJ5"; BINDING 116; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P9WKJ5"; BINDING 157; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250|UniProtKB:P9WKJ5"; BINDING 158; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P9WKJ5"; BINDING 232; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000250|UniProtKB:P9WKJ5"; BINDING 485; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P9WKJ5" CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:49072; EC=4.2.1.9; Evidence={ECO:0000250|UniProtKB:P39522}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810; Evidence={ECO:0000250|UniProtKB:P39522}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-oxopentanoate + H2O; Xref=Rhea:RHEA:27694, ChEBI:CHEBI:15377, ChEBI:CHEBI:35146, ChEBI:CHEBI:49258; EC=4.2.1.9; Evidence={ECO:0000250|UniProtKB:P05791}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695; Evidence={ECO:0000250|UniProtKB:P05791}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P39522}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250|UniProtKB:P39522}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P9WKJ5}; TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC17G8.06c; CHAIN 19..598; /note="Dihydroxy-acid dehydratase, mitochondrial"; /id="PRO_0000015635" MMFCKLLRCQNGIASKRAALSLKGFKTSSINLVEKKLNKYSETITGPKSQGASQAMLYATGLNEEDMKKPQVGIASCWYEGNPCNMHLLDLGRRVKEGVKKAGLTGFQFNTIGVSDGISMGTTGMRYSLQSREIIADSIETVMQGQWYDANVSIPGCDKNMPGCLIAMGRFNRPSIMVYGGSIRAGHSPCQNNAPIDIVSAFQSYGEFITGKIDEPTRHDIIRHACPGGGACGGMYTANTMASCAEAMGMTLPGSSSYLAGSPEKFAECEAAGSAIKRLLVDDIKPRDIMTRSAFENAMVLTMTLGGSTNSVLHLIAIAKSVGITLTLDDFQAVSNRTPFIADMKPSGKYVMEDLFAIGGIPSVLKYLHAEGLIDGSNITVTGKTLAENLRGFKDLAEGQKIIRPLSNPIKTEGHLRVLRGSLAPEGSVAKITGKEGLNFTGKARVFDAENDFIAALERGEFKKGEKTVVIIRFEGPKGGPGMPEMLKPSSAIMGAGLGKDVALLTDGRFSGGSHGFLIGHVDPEAQVGGPIALVQDGDVIEINAVKNTLDLMVDEKEMARRRSVWKAPPLKYQQGTLLKYARNVSTASKGAVTDSLE Q10319 AF9_SCHPO SPAC17G8.07; CHAIN 1..217; /note="Protein AF-9 homolog"; /id="PRO_0000215931" MAPNTRVSKCQISRPILVGNDAKPLTKEEKEKAPTDHTHTWRIFVEGVDGEDISKWVRKVVFKLHDTYNNPTRTIESPPFEVIETGWGEFDIMVRIFFAPEAHEKALTFYHHLKLHPYGPRMEEMKASGGLVESVQYEEIVFNEPFEYTYKLLSQNPIGDGHGLAVESEPDHPFSQQLEQDEADKLDFAIQEVKKTIEMYKQQVQSLQGQKSSTPVE Q10321 SHG1_SCHPO SPAC17G8.09; CHAIN 1..132; /note="Set1 complex component shg1"; /id="PRO_0000212514" MDRDVTLNVDELVSKFKKEGHFDRLRKQILETVNEKESGPLLDRLKKIIDEEMVKDRTLKSKDQFRAAPLIAGAVDRSSLYEDSMEHIRSNVLSDQDLREVIYNSLEQIGIEQIEHEDEEKLLNSKTMDGRK Q10323 IMT3_SCHPO MOD_RES 307; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17G8.11c; CHAIN 1..356; /note="Inositol phosphoceramide mannosyltransferase 3"; /id="PRO_0000116591" CARBOHYD 52; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 146; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNKILFYFFFFLTLILSATVYLFGGPMMLFFINYKTDLLKVDDVYNHEIYSNQSAAIPKIIHQTWKTNEIPEKWVGAQKSCIDLHPDYEYVLWTDESMREFIATDYPWFLTQYDSYPYNIERADVVRYFILYKYGGIYLDLDVGCNRTLDPLLHYPAWVRRTSPSGISNNVMGFAKGHPFLLQVVRNLPRFAFNYHFPYLTVMYSTGPLFLSIIWSAWRKLPDAEAWHHIWVMVPELYEKSHHAFFEIYEGSSWHDSDAGFVFYMLHHWAIFTFLGFLTFFIVVYFIFGYALKPAARVSRTGRRVFSSPFSKTSPSRWKIFHRFTSSNEKYDQTRSDSLPFMSDYDLESQTQSHSP Q10324 YD6C_SCHPO SPAC17G8.12; CHAIN 1..608; /note="Uncharacterized protein C17G8.12"; /id="PRO_0000116592" MASNPNAVEQEILQAVNSAQTTDKRKAHEQSLAYLPVEEERGVNVVGSKMKPRYIALTCDDVTRIFYIHRLKVNDKGGMTVVKSWPLFELQNITVINDHDVTMTINKPHLLRTQDTSARDRFVFSVAKNYMYYMGRPLSVTTTDGRKVDWAYRNSFADNKPNLYPAKSLAIPKARSSLPENSSEQVSSSFNSRVAHNRNFSDGPIVTNLETDQPRIEKKLTIDSSRSAKKKLSVEKERRFSDNKPSSNVSRGTPSSAHSDVIEISSSSAIARTSGDRKDDVLFDTSTQRRDNQTREMFIQEQAQLFPSKPSLRKTTRREQAPSFNSGTSSSERGKNSISGSYEKNTALALEAGKYNMSQKDVKLSSSLESNTFASDFSKVDRDATQAALSSSLETPSVLTSSYKPSSSSKVSAKSVSRKPTGAPAIPKLPPKHPSRQPTVRATPSTGKQIEPPNDEPSIGNELLPLFESLRFENRKTTSKPKAKKTLVTSIPTKPHQASVEKVYDLNSKINLKNIPEQSISRLSTLKWNEGTTIKDVLKQTEFSFDGAIISSVENLAEEEIELQNIKSQLQDCALGCESINSTINLFSLELSTALNGVINIEQQPSRR Q10330 RL25A_SCHPO MOD_RES 68; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC106.18; STRAND 47..50; /evidence="ECO:0007829|PDB:8ETC"; STRAND 62..65; /evidence="ECO:0007829|PDB:8ETC"; STRAND 79..85; /evidence="ECO:0007829|PDB:8ETC"; STRAND 106..113; /evidence="ECO:0007829|PDB:8ETC"; STRAND 119..125; /evidence="ECO:0007829|PDB:8ETC"; STRAND 127..129; /evidence="ECO:0007829|PDB:8ETG" HELIX 4..7; /evidence="ECO:0007829|PDB:8ETG"; HELIX 13..15; /evidence="ECO:0007829|PDB:8ETG"; HELIX 58..61; /evidence="ECO:0007829|PDB:8ETC"; HELIX 69..78; /evidence="ECO:0007829|PDB:8ETC"; HELIX 91..102; /evidence="ECO:0007829|PDB:8ETC"; HELIX 131..138; /evidence="ECO:0007829|PDB:8ETC" TURN 8..10; /evidence="ECO:0007829|PDB:8ETG" CHAIN 1..141; /note="Large ribosomal subunit protein uL23A"; /id="PRO_0000129481" MSVAKAKGAQKTVQKGIHNKVAKKVRTSTTFRRPKTLQLSRKPKYARKSVAHAPRLDEYKIIVNPINSESAMKKIEDDNTLVFHVHLKANKFTIKEAVRKLYSVEPVKINTLIRPNGTKKAFVKLSADADALDVANRIGFL Q10332 YBMA_SCHPO BINDING 262..269; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" MOD_RES 712; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC582.10c; CHAIN 1..830; /note="Uncharacterized ATP-dependent helicase C582.10c"; /id="PRO_0000074382" MEKASKNKESGVKKANNSFLQNFGVNTAGKENESTSLPRLPKSEDESIPKQSIKSKNKKKTQHFLSDAFESLKRQEIDTNEKEVIVSAPITSKPAQVFYSKKLERKDEGIRKWEKDPFAPISVKSGAWKKPYTKVPEVSINKATSKRTDLINDKPIVIPIPRASTSTLYFGKHNKPTSENRKGPIGIPTEEILTSQNTQAMLHKLFENNVLDNVKDDSMQRQSSFIPGMHIRLLDHQVQGLTWLKSRETVSKSSASGGILADDMGLGKTIQMIALILSHPLPKKKHSIKSTLVVAPLSLIKQWESEVQTKSKLTAIVYHGASRYKLLKVIHEYDVVITTYQILVSEWVSHNTTGTDGKSPTEAKSYEKKKPSLFAFYWWRIILDEAHTIKNKSSKSALACCALQGINRWCLTGTPLQNNVDELYSLVKFLHINPFNDQSVWKDQISLPLCQGEENLVFKRLRMLLSVIMLRRTKTLLEANAGKDGTGGALKLSKRLVYKVICKFEESERDFYSNLARNMERTMSNFVNSGKLGKNYTNILCLLLRLRQACNHPQSLNFQFEQDVDAFNALDGAANTNKLASDQDVDDLANLLETVEIGSRKKSFCTICMAELPPDFHEKKCKDCSRNFKELDKGIQDPNDKTLYKSSKIREILKILSLDEQEEDDTVRGLRKTIIFSQFTTFLDIIDLHLRKAGIGFVRYDGRMNNRAREKSLDLLRSDSGTQVLLCSLKCGALGLNLTCASRVILCDVWWNPAIEEQAIDRVHRIGQRRDVLVYKLVVENTIEEKIVELQNLKRDLAKQALGDGKKSVFTSKKLTLNDLLFLFNKRAAA Q10337 BRC1_SCHPO SPBC582.05c; STRAND 667..671; /evidence="ECO:0007829|PDB:3L41"; STRAND 688..690; /evidence="ECO:0007829|PDB:3L41"; STRAND 698..701; /evidence="ECO:0007829|PDB:3L41"; STRAND 720..722; /evidence="ECO:0007829|PDB:3L41"; STRAND 775..780; /evidence="ECO:0007829|PDB:3L41"; STRAND 803..806; /evidence="ECO:0007829|PDB:3L41"; STRAND 822..826; /evidence="ECO:0007829|PDB:3L41"; STRAND 847..851; /evidence="ECO:0007829|PDB:3L41" HELIX 681..686; /evidence="ECO:0007829|PDB:3L41"; HELIX 709..714; /evidence="ECO:0007829|PDB:3L41"; HELIX 715..717; /evidence="ECO:0007829|PDB:3L41"; HELIX 724..733; /evidence="ECO:0007829|PDB:3L41"; HELIX 740..742; /evidence="ECO:0007829|PDB:3L41"; HELIX 747..753; /evidence="ECO:0007829|PDB:3L41"; HELIX 757..767; /evidence="ECO:0007829|PDB:3L41"; HELIX 786..788; /evidence="ECO:0007829|PDB:3L41"; HELIX 789..798; /evidence="ECO:0007829|PDB:3L41"; HELIX 811..819; /evidence="ECO:0007829|PDB:3L41"; HELIX 828..830; /evidence="ECO:0007829|PDB:3L41"; HELIX 831..834; /evidence="ECO:0007829|PDB:3L41"; HELIX 838..841; /evidence="ECO:0007829|PDB:3L41"; HELIX 852..861; /evidence="ECO:0007829|PDB:3L41"; HELIX 872..874; /evidence="ECO:0007829|PDB:3L41" TURN 694..696; /evidence="ECO:0007829|PDB:3L41"; TURN 771..774; /evidence="ECO:0007829|PDB:3L41"; TURN 835..837; /evidence="ECO:0007829|PDB:3L41" CHAIN 1..878; /note="BRCT-containing protein 1"; /id="PRO_0000064983" MEKIKLLNVKTPNHYTIIFKVVAYYSALQPNQNELRKKELFIKNDGKALSFPYDWKLATHVICDDFSSPNVQEGSKRSLRLAKTNWIRDCVDKNTLLNYSFYSCNPYLLFKGICASSCQIDSYQSSLIDDALETFGGRFSKGLMKSMTHLFTYSGMGAKCKKVLDKPSLSIKLIHPQWLLDCLQFGQLIDQDPYLFPNPSYKKNDSSISKAEPTSLFRNVLHGKRIYFSNDLNLPTNFRHSLQKFSVGIGAKIAESINDCDIFIGLKRDTIEFNLASNKNTTIGTISWLLNLFVLGSWKSPLLNALHYPFPSVGFLKDQMVAVTNYTDAARIYLEKLLLACGATYTKDLKPTNTLLIAASSYGQKYGAAKVWNIPTVHHSWLYSSFKNLSSQAFTDFPVPLDDSYMDFIFPCPLNVEKGSFEDTLKSSLTKGNSEVLLDDLSDPSVSSIKGNKTNEELEKEFKSTSDNFGKHIILTSSFSNQSADKGSSLAAEDDRNDEGSTITGVNRELQDEGRLEIDAKSSKTNTPPSPLLVGTPSKESLKEASSDDELPVLATKLVDNVIKEKSPLSLTPKVVVPSHKETYTDEKKLIDELDRVNPLNSSQLLRSKRKSAATALSMLQNVIMPDVLAFEREKKRRQTHRSVSSGEVSRESSESRNTNAKASKRVYITFTGYDKKPSIDNLKKLDMSITSNPSKCTHLIAPRILRTSKFLCSIPYGPCVVTMDWINSCLKTHEIVDEEPYLLNDPEKELELGCTLESALKRARAQGPSLLEDYVVYLTSKTVAPENVPAVISIVKSNGGVCSTLNVYNKRLARHLEDGNVVLITCNEDSHIWTNFLDNASQNKTIFLQNYDWLIKTVLRQEIDVNDRIADEFARAV Q10339 EXO70_SCHPO MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 418; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC106.20; CHAIN 1..615; /note="Exocyst complex component exo70"; /id="PRO_0000118973" MSGGIFDDNKAGFETFQKNLNSVAKNVSDASNILLSMDKRLSGLEASAGILRDDVTNYNRVSSNIYDTLKEMESLQVIHSHLPVLQKGLQECQNLNKSVSQNLKSVMDILKSLAEDYTSLEGSPLQFASKSQQKVEMMLSEGCQILGALCYNILETYAASSLNKASTLLDLSIPWSFPNESLQQFIGLIQQFDADVLFPVSCSSDISNIYIKIKGECVVKLLHAVSMRTDEIKLNEGSVNFVTGKEDVSINLVALSRLLPAVASELLLLFDQVTAKALYPKIVKPAINTVTNATRQLEGVYEKRGAAENFVLLSLIDCIVVTRQNMNNLMPFEDASFLGFVNGVGREMEKILISSISRLYNGTCHNNKTVPLTTDRVSEMTHGIMSFLNELAEHENASYLLESIGNWGWRHEINADLSPARSVQDITRNYVMDCMDSYLTSVQTAAQAVDTIGWKMGVMLLNISVYFEAKCLESKIASFLQDVDLEKLGDRSQKYSTMYMEVWRQCSQNMLDSTYTKSQNKSTMSAKEREITKEKFRNFNEQVTSVVQVHRESVRFETGVATFLLQEVKKTVLPLYQRFYDKYINSDFTKNKDKYIKFTKADLDSFITSAFAPSL Q10357 CCS1_SCHPO BINDING 11; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:O14618" SPAC22E12.04; CHAIN 1..297; /note="Superoxide dismutase 1 copper chaperone"; /id="PRO_0000213547" MFEVEYLIKDCDDVNKNTLEQEFQDLNIEDWKWDAATGQLIVKGSVSPSKVLRRLENATSKPILIRGASNKESGVSILYEANEDITQIPKVYGLCRFIPTEEKIFLDLIATQLLPNREYTGLVTISGDISRGLKSAGDSLVTLFNANSNEQGKIVLDKEVSGSLPNWIGHCFVLKCVDDSDSATMGIISRSAGLGQNTKQICACTGKSLWTEHAELKSVNEGSSCCSKKDSSPSEKPSCCSQEKKSCCSSKKPSCCSQEKKGCCSTEKTSCCSQEKKSCCTSEKPSCCSNGKSTVCA Q10362 SET3_SCHPO MOD_RES 496; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 533; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 575; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 714; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 716; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22E12.11c; CHAIN 1..859; /note="SET domain-containing protein 3"; /id="PRO_0000076313" MWKIRCVCPFEDDDGFTIQCESCEVWQHAVCVNIDANNVPEKYFCEQCQPRPIDADKAHKIQLARLQREEEQSRILSRSRSSNNKRRTSFGKNGASPTHSASPRQGNNTGANGALFSQSTNSSNSGSYRNSVTGATLPNAHAPHSQNRRRRSNHLNNPPEAPITEASNEYVYSFHLEYVPLESNTFSASALEYSKNLDLKNLDESEVLMDGCQVVPISSSKFCCSRFGLVSTCEIPPNTPIMEVKGRVCTQNEYKSDPKNQYNILGAPKPHVFFDSNSQLVVDSRVAGSKARFARKGCQSNSVVSSVYMNGSNSVPRFILYSTTHIAPETEIIGDWTLDISHPFRQFAPGMSRPSFNMEELELLSEVLSTFLSFNECASQDKKNCVFSRVTKYIKAARRASTANRVSVAKDRLSLTPSSTPSTPSPAESLPQPSNPTSVYAKSLKEFWLDKYRLSILQKWPAVKSLPTESVGIDVVMEPKLQPSVKEKKPTKDLQSPLPSVEEDSSNRDKKTDIADLHTDSKVGIADVLSPISPDAALQSDGPLKKAKEPEESSITPTTPPSFNVGESLSRRSASPLQHPRTSPDMLDKTSPCKRGLGTITTVHKKHGSVDHLPSVKRRRSIANDFHGKPDYNKRSLSIERKPEAFKTKGDRPHKVHPSFHRNSDSKLKLEPSSKEKSGSMFFNTLRTVKDKSHVHDTQRSSDVNFSRQNGTRSHSPSVSPVGFSFDKSPVTTPPLPTAPAPVITSRHALVNNQFPTNNPNILDHKANNGDDISNALNTSRSENKPNSNLVQGSVVKPSNTSASALPTSAPKKLSLSEYRQRRQQNILHQQSKDNQAHGDTARPHTVPAATVSNPSFTR Q10366 PIK1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; MOD_RES 202; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 222; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 236; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22E12.16c; CHAIN 1..851; /note="Phosphatidylinositol 4-kinase pik1"; /id="PRO_0000088848" MPSSNSGNELLLRFFESAHFTSQLCVAYLSRYPNNIGIHHFLCEKLATFPYEEIEFFIPQLIHLVLNKDSESVALEEFIISQCEQNTQCALITFWYLQAHMVDLGLQPHSSCFKICKRLYNRIQILVFMSSSSLIQSQQKISENVTPALILSGIMLGGVCVPELLKKAGPIAIAQGRKAPRQDPDESDVDVLRRLSTEPRYSLDVLRSSLNNSIVEQHSEVSLRLKAPELTRTHSYQSSATLSIDEQRRVLRSNYFQQEIQFLFALQDISIRLIIVPRQARLSSLRAELALLNNNLPADVNIPLLRSYHKEVSHKIVRIDPKEATILNSAERVPYLIMVEVLSGELSFEPQSKKNKAKVQKIVSHKNQRKRWFDLTDVDPYTNLQDSTDNDISESESEGGDLSMSPLIKGLVPDTLSLSKSFSSFGNVSLQVPSSHRDTDVVLLSGRHSDSDGNGALKRSKIYASEITARMRAAATMLSQLDAEGSRRPKAETERIKNSIILDMQRLEEERLNEPSIYPVSVDISCAEDLRFGKETQKAERKGDRDDPSAATFQEDWYAKKERIRKSSPYGHYPNWDLVSVIVKTGADLRQETFACQLIYAFQRVWLECKEKVWVRRMKILVTGDNSGLIETITNAISVHSIKKNLTKQLREAELAQGKIAGKNVVTLKDYFIKQFGDPNSSRYRQAQTNFLQSLVAYSIISYLLQLKDRHNGNVLIDSEGHIIHIDFGFLLTNTPGNVGFESAPFKLTADYLEILDDRFDEYRSLMKAAFKSVRKNADQIILLVEVMQNNSTMPCFRAGENTSAQLLQRFQLQLGDKECDDFVDLLIQKANCSVWTRLYDLFQNITNGIY Q10411 SPO15_SCHPO MOD_RES 105; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F3.06c; CHAIN 1..1957; /note="Sporulation-specific protein 15"; /id="PRO_0000072135" MSNQSSSGSNTSDLDEESASSLVSSAASPFIDSDLETPRPNISRASTGQLAEDGDTSSQHEDSSEELKRQEVRGMRRHSDLSIDAKLGSSEGSTASSALPLTPRSPSNASWLLVRGGLLDSPILDINSVTQKSNLLNELKQVRSKLAALEHENGILSLQLSSSNKKDKNTSSVTTLTSEEDVSYFQKKLTNMESNFSAKQSEAYDLSRQLLTVTEKLDKKEKDYEKIKEDVSSIKASLAEEQASNKSLRGEQERLEKLLVSSNKTVSTLRQTENSLRAECKTLQEKLEKCAINEEDSKLLEELKHNVANYSDAIVHKDKLIEDLSTRISEFDNLKSERDTLSIKNEKLEKLLRNTIGSLKDSRTSNSQLEEEMVELKESNRTIHSQLTDAESKLSSFEQENKSLKGSIDEYQNNLSSKDKMVKQVSSQLEEARSSLAHATGKLAEINSERDFQNKKIKDFEKIEQDLRACLNSSSNELKEKSALIDKKDQELNNLREQIKEQKKVSESTQSSLQSLQRDILNEKKKHEVYESQLNELKGELQTEISNSEHLSSQLSTLAAEKEAAVATNNELSESKNSLQTLCNAFQEKLAKSVMQLKENEQNFSSLDTSFKKLNESHQELENNHQTITKQLKDTSSKLQQLQLERANFEQKESTLSDENNDLRTKLLKLEESNKSLIKKQEDVDSLEKNIQTLKEDLRKSEEALRFSKLEAKNLREVIDNLKGKHETLEAQRNDLHSSLSDAKNTNAILSSELTKSSEDVKRLTANVETLTQDSKAMKQSFTSLVNSYQSISNLYHELRDDHVNMQSQNNTLLESESKLKTDCENLTQQNMTLIDNVQKLMHKHVNQESKVSELKEVNGKLSLDLKNLRSSLNVAISDNDQILTQLAELSKNYDSLEQESAQLNSGLKSLEAEKQLLHTENEELHIRLDKLTGKLKIEESKSSDLGKKLTARQEEISNLKEENMSQSQAITSVKSKLDETLSKSSKLEADIEHLKNKVSEVEVERNALLASNERLMDDLKNNGENIASLQTEIEKKRAENDDLQSKLSVVSSEYENLLLISSQTNKSLEDKTNQLKYIEKNVQKLLDEKDQRNVELEELTSKYGKLGEENAQIKDELLALRKKSKKQHDLCANFVDDLKEKSDALEQLTNEKNELIVSLEQSNSNNEALVEERSDLANRLSDMKKSLSDSDNVISVIRSDLVRVNDELDTLKKDKDSLSTQYSEVCQDRDDLLDSLKGCEESFNKYAVSLRELCTKSEIDVPVSEILDDNFVFNAGNFSELSRLTVLSLENYLDAFNQVNFKKMELDNRLTTTDAEFTKVVADLEKLQHEHDDWLIQRGDLEKALKDSEKNFLRKEAEMTENIHSLEEGKEETKKEIAELSSRLEDNQLATNKLKNQLDHLNQEIRLKEDVLKEKESLIISLEESLSNQRQKESSLLDAKNELEHMLDDTSRKNSSLMEKIESINSSLDDKSFELASAVEKLGALQKLHSESLSLMENIKSQLQEAKEKIQVDESTIQELDHEITASKNNYEGKLNDKDSIIRDLSENIEQLNNLLAEEKSAVKRLSTEKESEILQFNSRLADLEYHKSQVESELGRSKLKLASTTEELQLAENERLSLTTRMLDLQNQVKDLSNIKDSLSEDLRTLRSLEDSVASLQKECKIKSNTVESLQDVLTSVQARNAELEDEVSRSVDKIRRRDDRCEHLSGKLKKLHSQLEEQHETFFRAEQQRMTQLGFLKETVKKQEKLLKKLNLRQEQLIPRSSILVYESYIRDIEKEIIVLQERLNGIELSQQLPKGYFGYFFKTNRVEMEVLDSFKQQVAKLQFLAGAEFIVKFKEDLEKCAAEEKEKQATFDNYSEKVENLGKSIEALYFALNREISFRKSLALSKSAYHNLLVRDSPKFNPDSQITYSIPVTNTKQSLLRSAILCVISLQRLRLLGQRHSFCEEVIENLSCV Q10412 RSC58_SCHPO MOD_RES 384; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F3.07c; CHAIN 1..403; /note="Chromatin structure-remodeling complex subunit rsc58"; /id="PRO_0000116597" MNAESCSLILSYISSAPAGNLVLNCTATTNKQTLEANLKSAVYQRYPEFLEDWTNVCVHIIHSYFPKDADYWNVDKLYTSVNRITTLEQSKVVGKEIKNGFTFDAENSTASLENDLQPQFRSHALFMVGSAGPLFSSTARTSRLDSRLPDGGIIAKPVALLPTPSVANSQEYTLDKLSPPSTAKPPASVIEFNPSLAKLPTVKYLQSGPFSSIAPYKNSSSSVIPDSSFHSVACYRASSHYKEAPVEKSIDIDIIQNNLSLLEEDSWTSVPIQGELVELNKLLQHLQLLQNQRITSHNVLSDEERQISVQVQNLILKLAKDYDMSPEDFLMDDFTLSLTQYGAFYRGTLPLSAQPLELPSQQLLRSQSNAALRSNSLSMNGSLSPSSTNVPLQSYRRTTKSRR Q10424 ZIP1_SCHPO SPAC25G10.03; CHAIN 1..330; /note="Transcription factor zip1"; /id="PRO_0000076540" MDFTPNSAINHLNLKFDDVPVSDDFSKDDLAEQLNVFTNPYFLDLEPSSMLSEGYYGFVSQPSGSSNSNKQEKNVQQQNPEKISTLQQVKEEEVSNTFSAPLNATGNFSSANPASIDLAYLDLQKLLTLPDHSKETQEKTSSQRELFEQKSSVASASKDNVSSSSILQGSASSKLLPDQSARQHQVLVGQTAIPTSEASSSINNTPLQAPVSSFADQNAFTNPLSTFASPDLASVSSPSLSSYKGAQSPNANSKRTKATSAIRTAAEEDKRRRNTAASARFRIKKKLKEQQLERTAKELTEKVAILETRVRELEMENNWLKGLIRPTSNF Q10437 BUN62_SCHPO MOD_RES 43; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12B10.03; CHAIN 1..543; /note="UBP9-binding protein bun62"; /id="PRO_0000051493" MQTMSSGIARPVLFLTAREGEYVLKDEFQLGSSSRSTPQITGSPLDPNTPVKRLFFMRINIAQFSRWDYPYPREYIEELKKIHGVHHVEENRDVPSILENYRNSKRKSHNFSSSNTPYLKLHRPASRAGAPLINAKSFISSLTFHDNIVRSFQPSIHGKTFVFANHEKSFYWLDVSAANSHSALLKMEFPRASPVCHDINSFTKSPKGLDVIIGFDTGDVLWYDPINFKYLRFNKNGQLNSSSVTAIKWVAGKDSQFLVSFRNGWLVLYDKYRHEQPLHIVVPEKNLKSLYLSSPGTFNILISINHRDDRKLNPVACYAFSKSPINGFCFSPDYQYLALVSERGTLKLFDFVKEHVLDVFHSYFAGLTCVTWSPDGKFIAIGGKDDLVSIYSFPLRKLVARCQGHKSWVTDVIFDAWRCDDDNYRIASVGLDRKLLLWDFSVSAIHRPKSAVYYVNHHSNNSKPAISDFDDVGDLTMGSEIDNSNYVNGDITIHPTLSRSLIPVISPITIYDVDDSPLSSVFFDPDCMITCATNGRIRTWQRP Q10444 EXG2_SCHPO ACT_SITE 338; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 439; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; SIGNAL 1..?; /evidence="ECO:0000255" SPAC12B10.11; PROPEP ?..47; /evidence="ECO:0000255"; /id="PRO_0000007895" CHAIN 48..570; /note="Glucan 1,3-beta-glucosidase 2"; /id="PRO_0000007896" CARBOHYD 91; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 116; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 121; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 184; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 203; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 248; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 364; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 525; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 552; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSNLLEAESSCDSKSLGVDDFTSKRCREIDKKALLITILLTFFVSLCVFLSIILPLIFLVIIPHAQSDRKIKDTNMETTNLGVNIIDEIFNSTQVPEWAKNSLLDTNTWLDTSDFNTSFTNETFAGLYTMGIFDKYDDSVQANPNVPPLNEPFPYGRLPIRGVNLGGWLSMEPFITPSFFQVKNETAYLVKDELSLHAYLGENATSVIENHYNTFVTKQTFYEIREAGLDHVRITFPYWILYSNEITNVSGIGWRYLLRSIEWAREQGLRVNLDLHAAPGNQNSWNHGGYLNQMEWLDGTVKGEENSQFTLKIHERLASFFSQKRYRNVVTIYGALNEPNFFVLDEHKITDWHKQAYAVIRQSNFTGLISLSDGFRGPGNWEDHFDPFHFPNILIDVHRYIIFNDFLIGLRPKDKLNVICKSWNEEMKLKAKLPTIIGEWSLADTDCAKFLNNVGEGARWDGTFTPNGGVASCSEKVGCRCDFANQDPENYEDSYRKFLYALATSQIETFDKTWGWFYWNWDTENATQWSYKKSWLAGLLPRLAYSTTKDFNCSMLDSKSFMEFDEQSEF Q10474 LYS5_SCHPO CATALYTIC ACTIVITY: Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7; Evidence={ECO:0000305|PubMed:15546125}; SPAC17C9.02c; CHAIN 1..258; /note="L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase"; /id="PRO_0000116616" MKQKVYRLLIDTQEAWPFERTRIPSFKKLSDSERQQIERYYFDMDAKMALASILIKRHLVSTALECSPNEVQISVTKAGRPYCQSAHCPPIIFDFNVSHYGGIVIVVGAWLPSDPSGMRPINIGVDIVECKPLAFEASWMEDFMSVFTPCEWKLIKSSISSIDVFFLLWTCKEAILKALGIGLSGNPLDIVVTFHKLNELLNSEEVSLRRAATAVYSGYSWDLEIHKLILHSSTFYVSVAFPQDCVIMDLNWETLNDL Q10489 ODPA_SCHPO BINDING 109; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 135; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 135; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 136; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 136; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 174; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 182; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 182; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 184; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 184; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 213; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 213; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 213; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 214; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 214; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 215; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 215; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 242; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 242; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 242; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 244; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 244; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /evidence="ECO:0000250|UniProtKB:P08559"; BINDING 309; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /ligand_note="ligand shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:P08559" CATALYTIC ACTIVITY: Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P08559}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P08559}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 6; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 306; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 310; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 312; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26F1.03; CHAIN ?..409; /note="Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial"; /id="PRO_0000020451" MFRTCTKIGTVPKVLVNQKGLIDGLRRVTTDATTSRANPAHVPEEHDKPFPVKLDDSVFEGYKIDVPSTEIEVTKGELLGLYEKMVTIRRLELACDALYKAKKIRGFCHLSIGQEAVAAGIEGAITLDDSIITSYRCHGFAYTRGLSIRSIIGELMGRQCGASKGKGGSMHIFAKNFYGGNGIVGAQIPLGAGIGFAQKYLEKPTTTFALYGDGASNQGQAFEAFNMAKLWGLPVIFACENNKYGMGTSAERSSAMTEFYKRGQYIPGLLVNGMDVLAVLQASKFAKKYTVENSQPLLMEFVTYRYGGHSMSDPGTTYRSREEVQKVRAARDPIEGLKKHIMEWGVANANELKNIEKRIRGMVDEEVRIAEESPFPDPIEESLFSDVYVAGTEPAYARGRNSLEYHQYK Q10668 SWI2_SCHPO SPAC1142.03c; CHAIN 1..722; /note="Mating-type switching protein swi2"; /id="PRO_0000072349" MNVNKKQESIPVNTGSESISSNDNERFEQGKGVGSNLGSHFFEPVEYYYSDGKPMNQTEASQMKGTFSRDFSLNEMNNEFITDSFFCTTTPDPKTESPSFVKYNAHCDDHPEISGHVSSNDKDFAYFEDKSENQPLVTLPNENNQVIEPLSSQSCKSQLSTQNYSESDFGWNQLCDLDPIFKSLAFTDDTNLFPAFADSEAALIMLKKREMTRVKHRAGRPRKYSYVNKDLNFEEGLPRRRGRPTGWRKYPEKEEIYPTLSPRIKKPRKVFDAVVIPVTIKPSIYTEPSLPHHIDWNNGCSEEFDFEPSREDEDFPDLTSDSTGQDPLSSEPTIFDISPLPSDMEPTFSENSLITINKMAIEERKQSRRLEQPLAESQHQEDLLNPYGVDQDFDETCINESEQQATHIPNSSIKFNYDYTPPKSATSHKHKRVDLLASRKENVWTGLYGKVQTEMVSNRGEAVLNENNSKNRTNVTKPNSYKNSVLSIGNNHSNHSNIIKPNTYKNTILSNENNTPNYSNVCLSTSLINRSLPSLKSTMHPGVNKDLITRPFKNVNKMSVRKALIKPFHPPISKISRTRLTVSSPERLYCAKPISMATAPSETDSKLINRIRNLELEIGGLKEQLSVVELALDTDKNSKQIQVVERKIQNWRKSAQLAVEVLFPVFSLKFTTMLQEVPQSVLRTSANDLRTKPCSIGTYLEQLQIPFHLLQYNSETESWDLE Q10719 FUS1_SCHPO SPAC20G4.02c; CHAIN 1..1372; /note="Cell fusion protein fus1"; /id="PRO_0000194902" MMTASFKGIRISKPIVKEISSFGSLTNIDLHTDPYEKVEAKALSRSRLKNQSVKKTDLRITNDYSSLFVSIENKKNTIPDIHCNNLSKRPVGFTDSYVPGEALLCPDDPNLVNELFDDVLKRLREEKSDSGEQFHWDANVTLSQENKWSFITGYLSRNDKFLKISSNDSELNVKASVISYIEKLSCTPLKLKYVESLAVALRTESVTWVRYFLLMGGHIVLAKILQAIHEKKHLKSPDITLEIAILKSMRCIIGQKIGTDFYLSNKYPIDSVVHCLLSTKLLVRKLAAELLTFLCYSEKPNGINAIMKCMKNFANLKVESMNVFDLWLSQWKRTLLEKVVTEEKKVLEEAALHDKITIEYIISQMLLINAFLENIPSKTALLQFKESLRIGNFKSILLILKKINDEGVLKQLEKCVKLVSLDTANEKHFLKHTPNSAAHQSLLNTNMFNDANFEFMVKEHIKNFLKLLKEHNNPVRIIKLLDCLVLTLQADKGNGNSNNDIDCFYKELKIGNEQGNNAPGYSSVTSGYGTTNSKKVVASYDNTDDNEYSVSKSELYATGDTNNTTNQGYENSERKYVESSKYETDLKNIFDCLCLLFPSEFDPQSSFSAEKIFSKLKHLLTRTRDSYISEDTKILRLLNRSSSKLQDRDQEYLISKNNVNGNGNRDWVQPVNTTSSVSAFASPRIKPKLLFQPNQDEKLKLCKLDLAKANSITLKSEPSSAVSTHSFEVHLSMPGTQIKSANLAEKMETSKHKVFNPKRIDVVSDLPLDYRKSYYGRFSITDTKRFSKIENMRIKEVIDGNPFKAPPPAPLPPPAPPLPTAMSSLQKFEKNDSQIFRKTIIIPENISIDDIFKFCSGSESEVYASKIPGELCNPSKRLKQLHWKRLEVPFEKTLWNIVVADPYLLTLKLTAEGIFKQLEDCYPLREVTVSNKKVKEYTGFMPVDLQQMVSIRLHRFNSLTPIEIAKKFFHCDHDIMELVDFFNDRKFFRQEGLKKQLKPYMSSRNEEVMEVSEKLLELSRFDQIYTLIVVDIDTYYEKRMAALKIKSFLANNFRDFRRQIRKLHCASLELKSSLHFKYFLNLVLHIGNFMNDAPRRAKGYRLESLLRASMIKNDKTGLTLLHTIEKIVRTHFPQLEAFLVDLKAIPEISRFNLEQLEQDCNDICERMKNVEKDFSNEGIFSNHKALHPDDHICEVMVPWIPSGKSMVDELNSDITELKTTLKTTLLMYGENPDEPTSSARFFNNLNEIILEYKKASTVNQKMEKEEELAFLRLQALKASVKSNNAENSGSSKNEEVSATMENLISQLQKGLCDDSLSNKTDCTESSKQTIETLMNYENDKQTLEGSNKKRQTVVLKAECMLKQLENNNELKR Q10752 CDC28_SCHPO BINDING 441..448; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC19C2.01; CHAIN 1..1055; /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28"; /id="PRO_0000055154" MSLEQYVSDKAISLLGMSEPSVVEYLIAEAKGSSSSNNLYQKLVSFGMDGDDPAVKEFAHTLYARIPREGSRPKENYNARKKKEQGILQMERLNSSYDLLIEPQSHETPGKPLKKKSRSKTPKREIARRQRDEDEWESDEYEEVVDGSASHPIEEDSVSTDFQNHDYEKSSDPETERLNDLREREEFEERLRRKDLEAATNEFVEDYSSKFSSEELALRKLADDPESWRKLASELRKKSRQQYLKPRAQQQLEILRREIRDEEQLFAGEKLTQAEIRELEKKKELLRIAEERQRLEKQATEYQMPEDYFTEQGKLDRKRKEEVLYQRYKDSNEGEQNEVTMGAAEQQRWEAQQINKALLFDQNEWLPPGEKQFDFVFDESQQIDFLLDTKLSAENPVDTDKMTDVKVEKSLESSRKSLPVYQYKDDLLKAINEYQVLLIVAETGSGKTTQLPQFLHEAGYTKGNKKICCTQPRRVAAMSVAARVAKEMDVRLGQEVGYSIRFENATSEKTVIKYLTDGMLLREFLTEPDLASYSVIIIDEAHERTLHTDILFGLVKDIARFRPDLKVLISSATIDAEKFSAYFDEAPVFYVPGRRYPVDIYYTPQPEANYIQAAITTILQIHTTQPAGDILVFLTGQDEIELMSENMQELCRILGKRIPEIILCPIYANLPSELQAKIFDPTPPGARKVVLATNIAETSITIDGVNFVIDSGFVKQNMYNPRTGMESLVSVPCSRASADQRAGRAGRVGPGKCFRLYTRRTYNNELDMVTSPEIQRTNLTNIVLLLKSLGINNLLDFDFMDAPPPETLMRSLELLYALGALNNRGELTKLGRQMAEFPTDPMLSKSLIASSKYGCVEEVLSIVSMLGEASSLFYRPKDKIMEADKARANFTQPGGDHLTLLHIWNEWVDTDFSYNWARENFLQYKSLCRARDVRDQLANLCERVEIELVTNSSESLDPIKKAITAGYFSNAARLDRSGDSYRTVKSNQTVYIHPSSSVAEKKPKVIIYFELVLTTKEYCRQITEIQPEWLLEISPHYFKPENIEELQKTQKRHKR Q11004 PPID_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPAC1B3.03c; CHAIN 1..356; /note="40 kDa peptidyl-prolyl cis-trans isomerase"; /id="PRO_0000064177" MSTYAYFKISIDGKIQPTIYFELFDNVVPKTVKNFASLCNGFEKDGRCLTYKGSRFHRVIKNFMLQGGDFTRGNGTGGESIYGEKFEDENFELKHDKPFLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGKVIQGKSTVRTIENLETKNDDPVVPVVIEECGTCTKDQIEAPKPDVTGDSLEEFPDDYEGDKSETAIFKIASDLKGIANKQFAQQNLDTAVAKWQKALRYLMEYPVPNDDSKESPDFWKEYNALRYSIYANLALVALKQNKPQEAIRNANIVIEASNSTELEKQKAYYRLGCAQGLLKNFEESEKALAKAGNDPAISKKLAEIRQKKKDYKKRQQKAYAKMFQ Q11119 UBP14_SCHPO ACT_SITE 309; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 730; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 28; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 41; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 56; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 60; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 153; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 155; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 174; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 177; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 186; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 189; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 194; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 207; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 211; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 217; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 236; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 239; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 456; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC6B1.06c; CHAIN 1..775; /note="Ubiquitin carboxyl-terminal hydrolase 14"; /id="PRO_0000080613" MSCPHLTETNVVIPDNSQVIYREECVRCFNSQDEEGGIDLCLTCFQSGCGETGLKHSLVHFEQTLHPIVVTIARQPKQKINDEPPQKITKLEIREDSDEDLYDYFYVPKCLVCNIILDIQDPLLSLSLEAMKNATKASNKSQLTAWENELTTCDHIINLPENETYVTNLDNATCSKCDLAENLWMCLTCGALSCGRKQYGGGGGNGHALSHYDDTGHPLAVKLKSISPDGQADIYCYSCDEERIDPNIKTHMLNFGIDIAKLNKTEKSLAELQLEQNLNWDFGASEEDDASKRLFGPGLTGLKNLGNSCYLASTMQSLFSIKEFAIHELNLFNTYNSVCQTPTTDLQCQLGKLADGLVSGKFSKPSKIGLLNNPSSSILPYQDGLRPFMFKDVVGQGHSEFGTSQQQDAYEFLLYLLGKIRKSSIAKTDITKIFDFETEQKLSCLSCKRVRYSSFSSQGLTLTVPRVKIGEIEGEQIYEEVSIDQCLDATIQPDQMEYTCEACKSKLGATTTTAMKSFPKVLILQANRFDLQGYQVKKLSIPIIVNEDGIYNFDRLMAKDHPNDEDYLPEKTETIEWNQSAIEQLQAMGFPLVRCQRALLATGNSDTETAMNWLFEHMEDPEIDKPIEVSELLPKADSSVSEENVQSLCEFGFTVAQARKGLLESNNNIERAVDWILNHPDESFEEPPLEGSDSSIKNENMGSWESTNVPVNYNLKAIISHKGSSAHAGHYVAFIRKEIDGKQQWVLFNDEKVLQVASLEEAKTTGYVYLFERLD Q12381 PRP1_SCHPO MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC6B1.07; CHAIN 1..906; /note="Pre-mRNA-splicing factor prp1"; /id="PRO_0000205755" MANFYPDFLNMQPPPNYVAGLGRGATGFTTRSDLGPAQELPSQESIKAAIEQRKSEIEEEEDIDPRYQDPDNEVALFATAPYDHEDEEADKIYQSVEEHLSKRRKSQREKQEQLQKEKYEKENPKVSSQFADLKRGLSTLTDEDWNNIPEPGDLTRKKRTKQPRRERFYATSDFVLASARNENQAISNFAVDTQAGTETPDMNGTKTNFVEIGAARDKVLGIKLAQASSNLTSPSTIDPKGYLTSLNSMVPKNANDLGDIRKARKLLQSVIETNPKHASGWVAAARLEEVANKLSQAQSLILKGCENCSRSEDVWLEAIRLHPAAEAKVIIANAVKKLPKSVTLWLEAEKLENQAQHKKRIIKKALEFNPTSVSLWKEAVNLEEEVDNARILLARAVELIPMSIDLWLALARLETYENAKKVLNKARQTIRTSHEVWIAAARLEEQQGNVSRVEKIMARGVSELQATGGMLQRDQWLSEAEKCETEGAVITAQAIINTCLGVGLDEEDQFDTWLDDAQSFIARKCIDCARAVFAFSLRVYPKSEKLWLRAVELEKLYGTTESVCSILEKAVESCPKAEILWLLYAKERKNVNDIAGARNILGRAFEYNSNSEEIWLAAVRIEFVNNENERARKLLARARIESGTERIWTKSISLERILDEKDRALQLLENALKIYPHYDKLYMMKGQIFEDKEQIELARDAYLAGTKVCPYSIPLWLLLAKLEEKQSVIRARVVFDRAKVKNPKNEFLWLELIKMELRAGNISQVRAALAKALQECPSSGLLWTEAIWLEPRAQRKTRATDALRKCEGNAHLLCTIARMLWLEKKADKARSWFLKAVKADQDNGDVWCWFYKYSLEAGNEDQQKEVLTSFETADPHHGYFWPSITKDIKNSRKTPQELLHLAINVL Q1K9C2 MET5_SCHPO BINDING 1328; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P17846"; BINDING 1334; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P17846"; BINDING 1373; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P17846"; BINDING 1377; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P17846"; BINDING 1377; /ligand="siroheme"; /ligand_id="ChEBI:CHEBI:60052"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250|UniProtKB:P17846" CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000250|UniProtKB:P47169}; COFACTOR: Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250|UniProtKB:P17846}; Note=Binds 1 siroheme per subunit. {ECO:0000250|UniProtKB:P17846}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P17846}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P17846}; SPAC10F6.01c; CHAIN 1..1473; /note="Sulfite reductase [NADPH] subunit beta"; /id="PRO_0000316860" MSVKASINNSQEAVSRIAFRCSDALYVVHPNNSILNGALTESLKDLKKFETLNVSGKVPHVLPLKSHADPFAHIADAILAEEEVASTQPKQITSVVASADALFFATPHLYKLAHEPLVAHVAIESTEAFDFASVRDTGFVILFSGNRPGDSSEAALEDTLETASLAHRLALKLNTGVLHFYSPVYDTTAALENIETLPSKEDAQHARVAHIPIEEKQEDSEKEGNIKEAFVPPKFDQPERDAATSEYLESLSIKPFEYSGSDDATDVLLVFGSAASELAKAAVTSSVAVAIVRVLRPWLPSKLQEVLPTSTKRLTVLEPITSLPRKWDPLYLDVLSSFVASGSSIELFAVRYGLSSSEQATEIIKAVRDNLSGALKPSLVCDFTDGVSQVFVPTPPSIEEAYHKLLHRVFKSRLNIVNDPASSATKQNIPSRLIISPQFALGSVLEYENQRRAFCDEVATLLKEKNSSVSSESLEVLSNWIVSVDNLESPVDPELVISELKKDSSAPIKSLLDRSEFFTNVSHWIIGSDAWAYDLGNSALHQVLCLEKNVNLLIVDTQPYSTREAVRSSSRKKDIGLYAMNFGNAYVASTALYSSYTQLISALLEADKFKGPSVVLAYLPYHSADDDAITVLQETKKAVDIGYWPLYRWTPALEDGEYSDFKLDSERIRRELKTFLERDNYLTQLTLRVPSLARTLTQSFGAEVRHQQNVDSRNALNKLIEGLSGPPLTILFASDGGTAENVAKRLQNRASARGSKCKIMAMDDFPIEELGNEKNVVVLVSTAGQGEFPQNGREFWEAIKGADLNLSELKYGVFGFGDYEYWPRKEDKIYYNRPGKQLDARFVELGAAPLVTLGLGNDQDPDGWETAYNLWEPELWKALGLDNVEIDIDEPKPITNEDIKQASNFLRGTIFEGLADESTGALAESDCQLTKFHGIYMQDDRDIRDERKKQGLEPAYGFMIRARMPAGVCTPEQWIAMDDISTKWGNHTLKITTRQTFQWHGVLKKNLRNTIRNIVKVFLTTLGACGDVARNVTCSSTPNNETIHDQLFAVSKQISNELLPTTSSYHEIWIEDPETVEKRKVAGEAVQDVEPLYGPTYLPRKFKVGVAAPPYNDVDVYTNDVALIAIIENDKVLGFNVGIGGGMGTTHNNKKTYPRLATVVGYVLTDKIMEVVKAILIVQRDNGDRENRKHARLKYTVDTLGVSTFVEKVEEVLGYKFEEARDHPQFIKNHDDFEGWHKTEKNKYWRSIFVENGRIENNGILQFKTGLRELAERLYTEKSEAEFRLTANQHVILFNVAENELGWINEHMAKYKLDNNAFSGLRLSSAACVALPTCGLAMAESERYLPKLITKVEEIVYEAGLQKDSIVMRMTGCPNGCSRPWVAEIACVGKAPNTYNLMLGGGFYGQRLNKLYRSSVQEKEILNLLRPLIKRYALEREDGEHFGDWVIRAGIITAVENGGANGAVHEGVSPEAF Q1MTN9 RLF2_SCHPO SPBC29A10.03c; CHAIN 1..544; /note="Chromatin assembly factor 1 subunit rlf2"; /id="PRO_0000372425" MNSESVDSDVAASTSNKGNELCSSSTDITSLSVSSPNESVIHSSHSASEADEYVCKLSYEGNRKKRIYNGSAEAGKEKKLQKQRAQEERIRQKEAERLKREKERQQREQEKKLREQEKIAAKKMKELEKLEKERIRLQEQQRRKEERDQKLREKEEAQRLRQEQILNKERQQLKLNNFFTKGVEKRIAPNENFVADKTDELNEFEKEFRPFFIKHQMSLSKYPSPNESDSFLDEVLSTSKSYPLKLNDIFTPSDAVSSANSLGVSNRNSENEVRQLMSAYQDPSVSKPQEILSCLSQIPIKFIFFYQDVRPPYFGSYTKTHSHGSNVLLNPWLEDEDIDYTYDSEAEWVADEEDDGEDLESEDEEVDNSDDIVEDGDNAFVDDEDDDKDSVNASNTHRSSGPLEVIVEGPVWDSKFLPDFNCLSLIEPISSFSASTYLQIDPKEDLWASQDTAPASSGMTIGPTSSLSDDLQVRFPSEDIPKFIEYVRNSHDNKVFLIENLRHMFPYVTKNIISETLGKVAVRKGKSVSDGWIIKENFASLLSS Q1MTR4 CTI6_SCHPO MOD_RES 187; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1685.08; CHAIN 1..424; /note="Putative histone deacetylase complex subunit cti6"; /id="PRO_0000303917" MPSNSTPANEEKEEESEKIQKSPVDTPHTPNGSVSDNEENETSSTGEVTRCVCGIVESDDEASDGGLYIQCDQCSVWQHGNCVGFADESEVPEVYYCEICHPEFHKVYQRGRGAKQSKYLGNGKPIEASQTEESSSTPPSPATKKSSKQRLTMNSRDAALDYEEYLAIAKEKSLIPRRSRGRTSSKSLSPPAPQDESQGTEINLKQKIEEENDEILEDSKESKDENEENKETSTTNVAETDAPEEETVDTVEEIADEEKHSVKEESGEASPQSSQQSTITSISTTTRSTRKAKREAAAEDKADLPAAVAPKPSKTRKVGGRRGKSSSNDNHRIPQLHPDGTFVETITKPKGLHSRITMTEMRRRVASMLEYIGHIQVEMAAQSAGNQSSTKSSKEGPEEEKETLRMVDNLTRDLLHWEQRFSRT Q4ZGE1 EMR1_SCHPO SPAC8C9.19; CHAIN 1..61; /note="ERMES regulator 1"; /id="PRO_0000343165" MLPNLRRIFASFRTEEEERSYSRKAFFHLIGYITCSVLFSWLVRKKVISSPVVSSPIHALS Q50HP4 DAD4_SCHPO SPBC3B9.22c; CHAIN 1..72; /note="DASH complex subunit dad4"; /id="PRO_0000176051" MNNPMEEQQSALLGRIISNVEKLNESITRLNHSLQLINMSNMNVELASQMWANYARNVKFHLEETHTLKDPI Q76PD2 HEL2_SCHPO CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q05580}; MOD_RES 482; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1223.01; CHAIN 1..732; /note="E3 ubiquitin-protein ligase hel2"; /id="PRO_0000353800" MSPSGPNLNNKEHNRASEKKNSRTHNKKTNRNQSKEKPVSSRSVETPKNAVCLEPVGTDPVSNVATVDASKEEQDEDEQICFICAEGITYSCVLPCNHRMCHVCALRLRALYKTKECTFCKTEWDTVLITKDHEIDIHDVDLAKLPFQDEKLGIVYSDEHAQEESNLLLQFNCPEDACDITCKGWFDLKLHAKVKHHKFFCDLCVKNKKVFTHEHTLFSKKGLTKHNEVGDQGSDLEITGFKGHPKCEFCNTHFYDDDELFKHCREKHERCYICDQVAGRPTHQYFKNYDSLERHFEKDHYICRERECLERKFVVFGTEIDLKAHQLDEHPHNFTQRELREARRIIPQFSYDPPGASGRNRRERTSSTPSEQSTSVNETANSLSNLHLSRGEIAHLRQEEYVREQQARHRDFGFTLSNPAPTSARPATSTRTISRGKTRTLRNEDFPSLAEVANQNSSSAPSVPVSAPRLSGKSASRNHVPSPPKGTKSPMASSEQAQHQQVIDRMQKLTNYDDHKINDFKFAVSSFRGNVMPAREAVARITKLVAKPHEQLSGVFNQIANLLENKEKSRELLEAWQEWKILNAKDDTRIGTTNSNLLRLKRSNRTAAQTASVWNRIERAAAHDGPSLSAPSSSINLANITSRPTNSSAANTPSWGVRKARASALNARSEEDFPALPPSTSKRISVQLGKKQARPVDSWGSTPNTSSNRNSNTMGVSKKKNGKKQTVLFHIG Q7LKX0 ELOH2_SCHPO CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000250|UniProtKB:P25358}; SPAC1639.01c; CHAIN 1..365; /note="Putative fatty acid elongase 2"; /id="PRO_0000350770" CARBOHYD 17; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 65; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MPDSPTLHHNHIIGLENGSLTSNNNHQGMASVSVGQFQYPIWSWLNSLADATFGKRPSSFEFIVNKTRFSSAPVVATIIISYYLLILVGGRIMRNRQPIRLQKIFQYYNLTFSIASAILALLIFEQVAPAIYKHGFFFSICNEKAWTQPLVFLYYCAYISKFLELTDTFFLVLRKKPLQFLHCYHHGATAVLVYTQIVGRTSISWLIIEINLLVHVTMYYYYYLVAKGIRVPWKKWVTRFQIVQFFADLGFIYFAVYTEVAYRLKFYKACMGHCSGHPLAAFCGLATISSYLVLFIVFYHNTYKKNAALKMKAKAAAATKGNSSESSKNADLKRLSKSNASIAEVKCNNIVTNLYPISSGLNNEK Q7Z992 SST6_SCHPO SPAC11H11.01; CHAIN 1..487; /note="ESCRT-I complex subunit vps23"; /id="PRO_0000353847" MSDHAINEHPSRILNTIEKIRFWKNGLAEELELLFRKQCEDTFTLQAINIEVDTQDENKIEEVRIYLSTPAFDKTILTSACITVRSYYPSQPPIVQLLDEKGGKHKYTSLLLQLWKNERSVFNIYRLVQALIKQDFEREHTSPPELPTKLVNTIEKLKVKEENEAPPVIPAKPFSSSSEQHFRKVPALPSKLPPKPLKITANSSLGQETNSNSSSFQSTLFSLNTAPFSATSQQLVHDSVSLRRPSSNIPAQKPIPPKPEQNEIIITKDTPSLKDKYSKPALLPQKPKVSKGQIVQQVSVFSTGKKIESQSLLNLIDTDIETPLKGSSELLYSEDFKPNVDPVKIQQILHKQNKIIEEKWISQIRISKNLEVKQRLLDQERHALETLAKNIENNRFILGKRRRKAREALQKLDNLKDLSVQELFIIPSERELKYYELKRKDEKLDEGIRALNQALHHESIMPASWLKGIKLLARQQFLIRDEMLQYS Q86ZU7 CO112_SCHPO BINDING 323; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0"; BINDING 329; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0"; BINDING 342; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0"; BINDING 430; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:Q9H7H0" TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: Specific enzymatic cleavages in vivo by mitochondrial processing peptidase (MPP) yield mature proteins including rsm22-2 and cox11-2. {ECO:0000269|PubMed:16835444}. SPAC19B12.13; CHAIN 40..753; /note="Rsm22-cox11 tandem protein 2, mitochondrial"; /id="PRO_0000352839"; CHAIN 40..568; /note="Ribosome assembly protein Rsm22-2"; /id="PRO_0000352840"; CHAIN 569..753; /note="Cytochrome c oxidase assembly protein cox11-2"; /id="PRO_0000352841" MPILTCRYKILFLYNLRNCFTFQNQRCLIPYGTTTTIRWYNANFQAVQNNFSDYKNELISSHRPEASSLLDFLVKDQKKSGDISLHTKFNLYVDDLLKKSEKGQIKKFINDIKKDLATESQLPLSAPFKDESTRTMTDPQVLAYIHQSMPYQYASLYSVLTDLKIVNSDVSCKSQHILDCGKGPGIGALASYSVFPTPNSVSIVEENPFLKKIIYDIHHNIYPSTSPNPTSPVTLNRLPLGKKDSYTLVIASNKLLEMKSEKELFDYLRSLWSLVSNDGGLLVLCERGTKRGFSLIQRARTFLLQKSKNTSDKQFNAHIVAPCPHDGRCPIDIENGVRANICSFKQHFFLSPFSRLYVPRSHRRSSDRSHYSYVVIQKGITRPLNNTTQRFKNDEDLLENVNVTSPTLKNWPRIIRPPLKRDGHVIIDVCDSDARLRRNIVPKSQGKLAYRLARKSAWGDLFPLEGKVQSTSPSSKITKHLKDASSTYSINPPSYNKPKVERNTTADPIFVGKRFYSTNRHKAFSRFADFNSHRFPCIFTSFSCYNCISGTRNISRQYSRDKFHYNQRTTIYYLVAISIFALGLTYAAVPLYRLFCSKTGYGGTLNTDQSRMNAERMVPRKDNKRIRVTFNGDVAGNLSWKLWPQQREIYVLPGETALGFYTAENTSDHDIVGVATYNIVPGQAAVYFSKVACFCFEEQKLDAHEKVDLPVFFFIDPEFADDPNMKDIDDILLSYTFFEARYDTNGNLLTKLN Q8TFG6 PPK18_SCHPO ACT_SITE 690; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 572..580; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 595; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAPB18E9.02c; CHAIN 1..1318; /note="Serine/threonine-protein kinase ppk18"; /id="PRO_0000256819" MVMQERNSNEDNKVNHGIDNIYVLELDLDGSVLFASTNFSQITGISSLELTGKPAALLSSDQEIFNAAIEQLLDDDSHSVKIHTVISKLPSLEENVFVQDEEMELQSKSVELDCVGVLIRDPLTSRPSHTLWVLQPLKPTRITRQEIGQQLTETLGFGAQLLAQHLEKLQTVPSTDSLPPFETVLCRVCDHEIQNWYFEHHTELCLLIHHAEARAQEANDLLNEQRNALQSLLDSLDDQIEPDVSYLGVPLAAVLPSSITSSAKSNSRSSLSQKIRNYISNMLFDAISYTDSCLAIHLPFIPESTTREDNQPFSEIRLLSPASEVFNAKTLSWCLPHIDDPGLQLMFENTDALVKKKLDAINRLSNIIYYSERVRCEIEDQVQTIIEQSIQVDGYDEPLSTTTPTLIEPIQETLMTQSPIIECEPFNTVKPSVSPEEVHDISQFNHRNDPPITAASVDSSNSFSVHRSSTNHSSTNSGSPNLSRRNNLAIPIASRRKSVSAVNTLYGVGSSYTSESFPFSKLTVPVERNSFRETESPKPFLSRQIGISTLSSNISSGKGTPSIQDYEIIKPISKGTFGTVYLSRKNTTGEIYAIKVLRKVDMISKNQVANVKAERAVLMAQEESAFVAKLYYAFQSRDYLYLVMEFMNGGDCASLLKSLYTIPESWAKIYIAEVALGLEHLHRLGIIHRDIKPDNILMSITGHLKLADFGLSQLGLTTRQLRLQKGKNNILSPPSFQSPTALGDPGDNIASSPLILPTSVSAFSYDEKSQKQKTELATFTTYKEDDTTTTTRTSIDSISSKYLESPVDSQKVNRTPNLQSVPFFRQPDAPKRFVGTPDYLAPETLRGSTQDDMVDWWALGCVLFEFLFGYPPFHAETPEKVFENILANNIAWPDLEMYPCSEEALDLINGFLQPNPERRLGFSDINEIKEHPFFNGINWDDIFSHEAPFIPAPETPLDTAYFDSRGAGAAESNMSSSVNSGEEVSKDNNVSQERGSQFLRSSHGRSRERSTSARRSRRFSEANSEFDEFGPFSYKNLSVLERANRNAIEKIRSEIAGKLHISPPDPHIGYTPGSDMPSAKLYDQQLTLSPSLMTNQGSNFSSTDSTPRKSINSSDVESRSKTDGPKSMHDLIKQLHMRKHSSHTNQSTGSSESDDLFNLDLPISNLETSYPFKIEEGQASPLSSPLSKTPPFFSSSVPLKALICVSKLNLFSELIKLLKSYKFQVSIVTDEDKMLRTLMADEKFSIIFLQLDLTRVSGVSILKIVRSSNCANRNTPAIALTPTRIDINAAIPRMFDGRLYLPINAFLLRGYIARLCNK Q8WZJ8 RPC7_SCHPO MOD_RES 103; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC839.12; CHAIN 1..210; /note="DNA-directed RNA polymerase III subunit rpc31"; /id="PRO_0000352832" MRRGARGSTNLGGMTWQEVLEFNANSTPTKLYPDRDIPLQRSIRPEELLELRFYKEIRTSFLDESAFYIRRNPISVVQRNEDGLVRYSDRNKPKRKNDNLSLSDLDLDPKFFPEELRKTLGAASATGRKRARRKLDMKTFIDFTIKAQDLKDESSEAAHPNIEEEPDEGLEEEDEDFGDDDDNDYGENYFDNGEGDDYDDYDGDEGAIYE Q8WZK0 US107_SCHPO SPBC839.10; CHAIN 1..695; /note="U1 snRNP-associated protein usp107"; /id="PRO_0000082027" MQRQNTQAAGMPMMPQVPMVGNGVPYVVPIQPVFAPLPPDYRSLYKKLYGQGAFLVDNPVEASSPYDFSQPILKFGKLPIKQVLRDNESQQKDRKNLPRNQKSNEIQEKQTFQTPSSEKSTTERESRPFVPPNSQQMRRMLFIGNIPKELDDFWMDKILRLSGKLASWRRVADADNSMTSFGFAEFESNEQFSRALEALNDFVVPPLYEGGPSTRLSLITDVENEGLYREWQTSRYARNKQKEINILQQIRFNLERICQDIGNFDVRSRIERAARQAREKNEKLLQNVKTSEIPINAADLEGINPELLPVIEEEIRSFRDQSAMKKREKQRSKDEYASLYKEYTRKEQEKLRKQNDDLQNLLSKHRISRIPMSTVNAFLRAEDSIPESFSDEQAYYEEKRRKDQLEAEEYYARERRWMNREKARTAALEREAAREEEERVNNTSFGTYLSEKLASFDDDEEARVSRDEYFVDRAAWIRHRAVARAREEDADALDRKEEERELRTRGEGATVETENYVENGKLVTSEMPQHENGPFKIKIQTKKPAVPSERREFGLPERLLLEEEDEEPQGYSPNPQKPKPAMEENDAEKTKRLRSLIEKIPVEAESLWALPIDWSKVTEDLLKEEMQAFVTKKIIEYIGIQEDSLITFTIDHIRQHKGAEQLVSELDLALAEDAPEFVSKVYRYLHVLLILRSEA Q8WZK2 MCD4_SCHPO SPBC839.08c; CHAIN 1..935; /note="GPI ethanolamine phosphate transferase 1"; /id="PRO_0000024106" CARBOHYD 86; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 134; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 315; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 398; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 925; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFGRLLLLGILFHVVFLKSIFDIYFVTPLIHGMKQYSAGEAPAKRLFLIVGDGLRPDKLLQPHSEKVIGEEQTYAAPFLRSIIQNNGTFGVSHTRVPTESRPGHVALIAGFYEDVSAVTKGWKKNPVNFDSVFNQSRHTYSFGSEDILPMFSEGASDPSRVDTFMYSSELEDFSSNGIVLDEWVFDRLDELLAQSLEDKELWDMLHRDKIVFFLHLLGIDTIGHNKHPDSVEYVENIQYIDGKIQELVDKMNNYYNNDGASSWVFTADHGMSDFGSHGDGNLDNTRTPIIAWGAGIQSPTHEKNYGHDEYSLPWNLTEIKRIDIQQADIAALMSYLVGLNFPVNSVGQIPLDYLDCSSRRKAEVALMNALEIGEQYNLKSASKDQTSIFFRPYSPLRNYTEVQASFYNSVIADIESGEYEIAIEHCFHFSQTVLSGLRYLQRYDWLLLRSIVFFGYLSWIGYVICFVFSLNIEPSSKIVKPVSVVKRVAFNIPFLLICIFFYIQSSPPFYYGYALFPTIFLQLIHSIFPNTKLGFKNFLTVAKQKHGFSLLKILFISLCILCLLQFIVYSYFHREGFSVILMGLAAWPWLLHADYAFSHKTISVSWSVLTSLLCFFTILPVNKKESLLFIFAGGFAMSVAGVFYILYRRNQAFQYSSTVTNKQLVLQVLIIMATVPVTLKIADSLQRNIAIPPILRLVAFGLFITSYIIPSHHIRSCKHYFLDRLAILFLTFSPTMCMLSISFEALFYVVLFITLGLWMELETELQKYTEQLHPEYSRKKDAKFHLSLSHIRISLFFYIFINVAFFGTGNVASLSTFALDSVKRFIPVFNPVTQGALLMYTILVPFIALSAAFGIMNKRLGGIQQVTFFLAVGMADIVTINFFYLVKDEGSWKDIGVSISHFCISNFLILFITALEHASAILCKNITYTIHEKVN Q8WZK3 IBP1_SCHPO ACT_SITE 70; /note="Phosphocysteine intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; SPBC839.07; CHAIN 1..138; /note="Dual specificity phosphatase ibp1"; /id="PRO_0000256254" MSTLSYVSPDALKGWLMESPNEISIIDVRDYDYEGERIPGSVRIPSDTFLASVDQHVDDLMKKRSLIVHCTYSQVRGPKAARVLSEILRNRITESKEKLSLSQKEKLFQNLPTVYILHGGFSAWKRRYGGQQGLIEYD Q92339 GHT3_SCHPO SPAC1F8.01; CHAIN 1..555; /note="High-affinity gluconate transporter ght3"; /id="PRO_0000050411" CARBOHYD 357; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNRFITSILVVFISMSGWLQGADTGSISGILGMRDFQSRFADRYNPISNSYSYSAWRQALLTGTINAGCLFGAMLSSPFTERIGKKYSICFFSGVYIIAELLLVTAVPSWIQVLVGKILAGVGIGALSVLSPGYQSEVAPPQIRGAVVATYQIFSTGAALVAACINMGTHKLRKTASWRTSFGINMLWGILLMVGVLFLPESPRYLIYKGRDEEALRIMCNMAELSPESEIIQTNFNTIKSDIEIEMAGGKARWIEIFGKDIRYRTCLGFLVMLFRELIGNNYYFYYATQVFKGTGMTDIFLPAVILGAINFGTTFGALYTIDNLGRRNPLIFGAAFQSICFFIYAAVGDRKLIYKNGTSDHRAGSVMIVFSCLFLFSYCCSWGPMGWVIVGETFPIRYRSKCASVATSGNWLGNFMISFFTPFINNAIGFKLGYIYACINLFSSFMIFFLAKETKGLTLEEVNDLYMSNIKPWESYKYVREIESHRIHFSKEEEKREREKSKGIRGQEEEFIENADEDNNDSSSSSGSVVSAVKPRRSAVSNDRFSEDSHPTYI Q92345 PDC2_SCHPO BINDING 33; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 120; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 446; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 473; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 475; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 479; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2; Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1; COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Note=Binds 1 metal ion per subunit.; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Note=Binds 1 thiamine pyrophosphate per subunit.; MOD_RES 233; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 521; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 522; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F8.07c; CHAIN 1..569; /note="Probable pyruvate decarboxylase C1F8.07c"; /id="PRO_0000090768" MTKDAESTMTVGTYLAQRLVEIGIKNHFVVPGDYNLRLLDFLEYYPGLSEIGCCNELNCAFAAEGYARSNGIACAVVTYSVGALTAFDGIGGAYAENLPVILVSGSPNTNDLSSGHLLHHTLGTHDFEYQMEIAKKLTCAAVAIKRAEDAPVMIDHAIRQAILQHKPVYIEIPTNMANQPCPVPGPISAVISPEISDKESLEKATDIAAELISKKEKPILLAGPKLRAAGAESAFVKLAEALNCAAFIMPAAKGFYSEEHKNYAGVYWGEVSSSETTKAVYESSDLVIGAGVLFNDYSTVGWRAAPNPNILLNSDYTSVSIPGYVFSRVYMAEFLELLAKKVSKKPATLEAYNKARPQTVVPKAAEPKAALNRVEVMRQIQGLVDSNTTLYAETGDSWFNGLQMKLPAGAKFEVEMQWGHIGWSVPSAMGYAVAAPERRTIVMVGDGSFQLTGQEISQMIRHKLPVLIFLLNNRGYTIEIQIHDGPYNRIQNWDFAAFCESLNGETGKAKGLHAKTGEELTSAIKVALQNKEGPTLIECAIDTDDCTQELVDWGKAVRSANARPPTADN Q92349 MUG79_SCHPO SPAC6G9.04; CHAIN 1..1318; /note="Meiotically up-regulated gene 79 protein"; /id="PRO_0000116628" MDFRITEGSSPTSLSVSEKIAKLESCNDSRITCRPVRESKPTYTSGQKHSALLSKLKRSKVTTDFCKLEESKGIICQENLHTEGAKSKTENISGEDKSSQRRTRLKQIQEFISHRRSFLNSNANSVESEKILAENNHMFNVKSKLSNKESFIKTRRPRTNGELSDLSLQPKRIFSEPVNSHPSQSMFGNGVRASSGSYSLKRDLKDYEEELPSSKKRQRTPPPIVVTNFPQEIFPSKKISLSAKRRIQGKYSGENVRARIELARERNRKRDYVSNLSKGHTTNALEENPFNLGPNYRASTRKCNRIKEAINLFAAKNGSMEVPPKVSVGDSVLTTSQKFLQVIREKTALLMNQDSNSVQPQALAAAESPTTKAPTTKAPTSEAPPKGHVKQLAKQLGNIYMPQSINNVEPTSHSSISKVVNPSEKVISKIERACLAGNGNVHPSIKMEKNLELNPHPRTLNATEHKINSRIQVSKLNTKNELANADPKMYLLENLSDRLYFCKLAKLLLRKYPLDIAEHQFALVYSRFQRIPLKQISCLKQSLVAYYSVLSEVGITNEIMLRENRFSSPKTPEGLVSISKLLLDDREHLSHDERSYIQQLQSQIKSQSVHHENAAEEIRKMRNLRNSRINSQQVGEKVFVNPDVKTMDIQETFLQDYEDETFANEGLSASKFKEEFLLISDSKSDLNSEEIATPNSLEFKNNPRIKVPRSLLTILNLHDRSQLKLFEVCHNSEFKDPINLSNCLRNLLEKQLLSYNFTDWFASLGSEYENVYVKFISHYDFSSLNVYASFQKLCCDLYYGSDDYIHSPILQVFASCWLKQNSNYGFLNEDIIVKIVLILIDLHKSTYSKKLNSYVVPMETFVKYALEKLRPLISPDSVCILSKEDKKHWLKYKKNRSTFAKLLFSTWSNLPSDIGFILECMLKEYYDTFLKSPFAVPNAVQAQLHNQVRGDLTPKRNRSSLISELMKSSKLLKQESSGNKNSTSLESDAFKESSFVLNEENGGIYAGKEIDLPEPSVIDGRPHFSVFNYTHHMQEEKTHNRLPWHRRGMISYKKMVLSKNNRWVAGYWKKKYCIVDSGKLIFYKSDHLDPNACSNVSPIHREFGLQSCLASPNLPPSINSNRNNVFYLNIPGNECYLFEAPSVLAMNEWIHSLNFNAAMITCPPLPENITNTEYGWGYILTRAEKKAYYTAADGTKTFVGDLAQLTRWSPMDIQGLQDIPRPLRDKVHILRDCVPSLLETCLLFQSLPEKMEKCFAAGSKNYLKAMDNWNRKMKFLYERSMMYKEYQRVLECEYEYRKSHDFYPTLSPVRYPYDFKGL Q92352 ARPC4_SCHPO SPAC6G9.07c; STRAND 3..5; /evidence="ECO:0007829|PDB:8UXW"; STRAND 28..30; /evidence="ECO:0007829|PDB:8UXW"; STRAND 47..56; /evidence="ECO:0007829|PDB:8UXW"; STRAND 59..66; /evidence="ECO:0007829|PDB:8UXW"; STRAND 69..75; /evidence="ECO:0007829|PDB:8UXW"; STRAND 104..107; /evidence="ECO:0007829|PDB:8UXX"; STRAND 113..119; /evidence="ECO:0007829|PDB:8UXW" HELIX 6..19; /evidence="ECO:0007829|PDB:8UXW"; HELIX 37..40; /evidence="ECO:0007829|PDB:8UXW"; HELIX 44..46; /evidence="ECO:0007829|PDB:8UXW"; HELIX 81..96; /evidence="ECO:0007829|PDB:8UXW"; HELIX 120..125; /evidence="ECO:0007829|PDB:8UXW"; HELIX 128..165; /evidence="ECO:0007829|PDB:8UXW" TURN 97..100; /evidence="ECO:0007829|PDB:8UXW" CHAIN 1..168; /note="Actin-related protein 2/3 complex subunit 4"; /id="PRO_0000124052" MSNTLRPYLNAVRSTLTASLALEEFSSEIVERQSQPEVEVGRSPEILLKPLVVSRNEQEQCLIESSVNSVRFSIRIKQVDEIERILVRKFMQFLMGRAESFFILRRKPVQGYDISFLITNYHTEEMLKHKLVDFIIEFMEEVDAEISEMKLFLNGRARLVAETYLSCF Q92353 UBP6_SCHPO ACT_SITE 110; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 415; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPAC6G9.08; CHAIN 1..468; /note="Ubiquitin carboxyl-terminal hydrolase 6"; /id="PRO_0000080607" MMIPIAIRWQGKKYDLEIEPNETGSTLKHQLYSLTQVPPERQKVIVKGGQLKDDVLLGSVGIKPNATLLMMGTAGELPTAMPIPAVESVEQEESEDDGYPSGLINLGNTCYMNSTVQMLRAIPELSDAVSQFNSSGGLVAEYRTLLNSMQSNAPVTPMRFLQSLRMEYPQFAEMSRETGGYAQQDAEECWSFLLSVLQRSLSSEWVQKNMAGKLLSTMKCDENEVQEQPSISHDTFLSLPCHISMHTSYMTQGILEGLTQKISKHSDVLNRDAMYSKISRISRLPNYLTVNFVRFYWKASIGKKAKILRKVKFPFELDAVEFCTPELSQKLIPVRDKLREIEKNDEEHERAAKRIKIQPSEDEKEAEAECRLTQVATCQSLVDPELADDEGANPTGLYDLVGVLSHAGASASSGHYQAWIRNSNNRAEWFRFNDAKVSIVPAEKIETLDGGGEADSAYILLYKAKDIA Q92357 CFR1_SCHPO SPAC6G9.12; CHAIN 1..620; /note="Cell fusion protein cfr1"; /id="PRO_0000089660" MDDTNQFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHNKEEEIARETAFDDVQKEIFETYGQKLPSPPVLKLKNATQTSIVLEWDPLQLSTARLKSLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLVLDTTAGTFPSKHITIKTLRMIDLTGIQVCVGNMVPNEMEALQKCIERIHARPIQTSVRIDTTHFICSSTGGPEYEKAKAANIPILGLDYLLKCESEGRLVNVSGFYIENRASYNANASINSVEAAQNAAPNLNATTEQPKNTAEVAQGAASAKAPQQTTQQGTQNSANAEPSSSASVPAEAPETEAEQSIDVSSDIGLRSDSSKPNEAPTSSENIKADQPENSTKQENPEEDMQIKDAEEHSNLESTPAAQQTSEVEANNHQEKPSSLPAVEQINVNEENNTPETEGLEDEKEENNTAAESLINQEETTSGEAVTKSTVESSANEEEAEPNEIIEENAVKSLLNQEGPATNEEVEKNNANSENANGLTDEKIIEAPLDTKENSDDDKPSPAAAEDIGTNGAIEEIPQVSEVLEPEKAHTTNLQLNALDKEEDLNITTVKQSSEPTADDNLIPNKEAEIIQSSDEFESVNID Q92374 RFA3_SCHPO SPCC23B6.05c; CHAIN 1..104; /note="Replication factor A protein 3"; /id="PRO_0000097278" MERPTPRVTKDMLPECSGKTVRIVGKANQVEGETAKVDSNGSFDMHLTVDNTLEPNHFYEFVVSVKPDSSVQLLTCVDFGTDIDMEVYQKLVLFSHKYNSLFFE Q92375 TRXB_SCHPO BINDING 11..14; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 40..41; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 45; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 54; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 87; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 145; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 288; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509"; BINDING 295..297; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P29509" CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P29509}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P29509}; MOD_RES 192; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 278; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 279; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3F6.03; CHAIN 1..322; /note="Thioredoxin reductase"; /id="PRO_0000166768" DISULFID 142..145; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:P29509" MTHNKVVIIGSGPAGHTAAIYLARGELKPVMYEGMLANGIAAGGQLTTTTDVENFPGFPDGINGTTLTENFRAQSLRFGTEIITETVSKLDLSSRPFKYWLEGAEEEEPHTADSVILATGASARRLHITGEDTYWQAGISACAVCDGAVPIYRNKPLAVVGGGDSAAEEAQFLTKYGSKVYVLVRRDKLRASPIMAKRLLANPKVEVLWNTVAEEAQGDGKLLNNLRIKNTNTNEVSDLQVNGLFYAIGHIPATKLVAEQIELDEAGYIKTINGTPRTSIPGFFAAGDVQDKVFRQAITSAGSGCQAALLAMHYLEELEDTD Q92399 RPAB3_SCHPO SPBC14C8.12; CHAIN 1..125; /note="DNA-directed RNA polymerases I, II, and III subunit RPABC3"; /id="PRO_0000074000" MSESVLLDEIFTVTSVDKQKYQRVSRITAVSGQNDMNLTLDINSQIYPLEKDATFSLQITSNLNSPDLKEAADYIMYGKVYRVEEAKDEKVSVYVSFGGLLMAIEGSHRKLYRLSLDHVYLLLRR Q96UP3 RIF1_SCHPO SPAC6F6.17; CHAIN 1..1400; /note="Telomere length regulator protein rif1"; /id="PRO_0000097335" MTKEIAVKEASNMLLQEPSTPSSQAVGLSSSPSSSIRKKKVNFSSELENSPGGNRPSFGLPKRGILKTSTPLSSIKQPNFQSFEGNESEKETSLQELQSSFCSGIENLQHVEKSARIETYSKLSSFLKIYTPSLPEDPIFPLLNQLCNFLLSDRCSNNSEGSPDFQLNTQANKLLSILLWHPTISSHIQPETATVFIEQSLNFLEGPKLTKALAAQHLHLLSCQKCPLSIHPLCNRILDVCFNISFPSLVIGQERLAVLTKILSQFPLEFSRRVVDWAPYLLACLVDASRPIREKALLLALDLSKHLYHDKLVARTILANFRSDIKGTAFVLIMTEQFEKLVIEEDDGVYVAHAWAAIISVLGGARISSWEYFNTWLKIIQLCFNSMNPLTKCAAQTSWIRLIHEFSLSETLTQATKRLTLLCQPISMVLGSRNLPTVKNAAMTTLIALIYACLRPGISDAMLSLLWDSVIVNILEKCALKNEVTIFESSNILLALFNTLSNGVWKDDRLVCRESVEAKELPKLNPVWVRANCSRTIEPVKTLLLLAKPDHTVKTTTPARKQHIRGLSYEQSSSVWSTYIKCLASAGQKEIKRSVETGRAICCICSSLHKFLYSKSIRKDELYVERVSRFALMVKSAIEAFGINTFVEASYLVSDNQLVLIDQTKAIDSYDHVPISPLIYLLHSLALLTNGTLFSTVHAAYSSILSSIEEYHLRFGLKLMLLWDCVSPLSDDGTLVLARVLVSHEVSRLTSEALLSELKSRNGNNSVEEGFSEEERSILLKLLSWNVKFCSISDAGSVNNLLQQYFTAIYKFEGCGSVFPFVVDPFTTILDDVLSFEANKVYSFAISLMKVSTFESCTKELPPVTLPENIRQHLDSYNHMVELYNTLLQRLSSSDQVDLQCRYLHELSEFIKKIPKEFIFHTICKLSKGLIPCFLMNAFPQLEKSTTLQKSCTNFCILILQLLLNSTATASNILESLSPLLTSGLKSISKEVVLAAIKFWNQVFGKFESEEYPIELQKTISYLSKTYIILLPFQSLCPGGKQANHQSSEKMSDILKGVDELRSVSKNGPYASSQDKGEKTTEFSGPGKPNNDNYIQIASVQELDDSSKGKAGKMPASKKNKRQKGDVKKIDETKNEATDMEESLTTPSGKVNKEVIVDDTSLRDEAIVPDKAIDVADNSNALLKENISSQSNRKADNNGTPSVNNSFTTANNDECSKENSQIEPEGQTASREGVLSTPRSTRKKRKLGRKSQSSNVNKEVAISEVSATLENVEVIERHGISEQGQNLDESACVLTNESSLSQTEIPEEKTENETTAVNGFENSKKRQFSSLLSGSIDTNNESNKVSSVEFDKSGPQDIIQSMTEATFEIEKNIQDLKSEEVQKLSDLLMRLQRAILSRIA Q96WV1 TRMB_SCHPO ACT_SITE 173; /evidence="ECO:0000255|HAMAP-Rule:MF_03055" BINDING 88; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03055"; BINDING 111..112; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03055"; BINDING 150..151; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03055"; BINDING 170; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03055"; BINDING 248..250; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03055" CATALYTIC ACTIVITY: Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_03055}; SPCPB16A4.04c; CHAIN 1..273; /note="tRNA (guanine-N(7)-)-methyltransferase"; /id="PRO_0000171436" MSATAKKSAAQLQREEEEARKKLKRLSKQGGVEGRLPMKRLFRQRAHANVLSDHELEYPRSPSEMDWSPYYPDFDVESNKKVEIVDIGCGYGGLTVALGPQFPDTLVLGMEIRMQVSDYLKEKIQALRYRADHEEPVPGGYKNISVLRMNCQKFLPNFFEKGQLSKMFFCFPDPHFKARKHKNRIITSTLASEYAYFIRPHGTLYTITDVEELHVWMAQHLDAHPLFRRFTKEEEENDICVTLMTNETEEGKKVARNGGKKFVACYERIPNPK Q96WV5 COPA_SCHPO MOD_RES 409; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 942; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBPJ4664.04; STRAND 2..10; /evidence="ECO:0007829|PDB:7S16"; STRAND 14..19; /evidence="ECO:0007829|PDB:7S16"; STRAND 21..30; /evidence="ECO:0007829|PDB:7S16"; STRAND 35..39; /evidence="ECO:0007829|PDB:7S16"; STRAND 44..49; /evidence="ECO:0007829|PDB:7S16"; STRAND 56..61; /evidence="ECO:0007829|PDB:7S16"; STRAND 63..72; /evidence="ECO:0007829|PDB:7S16"; STRAND 77..81; /evidence="ECO:0007829|PDB:7S16"; STRAND 86..91; /evidence="ECO:0007829|PDB:7S16"; STRAND 98..103; /evidence="ECO:0007829|PDB:7S16"; STRAND 105..114; /evidence="ECO:0007829|PDB:7S16"; STRAND 119..123; /evidence="ECO:0007829|PDB:7S16"; STRAND 128..133; /evidence="ECO:0007829|PDB:7S16"; STRAND 140..145; /evidence="ECO:0007829|PDB:7S16"; STRAND 147..156; /evidence="ECO:0007829|PDB:7S16"; STRAND 161..165; /evidence="ECO:0007829|PDB:7S16"; STRAND 202..208; /evidence="ECO:0007829|PDB:7S16"; STRAND 215..220; /evidence="ECO:0007829|PDB:7S16"; STRAND 222..231; /evidence="ECO:0007829|PDB:7S16"; STRAND 236..241; /evidence="ECO:0007829|PDB:7S16"; STRAND 246..252; /evidence="ECO:0007829|PDB:7S16"; STRAND 259..264; /evidence="ECO:0007829|PDB:7S16"; STRAND 266..275; /evidence="ECO:0007829|PDB:7S16"; STRAND 278..284; /evidence="ECO:0007829|PDB:7S16"; STRAND 290..295; /evidence="ECO:0007829|PDB:7S16"; STRAND 301..306; /evidence="ECO:0007829|PDB:7S16"; STRAND 308..311; /evidence="ECO:0007829|PDB:7S16"; STRAND 313..317; /evidence="ECO:0007829|PDB:7S16"; STRAND 320..327; /evidence="ECO:0007829|PDB:7S16" HELIX 167..171; /evidence="ECO:0007829|PDB:7S16"; HELIX 181..183; /evidence="ECO:0007829|PDB:7S16" TURN 40..43; /evidence="ECO:0007829|PDB:7S16"; TURN 82..85; /evidence="ECO:0007829|PDB:7S16"; TURN 124..127; /evidence="ECO:0007829|PDB:7S16"; TURN 172..174; /evidence="ECO:0007829|PDB:7S16"; TURN 285..287; /evidence="ECO:0007829|PDB:7S16" CHAIN 1..1207; /note="Putative coatomer subunit alpha"; /id="PRO_0000316543" MEMLTKFESRSSRAKGVAFHPTQPWILTSLHNGRIQLWDYRMGTLLDRFDGHDGPVRGIAFHPTQPLFVSGGDDYKVNVWNYKSRKLLFSLCGHMDYVRVCTFHHEYPWILSCSDDQTIRIWNWQSRNCIAILTGHSHYVMCAAFHPSEDLIVSASLDQTVRVWDISGLRMKNAAPVSMSLEDQLAQAHNSISNDLFGSTDAIVKFVLEGHDRGVNWCAFHPTLPLILSAGDDRLVKLWRMTASKAWEVDTCRGHFNNVSCCLFHPHQELILSASEDKTIRVWDLNRRTAVQTFRRDNDRFWFITVHPKLNLFAAAHDSGVMVFKLERERPAHALNINTLLYVNKEKSIVSYDLLRAQSTTVASVKHLGSAWLPPRSLSYNPAEKVALLTSSADNGVYELVNVSSRSNSLPLKDNIKGPGDDAIFVARNRFAVFSRSDQTIEIKDLSNKVTKTIQLPEKTRDIFFAGMGHVLLSTATQVHLFDLQQKKIVSSFNANRVKYVVWSNDNSQAALLGKHYVYIVKKNLELITSIHETIRIKSAVWVENNVLLYATLDHLKYALMSGDTGVIKTLESTLYLVKAKGNMVFALNRAAEPVSFEIDPTEYLFKLALLRKDYEQVLHLIQNSNLVGQAIIAYLQKKGYPEIALQFVEDPSTRFELALECGNLETALELARTIDRPEVWSRLASDAMSYGNHKIAEITFQKLRYFEKLSFLYLITGNAEKLQKMAIIAEKRNDTLSLFQNSLYLNEVESRINILEQAGMYPIAYLTAKSNGLEEKAQQILSHCNKTEEEIKLPSLGSAFTTPVPVNETYTHNWPLLDTSHSTFEKSLQERMEQLAIERQEEQESEEEYEEVEQSLMDVVDEMSDLAESVPEEEVDGWEVEDLAPEEAVNDVVDDASAFVGADEIFLWKRNSPLAADHIAAGDFESAMKILNKQVGAINFSPLKTRFLEIYTASRVYLPTISGLDPLVSYVRRNAETAERSQALPFITRNLASIKSHELHEAYRLVKANKILEAQICFRSIIYLALTTVANSEEEADEISALIDECCRYIVALSCELERRRLGEEDTKRALELSYYFASADLQPMHSIIALRLAINASHKLKNYKSASFLGNKLLQLAESGPAAEAANRAITLGDRNPHDAFEIEYDPHVEMRICPKTLTPVYSGDDFDVCSVCGAVYHKGYVNEVCTVCDVGGIGQKGTGRRFFA Q96WW4 IVN1_SCHPO SPBC11B10.07c; CHAIN 1..371; /note="Phospholipid-transporting ATPase accessory subunit ivn1"; /id="PRO_0000316867" CARBOHYD 99; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 190; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 212; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 216; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 233; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 284; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 297; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 75..111; /evidence="ECO:0000250|UniProtKB:P25656"; DISULFID 166..181; /evidence="ECO:0000250|UniProtKB:P25656" MSQTEIVKKPKHKRFKRPDKSRFVQQTLPAWQFIFTPWTVLPLLFLLGIVFAPLGAGMFVASRRVKELRIDYTDCMNIGDEFKQVPSTNIEFQYKNVKNVTAMWKSSGDVCTLRFQIPEEMTSPVFAFYRLKNFYQNHRRYTVSADMFQLLGEARTVAQLKSYGFCKPLEANEEGKPYYPCGIIANSLFNDSYSSLLRYESFDSSNSLGLYNMTTNGTAWPEDRERYKKTKYNASQIVPPPNWAKMFPNGYTDDNIPDVSTWDAFQIWMRAAALPTFSKLALRNVTTALQPGIYEMNITYNFPVTEYKGTKTIMFSTTSVIGGKNYFLGILYFVIGGLCAASGVILSIACLIKPRRVGDPRYLSWNRGKSS Q96WW6 ALG2_SCHPO CATALYTIC ACTIVITY: Reaction=a beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:19511, Rhea:RHEA-COMP:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132; Evidence={ECO:0000250|UniProtKB:P43636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29516; Evidence={ECO:0000250|UniProtKB:P43636}; CATALYTIC ACTIVITY: Reaction=an alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+); Xref=Rhea:RHEA:29519, Rhea:RHEA-COMP:19513, Rhea:RHEA-COMP:19515, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510, ChEBI:CHEBI:132511; EC=2.4.1.257; Evidence={ECO:0000250|UniProtKB:P43636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29520; Evidence={ECO:0000250|UniProtKB:P43636}; SPBC11B10.01; CHAIN 1..506; /note="Alpha-1,3/1,6-mannosyltransferase alg2"; /id="PRO_0000080269" CARBOHYD 299; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSQENSVHRSSTKKTPIKIAFIHPDLGIGGAERLVVDAAVGLQSLGKEVVVFTSHCDKKHCFEEIRDGTIKVKVYGDWLPSSIFGRLSIFCSSLRQVYLTMILLTNYMHFDAIIVDQLSTCVPFLLLASQMILFYCHFPDKYLAKRGGILKKLYRIPFDTVEAESVRLADRIVVNSKFTASVFKKAFPKIRKPLRIVHPCVDIEAASKPLEFQLPEKILQRKLLISVNRFERKKDIRLAIDAFSALRDLSANRFPEYLLLVAGGYDIRVSENRRYLKELQEFCEQKDLSYTTVKDNWDNITVAPSTNVLFLLSVPSKVRDALISSSRILLYTPENEHFGIVPLEAMLRKVPVLAQTNGGPLETVIDGKNGWLRPRDAKIWGNVIYEATTSTTYDTAAMGEAGSEWVKNEFSTDAMARKFESEIMSGIRSITPEKRLMRRVNGLLAVFVLFMLFWGTCIIAATVPFAIIKLYFAQTYSSVKLGFMLGTCIVSVSFLTFTVYAKLTNL Q9C0W0 CENPN_SCHPO SPBP22H7.09c; CHAIN 1..409; /note="Inner kinetochore subunit mis15"; /id="PRO_0000116774" MRTELSSNIRIKHDKKIQKLLNRFPRDFLVKLCVEWIQKQTYPPNAKDINLEDMLDDEEWNPEAFYKNVPKSMLKRSIIHRMLVYDWPNGFYLGQIAQLEILALAHGFVSMRWTASKVHHSAEKTVLPNPLVFLELLKSELESIFVYHTYISRHETLPITFIRLVLWDSKRPTALHTYPSSKQIFYLGLMDDSDVLLHNIFLRNDVCHSLFLQCLSRLLYRLKAGSALRPIDLVSKNLTTFCTNVGVNKEANALGAWQIYAKNLVDRSPLDTRPILSDDNSSLIADSTQNCEKHREMAIQRRFGDTHSQVLDKLLITLDHDYIEKSTEKDKVLEENVESYNPTEQRPLVVMQLRGQHILEGLKDICRQDALDPFTMPSYLTGETGLSILYVRDGLVLQRQESLGQQEIN Q9C0W1 NRK1_SCHPO ACT_SITE 38; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q9NWW6" BINDING 12..20; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 19; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 38..41; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 38; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 56..57; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 153; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 154; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 157..159; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 159..160; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9NWW6"; BINDING 203..205; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9NWW6" CATALYTIC ACTIVITY: Reaction=ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide D-ribonucleotide + H(+); Xref=Rhea:RHEA:14017, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.22; Evidence={ECO:0000250|UniProtKB:Q9NWW6}; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-ribosylnicotinate = ADP + H(+) + nicotinate beta-D-ribonucleotide; Xref=Rhea:RHEA:25568, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57502, ChEBI:CHEBI:58527, ChEBI:CHEBI:456216; EC=2.7.1.173; Evidence={ECO:0000250|UniProtKB:Q9NWW6}; SPBP22H7.06; CHAIN 1..230; /note="Nicotinamide riboside kinase"; /id="PRO_0000215897" MTRKTIIVGVSGASCSGKSTLCQLLHAIFEGSSLVHEDDFYKTDAEIPVKNGIADWDCQESLNLDAFLENLHYIRDHGVLPTHLRNRENKNVAPEALIEYADIIKEFKAPAIPTLEQHLVFVDGFMMYVNEDLINAFDIRLMLVTDFDTLKRRREARTGYITLEGFWQDPPHYFENYVWPGYVHGHSHLFVNGDVTGKLLDKRIQLSPSSKMSVRDNVQWAINSILNALQ Q9C0W2 ATD22_SCHPO BINDING 413..420; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O14114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:O14114}; SPBP22H7.05c; CHAIN 1..1201; /note="ATPase with bromodomain protein abo2"; /id="PRO_0000310283" MRRRARSIRFSSDDNEDNEEDDDYYSNAHSEKSEDHSNHIKVSHFDPSSYKQKLVSVRETQRNRKFSSLQKHLNTETPSFSVSIENPSKPSAAFNDASLGKKSTEHQIDGIRNGSSNLQMEGNDKELDTDNNEDESTTFKDEEDDLISPKSYLTSSKTFSYPKAPTESTNGDYLDEDYVDGQSDPESSNASDSDFADSPDDLTKVRSPIPSRRGRRKRKMRGPILPVKKNLRVKKAMSPLRAERNSPDFRRKLRSRDNRPNYHLFDYYNEIASSPNPSTTKITYNPPKLPMKDFATLPIGYQSTCDSDETSELSSTSSEQTSDVEGLNAYNNLGASSDIENAPSSQLHFGHIDEKTIRSTDPFANRENLDFNSIGGLEDIILQLKEMVMLPLLYPEVFLHLHITPPRGVLFHGPPGTGKTLMARVLAANCSTKNQKISFFLRKGSDCLSKWVGEAERQLRLLFEEARRVQPSIIFFDEIDGLAPIRSSKQEQTHSSIVSTLLALMDGLDTRGQVVVIGATNRPNDLDPALRRPGRFDREFYFPLPNKQARMKILEINSLHFSPKIPESYLLHLAESTSGYGGADLKALCTEAALNAVRRTFPQIYTSSDKFLIDLNEISVSICDFVVASEKIAVSTRRSDVKPNIPITDSHKILFKKSIEVITSKIRRLLKLDVYLPTVESLQKLPAEELMRQKEINSLKTTMSFRPRLLITDIYGYGCTYLSKVLFSMLDGIHVQSLDISELLMDTTTSPRSLLTKIFSEARKNAPSIIFINNVEKWPSLFSHSFLSMFLLLLDSISPLEPVMLLGFANTNQEKLSSTVRSWFPSHRSEYHDLSFPDYSSRYSFFHYLLKRISFLPIHQKSAEAASVDILPKVLPVSKTSDLTDKVNRRQRKNDKKIKNKIQVKLSSILEMLRSRYKKFKKPIIDLNDIYIDESNERVVKGKSKDNFEYFLSGNTVTRKKDNACFKMMNFEEIERRLWSGRYCTPKEFLRDIKMIKQDAILSGDVNLKHKAKEMFAHAELNVDELIDAKLLYDCCQVSKREKAYKQLKQKKLNNAKDAHEMQESKNEETFVRNDVAQEDNFIELSSNEVRNVSNDEHKHTLFHGQSLTHNNLIAVTPPSRTGVEHKEENKKYDNVNIQKTLAKCAEEFAEHTNFNKVELLDFVYSKLSSTIWENREEHDLLKIVRDVRQTFFRSLEDMGV Q9C0W7 AP2A_SCHPO SPBC691.03c; CHAIN 1..878; /note="AP-2 complex subunit alpha"; /id="PRO_0000193736" MVASNNMKGLRAFISDLRSLEHDDEEKRVNVELAKIRAKFQSSTLSAYDRKKYVSKLLYIYMLGYPITFGHMEAAKLLSGTKYSEKLIGYLAVALLLNENHELMKLVINSIKKDLLSHDSLQNSLALHTIANIGGRELCETVYYDIYKLLMSASNENIVRQKSALALLHIYRKFPDLINPEWFEPIVMILGDDDLNVSLAVSNFVNLIVIREPKYQKFAYGKAVGKLKNIVFEHGYSSDYLYYSVPCPWLQVNLCRILLACERPSDNPTRATLIRVLDRILSLPNDNSNVQQVNAVNAILFEAIKLAFLVDESHSLYEKCMDRLADMIADKESNIRYLAFETTAYLISCGHSITSLKHYKELILSSLRYKDVSLRKKSLELLYMMCDEENAKLIVADLLQYLPHLDSVTQEDLISKVAIISETFATDYEWYVDVTIQLLRIAGKSADDGVWHQLVHVIVNNEEIQEYATKRLFSLLQSETIHECLVKAGGYVLGEFGHLITDYPDSQPVHQFSTIYRKLNVSSPSTRVLLLTTLIKLANLQPELNDRIAKVFQEYSTIINPEVQQRACEYLQLLKMPRDFLQLVCDEVPPFLDGNRDGVHPKSRPSSKVNLVDTYPQTIPNVSKPSTPIDVPEYDISACLPGFYRLCWKDKGILYQDSQIQIGVRSEYHNSEGAIYLYYENRQSNTLKSLSSTLIRTFSTFHLATTFQDTNLPSGVQLQQKYVMSGVNEIFEPPIIHVSYVTGVIRSIDLQLPVLLSKFMKPTIFDSYDFFNHWGQMGVEREAQLTFGLNSKDRKLDAKRLTKIVSGFHWGICQNVDSIALNIVGAGIIRFGTQNVGCLLRIEPNYEQNLIRLSIRSTNTSIANTLAKEMQEILRNSF Q9C0X6 RUVB1_SCHPO BINDING 71..78; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPAPB8E5.09; CHAIN 1..456; /note="RuvB-like helicase 1"; /id="PRO_0000165658" MVQISEVKGNGRDNRITTHSHIKGLGLKEDGTCESVGGGFIGQEKAREACGIITDLIKSKKFGGKGVLFAGGAGTGKTALALAIAQELGPKVPFCPMVGSEVYSSEIKKTEALMENFRRAIGLRVKETKEVYEGEVTEMVPEEAENPLGGYGKTISHVLLGLKTHKGTKQLKLDPSIYESLQREQVSTGDVIYIEANTGAVKRVGRSDAYATEFDLEAEEYVPMPKGEVHKRKEIVQDVTLHDLDIANARPQGGQDIMSMMGQLMKPKKTEITDKLRGEINKVVNKYIEQGIAELIPGVLFIDEVHMLDIECFTYLNQALESTISPIVIFASNRGICTIRGTEDIQAPHGIPTDLLDRLLIVRTLPYSESEIRSILQIRAKVENIILTDECLDKLAQEGSRTSLRYVIQLLTPVSIIASLHGNKEIGVQDIEECNDLFLDARRSAQVVKSSSGFLQ Q9C0Z9 RPC9_SCHPO SPAPB1E7.10; STRAND 2..11; /evidence="ECO:0007829|PDB:3AYH" HELIX 13..34; /evidence="ECO:0007829|PDB:3AYH"; HELIX 35..38; /evidence="ECO:0007829|PDB:3AYH"; HELIX 43..57; /evidence="ECO:0007829|PDB:3AYH"; HELIX 67..75; /evidence="ECO:0007829|PDB:3AYH"; HELIX 84..93; /evidence="ECO:0007829|PDB:3AYH"; HELIX 98..104; /evidence="ECO:0007829|PDB:3AYH"; HELIX 108..112; /evidence="ECO:0007829|PDB:3AYH"; HELIX 117..127; /evidence="ECO:0007829|PDB:3AYH" TURN 58..60; /evidence="ECO:0007829|PDB:3AYH"; TURN 76..80; /evidence="ECO:0007829|PDB:3AYH"; TURN 113..116; /evidence="ECO:0007829|PDB:3AYH" CHAIN 1..129; /note="DNA-directed RNA polymerase III subunit rpc9"; /id="PRO_0000352805" MKVLEARDAYLTNAEVFFHLKEMENEQNARTQERGAAQALVCENLRTIQFEILKYLSSQGNCEGLTKERFLDCIAIFNEFELTKAEILVILNNKPSSVPELYACIEGIEERFKEEDIFKLVEKINTTFP Q9C100 PMT2_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; EC=2.4.1.109; CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; EC=2.4.1.109; SPAPB1E7.09; CHAIN 1..739; /note="Dolichyl-phosphate-mannose--protein mannosyltransferase 2"; /id="PRO_0000237686" CARBOHYD 167; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 404; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSYEQLHAQSGQLRQRFPSKHSEIEDEVANEKEELKDATKSALGEVKTNKKYYILGYFLVPLLLTVIAGFVRVWKIADSNVVIWDEAHFGKFASYYLKHEFYFDVHPPLGKMLNAVAGKLVGYDGSFDFSSGATYPEDLNYKFMRLWNAAFGTLCIPLVYFTALNFNYSFLAATLCTLMVALDNHLATISRFILLDSMLLFFIISTFFCLSRYHVYHKAPFTFYWFKWLFLTGVCIGCVCSVKLVGLFITAVVGLYTVDELWCLLNDKRVTWKAYAGHWIARVCLLIFLPILIYAFTFWIQFAVLYRSGPGDAQMPSLFQARLEGSPLTKNPIDLMYGSKFTLKSRNPTGALLHSHVQTYPEGSEQQQVTGYHHKDGNNEWMFVPTHGVAYNYEENDPMNPILNGSVVRLIHPFTNRNLHTHKIPAPLNKRMYEVSGYGLGDVGDEKDYWIVNILYDTAHRDAYNVRSLSTVFQLYNPVVGCYLSSSSSSLPSWGFGQIEMYCDPDPDPSNTDTQWNVEEHINPRLPEGSINDYPSSFWSDFLHLNRAMLRANNGLIPDEDKLDALRSEAYQWPFLLATLRMCGWGDNQIKYLLVGNPVAYWFATSSLIVFALFVVGAVLAWRRRVLRWSQEACDTFHYAGIYPFLGWFFNYLPYYIMGRVLYVHHYEPSYALSTFTAAFVVDWFTKKMPKIVRVVVFISLYAIIAGVFIYFKDVTFGMHGPASDFHRLRWLNSWNVHD Q9C1W8 PPN1_SCHPO CATALYTIC ACTIVITY: Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate; Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10; Evidence={ECO:0000250|UniProtKB:Q04119}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q04119}; PTM: Processing by proteases in the vacuole may be required for activation. {ECO:0000250|UniProtKB:Q04119}. SPBC713.07c; CHAIN 1..577; /note="Endopolyphosphatase"; /id="PRO_0000058549" CARBOHYD 363; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 370; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 375; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 399; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 481; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRPSVITVAVLFVQSTWASFAFGNPMSMRNKAHTNDLVNSKGKPLVGRFLHITDMHPDIYYEKGSTVDHYCHSYDHNSDDTPLGKSKVGYLSPGPGYECDSSPALIDKTLEWLKEHQDDVLGGIDFILWTGDNSRHDNDNHFPRTQSEILASNEDLVNKMIEAFPDVPIVSAIGNNDIYPHNIMEAGPSSMTRQLAGAWDALIPYEERHTFEKGSYYLCDVIPDKLAAISINTLYLSNKNAAVDGCPDDNLDEPGSLFMRWFKIQLEAYRLKGMKVWLLGHIPPTRGQWYEDCYTSFTDLLYEFRDIIVGQLYGHMNINHFVFLEFDKLPVDTESYGIKSAQPKYVKSLIDAQYAELPTFPENLTEEFLNGTVGNYSLATVGGSIIPEMFPTFRVYEYNISDIANQLDDREELTEITSFNWETLEEQSQSDYEIDKKKKKKKKNNKKKKKNKRKNIKPGPLGPAYVPSLFTPISFKQYFLNTSNYMDATKDTEISYELLYTSKDSPYNMPDLTVPEYMRLAKRIATCDKPEDPHQFKLQSGDQNTFRISKKKKPSICPIAYTYLWHAYIGSISDFED Q9HDU3 GAL10_SCHPO ACT_SITE 532; /note="For mutarotase activity"; /evidence="ECO:0000255" BINDING 7..38; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264, ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU10126}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; SPBPB2B2.12c; CHAIN 1..713; /note="Bifunctional protein gal10"; /id="PRO_0000197441" MAVQDEYILVTGGAGYIGSHTVIELINHGYKVIIVDNLCNSCYDAVARVEFIVRKSIKFFKLDLRDKEGLAQIFDTFKIKGVIHFAALKAVGESMKLPLEYYDNNICGTITLLNVMREHRVKTVVFSSSATVYGDATRFDNMIPIPESCPNDPTNPYGKTKYAIENIIKDLHTSDNTWRGAILRYFNPIGAHPSGLLGEDPLGIPNNLLPFLAQVAIGRREKLLVFGDDYDSHDGTPIRDYIHVVDLAKGHIAALNYLNKINNSEGMYREWNLGTGKGSSVFDIYHAFCKEVGKDLPYEVVGRRTGDVLNLTASPNRANSELKWKAELSITDACRDLWKWTIENPFGFQIDNYKWKLFNTLGIMDYKNRLHTICFQDLEVSIANYGALVQAVRYKGRNLVNGFNDFSRYKLKENPFFGATIGRFANRIANGQFEVDGHLYTLCKNENNKTTLHGGNNGFDKQFFLGPIARQYEDYNTLEFILVDKDGNNGFPSDLETLVKYTIKNNSLEIEYKSVIPEYSKLNVTAVNLTNHSYWNLASPNKTIDGTIIKSTTNVYLKVNSETSLPTGDIVEWQNDITKPTKLDPNISFDNCFIVDREASKFCLDTRKYSLKNIVEVIHPSVPVKLVVSTTEPAFQLYTGDGNDICEFQSRSGFCVETGRFINALNNEKWSKQVILRKGEVYGARSKFSLYAQDLEENKHFLDSASYNSGEYY Q9HDU5 GAL7_SCHPO ACT_SITE 185; /note="Tele-UMP-histidine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10033" BINDING 54; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"; BINDING 57; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"; BINDING 63; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P07902"; BINDING 79..80; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P07902"; BINDING 127; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"; BINDING 172; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P07902"; BINDING 183; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"; BINDING 187; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P07902"; BINDING 201; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P09148"; BINDING 300; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P09148"; BINDING 317; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P09148"; BINDING 319; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P09148"; BINDING 332..335; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P07902"; BINDING 337..338; /ligand="UDP-alpha-D-glucose"; /ligand_id="ChEBI:CHEBI:58885"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P07902" CATALYTIC ACTIVITY: Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989, ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=2.7.7.12; Evidence={ECO:0000250|UniProtKB:P09148}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P09148}; Note=Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role. {ECO:0000250|UniProtKB:P09148}; SPBPB2B2.10c; CHAIN 1..369; /note="Galactose-1-phosphate uridylyltransferase"; /id="PRO_0000169891" MTSKKFDFTEYSHRRYNPLTDSYVLCSPHRAKRPWQGAKEEIKKDDTVKYDPTCYLCPGNIRATGFENPKYETTYVFPNDYPAVRVDQPDYMQDESEITKGNTLKTRMFKTEGVKGKCFVICFCPNHNLTLPLMSAEAICNVVETWKHLYVTLKKESLEGPIRYKYLQIFENKGSAMGCSNPHPHGQAWCLDVIPSVVAQEMCNMTKYFELNNSHLLGDYVKLEMLEKERIVVENDSFIVVVPYWALWPFETLLIAKEHLKSLEEFEEKQKVDLASALKMLTTKYDNLFNTSFPYSMGLHQAPLYGSNEEVENSWFHMHFYPPLLRSATVKKFCVGFEMLGEPQRDLTSEQAAARLQELDGQKHYKNLL Q9HDV1 MU180_SCHPO ACT_SITE 200; /evidence="ECO:0000250|UniProtKB:Q5NUF3" SPBPB2B2.02; CHAIN 1..381; /note="Putative steryl acetyl hydrolase mug81"; /id="PRO_0000278630" CARBOHYD 193; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MISLSLLYRILTLPIILVGTTILYFTIGTNFPHDELRHNLLSTLFCSSMLHLSKGLTVKDVRIFFHDSIGSTLLKNRKKLNSENELPNYGEKFTHKYDNQDMPDSVWLAKVNGMTKSDPIILHLHGGMMALPYDKVILVGLSNLYKLFSTTMNRPPSILLVDYSLVSQGYTYPKQVRECLNVYQVLISKGFRNITVLGESAGGTLILSFLYQISELSKLNKVVWPKGVALISPWLDLTNAKKIGSYRANDGLDVICYETLNRFGKAYVNNEESLFTSSVVNINMNCDISIWSKIPPIQDGKVLVLFGENEVFRDEILSWTSKIGLLKAYPNRVLMDKQGIHIGLFLEESPSIGPGMTNLDIWKKKFSVNSLYTFLRETFEE Q9HDV6 MOR2_SCHPO SPBP19A11.04c; CHAIN 1..2196; /note="Cell polarity protein mor2"; /id="PRO_0000096536" MSLNEIAHDQPVENGPLYSEKQDHTAVDYALHILFTQFVRLSEQKISFLSRYHANEGKNAEPVRFNVGEQEAILLLKKGEDNEFDRCIQALVALASSKPVAVIESLLCWRKVRVDITSSSGTPRVVNERRSSISIYILCRVLTEIAETIPSNALEESTVSCLLECVFHQLLSAKNLPVSSSYFSLANWESFAFLVGSMSRFNFVMVSDRFIEEIEHLEKSGCDSRQKETVLVHLLRAMRYLRLQLYPTTLLEESIAFLQSLTSFFMKANTALKIEYAYLMEQLLRPLISRATFEVNIPAWSRTIETIYPVVLKMCTKTKYWNVFFPFCCTLLCLSPKQFFLKHWISSLDAAFFRVKDRRLRNTGLPHLSRVVWTYSNQYKEEPSIMNSNISNILKSGFSIGKKFSVVPFATLEELDGYAQIVRVVGAHFPELVIKEILTPLSTDAFTENIGPEKLMIVVRSVYYILHDMKYKKSDSTIFEYIEFEFVDLHEVAVGTPLQQFVHNLSQKLLFLVFQLSTNTNCYLDSKNATSLLALYINALKVFPCLMGKLEQRVIDAYVKCLNCSNKIIHTVCHNSLIYFSSGLKMSKSVISCLSRKLVKGSEYLLRTYHEVIRIWISQQEAVIEKRNSVLSNKSCASSESNTPASVKQDYDDIQSWTIIEEIQSLGVLHLSSPSVGIRKFAVALLNDVKQLNTEYLMLSSDKVEVGDIYSEPTIVDVLKDCDSSILSVESHLPTAAERSRLRKFINDGTKDMLLKLATSNSGVDISIWYNVFPRFIKVCFERFPTTMALLRNTVCEKLPSITMQLLSRIESSELNFNLKSAVKNDNFPEFLLVQWKLYLIVACCTITYTSNVDYSHTDLRRTLTAVQSGNHLRGLQETIKITSAESLFSMVLPLIFTEFSPIREAVVFAIGCINVNAFPQLVRSLKPYISVLKQDHQEFIFAGLNFPSVKRRNKPDLLLRSEIAHIFAMTSHLLLHELLNEDREALSVISEFLKDLKGFLSTPNVQADEKYLKLRCYFSQLLEKVLLVQNLHPSSEVLPFSGRASCWKLLDEWTGFGPARAITKNREELMRAHIRGNNKDIRERDKLLASFEAGKQNLEYLAIKAMIALCTAKLQQELTEGVFLFDIEILLNWFTAVFGSPSKAIVGLARKGLTALLLENSSNEVLLQKVINRCFSKEISQTISNYYFLSLSEMLIQINPNNLSKPKLLPLCLVNLSTNNLSVRLKAFELLGNFHLNNFTMTALMEFKTFLESSNPALYLKPQYLFSVQLASDFTEDSFTLTSECLRYFNYGHQHRRGLVTVLLPWLQNLELKMDVENKTFDSFTAVILIDLIEVTAKFTNDLPNEIEALWTSLALSRHKSNWTVILFFLMQQCYQRKTFSFVDCTRQITIYLAKTELLSDLYSTLLSFVCPANVSNENQEVYKFSLEDLSSTYVANLEDLFPSEKNHISYSPCQLSLLLLMDILPNPSIITVTDDVATILHAAFIQFDHYSRIVQEQCQQIFQYVVRKVLAMEGRLDYDDAYFDFNVESSLITGLRGKTKKEDDLVKYHNMILKTIELLSSSYPELKQIWGEVALSWATTCPSRRLACNSFQLFRSLLPDFDARMLLEIISRLVGTISDETSYLRDYSVEILRTFNSYVLVMNSDDLLSYSQILWTAIACLTTIHEDEFIESVKIAYAYFLRVEETDSATQQIMETFPQNWVGDYQGLQILILKGFRSTNSFEITMNFFLLLMDFKDNDLVGVGYLRILSCLLVSLPAMVYTYEHSDPITFDLSVFCHKLATLASQFNDDALIELLDTYLKRKFRSIKDFLKHTVSYLYSYYFEDYELEIVSTLTMFLSNNLTWFRKSTLDVLKELFPLIDFQKPIYSEHGLGIVSPLLRLLPTGYAMEALSLLTDSVLHVSAPTDMQTLKLLMVDPKLKNSDDRLAGFFEIPDEDGWYEPNSEYAAAITKSNVHAVFYSCSTTEASVSTPEVRFHADEVSNYPRHVPTDSHGSLDENSLGELVTTLHSLDVFFAEDRDEELIQPDVAVDPKLDITSEDYDDRIATILSGSLRRQKQGLMAYETESFRDYSPNEEIDASAKLPMDMPPVRVRKSSFISKLKPHYFMDAESYYPSLKALGNSAEHRLSLDEIRGAAELKQNKNWNSMLDQSVSMINEDSVEDHETHENYYHLRTMFQGSESNESFTDTTRSRGWH Q9HDW1 PGPS1_SCHPO ACT_SITE 148; /evidence="ECO:0000255"; ACT_SITE 150; /evidence="ECO:0000255"; ACT_SITE 155; /evidence="ECO:0000255" BINDING 58..65; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5; SPBP18G5.02; CHAIN 1..502; /note="CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase"; /id="PRO_0000350817" MDEGIEKNIFVNLESQIDGVCPKFYVNVDDIDIIHEPPEFYQRLKKLIKKAQKRIFLSTLYIGKEERELINCLSNALSNNPSLHVHILADQLRCTRESPGCCSASLLMQLKKKFPDRCEIKLYHTPNLRGLRKQLVPHRFNEGWGLQHMKIYGADDNLIISGANLSRDYFTNRKDRYYLFSDKGLADFFFKTHFLFSQLSFECIPHLSDSSIQLSSTSPVIPFTLKWNNSCPNPLTNPQEFRVAASAKIQQLLQGNREKFLSRNPSKPLSSVYGSELINQAGDDNNKPFHKYEESAIVYPLFQCVPILTSDVHSTEEKVLSIIGTLLSRKEVNWTLTAGYFNVYPALRKQLLKSEGIGEVIVASQQANGFYRSPGPSKLIPPAYQYIAEQFLKDSRKKKRNIDVLQWQNKGNTYHAKGFWLSTQHHKHPFLTTIGSSNYTSRSQQLDLESTLVVMTQNEKLKRKFSTEIELIKQHTKPMNTCQLEKVPMYVKALTSLMKKKL Q9HDW7 ATC2_SCHPO ACT_SITE 545; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250|UniProtKB:P04191" BINDING 498; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 503; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 545; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 547; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 547; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 638; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 691; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 736; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 807..809; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 856; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 862; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 881; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 884; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 947; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 977; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 981; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P04191"; BINDING 981; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P04191" CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; SPAPB2B4.04c; CHAIN 1..1292; /note="Calcium-transporting ATPase 2"; /id="PRO_0000362141" MPTYNDDDDSSRPPSVHSERNQKPSSSQFLGVPSSNYNQRENSSRSGSSTISREPSSSGTMYPMASRDSMKESYDKNKGTPPDYTSYVSHSDAEPEQASSKSSTSIEDLLHTEYDDAPFAFSIPLLQRLQDPKNTSLLHAIHGLKGLCKGLKVDPSTGISTHEPHYADKLQMSDILNDDSNPKLVVHLDRIRSQDNNPEAKVSHDSDRVKYYGKNVLPEHDSKGLIRLMLEAFKDKVLILLSIAAVVSLALGLYQTFGQPPTLDPITGKPEPRVEWVEGVAIMAAIVIVVTVGGVNDWQKELQFKKLNAKVSNFDVQVLRDGAVHSTSVFDLVVGDVLFVEAGDVVPVDGVLIESNNLVLDESAMTGETDNIKKVDANTAIERTSPDVEYRKNADPYLISGTTILEGNGKLLVTAVGVNSFNGRTTMAMRTEGQATPLQLRLSRVADAIAKLGGAASALLFIVLLIEFLVRLKSNDSSSKNKGQEFLQILIVSVTLLVVAVPEGLPLAVTLALAFATNRMQKDNNLVRHLQACETMGTATNICSDKTGTLTQNRMTVVAGGFGTDVLFFDHNDETPTNVDQGSDSSKFEDAGASAFAFKRLSPELRDLTLYSIAVNSTCRQLFEDNSDTPRFIGSKTETALLDMSVKELGLTNVDSMRSSVDIKQFFSFSSDRKASGAIFEYKDKYYFVVKGMPERVLQQSTSVITNGSLDEVEDMHSHADYFKEMITGYAKRSLRTLGLCYRVFDSWPPKDIPTNDEDSSNPLKWEDAFTDMTFLGFFGIMDPIRPDVPLAVKVCQGAGVTVRMVTGDNIVTAKAIASQCGIYTEDGISMEGPEFRSLSDEKRLEILPKLDVLARSSPLDKQLLIEGLQKLGNVVAVTGDGTNDAPALKKANVGFSMGKSGTEVAKEASDIILMDDNFSSIVKAIAWGRTVNDAVKKFLQFQITVNITAVFLTIISAVASTDQSSVLTAVQLLWVNLIMDTLAALALATDPPTPEVLKRKPEKPGASLFTFDMWKMIICQSMYQLAVTLVLHFAGNSIFHYPSNTADMNTIVFNTFVWLQLFNEINNRRLDNKLNIFERINHNFLFIAIFVIVAGIQVIIVFFGGAAFSVKRIDGKGWAISIVFGVISIPLGALIRCVPNNFLRKVLPVKTIDTVFSWILNPRFRSKRRSTDHDVESLSLIPYEPTSPNEVIDSIRHSLGFVQRIRGGRIRHLLNNSKFDKQMEALPERLRPRVKQRFMKIRSPSVSSATSVALMIPISTLVSEASGRLGGHDIWISHNRQALDKKSSNVH Q9HDW8 GLRX5_SCHPO BINDING 43; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:Q86SX6"; BINDING 51; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000305|PubMed:23615440"; BINDING 83..87; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:Q86SX6"; BINDING 95; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:Q86SX6"; BINDING 108..109; /ligand="glutathione"; /ligand_id="ChEBI:CHEBI:57925"; /evidence="ECO:0000250|UniProtKB:Q86SX6" SPAPB2B4.02; CHAIN 1..146; /note="Monothiol glutaredoxin-5, mitochondrial"; /id="PRO_0000102252" MNSMFRFWIPKTSISMQLRMLSTQTRQALEQAVKEDPIVLFMKGTPTRPMCGFSLKAIQILSLENVASDKLVTYNVLSNDELREGIKEFSDWPTIPQLYINGEFVGGSDILASMHKSGELHKILKEINALAPEQPKDSEEETTKKD Q9HE04 RHO5_SCHPO BINDING 13..20; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 60..64; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 118..121; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" MOD_RES 197; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPAC20H4.11c; PROPEP 198..200; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000281274" CHAIN 1..197; /note="GTP-binding protein rho5"; /id="PRO_0000198944" LIPID 197; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MTTELRRKLVIVGDGACGKTCLLIVFSKGTFPEVYVPTVFENYVADVEVDGRHIELALWDTAGQEDYDRLRPLSYPDSHVVLICFSVDAPESLDNVQEKWISEVLHFCSNLPILLVGCKVDLRNDPKTIEELSKTSQKPITFEEGQVVAQKIGAYKYLECSAKLNEGVNEVFETAARASMLKFKPASVPKTKKKKHCILL Q9HE10 DSC3_SCHPO SPAC20H4.02; CHAIN 1..250; /note="DSC E3 ubiquitin ligase complex subunit 3"; /id="PRO_0000350755" CARBOHYD 187; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSSSALKKWEIVIRFASSIPDLSLEISDAQTTTIHSLFKIVRNRIPECRDKQLKMVFQGRLLSPGFTVERAVRGNWQRDENDDPNIVQKAFIHCIVGPTLTEEELASQDQAQSGLNSNSESPDDLQNAQTGETLRGFDRLREAGFTETEVNNLRSQFHRLRGTNLDSLTEDAIREAEDDWIDNGGQNSSADELDMSYETLLAGVLIGFFGGAIACYFLWERTMFSLRMQLSILVGIICNFAYGLLHSYRW Q9HEQ9 TCG1_SCHPO MOD_RES 152; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC660.11; CHAIN 1..349; /note="Single-stranded TG1-3 DNA-binding protein"; /id="PRO_0000081971" MMSAEETVTQNAPNTVQDQVEASVDAAVHASAEQSNTPAQQADDFRVFVGRLSTSTKKSEIRSLFETVGTVRKVTIPFRRVRRGTRLVPSGIAFVTFNNQEDVDKAIETLNGKTLDDREIVVQKARPVQEQPIKDRKKSKNKNGEEPETSTSVENAESAKGSSDENEANTATAPSSNEANGVDKKQNEIKGKGGSGKNKAKPLPPNSIYVSGLSVTLTNEGLKEMFDAYNPTRARIAVRSLPPYIIRRIKLRGEQRRGRGFGFVSFANAEDQSRAIEEMNGKQVGDLTLVVKSAVFREDKQNDENEKNENEPIEASESAPTNVSDSTEPKASEVDSEEKSGVTASAITA Q9HFE1 FET4_SCHPO SPBP26C9.03c; CHAIN 1..584; /note="Low-affinity iron/zinc ion transport protein fet4"; /id="PRO_0000358871" CARBOHYD 522; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTASITEIDSISEESNVESVSHLQHSPSFEKKGADFSISLNEKKDFASPITEEIPSPDGIATPEPETKKKLSFGARVWDLICSPGRQHDVCVAAPTQLVRSCDDYANSASTLVTNDDGTKTKVDSDEKKHKHKNVRDYIRFKHVDIGGRIFDLITRLAGTSFTFILMLIILIVWAIVGGIYRAPDNWQIVMQDGSSIQCYVSDTLLMRQQQNQHIQVLTMISQLRSRLLTTSRLLGPVLNDKTKISSVNVALMKDDVGDAEKLPTENWFDFICNYVSFMVGSIIFLVVYWIGIFIWIGFGRMLGWSDEWQLYINTAVAVELTFTSVFLQNVRHRHMKYIDRCVTSIFRIDSVIEEELRRMMGDKEPNEEITIKMDKINLGERSIDYYADLIGSGVGVVVSTCVFVAWIAIGNVMHWDSNWWLIIGTYTGLVGFLDGFVLRNVYFRESSKEATEIQTLIDEDYALYQKLDLPLPHEHITNYKSTFGGSLSQWIGWLCALPISVLFSVFVILGLIIAAGSLRFNETAQLFCNTPTMIIEGALLIVLIEAHNIANLKRRIQFRQIHLRRLTILKMLAGDNYSTTSTV Q9HFR0 CSN2_SCHPO SPAPB17E12.04c; CHAIN 1..437; /note="COP9 signalosome complex subunit 2"; /id="PRO_0000120977" MSNDFMLEDDENYDFEFEDDDDDMIEPYVDVENCYYNSKSLKEENPESALTSFYSIVEKCEGEQNEWAFKALKQITKINFQLKKYDDMLQSYQRLLGYTNWLSITKNYSEKSIYNIVEYASSCENTEFLEKFYDVTTKALQNLNNERLMLKVLMHVARFLLTQKNYHKFKYLLRQMHELLSDENNSVADQNRGTHLLELYSLEIQMYSDIEDNKRLKELYQSSLRVKTAIPHPRIMGIIRECGGKMHMQENQWSEAQTNFFESFKSYDEAGSSDRIRVLKYLVLANMLSESEINPFDSPETQPYKDNPHIIAMTKLVEAYQIRDITAVERILQTYQHDILDDDFIRQYVDKILYSIRSQVLIELVKPYTSVKLSLLAKKLGVSISIIEQALVGLIIDERVNGKIDMVNEVFTISQPKNTIHNQLVEDVQKLWNTATK Q9HGM3 YTA12_SCHPO ACT_SITE 562; /evidence="ECO:0000250|UniProtKB:Q9Y4W6" BINDING 298; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 299; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 340; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 341; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 342; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 343; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 344; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 479; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 561; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 565; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6"; BINDING 638; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q9Y4W6" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P40341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P40341}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9Y4W6}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y4W6}; SPBC543.09; CHAIN 1..773; /note="Mitochondrial inner membrane m-AAA protease component yta12"; /id="PRO_0000317334" MRNPFLTFRAPTRKTGDYLVSKFVKKDNFSSLRLARAYTFSTRSTAVSQFSLLSLSQRSFQSLKINKGIPEKHKIPLISSKQFSVTSKRSQNGSSGSNSDANGRKNGQKNDDSKKKGLNGNDPKKVFEIALNGNTILGGILVAYILYNVLSPNANMQEITWQDFRQQFLDKGLVERLVVVNRNMVRVILRGGVASGSGQYYFSIGSIDSFDRKLEDAQRQLGIPPSEFVPVAYHDEVSVLATLLSFAPTLLIIGSVIYLSRRASGAAGGGQGGIFGIGKSRAKMFNHETDIKIKFADVAGVDEAKEEIMEFVKFLKNPKFYERLGAKIPRGAILSGPPGTGKTLLAKATAGEANVPFLSVSGSEFLEMFVGVGPSRVRDLFATARKNAPCIIFIDEIDAIGKARGRGGQFGSNDERESTLNQLLVEMDGFTSSEHIVVFAGTNRPDVLDPALLRPGRFDRQITIDRPDIGGREQIFKVHLKHIKAADNIDLIAKRLAVLTSGFTGADIMNVCNEGALIAARSNSNEVQMVHFEQAIERVTAGLEKKSRVLSPEEKNTVAHHEAGHAVAGWFMEYVDPLLKVSIIPRAQALGYASYLPKDQYLMSRGQILDQMGMALAGRVSEEIFFGPEKITSGASDDFQKVTRMAQAYVTQYGMSPTVGTIAYPIDTRETVQKPFSEATAQMIDEEIRKLVKHAYERTKKLLLEHKQGLENIAQRLLQKEVITYNEVETILGPRPYAYKHLNISELMRQSEYKNDHDPRNPPIPPSPQQPSA Q9HGM4 SCS3_SCHPO ACT_SITE 161; /evidence="ECO:0000255|HAMAP-Rule:MF_03231"; ACT_SITE 212; /evidence="ECO:0000255|HAMAP-Rule:MF_03231" CATALYTIC ACTIVITY: Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343, ChEBI:CHEBI:132023; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(9Z-octadecenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:65564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387, ChEBI:CHEBI:58343, ChEBI:CHEBI:156553; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65565; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:65568, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57368, ChEBI:CHEBI:58343, ChEBI:CHEBI:156554; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65569; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:58343, ChEBI:CHEBI:132018; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033; Evidence={ECO:0000255|HAMAP-Rule:MF_03231}; SPBC543.08; CHAIN 1..250; /note="Acyl-coenzyme A diphosphatase fit1"; /id="PRO_0000374041" CARBOHYD 149; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTEKTASHYWNEETSILKLRRKDILLFEIYATTLLLGSIYSIYVDKWSITSYFGNSKNLINLIFVKRGWFWTSLVYFYHAWDQKRNKIDFKFISRYIVATLWWMFVTQWFIGPGLIDRTFALSGGSCKNFDGDSSVFIPLTASTCKGLNGSWSGGHDLSGHVFLLTHSSLFMLSENFSFILNNGIKATSTKVLFGLLGLWWWMLFVTASFYHTTFEKCTGFFSGILEWSIVYVFSSRMPAVADLLGSSDY Q9HGN2 YO48_SCHPO MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC36B7.08c; STRAND 76..82; /evidence="ECO:0007829|PDB:5GPL"; STRAND 92..98; /evidence="ECO:0007829|PDB:5GPL"; STRAND 102..104; /evidence="ECO:0007829|PDB:5GPL"; STRAND 110..123; /evidence="ECO:0007829|PDB:5GPL"; STRAND 129..137; /evidence="ECO:0007829|PDB:5GPL"; STRAND 153..155; /evidence="ECO:0007829|PDB:5GPL" HELIX 3..43; /evidence="ECO:0007829|PDB:5GPL"; HELIX 49..56; /evidence="ECO:0007829|PDB:5GPL"; HELIX 59..62; /evidence="ECO:0007829|PDB:5GPL"; HELIX 67..73; /evidence="ECO:0007829|PDB:5GPL"; HELIX 106..108; /evidence="ECO:0007829|PDB:5GPL"; HELIX 161..166; /evidence="ECO:0007829|PDB:5GPL"; HELIX 178..187; /evidence="ECO:0007829|PDB:5GPL"; HELIX 193..206; /evidence="ECO:0007829|PDB:5GPL" TURN 188..192; /evidence="ECO:0007829|PDB:5GPL" CHAIN 1..244; /note="Putative nucleosome assembly protein C36B7.08c"; /id="PRO_0000317135" MEAAQAFENLANLEQEFGKAEIEILKKQNELFQPLFEQRRDILKTINNFWVVVLEAAGDEISQYITPEDSVLLEKLENIYVERFNEKEPRDVRISLTFQPNEYLQDDNLTLVKEVRIKEEKAKDDEGLEKKITKYTSQPVDIHWKPGKSLFRKNKKLPPNFFDYFQWTGEEEDDDFDGATLTIFLAEDLFPNAVKYFTEAMTEEASDEDESVDLEEDEEEEDEEDEEGDEEKQEPPSKKSKKSN Q9HGN4 MUG20_SCHPO SPBC36B7.06c; CHAIN 1..151; /note="Linear element protein Mug20"; /id="PRO_0000278495" MSEIITSLQTELSNRHANMVSEAVLAFSEHHDSALHSYFLNARVKDVILESLRTTEEKLRALDKLQLDASKNLSNLLVEYNSINAELESVNSKISSISSQEYALEEFQALSQNFEKNLVQHRRNSQNKLKCAMEKLKMIETSTHKAILDNF Q9HGN5 YO45_SCHPO BINDING 33; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 36; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 52; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 57; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 60; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 114; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 117; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; MOD_RES 200; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC36B7.05c; CHAIN 1..279; /note="Putative E3 ubiquitin-protein ligase C36B7.05c"; /id="PRO_0000310489" MDEDETTYPEALRRLLIETPAAIWQLDDESAQCNNCGGPFTWFRRRHHCRWCGKLFCYNCCNSFAKLPVSSVSVDPTEDLIPQDMFIRDPDFLANDNDDDNDSQDSSWINVRVCVNCRQQLSELKELDLPYPITTCLNDDTTTRSNNQVIQSSCGNNLQRIEEPDDFVECPVCYAPLSSFKTLSERESHVANCLSNNSSSPRNMTEFLKHARRYISMQLSETSPCLGQECIICFEEFAAGDRVARIEYCLCIFHLKCYRDWLSTGAAGCPVHAATLHLS Q9HGN7 SEC63_SCHPO MOD_RES 566; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 572; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC36B7.03; CHAIN 1..611; /note="Translocation protein sec63"; /id="PRO_0000311762" MSSEYKYDEQGIFFPVFLLVGTSCCVLPLTYSTILGPSASKEKKNVRDPFQKYRPKDLKVQRKSIFRLRYIFLILGWLAIGFLSYKIANSRLKLNIWDPYEILGIAKGTSVDDVRRHYKRLSIKFHPDKVRNMVNTTREEVEKHYIEITNAYRALTDDKTRENYALYGTPDVPQHISVGIALPKWISESENSIYILGFYGLVFGIVLPYAVGKWWYGSRTYTRDHVHVDTVDEWFPKMETSLTLDELLSLFASSKELTSLVPNEKNPKEYILKLLFDHLNRKKTNNFNTHQILSQSDVVLNALLSVATAFGFANPVDNVLKLWQHIVQAIPLDAPFPLLQLPHLLMEDVKNLSIRNISSIPQFLSLSEEQTKDYLPNYSKNQLKEMREIANGIPRISVVAAKVLVDDDEYITVGAIANLILDLKCSYGTEVVPEVSTDGTETATKKDEEDAEKYHQSKDVVLGDVETLPYAWAPYFTQHHKTAWWIYVVDPRQNRVIVPPFSITDIPKTLRTFRIPFQVPPVAGTFSFQLHIMSNSYVGEDVISNLTMIVKDTSVLQEQLQEEAVSDLEDNSDIDESANAGKDFSDDENIGSDEEDESEYDPMDTDTSDGE Q9HGP0 PVG4_SCHPO SPBC317.01; CHAIN 1..372; /note="MADS-box transcription factor pvg4"; /id="PRO_0000199444" MGRKKISIAPITDDRSRSVTFVKRKQGLYKKAYELAVLADCEVAVTVIDRKGRLHVFCSSDYQRTLQQLNTLSIYELKNRSHFSSSPVEESSTVSPETTTGSFTPLNNKHLKSQDQPLSDSQLDTGDSPATSETTVQDYNPQVQSYCRPEPLSSNHVRSCPPFPPTQHHHPHTRPPHHPPHPHFHNNNYPPPYCFQSPVSPGATVPLQHHSPYPSDNGFPGHRRQTHFAPYYYPQRATSPSLKQVPTYLGTHVLQQDQSTYDQKVLMPPASYLSSPNQYTLKNVSPGNPACPPFLYEHPNPQLTPEMFDVKQGSPIPPTAYSGSSCETSQHTIANTPFLAYDRSPSLTNQEAESSFQDVASISPHSLSDVKY Q9HGQ3 CIS4_SCHPO SPAC17D4.03c; CHAIN 1..732; /note="Probable zinc transporter cis4"; /id="PRO_0000206116" MNVNSSAFERTNRFPSFPVLKDDQKTSSDSIAAAKKKDLLSLISSKSLLSSETLGWFSVICAFSITGSGLEVNTMSIPFYLIFGIFAFVSFTTQYLGIYSFSFQPFQLLNVIIASLSMVFITLGAFVLGTLDTTCLLLLAFKLFFIRNDPTPFNARSANLKNYIAFPICLFVINHILILLGYFQCSYSVFYASVFYILLGVFIRVFYLVNKEKFEKKELAFLFSSIVVACLIQFNVLPLGTINLSVTRFTILCFMQIFCINWDGIARIQFYLGKFDISLIMALISAIINKTASQNSIKIISCLYQVGFCFFKIGSSITANLKLPDNSRIYRLYNDFIVNGVLADKESRSIFYFFLLNVSYMFVQVIYGLWTNSLGLISDAIHMAFDCIAILVGLVATTLAKMPLNYAYPFGFAKIEALSGFTNGIFLVLISFSIVGEALYRLFHPPQMNTDQLLLVSFLGLVVNLVGILAFNHGHNHDHGSHHHHSHSNHSMCLPNTTNDINIFEEFEEEKDNVEAQKMGYTNDDHVSQHEHTHENSQEHHHEHNHNHDHIHKYNEKCDHESISLQNLDNDHHCHHHHENHNMHGIFLHIIADTMGSVGVIVSTILIQWFSWTGFDPLASLIIAALIFVSVLPLIKDSAKNLLSVTDPESEYLLKQCLSNISLSNSVISLSNPKFWTNERGEVYGILHIQVSIDGDLNVVRNEVFRKLSIAVPNLKHICIQSERPNNCWCGK Q9P381 CDSH_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC13A2.03; CHAIN 1..439; /note="Putative phosphatidate cytidylyltransferase"; /id="PRO_0000316216" MARKRTNKRNNSDKENGNVGVVQNKDSASSKTTEPARLTKHKSLARKPSQNFITRTIWTFLLLGIFFTALAMGHFWVVLLVTIVQIGVYKEVIAIASVPSREKDLPWTRFINWYFLMTTLYYAYGESIYAYFHHLFIMDSFMLPLVLHHRFISFMLYIIGFVLFVASLKKGNYKFQFSQFCWTHMTLLLVVGQSHFMINNLFEGLFWFFVPVCYVVCNDVFAYLCGKMFGKHPLIQVSPKKTVEGFLGGWICTVVIGSLISYVLMHFKYFICPTRDLSTSAFSGLNCTPNSVFLPHTYTIPAVFVDTFRLPETITLAPIYFHLAIFATFSSLIAPFGGFFASGLKRAFKIKDFGASIPGHGGLTDRMDCQFLNGVFVYMYFQSFIAEKSTSVADLLDTAVYSLTTTQQVQLVEDLQNYLISHGKTSVQAICSKLLQNSK Q9P383 NCBP2_SCHPO BINDING 13; /ligand="mRNA"; /ligand_id="ChEBI:CHEBI:33699"; /ligand_part="mRNA cap"; /evidence="ECO:0000250"; BINDING 35; /ligand="mRNA"; /ligand_id="ChEBI:CHEBI:33699"; /ligand_part="mRNA cap"; /evidence="ECO:0000250"; BINDING 104..108; /ligand="mRNA"; /ligand_id="ChEBI:CHEBI:33699"; /ligand_part="mRNA cap"; /evidence="ECO:0000250"; BINDING 115..119; /ligand="mRNA"; /ligand_id="ChEBI:CHEBI:33699"; /ligand_part="mRNA cap"; /evidence="ECO:0000250"; BINDING 125..126; /ligand="mRNA"; /ligand_id="ChEBI:CHEBI:33699"; /ligand_part="mRNA cap"; /evidence="ECO:0000250" SPBC13A2.01c; CHAIN 1..182; /note="Nuclear cap-binding protein subunit 2"; /id="PRO_0000310818" MASITRLDAVSPYLIRRFKNDLRALDAVKQSNCVYVGNLSFYTTEEQIYALFSKCGEIRRIIMGVDRFTKTPCGFCFVEYFENQDALDSLKYISRTSLDERIIRADLDHGYEEGRQYGRGASGGQVRDEMREEFDPGRGGYAKNRQPTSSRQLANYSGISSAPLGSSLELQSNPRYNRWKKN Q9P3U0 UBP2_SCHPO ACT_SITE 623; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 1076; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 112; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 113; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 115; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 721; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 722; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC328.06; CHAIN 1..1141; /note="Probable ubiquitin carboxyl-terminal hydrolase 2"; /id="PRO_0000080603" MATVKNLRIGKSPNRLIQDLDVFDSPSAGWNDPWSPHSSRYHWQLHSNLGESAVFDENDFWCVCQKTRKHLHVKVRRDRGKPLIEEPEENYGIKDRIPVYYEEEELPEPHVTSPTKSEFATTSTCMKWSSKTTKSEIEVEWRDSYLDANCIKEIIDSRRPSFASLLTKKSSSHQGSSHSSQPSLFTTFTSLELFLRNVLVHNDQRAISAAPEGTFERHVGKGRQIQSLMKSLLFEYHHENVNYVPTIADAPLTDEQKLNLYLARNELIVLANHFRDTKEDPAIVANPFPVRLARPALINAFGVPNYDSVVPMYTTVFRDNSASLPDDPAFIALGITNDYPDSFVRYFYEEQKKNDEANVRVYADALAHIYNLRKSSFLRDLIAADRKNGIVSSDVIQAAYSSLGLEAEVGPDYRYSQEKIFEAFHSALLRKPEFARAIRNDLETIGYARKSSEILNYVLSTEQAFYTVNEAYQWLGIKSNTEDAMVASVALVKFEDDSDKAIEAVKWIAEERNSSILYDFLASQGRPSNKKPKEVPMDEDLAYNTLGVQDRALSDDVLINVYGFAVEDHPEQSDTLRAALKCIGEVRNSRLITHYLEHGNLDIPPEVSSLDTPIGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKDLNMIENKEAVKKVGGRIVTRIEFLRALQFTYELRKLFIELITSKSSSVHPSSVLTYLALIPLTLDQVKSGTSSVMDLSSSRELSNLNERSITIDPRAEEQAQGLEQEQGQDEAKSPAEQSSSVNLIDFPMANTNGESQTQPHYFEVSEEEINSSMDLGRQQDVLECIDHVLFQLEASLGRISNSEDRLGSDNDLIRRLFSGKLKQTLNDASQGVRSNYEIFSHLIVDLFEEKQTLYDALDGVFETVNIDMGSETAQRSLCITELPIILQLQIQRVQFDRTTGQPFKSNAFVEFGKELSMDRYVEDTDGKMAPLLQRYWDLKREIINLQKRQQLLLTTNSNLMSSVDTLSILSKWAAQQQDSRLPINPKLPDILQEEINNVVAEVDMLKKQEASLKEERTHLFDNYISHSYDLLAVFVHRGQASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADTTGNNANPYMLTYIRKEYRHIIECVHREHNLLL Q9P3U4 HEL1_SCHPO ACT_SITE 304; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" BINDING 131; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 134; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 147; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 149; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 152; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 155; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 178; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 217; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 222; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 244; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 246; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 251; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 254; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 259; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 264; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 291; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 294; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 309; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 312; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 317; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 320; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 327; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 334; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260}; SPAC328.02; CHAIN 1..504; /note="E3 ubiquitin-protein ligase dbl4"; /id="PRO_0000310488" MSDLLDDEFYEEEFENDLLDASEFEDEFDEDAEIDDDGFTVERKRRRAHSVSYRVVSVRDLRASLNEKINQLTSIIDLTREQVLGLYRYFKWNRERLLERYIDAPEESLQKAGVGLSGSKQREVVHHEGTCEICYDEGCLPFFSAECDHEFCLACYRQYLDSRISEGESVIQCPEESCTQIVSIQSITKVLDEKSLDRYHRLLDRSFVDDNDHLRWCPAPDCEFAIECHVTQASLSSVVPTVTCNCGKQFCFGCGHDNHQPTICPLVKIWLQKCQDDSETANWIHANTKECPKCSTTIEKNGGCNHMTCKKCKYEFCWVCLGPWTEHGNNWYTCNRYEEKSSTSARDSQSKSRASLERYLHYYNRFANHEQSAKLDHELYEHTHKRMTQMQVDSNLSWVEVQFLKNAVDILFQCRQTLKWTYAFAYYLARNNQTEIFEDNQRDLELAVENLSELCERPCQDCSLSVFKQRVLDKTVYVRSRRDVLLDDTARGLAEGRWEYVVDV Q9P3U6 GHT1_SCHPO PTM: Not glycosylated. SPCC548.07c; CHAIN 1..557; /note="High-affinity glucose transporter ght1"; /id="PRO_0000050409" CARBOHYD 357; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSKTLTITMLLFVSMAGWMFGADTGSIGGITNMRDFQSRFADRYNPVTDTYSYSSARQGLITGMVNVGSFFGCLISSPTTDRIGKRNSIIGFCVIYLIGVIIQVTAVPSWVQIMVAKIWTGLGIGALSVLAPGYQSEVAPPHIRGTIVVTYQLCVTAGIFIAACINMGTHKLYKTAQWRVSIGINLLWGIITLVGVSFLSESPRYLVSIGKDDEAIQVMCKNAELPPDSDIIQTEYKQIKSDCEAAVEGGPCTWPEIFGKEIRYRTFLGMAIMSFNQLTGCNYYFYYGTQVFKGTGMESPYLASLILDAVNFGCTFGGLFVLEYCGRRVPLIIGGVWQSICFFIYAAVGNRALTRKNGTSNHRAGAVMIVFSCLFIFSFAQTWGPAAYVIVGESYPIRYRSKCAAVATTSNWLWNFLISFFTPFITNSIGFKYGYIFASCNLCASIVTFLFAHESKGLTLEEINELYLSDAKPWMSRPKNLSEMAEAKEVEREETRPKGESARYLEHADSNSDSEDLSSSANNDVHEPVARQDPFNENEVEKSRTRPSQESYTTSSN Q9P3W1 T2EA_SCHPO SPAC458.07; CHAIN 1..434; /note="Transcription initiation factor IIE subunit alpha"; /id="PRO_0000211224" MSNAPEIVQRLIKMIMRAFYETRHIIFMDAILRHSALTDEQTALLMGIPIKECRFIAGKLREDRLLAIQSRTEMKEGQQRQYHTTYFYIDFCSTIDSIKWRMHQLVKTVEDRMRNDFDSKGYVCPFCNKKFSSLDVLSLVTNEGTFACNVCGTELKDDEESAEMMSSQKRLGKLMGQVNGIIDALKRVDEIVVPQNNFQSALEHAVPVSLDTQNLSQQNLSKSNSDVRLSTSSPSITVDFSADKETDEKRERNCDKQVKAAQNILPEWHATSTISGSITRAGAKDAALHSFRTETVNEVQDTKTDITSEKSALDAYYATLRAKQKEESEFMDSENVDDEEDDDFLDVTTATSLQNKSTDYGSVKRKTENLNSDSDIQNKRTKSIEENNSLPPIVSTNGITDGDTEMQESKKNVIINGFNEDDEDDEDEADFEDV Q9P3W5 TEL2_SCHPO MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC458.03; CHAIN 1..868; /note="DNA replication checkpoint protein tel2"; /id="PRO_0000353821" MKSFASELSKPIQKPRLKEILKELQHIGVPSPCNLRLYHELISVIVPTFWNGKINSEIDFLLAKCFSTLLGLKLLCVRLDNFVQEANLQNIHLVTVYLELLEKAFECIDLDDNCKLIWESTVLSDHQKQSLWTEFIFFLGNFKITNSMSAAMLTFKVYDDSKRLKASSMADYIGVLSSKLACIISKPAVKTPEIYSKLFHYLLHSSNLKAFINPLIPLTQKFCVQLQKLFADLTVSDQMLFLNQLLLEHNTKYPTNFSYSTARDDRITGSLATLLRLNFSSTHFLRLIEFYWGVPTNLIIKRVEVVCSSISYKESDKKELEKTVDSLFNIWSNAQFLRSYTLLAQESLTIYLLLFIPKLEAKYLNNLSKSLMFSNAISCRLDSLDDDIRMHGMIMAEVISTYSGVSLSNPLAFDVPIMKTTKAKVLKSLSSLKDEFLPIEILNDESVIAETSIEKEETNVTHLEKPVISKNDDLIRGDDLEPYDFPDIDSEDTDDDPTVSRSKTHSPVYVQDLCKMLKDTESFEKQRVALENASKLIKRKSAFGTELRDHADELLQTLISLQNRFDLMNFDEMQMTAIVELLLTCLDICGPVICTNLFVSDYSMRQKILILSCISLAASKFNDDDNERLFPSQLLPGNLHDQFYSPTIEKISDELERKLVFPVMSECKDYAEGPKFLQTRYISKQSEIESKKPLPKANRLSLKVDKSLFLLLTSGYMLASRKTAFIEPLFLVYYLKTLGILFFETFTSKIEGANRMLREYVDVLNEVCRLRSDTPEVNEGLLFSFLAILEISSGRTLANEFGKHLLFFEAYTKFLFESPDQGEKVKSLSAAVLILFENKLSEFRTLALEKLLDDSAPLVPERFGLAGL Q9P546 RSSA2_SCHPO MOD_RES 46; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPJ698.02c; CHAIN 1..287; /note="Small ribosomal subunit protein uS2B"; /id="PRO_0000134369" MAESIARPSVLNATDDDIKNLLAADSHIGSKNLEVRMENYVWKRRSDGIHIINLGKTWEKLVLAARVIATIENPADVCVISSRPYGHRAVLKFAAHTGATAIAGRFTPGNFTNYITRTYREPRLIIVTDPRADAQAIKEASFVNIPVIALCDTDSILNHVDVAIPINNKGYKSIGLAWYLLAREVLRLRGNISRTTAWEVMPDLYFYRDPEEIEREEEQKAAAAAAAEEEAQLAAQTAAAEFEVTDSAAGTVDPTILDNATAGQVGQTTWEGDAEWNITGAAPSEWA Q9P5N2 AAT1_SCHPO SPBC359.03c; CHAIN 1..579; /note="Amino acid transporter 1"; /id="PRO_0000054173" MSAKDYDFDIESVLPEEKAPQVSEAKKDYISQESTVLSGQVDFVEPEHKGFFQNLIDGFKPAREADGNGGPALKRGLSTRHMQLMSIGGAIGSGLYVGSGSALADGGPASVIINYILIGIMMFFVIYALGEMAVAYPVAGSFNTYATRFIDPAWGFAVSWNYFFNYFVTFPFELTTCAITFTFWTDVNCAVWISIFLVVVIGINLFGVRVFGEVEFVLALIKVVATVGFIILAIIINCGGVPTDHRGYIGGSIIKQKPFRHGFKGFCSVYTTAAFSFSGTEIVGLAAAEVGDPRKTLPGAVKQVFWRVAIFYIVSLILIGLLISPDDPKLMGNGSASVSPFVLAIQEANIKGLPSVFNAVIIISVISVTNSSTYTAGRTLHGMANLKQAPAFFKYTDRLGRPLIAMIVVLSFGFFAYINEANNNGNDISDTVFDWLLAISGLSNFFTWGSICLSHIMFRLAFKKQGHSLKELGFVSPMGIWGSVIGLGFNILCLMAEFYVSLFPIGGSPNANDFFQGYLAACITLVFFIGYKIYDRSHIPSLDKLDITTGLKTYEYEETKDSSDTGRFRFFKKIINTVC Q9P6I2 DUG1_SCHPO ACT_SITE 101; /evidence="ECO:0000250"; ACT_SITE 167; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 99; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 133; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 133; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 168; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 196; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 446; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; SPBC1198.08; CHAIN 1..476; /note="Cys-Gly metallodipeptidase dug1"; /id="PRO_0000185274" MKMSLDKLYEVIDKKKDEFVTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGAKMEKRDIGYHQMDGQDVPLPPIVLGQYGNDPSKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLEDLIRAEAEKYFAKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAIMSTLVKPNGEILIPGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADISIYPDPKRTLQHRWRYPTLSLHGIEGAFSGSGAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVYGITPDFVREGGSIPVTVTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIKLFCTYVHELASVSP Q9P6J2 PCL1_SCHPO CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P47818}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28487; Evidence={ECO:0000305}; MOD_RES 3; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1683.10c; CHAIN 1..242; /note="Fe(2+)/Mn(2+) transporter pcl1"; /id="PRO_0000355075" MWSIFEARPKEAHSVNKIGWLRASVLGANDGILSLSGLLVGVVAANADIKVILITGVAGLMSGALSMAVGEYVSVSSQADLEDADLQLERREMDADWDAEVDELAAIYRGRGLDEELSRTVAVQLMEYNALEAHARDELGINIHTTAKPTLAALSSAASFSVGGIFPLLTSLITPLEYLSLVLPIATMFFLGMLGFVGAHIGGAKRVRAILRAVVLGLLAMAATALVGRLLEIHALSLQYAI Q9P6J3 MALT_SCHPO ACT_SITE 212; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 269; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; SPBC1683.07; CHAIN 1..579; /note="Alpha-glucosidase"; /id="PRO_0000310319" MKVVPSEKIKPNWWRETSVYQIYPASFKDSNGDGFGDLEGIISKVDYLKALNVESIWLCPIYPSPLKDMGYDVSDYKQIDSRYGTLEDLDRLMKALHERDMKLVMDLVLNHTSDQHEWFKESRSSKTNPKRDWYFWKPARYNEKGERLPPNNWRSYFDTSAWEWDEATQEYYLHLWSVGQPDLNWETPKVREAVHDILRFWLDRGVDGFRLDAINMISKDQRFLDAPITDDRYEYQLAYQYYANGPRIHEYLNGIGNILTEYDAFSVGEMPYVLDTNEILHVVGADRRELTMIFQFDFVDLDLDPNQHKYIEGSWELSDLKKSLKKWQSALLSGGGWNASFIENHDQTRTVSRYLSDSPKYRAYSSKLMALFIIFQSGTPFVFQGQELALANIPRDWPIDEYLDVETQNFWKLFMSGNPSQEEIEKTMDIVNKRARDNGRTPMHWDSSPNGGFTKAGVKPWMRVTNDYKEWNAANQVNDPESPYTFWSKALELRKELKDAVVYGSFELISEEDPSIVAFVRESSTYKLIILLNFTGNKVSYDCPLNLTSYEILLDNYKDFICMTSPVTLNPYQAVLLKL Q9P6L9 YKQ7_SCHPO MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 113; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 114; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 436; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 618; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 856; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC688.07c; CHAIN 1..1038; /note="Uncharacterized protein C688.07c"; /id="PRO_0000304048" MEENTAQKQSNATGLQRHVSGRWISNVPSYEGNEWSSEESESEDKESNLTSSENIGKNPERELNSDGTDRIIEEEEEEDDIENEASSFSEQSENENYDFSYPGTFVYRKAASSSHETLATKVVSADESARLWAEKRRFLLQKLGKDPNSKPIDYKSSMASSSTRSSQSSQVSAIQPQSQDDNRVSDIRQMENRRELNVKRRSVSSPAEDLAIRPLSFSRYKKAEEIPESLPPIKGRDSFSSVRELNESNVFARAPNKNRFSFASVAETGSGSNFSRATSSRSSKTRSVVYEPNHRHTSFFGDTLSNLSSSLNDKKSPNDDHAVLDSELMEQTLPDSAEAVEIANNVKEDIVSTANDDANELDNTSEKATLETSSKPVTEQAIEQSEVVQEVEEGDTNMTTNTILKPTDEIINKGYAYSITSSHSNHSNEKFEQIPSPDEKLSRTDIDTHVKQLQTTKSTDSLSIPFVESPQQNPEEELSDSLSNDFGIDAEKEKDENLSKPEHHPSITSVNSPFLYSPSKQPSGELDEENLKLRLQDSDVDDEVATIRSLKQNNATNSEVETVTNDPSFSQQPGTHSRILRNFDAISSIDSIPDSFSDSAVDLPVDSSKYTLVGKTQSNSNLLQDNAEKHISKSNLEKVDVKGDTSPNSVEQGIEPQAASVVGSPRSSLVSNNSLEEGALLKNSESLESIYGYLSEEPDPALTKLNTEDPFWTKGSSDDEHTIASVEQDVYPYKTSLPTIVEATTSHTESSNSKAPAIEETTTTKVEVVAAHDAVSISSNSSTHKSHSEPLNRDELEVAALSRGSLPEPPKPNKQIVVQEEDQRDTLSLKTSTTGLSSHSKSAENNSTQQSTTSPSINSGASADAVSSGISKKADNSETNLNYFATLDAFVKSPLMSFDGLGELGSTDQRYNFFNQKIQEYSAYDSGLDNWIQFCLEKDGEAPKEAPPPPRSEPVSTTTKLAKRITQPSLSPARSTVTITHNIATEAKKKSKSAANDILHLFKKKAKSEQSNAKSSSSSIKESKKMKTLFGKKLGFKS Q9P6M0 SLX4_SCHPO PTM: Phosphorylated in response to DNA damage. {ECO:0000250}. SPAC688.06c; HELIX 352..366; /evidence="ECO:0007829|PDB:4ZDT"; HELIX 371..377; /evidence="ECO:0007829|PDB:4ZDT"; HELIX 384..393; /evidence="ECO:0007829|PDB:4ZDT"; HELIX 400..410; /evidence="ECO:0007829|PDB:4ZDT" CHAIN 1..419; /note="Structure-specific endonuclease subunit slx4"; /id="PRO_0000349134" MSAEEYIEVSSSPDIFTDDDDMITIEPELNKNPKDCNSKRKRSVTECCEIRLITSKCDFESTQQLVHHNCTGHKVHEHNLNAVDEEDFDTENLPLLFSSFSDNESDILEPDLNTRVAEDNDVLLSRYSKIKNSASCRNTFEHSAYHSNREEISSSGFYYHRKPQLFEKSLEKLGNKSIEANRSPLIKELCESANSTENVCFSVSTVDEIQQRHPSAGHSIDSTCQSNSFLEGDSATHKKKKTDNIKEFTSCEFNDRSRTLLNYAGYMDTNKNADNEAKSLKEKLENFPVEKLRAIAESYGFKSSDSKATLIKIVESCLDAIDSRSQSKKLGKETPHDYLITSTKTVLEFDDIVTQTHRAISQVVKQAKDNSVWIKILTYSAIDVEEFQLWLKRKNLNVSLDLIKSWCDKYGVLMKGSWH Q9P6M3 MIS14_SCHPO SPAC688.02c; CHAIN 1..210; /note="Kinetochore protein mis14"; /id="PRO_0000278390" MSSHGDASVLPKIALESINDYSYVKSVFRQAIQEKLAIHLPEQASREAGMGREDQLRIRVKEMLNELIESTFSIIQENVTINGFDANSALQDPKNSDQIEPFDLALRTRVQQLFNEVEDAHVLVARYRKSVPAQYEKAYVDAMEQQTAFLRNVKDDYVSLQDKEVENPDEQTSTTVFRKEDIDRYEQTIAKVAYLKKNLPRVVARLEKTP Q9P6Q2 ENOPH_SCHPO BINDING 8; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03117"; BINDING 10; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03117"; BINDING 115..116; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03117"; BINDING 149; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03117"; BINDING 172; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03117" CATALYTIC ACTIVITY: Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate; Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77; Evidence={ECO:0000255|HAMAP-Rule:MF_03117}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03117}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03117}; SPAC644.08; CHAIN 1..216; /note="Enolase-phosphatase E1"; /id="PRO_0000314113" MVKNLLLDIEGTVGSISFVKDKLFPYAASRYESYVNENYESDENLRELGKTPEEALINLRKLHAEGSKERSFKMVQGRIWKKGYESNELTSHLFPDVVPAIQRSLQLGMRVYIYSSGSVPAQKLYFEHSDAGNLLKYFSGYYDTTIGLKTECGSYVKIVGNSNPREWLFLSDNINELKAARKVGLHTGLVVRPGNDPVVDTSGFPVYNSFEILFTE Q9P6Q6 CET1_SCHPO CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Evidence={ECO:0000250|UniProtKB:O13297}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; Evidence={ECO:0000250|UniProtKB:O13297}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O13297}; SPAC644.04; STRAND 77..88; /evidence="ECO:0007829|PDB:4PN0"; STRAND 98..101; /evidence="ECO:0007829|PDB:4PN0"; STRAND 103..105; /evidence="ECO:0007829|PDB:4PN0"; STRAND 112..116; /evidence="ECO:0007829|PDB:4PN0"; STRAND 147..159; /evidence="ECO:0007829|PDB:4PN0"; STRAND 167..176; /evidence="ECO:0007829|PDB:4PN0"; STRAND 179..194; /evidence="ECO:0007829|PDB:4PN0"; STRAND 201..211; /evidence="ECO:0007829|PDB:4PN0"; STRAND 222..234; /evidence="ECO:0007829|PDB:4PN0"; STRAND 237..245; /evidence="ECO:0007829|PDB:4PN0"; STRAND 249..251; /evidence="ECO:0007829|PDB:4PN0"; STRAND 256..264; /evidence="ECO:0007829|PDB:4PN0" HELIX 56..67; /evidence="ECO:0007829|PDB:4PN0"; HELIX 107..111; /evidence="ECO:0007829|PDB:4PN0"; HELIX 121..137; /evidence="ECO:0007829|PDB:4PN0"; HELIX 266..277; /evidence="ECO:0007829|PDB:4PN0"; HELIX 282..299; /evidence="ECO:0007829|PDB:4PN0" TURN 68..71; /evidence="ECO:0007829|PDB:4PN0"; TURN 89..92; /evidence="ECO:0007829|PDB:4PN0" CHAIN 1..303; /note="mRNA-capping enzyme subunit beta"; /id="PRO_0000210117" MDLKGLLHEENELPSIEKRKIDENAVEHDKVERKRTKSVAVPKIEMNFLNKPIVPDTTKVISNFLTHYLITEPVEHVEIEAKLGTLIDLETQNRFEFPVMNETILNPEFNLRTRFESDMTASEHKYLNEFLNQAFRDSQKPGRLPFAYKHTKQVDLFYETEDNSRDKIRVSKNQSDNQVLACVKKRRVADLFLYCPNDAFDIRISISDELPVSMPSGNQQPSLTRLKDRVGYVHQEIKIDLTKTTQNDPVYDTTERHELEVEFGNIADLRDRAQKAKDGMEAPLFRRVQLFMDNVRILRREHS Q9P6R4 MU172_SCHPO SPBC13E7.06; CHAIN 1..331; /note="Meiotically up-regulated gene 172 protein"; /id="PRO_0000278517" MTTPIVFCNPSNIEESLLYINKSLFSKGVIQAEKLRLSHDIRDNCNIVNIIYRLLRATDEERLEKESLLDAIKNNEYEKQRDNNTIKRLKNELELYQNECQLQLNKVRTLERDQAELITQNKGLKDVNAKNELTLKALKNQLSVSLRQHEQQMETLKGNYGLVKARKGRNLNSMLIVKEPIKQNTNAPILPETASFLQQNDENSNFLNSRVNNDEFQLLKGLNNELKKSNGTLLTCLSGTLNSLVEMLSPLYERPNSNPFEVCELNAILLDAKIQNQLLFIRNLLHERKYVSIDELDAILEENEKNKHLINILQKENKRVFEFLTNMHDKF Q9P6R8 CWC24_SCHPO SPBC13E7.02; CHAIN 1..533; /note="Pre-mRNA-splicing factor cwf24"; /id="PRO_0000055892" MEQKNLNINQASGSKINTELAVPIFQSRRRHRPRQGLKRKKGFKRDDDSGGSSESSNEDMRDNIPIVSGRKKTVRLNRLQRESEQFENSALKDINVEYQSNLSATGESVNTTTVSAINEDTREVILGRPSPKLANQSTLPTELFQSQNDYSRFLPKRKDFEKKSQVGPVLSSNASTVRMNTIIDYQPDVCKDYKLTGYCGYGDTCKFLHMREDYKAGWQLDREWDSVQEKYKKGAKLEEGMVKNEKKEDIPFVCLICKKDYRSPIATTCGHHFCEQCAITRYRKTPTCIQCGADTKGLFSVDKNFDRLLKNRKSKNDEAVKQKVGGFESNNSATTEVSERKDREASFQGFADTLAKPNTSAQQKMPSLGDNSNTIISKYFIREITESNIVHFKRLVRVVLEASYSDKFYRLVLKNPDYARIATFEDKFVGAISSLVAEDNSLYVTVLCVLAPYRCLGIGSLLIDHVKKTAINNNIDRISLHVQTTNESVIKWYTAHGFKIVKQINDFYRRLENKSAFYMVCPLSAHNNIISNH Q9P6R9 CWC22_SCHPO MOD_RES 662; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 664; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC13E7.01; CHAIN 1..887; /note="Pre-mRNA-splicing factor cwf22"; /id="PRO_0000215675" MEKEDKSFGIGMLDYNRENPESSGHSRVAVIRKQKTEQENNNLSWEDRHYIPDLHKSNKIKTPTSLADEKKSHNELDPKAQIKKLMETRSGGTYIPPAKLKALQAQLTDVNTPEYQRMQWEALKKSINGLINKVNKSNIRDIIPELFQENIIRGRALYCRSIMKAQAASLPFTPIYAAMTAVINTKFPQIGELLLTRLIVQFRKSFQRNDKSMCISSSSFIAHLINQKIAHEIVGLQILAVLLERPTNDSIEIAVMLLREIGAYLAEVSTRAYNGVFERFRTILHEGQLERRTQFIIEVLFQTRKDKFKNNPTIPQELDLVEEEDQITHYISLDDNLDVQESLGIFHYDPDYEENEKKYDAIKHEILGEEDDDENEEDEEDSEETSESEEDESVNDEKPQVIDQTNASLVNLRKSIYLTIMSSVDFEECCHKLLKIDLPEGQEIELCNMVIECNSQERTYAKFYGLIGERFCKLSRTWRSTYEQCFKNYYETIHRYETNRLRNIALFFANLLSTDSIGWEVYDCVRLTEDDTTASSRIFLKIMFQEIVEALGLKSLVERLHDPNLVPYLHGLFPVDEARNVRFSINYFTSIGLGALTEEMREYLLTMPKSEPKEQDSEGYSSGSETGSTYSSSYSSTYSRGRSYSRSTRSYSKSRSYSRSRSVTPINNINHKKYIRKDRELSPRGRERSSNRNSYSDLSRSSSLSRGRSRSYTPEGRLIESEDKGYRSRSSSPASRKYRSRQRYRRSYAGSTSRGRSFSRSPSYRRRLSMSCSVSYSRSPSPAARPISRSPARNKRSYDSLSYNRQYSPKVSRKRSNESRSPSPYTLRKQKTYHLNKRNEDFVVKMDKKGSESPVILAPWLREVDDGELYKDRNSESDSVRKQPRAD Q9P6S0 GSF2_SCHPO SIGNAL 1..27; /evidence="ECO:0000255" SPCC1742.01; PROPEP 1540..1563; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000014208" CHAIN 28..1539; /note="Galactose-specific cell agglutination protein gsf2"; /id="PRO_0000014207" CARBOHYD 224; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 263; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 302; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 341; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 380; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 419; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 458; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 497; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 536; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 575; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 614; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 653; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 784; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 1510; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 1516; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 1529; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 1532; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" LIPID 1539; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MSVRRFLSTSARALLFTAALLPSLTSGLPSGNVRILQKGMEPEDYLSSASQNEVPHDISLPKTELADPNFLVDDMPTLLGRDAAVDPSMFTSTFTVKNGNDANYITASPVSNDASMTAISTFTSGKEASYAIQASPSTFLPDSTTTSGSQVSNAVEASSTFVADTTSTSCNPATVLIVTTSGSTSTSCPPPTTILIVTVPTTTTTTTVGYPGSVTTTLTGTPSNGTVIDTVEVPTTTNYGYTTITTGYTGSTTLTTTVPHSGNETGPTTVYVETPYPTTVTTTTTVGYPGSVTTTLTGAPSNGTVIDTVEVPTTTNYGYTTVTTGYTGSTTLTTTVPHSGNETGPTTVYVETPYPTTVTTTTTVGYPGSVTTTLTGAPSNGTVIDTVEVPTTTNYGYTTVTTGYTGSTTLTTTVPHSGNETGPTTVYVETPYPTTVTTTTTVGYPGSVTTTLTGAPSNGTVIDTVEIPTTTNYGYTTITTGYTGSTTLTTTVPHSGNETGPTTVYVETPYPTTVTTTTTVGYPGSVTTTLTGAPSNGTVIDTVEVPTTTNYGYTTITTGYTGSTTLTTTVPHSGNETGPTTVYVETPYPTTVTTTTTVGYPGSVTTTLTGAPSNGTVIDTVEVPTTTNYGYTTVTTGYTGSTTLTTTVPHSGNETGPTTVYVETPYPTTVTTTTTVGYSGSVTTTLTGSGSNSIVTETVDVPTTTSVNYGYTTITTGWTGSTTLTSIVTHSGSETGPTTVYIETPSVSATTTTTTIGYSGSLTTTLTGSSGPVVTNTVEIPYGNSSYIIPTTIVTGTVTTVTTGYTGTETSTVTVIPTGTTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTSTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTSTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTSTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTSTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTSTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTSTGTTTVVIQTPTTVTATETDIVTVTTGYTGTETSTVTVTPTGTATGTTTVVINTPTTTGSEVLPTTGATGTAGTETQLTTATEVQPTTGATGTAGTETQVTTGTETQATTATETQATTATEVQTTTGATGTAGTETQATTATEVQPTTGATGTAGTETQVTTATEVQPTTGATGTAGTETQVTTGTETQATTATETQATTATEVQTTTGATGTAGTETQATTATEVQPTTGATGTAGTETQVTTATEVQPTTGATGTAGTETQVTTGTETQATTATETQATTATEVQTTTGATGTAGTETQVTTATEVQPTTAVTETSSSGYYTTIVSSTVVSTVVPGSTVYPVTHVTTTTGVSGESSAFTYTTSSTQYEPSTVVTTSYYTTSVYTSAPATETVSSTEAPESSTVTSNPIYQGSGTSTWSTVRQWNGSATYNYTYYTTGGFTGGNNTNVTGLYPSSAGANKPIAYLTFVSLFVYIVTLI Q9P6S3 UDS1_SCHPO MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 53; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 57; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 59; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 60; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27.04; CHAIN 1..1052; /note="Up-regulated during septation protein 1"; /id="PRO_0000116855" MGFHGCLSTDEYEPELIEKYGNPEPPSSSILINTRPVNPFLSTFVYVGKASSSEDVSISTGEEEMRTLLVASAVKDAKGWVYLSGKDVEEIKQKIKNLQGLLGVSIKKLAVEAKIREAAKNLMVAQAKEKKGKHKQSTIEHYEQCSRRVRELSSKIWLIERKLAEFYMHLLKHMVAVCIAELKPGSCSKVSSPVSAITADESATGFRDEEIMNNEEIEQLVERMSRILEIAQSMGNSIREPSVLDAVQMNAGERLLEQVRHLELILKQIYEKKLEEDADAKDIAPRAIVNFWRLLTELFRGDNDTPEKSNALPDDELDKHLKSDFDIESFCFLLHHLLSLYQTQKKELASSNELLASVRDENTKKLKELQDIIEEQSKHMARLHREGFSEAAENNDKPKETMPCTYDSSLADDHSDTSNLSKDKANTLCAQCSVYLSEKYQQQQSLLQLESNIQQLENEKKAAKLIEKDLLSQISHVKLQFEQQIKAHHYAKDQVRNLNDEMVALRAELEVVKAMNSQPDDPDSDYAIKQNNALQNRLEALTRENELLQSRVTTLEMEKEVQEKNSATVSNLTLKQLQMENIFASLNLENSFDFGMPLMGPYTQQNLQLEDEISEISSPSYSSDDDRKTISETQPAPKQNINEEFENSTSTDGSETNKNEQGNSLSTPDNEPRLRKESLSSDVLLDGSEKPAQAELTINSENFPVDCSLPVQTGADVVVPDTTDEEVITSEPVKLEQPINENSNVEEAEKDYQPSEKDDKSLIGGILSTVEMTQSTDVNDEIENTLTIPVEVEHSDNIDKGSEENDLGKEAVDEANNNQNDVLESVVVEQSTTTDDCENKVYEGQMNDKNSSLDMVNACEGINQTAIGFVEKPDKVTELIDEAEENIDISQDISMTETNAVDDEVQAENSILQDEVEETRQDDIEKDELEDIKEVKEDENLTTLEETIEIPANDIEVQDPEQCSCMNSTENDNITTENSSEIVQVIHTEDDSLHFDDNVSTDSVSLGNKSRISMDSMRNDCEAFLPKKEKFGSLRTLHSFESSMRRVSTSAA Q9P772 GUAA_SCHPO ACT_SITE 96; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 189; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 191; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" BINDING 244..250; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"; BINDING 317; /ligand="XMP"; /ligand_id="ChEBI:CHEBI:57464"; /evidence="ECO:0000250|UniProtKB:P49915"; BINDING 475; /ligand="XMP"; /ligand_id="ChEBI:CHEBI:57464"; /evidence="ECO:0000250|UniProtKB:P49915"; BINDING 531; /ligand="XMP"; /ligand_id="ChEBI:CHEBI:57464"; /evidence="ECO:0000250|UniProtKB:P49915"; BINDING 537; /ligand="XMP"; /ligand_id="ChEBI:CHEBI:57464"; /evidence="ECO:0000250|UniProtKB:P49915" CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evidence={ECO:0000250|UniProtKB:P38625}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q4WFT3}; SPAP7G5.02c; CHAIN 1..539; /note="GMP synthase [glutamine-hydrolyzing]"; /id="PRO_0000286154" MSSTEVPGEVSTSVSSYFDTILILDFGSQYSHLIARRLREIHVYAELLPCTQKIEALPFKPIGVILSGGPYSVYDDIAPHVDPAVFELGVPVLGICYGMQEIAWLNGRCVEPGIEREYGPATVSMEPEIKTEVFKSFFNSMPKEFEVWMSHGDRLSALPNGYETIGRTKNSPFAVIAHVTKPIIGLQFHPEVTHTPLGLQLIKNFAIEICHAKPNWSMENFVDKEILRIRKMIGPSDHVIGAVSGGVDSTVASKVLKEAIGDRFHAIMVDNGLLRLNEAEIVRETLNKHLGIQLTVVDASEEFIGKLKGVTDPEKKRKIIGNTFIHVFEREAERIVKETNGKVEYLLQGTLYPDVIESISFKGPSQTIKTHHNVGGLLKDMKLKLIEPLRELFKDEVRALGELLGIEHSLVWRHPFPGPGLGIRILGEVNAAQLEIARKADHIFITEIRNHGYYDKISQAFAALLPVKAVGVMGDKRTHEQVIALRAITTSDFMTADWYDGFSIKFLKLVSSRICNEVSGVNRVLYDISSKPPATVEME Q9P774 PRP16_SCHPO BINDING 515..522; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC1711.17; CHAIN 1..1173; /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16"; /id="PRO_0000055149" MLSHNQNDLLFTKLIDKLTDYMSSKDAATSLASRVLTIAKGSSSSTEFSNALHTFGRFSDNDSVLIYDLCKSIIGLETNLGISKDKLPGNDGSQVAGLVLSNRSGLKGREPKKSQLGLDVLAVQKKKEKSQVEGRSELSQVENDSLESIGNYDRVEFKRPKNPHEKHFRPLRQRSSVDDHQEFESEDDKYRRNSYSSWSGSNFESSNGSNRRRYRTQMEEPLSSKRRNRFGNGSRRDVDSSKYSHDSDYSYGAHSSWDARDVEYPEEDPESKADRQRWEEEQAHLDRDWYMNSESQNLLGDEVHNPFSDFETVEDRAHEAEFIEKQKKHLSIEASDRFKENSMWEKNRMITSGVSKAPGLESDYSLMEERRVHLLVDELRPHFLDGAEFSSKKVGDITSVRDPQSDLAINARLGSRLVRERREFRERQKAASAATSLAGTSLGNVMGLKDSNDEDAKAGTTPVKVAGRSEQSNKKDTEFARTKSYREQREFLPAFAVREQLLSVIRDNQVLIVVGETGSGKTTQLAQFLYEDGYHRNGMIGCTQPRRVAAMSVAKRVSEEMGVRLGSTVGYSIRFEDVTGPDTVIKYMTDGVLLRESLMQNNLEKYSVIIMDEAHERSLNTDILMGLLKKVLSRRRDIKLLVTSATMNSQKFSDFFGGAPQFTIPGRTYPVDIMFAKAPCSDYVEAAVRQVLQIHLSQPAGDILVFMTGQEDIEATCEIIADRLNQLHDAPRLSILPIYSQMPADLQAKIFDSAEPGVRKVVVATNIAETSLTVHGISYVVDTGYCKLKMYNSKLGIDTLQVTPISQANANQRAGRAGRTGPGIAYRLYTEMAYIREMFETTLPEIQRTNLSNTVLILKSLGVEEISDFDFMDRPPNDTLMASLYELWTLGALDNFGKLTTLGKKMSLFPMDPSLSKLIIIAEDYKCTEEIITIVSMLSVPSVFYRPKERAEESDAAREKFNVPESDHLMLLNIYQHWQRNGYSNSWCSKHFLHSKTLKRARDIRQQLVEIMSKQKISLESVSDWDIVRRVLCSAYFHQAACAKGIGEYVHLRSGMPCHLHVTSSLYGLGYLPDYVIYHELVLTSKEYMNIVTSVDPYWLAEFGGVYYSVKERFRNETESYDRVFSSKPQLDAQIAADRELDAKQKLAKNQEPVKSKRKSVIRAKPPRRVRGF Q9P779 YNYB_SCHPO BINDING 44; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 70; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 89; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250" SPBC1711.11; CHAIN 1..390; /note="Sorting nexin C1711.11"; /id="PRO_0000315964" MLKCTIKNEQIETLRSGDTFVSYEIETESDLPVFEDKKFSVRRRYKDFEMLHNILSHDYNGYAIPPLPRKYTVSSFSGGSLSPIFIARRMQSLQTFLDRCSTHPVISNSMHMYQFLENNSWKSYYHNAWMQSENTKSKGNNVSGGIESSIQNLDPYAQSLYETAKQLLQNADTDLSKLEKTCVQYMNSVQNFPTDIPVPSNLSISNLDVVSVEFKRLKRNSIFLINSFHSKVITSIQDLEDYMVVFKSLIKSREQKVKQFEHFQQIVQSNSNNPDQSSRSDPNFVEATPVVQQTPELKPSPNTTIRTSSLFSIPKFFKKKRYSLGQDDANPMELLQLSFQELCIFNEKLEQELNFLRERIDVEMRKTLQMVCDCHVEYFSGILEQHAVKE Q9P780 NPL4_SCHPO SPBC1711.10c; CHAIN 1..572; /note="Nuclear protein localization protein 4"; /id="PRO_0000339454" MILRFRSKRGMARAEFQPTDTLAMLSAKILSDILKNDYSPENVSLCQNESDQGVIFSNLNDQTLQDAGLTHGQMLYLRLGTPNSDIASSNNEPALTVTGAPKQVSTPDVSEKKPSMPVIQDPIDDSLEKEDGLIRRSMTSLCRHGPKGMCDYCSPLEPYDESYRQENKIKHLSFHAYLRKINSNVNKYASSQSFIPPLEEPSFTVKEKCPSGHPPWPAGICTKCQPSTVMLNLQPFRVIDHIEFASPGIVDSFLNKWRQSGFQRIGYTYGHFEQYNNVPLGIKGVIEAIYEPPQVSEADGVTLEEWADEALVEQVATACGLRRIGIIFTDLTDDGSNSGKVLCKRHSDSYFLSSLEVYNSANFQTKFKNPCKWSRSGYFGSKFVTSVISGNLNGEIEVMSYQVSNIGTALYQADLIQPSVDPDRMLVKKEDQTRYVPDVLYRYTDKYGKQVSENAKPAFPVSFLLVTLTDGFPEKPDPLFSNNDTSIITTLESTDETGRLRQLAKLFDHNAIANGSLSNFSVLLAIAKLSILGKDDLAALASYATAPTEENEKNLNSRESYQTLLAILYSSL Q9P790 VPS72_SCHPO MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP35G2.13c; CHAIN 1..316; /note="SWR complex protein 2"; /id="PRO_0000339144" MSATESLVAGRTRRANAGNKMRELLEKEHLRMTQQNAEIEKEDEEYNIEEEEEAERDIEISSESSDEEAELKKLEEEGEEVEKILRDEERIKKRKIQKNRAANLQRTLQPPKRPTPSAASEVPKKKYKKIKVDPSARRTSSRMHTVLMAQSTETRLQEAKPRRKYTVSASANRQKGTMTQQQRFEEAAKTEAQNLSSLRNYVHLEEQRRLRLKRNAAKHRQLREPILKFISKTISTEDGREASNYYVAPLEHPLCHSAPPLQMPQHRAVECVITGKPAIYLDPVTQLPISNVQAFQQVREVYNQRYSWSAMLNLFH Q9P794 RU1C_SCHPO SPBP35G2.09; CHAIN 1..182; /note="U1 small nuclear ribonucleoprotein C"; /id="PRO_0000363373" MPRYLCDYCQVWLTHDSQSVRKAHNAGRAHIQNVQDYYTKVAQEEAQKQLEERASSGFLKKGNGSLDLPYAYAFPPKYNVFNLGCPPPPYIVSANTYMAPKGMNAMNAAAFVPMMPAVNLTNQVAFSAPQTTASSNTQLTQQQQSLPQTNEHQRARTHSNANNHFTKTHHQGQRSHQRFVRA Q9P795 AIR1_SCHPO MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP35G2.08c; CHAIN 1..315; /note="Protein air1"; /id="PRO_0000356248" MDMTVSNQKAESDDGSDIDDAALLQKINSLPIDQSITNSVSLEKHDFQGSDDHDSSTDLSDSTLEDVEGSEWADVSRGRYFGSDPSESIVCHNCKGNGHISKDCPHVLCTTCGAIDDHISVRCPWTKKCMNCGLLGHIAARCSEPRKRGPRVCRTCHTDTHTSSTCPLIWRYYVEKEHPVRIDVSEVRKFCYNCASDEHFGDDCTLPSRSNYPESTAFCEANCPSGNDASNKEFFETRRKEFQLERREQNRNQKSSKQRPFHKPGNSLASRLGSKPKSFKRKHSPPSEENGNLSFHSSDGRKFTKTSKKNRKRKW Q9P797 NU131_SCHPO SPBP35G2.06c; CHAIN 1..1142; /note="Nucleoporin nup131"; /id="PRO_0000290668" MFIVHRRFFQNEKAFTPAGKHEKVADGNKHETLATSEYPKVCASNDLYKILQISAPKVGNFTIHDAPVVGLIDSILEYYLYISVKVRKAWIAGYGSQPQNLICFDWERFTGILDQQSLNSPPLAGFVKPDPTSAEPGFLLLWPASGDLFYWERTSLMNVEVSAPEFPGFLHYRIQLKRYESCKNLVSAEPAGFFLTLSSGRLLHLNLKDSDGNSSIQVRILFPGLHIPNCLLSLYNSIFAFTSGRVIPIRCGSIKGPGERLVYSMHSGSTLRIWEIFGTGDHHLLRGFDIYDIILDSIQESFSYVNRFLILDFSVSTSDPYTLACLVSWRDNASLFNYAAIIISFNHQMIPHVSQFCHVRSYLSAILPSVCRIFLPSPGTVVFCVFDVTFAMFHKVRGKEGTFYVEENLVVNNLTSKSRVLDFGMEDAIYEKSTHTLLKTPALILLTEGHGIIRIESSASYLKTSFSATTYLRSRLSQFASQSPLFREQFLLNFDFTYNLSESEVYNTVFNLCDELYTTPCKKNMSVLETLHSQQRDLMEIVLVAFKYLHLSPSNRLQLWLKVAYCSALADLYELLMCNEKMSNLLRRVLKIMSSNDNIDELFLKKCLNINLLLQHLSSEYSQISGQDASNAQKRIEVIVNVNNVYGTIFGNELAYRQEKISKFTDPSSVIRSDLWTVEVDHLDLLRKQIEDSISLHRDVRDSKDAHILKVSNKLRKQILHLVEQNCLLIFDLHNGTDDTIVKSHNFQKFEEEFGNSRKEWLQYLASVGYLEKAIDLAEKVKDFQTMVILLDCLDPKDPTIKLQKQKACLNKYKEEFADVIFFYLVDTEQYASLLHDFLEYQSLLISFFEANDLLNLLWIFEAQNGNYGRASEILFRDCEPEENRIIGKISQLALAKLYSWTNRIEGENIILSNETEVIENHLAILLIQEQYAEMLSSLVDITEDEGEAVEAIVTSNCVNLSENSIRAWLVSSAVERLIQNEYTTLCEMVDFFSSFSLRECSFKEVDLALELLERATITKDVYFYLKDLVYRRFLLQVNWAEIIDAHEDLESSFFPMVKEIMLESDFLIWLQHMEHNIHDESKHYLKSEKNFLQSVYSSLSESQVEDYQMELFREKQIFSVLCKDRELYILIPKLLDVATKQ Q9P7B8 ARB1_SCHPO SPAC140.03; CHAIN 1..399; /note="Argonaute-binding protein 1"; /id="PRO_0000284724" MAEGDFKNDSTGCIGDSVEFTTFKKRTGKSLGNRRKKRGLSGWEPYFQEPELTAEEKLENETLYSRNIPLTVRMERFIQRYRSRRKWSDPTRIRLFTMYLDLGGVSTGQKQFTGGTDINNDAKAREVSAQTTTDYIEYDILDEYDIDFKWVAGVFLSSHILYNAGLTKEEDLQIACQIVRNFLLSVLHNNVAPEFEDNIRDACLLAEQAETELISNKRLSTKLPGRLQRALASIHVDNYKGLWDKSQSDRTSDSSVNFIESNNTKFMPNDELFEPDGISRFSTQQARDYIQRTLGPRYLTGKVVEQEYLTVKLVSKTLLNFSNQSLCKAVFIVWDPPGSKYSQDTNKERLEVILESDLLNNTVDGTHLEGSFTFLDNGLTILDTVLAVLPTFYEEVKDE Q9P7C5 YJU2_SCHPO BINDING 48; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03226"; BINDING 51; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03226"; BINDING 84; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03226"; BINDING 87; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03226" SPAC9.13c; CHAIN 1..270; /note="Splicing factor YJU2"; /id="PRO_0000079612" MSERKVLNKYIPPDYDPSIRPPKKKKKFQGPNGGKLTVRLMTPFSMRCHTCGEYIYKGKKFNARKEKTGEKYFSIDILRFYIRCTRCAAEITFITDPKHADYAAESGASRNYEPWHEKRLQEYEENELAERNDIPEEDEMEKLEQKTLDTKRQMQISDALDELREKSARRSRVNIDDAIALLKEDAYGSIEEEESKKRKFEEEEIDREAKSLFSSQDGEIIRRLNAETTVEKELPKPIDLVSEKLATSNIPNFQPPKYAKRKMEKKKVLV Q9P7C9 DCPS_SCHPO ACT_SITE 244; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 152; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 174; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 235..246; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616; EC=3.6.1.59; Evidence={ECO:0000269|PubMed:12366830}; SPBP4H10.20; CHAIN 1..304; /note="m7GpppX diphosphatase"; /id="PRO_0000362149" MEESSAAKIQLLKEFKFEKILKDDTKSKIITLYGKIRNEVALLLLEKTAFDLNTIKLDQLATFLQDTKLVENNDVFHWFLSTNFQDCSTLPSVKSTLIWPASETHVRKYSSQKKRMVCETPEMYLKVTKPFIETQRGPQIQWVENILTHKAEAERIVVEDPDPLNGFIVIPDLKWDRQTMSALNLMAIVHATDIASIRDLKYKHIPLLENIRNKVLTEVPKQFSVDKNQLKMFVHYLPSYYHLHVHILHVDHETGDGSAVGRAILLDDVIDRLRNSPDGLENVNITFNIGEQHFLFQPLTNMNA Q9P7D7 LCF2_SCHPO BINDING 252..263; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P69451" CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPBP4H10.11c; CHAIN 1..689; /note="Long-chain-fatty-acid--CoA ligase 2"; /id="PRO_0000311761" MDIKDYYCVETKDSKQPGESYIYRSIHSAGKLLDTPEDGVSTVYDLLCTAAKNHGEKQAMGSRKLIKENREEREIIRKVDNEEVVEKKLWTTYELGPYEYISFNKVYEIALALGSGLVASGITSETTMLFFAATSAKWFTTAQGCSSQAIPIVTAYETLGEDGIYTSLDECKSRAIFTDPNLIPKLLGPLKQSTWVKLIVCSSTPSEDLVELVKSTAPDVEIITYDNLLSLGKEKPQPPHPPKADDICCYMYTSGSTGKPKGVVLLHRNIIAALGGINRILSQHINVKDYVLAYLPLAHIFEFIFEMCCLYWGGVLGYASPRTLTDASVVNCKGDLTEFRPTVLIGVPAVYELIKKGILAKVSSMPAHRQKVFSGSLSLKQYLIERNLPGSAALDAIVFNKVKAATGGRLRYCISGGAALAASTQAFLSSCICPVLPGYGLTETCAGSFVLSPEQWHLYANTVGFPIPSIEFKLVDIPDLGYYTDSSPPRGEVWIRGPAVCNGYLNRPEDNKAAFTEDGWFKTGDVGEIAKGNTLRLIDRKKNIVKSLNGEYIALEKIEAQFFTSPLVSNVCAYADVNHAKPVVIVNPDENGLRTYLTKNSGSSFNGNPNDTLTNLCKDSGVQHLILKELINIGKQQRLASIEIPEGVVLSDFEWTAENNFLTASRKVKRQVIVAHYSDEIQKAYSKKH Q9P7E3 DCAM_SCHPO ACT_SITE 21; /evidence="ECO:0000250"; ACT_SITE 24; /evidence="ECO:0000250"; ACT_SITE 85; /note="Schiff-base intermediate with substrate; via pyruvic acid"; /evidence="ECO:0000250"; ACT_SITE 99; /note="Proton donor; for catalytic activity"; /evidence="ECO:0000250"; ACT_SITE 275; /note="Proton acceptor; for processing activity"; /evidence="ECO:0000250"; ACT_SITE 288; /note="Proton acceptor; for processing activity"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50; COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250}; PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain (By similarity). {ECO:0000250}. MOD_RES 85; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000250" SPBP4H10.05c; CHAIN 1..84; /note="S-adenosylmethionine decarboxylase beta chain"; /evidence="ECO:0000250"; /id="PRO_0000030031"; CHAIN 85..378; /note="S-adenosylmethionine decarboxylase alpha chain"; /evidence="ECO:0000250"; /id="PRO_0000030032" MSPTLVVDQENSEEFNTSSFEGPEKLLELWFSAPIKTNLSAGEKANLGLKAVSRNDWDDMLAQAQCKVLSVVNSEEIDAYLLSESSMFVFAHKIILKTCGTTTLLASLPRLLEIASSVGFDRPLRIFYSRKNFLYPERQLAPHTSWEEEVRYLQLFFPSGCSYVVGPTNKNHWHLFSDLADDYSLLEDSLDPEDETLEVLMTDMSPERSLQFYAPSLDVVRSARGDDYVREKNNLSGGHILGSYVADESGVRDLCSTSDKKAVLDAFQFEPIGFSSNMIYKDRYATIHVTPQEHCSYASFETNVSQFQFGRSISETIEKTVKTFGANKFCLTLFQAKGASQEKHFSAKLKSFSSYKREEFIVYDFPGYDLIFASFTAV Q9P7F3 AMT3_SCHPO SPAC2E1P3.02c; CHAIN 1..517; /note="Ammonium transporter 3"; /id="PRO_0000278389" MLNEPNALLRRDANSTIATVTELFPNEYSNADIAYVLLSTVVVFTVTPGIALYYAGMVRKNSALSILTQSFLVTAVVFIQWYLFGYSLACSSGSSFYGTLWQGGMNHLWLEPYIPGSTIPAIVYFPFGGLFAVATAQLFAGAMAERGRLIPSLVISFLYITLVYCPQAYWTWAPNGWLYTLGALDFAGGGPVHISSGFAALAYSLCLGRRIVVDEPDRPDSIRSTDNADLPSSSQNNCKANWKRWFGFKSVSWKNSFGRGKIAHNPPHDAGMVYIGVVLIWFAWLCFNSGTLLTVNIRTAYIMTNTLISSSFGALTWAIIDYIRYRKFSTIGICEGAIAGLVGITPACGFVFPWGAAAGGIVPALVCNFLHDLNEWIGVDETLRVFNLHGIGGIVGSIVLGVVAHPDVAASDGATVIDGGWAVHHWKQMGYQFAGFTSVAAWSFVITAIICLLVDLVPGLHIRASFEEELRGMDFVELEEQLPGQTLESKPMIIYAQEMDEPVTQGSNIKQEKQDEF Q9P7F7 SNF7_SCHPO SPAC1142.07c; CHAIN 1..222; /note="Vacuolar-sorting protein snf7"; /id="PRO_0000211444" MSGFLRWFGGNRSKDTTKDTIVRFQEMLALYDKKEEVLERQIAEQTEIARKNATTNKRLALTALKRKKMHENELVKIEGSRNNIEQQLFSIQNANLNFETLQAMRQGAEAMKSIQRGMDADKVDQIMDKIRDQQTISEEISTMISTPVGLNAEIDEDELANELDELQQMELDSKMLGAEKPPVHTPAVPAVPSQVKDLPSISKPQELDEEEELRKLQAEFSL Q9P7F9 CTR5_SCHPO SPAC1142.05; CHAIN 1..173; /note="Copper transport protein ctr5"; /id="PRO_0000195049" MSLSKMSMSGMSGMGMGSSSNSSAATCRMSMLWNWYIHDSCFLAKSWHINTGNKFAGSIIGIFFFAVAIEGLSLVQRMFDRWIVAHSNGKTLSGPLRIFFPSSTVHVTVWQQLIRAAMYSSFYLSATILMLIVMSFNGYAILFGFVGAWIGFFLFASDTYGTPSTGTGCCESR Q9P7G9 KAPS_SCHPO ACT_SITE 103; /note="Phosphoserine intermediate"; /evidence="ECO:0000250" BINDING 32..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25; SPAC1782.11; CHAIN 1..202; /note="Adenylyl-sulfate kinase"; /id="PRO_0000105933" MATNITFHPGSVTKEERIKFVGHPGMTIWMTGLSASGKSTIACALEQYLLQRGVTTYRLDGDNVRFGLNSDLGFSEQDRNENIRRIGHVAKLFADACVVAVTSFISPYRKDRDQAREFHKKDGLPFIEVYVECPVEVAEQRDPKGLYKRARAGEIKEFTGISAPYEAPISPEIVVSSHTQSIEECVEKIVNYLLEKDLITLK Q9P7H0 NHP2_SCHPO MOD_RES 119; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1782.10c; CHAIN 1..154; /note="H/ACA ribonucleoprotein complex subunit nhp2"; /id="PRO_0000136775" MAKDKKDHKHSGSTEDEYDSYLPALMPIAKPLAPKKLNKKMMKTVKKASKQKHILRGVKEVVKAVRKGEKGLVILAGDISPMDVISHIPVLCEDNNVPYLYTVSKELLGEASNTKRPTSCVMIVPGGKKKDMSKVEEYKESYEEIIKEVPALEV Q9P7J2 XLF1_SCHPO SPCC24B10.14c; CHAIN 1..203; /note="Xrcc4-like factor 1"; /id="PRO_0000116816" MSWVQLRGHRFHFIQASFDAESNEAVQVIHITDLVRVWSCTCSRNQIVNQAESERCPIDPFQTFETLVDVLAEVLVNVSSESRIQLRGSNDEGSLKIFCTSKIAKDIFLEWNWTLWLTPPETIAKMVWFPLINHHLFESETDTSPGSLMSIIRDQKSLLNDKTWFKEALNERSSSSNPSTPRKRSAFADIISPKRPRTRYDFV Q9P7J4 THOC7_SCHPO SPCC24B10.11c; CHAIN 1..202; /note="THO complex subunit tho7"; /id="PRO_0000361067" MEETAIRSRLTVEERPLKRLISRCLGFAAQNVDEANLRDLEIEFSALSAFWLRLQMQLDMNAKEVDVYEGELKKTQTFCEAEKTEISQLEQDLLVAQEELRKREQYDELAKPIMSKGLRSRTEQQESIGKLQDAIRELEEENANYVKAWNLRKDIFDETLKQMNHLQSILHPPSNPESDSEEGIASEGENPSSSSSTQYKAK Q9P7K5 GIT1_SCHPO SPBC21C3.20c; CHAIN 1..1098; /note="Adenylate cyclase activation protein git1"; /id="PRO_0000256253" MGFTSVEPPDFFDWTARAIFLLSTLRSRRNAKQIERENALLDQIKELLSIAIIQCHERNIPSIDLPPSFFNYVCEQLPRHPFAKIASSYIDTHTLFFQISISSFLCRFSNCSEDEIRLFKQHQSLDSFLLSLFDLLCSHHFSVEFTSISLIIKSSQWLFYTLSDYAHESLTGVEADITTKFLSTLADTWPEFEEQCTLSKHLFLLGDFSLISYVKVLCGVFNIPNYNAFILSVEDLLPENISFAAVADFQLSKYRAINDNSVLRSDDFSSKAVFDKYVERECYYSENAISKIFQNYPDLAVLFEELQYAEGNNDLLSAILNTNKYTLRPDDCAPYFYRLMDLCLRYCYSQSNEIGTNVLWSMTTSFINIWRIHPGTCCCVVLSIYWPYLEDKLLKFSDLGDIFEYFFSLIHDCDYAIWSVHDEHQFSELLAFYHRRALNDLVEELGSCPRSSDSCRAILDILNNYIFSCPLFLVTPEELEEQYTDFFKKLKEKYGEFFQNLLKKELTGKPESDLEGLRLVGVQLQATYENLKSNFSARIFNQLSVHSFFAEATCHLFLEKLPTITKTYVYSNCKEIPDHILEMINALYQQTRALVACTGYLSSDYPKIYEAFSGTFVYRNLSLIIDKGLANVLQTVLRESFIPKRSRFYSDSTKMILAPLQDCYDFLQKIDWPSSKDANRFYLHLGKLSENYIHYYVDSMYALFIYSTDIPLKAEPLVPDLPVKQLKEKASHFKRHSGDPNFLKLYRESFTLINTVSLVSGWLKMLHQRIDYKILTEKVMHFKDMEVPSATVIISIKMAHLLVTPKAPYSFSVLLQDPESEFCVHTRDVYDELVPNWKETYQMEITNVKRFKLIIYQRNIHTGLETVYGHATLEVDPDKLKQGHGKDVWLDITNKGQILIGLRVLLKRETPNYYCFAQMEYLTVTEVKMLNVLMISLSKFIRNSLRNSGLMDFVRYLDGDENDNAEAETKEKMDELQARCEKEQQSLLAELDDFFYWIYVNLLPKPLFYLLSRLWFGLLETFRDILVPPVTDSTLRRIPLNKRELKMVYSWLQLFYDFFRNFQDIAPFDFLNTDEYKSVMAIKDYYFVKSKDVKRVSS Q9P7L5 OAT_SCHPO CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 275; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPBC21C3.08c; CHAIN 1..438; /note="Ornithine aminotransferase car2"; /id="PRO_0000120498" MSAESLLHNTFSTEQIEVLENEYAAHNYHPLPVCFSKAKGAKVWDPEGREYLDFLSAYSAVNQGHCHPKIIEALVEQAQRVTLSSRAFYNDKFGPFAKYITEYFGYEMVIPMNTGAEAVETACKLARLWGYKAKKIPTDEAIILSCVDNFHGRTMGIISMSTDPDARDNYGPYLPNVGPKISGADRVLRYNNIEDLKYYLDTFGPKVAAFLVEPIQGEAGVMVPDDGYLEEAYKLCKAHNVLFIADEVQTGVARTGKMLCIEHSNVKPDVVILGKAISGGVYPVSAVLSSREIMLNFEPGTHGSTYGGNPLGAAVSIAALEVVKEEKLTERAAVLGEKFRTALIECKSPIVQKVRGRGLLNAVVIDESKTNGRTAWDLCLIMRSRGVLAKPTHGNIIRFSPPLVITEEDLMKGIEVIKKSLNDLPTIDMTPYAEKPIH Q9P7L8 SAP62_SCHPO SPBC21C3.05; CHAIN 1..217; /note="Pre-mRNA-splicing factor sap62"; /id="PRO_0000353820" MDYQNRAGVRFGGGGVAGYQETNAARRERLRKLALETIDLSKDPYLMKNHLGTFECRLCLTTHANENSYLTHTQGKKHQTNLARRQALENKKSQENAPQVLLGISQSHVQVKKSVVKIGRPGYKVSKIREAESGKFGLRFQIKYPDIEVNAKPRYRIMSAYEQRVEAPDRKFQYLVVAAEPYESIAFKIDRAPGKFWSYWDAPTYTIQFFYNLTKIS Q9P7M1 DEP1_SCHPO MOD_RES 204; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC21C3.02c; CHAIN 1..491; /note="Transcriptional regulatory protein dep1"; /id="PRO_0000116878" MTENLQSESIPHEILPKEPFDLPMNNLKSSPKNKDSEKRINNSIAESEQVVDSALSNPETNANEDIIAPQLPSQNSEIIEKNSPVNKLNSSTSLTTHQLASLPKLEVTDHDNVSEAETVVLNEDEEKETSLVGSVSVTEDLGDSSAIGRTILVNNSVEPQMENTANITIVSPSLKESDFESEEKATNDNNGLIETNHNSKLEESSEHEEEEDEESNIERTEDSDHQIPQRGGTLEAPRKGGPRSGVGSRKRKRATVSRKWSTNSESKIKRVALETSQEESDREIADRRSASEQAHEADDEKAIKRKEAFDALLNIETEFTFLRNRLYGKKLLKLNEHEEMIQNETHERFNACIDLITERRDDRVRLATENLMKQLGNIKNVMDYVTKQRKYQLLFDKRRIRQALLTKIATKCFQLLNKQKSVHDPTYITQKTMSYRQSALLQKQRIEYEAAVLCELNSFAGFPTAPIIETASFDDIRNDLLEMGCLSENQD Q9P7N1 BUD32_SCHPO ACT_SITE 148; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028" BINDING 26..34; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 48; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53323}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53323}; SPAP27G11.07c; CHAIN 1..238; /note="EKC/KEOPS complex subunit SPAP27G11.07c"; /id="PRO_0000278917" MSEKPDLRQRCSDIYREIKEKKLTVVKQGAEAITIKTEFYPGEVCLLKCRPAKRWRHPILDQKLSRKRCLVEARLLAKCHYVGIKCPMLYFIDANRGQIYMEWIDGPCVRDYIREICECEIEKKLIPLMKRIGSEVAKMHKNDIVHGDLTTSNMMLESHNNPVPIFIDFGLGSVSESEEDKAVDIYVLERALSSTLPESESLFHHVLDSYAQSWKQSKATLRRFEEVRMRGRKRTMIG Q9P7N5 CD123_SCHPO BINDING 96; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN"; BINDING 99; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN"; BINDING 101; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 103; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 164; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 165; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 166; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN"; BINDING 167; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 174; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 176; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN"; BINDING 190; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 227; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGP"; BINDING 239; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN, ECO:0007744|PDB:4ZGP"; BINDING 239; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000305|PubMed:26211610"; BINDING 241; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0007744|PDB:4ZGN"; BINDING 241; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000305|PubMed:26211610" SPAP27G11.03; STRAND 29..34; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 45..47; /evidence="ECO:0007829|PDB:4ZGN"; STRAND 93..96; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 109..114; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 116..118; /evidence="ECO:0007829|PDB:4ZGN"; STRAND 161..165; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 174..180; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 183..193; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 222..231; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 234..244; /evidence="ECO:0007829|PDB:4ZGP"; STRAND 268..270; /evidence="ECO:0007829|PDB:4ZGP" HELIX 7..12; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 15..21; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 23..25; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 37..43; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 76..88; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 103..108; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 119..127; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 130..138; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 171..173; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 197..200; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 202..214; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 254..259; /evidence="ECO:0007829|PDB:4ZGP"; HELIX 299..308; /evidence="ECO:0007829|PDB:4ZGN" TURN 139..142; /evidence="ECO:0007829|PDB:4ZGP"; TURN 215..218; /evidence="ECO:0007829|PDB:4ZGP"; TURN 309..314; /evidence="ECO:0007829|PDB:4ZGN" CHAIN 1..319; /note="Translation initiation factor eIF2 assembly protein"; /id="PRO_0000350948" MTLILTKNQVLHCQFSSWYSLFRKLTPKAKVIKPIPATVLKYLHEDSIYVEQPMNTVEEVDSEEDEESAPAYYPEREAIQLIEKAIKELGGAVVPKLNWSTPKDALWITTTGSLKCTTAEEVLLLLKSSDFVAHDLNHAFDDCKDFDNADGSVPKDFSFELVLKEWFPMHASTEFRCFVKSKRLIAFCQRDDNYYEFLKENIDCYEKLISDLLKKLDTFPDPDFVFDVYIHKDRAWLIDINPFYPRTDGLLFSWSELESMNSENMKPEIRLIPKGSMPSTGSAKYYTNRVPFDMIAASEGENLLEFAQKWQDLTNKSNE Q9P7P1 RPA14_SCHPO PTM: Phosphorylated. {ECO:0000269|PubMed:15647272}. SPBC1718.03; CHAIN 1..147; /note="DNA-directed RNA polymerase I subunit rpa14"; /id="PRO_0000073961" MATECPPKMILRKSEKLDKDASSKFLNRYIQTIERFQDEKSGSESVLSQLNRVLMYLKGEEIPLISLNLPVQGPPTEELIIPPEEMLETKEEESLKHAREENDDLHLDKETKKRLKKEKKKAARREKEEARKAKADTTQGVGEKEQS Q9P7Q7 MAK1_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; MOD_RES 1003; /note="Phosphohistidine; by autocatalysis"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"; MOD_RES 1559; /note="4-aspartylphosphate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00169" SPAC1834.08; CHAIN 1..1639; /note="Peroxide stress-activated histidine kinase mak1"; /id="PRO_0000081408" MRPPDDQINNNVGSNSHLEKLKEAMDHQLQKSSKIVGSFTNSQNSSVGSVHSPILESPTSLNRQHRNSFSFNNVSSPSLEDERLINFPRVNPNRLMTSKRPNELFKTSSMSSDCYSPQKSRESLNSLCHSPAPSVSSCGNALNNDNTSASHSLTDEQPFETDSSANLFKQLQEKRNRTIGNVYEMACLLVFKTGLMNFWKNIIDFFAQQFFSTQISVVEPRDLSDIYNTPWQLRCYYDGGSHYDPYSNPISVNDNLASSSYVTVVASDGSKGIIYKDPASLKHEGDLLIDSKVVQTVLERATLLVYTRKQQHIVKNTKVHDNDYFSSIPNVDDIRSIKNSWKVFHDEKLNELKKQVEISASAAQLNGLYPQKKRAFVSHFSQNRKPYSQSDISKAQSSSFSEEPSNIYDEYEQNLLSPWSRSPVASPSIQTDPNRNPFFQNCLQESSFATESSTEKSASESVSETAVNDDCKGMNFSGNRRQEDHLNDFTSFPTETAVSIVHVPLMFPCSDQTSSRGRAPIAILSFKSNLVPYPENLIASIERLIPFIFSSYSNSQSVPLLPCPTQRHLLFNTSSTDNTKELSMSASSENSDCPHKEGECVGSFCNINAKGSSLNNIPKLPRFVPVPSEFFKKNQRSWVTLKKHRLLARLKSRISKKNSKVNENLRFSLNDGENYSNETITLKKDEIVLDKSKSYACCTSESHKYVQGHCGGQAPPFPLLKVIIDSIPVHVFTADPGSGKLTWVNRKTLLYCGLNMNEQIELQFSRIHPDDLPNFLNDWKSSLFSGSGFYHEIRLQRFDNVYRYFICRAVPLRDCTGSVLHFFGTMTDVHDQKLAERELQKQSAIAANENSYRSLAEASPQIVFAANGKNGIIYANAQWLSYSGLSLESSLGLGFLSAVYHADRKKCLLPESLEGTFNNQDESNGTKTFAAEIRFRSTDGHYRWHLVKSVCVNNSADTSTNLWLGTCTDIHDHKMLEEKLQESNIEAQRIVRSKMQYLSNMSHEIRTPLIGITGMVSFLLETQMSAEQLSYARIIQQSAKSLLTVINDILDLSKVRAGMMKLTSQRFSVRAMMEDANETLGTLAFSKGIELNYTVDIDVPDIVFGDNMRMRQVALNVIGNAIKFTNVGEVFTRCSVEKIDYSTNTVVLKWECIDTGQGFNRDDQLQMFKPFSQVESSTLPRHGGSGLGLVISKELVELHNGSMSCQSRRGVGTRFMWTATFTMDKTPLKFEPPDGCCPVCFCPYEKSKQSTEDYYCADDGNDKSATNFVKLAVNKADPGRESNRRKLESDKNVQSNKYVNPFASESEFCRCGASADPYTVLFWRLYRNKPSGIKLDKSALAVVVSHTKYSSEAIGNMLQSIIDISSFKDIVRYGNTYEAFEELLENPMQSKVTHIILNLPDIEAYVLFVKSLQLCSLYKDTKFILVTSTRQKESLSKIFSDSEDCNSESIHYVLKLVKPSKFFPLFYSDSEEKGKIGALNDMTRKAAMEQKADAETLRYNLAKSGFSVLLAEDNIINIKVISRYLERIGVKFKVTMDGLQCVEEWKREKPNFYSLILMDLQMPVMDGYQACNEIRKYELENDYPKVPIVALSANALPHVVLSCKDSGFDSYLAKPITLQHLSLIISGILNYTNQSKLHK Q9P7Q8 PMO25_SCHPO SPAC1834.06c; CHAIN 1..329; /note="Mo25-like protein"; /id="PRO_0000209837" MSFLFNKRPKSTQDVVRCLCDNLPKLEINNDKKKSFEEVSKCLQNLRVSLCGTAEVEPDADLVSDLSFQIYQSNLPFLLVRYLPKLEFESKKDTGLIFSALLRRHVASRYPTVDYMLAHPQIFPVLVSYYRYQEVAFTAGSILRECSRHEALNEVLLNSRDFWTFFSLIQASSFDMASDAFSTFKSILLNHKSQVAEFISYHFDEFFKQYTVLLKSENYVTKRQSLKLLGEILLNRANRSVMTRYISSAENLKLMMILLRDKSKNIQFEAFHVFKLFVANPEKSEEVIEILRRNKSKLISYLSAFHTDRKNDEQFNDERAFVIKQIERL Q9P7Q9 ALG9_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a di-trans,poly-cis-dolichyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + H(+); Xref=Rhea:RHEA:29531, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, Rhea:RHEA-COMP:19517, Rhea:RHEA-COMP:19518, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517; EC=2.4.1.259; CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a di-trans,poly-cis-dolichyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + H(+); Xref=Rhea:RHEA:29539, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, Rhea:RHEA-COMP:19519, Rhea:RHEA-COMP:19520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519, ChEBI:CHEBI:132520; EC=2.4.1.261; SIGNAL 1..29; /evidence="ECO:0000255" SPAC1834.05; CHAIN 30..577; /note="Alpha-1,2-mannosyltransferase alg9"; /id="PRO_0000012142" MPSKAPRKSLSVSFVWTFSILAVLRLTSASFRVIDDCDEVYNYWEPLHYLLYGYGLQTWEYSPEYAIRSWFYIALHAVPGFLARGLGLSRLHVFYFIRGVLACFSAFCETNLILAVARNFNRAVALHLTSVLFVNSGMWSASTSFLPSSFAMNMVTLALSAQLSPPSTKRTVKVVSFITIGAVIGWPFSAALSIPFILLELVDLKGRFRHLFCRWFKAIFVALLITGICITVDSLFYHRIQFVAWNIVKYNVLAKDGRGPDIYGTEPWWYYFANLSLQHNIVLWFAMACGPLVLLAAFTNWINLDSFLDLSSVISPFYIWLFIFIIQPHKEERFMYPIYPVLCLAAAIGLDMSLKLMIQILSSINETVRSKFPVRFVVLCVYAIIGCLSIARILAIQNYNAPMIIYPAISFLETDNNVTTNVCVGKEWYRYPSTFFLPDNSRLKFVKSEFDGILPGEFVESNSTWWNREGYYQIPEHMNEFNNEEPTRYTSLESCDFLIDLEFDHSKATVNEPIYSKSDGWIPVMVYPFIDTKQTPFMGRAFAVPFIEPKWGRYEILVKKPVKIDFSNLRRASKQQA Q9P7R3 MTR3_SCHPO SPBC211.08c; CHAIN 1..257; /note="Exosome complex component mtr3"; /id="PRO_0000317211" MSDRKRVYGPSVSVPPYFEEPEQPVFTRTRDVDRCRKIYLKLGWATKAVGSSYFESEKIKIACTVSGPRPSKTFAFRSSAKLNCEFRLSPFSTSVRQGHVQTVEEKSYSQMIEAAISPSILLHLYPKSSIDVYIQVIESDGALATLAAAISCASSAIADANIDCIDLVTGSSVLFNPNTDEYWIDPDYVDERARAAKGSVVMGYMASLGHVTQVWERGTCSPSRLSFLTEKCIKNAKDTRLVINHALLLEKSKSEDP Q9P7R4 UBC8_SCHPO ACT_SITE 85; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPBC211.07c; CHAIN 1..184; /note="Ubiquitin-conjugating enzyme E2 8"; /id="PRO_0000310743" MSSPRRRIETDVMKLLMSDYEVTLVNDNMQEFYVRFHGPSETPYSGGIWKVHVELPSEYPWKSPSIGFVNRIFHPNIDELSGSVCLDVINQTWSPMFDMINIFEVFLPQLLRYPNASDPLNGEAAALLLREPNTYYAKVRDYIARYANKEDADITLNDSSDDDTMSSIDTESGDEIAGPMDSDF Q9P7R5 GFH1_SCHPO SPBC211.06; CHAIN 1..577; /note="Gamma-tubulin complex component gfh1"; /id="PRO_0000362147" MLHEIILLLAGNTSGLFIEKNGQILLHPSVQPLHPGERELINDIVSLASKRKRIERYIEIFDEDLIQQNQFLLKALRLLLSKKLFLYDESLANLERMIISSDPYFVGSGKFVSLAQLEAHLADWKETLSSLLVLQGNISQCLSVASTFQKLHNMYMGSTHLNFKKLVLECECAFQKTWLDELVQYLVNDSGDDSFKCSFLCGDTKDFVSCSNNVPFLTQDIVNCLVSIRTCMLNAKKCFTDAFCEILRCFYRLVYEMPLPLTKSSVTKLADEMFTLVSEKIIFQLASFHQIFDLVKMLEMVMLLENVEFLPTLSEMFRDVRGEYCSSNDVQGVVIDDILPVVLRKTISLLDLATEYGECVSFLKLVSIFDEEDEMIRSENRKIDVEGLNMQLLLCLKWPFNLFMDKNALNVYSDLWILLGSLHLSITKIKSLFYERKEYTAKGISQPWTQLWVTLWFLSSLQYYAYECVIKPSYCKLRESLTELYRTQKLRMQDCSQLHALTLTYAKKMLFFYDDDLHISLNSIYHELSLFRSQEVSKVDCQLAAHVSHSIECIRQKENDPSYDREIINALIVQLNL Q9P7R9 SYF1_SCHPO SPBC211.02c; CHAIN 1..790; /note="Pre-mRNA-splicing factor cwf3"; /id="PRO_0000205734" MGDVIPLKVNFDLINVDDEPFELELLRDPYSLKSWLRYIKTHEGSTLEKRVLLFERACSELPGSYKIWKSYLELRVAHVEHLNPYFHAEAFASVNDCFERSLILLHKMPVIWKLYLQFLMKQPNVTKIRCTFNSALRALPVTQHDDIWDMFTKYAEDIGGLFCIHVYRRYIQVEPRAIENYIEILCKLGLWNEAARQYEDILNRPVFLSAKRKSNYQIWLEFSELVVQHPDHTQNIDVEKVFRAGIKRFSDQAGKLWTYLAQYYIRIGDYEKARSTFYEGMNNIMTVRNFTIIFDAFVEFEEQWLSARVEASSGNANDELSIDFHMAWLEKILDKRPLYINDVLLRQNINNVDEWLRRVKFLEDDSEKVVQVYTDAIKNVNPKLAHGSLGKLFSEFARFYENFDDLEQSRIIFEKATHVPYKTVNELAQVWIDWAEMELRHQNFDAARKLIGDAVHAPRKSHISFFDESLSPQVRLHKSSKIWMYYLDLEESVGTIETTRKLYDRVFELKIATPQVVVNYANLLEENAYFEDSFKIYERGVALFSYPVAFELWNLYLTKFVKRYQGTHMERTRDLFEQALEGCPPEFSKSIYLLYADFEEKFGKAKRSISILEKAADKVKTADRLAIYNVLLVKVALNYGVLATRTVYEKAIESLSDSEVKDMCLRFAEMETKLGEIDRARLIYIHGSQYCDPRVETDYWKAWQEFEIRYGNPEETVKEMLRIKRSVQTKFSTDSLHIAKRAAKIESAAAPMDPMEQLEMEKSEGPKALAGFVLSKSNPQETSKITGEEN Q9P7S3 SSR3_SCHPO SPAC23G3.10c; CHAIN 1..425; /note="SWI/SNF and RSC complexes subunit ssr3"; /id="PRO_0000317337" MSNNSRLPENGVQSGNGEDAELKKSMRIIEREIPDSLLEKIPEAEDYIALQDLERKLDSLIVRKRFDLQDSLSRNSHKTRILRMYIHSTVANQSWQQKGENQENNSGDINSLPIPEWTLHIEGRLLVNPDDEDDKAFELAPFTNFFRKIAIQILRSDDLYPSGNYVEWNKLPDNSNTSNGITVTRKGDQSVDVKIMLYPEEHPERYKLSKAFANILGIREGTRPDIVSYLWQYIKFHRLQDMEEKRLINCDKALRDLFEADRLYFPRIPELMNRFLEPIDPIVIPYTINVSEHTVEKVTIFDIRINTEDPRHSQIRSFLATMMSQDKIRSIDDKLTELIQAITYSQSKYDFMKKFSESPIEFINEWIESQSRDLEIVLDGTNMNYAEKRSADYYQQPWVHESAFHYLNLLNSKKQQSVLNASAKK Q9P7S5 UBP7_SCHPO ACT_SITE 217; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 812; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" BINDING 56; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 58; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 83; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 86; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 101; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 104; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 109; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 116; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 120; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 127; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 140; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 143; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; MOD_RES 333; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 337; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 486; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 493; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 645; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23G3.08c; CHAIN 1..875; /note="Probable ubiquitin carboxyl-terminal hydrolase 7"; /id="PRO_0000080608" MPHSNTLIVPSTNPFDDPSSIKNGLNNLTSSELVNQMKKESLAASVKTPSTPPKECSHLKKGVKLSHLKGNARALRDPSKHLCFICTTEKIKREDYELTLCANCGYLFCCNHESDHSRKHFEKNKKHCVFVNIITLKCHCYSCDADIVIFDKKNLVVRDVQQFICSNLVSSLTKAPNVLKSNSSHFKKEKKSKHSSGKSSKKYKVISPGLKNLGATCFFNSTLQVLCACEALHDVISPFQYSHSSVIVRKLTKSPESSLLSAFIKFLETFYKSDGTISVYRPTTFFGEFRRLHPQFSESVQQDAHELLRLLLDDLISEEFRVLRFNLNSVSRSLQLSPCLTDDEQLSKSLTSFKQVNVTDASLSPNSHNTSDNEQNNEDYVSVSSLVGSETEDITYSKELSQSSDSSQHQHDSFLPANSSPLAASSTKSLPSSELLDSSSDKGQQVFKGQHEVAGTNSFEDPNSHFNVSNSSNHEEASPKKEVLKSPQFQRRSLDILRLGELSSDDMMLDKATMDEFSSSLVIKSIFTGRLTSVVMCQSCNEITNTPEPIQDLSIPIHYPSSRVSRRHRFHRALRSRFSRSPKKSSVKIVVDNANDDTDQAPTTNSSSLNENLLGGHASENDKSLKQSPFQKLTRRLSDLSVNSSGQISKQDFDNSNSIFSESSLSSPIIEEPKTLIDCLKNFTHVEELSGENMFACENCCNQPNEVGSPAKGGLTSDNDKYSFNNSVYRNAYKRMLLDDPLPPVFIIHLKRFFQEISHDGYANPKKISDFIEFEQELDLNEFVMPHLRASSSFRYRLFGVIVHSGTLNYGHYVAYVLSHKFLDLSAPSTNSKDFRSEAGIPERRWLYISDNIVRESSWDEVSKVEAYMLFYERV Q9P7S6 SNF30_SCHPO SPAC23G3.07c; CHAIN 1..274; /note="SWI/SNF chromatin-remodeling complex subunit snf30"; /id="PRO_0000349431" MSFVSKSPPIVNSASPTGQVNPMEVEKANKLLEINRLILWKCLELQHIKTAQNSTLEQRALSTELFNSYIQRLKANLAFVVSIASPRQMQVLTPPLSCPESLPQLEPLYKELRQYFQIAQTSTLSYPPSNGDSSSYANGTDLHGNTGTMQQEEKANPSLTRSDSVSSGSYITMQGANSLKAQQDLLNSFTGAPSNNSHNIPDPNLSQTFSATSMGPPNNNYSKFRTDNYLARSSNRSGTPNIQNEQSRFFDSQQAQVQARALMQRYQQGMEFNK Q9P7S9 IES4_SCHPO MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 90; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23G3.04; CHAIN 1..194; /note="INO80 complex subunit 4"; /id="PRO_0000372366" MSETLVLHLKVPTERFREVLSSLKEKQNFTASPSSQPKPQERPFQMKKPRAPYGMGPRAMKRREKAEKEKLGVVNDELAESSKPSSGAATPTRSAPKSSAGLINSGLRALDRSGKPCRRWEKKPISIRSISTIVWKLPLWIGTPDSIPNTPELPVKTTLDSVNEIAAALSTHAESSPMDATSPVDSMPESATGI Q9P7T0 SIDA_SCHPO BINDING 40..48; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 59; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 64; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 202..205; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 228; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 242..245; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 273..275; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 273; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 399..401; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:E9QYP0"; BINDING 402; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:E9QYP0" CATALYTIC ACTIVITY: Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78275; EC=1.14.13.196; Evidence={ECO:0000250|UniProtKB:E9QYP0}; CATALYTIC ACTIVITY: Reaction=L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+); Xref=Rhea:RHEA:41512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:46911, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78275; EC=1.14.13.196; Evidence={ECO:0000250|UniProtKB:E9QYP0}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:E9QYP0}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:E9QYP0}; SPAC23G3.03; CHAIN 1..431; /note="L-ornithine N(5)-monooxygenase"; /id="PRO_0000352807" MTEPLDLAIIGFGPASLSFLIALHDHSEEPLKNKKIRVFEKLPTFSWHEGMLIPGSNMQISFVKDLATPRDPTSYFTFLNYLHSHGQERLSGFLNMSTLEPSRYEYHDYLCWAASHFSKFVEYNANINKLHYDAATDLYIVGHGDTQWQAKNIIITTGCQPYIPPLYKSVDSPLIVHSSKFMSDHSQKLLRNSKHGILVVGCGQSAAEIWKHCHYSLDPKTPLAMCFRNLAPVPSDSSPFVNSLYFDSHNSHWWYNLPTEARLKGLSVGRTTNYSVVKESLLEEMFKECYLQKLRYGQEFHQIMGDTDIQSIKNEGDHLVVQLTSQMDKSKKPETRKIDVLYVATGYDHESFDVLMSSLFPNSQGAQISEEYCVLNAPSKQGKVYVAGITSNQHGIGETLLSWAAIRAGGLAKELFGPSKPTARVPASYLN Q9P7V3 TSN1_SCHPO SPAC30.03c; CHAIN 1..220; /note="Translin-1"; /id="PRO_0000278571" MNKSIFIQLQDQIDKEHSIREKLTAEVDLLDEKLRVLQLLLANCEQNLENQEEILEALEIIKSKTRGLAELASNFPYYKYNGVWDRSIQKVVYLYLLASWTGRLDKSLRPTYSLLSLSEVGQILQVPVFPEESTFHLSIEQYLHAVLSLCSELARQSVNSVISGNYHIPFEALNTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHKLV Q9P7W3 ACL1_SCHPO ACT_SITE 280; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250" BINDING 221..241; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 238; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 272..298; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 299..309; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8; MOD_RES 359; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1703.07; CHAIN 1..615; /note="Probable ATP-citrate synthase subunit 1"; /id="PRO_0000102786" MAGSVDKPSYELFSKDTRAFVYGMQTKAVQGMLDFDYMCGRTVPSVAAIIYTFGSQSISKLYWGTKEILLPVYRTIEEACTKHPEVDVVVNFASSRSAYASTMELMEFPQIRCIAIIAEGVPERRAREILVTSKEKNVVIIGPATVGGIKPGCFKIGNTGGMMDNIVASKLYRPGSVAYVSKSGGMSNELNNIISHTTDGVYEGIAIGGDRYPGTTFIDHLIRFEADPACKLMVLLGEVGGVEEYRVIEAVKNGTIKKPIVAWAIGTCSSMFKTEVQFGHAGSFANSELETAVAKNQAMREAGIYVPETFEKLPALLQEVYEGLVKKGVIVPQPEVAPPNIPLDYAWAKELGLVRKPSSFICTISNDRGSELTYNNVPISKVFEEELGIGGVISLLWLRRRLPSYATKFLEMVLQLTADHGPCVSGAMNTIITTRAGKDLISSLVAGLLTIGTRFGGALDGAAQEFSKAYDAGLSPRAFVDSCRKANKLIPGIGHRIKSRNNPDLRVELVKGYVKKNFPSTKLLDYALAVENVTTSKKDNLILNVDGCIAVCFVDLLRNCGAFTLEEANEYINLGILNGMFVLGRSIGLIGHHLDQKRLRAPLYRHPWDDFLYLS Q9P7W4 POF10_SCHPO SPBC1703.06; CHAIN 1..662; /note="F-box/WD repeat-containing protein pof10"; /id="PRO_0000051137" MKSEPTSLDFTSSNLRRMNRDHSSNNTNRTVLNLPKEILIIIFSFLDPRSLLSAQCTCKYWKKLLSDDLSWRTAFFHHFAGDQSQIFSPLGNGTWRQEYLLRSTITRAYEKGKGQTVQYDCRVGQLTNLYYDFSSGRLYSGNWLTGTISVSDPTTGKVERSLLHASTDGSFTHGLSTMTLGKQIFGFGFMDGRVGVILMSRQAETPRKFRYCLDSHADSVTCIDALTGDLPPTGEIGMVTGSDDGSVHCWDVKTGVSLQSFQFRSSQILSLCFRPKYKMLLVDTFNYELNSYQLYLIPGYARSRKNEQPILLSSRKCVLTDEEEPPCLMTADCCAGVAFLSRGAPKNCICRVSFKEFLEKNDNVGVQTSSIPLNGKPTSISLDTNDRVLSKSTPGRGARLLAVGDENGLVYVVNTRTEDPNKAILRTITAYSNFPITDIYLNEVAMVVGSASGYCGVYDTVTGNFLKKIASARNAARREPINCILLDSNPLSLKGVITMSKHVKSWSYTIPKPFVNKRSKVLPLRPSVTHDNLSKSSDYSKNEVEREIMLGLDQIAQERREKMEARQKFEQHFGEGLVGLSEEEIIAYVTMLSQEEEAKRMVQLSMDVDKIEEDFKENDEQATSSLNALSSNHEPPQEQANVAELNEQEQIELAMRLSLMEM Q9P7W5 RIO2_SCHPO ACT_SITE 228; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 123; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; SPBC1703.05; CHAIN 1..344; /note="Serine/threonine-protein kinase rio2"; /id="PRO_0000373995" MVNLNIKAMRYLSAEDFRTLTAVEMGSRNHEVVPTNMINQIAKIRGGSCTKSLSVLFMHKLIAKVPHISYEGYRLTYAGYDYLALKALSKRASVYSVGNQIGVGKESDVYVVGDQKGKQYILKIHRLGRISFRSVKNNRDYLRNRKTGSWQYLSRLAATKEFAFMKILHEHGFPVPAPIDHSRHCIIMEMIDAFPLRAVTDIRDPPALYQTLMDIIVRFARNGLIHGDFNEFNIIVREDGTAVVIDFPQMVSTSHPDAQFYFDRDVQCIVQYFEKNYQYKGDVPNFEDISKMEKENNLDIMIEASGFNKKQSKELEKYRQEEEKRKENGDDLSDNYEEEEEEKE Q9P7W8 RSC9_SCHPO MOD_RES 230; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 696; /note="Phosphoserine"; /evidence="ECO:0000250" SPBC1703.02; CHAIN 1..780; /note="Chromatin structure-remodeling complex subunit rsc9"; /id="PRO_0000318104" MSQVIQGAVEEPVYSNKSLTNENDSFLSLIESFSQERGVPIDINPKIGRKPILLYELYKKVIKRGGYDAVSATEDGWTNIAEEFNQSDPARSAGILQNVYFKYLISWEIHDHWHLLLPPPSTLELSENRQNVLERVKVFNSCSPPKPTNPITIIDNDKTHSFKKFYKSLVKEDEENGIEKKINEAMNSSASQPLPNSTNFASTTFPSVPFHPLPVDSGLQKYIDRNSNLTPPALGAGVPGPPLLVRVALALKSQQDKEVDWAIGHLIKISFERHQEFKLERLPSLAECLVYSLGFQVTKAKQVSDLTDISLCMDRAIGIALVLRNSVLSVENAKHVAQTKLVISVLEASIRCAKTFNNLEFLHYCLDISEMISSYLHVEDEKNVFYLALCEFLNSSDYSILIATLRTLARLALNDRNNRLLQDLKSNVIANIIALVETDNEEIVAAALDFLYQYTTYRTNTSNLLASQEAWMLVDQLIRLMMYQAQERFMTVTIENSESNPAVKHEATSSISLPMEELQQLVAMREPERSVKWMRCCFEPSSDDYVLQTDIWQLYCSDMERAQGPNVMGISPADFIKVSSHAFYNARAMTVSTPQLPVEYVINGIKRRKFPTSVNGMRYQPCRWCLDSGKECGELLLGTPLLHSHLQEMHIFPQILETGKCRWSDCKYEIQRLTPASELSHYQLLSHIVTHLHDDSLETLVEGRKLSPSREFRIPLLLTAVDDQGDATGIALTATLVLRNLVRSKQGKMLFSAIESRVLEVSSLNPAVAPYVSEMLLGQI Q9P7X0 DHSD_SCHPO BINDING 99; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_note="ligand shared with large subunit"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250"; BINDING 111; /ligand="a ubiquinone"; /ligand_id="ChEBI:CHEBI:16389"; /ligand_note="ligand shared with IP"; /evidence="ECO:0000250" TRANSIT 1..30; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP23A10.16; CHAIN 31..159; /note="Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial"; /id="PRO_0000006495" MLQTRLGLGALRQGRLLFAVKSFSTTSVAKIFPPPPQTIKGTVNDAAVFPHHSKLHGSYHWDFERIIAIAMVPQVMIPLFTGTSHPLMDAALACTLITHAHLGFESCVIDYFPARRFKKLSPLMHWILRGCTVLTLIGVYEFNTNDIGLTEGIKKLWKS Q9P7X2 ELL1_SCHPO SPBP23A10.14c; CHAIN 1..533; /note="RNA polymerase II elongation factor ell1"; /id="PRO_0000307924" MIRNSSISDALPVALGGNEEESPLLMLVQLPKEFLEGYLSGTITDVSLECSDVGTSILANDRSYKCTSVPETAPHEIYRLVDSNSLQLVGRVSQKLQLRRELDSLTAERVKNRTQEAQKEKEEKRIVTLQNDGGSKNTTARKQKQLKKNGLRPLNTSASRIGLSSSPTNTPSPNLPVSQPSASPHYSGDKNSAKGIDLRTRVIQLLAIAPETEDFLRLRTKASLSKLQALLPEVAWKNNMNQWELLNPVYKDVRVFDWRPYSIADRNAVLSRMSNAFDNMQLPPDAPERSLLVSKQKNITKLNNEKRIPPQLAQPTSHVPSFIDTNSPSMPSISSVSSYQQQHRIPKLNASNYSPLLSPSSHRKTSGNLSRTGSESSAVSLSDTTNLNTPISDIPSPGSSTTCSNLSSPHIKRKSRSPPQSLPSTPFPTSSSSTNGTLEPNANSPKKNEQDAWIAKKRRQQRYTTEEMRALAKRFRETYPRYKNLYLKVSSYYDNNDTNNPNLNKLQDELISLHSQLKSWKNTLYDASSELAL Q9P7X7 ARP4_SCHPO SPBP23A10.08; CHAIN 1..433; /note="Actin-related protein 4"; /id="PRO_0000089100" MTSAFYGGDEVSAIVIDPGSKWTRIGFSGEDIPKCVLPSYCGEFSDGRRLFGEEYIYKSNPGMEIKNAIRNGWVENWDVTVDLWRYGLEQQLKTNPLEHPILITEPFDNPPENRVKTLETMFESLRCPATYLAKQETCAAFASGKGTACLVDIGAERSSVSAIYDGFVLQKGYQVQHFSGNAINDILAQTLRDKNFEVMPKYLVKSKNPVEIGQPANCELRPRDTTDSYHQFQVQRVYDEWKEECALISDVPFSSETTIAESEFEFPDGSRMMFGAERYQIPEHLFVPGSDEEMNEEPSKPIEQTENNEVSQQDSSVTNTSSRILGIPQLFQNCISECDVDIRASLLNNVIVCGGTSLMQGFSLRLQNELSKLYPGSRLKIHASGHVVERSYASWLGGSILSSLGTFHQLWISRQEYEEHGSDRLALIEKRCK Q9P7Y0 SSR4_SCHPO SPBP23A10.05; STRAND 22..27; /evidence="ECO:0007829|PDB:7K7W"; STRAND 56..59; /evidence="ECO:0007829|PDB:7K7W"; STRAND 69..73; /evidence="ECO:0007829|PDB:7K7W"; STRAND 86..89; /evidence="ECO:0007829|PDB:7K7W"; STRAND 92..98; /evidence="ECO:0007829|PDB:7K7W"; STRAND 101..112; /evidence="ECO:0007829|PDB:7K7W"; STRAND 122..133; /evidence="ECO:0007829|PDB:7K7W"; STRAND 137..144; /evidence="ECO:0007829|PDB:7K7W"; STRAND 158..160; /evidence="ECO:0007829|PDB:7K7V" HELIX 4..11; /evidence="ECO:0007829|PDB:7K7W"; HELIX 15..17; /evidence="ECO:0007829|PDB:7K7W"; HELIX 37..50; /evidence="ECO:0007829|PDB:7K7W"; HELIX 51..53; /evidence="ECO:0007829|PDB:7K7W"; HELIX 155..157; /evidence="ECO:0007829|PDB:7K7W" TURN 18..20; /evidence="ECO:0007829|PDB:7K7W"; TURN 114..116; /evidence="ECO:0007829|PDB:7K7W"; TURN 147..149; /evidence="ECO:0007829|PDB:7K7W" CHAIN 1..395; /note="SWI/SNF and RSC complexes subunit ssr4"; /id="PRO_0000349433" MAATMAAQSLLSIPVEYRSQVWCRANLPYPPAPQLPIPAVVDILTKASQALPQISFSWTLIDQPPDGSLFLVWQAPTLPSPPDGMHFMSNERFFNMDVAGKVLEIHEAKHGFYPLSETRTMHVRCRYRLLGVGFDNFWLVHYFQGSETDSIPANISVAKPPHLRRYPLPDVKTSPFLLQEPKKHIPEGTALSQRETLPNMGSAQMKSQSRTPSFSNVTTSPVPPINSNATAQTAEGHMGATNMTVDNMNKPSIPPNGNTSILMQEDLEIEKGDVMDKLSPQQICTARFIKHAEWMSQVLLTLQSVKDIEPPALWQEPNSMEELGKELKDNKEQLVKQDQKYQSLQGDLSYTDSMSNLLKEFSNIKSAEECDVLQKKIEEFAEAKIVPLSHVTERS Q9P7Y4 MED14_SCHPO SPBC1A4.10c; STRAND 11..15; /evidence="ECO:0007829|PDB:5N9J"; STRAND 181..184; /evidence="ECO:0007829|PDB:5N9J"; STRAND 186..193; /evidence="ECO:0007829|PDB:5N9J"; STRAND 197..199; /evidence="ECO:0007829|PDB:5N9J"; STRAND 201..205; /evidence="ECO:0007829|PDB:5N9J"; STRAND 227..230; /evidence="ECO:0007829|PDB:5N9J"; STRAND 294..299; /evidence="ECO:0007829|PDB:5N9J"; STRAND 304..309; /evidence="ECO:0007829|PDB:5N9J"; STRAND 327..334; /evidence="ECO:0007829|PDB:5N9J"; STRAND 356..364; /evidence="ECO:0007829|PDB:5N9J"; STRAND 367..371; /evidence="ECO:0007829|PDB:5N9J"; STRAND 408..411; /evidence="ECO:0007829|PDB:5N9J"; STRAND 414..419; /evidence="ECO:0007829|PDB:5N9J"; STRAND 422..428; /evidence="ECO:0007829|PDB:5N9J"; STRAND 435..445; /evidence="ECO:0007829|PDB:5N9J"; STRAND 490..492; /evidence="ECO:0007829|PDB:5N9J"; STRAND 500..504; /evidence="ECO:0007829|PDB:5N9J"; STRAND 515..521; /evidence="ECO:0007829|PDB:5N9J"; STRAND 526..532; /evidence="ECO:0007829|PDB:5N9J"; STRAND 534..536; /evidence="ECO:0007829|PDB:5N9J"; STRAND 538..544; /evidence="ECO:0007829|PDB:5N9J" HELIX 16..37; /evidence="ECO:0007829|PDB:5N9J"; HELIX 43..70; /evidence="ECO:0007829|PDB:5N9J"; HELIX 71..73; /evidence="ECO:0007829|PDB:5N9J"; HELIX 74..111; /evidence="ECO:0007829|PDB:5N9J"; HELIX 118..125; /evidence="ECO:0007829|PDB:5N9J"; HELIX 130..135; /evidence="ECO:0007829|PDB:5N9J"; HELIX 137..142; /evidence="ECO:0007829|PDB:5N9J"; HELIX 151..171; /evidence="ECO:0007829|PDB:5N9J"; HELIX 177..179; /evidence="ECO:0007829|PDB:5N9J"; HELIX 212..218; /evidence="ECO:0007829|PDB:5N9J"; HELIX 235..254; /evidence="ECO:0007829|PDB:5N9J"; HELIX 258..287; /evidence="ECO:0007829|PDB:5N9J"; HELIX 291..293; /evidence="ECO:0007829|PDB:5N9J"; HELIX 339..344; /evidence="ECO:0007829|PDB:5N9J"; HELIX 379..401; /evidence="ECO:0007829|PDB:5N9J"; HELIX 448..458; /evidence="ECO:0007829|PDB:5N9J"; HELIX 464..485; /evidence="ECO:0007829|PDB:5N9J"; HELIX 506..508; /evidence="ECO:0007829|PDB:5N9J"; HELIX 511..513; /evidence="ECO:0007829|PDB:5N9J"; HELIX 553..575; /evidence="ECO:0007829|PDB:5N9J" TURN 38..40; /evidence="ECO:0007829|PDB:5N9J"; TURN 219..221; /evidence="ECO:0007829|PDB:5N9J"; TURN 300..303; /evidence="ECO:0007829|PDB:5N9J"; TURN 430..432; /evidence="ECO:0007829|PDB:5N9J"; TURN 486..488; /evidence="ECO:0007829|PDB:5N9J"; TURN 522..525; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..879; /note="Mediator of RNA polymerase II transcription subunit 14"; /id="PRO_0000096361" MEPPAIPHITEGFYPLPEIVETFSHHVLQELVSLAEVLPSMSNVEKKKKILDWLLRSRAFTMRLLVLARWVHLSPSVHRCIDVVAFLQGQKFCFQNLVHVLQDIRYQLSFARLRNSDLVTALDILSTGTSLRLANAPTSKLYMLSESPLSTKQILQTLHALNMLIRIRLSLYEIIPTPFQHFTIANGRCTFTVPNEFSVSLTTNSQDPKSTGISFQWIVVDFQFHLPDFSSTPAKYRVFIELHLNEEIAAAFVLQKPILPLIYNILHKFCLYQRLNLLSQQTFQLSRESWLGHLRGVYDEKPPRLRLYYWPQLNVKKEGKPGKIGHYIHIFVNTQPISAFERTLSSKRSSCEYDHFLLLVEWHHDGIVEHVPLDDHMDAQHLLLLITQKHAQLILEQIRKELHPNIFSEHVGGGLKIHVFDNEIIVKVNSVTGRLVLSSSASPLSPPRHLRAAEKNIALNTQPPAQILNRLYFFCIQTQLLEVAQCAELHAVQGYYSFPYLTFSKGKWRKDGDSLWVLAYNVESNSWSVRLLNAAGQTLYTQDVHTTKGTLSIESFSRLSYLLEVQILLFNVQTACQARGMPFEYLPIPPKALIEDDFTTYVQTGCLCIMMPSSNEDMLPVVFVRAHDGQLIFDSRIKGKLPYQSETETEKNCYIDWRTGRITIRVQNFSSFEKTWIGLLKLVALSKTSAFNVDCITLKHVDFTYLDDEKFRATIHDDNTFTLHFFNRHSPFHLISQFLQDTFSDGPSAIQPLRVIMDRTRGVLVAQELGYVVLARSLRQYRIILSKNHGIQVLLNRHGCILQDLSYLSADSRYLEGTQTLTSQWEPCSWLNTVWEGDLGDDELNGQIEAAPEMHLIKMNKTADLTAILKRILAISRKK Q9P804 TRM1_SCHPO CATALYTIC ACTIVITY: Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216; Evidence={ECO:0000255|PROSITE-ProRule:PRU00958}; SPBC25D12.05; CHAIN 1..548; /note="tRNA (guanine(26)-N(2))-dimethyltransferase"; /id="PRO_0000147677" MYEANMLRLSQRISNAVNHFSTAMMSGASASLTEGSAIIPFSNPNEVFYNPVQQFNRDLSVTAIRAWSETRSKKIVAKSHHRHQLLDQNSELSQENLTKCDTTHDFEKNCSEKTDSTSADNIAGFTILEALSATGLRSIRYAKELPNVKRILANDLLENAVKTIEKNVNYNNVSDIVIPNKGDANAVMHMNKFHYDVIDLDPYGSAAPFLDAAVQSVSKDGLLCITCTDSAVLAGNAYPEKCFSNYGGSSLRSNFCHEQAVRHLLYAIAASAAKYGRAIKPLLSLSIDFYFRVFVQIKAKPVLVKNLQSQSLLIYHCSGCGSFAEQPLGKTSPGRLPGTTKFSNASGPPVSANCEHCGYVHHVGGPLWGGPLHDAEFLKKMRAIAEDLDPEVYGTKRRILGMLALADEELPDVPFYFVLSQICSVLRSQSPPQNIFVSALLNAGYRVSGSHAKSNAIKTNAPWSFVWDVLRSWIKDHPVKLENISKTSAGAAILEKTPTAEVDFTFRPDSEFASKKEGYTRYQMNPTENWGPKSKPGKRTIAEVDSKS Q9UQW9 DCOR_SCHPO ACT_SITE 377; /note="Proton donor; shared with dimeric partner"; /evidence="ECO:0000250|UniProtKB:P11926" BINDING 229; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P11926"; BINDING 266; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P11926"; BINDING 296..299; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P11926"; BINDING 341..342; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P07805"; BINDING 378; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P07805"; BINDING 407; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P11926" CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P08432}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P08432}; MOD_RES 98; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P11926" SPAC144.04c; CHAIN 1..432; /note="Ornithine decarboxylase"; /id="PRO_0000149908" MPAIMEKNMLVSESLRTTELLGHVKPIDSVVTWSSPGSSRQAIGEAFKNTIEEIERAAVRGEPADSDAFFVADLNGVYRQLLRWHAKLPRVQPFYAVKCNPDPKVLALLNKFGTGFDCASKGELEQILGLGVSPDRIVYANPCKAITYVRYAASKGINLMTFDNADELYKVKQHHPNSRLLLRISTDDSNSLCRLSLKFGASLDDTGKLLDIAKSLELNVVGVSFHVGSGSYDPSAFLDAIQRSRQVFDQGLERGFNFDLLDIGGGFMNDSFDGVADLIRSALDTYFDPSIRVISEPGRFFVSSSFTLAVNVIAKRKLDDEEKVMYYVNDGVYGSLNCILFDHQHPVARVLKCGSRFVYNDLVGTGQHRCFIWGPTCDSLDVIANDAHLPYELNVGDWIYFEDAGAYTVAAASCFNGFKTSRIVYLDTDILD Q9UR05 DYL1_SCHPO SPAC926.07c; CHAIN 1..85; /note="Dynein light chain 1, cytoplasmic"; /id="PRO_0000195148" MAVIKAVDMSEKMQQEAIHAAVQAMEKFTIEKDIAAFIKREFDKKFSPTWHCIVGRNFGSFVTHESRHFIYFYLGTVAFLLFKSG Q9UR24 RHP26_SCHPO BINDING 302..309; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPCP25A2.02c; CHAIN 1..973; /note="DNA repair protein rhp26"; /id="PRO_0000372387" MSVNEDLSHLGVFSVDQENLERDVTNTASEYIAHESREIEKKRLQKVRKEISSVKEKIRRLDERIDSRLTKISVKENFRKQLSKFRDTLQSLQSDENDIKRRLNNEDSANAPGIGAFSTEELERQELIRTGKVTPFRNLSGLQKEVDFDDESSIREAVIKSEGTYYETAPHLSSEPSNIDHGIIPRDEKDEYVTVDAVTEKVVTAAIDDGDDLVYRQRLNAWCANRKELRDQASASENNKDRGEFEGKDEWLLPHPSKKGQTFEGGFTIPGDIRPHLFRYQVTCVQWLWELYCQEAGGIIGDEMGLGKTIQIVSFLSSLHHSGKFQKPALIVCPATLMKQWVNEFHTWWAPLRVVVLHATGSGQRASREKRQYESDASESEAEESKTSIKLRGASSSFHRYAKNLVESVFTRGHILITTYAGLRIYGDLILPREWGYCVLDEGHKIRNPDSEISISCKQIRTVNRIILSGTPIQNNLTELWNLFDFVFPGRLGTLPVFQNQFALPINIGGYANASNVQVQTAYKCACMLRDLISPYLLRRMKLDVAADLPKKSEQVLFCKLTPLQRKAYQDFLQGSDMQKILNGKRQMLYGIDILRKICNHPDLVTREYLLHKEDYNYGDPEKSGKLKVIRALLTLWKKQGHRTLLFSQTRQMLDILEIGLKDLPDVHYCRMDGSTSIALRQDLVDNFNKNEYFDVFLLTTRVGGLGVNLTGADRVILFDPDWNPSTDAQARERAWRLGQKKDVVVYRLMTAGTIEEKIYHRQIFKQFLTNKILKDPKQRRFFKMTDLHDLFTLGDNKTEGTETGSMFLGSERVLRKDNSSRNGNEAEDIPARDRKKHKIHDKGKKVNSSKVFEKMGIASMEKYKPPQESNVTKTNSDSTLGDDSVLDDIFASAGIQSTLKHDDIMEASQTESILVEKEATRVANEALRAVSSFRRPPRQLIPPQQSTNVPGTSKPSGPITSSTLLARLKQRR Q9URT8 RL34B_SCHPO MOD_RES 76; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1322.15; CHAIN 1..111; /note="Large ribosomal subunit protein eL34B"; /id="PRO_0000131844" MAQRVTYRRRLAYNTRSNKTRIIKTPGNNIRYLHIKKLGTIPRCGDTGVPLQGIPALRPREFARLSHNQKKVQRAYGGCLSANAVKDRIVRAFLIEEQKIVKQKLKQMSQK Q9URT9 GSK31_SCHPO ACT_SITE 150; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 31..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 54; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 184; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 185; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC8D2.01; CHAIN 1..381; /note="Protein kinase gsk31"; /id="PRO_0000085977" MSDDSHLETKVVTDGTTGEKKTISYEPCRVLGSGSFGVVIQAKLVGTPGFIAVKRVLQDKRYKNRELQIMRAISHPNIIKLIAFFHTHNPSKDETHLCLLLEYMPETVFDDMRWYTRRRKSIPNLSIKLYAFQLFRALAYLHSTGVCHRDIKPQNLLVDYKTGILKLCDFGSAKVLVPSEPNVSYICSRYYRAPELVFGATHYTTKIDVWSAACVIAELFIGRPLFPGDSSVEQLVEIIRVLGTPSYHEISVMNPNYVNHSLPNVRPHTLESVMPHNCTKNAMDLLHKMLTYVPSKRISAIEVLTHPFFDELRDPNCMYHCSRDEGTIERHLPPLFNFNLAELSIRPNLNKAILPPHVYESLDVDINNFEPIVVKQADADS Q9URU6 EXG1_SCHPO ACT_SITE 213; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 312; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; SIGNAL 1..22; /evidence="ECO:0000255" SPBC1105.05; CHAIN 23..407; /note="Glucan 1,3-beta-glucosidase 1"; /id="PRO_0000007887" DISULFID 295..406; /evidence="ECO:0000250" MLSFTSVFSFFLHALLLKTAFSYVIKRNNPVFDYTSEKVRGVNIGGWLVLENWITPQLFTQFSSMSNPPTDEWGFCEVLGADEAASQLAAHYSSFYTESDFATIASWGVNVLRIPIGYWAFNVVDGEPYVQGQEYWLDQALTWAEQYGLKVWIDLHGVPGSQNGFENSGKTGSIGWQQNDTVTRTLDIITYVANKYTQSQYASVVIGIETVNEPLGYGLDMDQLKQYDLDAYNIVNPLSSSVATIIHDAYVDLSIWDYGVVSPSSYNLVMDVHRYQLYESDECSKTLDDHLSDVCSIGDSIASSPYITVTGEWSGTLADCTIFEEGVDSSTFIGPNSGDISTWTDEYKGAVRLFIETQLDQFERGAGWIYWTAKTGGPSPTWDMGLLIEYGVFPQPFTDRQYSSYCG Q9URV9 SRX1_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-[peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-L-cysteinyl-[peroxiredoxin]; Xref=Rhea:RHEA:17545, Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA-COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974, ChEBI:CHEBI:456216; EC=1.8.98.2; Evidence={ECO:0000305|PubMed:15824112}; SPBC106.02c; CHAIN 1..124; /note="Sulfiredoxin"; /id="PRO_0000211434" DISULFID 83; /note="Interchain"; /evidence="ECO:0000250" MTSIHTGSNNNIVELDMSELIRPIPPVLDMNKVNSMMETMTGKTPPASCGLTSEDLEAGELPPVDVLTFKKSGKPYYFAFGGCHRLRAHDEAGRKKVRCKLVNCSPNTLRLYLGASANKFLDSD Q9URX7 ANM1_SCHPO ACT_SITE 128; /evidence="ECO:0000250|UniProtKB:Q63009"; ACT_SITE 137; /evidence="ECO:0000250|UniProtKB:Q63009" BINDING 29; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q63009"; BINDING 38; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q63009"; BINDING 62; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q63009"; BINDING 84; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q63009"; BINDING 113; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q63009" MOD_RES 19; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 176; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC890.07c; CHAIN 1..340; /note="Protein arginine N-methyltransferase 1"; /id="PRO_0000212337" MPGNTKKSADSGLTAKDYYFDSYSHWGIHEEMLKDDVRTLSYRDAIMQNPHLFRDKIVLDVGCGTGILSMFCARAGAKHVYGVDMSEIIHKAVQIVEVNKLSDRITLIQGKMEEIQLPVEKVDIIVSEWMGYFLLYESMLDTVLVARDRYLAPDGLLFPDRAQIQLAAIEDADYKSEKIGFWDDVYGFDFSPIKKDVWKEPLVDTVDRIAVNTNSCVILDLDLKTVKKEDLAFSSPFEITATRNDFVHAFLAWFDIEFSACHKPIKFSTGPFSRYTHWKQTVFYTHKDLTVKAGEYIRGTITCKPAEGNHRELDIDISYTFNPREPNREPVSEDLSYRMC Q9URY0 YTM1_SCHPO MOD_RES 140; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC890.04c; STRAND 96..102; /evidence="ECO:0007829|PDB:8ETG"; STRAND 107..112; /evidence="ECO:0007829|PDB:8ETG"; STRAND 117..121; /evidence="ECO:0007829|PDB:8ETG"; STRAND 126..129; /evidence="ECO:0007829|PDB:8ETG"; STRAND 131..133; /evidence="ECO:0007829|PDB:8ETG"; STRAND 135..138; /evidence="ECO:0007829|PDB:8ETG"; STRAND 146..153; /evidence="ECO:0007829|PDB:8ETG"; STRAND 156..162; /evidence="ECO:0007829|PDB:8ETG"; STRAND 165..171; /evidence="ECO:0007829|PDB:8ETG"; STRAND 188..194; /evidence="ECO:0007829|PDB:8ETG"; STRAND 207..215; /evidence="ECO:0007829|PDB:8ETG"; STRAND 219..229; /evidence="ECO:0007829|PDB:8ETG"; STRAND 262..266; /evidence="ECO:0007829|PDB:8ETG"; STRAND 272..277; /evidence="ECO:0007829|PDB:8ETG"; STRAND 283..288; /evidence="ECO:0007829|PDB:8ETG"; STRAND 291..297; /evidence="ECO:0007829|PDB:8ETG"; STRAND 302..308; /evidence="ECO:0007829|PDB:8ETG"; STRAND 313..319; /evidence="ECO:0007829|PDB:8ETG"; STRAND 324..329; /evidence="ECO:0007829|PDB:8ETG"; STRAND 332..337; /evidence="ECO:0007829|PDB:8ETG"; STRAND 348..352; /evidence="ECO:0007829|PDB:8ETG"; STRAND 358..363; /evidence="ECO:0007829|PDB:8ETG"; STRAND 370..375; /evidence="ECO:0007829|PDB:8ETG"; STRAND 378..386; /evidence="ECO:0007829|PDB:8ETG"; STRAND 392..396; /evidence="ECO:0007829|PDB:8ETG"; STRAND 408..414; /evidence="ECO:0007829|PDB:8ETG"; STRAND 418..423; /evidence="ECO:0007829|PDB:8ETG"; STRAND 427..432; /evidence="ECO:0007829|PDB:8ETG" TURN 298..300; /evidence="ECO:0007829|PDB:8ETG"; TURN 320..323; /evidence="ECO:0007829|PDB:8ETG"; TURN 415..417; /evidence="ECO:0007829|PDB:8ETG" CHAIN 1..440; /note="Ribosome biogenesis protein ytm1"; /id="PRO_0000051465" MDAQSAPSGQVQVRFTTRNEDLAVGDTPIFVPTSLKRYGLSQIVNHLLKTEKPTPFDFLVQGQLLKTTLDEYIVQNGLSTESILDIEYIQSTLPPAYLASFSHDDWISGIQLTSDTILTSSYDGIARVWDKSGEIKFQSTGCGSSLKSASWHIPNQSFLTASLDQKIFHWVIEEPESMLDAEKKSSGILQTLFVGHKDIVERVRSLESSSVFISASADNTVGIWDFERSPETTLESFSSSISKKRRRKNAEFTPQAGARSPLILCEGHTGPVMDIVFSDDPSVAYSVGQDHTIKTWDLITGQNVDSKITKAPLLCVEKLTDLHLVICGSSARHIVVHDPRAGSDKIVSHTLSGHKNLVSGLSASPENPYMFASVSHDNTCRVWDVRATSGSIYTISRAEKTGSQWDKLFAVDWNKSIGIVTGGTDKQLQINQSSSFGKSE Q9URZ0 AGAL_SCHPO ACT_SITE 154; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 214; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; SIGNAL 1..24; /evidence="ECO:0000255" SPAC869.07c; CHAIN 25..436; /note="Alpha-galactosidase mel1"; /id="PRO_0000001006" CARBOHYD 84; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 180; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 45..77; /evidence="ECO:0000250"; DISULFID 126..156; /evidence="ECO:0000250" MISISFLNCFFLVFLFLFFSDVHGSYNGLGLKPQMGWNSWNKYACDIDESIILNNAKAIKEEGLLDLGYEYIVMDDCWSKHERNATTGRLEANPDKFPNGIGSMAKKLHDMGFKFGMYSSAGKYTCAGFPGSLNHEQIDADTFADWGVDYLKYDNCFNEGKSGVPLISYERYKRMSDALNKTGRPIFYSLCQWGEDFVWNWGNTIANSWRISGDIFDTFSRKDVRCPCETIECFALQGDHCSVMNIISKASFLSSKAGMNSGWNDLDSLEVGNGGMSFEEYKTHFTMWAILKSPLILGNDVSSMSPMDKLIVSNKELISINQDIGTNPAALIWKKKYGDEYIELFSGRLSNNDWVVAVLNAASEPLKMGIHLSDIFVDALGNAEHDWLATDLWNNNVKLVSDRIRANVASHGVQVWRFQQYKVKNTNDKFFSFNKH Q9URZ1 PIMT_SCHPO ACT_SITE 60; /evidence="ECO:0000250|UniProtKB:Q27869" BINDING 57..60; /ligand="S-adenosyl-L-homocysteine"; /ligand_id="ChEBI:CHEBI:57856"; /evidence="ECO:0000250|UniProtKB:P22061"; BINDING 65; /ligand="S-adenosyl-L-homocysteine"; /ligand_id="ChEBI:CHEBI:57856"; /evidence="ECO:0000250|UniProtKB:P22061"; BINDING 89; /ligand="S-adenosyl-L-homocysteine"; /ligand_id="ChEBI:CHEBI:57856"; /evidence="ECO:0000250|UniProtKB:P22061"; BINDING 110..111; /ligand="S-adenosyl-L-homocysteine"; /ligand_id="ChEBI:CHEBI:57856"; /evidence="ECO:0000250|UniProtKB:P22061"; BINDING 148..149; /ligand="S-adenosyl-L-homocysteine"; /ligand_id="ChEBI:CHEBI:57856"; /evidence="ECO:0000250|UniProtKB:P22061"; BINDING 221; /ligand="S-adenosyl-L-homocysteine"; /ligand_id="ChEBI:CHEBI:57856"; /evidence="ECO:0000250|UniProtKB:P22061" CATALYTIC ACTIVITY: Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596, ChEBI:CHEBI:90598; EC=2.1.1.77; Evidence={ECO:0000250|UniProtKB:P23506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706; Evidence={ECO:0000250|UniProtKB:P23506}; SPAC869.08; CHAIN 1..230; /note="Probable protein-L-isoaspartate O-methyltransferase"; /id="PRO_0000316247" MFWSFNLSSNAALVQHLVESKFLTNQRAIKAMNATSRSFYCPLSPYMDSPQSIGYGVTISAPHMHATALQELEPVLQPGCSALDIGSGSGYLVAAMARMVAPNGTVKGIEHIPQLVETSKKNLLKDINHDEVLMEMYKEKRLQINVGDGRMGTSEDEKFDAIHVGASASELPQKLVDQLKSPGKILIPIGTYSQNIYLIEKNEQGKISKRTLFPVRYVPLTDSPDDSSDY Q9URZ5 VPS1_SCHPO BINDING 34..41; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 153..157; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 222..225; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" SPAC767.01c; CHAIN 1..678; /note="Vacuolar protein sorting-associated protein 1"; /id="PRO_0000206587" MDPSLIKVVNQLQEAFSTVGVQNLIDLPQITVVRSQSSGKSSVLENIVGRDFLPRGTGIVTRRPLVLQLINRPSASGKNEETTTDSDGKDQNNSSEWGEFLHLPGQKFFEFEKIREEIVRETEEKTGKNVGISSVPIYLRIYSPHVLTLTLVDLPGLTKVPVGDQPRDIEKQIREMVLKYISKNNAIILAVNAANTDLANSDGLKLAREVDPEGLRTIGVLTKVDLMDKGTDVVDILAGRVIPLRLGYVPVINRGQKDIEGKKSIRIALEAERNFFETHPSYGSKAQYCGTPFLARKLNMILMHHIRNTLPEIKVRINAALAKYQAELHSLGDTPVGDNSSIVLNLITDFCNEYRTVVDGRSEELSATELSGGARIAFVFHEIFSNGIQAIDPFDEVKDSDIRTILYNSSGPSPSLFMGTAAFEVIVKQQIKRLEDPSLKCVSLIYDELVRILNQLLQRPIFKRYPLLKDEFYKVVIGFFRKCMQPTNTLVMDMVAMEGSYINTVHPDFLSGHQAMAIVQSQNSKPIPVDPKTGKALTNNPVPPVETSSSSGQNFFGSFFGSKNKKRLAAMEPPPPVLRASTTLSDREKTDTEVIKLLIMSYFNIVKRTLADMVPKSISLKMIKYSKEHIQHELLEQLYKSQAFDKLLQESEVTVQRRKECEQMVESLLQASEIVSNV Q9US09 BTN1_SCHPO SPAC607.09c; CHAIN 1..396; /note="Protein btn1"; /id="PRO_0000065006" MIKLRLTKDAKVGCCFLIFGLLNNLLYVIILSAALDLVGANVSKGVVLLSNIVPSLACKLSASILHVHKFKFAKRIGFCVFMSILGMQWIAWSSSVPSKMLGVSLAAISSSFGEISFLHLSSRYHSVSLPCWSSGTGLAGLFGASSYLVMTTWFNFSVRSTLIISSFLPLFLLIMYFFVLPESESTSPSINNNYTPIESIDLRAGHVSFNFVNSLKQTFIFMQPYLLSHMFPQFLVYFSEYTINIGVAPTLLFPPEKAGFSSFRDFYPTYQTVYQIGVFLSRSSISFFTVPYLRTLAITQFIILLFTILQSALYLTSSYHFVLFLIFVEGLIGGTVYVNVYHSLQTTESSQRELAISTVGSSDSSGIFLASLVSLFLEPSLCHFQADRGRDWCALT Q9US14 IPMK_SCHPO BINDING 27; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07250"; BINDING 86..88; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07250"; BINDING 99; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07250"; BINDING 127..135; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 235; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07250" CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+); Xref=Rhea:RHEA:32359, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.151; Evidence={ECO:0000305|PubMed:9794810}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:17717, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57627, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:9794810}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17718; Evidence={ECO:0000305|PubMed:9794810}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11020, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.127; Evidence={ECO:0000305|PubMed:9794810}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021; Evidence={ECO:0000305|PubMed:9794810}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11856, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57627, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:9794810}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11857; Evidence={ECO:0000305|PubMed:9794810}; SPAC607.04; CHAIN 1..268; /note="Inositol polyphosphate multikinase"; /id="PRO_0000318137" MKLKLFPFQAAGHGQVLVSEDDKILIKPCIKSEVDFYKTCNDNITLYNWIPKNFGEWMPSSRDIEGINPIAESVAFSLTGKAIILENILYQMETPCVMDIKLGKQLWADDAPLEKRKRLDAVSRSTTSGSLGFRITGILSWDRTNNTYIKRSTAWGKTLTDSDVVEGLNDFFVSCSLSQKARLVESFLNLLKLFEVDLSESYIELKSSSILFVYDYSSLNPTYHCESNVVLKLIDLAHSRWTKNTIDHNTLIGVKNLIHCFAMLLKNE Q9US22 RL15B_SCHPO MOD_RES 183; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1783.08c; CHAIN 2..201; /note="Large ribosomal subunit protein eL15B"; /id="PRO_0000127565" MGAYKYLEELAKKKQSDVNLFLSRVRAWEYRQMNVIHRASRPSRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGQTYGKPVHQGVNHLKYQRSARCTAEERVGRYCSNLRVLNSYWVNQDATYKFFEVILVDPSHKAIRRDPRINWIVNPVHKHRESRGLTSIGKKSRGIGKGHRYNNSPQHATWLRHNTLSLRRYR Q9US46 ITT1_SCHPO ACT_SITE 381; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" BINDING 174; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 177; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 192; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 194; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 197; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 200; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 219; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 224; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 266; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 286; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 289; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 294; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 297; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 302; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 308; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 368; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 371; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 386; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 388; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 393; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 396; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 408; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"; BINDING 416; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9UBS8}; SPAC1002.14; CHAIN 1..435; /note="E3 ubiquitin-protein ligase itt1"; /id="PRO_0000372422" MLEVEVESDNKHLVADELIALQSIYPEIHLDGNNYGRLNIPVNTESDYFLSFKSPDESTLTDTIVVRHFPDLVMEFFLPEAYPFNSPPTFFLKSSWLPLKQKRVLTSSLIKLWNEIHDCVLFDAIEHVRSIATIAFHLPTEMVFPGGFDDLKKEILAFDKNAKLLEFQIRKFQCNVCFDEFNGTDCFQLTRCGHVSCQSCLRDYYTMCIQEGMFSQIKCIDLDCGKDAPVLTLKELESIVGVQLTNRYKELEEKRRYENDSNIIFCPRSFCQGPSKRDPGQKLAICQKCDFAFCSFCQATWHGDLSPCKLEGDSKKLVEMYLNYQENEPEKALELEKRYGKRIIDRLVEQVKNDEEAEKWVLLNGQRCPTCDRVVERIDGCCHMNCLCGTHFCFLCGAYLMEQNPYKHFNDPVSSCYGMLFASAAEKQRFSENWT Q9US51 MTF1_SCHPO BINDING 38; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 91; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 117; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026" SPAC1002.08c; CHAIN 1..366; /note="Mitochondrial transcription factor 1"; /id="PRO_0000316606" MKLPKILYDAAAFGGPRSTGFVKILNLNGRSSYKSSYLVNQNLMDEALVKSNLLKEYNSEKMTILEMAPGPGVTTTSLFNYFQPKSHVVLESREVFSKPLQKLCTLSDGRIKWVHQDGYYWQTYEDVYVSKVLDPRIQTEEEQKLSPHRELLFFAHLPHGYAGLLFVSQILDFLSARDWLGIFGRVRVLLWLPCSPTVTLLGSRGFSKRSKTSVFREAFTDSRVLAASESTLQKLCMGYSKEAKENYQISPNPLLVSPTPITSEPHKEDLTLVEMCSKPQDKQLSIPVFESIVRILLTCKATSLSKSIYYLGPGAETLLPSFTQCGINIDMPVGLLSAADFLTISKIIQKYPFKHHLHLGTIIEDS Q9USH6 NAA40_SCHPO BINDING 64; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q86UY6"; BINDING 107..109; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q86UY6"; BINDING 118; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q86UY6"; BINDING 120..122; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000269|PubMed:25619998, ECO:0000312|PDB:4UA3"; BINDING 128..133; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000269|PubMed:25619998, ECO:0000312|PDB:4UA3"; BINDING 154; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q86UY6"; BINDING 159; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000269|PubMed:25619998, ECO:0000312|PDB:4UA3"; BINDING 176; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q86UY6" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H4]; Xref=Rhea:RHEA:50596, Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257; Evidence={ECO:0000250|UniProtKB:Q04751, ECO:0000250|UniProtKB:Q86UY6}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]; Xref=Rhea:RHEA:50600, Rhea:RHEA-COMP:12742, Rhea:RHEA-COMP:12744, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257; Evidence={ECO:0000250|UniProtKB:Q04751, ECO:0000250|UniProtKB:Q86UY6}; SPCC825.04c; STRAND 36..43; /evidence="ECO:0007829|PDB:4UA3"; STRAND 86..92; /evidence="ECO:0007829|PDB:4UA3"; STRAND 98..109; /evidence="ECO:0007829|PDB:4UA3"; STRAND 112..122; /evidence="ECO:0007829|PDB:4UA3"; STRAND 150..156; /evidence="ECO:0007829|PDB:4UA3"; STRAND 192..199; /evidence="ECO:0007829|PDB:4UA3" HELIX 28..32; /evidence="ECO:0007829|PDB:4UA3"; HELIX 46..66; /evidence="ECO:0007829|PDB:4UA3"; HELIX 73..80; /evidence="ECO:0007829|PDB:4UA3"; HELIX 124..126; /evidence="ECO:0007829|PDB:4UA3"; HELIX 131..145; /evidence="ECO:0007829|PDB:4UA3"; HELIX 160..168; /evidence="ECO:0007829|PDB:4UA3" TURN 33..35; /evidence="ECO:0007829|PDB:4UA3"; TURN 93..95; /evidence="ECO:0007829|PDB:4UA3" CHAIN 1..204; /note="N-alpha-acetyltransferase 40"; /id="PRO_0000310299" MHFLKQYLFYSPRRMKTQEIKNVTLEDVDFLKNLGVWVEIYHHLEKGLLQQCFNLVKKNMEALYRQSSFGWDDSEKLKEMEMEKLEYICIFEKTSKKLVGFLSFEDTVEAGLTCLYIYEIQLDEHIRGRNVGKWLLKNASILAYRRNLKYIFLTVFSANLNALNFYHHFDFVPHESSPQEKKFRSGKVIHPDYYILYTKSRKDW Q9USJ4 NTE1_SCHPO ACT_SITE 1044; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"; ACT_SITE 1163; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" BINDING 516..644; /ligand="a nucleoside 3',5'-cyclic phosphate"; /ligand_id="ChEBI:CHEBI:58464"; /ligand_label="1"; BINDING 640..763; /ligand="a nucleoside 3',5'-cyclic phosphate"; /ligand_id="ChEBI:CHEBI:58464"; /ligand_label="2" CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SPCC4B3.04c; CHAIN 1..1316; /note="Lysophospholipase NTE1"; /id="PRO_0000295330" MDITDRILQNRIVSKVIFFVLRSVTLSLVSVTRFSLFLLSFATITVPKWAYKIVTYSLTIQFNFKSLLFLFFVSICVVILVVRYRYLNKYARLPHEAPIKEAKLGPDTNIRPSEPRIGFQNYLDEFLSAISIFGYLEKPVFVELARHIRTQRVAEGNTIYLGEQSSFILVVDGCFQVFTAPEKDSAEVVEEAGQPEYRLLTEVSNGAPLSSFFTVLELFTELIPEATSKENPFKSTTSSLRPGSSTTTEAGANNASKPHMPQPKKARIIAKAKIDTTIAVIPANAFHHLVHKFPNSSAQIVQVILTRFQRVTFSTGYEYLGLSDAIFSIEKNFNSLTAYELPNYIRSDIIDDFKKEAMSEHLSQASNESFIVLRSKGAQSRLSNQYFSKAFDKEHGNFVSDIDRSTANAGDLLSSTNPHSTLLSTSVGPLRKFPLNRSYSREVGDYDISASFRDGLLQCIFKSLGVFNYELKEDNDDLCTENDSSEGDSDSLKKVDFLGQIAMMSATDREEVKSSIVVSTKKSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATCPSKLTFSTSYDTDLGMHSFMIKPGGIVNYQACVSNYRSFINVTARSDVLVGFLPRSCLERIIDQEPLISLTIAKRLISLVPSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLRSIEDERGSARTQVDYFNEYGKGDSVGELEMLLNNRRSSTLFAIRDSELAKIPETLFNALSLSHPAVGLQLSKIIANRMNLLLNNKSMDGMQHQPHEKHSIRTLAIVPSSSTGLLILFSQKLTSVLSVMGKSVKVLRQSSVLEHLGKHAFSRMGRFKLSSYLSDLEDKYDILIYVADSGVGSAWLQTCIRQADCIYILAEADQNPNIGEYEQHLIAMKSTARKELVLLHPERFCPSGLTRLWLKERPWVYAHHHVQLRIGLDNEISQNNEAKVFLNIIRAKVQNLHYGFRKYIDWKHLHPVYQANRAQDSDFARLARRICGKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMANLWRFVLDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMLSDSGDMLLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSREPMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRLTYVTSVATGEKVKSMPGCFYMRPPVKDFPTLEFGSFEKIYNVGYNYGKEYVEKLKTSHKLDDILSPRDTSKRHPKFLSSRRNSL Q9USJ7 ETT1_SCHPO SPCC4B3.07; STRAND 161..163; /evidence="ECO:0007829|PDB:3QTM" HELIX 14..32; /evidence="ECO:0007829|PDB:3MSV"; HELIX 62..81; /evidence="ECO:0007829|PDB:3QTM"; HELIX 85..105; /evidence="ECO:0007829|PDB:3QTM"; HELIX 109..111; /evidence="ECO:0007829|PDB:3QTM"; HELIX 114..129; /evidence="ECO:0007829|PDB:3QTM"; HELIX 131..134; /evidence="ECO:0007829|PDB:3QTM"; HELIX 135..137; /evidence="ECO:0007829|PDB:3QTM"; HELIX 144..157; /evidence="ECO:0007829|PDB:3QTM"; HELIX 158..160; /evidence="ECO:0007829|PDB:3QTM"; HELIX 166..189; /evidence="ECO:0007829|PDB:3QTM"; HELIX 198..217; /evidence="ECO:0007829|PDB:3QTM"; HELIX 235..244; /evidence="ECO:0007829|PDB:3QTM"; HELIX 246..248; /evidence="ECO:0007829|PDB:3QTM"; HELIX 251..267; /evidence="ECO:0007829|PDB:3QTM"; HELIX 276..301; /evidence="ECO:0007829|PDB:3QTM"; HELIX 309..332; /evidence="ECO:0007829|PDB:3QTM"; HELIX 336..338; /evidence="ECO:0007829|PDB:3QTM"; HELIX 339..352; /evidence="ECO:0007829|PDB:3QTM"; HELIX 356..375; /evidence="ECO:0007829|PDB:3QTM"; HELIX 382..390; /evidence="ECO:0007829|PDB:3QTM" TURN 191..195; /evidence="ECO:0007829|PDB:3QTM"; TURN 229..234; /evidence="ECO:0007829|PDB:3QTM" CHAIN 1..393; /note="Negative regulator of ofd1"; /id="PRO_0000116807" MIGRRPQGLRAAASLKKQQQLEKQKQEASYELSGNSSPSKENGSENVDNGEMEDETMLVYTEEDNISQLWGLYEMSREKLENDDIDASVSLVFGTIHEADRILRNTEDISTLPKDFHAAYSSALLAVSELFEIAQKRLKETNTEESYIDAAIERAQLGLDAPGNESRLFLALARAYLEKVRVLVWRHDNEESLANIPVTQLVNPYIEKAIQYLRPLAQDSTEYFDALTPDSLRPLYILSSYLFQFGDQFSEAFLLDVCSIITALWLKSVVDPNTPAYYKLIAQEAVLNNYTTFAEYYMDLLDNSESNVDDLINKASSWLNNSVDTWNVIYTLDKSPERLLKLADIKMDLAQIVQDEASQDNYLKEACNAIKEAQGSGVELSPDYVEFVEAYSA Q9USJ8 CTK3_SCHPO SPCC4B3.08; HELIX 3..14; /evidence="ECO:0007829|PDB:5CE7"; HELIX 21..23; /evidence="ECO:0007829|PDB:5CE7"; HELIX 25..33; /evidence="ECO:0007829|PDB:5CE7"; HELIX 35..37; /evidence="ECO:0007829|PDB:5CE7"; HELIX 38..51; /evidence="ECO:0007829|PDB:5CE7"; HELIX 54..73; /evidence="ECO:0007829|PDB:5CE7"; HELIX 80..86; /evidence="ECO:0007829|PDB:5CE7"; HELIX 88..95; /evidence="ECO:0007829|PDB:5CE7"; HELIX 100..118; /evidence="ECO:0007829|PDB:5CE7"; HELIX 124..139; /evidence="ECO:0007829|PDB:5CE7" CHAIN 1..218; /note="CTD kinase subunit gamma"; /id="PRO_0000338604" MDPFEGRMTFLQLLGKLNASQFSQIKPAQFAIKHLDLEEDLYSCIWEELESGSFNTRVNIMYFVDTLCEMCLKNGLTGGYLNMISRDICKLVQNVAPIGAAGAANAPEVRKVLQSLHEKKVIDDNQYKDAMATVEAHEQASKSGDTSTSGAISKNDILKRIEEDRERHKRMRENIWAISEPELEAEIAWNTTQGITESDLESLKDEYEKFNECLHATS Q9USK0 IPK1_SCHPO CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733, ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158; Evidence={ECO:0000269|PubMed:10960485}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.644 uM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate {ECO:0000269|PubMed:10960485}; KM=62.8 uM for ATP {ECO:0000269|PubMed:10960485}; Vmax=0.02 umol/min/mg enzyme with 1D-myo-inositol 1,3,4,5,6-pentakisphosphate as substrate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:10960485}; MOD_RES 372; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4B3.10c; CHAIN 1..640; /note="Inositol-pentakisphosphate 2-kinase"; /id="PRO_0000110526" MPLKNYTKTTSKKEPKQLDIAASDQQIEQWSDQIHKLDKAIRSTIDNSRLFYDAWRCMVCIAPSVTASWISLYRQLPPEKQPAASVGTLVDWNKALERQRREVLLALQNFHVIVIAPCKEVKGYVKKAVEMIKRRDKKVKELEKIQKELLVVYELPDPETKKSKIKALQSQLVRVNGELDDLQKHLTLSFPTLIAKSRVFFGQLMKHFYCLQLQMFRKMHNIVRPWDCFQDDIPQTWLVEFSSVCQAAESISLIAVNNNRPPVELPKSGDVLSNREWEAGKIDAMNSLIAQNLHTSASQVSLSPMASTASSSVTNSPVDTHTPSTPIMSRPPSMKALSSGVESQDESVASSNFQVPIISNPLFKSPAPYSPTSVISNHSSTGKSLVISEWAYLASGSANVVFEYVGKNPYFQDKVIRLRRRGQVFTTEQVYEYYQNVIYPLFAGMESFLIEVFLQPVTRDFLLAAQNASGIYLNLNEQYCLVMKDLKDGIEMKPKWLTQSPAAPPDWVVCRTCALSRMRGRPVGFCPLQLDFNNWPKFLCCLQGFVSPDIAMRLFQSGILRKLRDLQEQYSRTDVALAMTLRDVTLYIGKDHITLLDLDPKDMNTKMSKWERDERNLIEGGWYYGRGMKSTDKACRSSIK Q9USK2 SET9_SCHPO CATALYTIC ACTIVITY: Reaction=L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64456, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.372; Evidence={ECO:0000255|PROSITE-ProRule:PRU00900, ECO:0000269|PubMed:15550243}; SPCC4B3.12; CHAIN 1..441; /note="Histone-lysine N-methyltransferase set9"; /id="PRO_0000281807" MRQTNTHLETFSLFDDVCTCLLVDKVFYWSQIHKVRKLVDRSIERMESCSIINIITKYIIEQTDLDQAAKNILQFRELDPLLRRLSSTSLLAFTRHLKYYLSLYLPSCKFEICSTNQYFSSSKPEACVIARESINAGEDITDLCGTIIKLSPKEERNIGIGKDFSILHSSRLDSMCLFLGPARFVNHDCNANCRFNTSGKRIWLRCVRDIKPGEEITTFYSSNYFGLENCECLCVSCERMGINGFKKLFHTSATSTSCSSKSSSDVSDLSSLPQSNRYVISEEDRSFLNIWDSGGELSDASSSDLDEEFSLFIPRHKKRVWSREKRLLSEMAITNHSPLLNVDDYRKFREDLWKKRHGKRKVYQCSNCSQTFINEDIQNSSAFCPKCIRHSKLFSLPWPCRHKVNRELKLEKEKEINTKRNLVTSSHSMSLRHKKAVDYQS Q9USL4 NUP61_SCHPO MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 347; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC18B5.07c; CHAIN 1..549; /note="Nucleoporin nup61"; /id="PRO_0000204864" MSKRGADHQLTKDQDDSDDDRHGPVEVPKEASADVMATRKIAKPKSRKRPTSGVSSPGIFANLAAKPVSLPASTTQFTFGKPAVTANNDSDIHLKKRGLNKSFIDAVIKSVDNNPFGNLSPLFDEYRQHFSSIEKKPAEEQPTSNAVVSEVNPQQQKSQDSSSFVTEKPASSEKEDKEKPLVPPGAPRFGFSAPALGSSFQFNSSAFTPKGSFGEKSATEAEAKEKETSSNQTATGTAATTTNQFSFNTAANPFAFAKKENEESKPLTPVFSFSTTMASADASKETKQTHETKDSKSEESKPSNNEKSENAVEPAKGNTMSFSWTPDKPIKFDTPEKKFTFTNPLSSKKLPASSDVKPPSAAAVGFSFGTTTNPFSFAAPKSSFPTSSTPASVGAEKSEETSNGNKSEQEEKENGNDETRSNDSLVSGKGKGEENEDSVFETRAKIYRFDATSKSYSDIGIGPLKINVDRDTGSARILARVEGSGKLLLNVRLCQDFEYSLAGKKDVKVPAASTDGKSIEMYLIRVKEPSTAEKLLAELNEKKVSKSEN Q9USL6 YJK5_SCHPO BINDING 54; /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"; /ligand_id="ChEBI:CHEBI:16892"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+); Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:Q08975}; CATALYTIC ACTIVITY: Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP; Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7; Evidence={ECO:0000250|UniProtKB:Q08975}; SPCC18B5.05c; CHAIN 1..327; /note="Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c"; /id="PRO_0000343140" MEANQSHNAKTNHPTCLTIAGSDCSGAAGIQADLKVMTAHQVYGMSVLTALTCQNSHGITGIYPLHPSLIQRQIDACLSDIQCRVVKIGMLPDPKSIPVISQALTKYKITDVVMDSVIISSMGNVMCETPTIPATIQHLFPHLLVYASNVMEAFILVEKTLKKSPPPLKSFPDIQNLMSIIHRLGPKFVVLRGHHVAFDKNMMITEKPDSKSWTADLIYDGKEFYIFEKPYNTTKSIHGESCSLTAAIASNLACNIPPLQAIHEALYSIEWAIQRVHKKSSDPYKSAQLFTALGHSSKFSGSLISLKSENYIPQADLTSVLLSHIPS Q9USM1 RP13B_SCHPO SPCC16A11.16c; CHAIN 1..388; /note="Proteasomal ubiquitin receptor ADRM1 homolog rpn1302"; /id="PRO_0000351078" MESVFGRVRNETSERGKYGLVSVKAGKLQRKPGTNILQADHRKGVIYMQMASDELLHFYWKERARVSREVEDDYIIFPEEAEFIKIDECTTGRVYALKFKSSSQIHFYWMQEYSDEKDKETASLINQLIADPVNTTRTINSHNNSSSRGTDDSSTSQLLQLFGAASQDALQDFNWEVLSPTAEAPAILPRFPNVNESANMYRASSESNLNGPHATAGENGEDHEEATASPLDENIDYTHSRTLELLEQLQPLILNETTFVEPFSIDRESHRVITHPRVYPKIFPHSPSDLLRISGRAELSENRDFFKHLSSLMEAVAKPESESLREICNLSLEQVQSASGAELFLHALYDRLVNEGVIVISHITQEGSDGEVEEEGDVEMRESNEKDE Q9USM4 LUC7_SCHPO SPCC16A11.13; CHAIN 1..264; /note="U1 snRNP-associated protein usp106"; /id="PRO_0000362156" MAAEQRKIIEQLMGSNLSNFTSRGLVHFTDRKVCRSFLCGICPHDIFTNTKMDLGPCPKIHSDKLKSDYERASYSHDYGYEWDYLEDLERHVDDCNKRIDIAEARREKTKEEEERIDELMRDIIHTDHSIEVIITEMEALAKRKLVNDAVKHFIELNRLKTYRKELYDEVISMNEIPSQASTTHQKLQVCDICSAYLSRLDNDRRLADHFSGKMHLGYAMLRNIARDLRAQLEDREKSRDKKDGEKQRDNLASFEDKISTSFVA Q9USM8 ATG20_SCHPO BINDING 55; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 57; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 81; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 104; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250" SPCC16A11.08; CHAIN 1..534; /note="Autophagy-related protein 20"; /id="PRO_0000314769" MAQDDSYEEKPEVISSDSGGSGYSTEIQIVGTVTSSDGSYVEYEIVHQKRSVWRRYSDFESLVKLMRRQYPAAIVPPIPGKQSLLSYAKHPRKAKSDAEFLNFRSRMLELFLRQCLLHPCIRSNPIFDKFIHSTVSWHVTLSSLDLPKDSNTDPLRLPPIATEHDPFAHLRSSMPLVMANSLSPPSSRALKPIHSLSNPSTASSLEPSSPLGSEDECHPPTSDMQPTHELNESPSTPTAPDFPHYNSSPSELSPTQRRSSISNGKDAPSPVLKDLTSYTQEVIVCRKFLHHSLSPSIHSTLSSISKMESCLSKLGSAFHSLTALNEIQLANHLQVIANAFEFSGMYAKEFEQEFNSSVYEKMVQSMQLAKCAADALKYKQLKIQQRDFLQDQLIHSNTMSATDSMVAASPTIHPATRLNTIQRAVVSQAKKGYTIFGRLQNVLHDFVEGETSISKESLQQHKNTIENQLAAANWDCQKIDEFMDAELKFYKECQTSQWEEIIKSVHECIYKWAQTNLQRWLRTREELENLSKDI Q9USN8 RQC2_SCHPO MOD_RES 478; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC132.01c; CHAIN 1..1021; /note="Ribosome quality control complex subunit 2"; /id="PRO_0000116820" MKQRFSALDIAAIAAELREQVVGCRLNNFYDLNARTFLLKFGKQDAKYSIVIESGFRAHLTKFDRENAPLSGFVTKLRKHIKSRRLTGVSQLGTDRVLVFTFGGGANDQDPDWTYYLVCEFFAAGNVLLLDGHYKILSLLRVVTFDKDQVYAVGQKYNLDKNNLVNDNKSQSTIPHMTAERLNILLDEISTAYASPTSINEPLPDQQLSSSTKPIKVPKPVSLRKALTIRLGEYGNALIEHCLRRSKLDPLFPACQLCADETKKNDLLAAFQEADSILAAVNKPPVKGYIFSLEQALTNAADPQHPEECTTLYEDFHPFQPLQLVQANRKCMEFPTYNECVDEFFSSIEAQKLKKRAHDRLATAERRLESAKEDQARKLQSLQDAQATCALRAQAIEMNPELVEAIISYINSLLNQGMDWLDIEKLIQSQKRRSPVAAAIQIPLKLIKNAVTVFLPNPESVDNSDESSETSDDDLDDSDDDNKVKEGKVSSKFIAVELDLSLGAFANARKQYELRREALIKETKTAEAASKALKSTQRKIEQDLKRSTTADTQRILLGRKTFFFEKFHWFISSEGYLVLGGRDAQQNELLFQKYCNTGDIFVCADLPKSSIIIVKNKNPHDPIPPNTLQQAGSLALASSKAWDSKTVISAWWVRIDEVSKLAPTGEILPTGSFAIRAKKNYLPPTVLIMGYGILWQLDEKSSERRKARRLEMEVVETQGKVSELKMEGTSVTSEDNIQDVVSEVSYNEDTNNQSTPDTTGSDIHIVSEKRGKKGSKVITAKKVSAKERREARRARRQTALEESLKAPISIEDATDPQTILAILKQKKAKKKHAAREMEISSQIPSNDSSNVQTPTAESEIEEDGVSEPISAEVIEDQSRNSEAENEKGLSTEQRDEKKHAKVESFQRQEMPRSLFEEIFFAIDSLTPNPQQQDTVINAVPTFAPYNAMTKFNQKVKVMPGTGKVGKAARESIAYFMKKLPKSSKEAAYLENLKDGEIVAPISVSRLKMVFGSSGNTKKSKK Q9USP1 ELP4_SCHPO SPCC11E10.06c; CHAIN 1..361; /note="Elongator complex protein 4"; /id="PRO_0000339338" MSFKRKAAPQIAPTNLPTGVRLSSKDARWITSSGSSSFDYYLSGGIPMKSLLVIEEDSMDYASVLLKFFAAEGLKQDHVIWLGPSIGEMWFRQLPGDSDRPNKNENSAGEDNHSSPPSKNPQQERMKIAWRYEQVSKTKAPTLDMIPPGYTHSFDLSKNLIVKSDMKYAVSPFPLETGSNPYAPVIESLTRFLSTLTPGTVCRLVLPSILSPAFYSIRATHPQHFIRFIHTLSSLIKCTTSVHLICMCSVPSTLFSRDCEQIFWLENLASAVFSLHPFPVKETVNGLVTQPLGLFRIHKLPLALPFTNHANSNEAGDLSFTVSKRRFTIEPWVLPPLDDEQKDTKISNTNPQKQPVKSLDF Q9USP9 YHP4_SCHPO MOD_RES 330; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 332; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC902.04; CHAIN 1..589; /note="Uncharacterized RNA-binding protein C902.04"; /id="PRO_0000082026" MPLFLEEHAEYLKRYLEQALEPISDADASVLSDYAMALLRHDSSEEEVRQLCYSQLEDFLRQETIPFVDKIFDVLREKSYLEGASNMPSTGMVTEEVSRYSPTSSMIPATNSMETNFNNSLPAVGKTNTFPSQVPNMFGPPLYHPAATAPSEFMPSIPGFGNLPNPAMPPIPFLPFNPAAQPPFPPPFKMRGKRGFGMRHEHNSELRRHSPGNRRFNPYKAYPQPHLGHRFSRNAGNDPTSTALEVRNIPEEHFNEENIRSFFSKFGVLEKVELNPTHHSCVLEFTSHEAANNAWSSPEPIFNNRFIKIFWYNPSKGFHNRPKKFASHKSPTTSDSSNVESSEDVDPASLLQNEEFHKLIEERQRQHEERLKRINANKKALEELNQKKRELAQQQLKEQELLMQKIKETDRSGNKRLMLLETQHSLLKAEADCLGLPVSNVSESPAASNGSHHPYASGLPQRGTNTFFRGRGRGRGDMFASMSIDNRPTKLRVINVSPEKNEALLQYLFTVGGYEEITEPSTTERLISFQNRNSAEKFFGGVRNVEKLQELELAWVPKTAVTTNTTSMETGESNTSDNMNIEVEEGRWR Q9USQ1 CTF18_SCHPO BINDING 423..430; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC902.02c; CHAIN 1..960; /note="Chromosome transmission fidelity protein 18"; /id="PRO_0000239058" MDSIPNEDDLEKLLVAEQNVPYGKNYESFEDEENYLLELRNANALENLEHRSIPNDLFHSSQPVGSPTRNGDDIPSTLDLYSSDNAAIDTDISEDETINQRHAPQTDYRYPNTSANPKMGLEESMDIDMPSIDLDISNAAAFPRDSNLLFRNYNSHTKTSEKGSPVNFEKENQDSNVLFSTGRTSVLHIDAEQSQTNNTVTPLKDDALSLFSFENDVNGAVNDNSLDQKLSASKNSQRVSLPFFSKIELDEGSSFSGPKISARTSSGKIIYFPKKKNRHSDGLLLQPKRLADEISQVNEIGKDFNQDLLNSVRIWSENFLIVSKEKSVALKTEKLDSLQITNCTTKPQSQKLWVDTYRPQLFRDLLGDERVHRAAMHWIKAWDPCVFGKSRLQPSKSMRFNPRFTNITSDSDRPDKRIMMLTGLAGAGKTTLAHVIAHQAGYKVLEINASDDRTAHTVHEKVSSAISNHSALSSQPTCVIVDEIDGGDPAFVRALLSLLESDEKATEYSQAGNSKKKKKFKKLCRPIICICNDLYTPALRPLRPYAQIIYFRPPPQASLVGRLRTICRNENIAVDSRSLTLLTDIYNSDIRSCINSLQLLSLNNKRIDSETIKLLQPKSNSFSTSSLIQSLFLQLDNKQIRAIEASQPTYSHLDALLARIDGANDSESVLMNCFHTYLDLPFTDSLLSKPALTSEWLYFFDQLHSQCYKGNYELWRYIPYSIIHFHYLYATPEKCRLPHPPRSDLEALKLYRTRKEILDSFISTLNAYENQMHGERSILLELIRTILITINPTLKQKEDSMPRSALPSKIEHAINILNHYNLRFQQLPVGDGNYVYRLEPPLDELVWDAPTSSYSVRQMLSQELLKKRLADIKKQTLTDNPTSSNSSRKRKDFNSGKAIKRDFFGRIISEPKSEAVTSNNAALNTGDHPVSIKHAINIKFHDGFSNAVRKPISLNEILNF Q9USQ4 SIM3_SCHPO SPBC577.15c; CHAIN 1..396; /note="NASP-related protein sim3"; /id="PRO_0000363381" MSSDTKTLENSKGNSATDADTKNPSSSDSRAIEQLVTQGNMAYAQKNYEEAVDKYGQALMQSESIHGSESLENRNVLWLYGKSLFQIAIENSQVLGNALGAKESVSQATESFEEPEAIGSFTFSGQKIENKYTVNEENSSIAHPEKESEEKETNEASPASEEDEDDFNVAWEVLDLTRVMQSKAVDAYPDSKDEKIRLADIYDLLGELSLEIENFSQASQDLKTALEWKEKVYNVSNNTLLSEAHYKLALALEFTNPEDPSNKSRACEHVEKAAEILKNVLNERENEVTDKKGKGKQKAEESTLTSDLENLREMLSELEQKTLDLKHGAPSLEEAVMSKMHESSLLSKDSSSLAQAVAEAVKNANDLGGLVKRKRTKQEVTSSSQKEGPKDKKKKD Q9USQ7 DPH6_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) = AMP + diphosphate + diphthamide-[translation elongation factor 2] + H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696, ChEBI:CHEBI:456215; EC=6.3.1.14; SPBC577.12; CHAIN 1..606; /note="Diphthine--ammonia ligase"; /id="PRO_0000278564" MKVLGLISGGKDSCFNLMHCVSLGHEVVALANLHPEDGKDEIDSFMYQSVGHDVIPLYAECFDLPLYREKIGGQSINQNLDYQFTEKDETEDLYRLIKRVLTNHPDLEAVSTGAILSTYQRTRVENVCKRLGLKSLSFLWQKDQEKLLNDMVVSGLNAILIKVAAIGLTRKDLGKSLAEMQDKLLTLNKKFELHPCGEGGEYETLVLDCPLFKKRIVLTDKEVVEHSSGEVCYLKVKACVKDKPEWQPISLKSELVPNEELLGEEYSHIYHTISKKYELIDDQEETPTSLIPIPLRESAFQQKKGSFLVLGNVVATKGSYNTFQGEAESAINNLNELLGTYGYSNKNVYFVTVILSSMSKFAEFNSVYNKYFDFTNPPSRSCVAAPLASEYRIVMSCIVGDVTEKRALHVQGQSYWAPANIGPYSQSICANGVVFISGQIGLIPSVMELKLHDKIFEMVLALQHANRVAKAMRVGSLIACLAYVCDSRDADCVVKIWSEYTKNTGESSPVLVALVDALPRNASVEWQLLYNDSSCDVPLLSSLVTNQTLFGSDTAWDVALLNQNGLRMESSFIHHEHPSAYAIVLNNAFPNSQLLHVRYTARDQNV Q9USR0 CKN1_SCHPO SPBC577.09; CHAIN 1..404; /note="DNA excision repair protein ckn1"; /id="PRO_0000316565" MNSFLLAREWGQEPNSSFRRQLLQHRLQRLALNPDVKIKRRHGAGILGSVNALSIDNTIHQLMVSGGANSSINVWDLQNIDQKEDEDLILDTLNAVPARTSHKFGITDLHWFPFDNGIFTSSSFDHTLKVWDVSTLQEAYTFTMEDMIYSHAWSPIASHCLIATAYRSSSIRLCDMQSGSYTHSLSGHTGNVLAVDWCPKNEFVLASGSADGTCRLWDIRKVSSSFACMDLHNKYLPSNQTNISHYGTVNGLAWTSDARYLASCGTDDRIRVWNMESGRNTLREFGPIIHNQTTSFAVHPCMIQPSMDSDVFVLFPNDDGSLALLNLLEGSFVRRLSTHSLKRINCAAYRPDFEQCFTGDMNGNIYMWSPKALKSPTKISDLETRRNIIQEVYDSLINIPVTYQ Q9USR1 TXL1_SCHPO SPBC577.08c; CHAIN 1..290; /note="Thioredoxin-like protein 1"; /id="PRO_0000372631" DISULFID 31..34; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" MSVIEIRSYQHWISTIPKSGYLAVDCYADWCGPCKAISPLFSQLASKYASPKFVFAKVNVDEQRQIASGLGVKAMPTFVFFENGKQIDMLTGANPQALKEKVALISSKATGTGALASSSSAPVKGFASLQGCIENPQLECLNQQDDHDLKSAFNSNPSSFLESDVDEQLMIYIPFLEVVKVHSIAITPVKGETSSAPKTIKLYINQPNNLSFEDAESFTPTQVIEDIVYEQDDQPTIIPLRFVKFQRVNSLVIFIYSNVGEEETTKISRLELFGEPVGDSSKGKLQKVEA Q9USS2 PPK29_SCHPO ACT_SITE 163; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 31..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 58; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 472; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 596; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 657; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC557.04; CHAIN 1..872; /note="Serine/threonine-protein kinase ppk29"; /id="PRO_0000256826" MSVASFLTGEKLLAGSKFVIGKYNVTIEKYIAEGGFSHVYLVQTNSKTDGSPITAVLKRMYSPDENALRFVKTEIETMELLKSNPHVVSYIDSCIFPLEKAGVNTGFEILLLMEYCAGGGLIDFMNQRLQTRLSEHEVLKIISDIVQGVASLHYLRPPLIHRDLKVENVLLSFNTFKLCDFGSVTEPMHAAENSSEIQALEKSINTFTTYQYRAPEMINLYSGLGIDEKSDMWALGVLLYKLCYYTTPFETQGPNAILTASYSFPPFPPYSHSLKNVIIALLQPNPCLRPNIFQLMCEICRLRGTALPFRDIYSGRESSFYDLHNRKIMSLLRQTTTTPFAGNQVMPTPQVQGSRPPPPPPMPAPIYNVPNVPTVPTVSPNPFLQPTFSGTSQASAHPSIHSQSATFNNTQDVNRQSVSSPKVVSSSSVTGSGASGRKVYTPQSKNPFPISQGVTGTSSKFSASEVTEDNGSPNAGLDADNVDVEEVVNQRYPDLNELESQLTSHTNITTSSHHNPREQEIAKLADDAFASFRQTAGTSTANSTHTTGTQDISAFDTNFSEGVGSVRSSFDFPDRPVSRRPSSTSRSSVKITGPSSPNARSMAYEQHSFNLDDLSNTNFGSNNSLRHAKSFSKYYSPSHKDSNKTSRNTSKEGLPSSPTMLYRTTSNTRGDYIVQRTQQSANPLTNIEPQDMSNLSTDINASDVVADSTNSILYPTSTASSVANTIASDVDDFGTFNGLQRTVSLHSERASLDKKRPSFHDKNPYFKFSPSKYVDEGLEGESELRERVRSYANRSSSSFHNPDLTDTEIQETSFNNDLRPVASIQSAETSRSVSDRPANFPEELNDTLFEQKYPGIVDYEEPNSNAEKNVNI Q9UST1 PAN3_SCHPO BINDING 255; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03181"; BINDING 302..309; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03181" SPBC336.14c; CHAIN 1..589; /note="PAN2-PAN3 deadenylation complex subunit pan3"; /id="PRO_0000256831" MSVRKNSPASPKPTSRSRESSRSPSVTDLKDHSKAKRTLCRNILLYGSCKHSENGCAFRHDGPFIPSSENLEQYSVKKKLNAASASFQPVRALPVKAAGAAVFVPKSQEKSLFLSRERTPVALSPGSHAINPYNNASMLVNEPFHDDSGVYYTRQNQFKPTLYNLYNPQPSPMPTLLPYERTVNGLFIDDTTRERIERKSEASRQTISALPSIISSYTSLAPLNTKLYRYKEQIGFSSWTYKCTSSIDGNAYVLKRLQDCSINIDTSTVDKLKNVFHPNIVPFHSAFHTDTFHDSSLLLIYDFYPCTTTLGELYLNNSKNSVKLEENRKIPERELWNYFFQLTIALSYLHKSGFACNKLTPSRILVDQTERIRISGCADYELVVSNKPPLEERKKQDFVDLGVVIANLATGRTDMDMSSAARAIYSTYSREFYKAVLYFVSEVPEDKNLELFLQNHIESFFPIMSSPYVECEKMERKISDAFQHGRFFNILCKIMFIIDNNRASREYPIAREKEISLIYLLRDYLFHQIDEDECPVIDLYQVLNRLGKLDAGINQAIALISRDELDCVSVSYGELKAWLDNVYEMEINS Q9UST5 RRN7_SCHPO BINDING 11; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 16; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 30; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 34; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" SPBC336.09c; CHAIN 1..537; /note="RNA polymerase I-specific transcription initiation factor rrn7"; /id="PRO_0000097449" MEGNWFEGPPCSVRNCKSTWYFKNAGQTFCRRGHAQHGIEIAQDDEPGAGTFYQTRKRKVVRNHLDTGDEDEIVYGTAGRSLYLQAFQIILQLQCQALTTKLGFDQRIEGMIRDLWALYLSLSYESFTSSFLSLNQNSTQSESSDSDFDLIDPESQPGADPSSRKTKETSQSHSISYPRLLYSSAFIYVACLLLRLPLTIHKLEVLIRKNIIPYYRAYKQIPLKIFKRLQKNYVRMLIPFHYPTYQRIQSAVLTLVDVLVSKYELKVPPPNEPLILFELINSFFFPLEIFIPASRLLNLVHSQISLQGTSSDNYQSKIRSAQSIHEKLSDAEVMLLATILVAANVCYGFDDAQTRNSKYKDSMFTVKTNWNMWLSQVQKINEKEKDKFYEIDEQSILTLNNSEMDKYFQWYEKEFVEENNPNNIPEGILNVFPILSKDSHLQENQPTDILTDESVIAEDVKLEQVFKPVGIKESDKMDFSRRKDAYISMLPFSPNTENTAHRVTIMVAKLYNIKLDSLIAAIRYVESCLKTGIHNQD Q9UST7 SFC3_SCHPO MOD_RES 595; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 596; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC336.07; CHAIN 1..1339; /note="Transcription factor tau subunit sfc3"; /id="PRO_0000307794" MDSLIRHCSEEIALDGSSGCSIDRLWEFAANFFFRQGIVQNLDDNYKTFVWPLILKEDGIEVWIEDEDATGLRSKMQEIPWNYQDITIELRARIRLFASEDRQWLTLTYKTKTDSKIQPLAFELLSCISRYRQEGVDRIQLCKETKQEPRSVYGRIQALEDASLISKVAINRSRAQTALLVLKRFESENSTINETVAQVSGKQIYNTEKIRSNICDAVQSSRNGICRHVDARAMVNLNHSRWERRYYARQVTYLHNNGYLRKCLTFVPNSPERCIRCLQFIKPYISSLDATEDDVDFTEVDDIPEDDELEEEEPLLPSKEEFDASFLQPLADVGPTLPQWSRFRPLEFQCFVLIRNAGFHGVITLQILSGLTGIRFNKPLFKLLGSLVEHRSSVPNHLSHMSITRFEDKTKKSRQYRYFTLQSQLNRLIRDGIPAETISKLLPHVHSLAGEFSPIDSSLFLNSLHHKGNMESNAEVSPDGMTLLPRKRGRPRKSANISVTSSPIRPSKNENNLPSLAISPVSEGFIQNATISTPSTSSNLSIAGSLTPSKTSRIYRGLAPLKNPEFNEDHVKKAEHLEPLLNVSSSVPSKNFTVSSPDHLKYGNTSSLQVSDSQSSIDLDSSFHYPVSVDSQLSHSTGSLMANFSSPTKKRRLESVDFIFLQRKGLILSYLVEQNGAFEISRKMFEDLADLKVRRNPETSRTVMDRRTFQQTLEKLMQEKKVRKLVIATNNGLGKLVRKDIVVQYDMKPDSPRFQQLRAQITTPEIEKQSTPEILKDVDVDFLKRNTSLSRRKSMPAEIKRHKESSETKPVDKEEVKKNEKEKDDPMRLAQQLLESLAPDFALHENTQQKSPVEKPKKLRKDRYASVEEFDYFSSTEHASKRSVKRFKNDFTSDEDETLIRAVVITQIYYGGTNRLIKWEAVQKCFPNRDIYALTRRYLSIRQHTKFKGLQQFLSENWQQMYKDAVSRKDLMPYPDSVDDFDPTPYVKASCRPYMISSSNLATTRLPRDLVDVYETYNIEVVKQETNFREMIFDPSLSVASKMNAYCDMPFTMPLSLNDKQNNEGDENCEKGQLFDAKSTIKSIVAIPDATYDARFSQERLMQYPEDILIAAHQELLDKRIITRVNSENSRLQPGRNFQFTEKFASSLKSPLPPFLLSQAKRFNKFLLEGFQNHKNHLFEETSNSGTLACILDLLSQGKLQISIVGSKFNEYGLSEGYRTRLLEHDNINVTLVLSGKESESKKNYGVTEKLATPPSHEPRLWLNGKCELIEMIWMNIEQSIVYQLLRKPGILRSQLTNLLFPGLEPREFNEVLDYFIAAGAAIEKDGLYLNHNYLFKLT Q9UST8 RNH1_SCHPO BINDING 129; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"; BINDING 129; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"; BINDING 171; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"; BINDING 191; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"; BINDING 255; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00408" CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding. {ECO:0000250}; MOD_RES 97; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC336.06c; CHAIN 1..264; /note="Ribonuclease H"; /id="PRO_0000195437" MGGNKRAYYAVARGRNTGIYSTWDEASDQVKGYGGNRYKKFDSYEAAQEFCRTEGSRYSSSSGPYRRSTTSYGYSPYSSSSSNYSARHSDKYRKKISRSYSTEKDIEIFSNDTHEKSIACSDRQVVYADGSSLRNGKKGAVAGCGVFFGNDDPRNISVPLAGEEQTNNRAELQAIILALENTSGDLTIRSDSNYSIKSLTTWLPKWKKNDFKTSNSQPVKNLDLINRASDLMSDRNVSLEYVKGHSTDYGNQQADMLARRGASE Q9USU1 EFC25_SCHPO MOD_RES 552; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC336.03; CHAIN 1..987; /note="Ras guanine nucleotide exchange factor efc25"; /id="PRO_0000372377" MRRPNLDRLRLKSRQGFETSVSKPSTPSYSTYSLSPTFSDKSVLSPSTMSDSYALSSTYTAGSSYQNGESDYFGSLPTPSSDKSSTSPFPYLKGSFDDRFSSTHSLTRQPSPRSPLTPLKGNTRASPEIRYVSDFTPPSSPFEDMQASVHSLPLSGCSIGPVRTNHSSSLSNSSNSLLQTESSLRPNSSFVNSPFFPLPSSDDLFLNDRVINLFLFYEKFSYLFTHLLSAIKSRDALSIPSLVLSLQEELFNLCQQTGTFYLLQHNLLQNFEFENPIKLHFDKIIPYFSRLTVLTFSNRAFIFPDHTFPRLQQSAEDFLYHLQFFFTLCANNSLYLSRFCYYPSFVPNTPFGGKWTNNGLSAVSSAYRTRLLEPCLPELDKCVWFLLKNCDEFIENFSDFADEEYVFEICSTITSHSEQIFNKLESWDMSIYFDKDLSECEQATNFAVQSYFVTKQRCYDLLTDLVCSSQDLMMEHSNDFSTMPTMIASIAVAFQTLFENVCDFLKVRAALVDEMQELATKEFENKFSNANTAKDDEPARQTNKGTTRISRSSDFTAVSEMSKDTLTLGRNSLQSILMLDNLLTNKVVQSDNNVKGGTLPALVHYLVQNVHLNKDFRHSFLLTYKTFTTPQELFTLLVILFHELPPPGLDATAYSSWEKGDNFVTKKNVCTVMNLWVQKYFFEDLKARNTLYLISEMRTFLRDHVVPSFHIGSVILSEIDNLWTEEPPDSLTQRLLSSPMATFISLNVYAYTPEEFASQMTLLEFDYLKQIPSREWIFRSWVSRDSRSAVRNYINFSNCFTYWIINCILEKKNTKARTAVISFFIQTAYKCLSLQNFSTLMSIVSALNSAPIYRLHAAYKLVKAEDIICLSGLREIVETKKNFSTYRALLRKAELPCVPFLGVILSDLTFIDEGNPDVLDSSPHLLSFNKRHRLADVVADVCRFQSSSYEMQSNTDLQSYILHRCRFVNQDLSYLFDKSLSLEPRSS Q9USU8 NGG1_SCHPO MOD_RES 120; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 144; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC28F2.10c; CHAIN 1..551; /note="Chromatin-remodeling complexes subunit ngg1"; /id="PRO_0000353803" MSSEQQNEADSKPAVIPQCFKIENQYETFSRLSETSTPGVVPSVSTLWRLLFELQKMIECEPSCVEYFRQRKEELESHVDSEIETSKDESSVNKVEEKVEEFKEDNVEQEIKQKRSLSESPQESMLEKVSKKPKVSEAHNEEISPENVETIENELDLPVKGKDEQTTGLVYKNANDLLTGSLLSFIVDDSFSYEQKKKLLCVDSFPTSDVRSLVAGTPATDDFSHNKPNNQISISTFYSSLDPYFRAFNDDDIAFLKKGFDVSSSYNIPPLGERYYDLTPEDEMTNLCANSIYQNLQTSAQGSLEAFNEADTVSEEVRCGPLTERLMASLIPCYTQNDEEQKPSIAVGEFAETDSGSEKSKIGTSIDGIESGNNEYTEQPDIQESSLSICEDRLRYTLKQLGILYDGDVDWSKRQDDEISATLRSLNARLKVVSDENEKMRNALLQMLPEEMAFQEFQNVMDDLDKQIEQAYVKRNRSLKVKKKRIVTDKIGSSATSGSFPVIKSLMDKRSMWLEKLQPLFQDKLTQHLGSPTSIFNDLSDHTTSNYSTSV Q9USV3 SPF27_SCHPO SPBC28F2.04c; CHAIN 1..187; /note="Pre-mRNA-splicing factor cwf7"; /id="PRO_0000079616" MSYNISLDSLPYFESTYNEEDRSAAAQIVEEELKRSGGLLIKQEEQKKKFQSHRLSDRLENAIVAAGKGEKLAAIDVQRYIQLKPPGTRESLLQSAVVWEYQKSRNDNLYLLEKHGEKAFDSSLEALEVQLELLEKELVNTKKLSQGCNRKRKHYQMEVGARLAEAEVKFGQLLQSSIQCRVATLLS Q9USV7 CTR6_SCHPO SPBC23G7.16; CHAIN 1..148; /note="Copper transport protein ctr6"; /id="PRO_0000195050" MNHGGNSTMRHCSMKMTFNTDYDNLCIVFKSWHIGNLSQFLLSLLAIAILGYLFERLRSFTSLKETEFQRGYAGQQSEGLLTHHSKSLKSGRPFRLCALYAVQLVFSYFLMLVAMTYNAYVILAIAIGAAFGYRRSHCDTVQTVGLCH Q9USW1 ATH1_SCHPO SPBC21B10.03c; CHAIN 1..791; /note="Ataxin-2 homolog"; /id="PRO_0000450800" MATRSVSMKQTSQRAASPNKTQGAKKWSAVAARGSKIAQSATNDHRNVESIKVVPENRVRGGVAAKATDSSSNVTSLASSEENVSSVSGSAKSNNSQQRVWKTDVAISAEKRTETRQRELRRWMPDPEDAGVPLAGLEESTDNVEWDQFATNEKLFGVKSHFDEDLYTSRIDRSHPKYKEKEQEADRIAKEIEGTVTNNIHIAEERGLKVDDSGLDEEDLYSGVHRSIDVVRNYTRSNAYNKNNKDQKPKNHEAPHQHPQQKVVPPDDPAIVSHRHLALPRAPGPDSRAAERFFNARRKAGPLSRREKEGQIKEFMQFSQSLKIGSLDSKQPSSTKSVAEVKVADEKQLPDASSQATPADSKEPRKEEAEKPVTSATEVSSEKVEKVDGNTSSPSKEEEKPSTEPEKPSVVTQRKETTGTKLGTKLNAKAISFKPNVAAPVFTPGKFTIPSKPAPVNASRPMMPQQSNNSEASIPSTTPQSPSVVSNGENKPSSSPVFFNGPVSSEKEPILDNFNVFKNVGEEHQGAEQIDKPFSCPPTWNTGPNSLQQTIANSRPEGNSGSAKKAAAANPMIPSIVLPNSAMPSAMPMYPTPTMPYIPVGYPVPGYTPYMRNPSQHTSVAPSPNGTPTSGNSSTVGSPMIGYMAPQFIPPYAMPQFPPSGNGRGASAPATYFVPQMGGMMAYTMNGVPPMYGQYAPNNGMMNMHYPMYGDSRRSNSQRSFNSSNGKRSNVHKNNNASNTFSHSNASTSSSLNAAPNTTAKSSSQTAPPVSKGDATEKTEKDASANQEAKP Q9USW5 RS4B_SCHPO MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC21B10.10; CHAIN 1..262; /note="Small ribosomal subunit protein eS4B"; /id="PRO_0000130840" MVRGPKKHLKRVAAPHHWLLDKLSGTYAPKPSPGPHKARECLPLIVFLRNRLKYALNGREVKAILMQRLIQVDGKVRTDSTFPTGFMDVISVEKTGEHFRLVYDIKGRFTVHRITAEEAKYKLCKVKRVQLGAKGVPFLVTHDGRTIRYPDPLIKVNDTIKLNLETNKIESFIKFDTSAQVMVTGGRNMGRVGTIVHREHHLGSFEIIHVKDALDREFATRLSNVFVIGEAGKSWISLPKGKGVKLSITEERDRRRALKGLA Q9USW9 SGF29_SCHPO SPBC1921.07c; CHAIN 1..244; /note="SAGA-associated factor 29"; /id="PRO_0000116868" MVRPINAEEDVTSMWVKFHESLNPIRSSLIKQEECYKTVDGDDNPIEERIKACDAGIQTSEEQKKELEHTMQSLEMIINVLEKANEKPVITNSPLTRSRRNRGTSFTANTVTFTPGMSVAFKLPYTRHNEGGDWIQCIIIKVTGEGAKQRFEVQDPEPDDDGNAGQIYKTTANHLIQIPAKGTPLPPISPKTNVLARYPETTTFYRAEVIRTLPDGSCKLRFEGEEEVGKETVVERHLVLEYNG Q9USX0 PVG3_SCHPO CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:11780, Rhea:RHEA-COMP:12570, Rhea:RHEA-COMP:12571, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:132088, ChEBI:CHEBI:132090; EC=2.4.1.134; SPBC1921.06c; CHAIN 1..378; /note="Beta-1,3-galactosyltransferase pvg3"; /id="PRO_0000076296" CARBOHYD 53; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 97; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 180; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 354; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFSNSKKKIFLYVLIAGVATFSFAFLVLNRLQAEEHSLAYVENLFLDPFIKQNESLAHANDRPFKLYLGIFSQAKNVDRRNFLRTDYNEYIKEFAVNDTVDVRFILGLPENEQELATIREEQRTYGDLAVLPIPENVDAGKSIVYFQTFLEGYQPFPLFSELADNLIMPSTQFHGSFIYNQSIKTYELPGMKEFQDLGEPKHDYDFIVKADDDSFLNLPRLFEMLKEHVGKSRFYFGRDCTRRELPTAVRDFPYMCGFFYIVSPDMAYEVAKRRNIIIPFEDAQTGYSIYLSGNVKNAEFSKCTLYDLILPNEGFNYRQSYLRIDAIAVHKLKSIPLLSTVSNWFKKMYEHRANCSALIETERLSCLQATIPLPSLDV Q9USX1 APE1_SCHPO ACT_SITE 317; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 144; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 281..285; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 316; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 320; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 339; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC1921.05; CHAIN 1..882; /note="Aminopeptidase 1"; /id="PRO_0000095103" MQVTIPKSTSKEDDKNRNLLPKNVKPIHYDLSLYPDLETFTYGGKVVVTLDVLEDSNSITLHGINLRILTAALEWGSQTVWASEVSYGDERIVLQFPSTVPANSVAVLTLPFTARISSGMEGFYRSSYVDSDGNTKYLATTQMEPTSARRAFPCWDEPALKATFTIDITAKENYTILSNMNAVEETVKDGLKTARFAETCRMSTYLLAWIVAELEYVEYFTPGKHCPRLPVRVYTTPGFSEQGKFAAELGAKTLDFFSGVFGEPYPLPKCDMVAIPDFEAGAMENWGLVTYRLAAILVSEDSAATVIERVAEVVQHELAHQWFGNLVTMQFWDGLWLNEGFATWMSWFSCNHFYPEWKVWESYVTDNLQSALSLDALRSSHPIEVPIMHDYEINQIFDAISYSKGSCVIRMVSKYVGEDTFIKGIQKYISKHRYGNTVTEDLWAALSAESGQDISSTMHNWTKKTGYPVLSVSETNDGELLIEQHRFLSTGDVKPEEDTVIYWAPLKLKTMKDGKAVVDEKAVLSDRSKKIKVDKEALESYKLNSEQSGIYRVNYSADHLKKLSQIAVEKPDYLSVEDRAGLIADVASLSRAGYGKVSSTLDLIKTWKDEPNFVVFAEMLARLNGIKSTLRFESSDIIAAMKKLVLEVSATKAHSLGWEFKANDDHIIRQFKSTVYNYAGLFGDDKVVKDALSKFDAYASGNKSAINDNLRSAVFNIAIRYGGAKSWDQLLEIYTKTNDPYVRNSCLRAFGVTEDEKYIQKTLDLTLDPIVKEQDIYLILVTLSTHKNGVLAMWKFATSNWDKLLSRLPVAGTMRGYVVRFVTSGFTHASAIDKIKEFFADKDTKLYERALQQSLDTISANSSFIDKSLDDITRWLKENRYM Q9USX3 RAD60_SCHPO PTM: Phosphorylated by cds1. {ECO:0000269|PubMed:12897162}. SPBC1921.02; STRAND 333..343; /evidence="ECO:0007829|PDB:3GOE"; STRAND 346..351; /evidence="ECO:0007829|PDB:3GOE"; STRAND 376..379; /evidence="ECO:0007829|PDB:3GOE"; STRAND 400..404; /evidence="ECO:0007829|PDB:3GOE" HELIX 356..367; /evidence="ECO:0007829|PDB:3GOE"; HELIX 390..392; /evidence="ECO:0007829|PDB:3GOE" CHAIN 1..406; /note="DNA repair protein rad60"; /id="PRO_0000097154" MDNLDEDDLAFFSKPIKKPPLNYAKQLIASSSDSEEESELDTNKQALEHINAQKNITHNENKSAEPLSRQSTILDADEGNQDVSDTTPNACLNEGRHSPKSAISCVTQPVSPVYNTRAAANLRNNSINSEAALSTTSSLLDDDFARRLEEIDRQVQEFEKSSSDMDVQIHTHKREIEEDDDNTSADVPLLKHSKSDHSTLYHSKSEFSTNEPVISVVLQLAVIGQRIPNSNISLPRDWEAPLFFKVKSNQQFRRVRIAYSERKKVDNVVLVFQNQRLWDYGTPKGAGMLKVDTRLVVHAYCHSDFISLKRIKELEVEKLSSVTEDSTAQTCKLITLLLRSSKSEDLRLSIPVDFTVKDLIKRYCTEVKISFHERIRLEFEGEWLDPNDQVQSTELEDEDQVSVVLD Q9USX7 PPK22_SCHPO ACT_SITE 280; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 161..169; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 184; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 154; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 339; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 341; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 348; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1861.09; CHAIN 1..526; /note="Serine/threonine-protein kinase ppk22"; /id="PRO_0000256821" MARETEFNDKSPSSTDDGMSQSHFSDKLKNLFHFRRNRAATVSTSVRNDQRDNDSDDSTFDINVNQLNELDLNDSSDQLDSRPSLRRVSSAPDSHKGVEAPPPRPLINMSNIRKAQVKILKNPGNYIFGRTEYGKRTYSGNSTKISRVEVTPHSFEKIRLLGQGDVGKVYLVRQKSNHRLFAMKILNKREMIKRHKVNRVLAEQEILTKSKHPFIVTLYHSFQSRDYLYLCMEYCAGGEFFRALHSLPKHILPEKDACFYAAEVTAALEYLHLMGFIYRDLKPENILLHQSGHIMLSDFDLSKPISIVTHPTVVLPKHSTFSQEKPALDTNSYFSNFRTNSFVGTEEYIAPEVIRSCGHTVAVDWWTLGIFIYEILYGTTPFKGKNRHATFSNILYSDVSFPEYHGAPNVSSTCKSLIRRLLVKDESKRCGSVAGASDIKQHPFFRHIQWALLRSMKPPIIPKIEDGMEAVEPSDNDNEEEDFLNSQYLISANLPAVDMHSSTPVNEQSNPFDSFSSVTLHHAGDE Q9USX8 RU2A_SCHPO SPBC1861.08c; CHAIN 1..239; /note="U2 small nuclear ribonucleoprotein A'"; /id="PRO_0000074186" MRLNAEFLSQVPSFISPLKETELDLRWYQIPIIENLGVLRDVHDAIDFTDNDIRYLGNFPRMKRLQTLLCGNNRITAIAPDIGKVLPNLKTLSLAQNHLQEIADLDPLASCPQLTNLSCIDNPVAQKQYYRLYLIWRIPSLHILDFERVRRNERLRAEEVFGQIQNPTEIASSIMGVKSRVFDLAALVQSHPEANSPITTGYTLTPEEREKIKEAIKNASSIAEINRLEAMLLEGKIPK Q9USY1 YOW5_SCHPO ACT_SITE 61; /note="Proton donor; for PsiMP glycosidase activity"; /evidence="ECO:0000250|UniProtKB:P33025"; ACT_SITE 196; /note="Nucleophile; for PsiMP glycosidase activity"; /evidence="ECO:0000250|UniProtKB:P33025" BINDING 123; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P33025"; BINDING 143; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P33025"; BINDING 175; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250|UniProtKB:P33025"; BINDING 177..179; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P33025" CATALYTIC ACTIVITY: Reaction=D-ribose 5-phosphate + uracil = H2O + psi-UMP; Xref=Rhea:RHEA:18337, ChEBI:CHEBI:15377, ChEBI:CHEBI:17568, ChEBI:CHEBI:58380, ChEBI:CHEBI:78346; EC=4.2.1.70; Evidence={ECO:0000250|UniProtKB:P33025}; CATALYTIC ACTIVITY: Reaction=ATP + pseudouridine = ADP + H(+) + psi-UMP; Xref=Rhea:RHEA:22448, ChEBI:CHEBI:15378, ChEBI:CHEBI:17802, ChEBI:CHEBI:30616, ChEBI:CHEBI:58380, ChEBI:CHEBI:456216; EC=2.7.1.83; Evidence={ECO:0000250|UniProtKB:P30235}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P33025}; SPBC1861.05; CHAIN 1..747; /note="Pseudouridine-metabolizing bifunctional protein C1861.05"; /id="PRO_0000362159" MLIVMNRGCRLVSRIPLGFRRLKRNPNPGLRNILCRRYSPLALSKEVTEALKNNVPVVALESTIITHGMPYPQNEELAIQVESKVRSMGAVPATIALLNGQCTIGLEQFQLSELAKSGETAYKVSRRDLSYVASQRLNGGTTVAATMILARAAGIDVFATGGIGGVHRGAENSMDISADLIELGRTRVAVVSAGVKSILDIGRTLEVLETQGVPVVTLGPPKSAFPAFFSRESKFQSPLSLETPQLIANMLFSNIQLGQECGTLVAIPTPHHCSIDYEKMEALIETCLQRSVQLGITGKNVTPWLLGELLRESKGKSLNTNIDLVLNNAEKASLIAKELAVLKEKSSFFPTNTGNTFETKPVKQDFFYGKVSDKGVSSSKKKITETTSKPAEVVCVGSVSIDSVLKLDNPLTSKFLGTSHPCHSEQAFGGVAHNMALASSLMGASTKLVSCVGTKSVPTSSIKEYLTKSSLQHTIVEKSNFTSCSYTAINDCNGNLLLAGADMAIMENLSYSEIKDDLNDAKYICFDGNISPSLMLDITTSKSSKQRVVFEPTSGPKTLKILKVLSVASIDFITPNKFELDVLFQAMKDGNFFENESWWQKLNSFGITSSFYNEIERFTKSTGIEEITENGILQKCFHLLPFIKNIIVKLGPNGALLISSEKLQGVNSNSASLFTPGNVTVKYYPVPKVIATPVNASGTGDTFIGTFTALLSKGWGMDDAIDTAQKAAGLTLQCNFSVNPEIKTLLK Q9USZ3 RUXE_SCHPO SPBC11G11.06c; CHAIN 1..84; /note="Small nuclear ribonucleoprotein E"; /id="PRO_0000349132" MSGRVQKVMIPPINFIFKLLQQHTPVSIWLFEQTDIRLQGQIRGFDEFMNIVLDDAVQVDAKNNKRELGRILLKGDNITLIQAI Q9UT12 YLW2_SCHPO SPAP8A3.02c; STRAND 51..54; /evidence="ECO:0007829|PDB:5YLB"; STRAND 78..80; /evidence="ECO:0007829|PDB:5YLB"; STRAND 83..89; /evidence="ECO:0007829|PDB:5YLB"; STRAND 117..123; /evidence="ECO:0007829|PDB:5YLB"; STRAND 129..132; /evidence="ECO:0007829|PDB:5YLB"; STRAND 142..149; /evidence="ECO:0007829|PDB:5YLB"; STRAND 151..157; /evidence="ECO:0007829|PDB:5YLB"; STRAND 162..168; /evidence="ECO:0007829|PDB:5YLB"; STRAND 173..176; /evidence="ECO:0007829|PDB:5YLB"; STRAND 184..188; /evidence="ECO:0007829|PDB:5YLB"; STRAND 190..198; /evidence="ECO:0007829|PDB:5YLB"; STRAND 201..206; /evidence="ECO:0007829|PDB:5YLB"; STRAND 210..216; /evidence="ECO:0007829|PDB:5YLB" HELIX 45..47; /evidence="ECO:0007829|PDB:5YLB"; HELIX 60..68; /evidence="ECO:0007829|PDB:5YLB"; HELIX 72..75; /evidence="ECO:0007829|PDB:5YLB"; HELIX 92..95; /evidence="ECO:0007829|PDB:5YLB"; HELIX 96..100; /evidence="ECO:0007829|PDB:5YLB"; HELIX 103..109; /evidence="ECO:0007829|PDB:5YLB"; HELIX 136..138; /evidence="ECO:0007829|PDB:5YLB"; HELIX 178..182; /evidence="ECO:0007829|PDB:5YLB" TURN 158..161; /evidence="ECO:0007829|PDB:5YLB" CHAIN 1..225; /note="Uncharacterized protein P8A3.02c"; /id="PRO_0000315939" MLYENMSDSFLLSDAGLEFDEALLEVDQEKDDYLDDFENWTVVPVETIEGINYYPNCLPESVQRNLINNVPKELLSIYGSGKQSHLYIPFPAHINCLNDYIPSDFKQRLWKGQDAEAIIMQVYNPGDGIIPHKDLEMFGDGVAIFSFLSNTTMIFTHPELKLKSKIRLEKGSLLLMSGTARYDWFHEIPFRAGDWVMNDGEEKWVSRSQRLSVTMRRIIENHVFG Q9UT30 BRR6_SCHPO MOD_RES 90; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC8F11.06; CHAIN 1..297; /note="Nucleus export protein brr6"; /id="PRO_0000317216" MEMYVEDVPMPDIGPDSVLNTPIRPKYEILKSKKKTQNENDPEPMDISMSPDEKNLKKSTVRRKLRKSKPNSSSNQVSSRTRALTKRSNSSNAIIKANNQDSVYVSDWTNVHRDIPIVVSGYLQLMFNACVASIFLYFLFKIVFGIQNDVRNRVEYHKILQEEQAADCQREYLSINCDSPGPAIFEVCQKLKQCKMESSNNVGSTKLAALVFAEIIDAFISHISYKTMVFSLILVFGSLLTSNYAFGLYRARHSQNIHDYAANAIPAMIPSSRFLPSNLSDISNRNLIEAASQEEEI Q9UT33 DPH3_SCHPO BINDING 25; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:Q3E840"; BINDING 27; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:Q3E840"; BINDING 47; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:Q3E840"; BINDING 50; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:Q3E840" CATALYTIC ACTIVITY: Reaction=[3Fe-4S](1+)-[protein] + Fe(2+)-[Dph3] = [3Fe-4S](0)-[protein] + Fe(3+)-[Dph3]; Xref=Rhea:RHEA:71235, Rhea:RHEA-COMP:17996, Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33751, ChEBI:CHEBI:47402, ChEBI:CHEBI:83228; Evidence={ECO:0000250|UniProtKB:Q3E840}; CATALYTIC ACTIVITY: Reaction=2 [3Fe-4S](0)-[protein] + 2 Fe(2+)-[Dph3] + NADH = 2 [4Fe-4S](1+)-[protein] + 2 [Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71239, Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:17998, Rhea:RHEA-COMP:18001, Rhea:RHEA-COMP:18002, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:33723, ChEBI:CHEBI:47402, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228; Evidence={ECO:0000250|UniProtKB:Q3E840}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q3E840}; SPAC8F11.02c; CHAIN 1..79; /note="Diphthamide biosynthesis protein 3"; /id="PRO_0000082636" MSFYDEIELEDFTFDAGTNLYTFPCPCGDRFEISLEDLQLGEDVARCPSCSLIVRVIYDEDEFMEVDNDASTAPIIIAA Q9UT42 LSB6_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; SPAC343.19; CHAIN 1..624; /note="Phosphatidylinositol 4-kinase lsb6"; /id="PRO_0000088849" MESTFHSDTLDSFPNYQENSLNTNEEQTNPLESLRDGWASSNSSSSSSLLLPDENEGNEVFGSLKGLVTQSKFGQWANKLSKSLQARRRKSESISKPRVYYSVFMAPSWVLHAEKHWEEYPHYAGYDYKDYVRLLDATKEAIAHGVFPVLISKGSSGSYFVKNKVQKNIAVFKPKDEEPYGKLNPKWTKWFHRNLFPCFFGRSCLIPNTSYLSEAAACVLDRGLGLYLVPYTSVASISSPTFNYDYFARKAFLTRNKPLPEKTGSFQQFLDGFVVASKFFAQHPWPGTRHRETREYTESVASSEDFDIFDPFLAENEIETEFWTEELRLKFRFEFEKLVLLDYLMRNTDRNLDNWMIKICYEPCDNEEYYKSINLLSTNLTPNMSANSVDPAISQTSDFWKGPHFQIGAIDNSLAFPYKHPDSWRSFPYGWLSLPRSLFTQPFTEFTRQLFLHKLTSREWWEKLSDDLRNVFNQDLDFDEKMFSRQLSLVKGQAYNIVEVLKNPLMNIYDLLELPNLYVVEDVVRIEVNEPTSANSEEAEFGLPIKRDYGSILHPSCSQTFPPYPGSQLLQATPGRSFSSNAEALLPLNYITLLSKDSSSPKMLKDVIFERLQCASSNAVFSTC Q9UT46 MOC3_SCHPO SPAC821.07c; CHAIN 1..508; /note="Transcriptional regulatory protein moc3"; /id="PRO_0000115010" MNPYVSYPEIHMKRNRTGSINSNPLYIPNPNVEPTPKPTKRRTKTGCLTCRRRRIKCDETKPFCLNCTKTNRECEGYPNSAAQMQAMGSVSPPELSVHSAQQPLIPTSIASSSAQTGDTFSGSSQSNFNTNDLNQMTSSSNLSTVTPIKQDHQKPMNLQGFPSAYQQHQYLQSNHNVPTNNSSSATSSTKPSVQSVGQASYPFLSSVSNFPSNFNSELFPFYFHDVVPSICAFEFDNNIALHFWSVTVPQFAQSMPCIANSLMAFASIKKLDVFGAYSHLTRALRCPMPGPNSFEYLLVSAFLTLTQLNLPAYDLNFCNNFIRKLSWSSSTKSNYVSLLIAMVVRELVFAILPRGCIWGFNGKPLSEVSVSRSHAPVSDSLFTIGLDILSQPTLSDDLHRERMVAWRDEYHVHLYSASRSPLTKVIDCVGHAVTKNNNDVLSGLQQLMQEECTDIAVLRTSYLCVLSLQNVFASNSKEFKLRAQIESHFGRLMLEHFMDCNVLNRPVL Q9UT48 EIF3H_SCHPO SPAC821.05; CHAIN 1..357; /note="Eukaryotic translation initiation factor 3 subunit H"; /id="PRO_0000316244" MSDTTSLNVPELESPPIERVELESLLVMNIIKHCRDSFPNMGTIGQLVGIDIDGVLQVSSSFESPSVLENEESAVNKSVSGKARQAHTEAMLNRLQYIGAVTGHVGWYLGAYVSSFLSSPFFVETQYAYQKANPNSIAFLYDLSQSSNGTLYMRAYQLTPEFMAAHEEKTWTASSLNSHNLTPSNVIRELPIVIHNSHLATCLLHSLSEPPTPASTLTAEAALEDCESNLPLTETFSNFEVSLGTRYRKNIELLLESTDEFHYEQGNLGFHQRQLAREQAKIQQWIAKRKAENANRAAENLQPLPLDDWKRIFKLPAEPRLLDSLLISSQIMKSTQIDEQSSAFLSKLAGVRNAYAS Q9UT52 MOD21_SCHPO SPAC806.08c; HELIX 5..17; /evidence="ECO:0007829|PDB:6L80"; HELIX 26..38; /evidence="ECO:0007829|PDB:6L80"; HELIX 46..62; /evidence="ECO:0007829|PDB:6L80"; HELIX 66..82; /evidence="ECO:0007829|PDB:6L80"; HELIX 86..102; /evidence="ECO:0007829|PDB:6L80" CHAIN 1..677; /note="Gamma-tubulin complex subunit mod21"; /id="PRO_0000352819" MTMSRADQILQHLLRELIHNDSLVASEWLKHSKKIIQNVPSSTLVFHEMIEHIKGICDKMGIQGREDLEMPLRNACEVLNRQTVSVKQSILHAQILKLFLELSKPPSDIHVPQIPVYKDCNKNEQEAIIQLLTSCEGDHWLMPDWSSMPDDETITEDSEEETFNGNANEITIPANIHIPIIEESDNASNNKLCTLFKKSKQPNLDFLQIKPFMFWDSSLNETVRISERSIIRDSIYMLIGYPSFFFLKNGSKIETRLSLLPKLHHMSEEILRSIMTELADYGSNLEFFRQKLTSPSDSFFKSDDQSTKNEPFLSVVFIYPQIKPHLLSCLKNTHQELIKLETEVYNATKNCTLFQFFQHVKKFVDPLLCFRFAYEKSATNMWDFVKTLEFIYSTRNYSSQMFKLYKASAIAMLLWMVNQASQITSSMTIARPLYNILILCKDFPNNFLEKDNIALQLGSIVFDQSPTLNNLLVEMEILIRSKILKLGKSLDLSFDFQSLMGEFENLIKQQEEAKKSLWSKRFSRFYYGHYVFVNTCHNFFLTLYQSFTEVDENSIFNGVFETLNNDVDDESVIGEKEKLILKQKQKCLSEFFVDDIKKLLNEELLNCQKQELPDVMENTYQISTVSGIKNDPLFTLDQTCNIIAKLADNLIHPSVPIGSSAYRCRRNLADLLFLIMP Q9UT53 NMAH_SCHPO BINDING 135; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 136; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 143; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 215; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 250; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 252; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 263; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 282; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 313; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 318..321; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q96T66" CATALYTIC ACTIVITY: Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1; Evidence={ECO:0000250|UniProtKB:Q06178}; CATALYTIC ACTIVITY: Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, ChEBI:CHEBI:58437; EC=2.7.7.18; Evidence={ECO:0000250|UniProtKB:Q06178}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q06178}; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 75; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC806.06c; CHAIN 1..368; /note="Nicotinamide/nicotinic acid mononucleotide adenylyltransferase"; /id="PRO_0000316624" MHTMNGDNFANSFPKNPLLSRNSSSSNVIQYSDEFSPDEDWLNEHAAKEHEERIRRPSVNRAWQKNSTSGGPSVSLEKREADVASLGEVMDLEEVPRGITRQARQLNEYIFPKHRFRNHLVDEGKIPLVLVACGSFSPITYLHLRMFEMATDTIQEQTNMELVAGYFSPVNDHYKKEGLAPAYHRVRMCELACERTSSWLMVDAWESLQPSYTCTARVLDHFDEEINQKRGGITLSDGTKRPCKIMLLAGGDLIASMGEPGVWSDKDLHHILGKFGCCIVERTGSDVWAFLLAHDIMFAYRGNILVIKQLIYNDISSTKVRLFIRRGMSIRYLLPNSVIQYIERYALYRDAEPVKTIFYQSPFVRMEP Q9UT55 ART1A_SCHPO BINDING 27; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 113; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 248..249; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 248; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 249; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 286; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 363..367; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371"; BINDING 401; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q04371" CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate; Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721, ChEBI:CHEBI:43474, ChEBI:CHEBI:138881; Evidence={ECO:0000250|UniProtKB:Q04371}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; Evidence={ECO:0000250|UniProtKB:Q04371}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q04371}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250|UniProtKB:Q04371}; SPAC806.04c; STRAND 84..86; /evidence="ECO:0007829|PDB:7T7K"; STRAND 99..101; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 106..108; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 223..226; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 240..246; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 269..276; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 323..326; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 356..361; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 394..399; /evidence="ECO:0007829|PDB:7U1Y"; STRAND 430..435; /evidence="ECO:0007829|PDB:7U1Y" HELIX 19..25; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 27..47; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 54..74; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 87..98; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 109..125; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 137..146; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 148..159; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 161..171; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 174..191; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 196..200; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 204..207; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 208..210; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 213..218; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 220..222; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 228..235; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 252..266; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 289..302; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 306..320; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 330..333; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 338..340; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 341..344; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 346..352; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 362..370; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 381..384; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 386..388; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 412..419; /evidence="ECO:0007829|PDB:7U1Y"; HELIX 423..425; /evidence="ECO:0007829|PDB:7U1Y" TURN 128..132; /evidence="ECO:0007829|PDB:7U1Y"; TURN 283..285; /evidence="ECO:0007829|PDB:7U1Y"; TURN 389..391; /evidence="ECO:0007829|PDB:7U1Y" CHAIN 1..438; /note="Damage-control phosphatase SPAC806.04c"; /id="PRO_0000230801" MKFLNPPFPYSMTSDPESFGHECFTRRWGIILTGIEKDVSERLSKLASTSKDSEVVAQGKPLLNDLEAFKSDIKNDRPLVPLEGEGQDIVEYNEELKQLDNASWGNAPWLYSECYYYRRISLIFARYSEWKAYDPFFQQKDSTLKSSRAAVEELAGRYCLLEEELNSIAKKGDSHIAYMVFVEMAQISLWGNATDLSLLTNLSYEELQNLQGQKVVEESQKNILVNDFPTVWSKLKDVHNGRIDFVLDNAGFELYVDLIFAAYLLKAGIAKEIVLHPKDFPWFVSDVLPYDIEYLLTNLDTIFPTESVTKFATDLRSFSAKGQLRLRTDPFWTTAHYFGRMPDFAAGLLTELEKSDMIFFKGDLNYRKLTGDCLWPRTTPFGKTLGPIANAINACALRTCKADVVVGLPDGLYEKIAKDLPHWERTGKYAVVEFCPKA Q9UT61 MAN1_SCHPO ACT_SITE 402; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 290; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 292; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 402; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 615; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPAC513.05; STRAND 42..45; /evidence="ECO:0007829|PDB:7DD9"; STRAND 58..60; /evidence="ECO:0007829|PDB:7DD9"; STRAND 62..69; /evidence="ECO:0007829|PDB:7DD9"; STRAND 71..73; /evidence="ECO:0007829|PDB:7DD9"; STRAND 89..91; /evidence="ECO:0007829|PDB:7DD9"; STRAND 103..111; /evidence="ECO:0007829|PDB:7DD9"; STRAND 123..131; /evidence="ECO:0007829|PDB:7DD9"; STRAND 141..143; /evidence="ECO:0007829|PDB:7DD9"; STRAND 152..154; /evidence="ECO:0007829|PDB:7DD9"; STRAND 157..159; /evidence="ECO:0007829|PDB:7DD9"; STRAND 165..174; /evidence="ECO:0007829|PDB:7DD9"; STRAND 180..182; /evidence="ECO:0007829|PDB:6LZ1"; STRAND 193..201; /evidence="ECO:0007829|PDB:7DD9"; STRAND 282..288; /evidence="ECO:0007829|PDB:7DD9"; STRAND 293..297; /evidence="ECO:0007829|PDB:7DD9"; STRAND 325..327; /evidence="ECO:0007829|PDB:7DD9"; STRAND 356..358; /evidence="ECO:0007829|PDB:7DD9"; STRAND 362..364; /evidence="ECO:0007829|PDB:7DD9"; STRAND 368..371; /evidence="ECO:0007829|PDB:7DD9"; STRAND 397..399; /evidence="ECO:0007829|PDB:7DD9"; STRAND 421..423; /evidence="ECO:0007829|PDB:7DD9"; STRAND 438..443; /evidence="ECO:0007829|PDB:7DD9"; STRAND 447..453; /evidence="ECO:0007829|PDB:7DD9"; STRAND 456..458; /evidence="ECO:0007829|PDB:7DD9"; STRAND 460..462; /evidence="ECO:0007829|PDB:7DD9"; STRAND 485..490; /evidence="ECO:0007829|PDB:7DD9"; STRAND 493..495; /evidence="ECO:0007829|PDB:7DD9"; STRAND 547..550; /evidence="ECO:0007829|PDB:7DD9"; STRAND 654..656; /evidence="ECO:0007829|PDB:7DD9"; STRAND 666..669; /evidence="ECO:0007829|PDB:7DD9"; STRAND 672..674; /evidence="ECO:0007829|PDB:7DD9"; STRAND 678..686; /evidence="ECO:0007829|PDB:7DD9"; STRAND 688..692; /evidence="ECO:0007829|PDB:7DD9"; STRAND 697..702; /evidence="ECO:0007829|PDB:7DD9"; STRAND 712..715; /evidence="ECO:0007829|PDB:7DD9"; STRAND 720..723; /evidence="ECO:0007829|PDB:7DD9"; STRAND 725..731; /evidence="ECO:0007829|PDB:7DD9"; STRAND 737..742; /evidence="ECO:0007829|PDB:7DD9"; STRAND 747..749; /evidence="ECO:0007829|PDB:6LZ1"; STRAND 753..756; /evidence="ECO:0007829|PDB:7DD9"; STRAND 761..768; /evidence="ECO:0007829|PDB:7DD9"; STRAND 786..790; /evidence="ECO:0007829|PDB:7DD9"; STRAND 794..800; /evidence="ECO:0007829|PDB:7DD9"; STRAND 802..814; /evidence="ECO:0007829|PDB:7DD9"; STRAND 817..826; /evidence="ECO:0007829|PDB:7DD9"; STRAND 828..830; /evidence="ECO:0007829|PDB:7DD9"; STRAND 837..845; /evidence="ECO:0007829|PDB:7DD9"; STRAND 848..857; /evidence="ECO:0007829|PDB:7DD9"; STRAND 863..869; /evidence="ECO:0007829|PDB:7DD9"; STRAND 872..879; /evidence="ECO:0007829|PDB:7DD9"; STRAND 889..892; /evidence="ECO:0007829|PDB:7DD9"; STRAND 894..900; /evidence="ECO:0007829|PDB:7DD9"; STRAND 905..912; /evidence="ECO:0007829|PDB:7DD9"; STRAND 915..919; /evidence="ECO:0007829|PDB:7DD9"; STRAND 922..929; /evidence="ECO:0007829|PDB:7DD9"; STRAND 941..956; /evidence="ECO:0007829|PDB:7DD9"; STRAND 972..977; /evidence="ECO:0007829|PDB:7DD9"; STRAND 979..981; /evidence="ECO:0007829|PDB:7DD9"; STRAND 988..993; /evidence="ECO:0007829|PDB:7DD9"; STRAND 997..1004; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1006..1009; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1011..1021; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1023..1029; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1034..1040; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1046..1050; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1061..1065; /evidence="ECO:0007829|PDB:7DD9"; STRAND 1070..1077; /evidence="ECO:0007829|PDB:7DD9" HELIX 17..22; /evidence="ECO:0007829|PDB:7DD9"; HELIX 23..26; /evidence="ECO:0007829|PDB:7DD9"; HELIX 34..36; /evidence="ECO:0007829|PDB:7DD9"; HELIX 38..41; /evidence="ECO:0007829|PDB:7DD9"; HELIX 51..53; /evidence="ECO:0007829|PDB:7DD9"; HELIX 114..117; /evidence="ECO:0007829|PDB:7DD9"; HELIX 205..223; /evidence="ECO:0007829|PDB:7DD9"; HELIX 229..244; /evidence="ECO:0007829|PDB:7DD9"; HELIX 251..264; /evidence="ECO:0007829|PDB:7DD9"; HELIX 271..275; /evidence="ECO:0007829|PDB:7DD9"; HELIX 299..319; /evidence="ECO:0007829|PDB:7DD9"; HELIX 330..339; /evidence="ECO:0007829|PDB:7DD9"; HELIX 341..352; /evidence="ECO:0007829|PDB:7DD9"; HELIX 373..390; /evidence="ECO:0007829|PDB:7DD9"; HELIX 410..416; /evidence="ECO:0007829|PDB:7DD9"; HELIX 426..429; /evidence="ECO:0007829|PDB:7DD9"; HELIX 466..474; /evidence="ECO:0007829|PDB:7DD9"; HELIX 500..515; /evidence="ECO:0007829|PDB:7DD9"; HELIX 528..538; /evidence="ECO:0007829|PDB:7DD9"; HELIX 558..561; /evidence="ECO:0007829|PDB:7DD9"; HELIX 565..591; /evidence="ECO:0007829|PDB:7DD9"; HELIX 599..611; /evidence="ECO:0007829|PDB:7DD9"; HELIX 624..652; /evidence="ECO:0007829|PDB:7DD9"; HELIX 663..665; /evidence="ECO:0007829|PDB:7DD9"; HELIX 781..785; /evidence="ECO:0007829|PDB:7DD9"; HELIX 831..833; /evidence="ECO:0007829|PDB:7DD9"; HELIX 883..887; /evidence="ECO:0007829|PDB:7DD9"; HELIX 958..967; /evidence="ECO:0007829|PDB:7DD9" TURN 79..84; /evidence="ECO:0007829|PDB:7DD9"; TURN 147..149; /evidence="ECO:0007829|PDB:7DD9"; TURN 160..163; /evidence="ECO:0007829|PDB:7DD9"; TURN 477..481; /evidence="ECO:0007829|PDB:7DD9"; TURN 539..544; /evidence="ECO:0007829|PDB:7DD9"; TURN 615..620; /evidence="ECO:0007829|PDB:7DD9"; TURN 658..660; /evidence="ECO:0007829|PDB:7DD9"; TURN 743..746; /evidence="ECO:0007829|PDB:7DD9"; TURN 775..777; /evidence="ECO:0007829|PDB:7DD9" CHAIN 1..1077; /note="Alpha-mannosidase"; /id="PRO_0000363389" MTLFPVLNNTPVGKQVDSIYESRLDQFLSEGQYRDFNLPSVYDHARIDNPSGDVNNDLSKGFVDLKVYRVPDLSRPSFNEVVGHKKFDETASKGDTFGPSWATFWFEVHIRLPKSWAKYEQVIFQWNCDNEGLVYSQDGVPLQAFSGSERTDFILPDSWKTTEDTFYIEMACNGMFGTGAGSQIAPPDPNRYFTLTKADLVAPNLPAMALAYDFLLMQQCVKQLPSNCWQKYKARQICNDIMNTFHPNDLSTINECRNLAKAFLGNDIDSEAVFEKNNDKANVFAIGHCHIDTAWLWPFAETRRKIVRSWATQMNIMDRYPEYQFVCSQALQYLWLKEDHPDVFEKLKEYVNQNKFIPIGGSWVEHDTNIPNGESLIRQFLLGQHFFEKEFGVRCRTFWLPDTFGYSSQIPQICRLCGMDRFLTQKLSWNNINSFPTSTFNWVALDGSQVICHMPPANTYTADTNVNDVLHSIDQHKNLVNDQAGLLVFGIGDGGGGPTPEMLEKLRRCKGIANTVGYLPNVKLGNTVDEFFDGILKRTNAGQTLPSWNGELYFEFHRGTYTTQAELKKLMRKVEIALHDAEYVSTLASIFSKDYSYPKESLQDLWRDTLLCQFHDVLPGSCIEMVYKDAIPIMSKVLKNTEALLWQAIEQLGFKKASSSDNKEQLCLLNTLPWNVRGVITETEENKLVYFESCDGKGILTAAHTSLKHPAAAYQKDDNFILVNDHLRVTIAPNGLILSLFDLHKEREILDLKSGKNHAGANQYVLFEDTPLSWQAWDTEVFSLEKYEVLDKGKVSIKESGPLRASVVVDIPISELSHMKATISLEGYNDCSEFTGVNFTCEVDWHESCKFLKVEFPVDIHSEFASYETQFGITKRPTHYNTSWDVAKFEVCHQKFADYSDFTYGVSVLNDCKYGFSTHGNLMRLSLLRSPKQPDAHADMGKHTIRYAVYPHSKPLDSSTVRAAHKFNSNFRLLTRASDTANLDIFDAFQLVGEPNVILSHIKMAEKGKSIILRVYESLGGKSRARLVIKSLTVASVTKCNGLEEDLEELCTLKSNDYYEVPIELRAFEIATFKVNL Q9UT67 IMT2_SCHPO SPCC4F11.04c; CHAIN 1..345; /note="Inositol phosphoceramide mannosyltransferase 2"; /id="PRO_0000372336" CARBOHYD 55; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 269; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVKVIYKFAVFAAVNFFLMSSIVLYFNNEFLMFADRCTKDIIPSEELRYLRQVLNDSIPSKDEPLPTLKLDSLNDISGEPVIPKIIHQTWKTTEVPEGWKGAQQSCIDLHPDYEYILWTDEMSRNFIADNYPWFLPYFDAYPFNVQRADVIRYFVLYHYGGNYIDLDDGCRQRLDSLLYYPVWVRRTDPVGVSNDVMGSVPHHPYFELIIQNLEKNAKSYWLPYLTIMLSTGPLSISFLWEKYKRQLPNPPAFYDHIRVLLERDYKFSNDSYFTFYEGSSWHNNDAGIILWANRHLAYVIVAGFCLYFILSYMFFSKLLDSRYVQRFVTSKRKQPTLPLALQEDV Q9UT74 LYS4_SCHPO BINDING 377; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 437; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 440; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2R,3S)-homoisocitrate = cis-homoaconitate + H2O; Xref=Rhea:RHEA:15485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15404, ChEBI:CHEBI:58174; EC=4.2.1.36; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC343.16; CHAIN ?..721; /note="Homoaconitase, mitochondrial"; /id="PRO_0000247927" MDSGEMHHPYQAFSKVGKCEISQTNPSFSSGMRCLVRSADIQFKGICGLTRGFASFNKPPQTITEKIVQKFAQNIPENKYVRSGDYVTIKPKHCMSHDNSWPVALKFMGIGAKKVFDNRQIVCTLDHDVQNKSEANLRKYKNIESFAKGQGIDFYPAGRGIGHQIMVEQGYAMPGSMAVASDSHSNTYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPIARVNLVGQLPKGLSGKDIIVSLCGAFNHDEVLNHAIEFYGEGLNSLSIESRLTIANMTTEWGALSGLFPTDEKLLAWYEDRLKFLGPNHPRVNRETLDAIKASPILADEGAFYAKHLILDLSTLSPAVSGPNSVKVYNSAATLEKKDILIKKAYLVSCTNGRLSDIHDAAETVKGKKVADGVEFYVGAASSEVEAAAQKNGDWQTLIDSGARTLPAGCGPCIGLGTGLLKDGEVGISATNRNFKGRMGSREALAYLASPAVVAASAIAGKIVAPEGFKNAVSLVSAVDITDKVNKQTASKSSTEAVDSETAIIDGFPSIVAGEIVFCDADNLNTDGIYPGRYTYRDDITKEEMAKVCMENYDSEFGKKTKKDDILVSGFNFGTGSSREQAATAILSRGIPLVVGGSFSDIFKRNSINNALLAIQLPDLVQKLRTAFANESKELTRRTGWHLKWDVRKSTVTVTTSDNKEMSWKIGELGNSVQSLFVRGGLEGWVKHEISKSN Q9UT76 EI2BB_SCHPO MOD_RES 106; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 108; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC343.14c; STRAND 204..209; /evidence="ECO:0007829|PDB:5B04"; STRAND 228..232; /evidence="ECO:0007829|PDB:5B04"; STRAND 255..259; /evidence="ECO:0007829|PDB:5B04"; STRAND 273..276; /evidence="ECO:0007829|PDB:5B04"; STRAND 279..281; /evidence="ECO:0007829|PDB:5B04"; STRAND 287..290; /evidence="ECO:0007829|PDB:5B04"; STRAND 307..310; /evidence="ECO:0007829|PDB:5B04"; STRAND 347..350; /evidence="ECO:0007829|PDB:5B04"; STRAND 355..358; /evidence="ECO:0007829|PDB:5B04"; STRAND 365..368; /evidence="ECO:0007829|PDB:5B04"; STRAND 371..373; /evidence="ECO:0007829|PDB:5B04" HELIX 4..7; /evidence="ECO:0007829|PDB:5B04"; HELIX 11..21; /evidence="ECO:0007829|PDB:5B04"; HELIX 28..45; /evidence="ECO:0007829|PDB:5B04"; HELIX 51..68; /evidence="ECO:0007829|PDB:5B04"; HELIX 73..96; /evidence="ECO:0007829|PDB:5B04"; HELIX 141..144; /evidence="ECO:0007829|PDB:5B04"; HELIX 170..184; /evidence="ECO:0007829|PDB:5B04"; HELIX 187..191; /evidence="ECO:0007829|PDB:5B04"; HELIX 192..197; /evidence="ECO:0007829|PDB:5B04"; HELIX 212..222; /evidence="ECO:0007829|PDB:5B04"; HELIX 239..251; /evidence="ECO:0007829|PDB:5B04"; HELIX 261..263; /evidence="ECO:0007829|PDB:5B04"; HELIX 264..267; /evidence="ECO:0007829|PDB:5B04"; HELIX 268..270; /evidence="ECO:0007829|PDB:5B04"; HELIX 293..302; /evidence="ECO:0007829|PDB:5B04"; HELIX 313..315; /evidence="ECO:0007829|PDB:5B04"; HELIX 324..327; /evidence="ECO:0007829|PDB:5B04"; HELIX 333..335; /evidence="ECO:0007829|PDB:5B04"; HELIX 342..346; /evidence="ECO:0007829|PDB:5B04"; HELIX 360..362; /evidence="ECO:0007829|PDB:5B04"; HELIX 375..377; /evidence="ECO:0007829|PDB:5B04"; HELIX 378..385; /evidence="ECO:0007829|PDB:5B04"; HELIX 388..391; /evidence="ECO:0007829|PDB:5B04" TURN 98..100; /evidence="ECO:0007829|PDB:6JLY"; TURN 235..237; /evidence="ECO:0007829|PDB:5B04" CHAIN 1..393; /note="Translation initiation factor eIF2B subunit beta"; /id="PRO_0000317323" MSTINVEHTYPAVSSLIADLKSRKVQGPFAVAVETALVMRQVISQTRWSTVDQLIDTVRAVGSTLVKAQPTEFSCGNIIRRILRLIREEYQELLKTADENEKLIVSSSNSSSPSQKRDIPSNEKLVQSHEPVSVQMYSSMLNLLGRPTLESPTHSKTVGDSRVTGGMDMRAVIISGIQDVIDELDKINTDIEVQSMDHLHSNEIILTQGCSKTVEAFLRFAAKKRKFSVIVAEGFPNNQKGSHAMAKRLAQAGIDTTVISDATIFAIMSRVNKVILGTHAILGNGGLVTYSGAQLVAQAARHHATPVVVCSGIYKLSPVYPYDLESIIQLSSPDKIMSFNEGDLISRAEILNPYYDYIPPDLVDLFITNLGGYPPSYLYRIMNDTYDASDTIL Q9UT79 MSC1_SCHPO SPAC343.11c; CHAIN 1..1588; /note="Multicopy suppressor of chk1 protein 1"; /id="PRO_0000096590" MRKNSSHENQSSENIIEFPYVDFEELNVHSNIFSELEHAKPSTQQQQQQQNISNETTSTGPRICISRDEFKAVNLLTKEEINVRVTPKKEEFSRGLDFISDLYDQTARKSGAVRVIPPDNWKCPLTINTTTFKFLTRKNNPSSMSLVSNYPLDAISSQQKFHGNDKTLEKNSAKATINKSNSTAETSSTATVEPYDSNDLYRIFDRPDAVVLSYIFVLGKAVDLLQIKQWLQLSKQKNLLEFEFWSQAAQHYKLDVNSLRNAYNLYAETGVTTRTGNDGGSPINRPAKRVKRQNHIPKCKLCAQEGSSLVTCCICQSNYHYACVEAPFAPFSDIHYWTCNSCIPSSLKILWKEVDYHCISSFLQSSNELASSLKKQLPSFLAQTPLTLPSNTKTPPASARQSSRRTRSTSGKGFETKISINLDSDIKLLNTLSPLETFFWCCSFPSTASTSSPFSYYPESLPTPLLGRAVNTTAFPTSRQNAYYNDPWNLYFIHFSKLSPLRFTPPGILTSTISLGQPLTCQGWQRDSMSLFGMHYHHYGAQRIWYVIPEVDGPKYEKLLNDLSPSFIQEKPETLIKSKILLPISMLISNGIQVLTFVQNSNEFVITSPNTYYTVLDTGFSLSESVPFATKEWIQDMHAENSFNMYKNLHISAPFSLDHILLANATLDKTVHSAYWLMTCLKDRVDRELTLRNEFRKRHPLLTWIPTPLESSVMACAFCKTFAYLASIEEKNGTKTACLSHKDECFPNTDSDLTVLVRYDDNALLAAYSKVVERAHKADTWLENYKEALGSDNSRPSLKVLKTLLNEAETICCPLQEVSLVRNLVKTAQQWLDKFAIIFKKKSMVKKEKRKPKRGSATHSHLESPSEEVEDLNSSNINEADLLINLVEEAEQFTFDFPEMAVAFEKAESLKIFREKANAMKERSLSYEECLAIVEEGESLQLKTPELLYFKQYMEKTEWIDSFNQISQKTDSTMEELVELIERGEKIGLTSDNENMATALLLKEKSENWMKQVEGLLSQETLSTSKLFQLKSEANSICINRGLLEQLNEVLQKSENFHTQLVSLISRARDPDYYSRPTIEEAKTVLAESENLTNKPEEYTVAQKLLTQTYEWVRRGKRLFGKANAPLEIFNQHLEFVEQRNTNAMVDEGSDAPFHVGNEYYVIAGSDPSDFHYCFCRQPEAGMMIECELCHEWYHAKCMKMSKKKLRADEKFICPICDYRVEVPRHSHRPPLIELQKMVDDIPTLPFQPIEIELLKRVVKQAEEFKNKMQSEVCDPTQLSEKDVPLLQFYLRKLEGSEILFTEELNVFRQKLHEFMPVAPQPPPFIGESRSNRKPRPTKRQREIMEQVESGKLTSAEGAAAIAATQTRNQNNFISKPFNVHTLSTTLSPWAMKSLAQAAISPNPMPSAHDLLPTSNPAELFTNISPEIKELSVDSTSTLGGLNSSHLVSDQNASVICLCRQPFAISDGTVQCHNCLEWFHYECVGLSSDIVSTLSNYACPDCCSKEGKLYPWNTRPRSTPSVWLSQAYSPSVLQGTTENVAFLNKAFSASANLFDVLPVSNTPSHFSKMDYVLEDRKPDLFTETYLSM Q9UT81 UBX3_SCHPO MOD_RES 156; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 167; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 186; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 190; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC343.09; CHAIN 1..410; /note="UBX domain-containing protein 3"; /id="PRO_0000211006" MDREDILKEFCNRNNIDVSQGRFFLESTNWNYELATALLHEVIPPEEDHGLQPSSDVSKVPEVTGSSSGISGGDQQPPRPLQRQQNTQGQGMKSGTASKKFATLRDLEGNDESAEEKSHLFTGGEKSGLSVEDGDPDPKKQLVRDILEKARQHTISPLDEQDSGPSSLASSWASVGQRLGTENEASGSTTPVTQSGPPRENPPTESQPEKPLRRTLYFWRNGFSVDDGPIYTYDDPANQEMLRYINSGRAPLHLLGVSMNQPIDVVVQHRMDEDYVAPFKPFSGKGQRLGSTYMQPRMSQMPGGLYTDTSTSSSVPINVKPNSTTPHASLQIDENKPTTRIQVRLSNGGRTVLTVNLSHTLHDIYEAVRAVSPGNFILSVPFPAKTLEDDPSVTVEAASLKNASLVQKSL Q9UT86 APC11_SCHPO SPAC343.03; CHAIN 1..94; /note="Anaphase-promoting complex subunit 11"; /id="PRO_0000055750" MKVKILRYHAIANWTWDTPKDDVCGICRVPFDGCCPQCTSPGDNCPIVWGKCKHIFHAHCIQNWLATSGSQGQCPMDRQTFVVADSTNEKSETQ Q9UT91 RMP1_SCHPO MOD_RES 156; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC323.08; CHAIN 1..211; /note="Ribonuclease MRP protein subunit rmp1"; /id="PRO_0000372385" MQELQYDVVLLQKIVYRNRNQHRLSVWWRHVRMLLRRLKQSLDGNEKAKIAILEQLPKSYFYFTNLIAHGQYPALGLVLLGILARVWFVMGGIEYEAKIQSEIVFSQKEQKKLELQSQDDIDTGTVVARDELLATEPISLSINPASTSYEKLTVSSPNSFLKNQDESLFLSSSPITVSQGTKRKSKNSNSTVKKKKKRARKGRDEIDDIFG Q9UTA4 POPI_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; SPAC25B8.16; CHAIN 1..698; /note="Ribonucleases P/MRP protein subunit pop1"; /id="PRO_0000337990" MKRSTGGTQPKGLNVKRSKLADARFIEVESPALSNGAVDLKKFIESRSFEITALQDAMKRSKESSAQRAFQALPRCLRRRAASHNIKRIPKGLRDRALYEMQLSSSSTLPIAPSRQRLKRFIKRLRRKLAKSGETKAIDSTGSLVTDNSTDDSRIPSLAAVKLIRGKFAGRQLRKVWLPTHLWVCKRAHMINAWGYAIPEKPTEKSYRPTHRAAFRKDAIAFDMSYEPLFCISGPYEALKEKFGNSFANGLPPVFLNSSRSFTSYLVKSDIHELICPCFLQWNNPTEDDKKQIPVKNPTECVQLVIRLHPSAFLQAWNYLSGIAVLDDRIAMHDWRLDLASFDIHGPDSNIMLHKVFDDVELDEAGKVWQSISNYSSACLPMGASISVKALVNTRCDKNLSEKGEKSLLDSAENSLPASANQYSTHFRYWERQEIPSFAVFENKNRHTHEKKSSEKEVIPVYITYRKEWNGLTVILPWDYAKFVWRKMMYQKGIRFGGLENLHQIAFEKRMPFFPIDYPDTISGQLCEEERKKRNEDSWKRRPPAKRVNYQKFGDNFSEIGNPFCCDWVYLNEMVKASRDEDKTLQLVRVQVQLVQRGSLQDRARIYCLSDDELSKWKTIIYKENLTAENLLYPKCPNETAIIGFVTTGNFNLNAGKPSGIANVLAKTIKNEKSGYCIIRNVGCSVPRLAQWKFNQSH Q9UTB6 SDS3_SCHPO SPAC25B8.02; CHAIN 1..267; /note="Transcriptional regulatory protein sds3"; /id="PRO_0000352833" MDVLSRVFDNEKEELDPLLNNPLTASEFRAKKAELEAELESIRNGTCKTLLDLADELRRSRDEELEIAERWRTFLVNRAQEEYEVEMKAAKEEYEYRCKTLKEMVLSHLNEKKRKIYEAKDMFDIGSESSTLLLHDASSQFIDRRKLRHRRNAGNQQNTQQLPSLNFFDDYLLFPTDETAVIPQSVKNAVRNSVNSVKPTSAEASLFSPLLSMANANPTNGRERDPRASERAERDREKAVEKGLSGATEEDIQSDLQLLKKELAKKK Q9UTC6 ISU1_SCHPO COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:11939799}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:11939799}; TRANSIT 1..53; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC227.13c; CHAIN 54..192; /note="Iron sulfur cluster assembly protein 1, mitochondrial"; /id="PRO_0000019698" MSVFRRSVQCVGVLPSILAQRSSLLARPANLQFLKTNSSKFVPQVTANVSRRMYHKNVLDHYNNPRNVGTLPKGDPDVGIGLVGAPACGDVMRLAIRVNKDGVIEDVKFKTFGCGSAIASSSYVTTMVKGMTLEEASKIKNTQIAKELCLPPVKLHCSMLAEDAIKSAVKHYRSKQLTPVGTTAGAIESATA Q9UTD5 ATG10_SCHPO ACT_SITE 132; /note="Glycyl thioester intermediate"; /evidence="ECO:0000250" SPAC227.04; CHAIN 1..179; /note="Ubiquitin-like-conjugating enzyme ATG10"; /id="PRO_0000310849" MSFKSQLLILAQKLSKGGISCELIEFDECILKLEWHTELLDKNDSLLYEQEEDDILSLMNPMITMHAWIRDSPSFEVPQFFFQPYANGSDPLTKMEQIFELLEGSSQNLAYDALAIGDCPGTVGIAWYIHPCRTRDYFEMLQIDKEDPKYLSLWLLYIHQVLSPLTQPIIKAVDDAEKS Q9UTE0 SEY1_SCHPO BINDING 46..53; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03109" MOD_RES 746; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC222.14c; CHAIN 1..762; /note="Protein sey1"; /id="PRO_0000155139" MSTASNRVSTQIVDEHKQFNNELPKFMQSVGLLDAGFNYHVVAVLGSQSTGKSTLLNNLFGTSFSVMDASKRQQTTKGIWLSKANNSPILVMDVEGTDGRERGEDQDFERKSALFSISTSEVIIVNMWENQVGLYQGSNMALLKTVLEVNLQLFHNKKERCLLQFVIRDFLGNTSMENLADTIMTDLNNIWASLSKPEGFENSVINDFFDVGFTGLPHKILCSDAFSEAVDSLRERFVDNNNSDYIFNVSYHKKIPADGFSLYTREIWDTIENNKDLDLPTQQQLLAQYRCDEIITEVMEPFSTACTILQKEFLPGNLCKDLPTKLLNMFETVIEAYDRQASRYNVHIYQKKKQELIASVDSHLYVFFQAQLNALHKELIKSFFDASNEFPSDTPFKESSSIKINELVNKMREEGESLSLPHVHWDVDPFILKLSEELTQNSETLCKEKLKEKLEELFTGFEFEVSEAVEVAFQKLSHNVWDTLLNEFLAAQNTTIEKIKNIVPFYVDIDDTKTTEEYIINFKKNSWLFFRKKIDSEMSEVLLQQRLRVYFEELFRYDSDGMPKLWKKSGTIDRDYRESLTKTLDLINVLASIKVSDGNYPDLNVDIKTLEPEYTSPASFFTILNRRRVSDISVNFKRSADLIFMDCKRSVINTTTRIPPYFWVLLIVLGWNEFMAILRNPFVFMILMFGGTVVYGLYISGLIWPAKMVLERATNNLVDLATDRFSNTYQEQVQQRAMQRTEKSGSPVASADDAEAEKTALS Q9UTF7 ELOH1_SCHPO CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000250|UniProtKB:P40319}; MOD_RES 325; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B2.03c; CHAIN 1..334; /note="Putative fatty acid elongase 1"; /id="PRO_0000316229" MDLTGAHMLKIHRPSIDHPFGVDLWHLFEQLSIKTIGWNPSEFEYIPGKTPMSQWSSVIVSITAYYVIILSGRAIMTNRKPLKQRRLFQLHNFILTIISGALLALLVEEVFRNYMRNGLFYCVCDSRHFTQRLVTLYYLNYLTKYLELMDTVFLFLKKKPLAFLHCYHHGITALLCFTQLLGRTSVQWGVIGLNLYVHVIMYSYYFLAACGRRVWWKQWVTRVQIIQFVLDLILCYFGTYSHIAFRYFPWLPHVGDCSGSLFAAFFGCGVLSSYLFLFIGFYINTYIKRGAKKNQRKAAGKADNTSVAAAAGSEALAATTATNASPFSARSRKL Q9UTH3 PPK6_SCHPO ACT_SITE 636; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 509..517; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 533; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1805.01c; CHAIN 1..775; /note="Serine/threonine-protein kinase ppk6"; /id="PRO_0000086147" MSQDVFKHLTSKQVQRTRARSFGASFERPLASFLPKKENKNLLSNAARVKLLTFSSSSPYSFSYSPVLSRDANDGYIPLDTSSRANLWESVTDYDLQHANEPLVGNYYISTEALGDGLNRSPFTINPEKRRSLSDISYVPIPHKEHSNWPVHCSSQAIVTTSNTTFSIWSANDYFCLLFGYAGSQLNRHSVFDIFPKSFSSHLSNLIVSFPIDNEHERILFCGDVFPVITVDGVRLMDFWVKEKQGKLIWILEFVEESYIDIKLQDGVAVDERTEQPLTSDLLPSRLPKTWDQRLYLTTKTTEGYYCPSMIYPLSKSSFQYIIFHYAAGLLFINSDFKIISLNEALFESMLGYSDLLTKDISLIFPDFKLVLQQLADSHALDPGRVVSEIHVRHAYRTCTADKMKKADYPYLIHSDGNIIQIDCQIISVSPHSVKSNEPAFGVWLIFDSVDNRASDFVRSMRSSVILEEVVISDESEEEEDLSADEDYVDSEWEVVPHNIASYTTIKELGIGAYGQVKLATYKSNKVHEVILKSISKSRILLDSWMRDKDLGTVPMEISILHFLKAHSHPNIVKMITFFEDNENYYLLTEPQKPGIDLFDYIELKPSISEKESKAIFFQIALAVAHLHSFDIIHRDIKDENVILEGNGCARLIDFGSSSLTKNGPFDTFRGTVGFAAPELLRGEKYLGKEQDIWALGILLYTIVYRENPYYNIEEILDAKLRIPFELSKDNVDLICRMLDRNVHDRITIEETLQHHWFDDIRYLDTSHIRIPLSS Q9UTI3 ARD1_SCHPO CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, ChEBI:CHEBI:133369; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P07347}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500, Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P07347}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504, Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P07347}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508, Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741, ChEBI:CHEBI:133371; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P07347}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P07347}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516, Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739, ChEBI:CHEBI:133375; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P07347}; SPAC15E1.08; STRAND 3..5; /evidence="ECO:0007829|PDB:4KVX"; STRAND 43..46; /evidence="ECO:0007829|PDB:4KVX"; STRAND 52..60; /evidence="ECO:0007829|PDB:4KVX"; STRAND 71..78; /evidence="ECO:0007829|PDB:4KVX"; STRAND 84..86; /evidence="ECO:0007829|PDB:4KVM"; STRAND 106..113; /evidence="ECO:0007829|PDB:4KVX"; STRAND 130..135; /evidence="ECO:0007829|PDB:4KVX"; STRAND 145..151; /evidence="ECO:0007829|PDB:4KVX" HELIX 8..10; /evidence="ECO:0007829|PDB:4KVX"; HELIX 11..16; /evidence="ECO:0007829|PDB:4KVX"; HELIX 22..25; /evidence="ECO:0007829|PDB:4KVX"; HELIX 28..36; /evidence="ECO:0007829|PDB:4KVX"; HELIX 65..67; /evidence="ECO:0007829|PDB:4KVX"; HELIX 80..82; /evidence="ECO:0007829|PDB:4KVX"; HELIX 87..103; /evidence="ECO:0007829|PDB:4KVX"; HELIX 117..124; /evidence="ECO:0007829|PDB:4KVX" TURN 17..20; /evidence="ECO:0007829|PDB:4KVX" CHAIN 1..177; /note="N-terminal acetyltransferase A complex catalytic subunit ard1"; /id="PRO_0000310300" MDIRPARISDLTGMQNCNLHNLPENYQLKYYLYHAISWPMLSYVATDPKGRVVGYVLAKMEEEPKDGIPHGHITSVSVMRSYRHLGLAKRLMVQSQRAMVEVYGAKYMSLHVRKSNRAAIHLYRDTLQFDVQGIESKYYADGEDAYAMHKDFSTLKFDTPETNDELAKTVQSLALNN Q9UTI5 VPS29_SCHPO SPAC15E1.06; CHAIN 1..187; /note="Vacuolar protein sorting-associated protein 29"; /id="PRO_0000339646" MLVLVIGDFHIPDRAPKLSEKFRQLLIPGKISQIICLGNLTSTSVYEYLKHVCSDLKLVKGAFDISSKAPIAGKITLGSFKIGYTNGHLVVPQDSPEALSILAREMDADILLFGGTHKFAAYELDGCFFVNPGSATGAPNVSAVEDDEKIVPSFVLMDVQGAVLILYVYRIFDGEVRVEKMQYRKPE Q9UTI7 TYSY_SCHPO ACT_SITE 497; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P0A884" BINDING 350; /ligand="dUMP"; /ligand_id="ChEBI:CHEBI:246422"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A884"; BINDING 477..478; /ligand="dUMP"; /ligand_id="ChEBI:CHEBI:246422"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250|UniProtKB:P0A884"; BINDING 524..527; /ligand="dUMP"; /ligand_id="ChEBI:CHEBI:246422"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A884"; BINDING 527; /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"; /ligand_id="ChEBI:CHEBI:15636"; /evidence="ECO:0000250|UniProtKB:P0A884"; BINDING 535; /ligand="dUMP"; /ligand_id="ChEBI:CHEBI:246422"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A884"; BINDING 565..567; /ligand="dUMP"; /ligand_id="ChEBI:CHEBI:246422"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:P0A884" CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000250|UniProtKB:P06785}; SPAC15E1.04; CHAIN 1..625; /note="Probable thymidylate synthase"; /id="PRO_0000310825" MSQPLHARFATRAVKNPMILEKERQLTDSKYHILVAATGSVAAIKLTLIVKSLLTYKGVDVQVVLTDPARNFVEKEDLTALGVNVYNNADDWKNWDGLECPITHIELRRWAHLLLIAPLSANTMAKMANGLCDNLLTSLIRAWAPLKPILLAPAMNTLMWTNPITQEHLSAISRIYKNSEFIMPIEKVLACGDIGMGGMAEWRNIVGRVADKLQLEQKSVLPNAVKNIDGQDDDSSEQTAAFEEYDDDDDDDVDDNEQSNSMIETSANADITPKASLLPSTTESSISKDHETSQAPLGSESVDTQASENVTTKPEPPVPFTSSEYRNTEEEQYLNLIRYILENGQSRPDRTGTGTRSVFAPPQLRFSLRNNTLPLLTTKRVFLRGVLEELLWFIHGDTNANHLSEKGIHIWDGNGSREFLDSRGLTDRKVGDLGPIYGFQWRHFGAQYVDCDTDYTNKGVDQLAQVISTLKLNPYDRRIILSAWNPLAIPEMALPPCHIFCQFYVSEPCKPGGKPQLSSMMYQRSADMGLGVPFNIASYSLLTHMIAHMCGYEAAEFVHVMGDCHIYNDHLEALQTQLERVPKAFPKLFFKRDAKDIGSIDSFSVDDFAVEGYNPYGPIKMKMSV Q9UTJ7 SDHA_SCHPO ACT_SITE 333; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q9YHT1" BINDING 61..66; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 84..99; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 268; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 289; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 301; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 400; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 434; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 445; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9YHT1"; BINDING 450..451; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q9YHT1" CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; Evidence={ECO:0000250|UniProtKB:P31040}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q0QF01}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 92; /note="Tele-8alpha-FAD histidine"; /evidence="ECO:0000250|UniProtKB:Q9YHT1" SPAC1556.02c; CHAIN ?..641; /note="Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial"; /id="PRO_0000010341" MLRFRKVAPSLKNGGNLKLFSTSSTLKKIASSQPLRAKQVSTSESVKYPVIDHTYDAIVVGAGGAGLRATFGLAEAGFNTACITKLFPTRSHTVAAQGGINAALGNMTKDDWRWHFYDTVKGSDWLGDQDAIHYMTKEAPKAVLELEHFGVPFSRTKEGKIYQRAFGGQSLEYGKGGQAYRCAAVADRTGHSILHTLYGQSLKHNTNFFIEYFAMDLIMEGGECRGVIAMNLEDGSIHRFRAHKTILATGGYGRAYFSCTSAHTCTGDGNAMVSRAGLPLQDLEFVQFHPTGIYGAGCLITEGCRGEGGYLLNSKGERFMERYAPTAKDLASRDVVSRAMTVEIREGRGVGPEKDHCYLQLSHLPAEILKERLPGISETAAIFAGVDVTKEPIPVLPTVHYNMGGIPTRFTGEVLTIDENGKDKIVPGLYAAGEAACVSVHGGNRLGANSLLDIVVFGRACALHIKDTLEPNTPHKPLAADAGLDSLKFLDQIRTSQGPKHTSEIRLDMQKTMQRDVSVFRMEETLQEGVKNIARVDGTYKDIGIRDRGLIWNTDLVEALELRNLLTCAVQTANAALNRKESRGAHAREDYPERDDKNWIKHTLTWQHKTGDPVTLKYRAVTRTTMDENEVKPVPPFKRVY Q9UTK0 NOB1_SCHPO BINDING 256; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8BW10"; BINDING 259; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8BW10"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8BW10"; BINDING 274; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8BW10" SPAC1486.09; CHAIN 1..388; /note="20S-pre-rRNA D-site endonuclease nob1"; /id="PRO_0000374003" MSKSITHLVLDTGGIICSSTLLRNSAESFYTIPRVIAEIRDETSRKNFELWGDQVIQRVPKPEFIKKVSEFAKQTGDYSSLSVTDIQILALTYELEVEFNGGDWRLRKYPGQKHINGKPPSNSNSTEDASKPTSSDTASVKETENSDPKSAENEVLEGETTQHSNNKEAHPNTEENKEQEDNEEDDEDDGWITPSNIRKKKAEDGVGESLVQPKHLKVACATTDFSMQNVLLQIGLNLVSSDGFKIQNVKRFVLRCHGCYTVVKDMEKKFCPSCGGNTLIKTTCSINSKGEFQVHLKKNFEWKTRGTKYSLPKPVHGTSNGKGKKNPVLREDQPEYQRAVRRMQRKKEIDLMDEDYLPSLLTGVTKDRMYVQIGAGRKNPNEVRRKKR Q9UTK9 YIVH_SCHPO ACT_SITE 142; /evidence="ECO:0000255" BINDING 59..67; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 116; /ligand="beta-D-fructose 6-phosphate"; /ligand_id="ChEBI:CHEBI:57634"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 144; /ligand="beta-D-fructose 6-phosphate"; /ligand_id="ChEBI:CHEBI:57634"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 181..186; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 207; /ligand="beta-D-fructose 6-phosphate"; /ligand_id="ChEBI:CHEBI:57634"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 359..362; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07953"; BINDING 404..408; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07953"; BINDING 408; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:P07953" CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, ChEBI:CHEBI:456216; EC=2.7.1.105; MOD_RES 25; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC144.17c; CHAIN 1..449; /note="Putative 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase C144.17c"; /id="PRO_0000318493" MSRRNSIAVEQAINPNMLRAANRSSEALLDNEKFGGVQPYSTESGMLFHAGKLVIIMSGLPARGKSNIAVSIDRYLRWLGFNCRFYSLAKYIDERTREMTSSPVKSAASENHVFSRNDTIERCLADLEIFLLKEKGQVAIYDATNGTRRTRRILYDRFKNCGFKILFIESLCNKEDVINANIQEAIHVSEEFRNWDLEMAEKEYCRRIDILKCHYETIDEKDYSFVKMINFAETIIANKSNEGYLLSRILFLLMNMTLARKRIFLVPKASMRPLKLREPEDDIENRQFSEYVADRIRKSFPDVSFKNLHVLSCMEDSVMSPFRELGSVTSSMSSLSPILMDSFGDDLQKLKETYGEEEYNLYLVDPYRYRVKRKESFYDLAVRLEPLILELGREQRDVLLIGSKSIIRVFYGYYMNVPAKDIPQLCLSSSSIYELIESSTGMTVNEYDL Q9UTL2 KLP8_SCHPO BINDING 107..114; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" MOD_RES 278; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 279; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 284; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 456; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC144.14; CHAIN 1..511; /note="Kinesin-like protein 8"; /id="PRO_0000125390" MSTANVRVIVRVRPKSLRELSKSAEDLLSVDSHNKTVTITPPKHGLKHSRHKNRVNGPRTFAFDECFAPSAPESKNLSGQEDVYESTGPLLVKSILEGFNSCFITYGQKGTGKTYSVVGLRGQPGIIPHISESIFEEIDKLKKKSPNTTITVSISLAEIIEETPYDLLQPNVNSSHTPGETVFVQKDSLTGYHLHGLSEFEVGSAQEIDAFLRLAAKNIRTELSDISGVRKGHSVFSLVVQQRIIDPKTRHSLKKASRLQIIDLASFSKGSQRNESISSFESSSNNKSLSVLNRVIAALTSKKNDVLIPYKDSVLTTLLQDALGGNCRTIMLTCVSPCDFDDTFSALRYSEAARRIKNISNINCKEAYSTNNEGELDDILTTLESDREQLRRHEEHSQKLLKFIEEIRNDYEERIHALESQNSALKAHLRLAVDAYLNPLEFNFDDKNVKLKEFGSPNIAYKQELNSFQGELSSLFKDLKLVKSQLHDYPKPEVSDIDMDMESLRHDSLLD Q9UTM0 IEC1_SCHPO SPAC144.02; CHAIN 1..249; /note="INO80 complex subunit 1"; /id="PRO_0000046868" MSISSDTSGSVPGSPIDLEPESETICHWQSCEQDLLTLDNLVHHIHNGTTSNLRLISNINSILDHIGNRRPKYTCEWDDCPRKGMVQTSRFALVAHLRSHTGEKPFICSVPECDRSFTRSDALAKHMRTVHEADTLRPSDPIPKAHPMHPQNVANAMVQSAREARAQQQMHGVGNTNEDVENWLDAASMPKTSHDMYRLQKRKLQWVKEERTMLANHLEALERKLIDARNRKEKILNEIVKQVDPSISR Q9UTM7 HAT1_SCHPO ACT_SITE 238; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q12341" BINDING 203..205; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q12341"; BINDING 210..216; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q12341" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q12341}; SPAC139.06; CHAIN 1..378; /note="Histone acetyltransferase type B catalytic subunit"; /id="PRO_0000116791" MSAVDEWVHNANECIEIVQVNEKHEKDCQYHPSNTYAIFGDAEVIYGYKDLNVTITYECPLMVPKLEISYSERLAPDSGVEPTDIEGTLNTYLKDRSIKVEGNSFDVHSANSIHNYSFNGKTFKILQATVLEASEIMQHLQIFSLFFIEGGSFIDLNDPRWMVYLLYETTEDDYCLRGYCTVYKYYKWDKLIHDGIRARISQFVILPPFQHQGHGSQLYNAIVSTFLKNPKILDFTVEDASEAFDSLRDHCDYKRLLSMGIFSEPDFHPSLSRQWINSKIAETKLTQRQFSRCCELAFTTKLKKLSLLERKSVRLGIKERIFRQNLDVLLQLDKSERIEKIHNAYENQFDEYKQIVKKLPKLKEDSPRKRQKLAQSSS Q9UTM9 FAP2_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + L-saccharopine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + L-glutamate; Xref=Rhea:RHEA:28210, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29985, ChEBI:CHEBI:57951, ChEBI:CHEBI:58321; EC=1.5.3.18; Evidence={ECO:0000269|PubMed:16233628}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16233628}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.02 mM for L-saccharopine {ECO:0000269|PubMed:16233628}; Vmax=6.72 umol/min/mg enzyme for L-pipecolate {ECO:0000269|PubMed:16233628}; SIGNAL 1..18; /evidence="ECO:0000255" SPAC139.04c; CHAIN 19..433; /note="L-saccharopine oxidase"; /evidence="ECO:0000255"; /id="PRO_0000347275" CARBOHYD 24; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 119; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 188; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 229; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSRTIVIVGCGVFGLSTAVELAKNHSFDNIIAIDAEPVPSSMSAANDINKIVRPEYADLKYMKLALEAMEKWRNDPELSSVYFECGRLSTISKDPYRARFDEVAQRNLRKLLGDSALINLSSSEEIRKKYPSLFSNSPLRSDMQAVVNEHAGYANSAASLKLLELKARELGVEFVFGKAGKFKKFVVNHSETDIDKNDNHVSVQTEDGTIYHADTILLAVGAYLNAYLNTSHRVCAKGLPVAHIQLTDEEFKTYKNMPIIFDPDCAYAFPPYPVTKLIKLASTGYEYVCNVETDYDENSKVVSIPHSGPSKSSLPKYAIIQMRRFLDTFLPDLADRSLINTKMCWISDTEDANFLIDKVPQFDNVFVANGDSGHAFKFLPNIGRYIAQRILGDLSEEWKDAWRWREDDKASELKWRCVRSLIDYKDAEFTYDK Q9UTN1 OAC1_SCHPO CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in) + sulfate(out) = a dicarboxylate(out) + sulfate(in); Xref=Rhea:RHEA:76595, ChEBI:CHEBI:16189, ChEBI:CHEBI:28965; Evidence={ECO:0000250|UniProtKB:P32332}; CATALYTIC ACTIVITY: Reaction=(2S)-2-isopropylmalate(in) + sulfate(out) = (2S)-2-isopropylmalate(out) + sulfate(in); Xref=Rhea:RHEA:76343, ChEBI:CHEBI:1178, ChEBI:CHEBI:16189; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76344; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:76345; Evidence={ECO:0000250|UniProtKB:P32332}; CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate(in) + sulfate(out) = (2R,3S)-3-isopropylmalate(out) + sulfate(in); Xref=Rhea:RHEA:76347, ChEBI:CHEBI:16189, ChEBI:CHEBI:35121; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76348; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:76349; Evidence={ECO:0000250|UniProtKB:P32332}; CATALYTIC ACTIVITY: Reaction=malonate(in) + sulfate(out) = malonate(out) + sulfate(in); Xref=Rhea:RHEA:73195, ChEBI:CHEBI:15792, ChEBI:CHEBI:16189; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73196; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73197; Evidence={ECO:0000250|UniProtKB:P32332}; CATALYTIC ACTIVITY: Reaction=oxaloacetate(in) + sulfate(out) = oxaloacetate(out) + sulfate(in); Xref=Rhea:RHEA:76351, ChEBI:CHEBI:16189, ChEBI:CHEBI:16452; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76352; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:76353; Evidence={ECO:0000250|UniProtKB:P32332}; CATALYTIC ACTIVITY: Reaction=sulfate(out) + thiosulfate(in) = sulfate(in) + thiosulfate(out); Xref=Rhea:RHEA:73215, ChEBI:CHEBI:16189, ChEBI:CHEBI:33542; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73216; Evidence={ECO:0000250|UniProtKB:P32332}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73217; Evidence={ECO:0000250|UniProtKB:P32332}; SPAC139.02c; CHAIN 1..320; /note="Mitochondrial oxaloacetate transport protein"; /id="PRO_0000310788" MSEKQTIKALPAHNPTQVKKLGPVSGFLSGGLAACGAVTLTNPFEVIKTRFQLQGQLTKLDPSKRIYKSVGQAFSLIARHEGIRGLQRGLGTAYVYQICLNGCRLGFYEPIRRTLNTWFLDDPKGNKLAINVASGAGSGLCGALFGSPFFLVKTRMQSYSPKFPVGQQYGYKHIFNAFSRIIKENGVKGLFVGADAAILRTVSGSSVQLPIYNWAKRMIEHYNLLEEGMIKHLTASAVSGFGVCCTMQIFDTVMTRMYNQKNKELYKNPIDCILKTIRSEGFFALYKGFGAHLARIAPHTIFCLTFVEQTNKLFLKFQKD Q9UTN2 MKT1_SCHPO MOD_RES 227; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 228; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 230; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC139.01c; CHAIN 1..802; /note="Post-transcriptional regulator mkt1"; /id="PRO_0000154048" MTIRSLNLFIIDKKHQHKSSLSSFQNCKLGIDASFYLTQIIHSFTPQELQSLAVNGESEYLQHRISEFLEQLRTENITPIFVFNGIPLTFEASSQLEVPGKQKSHSALTDFEAFDPYDANIQRNMYRMDASGPANYGESKPTLLYTNQRDHLDRLCDQVKFYLDQCNVEYFVAPYLAMAQLAYFLNGTSSPYIDAIYGSTDLLLFGVKKFITSMNTSSNVKISSDPSSPSTQTTINSAAKSSFTWLDGNALLQDTNGLSWQQFIDSCLLCGTAISPTFPQIEGTFLIKSAMELVRMFGSAYRAVLHFAEIFPQPIFQDYLQQYKRAVCFSKFGIVMDTKGLTLPPVPTESVPNDINIYFGTRLPNEIYFYISRGLIPCKMIGALVSGCFSDPVSILEQHIGDKASQGTFSGANSGLNPGRDNAAAVAAVDQRRFVDDLEEIWSQGLNLLTQPLNRFYQARDIVSLHGHNQQASLKVMHSYDPPLYNDTRAWMIYEENLPSYLSSNFLKEEPVVLFDLLRALNDPVFVKKSFCTEGNIGIKNPPKHPLSSTAEIVLSSCYRFLQIRSFVLTSHQLTSWGCPLLKALENCHLQNQTSVVVLFELLRLRQLKEPSLLSSSSASIADLSITSATEFLAKVATFLPIKQRPEVSKISIVDENLLQFYQLQTSFGSNLKELMAMILASVILNRNVDKSKIDPKLIRKTLPFQNINGSLVSGFVVKRFFEIISKEQEASSQQENIQKAYEIIEKEFPTIGSAENHIAQFLEFWKTFMEGVKEAENTSAIGKLVLSKLFLTNQWIFSLGL Q9UTN9 ATL1_SCHPO SPAC1250.04c; STRAND 22..24; /evidence="ECO:0007829|PDB:3GX4"; STRAND 70..72; /evidence="ECO:0007829|PDB:4HDV"; STRAND 90..92; /evidence="ECO:0007829|PDB:4ENN"; STRAND 93..95; /evidence="ECO:0007829|PDB:3GX4" HELIX 3..14; /evidence="ECO:0007829|PDB:3GVA"; HELIX 25..31; /evidence="ECO:0007829|PDB:3GVA"; HELIX 35..37; /evidence="ECO:0007829|PDB:4ENN"; HELIX 38..46; /evidence="ECO:0007829|PDB:3GVA"; HELIX 56..58; /evidence="ECO:0007829|PDB:3GVA"; HELIX 73..84; /evidence="ECO:0007829|PDB:3GVA"; HELIX 101..104; /evidence="ECO:0007829|PDB:3GVA" TURN 62..64; /evidence="ECO:0007829|PDB:4ENJ" CHAIN 1..108; /note="Alkyltransferase-like protein 1"; /id="PRO_0000249237" MRMDEFYTKVYDAVCEIPYGKVSTYGEIARYVGMPSYARQVGQAMKHLHPETHVPWHRVINSRGTISKRDISAGEQRQKDRLEEEGVEIYQTSLGEYKLNLPEYMWKP Q9UTP3 FTA6_SCHPO SPAC11H11.05c; CHAIN 1..59; /note="Inner kinetochore subunit fta6"; /id="PRO_0000290641" MEDKYILLSAVETFKSRLEELLMQSAKVQKQTMLRKELASSMNDMASTVQEALNKKKSS Q9UTP9 DBP4_SCHPO BINDING 83..90; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; MOD_RES 500; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 503; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 504; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 545; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1093.05; CHAIN 1..735; /note="ATP-dependent RNA helicase dbp4"; /id="PRO_0000232203" MPKNRTGRSREAREKKRKEEEEEIEELNSQIEALSETVDHFAELPLTQPTKSALKNAHFITLTEIQKQCIPSALKGRDILGAAKTGSGKTLAFIVPLIENLYRKKWTSLDGLGALVISPTRELAIQTFETLVKIGRLHSFSAGLIIGGNNYKEEKERLSRMNILVCTPGRLLQHIDQAVNFDTSGLQMLILDEADRILDMGFRTTLDAIVSSLPVHRQTMLFSATQTKSVKDLARLSLQNPDFISVHENDTSSTPSNLNQFYLTVPLTEKLDILFGFIRTHLKFKTIVFLSSCKQVRFVYETFRRMRPGISLLHLHGKQKQTTRTEVTAKFTSSRHVVLFCTDIVARGLDFPAVDWVIQLDAPEDVDTYIHRVGRTARYNRSGNALLLLLPSEEAFLKRLESKKIAVERINVKDGKKTSIRNQLQNLCFKDNDIKYIGQKAFISYLRSIYLQKDKDVFQLDKLPVEAFADSLGLPGTPKITFGKLKNHSQSQKDYNSSTSLDSSEESEVDVENKQNVRTKYDRIFERKNQDVLAAHRQRLVEVNSDEDDGDFLQVKRVDHDLPEETGERFNANSKRKEKMASSKKAMLKYKKSADKVYFDDEGNAIPFYAMNTEDTFQKAGDPAALIASHLAEERKALEKADITDKETVRQKQLEKKRRRQELERITQQDATPDEYVPEGPIVAFVDDELPETSKKQKKWFEDNDERDHGGIVEVENLNSLEDQEALALKLMGAA Q9UTQ0 CCA1_SCHPO CATALYTIC ACTIVITY: Reaction=a tRNA precursor + 2 CTP = a tRNA with a 3' CC end + 2 diphosphate; Xref=Rhea:RHEA:60008, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:15488, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83069; Evidence={ECO:0000269|PubMed:30988468}; SPAC1093.04c; CHAIN 1..500; /note="tRNA nucleotidyltransferase cca1"; /id="PRO_0000139089" MASSSSILELNETEKELSDIFLNVSKKIGQMDRKEPEVRFAGGWVRDKLLRIESHDIDVAIDCMSGFEFAQHLQSYLAQQHPDWETKVIKIDANPLKSKHLETATARIMGMDIDIVNLRHHDYTNSNSSNKLVFGTPLEDALRRDATINALFYNLKSKTVEDFTGKGLVDLSNKIIRTPLVADETFGDDPLRAVRCIRFATKYDFNIHEETIKGLKNPELHERLRSSISRERIGVEVDKMLKHCNTNRALKIIHSLGMFACIFGPLEIHTKKLQSKNIESLSLIPYAIDLFGYLQKKDVSIKNLSSSSKYIFWLAIATLPWYNWSILEKSKIKILPPILIRDSLKYSKPIMSQVENFFVHYPLIMSKINVLEKEGKLTRLGCGRLVRELGPHWRDIIDWAFFMNTLISNSDIQRLNKDEEVTWFHVLVKHIEEYGMEEAYNIQPIINGNEITRILGIRPGPHLRKMLDDSIEWRIQNPESTKEDYIAIMLEKGTSAVVDS Q9UTQ7 ARP9_SCHPO SPAC1071.06; CHAIN 1..523; /note="SWI/SNF and RSC complexes subunit arp9"; /id="PRO_0000310305" MPSFRDDHIIVIQTGSLYHRATFGLAESLEPPTIRVRTRVGKNDNGEYVFTNKEDINMEDPNVKTDETKVETSESTSEQPSNSNVTEEKNMGSSFHSECKVDDFTPLPNEIQPIQRGRVVDWEALKAFWKHLYSLLLKDPNDTTFRYPVCLVIPTYWSLYDRELATQFFFEECQVPGFTIAYEPLMGLYAIGILHGLVIDIGYEKTDITPILDGQIIFTATQQLPLGGRYMTQHLQNLLRESLPTLKSSGQYVSKEDITELFAEQVKCSEIAQVVRDEQDTAKDPVKALTSTNNVEEEDPAEDIGKIIASGQTRAYLAQKEREKNGESEKDEKPDNTDVEFQTIAIEPLGDCIVGRERFKICEPIFHRPSNETVSLPEAIYITIKNYAANYKRRNDLWENIIVLGCGSRIRGFRECLIQQLQFKYQLSGSLEPYYAAQGTDSILGMTTMPPTPYPALINPCKILPDYFPSWKPDAGTNAMFEELAFLGGSIVAKTSFNESVSSHYVTLEEYAQHGPTAIHTKQ Q9UTR4 ETD1_SCHPO SPAC1006.08; CHAIN 1..391; /note="Septation protein etd1"; /id="PRO_0000087073" MGVVYGSQQNLSEYFYSSVNMAEVPDTFEENRGHSFEGVTLQRRHVKGMKSYGSDITPRRPKQLGLPKEVNTSECIDQGSWRKPSAFESLRSYSRKFSKRIFSFIGVESKSTVQRNASGADSTSLSHFTANEINKGNCKKTALSNEFNSANKGSKASGVGAELPSVNGFIEGELHDDNETDSFRINELAKQIQETSLGATTQEDESSDGICWDELSTTSPESSKVSEPIIQDNTQTTHINNDSSDIRFSSRCDLFADDADSDWEQDFNVKFDSPLIIPETVNSAGHTVREQLFEVKEFTRSIKDLKDLYEKANSKDIYDKDSEILGEAKAILRLADPANYSDLKDEDAQNILSKYKVKLEGDSSLDFDASMLPGLNDHVHYLMSQLQLLLH Q9UTT2 RSE1_SCHPO SPAPJ698.03c; CHAIN 1..1206; /note="Pre-mRNA-splicing factor prp12"; /id="PRO_0000218635" MDTFPSLFLYSLTIQNSNYVQSSCAASLSGKKAQEIVIATESRLLIYKVDATDGRMNCILNQNCFGIIRNVAPLRLTGFKRDYLVVTSDSGRITILEYNVEKNKLVPIYQETFGKSGIRRVVPGEYLAIDAKGRAAMIASVEKNKLVYVLNRDSEANLTISSPLEAHKANNICFHLIGLDTGYANPIFAALEVDYSEIDHDSTREAFTSSEKVLSYYELDLGLNHVVKRWSKVVDRNSYMLIPVPGGNDGPSGTLVISNGWISYRHLQKAFHQIPILRRQAASANAISTPWNQVNSNSANDGPLIVSAVLHKMKGSFFYLLQTGDGDLLKLTIEHDGQGNVVELRLKYFDTVPLAVQLNILKTGFLFVATEFGNHQLYQFENLGIDDDELEITSLDFQAQDNEVGTKNVHFGVRGLQNLSLVEEIPSLYSLTDTLLMKAPSSGEANQLYTVCGRGSNSSLRQLRRGLETTEIVASELPGAPIAIWTLKLNQTDVYDSYIILSFTNGTLVLSIGETVEEISDSGFLSSVSTLNARQMGRDSLVQIHPKGIRYIRANKQTSEWKLPQDVYVVQSAINDMQIVVALSNGELVYFEMSDDVEGGQLNEYQERKTLTANVTSLALGPVQEGSRRSNFMCLACDDATVRVLSLDLYTTLENLSVQALSSPANSLCIIPMNVNGVSTLYLHIGLMNGVYLRTVIDVTSGQLLDTRTRFLGPRAVKIYPITMKNQNTVLAVSSRTFLAYSYQQNLQLSPIAYSAIDHASSFASEQCPEGIVAIQKNTLKIFTVDSLQDDLKSDIYPLICTPRKIVKHPNFPVLYILQSERNFDSFKYAQENGDVGSSYTKEKQNEHTSKSWVSFISVFDMISKKIIHESPLGDNEAAFSMTAAFFKNRDEFFLVAGSATNMDLECRTCSHGNFRVYRFHDEGKKLELISHTEIDGIPMALTPFQGRMLAGVGRFLRIYDLGNKKMLRKGELSAVPLFITHITVQASRIVVADSQYSVRFVVYKPEDNHLLTFADDTIHRWTTTNVLVDYDTLAGGDKFGNIWLLRCPEHVSKLADEENSESKLIHEKPFLNSTPHKLDLMAHFFTNDIPTSLQKVQLVEGAREVLLWTGLLGTVGVFTPFINQEDVRFFQQLEFLLRKECPPLAGRDHLAYRSYYAPVKCVIDGDLCEMYYSLPHPVQEMIANELDRTIAEVSKKIEDFRVRSF Q9UU78 RLA5_SCHPO MOD_RES 99; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP1E11.09c; CHAIN 1..109; /note="Large ribosomal subunit protein P1C"; /id="PRO_0000157709" MSASELATSYAALILADEGIEITSDKLLSLTKAGNVEVEPIWATIFAKALEGKDLKELLLNIGSAGAASAPTAAGAGAAAPAEAAEEEKKEEAKEEEESDEDMGFGLFD Q9UU80 CWF18_SCHPO SPCP1E11.07c; CHAIN 1..142; /note="Pre-mRNA-splicing factor cwf18"; /id="PRO_0000079613" MSSLDEVAESRKQRLAELRKIKQLENKTRDSQEVQKNVIEHRNYDPEVQAPKMGFVEPPNMIESVEALSKEIEEKTKRKIEEQSSVPVEELDLVTLRPKKPTWDLERDLKERMRSLETQNQNAIAFYIQQLISERAHSTEKA Q9UU81 AP1G1_SCHPO SPCP1E11.06; CHAIN 1..865; /note="AP-1 complex subunit gamma-1"; /id="PRO_0000193762" MQTTHPKNLHLTCSGVERGFTNSPKTHPKMSSLKSFIKAVRASKTTAEEHTTILKESAQIRKNIRQGSNDMRMRRKNVAKLLYLFLLGEPTHFGQIECLKLLSSSRFMDKRLGYLAAMLLLDENQEVLTLLTNSLQNDLKSRDKFIVGLALSAFGNVAGPELARDLSNDIAELCSNHHNYISKKAVLCALRVIQKEPDLESLYIEKTDELLHSKSHGVLMAALAFAISACKINPSLISRFESQADDLIYRIRQLSTSTYSSEHNIGNISDPFLQVKILQFLSILGQNNPKIYDKMSDLLAQVCTNTDSSRNAGNAILYQAVRTILDLNSDSSLRVLGVNILAKFLGNRDNNTRYVALNMLKLVVNSEENAVQRHRSTILACLNDVDSSIQSRALELSTFLVNEANVRFMVRELLSFLDNVSDELRGSTAQYITEVTNAFAPNKRWHFDTLLRVFKSAGNFVSESTLSTFLRLIASAPELHEYAVVKLYAALKEDVSQEALTLSAFWVIGEYGQMLLSPTMNFDDDQTLPHSVSESDIVDIIEEVFNSVEASRYIIVQYGLFALTKLSARLGSSSTASRIDKIIYSYKRNKNTEVQQRSVEFHLILNDSKLSKTILEPTPAPLPPPRTTPYQNAEQKLKANKHVEKRVQESNELLDLIGLTTPSVAEPLETPVDEMTQSPQSSLSRAPSTSKKSHFEDILGLFASPAPSAQPVDSLASSFASLDFNASASQPSNNLSLLSSIPSTSKSYPPIVVFDKHDVTLTLVPSKEESTKTAVIEAKFKNKNPMTRVEKIHLEVAVPKSQKLKIQPLRTTSMEPGGETSQTLRVHGPSGSQVKLRLRISVVRQGGSNTLDQVDFGKLPSDLLQ Q9UU82 AREH2_SCHPO ACT_SITE 409; /evidence="ECO:0000250|UniProtKB:P35610" MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP1E11.05c; CHAIN 1..472; /note="Probable sterol O-acyltransferase 2"; /id="PRO_0000315968" CARBOHYD 161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 233; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 342; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIAATPAKSKPSDVNLEQTFKGVSETSKIDLRRSRAAYRPLELSPTPSIFARNYQRNAVDFTGFFVLFWVAVSIMIFMSFLENFELTGRPVVGTIFKYFQSNLLDLAKADLAMSSMFLLAFPFQKIFALGYLRWYGLGVYLYSILILLFLSHCVLRCCLSNWSWTHRAMFILHSMVILMKLHSYNVVNGWYSYCYHSLNKLQSKKTDLDDDERSSVEFYEHCLNHHGNTYPENLTIPNALDFLFMPSLCYQLYYPRTAHVRIHYLIECALGTFGCIFLLVIISDHFMVPVLAKAIRTIIEAPEDASATYFAIRLGHTVAFLMFPFMLSFLLVFWVIFEGVCNFSAEITRFADRNFYDDWWNCWTWDQFARTWNKPVHYFLLRHVYVPLNSFMSKSLSTFFTFFVSSVLHELVMGCITLKIRGYGLFFQMTQIPYIIIQRQKFVRRHRLLGNIAFWFSIIIGIALIAALYILF Q9UU83 PAL1_SCHPO MOD_RES 66; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 119; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 339; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 358; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 370; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP1E11.04c; CHAIN 1..425; /note="Protein pal1"; /id="PRO_0000116895" MMVIENPFLSTATSSQTPQEDGVYTSSLHNSNNPFLAPKTERVADPVMESMADDLFNSIQKKKEPSPASSASASPVKKSAEALAERSNSSMGTFDPPPRYSKIARARSTHVASSSRHRSPSHNDSSPSTQSSLKSRGSIRRYKSVREGSHRPGRSSKEPLDQIDRLDVTGLYGSGSFHHDGPFDACRPHRNRNSKKAPVAAFPKDSIANSIPKVGETYNDPSVPKDFSRKAIHESLRTKNILQSPYKSVGIEEEFPSSGNNDTPGLTDSTRIEGAMASKNAIARNEEMLAMEKAGLGRKNSLIRKLGLNRSASMMSRTPNTLNRPSNYRSHSSMGTRRSPLNSPSQLDPISNENESDTDDSNTGLRNRTSPTAAPPPPSRRKTGGLNTRPYPQHAESQMSLPLTAKERSKPKKMGFFRRLFHKKS Q9UU87 PPK34_SCHPO ACT_SITE 200; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 46..54; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 69; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPCC1919.01; CHAIN 1..354; /note="Serine/threonine-protein kinase ppk34"; /id="PRO_0000086075" MSLPLPSFLSSNNYNSSETSLLTEGPESDEEDEGPLLKQYRLKNMLGYGACSTVYLAVDVSTNIEYAIKEFKKTSLRRREKFRLMQLEKELGSFNDMDSSTIEDQIRNQEKKDPYYYIRKELDVLKVLDHENVVKLYQVINSDYKDSLCMVLNYCPGGKLASVDHGISFDPMPLETCRKSFRQLVLAVNYIHGKGVIHRDIKPDNILFKENNNLCVIDFGLAEFLPKDGFVKPASGTPAFMAPELFDNELKKIKGKPLDIWSMGVTLYVIAFAEFPFNGSTILDMINVIKGKSLMIPAYCNSDLRKLLERCLEKNPEKRITIEELLRDPFLTERGKHHLTSSSIVTAFSSIWEI Q9UU88 KAD6_SCHPO BINDING 18; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03173"; BINDING 20; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03173"; BINDING 21; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03173"; BINDING 22; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03173"; BINDING 23; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03173"; BINDING 114; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03173" CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03173}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_03173}; SPCC830.11c; CHAIN 1..175; /note="Adenylate kinase isoenzyme 6 homolog"; /id="PRO_0000363367" MGNEERELPNIIICGTPGTGKTTLAEQVAETTELENICIGDVVKENHLHFGFDEKWKTYDVDEDKVLDYLEPKLLKGGCIIDWHTCGLFSEELIDLVVVLRTDHSKLWERLESRGYSLEKIQENNEAEIMQICLEEARESFDPKIVVELPSESIEEMESNLSRITQWVTNWKKNH Q9UU91 YOP1_SCHPO SPCC830.08c; CHAIN 1..182; /note="Protein yop1"; /id="PRO_0000101856" MSFQVRVKQNMQDLDNRLAAFPQLNSLEKNFGVSKLYVFLTAAGIYALFLFLNWGGFLLTNLLAFAMPAFFSINAIETTNKADDTQWLTYYLVTSFLNVIEYWSQLILYYVPVYWLLKAIFLIWLALPKFNGATIIYRHLIRPYITPHVIRICKSVSRQNAAPAPTASSFAHTTATDIPPSI Q9UU93 CANB_SCHPO BINDING 34; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 36; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 38; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 40; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 45; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 66; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 68; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 72; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 77; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 103; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 105; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 107; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 109; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 114; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 144; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 146; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 148; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 150; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 155; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SPCC830.06; CHAIN 1..174; /note="Calcineurin subunit B"; /id="PRO_0000073496" MGQSQSQIFEDLISNSSFSNEEIERIRKRFIKIDANQSGSIDRNEFLSIPSVASNPLASRLFSVVDEDGGGDVDFQEFINSLSVFSVHGNKEEKLKFAFKIYDIDRDGYISNGELYLVLKMMVGTNLREDQLQQIVDKTIMEVDKDRDGKISFEEFKDIVSGSNVTSSMTLDSF Q9UUA6 DPP1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; SPBC409.18; CHAIN 1..279; /note="Probable diacylglycerol pyrophosphate phosphatase 1"; /id="PRO_0000358314" MEAVGKHVKLFWNVYSDYAVLIAISLSYFVFDVLMLPFTRQFSLEDITISHPFALHEQVPTKYLGIICVFFPALVLYGFGKLRNNSLLFWKSLMGLLYSTMVCGLCVSLLKNAVGRPRPDFLARCQPFESTPKTGLVDVLSCSVPWSDKVLQDGFRSFPSGHTSFSFAGLGFLAIFLAGQLKMFRNKTSSWKVVVPLVPLSIASWIGLSRSQDYRHHKEDIAVGALFGFAIAYVVYRQLFPPLDHHNADILYVQAELDEGYTNVHSAGNSSATNAEQMV Q9UUB5 MIS13_SCHPO SPBC409.09c; CHAIN 1..329; /note="Kinetochore protein mis13"; /id="PRO_0000290643" MKRKPEEQEGFVFVRKGKEKAGSKRRKSSVEDDPDTSQTDGLVELPVSDTPIVKRNKELRKGKGRRSSLDQRGKRASSIGTGFEALPHADVPSHEYYRHISKDLSEPLRIKQLLLWASSKALEEQRKKYGETEEASEAAIARSIVQEVLNELLANKVSVSWYQRPPDAVIPNKPHPQNLKNAQLVDELSAKLTQLHNEEAAWRAVAANSVSSDKSILSFKKAVESIDSKQDLDKQDSPLPPDDAPELPNISKLKPKFHTLLDMLAENIHTLHSLTNAGPEVRSSYGRLAAQDFIAHRKSLLSFSKYVDTMNLLRLLSEASYKSSSNESV Q9UUC7 CTU2_SCHPO SPBC19C2.13c; CHAIN 1..366; /note="Cytoplasmic tRNA 2-thiolation protein 2"; /id="PRO_0000359408" MQNTALDNSADSKCSKCDNKATVLTKSDAVCDSCFVRRIENKIRRQFELVRPNLQGRKSKRAMLAISGGISSMAMLETANYLSKYRDDNYRPMFDELLAVHFQWGTDSAVAKTIEESISKNYPKCPFKVIGEAELLNRTIATDSRGNIEINADNEKFNPEVISSLASRQDLLYRIRDKLLVSYARKANCDTIVFGDSGTTIAARVLELVAEGRGFAIPWYTSVCSKLPNCDTFLLRPLREVLSSDLKSYMNIKGLAFCDSLIEARPNTIHGVTESYFSSLNDTFPSLVSTVVKMSSKLHVPSTEAICTICNLPMQEDAETWLQKTTVEHPDSVEGIKNQNVCYGCSVSLKSLKGTLHIPDIEKEGI Q9UUE4 PPIL4_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; MOD_RES 206; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17G9.05; CHAIN 1..432; /note="Peptidyl-prolyl cis-trans isomerase cyp6"; /id="PRO_0000232980" MSVLIETTVGDLVIDLFVKEAPKTCENFLKLCKLKYYNFCPFYNIQHNYTCQTGDPLGPTGDGGRCVWNVLNKGTRFFKAEFNPSLVHNKMGLVSMSTATISSRDDKLLVCGSQFIITLSDNLEGLDERYPIYGQVAEGFDTLLKINDAICDEEGQPYRDIRIKHTIILDDPFEDPPDLVEPLRSPSPTPEQLATVRIGENEQIESETSEDKLQREKEMEAEAEAVTLEMIGDLPFAHVAPPENVLFVCKLNPVTQDEDLELIFSRFGKIISCQVIRDKETGDSLQYAFIEFDNKESVEKAYFKMQNVLIDDSRIHVDFSQSVARYRQYYNSNRDRKRSSSRSDDREYHRRSDGRYDRSNYRDDYRHRRKERDHRDDQSSFRNERFSNYYGDDRSYHKRRNTGNKNCDDHLRDKSPERRYRYDRRYRDDRYR Q9UUF0 PEX10_SCHPO BINDING 256; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 259; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 273; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 276; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 279; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 290; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:G2Q0E2"; BINDING 293; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:G2Q0E2" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q05568}; SPBC17A3.10; CHAIN 1..306; /note="Peroxisome biogenesis factor 10"; /id="PRO_0000056380" MHLSAHIDPLQIILCTEIDEACIQFIKSQIEGIARACGPRMQANFEGVLIPYVDVLGKFLYRACCLRYATMGEEAARIVLAKQDRSKGLVLATTGERMTSLIFSLVIDLVGVHVNKLLKQASYSSSFKLPFGLRNLLPEAVISKEKHLVYILNSFKPILLKLVSIIRFLCLTMKGHCATVSQLLLGLKYISLDEINPEEKKKVLTLLLLLGSRLIASILQHSNSYFDQHTISSITDERDLEDKNKLPFIPEGNRKCSLCMEFIHCPAATECGHIFCWSCINGWTSKKSECPLCRAFSSPSKIILLR Q9UUG1 RPF2_SCHPO MOD_RES 293; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 300; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 313; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 316; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC926.08c; CHAIN 1..317; /note="Ribosome production factor 2 homolog"; /id="PRO_0000120229" MLRQVKPKNARTKRALEKREPKLVEGAKTAIFLRGNATSQISLDVLGDIHALKKPFSVNFQKKNNILPFEDASSLEFFSEKNDAALAVMATHNKKRPHNLTWVRFFNYRVLDMIELGIVNYKSIQSFSATPIVPGTKPMILFQGPVFDAHPTYRHIKSLFLDFFRGEPIQKLDSAGLSYVIVVSAAEAQEDETKPLPLVHFRVYGTKLLKTKTNLPRVELEEMGPRIDFNIRRVQPAESDVLEEALKKPKTQEPKPKKNVDVDIIGNKVGRIHVDQQDLGNLQTRKMKGLKRSVEEREDSENEEVEIEEDVISDASE Q9UUG8 TUP12_SCHPO SPAC630.14c; CHAIN 1..598; /note="Transcriptional repressor tup12"; /id="PRO_0000051311" MLFLVISQTTSFMITVRQFTFTIFKFQFMATSNVSSRVNELLEAVKKEFEDICQKTKTVEAQKDDFEYKAMISAQINEMALMKQTVMDLEMQQSKVKDRYEEEITSLKAQLEARRKEIASGVVPQSSKTKHGRNSVSFGKYGNAGPFNSDNSSKPLILNNGSSGGTPKNLRSPAIDSDGTVLAPIQTSNVDLGSQYYSSPHVRPAVGATMAGSAMRTFPSNLPLGHPPPPSDSANSSVTPIAAPLVVNGKVSGNPPYPAEIIPTSNVPNREEKDWTVTSNVPNKEPPISVQLLHTLEHTSVICYVRFSADGKFLATGCNRAAMVFNVETGKLITLLQEESSKREGDLYVRSVAFSPDGKYLATGVEDQQIRIWDIAQKRVYRLLTGHEQEIYSLDFSKDGKTLVSGSGDRTVCLWDVEAGEQKLILHTDDGVTTVMFSPDGQFIAAGSLDKVIRIWTSSGTLVEQLHGHEESVYSVAFSPDGKYLVSGSLDNTIKLWELQCVSNVAPSMYKEGGICKQTFTGHKDFILSVTVSPDGKWIISGSKDRTIQFWSPDSPHSQLTLQGHNNSVISVAVSPNGHCFATGSGDLRARIWSYEDL Q9UUH4 ERG25_SCHPO CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4beta-methylzymosterol-4alpha-carboxylate + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:55244, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18364, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:64925; Evidence={ECO:0000250|UniProtKB:P53045}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55245; Evidence={ECO:0000250|UniProtKB:P53045}; CATALYTIC ACTIVITY: Reaction=4alpha-methylzymosterol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxyzymosterol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:47056, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:1949, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:143575; Evidence={ECO:0000250|UniProtKB:P53045}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47057; Evidence={ECO:0000250|UniProtKB:P53045}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045}; SPAC630.08c; CHAIN 1..300; /note="C-4 methylsterol oxidase erg25"; /id="PRO_0000117038" MNTTSEVIVGTGFQAIRQQLAQMHPELNFVEQLWLAYYKWFDNDVVATGLMSFLLHELIYFGRCIPWMIIDAMPYFRRWKIQPKKVPTLAEQWECTRLVLLSHFTVELPQIWLFDPMCATFGLSTSVPFPPVTKMIWQITLFFFLEDTWHYWAHRLFHYGIFYRFIHKVHHRYSAPFGLSAEYAHPLEIILLGAGTVFVPLMWCYFTHDLHLVTMYIWITLRLFQAVDSHAGYDFPWSLNKFLPIWAGADHHDYHHMAFKDNFSSSFRWWDAVLKTDQNYHQFKARRLAAKYEAESKKAK Q9UUI2 SHF1_SCHPO SPAC22F8.12c; CHAIN 1..165; /note="Small histone ubiquitination factor 1"; /id="PRO_0000304068" MSSRRNDYHYDGNDHQYRSPLKSNVDQNSFYESSYRSRQSYHQRTKTPRSSYDSPSSSTNSKEHNSPYHYRVPSNNSTRASFGAASTDTNVELPKINLPDSSLSSKLQSCKSACENSSQSLLNVEQQYAQQVHFWEKIRTDIYREGLRSDAAVKSLNDFVNNVSF Q9UUI3 SA145_SCHPO MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22F8.10c; CHAIN 1..601; /note="Pre-mRNA-splicing factor sap145"; /id="PRO_0000343537" MYLLTRPKHCCLDFLLMAEIQTAQNPLKELEKILERNNKQKNKKSRNQVRREKKKLLREKTNSGAKLAEKNSDDKDQLTENNDNLYNDKKSNGNFYDTNKTDSVDGMVYTTIVDSVELDPNDPLIEQFKDVFNRFKADGQEKDFEDTDKGQIMYSDDEILSEGEEDALQKQQEEKLSKKKLRKLKRMTVAQLKMLSEKADVVEWWDVSSLDPLFLTHLKAYPNTVPVPRHWNQKRDYLSGQRGIERQLFELPSYIRATGIVQMRNAVHENEADMPLRQKMRERVQPKMGKLDIDYQKLHDAFFRYQTKPVLTGFGECYFEGKELEADVKEKRPGDISEELREALGIAPGAPPPWLFAMQRYGPPPSYPDLKIPGVNCPIPTGAQWGFHPGGWGKPPVDQFNRPLYGDVFGNVKPRIHAGTGSPVSTQHWGELEEFEEEESSEEEESEDVEYPTEEITERETIEEYQSASEPRSQREDLHAEPLTYFNQSNVEVDNVELRKNTQPSSDAANRDLYQVLPEKSTNISGFMGPQHQYDIPTAEDTLPQKRNAHSMLSSTNKGDVALNQSSNWQDELSELVSEQAMKVGAAKRQKTQSKRDKFRL Q9UUI5 SEC24_SCHPO BINDING 256; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 259; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 278; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 281; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" SPAC22F8.08; CHAIN 1..926; /note="Protein transport protein sec24"; /id="PRO_0000205162" MSQEDAFYGKGSYGASSGNSNIPPQGFQPVYPVAGQLDNTAPYVGAVAEGTAEGIVSNGEYAVGAMGAAPTNIIGSVDQQPPVSHTSHKSRRQYPAEVFELTNTLAASPAPPSLSEPSYVMARTPSSSPYPHDRAEVGTKSLSAQFGGMSLGADGAAAMPTNELVSVDLYNQTPEISDLTSPPPPINLPLSYSATGAATSNCPPKYVRSTINCVPTTNSLLKKSKIPFALVIRPYTSLVEEDDPVPVVTDTIISRCRRCRMYINPFSIFIDNGHRYRCNSCGIVNEVPQSYDWDSFRNVQRDRWQRPELNYAVVDFIAPQEYMVRAPQPLVYVFLIDISFVSISSGMVGTASRAILESLDRIPNKEGRAKVAFIGVDSALHFFSVSPGAEEATQLVVSDLEEPFLPRNQDLLLNLRECRQGIENLLERFQSMFATTRDSSNALGPGLKAAHRLIENIGGKICCLISSLPNVGVGKLELREDPKLLGTNRESSLLHPNDSFYKSFAVECSTSQVSVDMFLFSSQYQDVATLSCLPRYTSGKTQFYHRWNASRSEDALKFASELTNYLSMEIELEAVMRVRGSNGLRMSSFYGNFFNRSSDLCAFPSFPRDQSYVVEVVIEDTITKPFVSFQTAMLHTTCNGERRIRVLTISLPTTNSMTDLYASADQVAIAQYLTVRASEKALSSTLNEARDSIISKLVEILEVYKKNLAGQNTGAAIPLQISTNLRLLPLLCLALTKHTGFRRSSHISSDLRSIALCYLSTLPTPLLMRYIYPTLYSLHDMPIEAGTVTEQGVVLPSALNLTSALLQSFGLYLVDTHIHQFLYIGKDAVPQLLIDAFGVNSLADLKAGRFTMPVIDNPLNVRINAILGKLRSLDKGSTIMPSLYLVRGDGDPQLRSWFFSHFVEDRSENSPSYLQFLQTLKEKVRD Q9UUI6 RTF_SCHPO SPAC22F8.07c; CHAIN 1..466; /note="Replication termination factor 1"; /id="PRO_0000372310" MQGKNNLSCRPDTEDNEELFVDDQLLSPIGDSKNTSSFIYLGNPISFHEYNYDETMVSPENVKTAIAGSAKDHETCRGFKKTGTTSYKDFVFSRDYTNWTPTFWVLLSQLIDEFLKESELNFVAARDLLIKTKRLPKPFNNLLIQFQIQVPNVSRRTVYRHLKGYFNIPGYERFQYVKKASSGSWGANDIITLEKEIAMFKKKKNWSDEQFLQYVWSDNHRDEMKTLYNCLYELIDRDKKSIYNYLRRKYNPFKKKCKWTIEDEAELKKLVEKHGTSWSLIGKLSNRLPMHCRDHWRDYIQPGEINRSPWTIQEKEKLIKTVNQYLQSNPSSPIQWSLISKNMRNRHRHHCRWKYYTLISRDIHNSSPFKLGDSIWLIERMMDLNVAEERMIDWKCLSEYANHLWTADACKSHFERIKKTLFIDGLSTFSDTLIHLHKMLNSSPEETYISNLHDSYTAFSNADDLC Q9UUJ6 NED1_SCHPO MOD_RES 99; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 103; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 106; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 107; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 321; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 587; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1952.13; CHAIN 1..656; /note="Nuclear elongation and deformation protein 1"; /id="PRO_0000209886" MQYVGRAFDSVTKTWNAINPSTLSGAIDVIVVEQEDKTLACSPFHVRFGKFSLLLPSDKKVEFSVNGQLTGFNMKLGDGGEAFFVFATENAVPRELQTSPIVSPTTSPKQTPSINVTEPQDLELDKVSQDHEKDQSNTYLMEDGYEFPLTRDLIRRSKSDADQTPPTGFKHLRHSSCLEMAGSDRTPSMPATTLADLRLLQKAKELGKRLSGKELPTRVGDNGDVMLDMTGYKSSAANINIAELARETFKDEFPMIEKLLREDEEGNLWFHASEDAKKFAEVYGHSPPASPSRTPASPKSDSALMDEDSDLSRRHSLSEQSLSPVSESYPQYAKTLRLTSDQLRSLNLKPGKNELSFGVNGGKAICTANLFFWKHNDPVVISDIDGTITKSDALGHMFTLIGKDWTHAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVILSPDRTMAALHREVILRKPEVFKMACLRDLCNIFALPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIELLQRSGHRSSYVYMNELVDHFFPPIEVSTRDEVSSFTDVNFWRSPLLELSDEEEDDTNKSTSKSPKTPKNTKFGYQEFEGIDEEDAQDYSPSPLIKSFNELMFEGEEDEEGEEDVENAV Q9UUL2 RAD57_SCHPO BINDING 100..107; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC20H4.07; CHAIN 1..354; /note="DNA repair protein rhp57"; /id="PRO_0000122957" MDISNYVDNFYFDEKIASAFELGEVSTVDLLTLDITELERRTHCSQSELLQLIEQISLLLQPVRCSASKVTSKYLTTGDVKLDETLHGGIPVGQLTEICGESGSGKSQFCMQLCLMVQLPLSLGGMNKAAVFISTESGLETKRLFELARYLPERYPKADKKDIIIKNPGDRVYTILCPDLESQEHIIQYQLPILFNRDKIGLVILDSVASNYRAELRYNRSKSHFRDLDNIAKRGNQLGKLAMTLRTLAHQHEAAVVIANQVSDRIPRDYDAIGLFSLDYQSQWFSGWDDTDPNPKIPSLGLVWTNNISTRLALIKKTDSATNNSGRIFRVVYSPNSPRLDVRICIGSVGIYSC Q9Y703 TBCA_SCHPO SPAC8E11.07c; CHAIN 1..119; /note="Tubulin-specific chaperone A"; /id="PRO_0000080044" MSNTVRSLVIKTNVVKRIIKDVELAHIDINEAEKRVQSKIDNGEDSAEIEHQKFVLKKHLEALPDALVRLRNATNDLESISSDSAYEGTPELEQANEYLEKAKEVIEKEQTNFPTNGYH Q9Y7I4 ALG3_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a di-trans,poly-cis-dolichyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + H(+); Xref=Rhea:RHEA:29527, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, Rhea:RHEA-COMP:19516, Rhea:RHEA-COMP:19517, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515, ChEBI:CHEBI:132516; EC=2.4.1.258; Evidence={ECO:0000250|UniProtKB:P38179}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29528; Evidence={ECO:0000250|UniProtKB:P38179}; SPAC7D4.06c; CHAIN 1..406; /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase"; /id="PRO_0000327764" MSSVETRNSFNPFRVLFDLGSYGWLHPSRLLLLEIPFVFAIISKVPYTEIDWIAYMEQVNSFLLGERDYKSLVGCTGPLVYPGGHVFLYTLLYYLTDGGTNIVRAQYIFAFVYWITTAIVGYLFKIVRAPFYIYVLLILSKRLHSIFILRLFNDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMSSLLYVPAYLVLLLQILGPKKTWMHIFVIIIVQILFSIPFLAYFWSYWTQAFDFGRAFDYKWTVNWRFIPRSIFESTSFSTSILFLHVALLVAFTCKHWNKLSRATPFAMVNSMLTLKPLPKLQLATPNFIFTALATSNLIGILCARSLHYQFYAWFAWYSPYLCYQASFPAPIVIGLWMLQEYAWNVFPSTKLSSLIAVCVPLITILKLYTSDYRKP Q9Y7J0 NPY1_SCHPO BINDING 182; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 185; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 200; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 211; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 222; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 258..260; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 258; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 274; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 274; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 274; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 278; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 278; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 278; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 321; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 321; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000250|UniProtKB:Q9DCN1"; BINDING 321; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9DCN1" CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876, Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029, ChEBI:CHEBI:144051; Evidence={ECO:0000250|UniProtKB:Q9DCN1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877; Evidence={ECO:0000250|UniProtKB:Q9DCN1}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence={ECO:0000250|UniProtKB:Q94A82}; CATALYTIC ACTIVITY: Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence={ECO:0000250|UniProtKB:Q94A82}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9DCN1}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9DCN1}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9DCN1}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9DCN1}; SPBC1778.03c; CHAIN 1..376; /note="NAD-capped RNA hydrolase"; /id="PRO_0000056960" MQGFKIARHFELPTAPSQFFAGSSLNRLSFLRSNREFLNKAFYDHTTRFLPFCDLNPALLVKDDKLVTLSYPQISKYFTFSPFEHTDKQIAERFSKGESLPVLVYMGNEERNGPTDNWSQHNVFAIDITGIDELQQSIRDNGGTFVNLRSIFTEQYQLSASDSGACAFARSILDWISRYRFCPGCGKRNIPTMGGTKLVCSDVLLNDDSNCPSKKGINNYQYPRTDPCVIMVILSHDMQHILLGRALRHPKGLYACLAGFLEPGESLEEAVVRETYEESGVDVEKVLYYASQPWPFPQSLMLACFGIARKNAKIQRDKDLELEDVRFFSREEVLRSLEWDAKDGPAPILFPPKLSIARNLIQAFAYDDWTNSQVKM Q9Y7J1 SPO6_SCHPO BINDING 428; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"; BINDING 431; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"; BINDING 441; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"; BINDING 447; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00600" SPBC1778.04; CHAIN 1..474; /note="Sporulation-specific protein 6"; /id="PRO_0000072139" MDFYSVKSQPFVRSPLVDQNPSIQNINEEVKRDIQNPLSYKTETSDKELCQTAACATSCSDWYPQQQTHMPHQNAFDSAKATAKMALPPTAFSNYCVKPSLTRNKDIPRTSIRVSKLRYWQRDYRLAFPNFIFYFDNVDEEIKRRVTQKINNLGAKVATLFTFEVTHFITTRTTDPEMCQPNDVLYLSKTANMKIWLLDKLLNRILFTLLNSDSLVNTSASCLQSLLDGEKVYGTSDKDFYVPSKNVEYFREYFLCIRDLSQYYKPIAVREWEKTLDSGEILWPSLAITAQGRCPFNTGRRRELKITKHNHPAHEIRKQLLSCTNQTNQNNVVKNSASVLVRQIMGDYNITESAVDGAKQMPTEFPKPENLLPVEKRAAMSPLNLLEPRLINKQNTLANQSPRQPPNAFDADPLAHKKVKIETKSGYCENCCERYKDLERHLGGKHHRRFAEKDENFQGLDDLFLLIRRPIRTN Q9Y7L0 SEC22_SCHPO SPBC2A9.08c; CHAIN 1..215; /note="Protein transport protein sec22"; /id="PRO_0000206767" MVKSTTVTRLDGLPLAASVDDESTERNLESHKKQAKLILKRLSPTSEKRASIESGDYTFHYLIDNGICYLCICEQSYPRKLAFSYLEELAGEFWNSFGEEALQPGLRPYAFVQFDTFMQKSKRVYNTPRANDNLDKLNTELKDVTRVMTKNIEDLLYRGDSLEKMADLSSDLRYSSAKYKKAARRVNLEALWRQYGPVSIIALLFLIFVYWRFFA Q9Y7L4 EXO5_SCHPO BINDING 86; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 386; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 389; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 395; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; SPBC685.02; CHAIN 1..409; /note="Probable exonuclease V, mitochondrial"; /id="PRO_0000116758" MEEYEDFEMEDLSELVSYMDYLETQRLTISQLDYSLSIPPQLLVSREISKLEDEVCEMLKESSLFQLFRKHKGYLNVTDLVLPLWCEVQHEYYLLRRIKKKTPKMERGIKLHQILEYETSPPSERRVLDRTSKEEPWALRLLRQLEGIMLLQKNGITREFPIWGYYKESSIFGIIDEISLNNPSKSNFNSDIRNYFNFKMYDLSFVDNKTRFSSRKPGASQILSSKVQLMYYVHLFLNYFPSLGEKQQSIFRDISPTYSNRLHSQSHWWNMFLSQLSLDGTKDLGPKFLEQSILSIPDIPEDVFAGHNSLNGLYALVFASAKKLHLRLTDDNLTIAYRNDKTGEVVYKDKFSFSNKLLEASYTKAYQFWHNLREPEGVPAEEVYKCRSCEFQKECWWLKKKQYYPLSSP Q9Y7N2 MED19_SCHPO SPCC1450.05c; STRAND 40..42; /evidence="ECO:0007829|PDB:5N9J"; STRAND 53..55; /evidence="ECO:0007829|PDB:5N9J"; STRAND 62..64; /evidence="ECO:0007829|PDB:5N9J" HELIX 26..29; /evidence="ECO:0007829|PDB:5N9J"; HELIX 33..39; /evidence="ECO:0007829|PDB:5N9J"; HELIX 56..59; /evidence="ECO:0007829|PDB:5N9J"; HELIX 73..79; /evidence="ECO:0007829|PDB:5N9J"; HELIX 90..97; /evidence="ECO:0007829|PDB:5N9J"; HELIX 109..112; /evidence="ECO:0007829|PDB:5N9J" TURN 8..11; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..138; /note="Mediator of RNA polymerase II transcription subunit 19"; /id="PRO_0000096369" MAQAPEYHYVGSVDYQPTRPSAHQNLIELYGLTELAKKVGRVDEFGNKRKMRRSYKAYIQDLPGYNEILRDNTIKQWLTNPIREEVPIDIEFLHHVFSVEPGIIPGFNPKVFGLEDDVVMGNVSRDSSQPRSPSRRKK Q9Y7N3 GLRX3_SCHPO BINDING 76; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250" SPCC1450.06c; CHAIN 1..166; /note="Monothiol glutaredoxin-3"; /id="PRO_0000102251" MANRKIFLITSLIISLLLIHIFIFSPLNEPEKNAKAGPLGLSDVSVPSAPKLPAKDSTDFEVFLENPVIIFSRPGCPYSAAAKKLLTETLRLDPPAVVVEVTDYEHTQELRDWLSSISDISTMPNIFVGGHSIGGSDSVRALYQEEKLQSTLDEWTHNKVLILPTD Q9Y7N4 OXDA_SCHPO BINDING 15; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:A0A499UB99"; BINDING 18; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 40; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 52; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 56; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 58; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 232; /ligand="(R)-lactate"; /ligand_id="ChEBI:CHEBI:16004"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 232; /ligand="anthranilate"; /ligand_id="ChEBI:CHEBI:16567"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 295; /ligand="(R)-lactate"; /ligand_id="ChEBI:CHEBI:16004"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 295; /ligand="anthranilate"; /ligand_id="ChEBI:CHEBI:16567"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 295; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 323; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 326; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 327; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324"; BINDING 328; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P80324" CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:22986818, ECO:0000269|PubMed:23085840}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000269|PubMed:22986818, ECO:0000269|PubMed:23085840}; CATALYTIC ACTIVITY: Reaction=D-serine + H2O + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:22986818}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; Evidence={ECO:0000269|PubMed:22986818}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000269|PubMed:22986818, ECO:0000269|PubMed:23085840}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000269|PubMed:22986818, ECO:0000269|PubMed:23085840}; CATALYTIC ACTIVITY: Reaction=D-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:22986818}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78220; Evidence={ECO:0000269|PubMed:22986818}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q99042}; SPCC1450.07c; CHAIN 1..348; /note="D-amino-acid oxidase"; /id="PRO_0000315956" MTKENKPRDIVIVGAGVIGLTTAWILSDLGLAPRIKVIAKYTPEDRSVEYTSPWAGANFCSISATDDNALRWDKITYHRFAYLAKTRPEAGIRFADLRELWEYEPKHDKIRSWNTYVRDFKVIPEKDLPGECIYGHKATTFLINAPHYLNYMYKLLIEAGVEFEKKELSHIKETVEETPEASVVFNCTGLWASKLGGVEDPDVYPTRGHVVLVKAPHVTETRILNGKNSDTYIIPRPLNGGVICGGFMQPGNWDREIHPEDTLDILKRTSALMPELFHGKGPEGAEIIQECVGFRPSRKGGARVELDVVPGTSVPLVHDYGASGTGYQAGYGMALDSVMLALPKIKLA Q9Y7P1 ERO12_SCHPO ACT_SITE 389; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q03103"; ACT_SITE 392; /evidence="ECO:0000250|UniProtKB:Q03103" BINDING 188; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 190; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 201; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 258; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 261; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103"; BINDING 290; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q03103" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q03103}; SIGNAL 1..22; /evidence="ECO:0000255" PTM: N-glycosylated. {ECO:0000269|PubMed:15449306}. SPCC1450.14c; CHAIN 23..567; /note="ERO1-like protein 2"; /id="PRO_0000008427" CARBOHYD 49; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 546; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 88..386; /evidence="ECO:0000250|UniProtKB:Q03103"; DISULFID 98..103; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:Q03103"; DISULFID 154..325; /evidence="ECO:0000250|UniProtKB:Q03103"; DISULFID 389..392; /note="Redox-active"; /evidence="ECO:0000250|UniProtKB:Q03103" MKIAKGLVGLLILYKNVCQVLCKSGSSVKSGSPWSIKNDGKSIIHDTLNSSYSDIENLNSRVSPLLFDLTEKSDYMRFYRLNLFNKECRYNLDDNVACGSSACNVLVTDEQDVPEVWSSKSLGKLEGFMPELSRQIVETDRSVMEHVDKISQSCLLERLDDEAHQYCYVDNELDSGCVYVSLLENPERFTGYSGPHSTRIWEMIYNQCLPDSSAPTIDFPALFMQGPLAPPPKPQEQLLKERMDAWTLEQRVFYRVLSGMHSSISTHLCHGYLNQRNGVWGPNLQCFQEKVLNYPERLENLYFAYALMQRAIDKLYGHLDSLTFCHDSVLQDSEVRQKIAGLVSLIHNSPKMFDETMLFAGDPSISTALKEDFREHFKTVSALMDCVGCERCRLWGKIQTNGFGTALKILFEVSNIEDEVTNFDSRSFSLRLRRSEIVALINTFDRLSRSINFVDDFKQIYSEQHKPASFKRRVLRRIKQLLFSVTPVALHPFLQKTSSILVDLYFDFKAEWDNVMLGFRYVFASYLRFPRLFKFVLFSQESPFLNWTSHHLQRYIPKNWFPEVASV Q9Y7P2 GPI11_SCHPO ACT_SITE 166; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 170; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 20; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 22; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 24; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 25; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 45; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 49; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 54; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 74; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 75; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:P0CR36"; BINDING 166; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 170; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 199; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" CATALYTIC ACTIVITY: Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH; Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349; EC=1.1.1.102; Evidence={ECO:0000250|UniProtKB:P38342}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22642; Evidence={ECO:0000250|UniProtKB:P38342}; SPCC1450.15; CHAIN 1..494; /note="PIGF/3-ketodihydrosphingosine reductase fusion protein"; /id="PRO_0000339877" MGFWGRNSFEADKKHILVTGGSQGLGKAIAKELVLRGANVTIVARTVTKLQEAVAELSDSKIHEDQQVSFESVDLTSYESVHSMIERLPFCPDHVVHCAGSCIPGFFTELDPSVFEKQMRQNYLASVYVCHAAIRRMKEISPSYSRRILLVGSLLSSLPIIGYSAYSPVKAAVRNLADSLRQECILYDIEVSVYLPSTILSPGYEQENTLKPELVLQMEGMDSVQTCEEAASHCMTGLDRGDFLIANESTGHLMKNHCRNSSPHDNPILEYLFALVSLLAWPFYRRKLDSLVYQYALEKGYRQPSSSRNSWIFTLLLTFTQLTIFYLSLNCLIENPYRMLRNTFPIWFIMQTLQIYIQSPRPPLTPKRLLAGAASMLIGSLLISFILVAFGAPLLHDFHLTYFCALTLSVFTVYPLASTLAFNTEQWQRFLTLKSFNVIGSMQLRSWGPIIGAWFGAFPIPLDWDRPWQAWPITIVIGAFLGYAFAAIVGEILQ Q9Y7T7 PRP28_SCHPO BINDING 293..300; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPCC63.11; CHAIN 1..662; /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp28"; /id="PRO_0000232377" MTAQDSIPSLEQLVQQKRVKEEKAARPKFLSKAERARLALERRQKEVEEAKAKQNDKLLDLRKRTFTNHLENNELADDEKKSQVSSVSSNNSGTESSATDEAFSMTIRQRYMGIKPPVVKKRRRNADKKFVFDWDATDDTMKDAETSASPEATIAVFGRGKLGGFDDQSIRKAKSNSGLIQRLLQGTEQDKARAHELIQLQEKRAKKIDWDDVPWREKPLEAMKPRDWRILKEDYNISIKGDDLPNPLRNWEEAGLPSEMLKVLKKVNYKEPSSIQRAAIPVLLQRKDLIGIAETGSGKTAAFIIPLIIAISKLPPLTESNMHLGPYAVVLAPTRELAQQIQVEGNKFAEPLGFRCVSVVGGHAFEEQSFQMSQGAHIVVATPGRLLDCLERRLFVLSQCTYVVMDEADRMLDMGFEDDVNKILSSLPSSNASEKDGSILATANSSSSRRQTIMFSATLPPRVANLAKSYLIEPVMLTIGNIGQAVDRVEQRVEMISDDSKKWRRVEEILESNRFSPPIIIFVNLKRNIEAIAKQLNAIGWHAVTLHGSKSQEQRERAIEQLRNKTADILVATDIAGRGIDIPNVSLVLNYNMAKSIEDYTHRIGRTGRAGKSGTAITFLGPEDTDVYYDLRVLLSRSAKAHIPDELRNHEAAFVRHAAITQ Q9Y7U9 CCA2_SCHPO CATALYTIC ACTIVITY: Reaction=a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate; Xref=Rhea:RHEA:60012, Rhea:RHEA-COMP:10468, Rhea:RHEA-COMP:15488, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83069, ChEBI:CHEBI:83071; Evidence={ECO:0000269|PubMed:30528393}; SPCC645.10; CHAIN 1..484; /note="tRNA nucleotidyltransferase cca2"; /id="PRO_0000316214" MYSRIVLNDVEKKVVNLLKKTADFIESKSSSSSSLEVRLAGGWVRDKLLGLSSDDLDVTLNKVTGVDFANSIFEYVHSLDSDSVIPYKDALGKLTVNPDQSKHLETATLSLFDLDIDFVGLRAESYDDKSRIPSVTPGTVETDALRRDFTVNTLFFNIRTEKIEDITKRGYKDLQTKVLVTPISPLQSFLEDPLRILRGIRFASRFEFTIDPSVVSAIQDPKVCKAFEKKVSKERVGEEIEKMLKGANAKLALQLLYSTNTYQFTFDTLPAEKEFQIPKALEATESLFQSLALTFPKLMKLSEDEKIGLWLYVALIPWSSQTVMVKKKQFYIPAIIAKDKLKLRSTYVNQLNQCCTFNPIFDELVNDTSTKNCSSIGSLIRQLNKSWEVVFLTSVIYSCCKTPAASVSNTFSSYKSLYDFIYDKNLQNAYNMKPLLDGKQIMKNVGVKPGPQLKETMDNMISWQFKHPEGSVEDCVAYLQSLKI Q9Y7X5 UGE1_SCHPO BINDING 8..39; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; Evidence={ECO:0000269|PubMed:19942659}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; SPBC365.14c; CHAIN 1..355; /note="UDP-glucose 4-epimerase uge1"; /id="PRO_0000318143" MTGVHEGTVLVTGGAGYIGSHTCVVLLEKGYDVVIVDNLCNSRVEAVHRIEKLTGKKVIFHQVDLLDEPALDKVFANQNISAVIHFAGLKAVGESVQVPLSYYKNNISGTINLIECMKKYNVRDFVFSSSATVYGDPTRPGGTIPIPESCPREGTSPYGRTKLFIENIIEDETKVNKSLNAALLRYFNPGGAHPSGELGEDPLGIPNNLLPYIAQVAVGRLDHLNVFGDDYPTSDGTPIRDYIHVCDLAEAHVAALDYLRQHFVSCRPWNLGSGTGSTVFQVLNAFSKAVGRDLPYKVTPRRAGDVVNLTANPTRANEELKWKTSRSIYEICVDTWRWQQKYPYGFDLTHTKTYK Q9Y7X8 ARP5_SCHPO SPBC365.10; CHAIN 1..721; /note="Actin-like protein arp5"; /id="PRO_0000310307" MKIYAVREPVFSGPTPSFQNVSNDIPLVIDNGSWQLRAGWGGEKDPKLVFDNLVSRYRDRKLSRTSTLVGNDTLIEVGSRSIARSPFERNVISNWDLMEQVLDYTFLKLGIDRMEHPICMTEPLANPTYVRSTMTELLFELYNAPSVAYGIDGLFSFYHNTKPSSSGIVLNLGNAASHVIPVLNGERILSEAKRISWGGSQSSSYLLKLFQIKYPSFPIKMLPSQAELLMHDHCHVSSDYTHDIAHALDRDILERDEIVLQFPYTEAAAQEKSQEELELIAERKRESGRRLQAQAAIKRKEKAAERDRELATLTELQQQSLVLSRRAFQRALEEAGFEDESQLNAQVKNVQAKIRRAQRDQQRQEESEGSLDVTEIDVEQAFPLLNVPDAELDEAGLRQKRHQRLMKANYDARVRAKAEKAIEEAAEAERAEADERLRLENFSTWVNEKRETHKILLEKISKNKRLKFELNDRKSHASQMRMKSLATLASEQPIQKRKRKDQSEDNFGARDEDWKVYHDVLTAEQLEEERKKLLDQIYSLEKQLLEYDSQFTQANTYDTLNDPRATLLYAFTRGVSDFDVNDVAQAFQLHLNVEQIRVPEVIFSPSIVGIDQAGILEIMRSILQRHSLEEQQKLVSNVLITGGLGSLPGMETRIKRELTSIMPVGSSINVFRASNPLLDAWKGASEWSVTEKFKAAKVTREEYLEKGPEYIKEHSLGNINS Q9Y7Y5 RT109_SCHPO ACT_SITE 219; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q07794" BINDING 117; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q07794"; BINDING 136..138; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q07794"; BINDING 146; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:Q07794" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:17369611, ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:20656950}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:17369611, ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:20656950}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:Q07794}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; Evidence={ECO:0000250|UniProtKB:Q07794}; MOD_RES 221; /note="N6-acetyllysine; by autocatalysis"; /evidence="ECO:0000250|UniProtKB:Q07794" SPBC342.06c; CHAIN 1..369; /note="Histone acetyltransferase rtt109"; /id="PRO_0000353836" MPDLWSESILEGRKLSIYHLKSTLEKCPFLFGQSKKSKDFQFGSHLFLVEEQNVFIFGMECIVYEKNKEFIVFVSKADSTGFGSKGVSCNSLAFCCLVTLIDGLRKQGAENVTLTLFAIAQGQYLFPESVDNGQKHVLNDSGLLRWWVNCLEKLRKYYTDSEAPNDSEKQKNSTLLPKAYLFVPGLENIRSYLPNRHWIESNAITTGKAVEELPRFPDDPKCRYLCELQDEKSDMSVEEFWDTLTYRQECSSGKLVGFFTLQLQFYQTREFIAKDNFGDSGVMIPAKLYRVTYDTLLKHPFGSLSDAQSSTEKFLSNTLSAVQNLKDFHYKRYKLDICGLAKRDDRKNHNHSKPATQANILQPRKKVKK Q9Y7Y6 RP13A_SCHPO SPBC342.04; CHAIN 1..291; /note="Proteasomal ubiquitin receptor ADRM1 homolog rpn1301"; /id="PRO_0000351079" MSLITFKAGKLRRVPGTKLLRADPEKGYIVMNRDAYGLIHFQWAKRNDLENPEDDIIVFSSECTFEKVTECTTGRAYMLKYPSSAHSLFYWMQEASDDNDTSYAERINSYIKDQDLLDPARSDVATVSDMMEVDTVEQSEPIAQPTESSKESSEIGAPNSDEINSSEAVRNLLATISAQAGFGGSTVDLCEILKPSNLTDLLCQEGVIDRLMPYMPPDTPNNLEGVLAIVSSPQYAQALRSFSQALNSPGGVNIISALGLSLDESANPNEGGALQFLKAIARFVSRNNGSE Q9Y805 CWC25_SCHPO MOD_RES 266; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 268; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC146.05c; CHAIN 1..376; /note="Pre-mRNA-splicing factor cwf25"; /id="PRO_0000079593" MGGGDLNMKKSWHPLLMRNQEKVWKDEQAHKEEMKRVEQLRREIEEERQLLELHRLQEAAGGKKRKDRVEWMYAVPNTNGPNRDSSEMEEYLLGRRRLDDLLKDKIEDQNNSLEKTEFIALQNANSLQDTQAKLRLDPLLAIKQQEQKQLQTLMEKRKYSLDSDRKSKERRHRDRHHRSNQDRSRERSDNEQHSSDKREHSRRSYRNDRNNWRERTHNDRYRHRDKYDSGYFKKHYDDDMRFDQGHFQDERDLKKYVRTSRQYSRSPSPDFRTRNHQFHSRDSQPITQRHTDIESRLQKMQDNAKELDESRRKKIELLEKKERDEEQFLEKERRDTARKWDNQGDFIRNMRKEIYSGDSVSLADRVNSSRHNMLRP Q9Y806 ERV2_SCHPO BINDING 74; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q12284"; BINDING 138; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q12284"; BINDING 141; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q12284"; BINDING 145; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q12284"; BINDING 162; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:Q12284" CATALYTIC ACTIVITY: Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PROSITE-ProRule:PRU00654}; SPBC146.04; CHAIN 1..192; /note="FAD-linked sulfhydryl oxidase erv2"; /id="PRO_0000339122" DISULFID 138..155; /evidence="ECO:0000255|PROSITE-ProRule:PRU00654" MILNRRIQVILPTLLILSFIIWIFHSVMVDKDWRLFMPEIKSLPDREGQGRKPIEMMSTKHDNNTNNLMVNAYWKLIHTVVSNYPNRPTLDERDILRHYLFSSAITMPCGEYSVELQKILDVHPPQTSSRKAATTWACKVHNQLNEKMNQPKTSCDGFNERYVIGSPTYRESEAENVPERVQVINEDHDYSG Q9Y808 MED15_SCHPO MOD_RES 948; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC146.01; CHAIN 1..1063; /note="Mediator of RNA polymerase II transcription subunit 15"; /id="PRO_0000116849" MRDRALPCKCMPSFFKTLHLTFVFSAQTLRIISPSISEVQLMNMALSFERQAFDGASSKNEYLTTCGKKTAQLRDQIRDTLQATQMKQMPSVYNNAGNVGALPTAGPNRLANNPRVMPRLQNQNVPMQAGMQQFARNMKLTPQQRQFLLQQSQIQQQRQQQQQQSQQPQQTQQPQASSPTAPNTEANQQRSGSVPGRIVPALTQQQLNNLCNQITALLARNGNPPIPMQKLQSMPPARLISIYQNQIQKFRSLQHMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQKQAPQNAFFPNPQGNVGAQSLQSMSPQDQPSTQQQQPQRTAAPPNNPNVNATNNNRINIEMLNIPVPKQLFDQIPNLPPNVKIWRDVLELGQSQRLPPEQLKLIGMLYRKHLQIILQHRQQQLNKIQNARMNSQNAPNTNKLGNPQPDNTGNPQAFSQQAFAQQQQQQQQQLHRTSNPTSASVTSQNGQQPINTKLSANAAKTNYQSYLTNKARNATQPTQPPVSQVDYSNNLPPNLDTSSTFRSSASPPSAFTKAGNEALSVPLSGARNTAASRPTNLAAGNSSASIVQQLLECGGTMGQQKMTSRIRELTERVMHSLMRPVPLDLPHDQKVMIASLIKSAYPMFSRTNQLICLFYCLTGNEEATIQLIQMRHIFKLQLEGLQQGVFTCAPQTLAKIKEKTSRYFAFVKAQLLRLHHEVNNNNMSIQNALAHISSLRTASINQQQQPQPQSQQQQQASQFPQAPSVSSNVRPINGSIPNAQPSVPGQAQPAAKANSVGNTSFPVDSKLAFQSLDVSQPDLQAKQKIASQVMKHGLKPEDLKLPPSKKKKIENLSTVQKPKDSVVNTPDVIMSSVDEIPSSVSPGTIAKEEGMAKAREEAIANPLKYAIDAFVAVDHEEEVSAIKSSQTPSSILKTPQSFFIPPSTPDLSFTDNKNSLSPSNILSLDGKFSFNDDSELWADLGNEINSEIGFLKEPDTMNLALDADKDKTKMQNKLTQINFDESCFLDPAIDDKDPWNEMLHEKKVLLKQLQVGNEDEDNIAFPTSTNIWQVVI Q9Y821 MED4_SCHPO MOD_RES 204; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1105.06; HELIX 3..23; /evidence="ECO:0007829|PDB:5N9J"; HELIX 27..85; /evidence="ECO:0007829|PDB:5N9J"; HELIX 104..117; /evidence="ECO:0007829|PDB:5N9J"; HELIX 143..148; /evidence="ECO:0007829|PDB:5N9J"; HELIX 150..158; /evidence="ECO:0007829|PDB:5N9J"; HELIX 164..172; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..239; /note="Mediator of RNA polymerase II transcription subunit 4"; /id="PRO_0000096385" MEYQRAIDSIEECLNKQLRLSSEKVDQYVLIENWTSLVGHLKTLHSLISNYTNGRELQNEISSLLKQDKELDLQIQDCMREMTSIYDTHLPKTVSGRKRQKVNAETLLDYGRKLSKFSSAPPGYNPETGQDAKAPVHYPWPSEDQMRKTLLFQFSTSMVPNLSATASQLFSEQPPKTNEPTETETEIDANKAVEEKTKMNYPASPTFTTQEENKEVESPANKDVFAGFDLFDPEMEEDF U3H042 SOS7_SCHPO SPAPB17E12.06; CHAIN 1..264; /note="Kinetochore protein Sos7"; /id="PRO_0000429002" MDQNKSTQATGNGKKTEEINELLESFIKEGPKLLWGSTNLKYEDQISRSSEHELQQYRELFTRLKFSYIEQGTKERYLRAILDDPPMLVEAEDNEKLETTNSSLKGRLKSEKREVDLLTEELKTTSRELSSNYESVMEECKNTKSTLSKLESLESELLKLQQDSSTKTPILPEVEAAIHDLESELNITNESIETIDGKIDNDEKYFIQLTKNLSLLEKEYKIASERSNQIKAAIHTRTPDADAKKQVQNWYTSMLEIYDQLLQK A6X980 SFC7_SCHPO SPAC1250.07; STRAND 15..24; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 34..38; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 42..44; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 46..49; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 52..59; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 62..69; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 81..83; /evidence="ECO:0007829|PDB:4BJJ"; STRAND 87..93; /evidence="ECO:0007829|PDB:4BJJ" CHAIN 1..120; /note="Transcription factor tau subunit sfc7"; /id="PRO_0000307346" MSSNSPSLETDVDDVENIVFQFQNSSLDFQSSDDFSILGIDQPHPIVRIGGMFFRGTWHQPIGTDIVVPSVNDSELSRDGLVLCKRRLMLEQIRLVPKNPSPSSSIHSPTQGEPENISEN A9ZLL8 LSD90_SCHPO BINDING 717..724; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC16E9.16c; CHAIN 2..756; /note="Protein lsd90"; /id="PRO_0000415924" MVGTINESMQNMKIGAKETAQSAKQGIKNAGQSSSKTARDVMGNPVPGSYTAGNTANDGDSSYASSKNPSGNADIGATSSERTAYAAPQRAAVDTSNVSPPSTQTGGYASKDTTSTYEGAQPLSSQSSRSSNYTNVKITATQNNVDALTGAPIRIVTTTNARIQPDEKTLQDLLEQRQVALREAREAEEELQRARQYNDRSTSEALELEARAKKAAQDAELASERAREAQSSIERSASLREKQAREEAERAATALREAELKHRLAQANADVDVANSKLDIALKNEAAWKAERESSLAHQKAVIDSARAELERARHEAAVADATYKKEHYEYNALVAELEERNDNTLRTASIREAEARNLEVHMEDTLKDARMRSRNATEQVEVVKREINSEIDVYRSSVEKTKAELASYQKGLPSQKEACDRELDDATRALQAAQDRFNAAKLRVNQFDVDSRQQLAMLTKKVRDAEDAEEKYRISCHQREEEITRCATQAYDAVKAAEKRNETIAEAARAKENEAKDLYSKAESITQDLNAKRSHPPQPANLDYSSAIQRAQERLTLEESKLTDLRTAEPSQYVNDVEVARRALRDAQAEQSKVESEYNSVKGSKLYTTEPVHPHAVTTNEPTDVSTKSKSAAYHYPATTETVSSKAARSATTPAYVGGATKTPSTTKAVESTPSTLPTSASTNAAATTTTKKPKAAKSTAVRDDVSSASSDSDKGTTGLGKSESKSSRKERRSSTSSGHGLMNNVRHALGMSNK B5BP47 YP53_SCHPO SPBC460.03; CHAIN 1..567; /note="Uncharacterized transporter C460.03"; /id="PRO_0000415921" MNVQKSNNAEETITPFSEESSLLNSNSYIPATFVDPTTIPQTSTEDIDIHGFNSIFDIPNLAWIEVSLLLNVFLAGFDGTVTASAYTTIGEEFHAANLASWITTSYLITSTTFQPLYGSFSDVLGRRVCLFMASGLFCLGCLWCYFSSGMVSLIFARSFMGIGGGGLITLSTIINSDIIPTRNRGLFQAFQNLLLGFGAICGASFGGVLSEVFSWRLCFLVQVPFSVLSIAVGFFFVKNQSGYSRFHHYCVLFKKIDILGGLLLVSGLTSLLLVLTFGSSRSIQTYRPSQLLLLLGILCIVAFVYVESITEAAPIIPLKLLKGLYSSLVLTTGFLIGLAGYAYLFTLPLFFQLVLGDSPSKAGLRLALPSLSTPIGGLICGILMHRNFRVGKLLFSGVFLMSLGYFLSLFIHPGISPIVLGIFLIPANVGQGIGFPSSLFSFIFAFPQNSHATSTSTLYLIRSIGSLFGVGGLSAVIQLTLRKKMLADLTKFTDLDSKSIQKIIHDVSKSISALYELPEAIQEIVLSDYTFSIRKAQQFTTICCVLALGLCILKDTIKPRTPSGFRY B8Y7Y5 IEC5_SCHPO SPAPB1E7.14; CHAIN 1..144; /note="INO80 complex subunit 5"; /id="PRO_0000389111" MAAQKKQGERVLPARSTRKRRQLPDMLYYDERTDSYVTPQERSLSEANAQTRPAPNTINQAVDAKQSAREARVQELMKSKLYHLRKQQKQARHKRDQWAIDYLEWKKNEDEDVWNSDAEATGPAEHTSSFLDALRFSQQFMKAE C6Y4C2 SPO2_SCHPO SPBC16C6.14; CHAIN 1..133; /note="Sporulation-specific protein 2"; /id="PRO_0000389117" MSITMSDSSAYGEELMRERFEHLLKAYEKMALMVAEQEEFNAKIEDMALKLLSEKYDNEAYQAELFYRLSNCVEKVLHNKISITDLKTEYEEILEQTLKKECKAYERSCIENVKLKKRTEQATAYYASSSSEP C6Y4D3 ECL1_SCHPO SPCC70.12c; CHAIN 1..80; /note="Extender of the chronological lifespan protein 1"; /id="PRO_0000389114" MDLDFCTVCGATTQDGSLYCSSECHLLDFTKLDTQTTSNISVSSEYQFLVSEHLAHFHRKSMTSADFPTPRFSAYTKLHA G2TRK8 GEMI6_SCHPO SPAC4D7.15; CHAIN 1..93; /note="Uncharacterized protein new12"; /id="PRO_0000416506" MDSHTTEKRRGSYLRVLFKNGRLPVEGFLWNCDPLTGTLILIQPLTPNTDEVEDTHYRFYGIMSDAIQTIEPDESMSPLNQQSLAEYDSLLTS G2TRL2 CENPW_SCHPO SPAC17G8.15; CHAIN 1..73; /note="Inner kinetochore subunit wip1"; /id="PRO_0000416502" MSYPKARIRRFFRQHCQRSLESSALDLVYLDYCLFLQSLLKEANIEAAKTGERRVQPEHVRSIQRKILAQFKG G2TRL9 ACPS_SCHPO BINDING 6; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 67; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7; SPAC3G9.17; CHAIN 1..132; /note="Putative holo-[acyl-carrier-protein] synthase"; /id="PRO_0000416491" MGLGIDILKISRISRLIQRSPEWEKNFLKKCLCENEIKKYNLIKSNSSLPRLSEQAKWLAVRWCVKEAVFKALQPNFRVYMSMMEYVRTPTGYPSVVIHDPRFPLSPVMVSVSHEEDLVVANALYLPSMPKT G2TRP5 COX7_SCHPO SPBC2F12.17; CHAIN 1..59; /note="Cytochrome c oxidase subunit 7"; /id="PRO_0000416680" MKNTIVQQQRFLQSIHKPTYLQRPGSFALVYPYYAVMAGLGLYSLYASGRVIFGKKDAF G2TRR1 GEMI7_SCHPO SPBC32F12.16; CHAIN 1..91; /note="Gem-associated protein 7 homolog"; /id="PRO_0000416501" MAENNKKSTAYIQRMRTLKFYQKMASARIPITVYLHDQREVKAEFGAIDSSESKLAVSNLQTDWGVINRAVIRTGDVVGIEYNLVQEEGEL G2TRS3 KISH_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPBC530.16; CHAIN 22..73; /note="Protein kish"; /id="PRO_0000416500" MTAIFNFESLLFVILLTICTCTYLHRQFPALLEKRKEGVTMVFWKCARIGERASPYISLFCVFMALRFIFGSS G2TRU7 WTF15_SCHPO SPCC663.17; CHAIN 1..255; /note="Wtf element wtf15"; /id="PRO_0000416675" MSNNYTSLSSSLDEEMGLKAGHEIDLEGSPPSEHNSEEKSTLPSNSDILTSANPVSQASETPDHSIESNTGSTQSPTSHSLLLKFSFCIVYYSYFAIVVLGCVLPFEHTHTFLIAFLVIFGIISVILFSGSIYYYETWTKTVKHFLKKVISPFKKEYIVCAFLKTFVFYGLLKTIEHFLVLLSGDKWGWKCSTLSSILTPVSCISFCLNESVQLRSCSTHLFINTVAWIKSLGGGKNAFENNYNQLNETSPEDLV O00091 G6PD_SCHPO ACT_SITE 247; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P11411" BINDING 18..25; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 52; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 155; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 155; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 185..189; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 223; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 242; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 338; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 341; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 347; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 351; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 373; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 375; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 381..383; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 401..403; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 483; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413" CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; SPAC3A12.18; CHAIN 1..500; /note="Glucose-6-phosphate 1-dehydrogenase"; /id="PRO_0000068106" MSSANLSIKENGAMVVFGASGDLSKKKTFPALFSLFSEGRLPKDIRIVGYARSKIEHEDFLDRITQNIKIDEEDSQAKEKLEEFKKRCSYYRGSYDKPEDFEGLNSHLCEREGDRSTHNRIFYLALPPDVFVSVATNLKKKCVPEKGIARLVIEKPFGVDLKSAQELQSQLAPLFDEKEIYRIDHYLGKEMVQNLVHLRFCNPVISHLWDKNSISSVQITFKEPIGTEGRGGYFDSSTIVRDIVQNHLVQILTLLTMETPTTFSADDLRDEKVKVLRRTRLGDLKDIVLGQYVKSKDGKKPGYLDDETVPKGSRCPTYSAIPCFIDTERWRGVPFLLKAGKAMDIGKVEIRVQFKAAANGLFKDAYHNELVIRVQPDEAIYFKMNIKQPGLSEAPLLTDLDLTYSRRFKNMKLHEAYEALFLDAFAGDQSRFARIDELECAWSLVDPLLKYMEEEKPVPEPYEYGSDGPECLYSFLKKFGYIYDSPDYYDYPVMSVPSDH O13610 FCF1_SCHPO SPBC32H8.04c; STRAND 63..69; /evidence="ECO:0007829|PDB:5YZ4"; STRAND 96..101; /evidence="ECO:0007829|PDB:5YZ4"; STRAND 128..130; /evidence="ECO:0007829|PDB:5YZ4"; STRAND 154..156; /evidence="ECO:0007829|PDB:5YZ4"; STRAND 174..178; /evidence="ECO:0007829|PDB:5YZ4"; STRAND 181..188; /evidence="ECO:0007829|PDB:5YZ4" HELIX 73..79; /evidence="ECO:0007829|PDB:5YZ4"; HELIX 84..92; /evidence="ECO:0007829|PDB:5YZ4"; HELIX 102..110; /evidence="ECO:0007829|PDB:5YZ4"; HELIX 112..115; /evidence="ECO:0007829|PDB:5YZ4"; HELIX 116..122; /evidence="ECO:0007829|PDB:5YZ4"; HELIX 139..149; /evidence="ECO:0007829|PDB:5YZ4"; HELIX 160..166; /evidence="ECO:0007829|PDB:5YZ4" CHAIN 1..192; /note="rRNA-processing protein fcf1"; /id="PRO_0000339875" MGKAKTTRKFAQVKRVINLKDQRLQKKDQKKEKEKTTKNGELVREIPQMASNLFFQFNESLGPPYHVIIDTNFINFCLQQKIDLFEGLMTCLYAKTIPCISDCVMAELEKLGIRYRIALRIAKDERFERLPCTHKGTYADDCIVQRVMQHKCYLVATNDKNLKQRIRKIPGIPILSVANHKIRVERLVDVVD O13614 RS10B_SCHPO SPBP22H7.08; CHAIN 1..147; /note="Small ribosomal subunit protein eS10B"; /id="PRO_0000116375" MLIPKENRKAIHQALFQQGVLVAKKDFNLPKHPEVGVPNLQVIKACQSLDSRGYLKTRYNWGWFYYTLTNEGVEYLREYLHLPAEVVPATHKRQVRPAAPRAGRPEPRERSSAADAGYRRAEKKDDGAAPGGFAPSFRGGFGRPVAA O13619 YHI3_SCHPO SPBP22H7.03; CHAIN 1..181; /note="Uncharacterized protein P22H7.03"; /id="PRO_0000304012" MSQSPIDYNESLRPDDMLDNELNYELANEVSAGDEEPYDDDIWESEDLEPVGHDIQPMDSVSDFHVKDFSEKKYSPYTDEIASAQLTGPSESAFGSASSLGTVESPVTMQSATLLWDPSVKEVDDILHNEDFYDGRDLNIFTLRGFVNILTLILLSCGLLMLFIGYPILSAVEVEKQRKKN O13620 MRD1_SCHPO SPBP22H7.02c; CHAIN 1..833; /note="Multiple RNA-binding domain-containing protein 1"; /id="PRO_0000081644" MSRIIIKNIPRYYDKEKLSTYLKSLPQLDAEITDVSVAKTKEGVSRRFAFIGFKNEEDADKAIRYLNKSYVETSRIEVHRALDYRSANEKLRPYSKYASKNIELKLQKKEKEEELRNLEEEKAKKKKDANLKRKFLDTLDPKAREFLKLSSSISNSRSWENEEVFDTEITNPVIPADEDDDEYQDLPAAKRHEGDSIKSTEHDSTLDSGVVIDGREKSSSELHEEESEQAAEGDTAKNSGTDAQAPLSDDEWLRLHRTRIKEKQPEEEVSVVGDELKSFDKENNDEHLERVTNDKIADASMLQKAENNVSEQERNIQLISETKRLFLRNLTYSCAEDDLKSLFGPFGQLEQVHMPIDKKTNNPKGFAYIDFHDADDAVRAYLELDAKPFQGRLLHVLPAKARSSILLDDYALSKLPLKKQRELKRKNTAASSTFSWNSLYMNADAVVTSLASRLGVKKTDILDPTSSDSAVKQALTETHVIQETKNFFEEHGVDLDAFKNAARSDNVLLVKNFPYGTSAEELTSLFSPFGELGRILIPPAGTIAIIEFLNAPDCRQAFSKLAYTRIKSSILYLEKAPRDVFTTSFKQSGKPELAQKVNAVEATTSEKVGTEDIESLDTATIYVKNLNFSTKQEEFQKVFKPLEGYLSAVIRAKPDPKRPGKYLSMGFGFVEFKDKASAVAAMHAMNGFVLDGHKLEIKLSHQGVDAAAEVRKQDSSKPKGTKILIKNLPFEATKKDVQSLLGAYGQLRSVRVPKKFDRSARGFAFAEFVTAREAANAMRALKNTHLLGRHLVLQYASNATMDDMQHAIEKMAKEANAEAAAPSITGKRLIETD O13622 MS116_SCHPO BINDING 83..90; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; TRANSIT 1..27; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC691.04; CHAIN 28..535; /note="ATP-dependent RNA helicase mss116, mitochondrial"; /id="PRO_0000256013" MNISLKGAIFSTVGRFNLPKVQGFIRWNSTMKSQQPTLFSEVASLSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILNIHEAVTTTKTRKLCFSATMPPKVSNVFRGILGTDFKLINCLDPNEPPTHERVPQFVIETKLDKVFSSSLSLLQQLTSSNPSSRIIVFLPTISMVDFVGGVLENHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHLPLKRATIEPLSDQALSTLRSDIEKSSKFSRTNALKTLYGSKPHVFSGSSQRRATGKNIHESAIALFSLHDVPGLMEELIYKSRGRGSPKGFRGSQLKYPSSSSSSFQRRPRSLPSRGRYQQSRR O13629 LPLA_SCHPO BINDING 91; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 96..99; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 152; /ligand="(R)-lipoate"; /ligand_id="ChEBI:CHEBI:83088"; /evidence="ECO:0000250"; BINDING 152; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP + diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein]; Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099, ChEBI:CHEBI:456215; EC=6.3.1.20; SPBC17A3.09c; CHAIN 1..363; /note="Putative lipoate-protein ligase A"; /id="PRO_0000315634" MLEAVTNPKSSLATFSKQLNGLLQAKVVVCKSVNPYFNLALENYLYENSTAKHCLLLYTNSPSVIIGRNQNPWVEANVKLCRDNFVNIIRRKSGGGTVFHDFGNLNYSVLMNREEFSHTENASIMIQALRNLGVHARLNQRHDIVLAQSQRKISGSAYKISRNRCYHHGTMLLNSDLEGVREYLRSPSTGILSKGVSSTRSPVSNTKLLKAEFIKQVISCFLLHKSHSTTTKPLSKPRASSKRLYDIEPKSVITLEQNDLLGVPSILKAVNELQSWEWTFGQTPSFKQHLESTELSVSMDISVVHGRLEKVIFSTPNATLEHELSSIPWTGLCYESGFANTFLISGIHSKEAISILKWISDSI O13632 PVH1_SCHPO ACT_SITE 131; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; SPBC17A3.06; CHAIN 1..330; /note="Tyrosine-protein phosphatase yvh1"; /id="PRO_0000314761" MSNKSAWQPQFDEIHSSVQEAEGFLQSSNDVQKAIDEVHYPDSLNDLSEISKNLYISSWKTASELVSTSDKGIDYTLSAMSINPNLSVPEQQHLWLQIEDSSSQNILQYFEKSNKFIAFALSKNAKVLVHCFAGISRSVTLVAAYLMKENNWNTEEALSHINERRSGISPNANFLRQLRVYFECNYQLDRSLRPYRQWLFRRYGDFAVLNTRVPSEVAYAETVRARAGQLELRCKKCRFVLASSDYLVSHEPKDENNYSHTRCTHYFLEPIRWMQPELELGNLEGRFDCPKCNSKIGSYKWQGLQCSCLQWVCPALSILQSRVDAVRKLG O13633 YNF5_SCHPO MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17A3.05c; CHAIN 1..403; /note="Uncharacterized J domain-containing protein C17A3.05c"; /id="PRO_0000363406" MESSREEALRCIGLARKYLNAGEYDKALKFANKSLRIHATTEGEDFVKQIEKQKLTGSPNPQATPKQENKSNFFSEKQSVRENGNSSAGEKKQKWTSEQHLLVQKIIKYKNHQYYEILDLKKTCTDTEIKKSYKKLALQLHPDKNHAPSADEAFKMVSKAFQVLSDPNLRAHYDRTGMDPESRASAASSSFSSNAGGHPGFSAYPQANMSPEDLFNSFFGDQFFSGPGTFFFGGGPGIRVHQFGGRPRNFARRQQAQDMPPKSIFYQLLPLIVVILFAFLSNFSWSDSTSVNTRYSFQQNYKYTVPRTTAKHNIPYYMSQKDLDKLSSRDIRRLNEKVEHTYTQNVHNACLREQQIKEDEIRRAQGWFFPDKEALKKAKELRLPNCEELNRLGYRTYSNSYYF O13636 TIM50_SCHPO TRANSIT 1..27; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC17A3.01c; CHAIN 28..452; /note="Mitochondrial import inner membrane translocase subunit tim50"; /id="PRO_0000043136" MLNRSLLFRNLRLARPRPFLPLVGKRFVTEKSQSQEEKDTSKITENAKEEVKRDTSSLAKESLKLLDLNGLNDESYTGDPGKGPEYTSSTMLKREKQARYAFWGFLGLTGGGLLYYGRRYGPDEKELEKQYPAAGYSPSDWWNRVKARTNNFFSYYQEPAFEKLLPDPLPEPYNRPYTLVLSLDDLLIHSEWTRQHGWRTAKRPGLDYFLGYLSMYYEVVIFTRQYLATAKPIIDKIDPYHVSISAVLTRESSKYEKGKVIKDLSYLNRDLSRVIMIDTNPESWSKQPDNAIAMAPWTGNPKDKELVGLIPLLEFIAIMDIKDVRPVLKSYQGKNIPLEYARREEKLRTKLIEDWNEKKKKGSSFLFGGRSVSEEPPKLIIDIQRERQKAAYAEFKKYIDENGPKMLEEEKAREAEQKTSIFNLLFHPEEVQQQQLEQMQQQQFSPETNASK O13639 SAHH_SCHPO BINDING 56; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 132; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 157; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 158..160; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 187; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 191; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 192; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 221..226; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 244; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 300..302; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 347; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Note=Binds 1 NAD(+) per subunit.; SPBC8D2.18c; CHAIN 1..433; /note="Adenosylhomocysteinase"; /id="PRO_0000116936" MATQNYKVADISLAAFGRKELEIAENEMPGLIAVREKYAKSQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAATGVPVFAWKGETEEEYLWCIEQQLKSFPSGKPLNMILDDGGDLTALVHERHPELLVDIRGISEETTTGVHNLYKMFKENKLKVPAINVNDSVTKSKFDNLFGCKESLVDGIKRATDVMIAGKVAVVAGFGDVGKGCSTSLRSQGARVIVTEVDPINALQAAMDGFEVTTMEEAVKEGQIFVTTTGCRDIIRGEHFNEMKEDSIVCNIGHFDVEIDVAWLKANAKDVVNIKPQVDRYELKNGRHIILLADGRLVNLGCATGHPSFVMSCSFTNQVLAQIALWTDNTSYPLGVHMLPKKLDEEVARLHLGKLGVKLTTLTSVQSDYLGIPVDGPYKADHYRY O13642 LIPA_SCHPO BINDING 100; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123"; BINDING 105; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123"; BINDING 111; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123"; BINDING 131; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123"; BINDING 135; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123"; BINDING 138; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123"; BINDING 346; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03123" CATALYTIC ACTIVITY: Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_03123}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03123}; Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_03123}; SPBC8D2.15; CHAIN 1..370; /note="Lipoyl synthase, mitochondrial"; /id="PRO_0000017725" MLKIGRNATILKNNFWFASVRFQSGGFSEKLAKGPSFADFLNMDKPLTADEAFELDRKVELPNGSIHKRLPSWLKTKVPLGTNFNRIKHDLRGSHLHTVCEEAKCPNIGECWGGKDKSRATATIMLMGDTCTRGCRFCSVKTSRRPGPLDPNEPENTAEAIKQWNLGYIVLTSVDRDDLTDLGANHIAKTIQKIKEKAPHILVEALTPDFSGRMDLVEIVAKSGLDVFAHNVETVEELTPFVRDRRATYRQSLSVLKHVKKTCPHLITKTSIMLGLGETDAEILTTLKDLLEHNVDVVTFGQYMRPTKRHLKVQEYVHPKKFEYWKEVAEKLGFLYVASGPLVRSSYKAGEYFMENLIKKRSGNPASMSV O13644 SED5_SCHPO SPBC8D2.14c; CHAIN 1..309; /note="Integral membrane protein sed5"; /id="PRO_0000210272" MSFQDRTAEFQACVTKTRSRLRTTTANQAVGGPDQTKHQKSEFTRIAQKIANQINQTGEKLQKLSQLAKRKTLFDDRPVEIQELTFQIKQSLSSLNSDIASLQQVVKGNRNKPAQMNQHSENVVVSLQNSLANTSMTFKDILEIRTQNMKASQNRTEKFVASSSMNANPLINSGNSISPFADYNDPKPEANEDYLSLNLGDGANTRYEQMALLESQTDTYSQQRMSSIQNIESTITELGGIFSQLAQMVSEQRETVQRIDMHTDDIVSNIGSAQREIVKFYERMSSNRALLFKIFGIVIIFFLLWVLVT O13651 SYIC_SCHPO BINDING 600; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5; SPBC8D2.06; CHAIN 1..1064; /note="Isoleucine--tRNA ligase, cytoplasmic"; /id="PRO_0000098603" MSFNVPKEEEKIVEFWREIDAFHTQLKLSQGRPTYTFFDGPPFATGRPHHGHLLASTIKDSVTRYACLKGYHVERRFGWDTHGLPVEHEIDKKLGITGSDDVMAMGIDKYNAECRKIVMTYASEWRATVERLGRWIDFDNDYKTLYPSFMESVWWVFKELHTKGKVYRGYRVMPYSTACTTPLSNFEAQQNYKEVPDPAIVVAFQSISDPEVSFLAWTTTPWTLPSNLALAVHPDLQYIKILDKDSNKKYILMESCLGILYKNPKKANFEILERFQGKALDGQKYEPLFPYFKSTFGERAFKLYSADYVEEGSGTGIVHQAPAFGEADYDAAWAAGIIDADHQPPCPVDEQGLLTSEITDFAGQYVKDADKEIIRSLKASGHLVKHSQIFHSYPFCWRSDTPLIYRAVPSWFVRVKEITNEMVENVMSTHWVPQNIRDKRFANWLKNARDWNISRNRYWGTPIPLWVSDDYEEVVCIGSIKELEELSGVSNITDIHRDSIDHITIPSKKGKGTLHRVSEVFDCWFESGSMPYASRHYPFERIEEFKHGFPADFISEGVDQTRGWFYTLTVLGTLLFDKAPYKNVIVSGLVMAEDGKKMSKRLKNYPEPNLIIEKYGSDALRLYLINSPVVRAEILKFKEDGVREVVTRVLIPWWNSYKFFEAQAALYKKVTGKDFVFDDAATLSSNVMDRWILARCQSLIGFVDEEMKQYRLYTVVPQLLGLIEEMTNWYIRFNRRRLKGEDGEIETINALNVLFEVLFTLVRIMGPFTPFITENIYQHLRNYMPIDKNEISLRSVHFLPFPTYKSELDDETVLRRVKRMQTIIELARYVREQNNISLKTPLKTLIVILTNEEYLEDAKLLERYIAEELNVREVVFTSNEEKYGVVYSVQADWPVLGKKLRKDMARVKKALPNVTSEEVKEFQKNKKMVLDGIELVEGDLQIIRSVEVKNEFLKSNTDGICIVLLDIEIDAQLQAEGLAREVINRVQRLRKKSNLQVTDDVRMTYKIKNDTIGLESAVDSNEALFSKVLRRPIEKETGADESNIIASEEQDVQGATFLLSLLRL O13652 SFI1_SCHPO SPBC8D2.05c; CHAIN 1..840; /note="Protein sfi1"; /id="PRO_0000290647" MSKNGAPKYVDGGRKIMDEDLRRDLEILRLILLRLSHAADDTSPLDVFNAYESVLRENGLNPARHRSYIRILYRLISSKKLSWNDEWRNLMRRIGFSQVSSDLNTPLFPLNNTDMENDPFIVNGDDYRSRSNQQKSSQFASEVAQTIKSQTAMFRRADQYRSQKDKILLANSLDFMLEKYRYYKKIDAVYLRKADAVYRAFIMLKYFPRWVQKLRNIQSRIYSAGEAYRLILIGQMVNRWRQKTRERLHQKLRFQKNAFLLDVLLKWSALTVNWNRKHEYMLKRRVFTNWMSKRRRNESLIQKANVFFQHSVLAHSFKTWKANLSIKNAATLYEKKVVFMSFNRWHANYESHVLDLQKAELFSQKAYYSIALHKWKLRIEELSDLMNKADDLYEVNLLQRMLVLWRRKATTYEKIDFWMDGHDVDIVKSAFFKWKNKFIKVDRNFELADTILQNTFLTKWRLAVRVKVVQEKRNKDRLIVTFRFWYYLMKAKSFQHKRDHRLLTIAWEAWKDNYQRRIKLQKEAQELQLTRIQKIAKQYLIKWRISLLDIKELSIRAEKLHTTNEIIGVWNQWVVSYNRKVGMQQNADLFFKRKTLRVVFEHWRYLRETNMLLRLENKVVDFREVQSEKLVLRCWNAWVARLLSVSQMLDTAELSTQKVVVRAYEAWSFRYNHQKEIMSQADQFYNERLMRSAMVFWRYQLRAIKFYFNISDWKRREFNRQTLRNAFDAWHLLMFRVTSLVMQADRFHEQKKNKLLGKYFRKWLQRMQLNQEESSLLEAEATIEGNRTSRYMHTFDTTLPMQNDEFTDESVNFENRWKQELKTPISRFSKFLRPIPPNTR O13656 TOM40_SCHPO SPBC27B12.13; CHAIN 1..344; /note="Probable mitochondrial import receptor subunit tom40"; /id="PRO_0000051534" MDYIQTLFTSVNQVGEKIDSYKSSLNLINPGTCENLSKEVSKDILLSNYAFTGVRADVTKGFCTSPWFTVSHAFALGSQVLPPYSFSTMFGGEPLFLRGSVDNDGAVQAMLNCTWNSNVLSKVQMQLSNGAVPNMCQIEHDHKGKDFSFSFKAMNPWYEEKLTGIYIISLLQSVTPKLSLGVEALWQKPSSSIGPEEATLSYMTRYNAADWIATAHLNGSQGDVTATFWRKLSPKVEAGVECQLSPVGLNHSAALMTGPKPEGLTSVGVKYEFAQSIYRGQVDSKGRVGVYLERRLAPAITLAFSSELDHPNRNAKVGLGLSLELPGSDEMIQQQQQQLAAQTA O13657 YBCC_SCHPO MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 449; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 452; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27B12.12c; CHAIN 1..803; /note="Putative metal ion transporter C27B12.12c"; /id="PRO_0000316218" MSFQQPSNGAQGGNNNALEKTSSNEATSSSSTQVSSLSASGISVSTPRVSPFEPERNMQVQSSQHLEANVQSPVSSQTTYATPSAYAVPQESEIELHESEMVPQKPKKKKRSRRNRKASRKKIPATQSSSADMDTLHVCPTCGSCSDSKKPQSNKKHRGRRVKHSPKSTLEVPDGIPDIKALSASMGSSSQHASRYNEGRGSFDTLGTHYHLSKSRKSSSSDSLYSVSSMSIKNDSNSDSLSSSSSSDVSGSDENLPIDKTLYLSVEDPSFMVHPRRPSATKSCSAAVDCPHTTIPKPPYQSDTDLTELPTKSTAQFSDETFTVQPRLKSTHSSIADNEDREVDSQVDENTRVVEEDVCFPMQEESHVNKGIDFDELDNFAEEELQKQRQNTDHFRSRQYSTCKPFEPHWNDLSPHDPNDPSSSLHSNNAEKAAEVPLRSSYYSGGRRSVTSMSDSPYRFSFFSSNQNETIHASVLSDLLDDGATSFRSLFCPEKGVWWLDCLDPTDIEMRVLSKAFSIHPLTTEDIRVQEAREKVELFGSYYFVCFRSFEQDPELANYLEPLNMYIVVFREGLLTFHFSSATHPASVRRRARQLRDYVHVSSDWLCYALIDDITDAFVPLIRGIETETEAIEDSVLVGRSEDSSDMLRRIGECRKKTMGMFRLLYGKADVIKMLAKRCNEKWTIAPTGEIGLYLGDIQDHLVTMTSNLSQFEKILSRTHSNYLAQLTSNSIEENSRTNGALGKITLIGTLLVPMNLVTGLFGMNVPVPGRDTNNLAWFFGILGVLLGSIAIGWIITMRYNAF O13663 GPI13_SCHPO PTM: Glycosylated. {ECO:0000250}. SPBC27B12.06; CHAIN 1..918; /note="GPI ethanolamine phosphate transferase 3"; /id="PRO_0000316600" CARBOHYD 54; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 71; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 101; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 197; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 399; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MEEKRVKCKKKLTSTIGTWKYIQACIFFAIILISNFYGLKSFTDGFLLRRAVLNQTSLCENPPADVREWKNSSGCWAPKIFERAVIVIIDALRYDFLIPYNDSNYYHNAFTTPYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPTFIDLGSNFAGTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLFHDYLNETLSQPAFSFNVPDLHGVDNKVNQYVFDYIKDANFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYSKKPTFGYLKQPGKVLSANQVDLVPTLSLLLGNPIPYGNLGTLIPEPFYYYGDEYLSKAQKINIGQLNRFFSEYDLDASDFLSSSVHKNNNSYLDQYFLDFDYARDAFSYFKAIWAEFSLFPMIIGFLLLIIGGFNLALLMQDKSVIFRMSANMAPSVMKCLPVCLILILANNELHSPFPAEFYVLLPSFYILLNSFNQKLMEYFKGFVKLDYFSIFITFLHVCSFGSNSFTVWEDRLCHFLIITIGLVMFCKCFSEMSPLFACSTYSALAFILLQVISSYVTNCREEQGAFCVSTYISTPDNSLRTLIVLALMALSSIILPLILQLHLRRVLGLSLKLYHLSILYFFELISSIFWIAHHVFANDALLEKQYHHVLYSLANTYVICILGVLIWQFFLLSRSKFAKINVIERSYFVFALLYSFLSFLQRPLGHLSLFSCFLQILLLIQLKQWQPSVGHNFFSVTLGLLGLSHFFTTGNQAAISSLDWNFAFIHSKSAENQAISAIFMFLHTVGAPILTCISIPLFSFEPLSKKNRFLINLFRFSFSFILYNLLISTSTVFFAGFFRRHLMVWKVFAPRFMLSGILLVTHQLFVLIQCFGSSVVKFPEDAE O13670 MTO1_SCHPO BINDING 23..28; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; TRANSIT 1..16; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC30B4.06c; CHAIN ?..666; /note="Protein MTO1 homolog, mitochondrial"; /id="PRO_0000042790" MFRTTKRYFCTSFNRRKNVVVIGGGHAGVEAAAAASRLGAKTTLLTKSFDNIGQMSCNPAFGGIGKGTLMREIDALGGVVSGVCDESAIQFHMLNRSNGPAVWSPRAQMDRSVFKKNMQKTISTYRKNLQVREGAAVSINVLTEDDGKQVCDSIVLEDGTAIPASCIVITTGTFLGGQINVGLTQLAAGRYGERPSLPLSKCLSNLGFKMGRLKTGTPPRLSSPINISKMTEQTGDEIPETFSFLNLERDFSPALPQRSCYRTYTTELTHEIVRKNLAFAPHMLAGDILSPRYCPSLEAKVTRFPHKARHLIWLEPEGLDPNSWWYPNGLSNSMPEEIQHNIIRSIPGLENCNIVRPAYGVMYDYVIPTQLKATLETKKIQGLYLAGQINGTTGYEEAAAQGILAGLNAGLSALGREPVDIPRNTALLGVMVDDLITKGVKEPYRVFTSRSEYRLTTRADNADLRLTPLAQSIGLLDDQTHWESFQRTKSLLDFSNKIAKEFILSPQQWSKLGMPIPNDGKYRSAWDLLSFTNLDLFCVISCIPKLKDIPKRVLQRLIIEGKYTYYIKRQGTQNKQLNCRDESTVIPSDFDFDTLHSVSAEELMLLKTIRPATIGQLKRIQGIKPGTIIRLLRHTYYNPAKEAWLRKVYMPMYDMHSSEENQSTNL O13671 CSE1_SCHPO SPBC30B4.05; CHAIN 1..967; /note="Importin-alpha re-exporter"; /id="PRO_0000117292" MDDIPTLLARTLNPTTSKSAEEALKVWELQDSSFALKLLNIVAEDTVDINIKLAASLYFKNYIKKHWDSEEGASIRISDEVAELIKREIINLMLKSTTIIQVQLGEVIGYIANFDFPDRWDTLLPDLISKLSAVDMNTNIAVLSTAHAIFKRWRPLFRSDALFLEIKYVLDRFCEPFLALFVQTNNLLRNGPQDAESLNSLFQVILLECKLFYDLNCQDIPEFFEDHMSEFMTAFLNYFTYTNPSLEGDEGETNVLIKVKASICEIVELYTLRYEEVFTMLYDFVNVTWTLLTTLTPDEKYDGLVGKAMAFLTSVIRIRKHAEFFQQDQVLQQFIELVVLPNICLRESDEELFEDDPLEYVRRDLEGSNSDSRARSAIVLVRGLLDHFDQKITSVVSTHINANLQQFSTNPSLEWNKKYVALQLFSAIAIKGQSTRLGVTSINLMVDVVAFFENNIKPDLLQPAGVIHPMVLAEDIKYVFTFRNQLNSQQLIDIFPTILRFLEMPSFVVYTYAAIALDQLLTVRHNHVHIFTSLLIAPHILPALNQLFLIVESASTPQKLAENDYLMKAVMRIIIMSQEAILPAASLLLQHLTKITEEVSKNPSNPKFNHYLFESIGALIRSLSKSGPQTVSQLENALLPVFQNVLIEDVTEFIPYVLQLLSQLVEASGNEPLPDFVVNLIQPCLSPALWDSKGNIPALVRLLRAMIFRGPQIFISNKFVEPVLGIFQKLISSKVNDHFGFDLLDRVFTVFNANILAPYINHIFFLLLSRLKNSRTERFVLRCTIFFFFVASEQTGTCGPDNLIQGVDAVQSGVFGQLMTSIILPQAQKLALPLDRKISALGLLRLLTCDLVLAPDAIYENLIIPLLTCILKLFEMPIEQAQTDADEELFMDEIDADSMSFQASFSRLATTGGKRVDPFPQITDLKQYCATEMNLANRNMGGRLSQIISTHLPGDGQSVLQSYGYVI O13672 RL8_SCHPO MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 33; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC29A3.04; STRAND 69..71; /evidence="ECO:0007829|PDB:8ETC"; STRAND 133..135; /evidence="ECO:0007829|PDB:8ETC"; STRAND 149..154; /evidence="ECO:0007829|PDB:8EUY"; STRAND 177..181; /evidence="ECO:0007829|PDB:8EUY"; STRAND 196..200; /evidence="ECO:0007829|PDB:8EUY"; STRAND 224..228; /evidence="ECO:0007829|PDB:8EUY" HELIX 54..66; /evidence="ECO:0007829|PDB:8ETC"; HELIX 73..76; /evidence="ECO:0007829|PDB:8EUY"; HELIX 77..79; /evidence="ECO:0007829|PDB:8EUY"; HELIX 84..94; /evidence="ECO:0007829|PDB:8EUY"; HELIX 95..97; /evidence="ECO:0007829|PDB:8EV3"; HELIX 102..118; /evidence="ECO:0007829|PDB:8EUY"; HELIX 136..144; /evidence="ECO:0007829|PDB:8EUY"; HELIX 160..162; /evidence="ECO:0007829|PDB:8EUY"; HELIX 166..172; /evidence="ECO:0007829|PDB:8EUY"; HELIX 184..189; /evidence="ECO:0007829|PDB:8EUY"; HELIX 205..207; /evidence="ECO:0007829|PDB:8EUY"; HELIX 208..221; /evidence="ECO:0007829|PDB:8EUY"; HELIX 229..231; /evidence="ECO:0007829|PDB:8EUY" TURN 163..165; /evidence="ECO:0007829|PDB:8EUY" CHAIN 2..259; /note="Large ribosomal subunit protein eL8"; /id="PRO_0000136759" MAPKSKKVAPSPFAQPKAAKTTKNPLFVSRPRSFGIGQDIQPKRDLSRFVKWPEYIRLQRRRKILNLRLKVPPAIAQFQKTLDKNTATQVFKLLNKYRPETAAEKKQRLVAEAEAVANGKSAQDVSKKPYNVKYGLNHVVALIEAKKAKLVLIASDVDPIELVVFLPALCKKMGVPYAIVKNKARLGTVIHQKTAAVLAVTEVREEDKNELASIVSAVDANFSAKYDESRRKWGGGIMGGKTQALLAKRAKAAAATVRL O13683 YDY2_SCHPO SPAC11E3.02c; CHAIN 1..1237; /note="Uncharacterized protein C11E3.02c"; /id="PRO_0000116677" MNCRRKPLPLHSNEVQAAESISKDELYSWTLKNVLILFLVQYRASTPSALQTSSFSTPVEKKTNGAFSGSLFSAKEKKDNPKYPKDFIKYLSLALESISMGKEPEYQDQLIRGCFAAFYNNINKSHISKQLKDSRKIEDMFLIFASSVSSELTKRLGTAYDSNLADRITASFIELCKRVTLKGQLASPSSEFVSHLDMYHSKLLNKSEILSTKRVNRGQDQFDLSSFPLLKVFSSVFKVAYSKALLDAEKLFPSIDEAAIAEDIGILIEDLESDACKFSHSVVDFSNYKSYSTWKARELQTLEQHRKIMLSLIPLSSSPNHPIQPIGFPASRKTPTYVPPIARPYFRQLLSLCLEYRLQVTDPVEVKQINTFIRECSIYWRILPSTRCALSMDFAREHLQKGLITSADVLTHFGELHKSLKEWEITYWPKIDVSIFSSALFGIRNALAQLLKKSLLDLLHEKKADFHRWLNIMSICVEDGKVINQDLSPKSEISSVALALQEHCKVIFDEEFDLSKLPSSNFLDEIILASNRISVRIKFLERNCSECIYGVLSLPQIFINIVLPNYIRAALVVAKEYLREKANADINDLTKDMLEIYSDLKQMIHVLQEYHNEEYRIGSFEGFFQPFIDSWLDNVEASAEQWFLRSLEKDNFDENSSEGQYSSSIVDLFHAFHQAFRTLEGFEWEDDLANARFFTRFFRVIYIVLSKYTQWTTQKFFEEANKQDDTSEVQNDNSSSWFSKARNILSGSNEVLPFRFSPTMCILLNNIHFAMHAYEELEQKIDLQRLIEALDVAESTKRHKISATNYLYTIKVVRGEGLHPDGAGKIRTSYIVLTDNKGRRIGKTRPIHSMNPRWDDTFEVKTKDALMITANLWSKGKFNDHEIFGRSSFTLSPKIYGDYLPREEWFDLNPHGELLLRIEMEGEREHIGFYVGRTYHDLERAQREMIKFIVNKMEPVINQNLSTATLKKLLSANTWMDLDKTMTSVTSLLNRTGFSSKSSENVKKEGELTDVQIEAAIYELLDYFDLNFSIIAKHLTKDVFVTVMSYVWDEVVCTTEELLLPPVSVKPINRKPLSPAQMAIVYRWLQFLKDYFYANGEGVKLPVLETDHYKELLRVQEYYDKPTDFLLQECDKIASQLYLSSRMVNNEPVESLPRHSRIKFANKEIYRSGTIRKVHIQTNESELERNERIILRILRMRADSKRFLSKHFQRKGRLLMADAMRNGYVMPLGHLKKLDSR O13698 FABD_SCHPO CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC11G7.05c; CHAIN ?..318; /note="Malonyl CoA-acyl carrier protein transacylase, mitochondrial"; /id="PRO_0000314111" MSAILFPGQGVDWKTWMQPYLENNIVQNTLKEAENVTEIEIRKYIVEAEAKSNLRQPITTIAQPAILACSIALLRAFPPFTKKFRFYVGHSLGEYSAFVASQTLSFSSALKLVQARAKAMSYASALCQNPTSMLAITLTSRFPTDNFLNTVYSAVQKYRLIDIANVNSDRQIVLSGDKKELESITSTLSELVRSLGKLRSNWLDVSGAFHSRYMLPARDSLKNALGETEFNISPELCYTDSGKRFLPIISNVTAELYPADEEDIRRQLLLQCFRPVLFKNCLKTVKSKYGANLFYAYGPGTTMQSIAKQNGISTKSRP O13703 VTA1_SCHPO SPAC13F5.04c; CHAIN 1..389; /note="Vacuolar protein sorting-associated protein vts1"; /id="PRO_0000372360" MIQIDTIPKELQSIQPFVRRFNELEAHNPVIAYWSLYWAAQMALSSSHGVSNECKDFLLSLIEHLEDLRKNLGENENVSDETSAKAYVESFSLEVLVQAERNSKNGKPDVQAYLAARDFLELSRIWGPPTEQITKSIKFCKLRALQVANPQRKAKTPSNHATEELQQSSTNSTTLPTQEAAVETNASASHETSFALPTTSPAASLSISPTKSAAVSSEPNVEADVKSLSSTPAAPQLNSPSHSYEPTTFPSTTSITENLPTIDPTRSTRSSSHIQSLSPESKQTSDGHRPPSPTSITTTSTSIDPSVAFSSKSTLATTRTNAPLSRPSQPTKASPLNKFSALEAIQSARSHARYAYSALDYEDTTTAIHHLKSALKLLEEEEQGNHTAD O13726 YDO6_SCHPO MOD_RES 515; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC15A10.06; CHAIN 1..567; /note="Uncharacterized Na(+)/H(+) antiporter C15A10.06"; /id="PRO_0000317232" MLDTILINVFRRDGDDDDDDGQDPALQELYSSWALFILLVLLIGALLTSYYVQSKKIRAIHETVISVFVGMVVGLIIRVSPGLIIQNMVSFHSTYFFNVLLPPIILNSGYELHQSNFFRNIGTILTFAFAGTFISAVTLGVLVYIFSFLNFENLSMTFVEALSMGATLSATDPVTVLAIFNSYKVDQKLYTIIFGESILNDAVAIVMFETLQQFQGKTLHFFTLFSGIGIFIITFFISLLIGVSIGLITALLLKYSYLRRYPSIESCIILLMAYTSYFFSNGCHMSGVVSLLFCGITLKHYAFFNMSYKAKLSTKYVFRVLAQLSENFIFIYLGMSLFTQVDLVYKPIFILITTVAVTASRYMNVFPLSNLLNKFHRQRNGNLIDHIPYSYQMMLFWAGLRGAVGVALAAGFEGENAQTLRATTLVVVVLTLIIFGGTTARMLEILHIETGVAADVDSDTEIGMLPWQQSPEFDLENSAMELSDASAEPVVVDQQFTTEHFDEGNIAPTLSKKVSSTFEQYQRAAGAFNQFFHSSRDDQAQWLTRFDEEVIKPVLLERDNLKNGTKK O13729 PUN1_SCHPO SPAC15A10.09c; CHAIN 1..288; /note="SUR7 family protein pun1"; /id="PRO_0000116645" CARBOHYD 33; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 50; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 59; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 66; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 122; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 153; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 160; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGMGFNPIKALFTGIGTVCVGVGALLSILCIINQTQHNIAFQNIYFIQLNTTSIFSVANQTAVVNNTSNLLNELTGTLVDTLETYIDQGATDLIEQVEQEMKDVSELPDWYSIGLWNYCQGNSSDYTNPTYCSTPSPSYYFNPLTMLETSINNATGSQINITLPSEVDLGLKVLKGACYAMRAMYILGFIFFALTIVSIVISCLPFFGPLFLNVFSFFATIFTFIAAVIAVATYRIAISELEKNIEILNIPIVLGKKIYAYSFLSAAAGLAACILYFIGNLTSGYSPL O13737 MPO1_SCHPO CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyhexadecanoate + O2 = CO2 + H2O + pentadecanoate; Xref=Rhea:RHEA:62404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:75927, ChEBI:CHEBI:78795; EC=1.14.18.12; Evidence={ECO:0000250|UniProtKB:P25338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62405; Evidence={ECO:0000250|UniProtKB:P25338}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P25338}; SPAC16E8.02; CHAIN 1..222; /note="2-hydroxy-palmitic acid dioxygenase mpo1"; /id="PRO_0000372356" MTYLSRSYSFYAAYHSNPVNIKIHQVCIPLLLLTALVLLHNFVITLINSKLQINVAHLVGLAYQIFYVTLDPLDGLLYSPVLYLFSYILPSKLFTIFSRSLVNRSAAVVHVICWILQFIGHGVFEKRKPALLDNLIQSLFIAPLFAFLETGPFVGYYPSVVSKIRANIKLKDVGENYPNLSEFLFPPSMVEDAVSGVVEDASQLSYCIRPLRLSDIDDGIVF O13738 GNA1_SCHPO BINDING 33..36; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P43577"; BINDING 45..47; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P43577"; BINDING 47..49; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:P43577"; BINDING 55..60; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000255"; BINDING 76..77; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P43577"; BINDING 81; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P43577"; BINDING 90..92; /ligand="acetyl-CoA"; /ligand_id="ChEBI:CHEBI:57288"; /evidence="ECO:0000250|UniProtKB:P43577" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4; Evidence={ECO:0000250|UniProtKB:P43577}; SPAC16E8.03; CHAIN 1..111; /note="Glucosamine 6-phosphate N-acetyltransferase"; /id="PRO_0000074558" MKKDFHSTYYIIVVEDLESHHVIGTATLFLERKFLRGKGICGHIEEVIVHPDHQRKAIGKLMVLTLIKLAFSLNSYKVILDCSDSNVGFYEKCGLSRAGIEMKKYASHSII O13739 CHMU_SCHPO BINDING 74; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 75; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 134; /ligand="L-tryptophan"; /ligand_id="ChEBI:CHEBI:57912"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 134; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 136; /ligand="L-tryptophan"; /ligand_id="ChEBI:CHEBI:57912"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 136; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 137; /ligand="L-tryptophan"; /ligand_id="ChEBI:CHEBI:57912"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178"; BINDING 137; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /ligand_note="allosteric effector"; /evidence="ECO:0000250|UniProtKB:P32178" CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000250|UniProtKB:P32178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000250|UniProtKB:P32178}; SPAC16E8.04c; CHAIN 1..251; /note="Chorismate mutase"; /id="PRO_0000119205" MSLVNEKLKLENIRSALIRQEDTIIFNFLERAQFPRNEKVYKSGKEGCLNLENYDGSFLNYLLHEEEKVYALVRRYASPEEYPFTDNLPEPILPKFSGKFPLHPNNVNVNSEILEYYINEIVPKISSPGDDFDNYGSTVVCDIRCLQSLSRRIHYGKFVAEAKYLANPEKYKKLILARDIKGIENEIVDAAQEERVLKRLHYKALNYGRDAADPTKPSDRINADCVASIYKDYVIPMTKKVEVDYLLARLL O13741 NOP12_SCHPO MOD_RES 94; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 95; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16E8.06c; CHAIN 1..438; /note="Nucleolar protein 12"; /id="PRO_0000081673" MGETNSSLDNENTSFVGKLSSSSNVDPTLNLLFSQSKPIPKPVAKETTVLTKKDVEVEEANGVEEAAETIESDTKEVQNIKPKSKKKKKKLNDSSDDIEGKYFEELLAEEDEEKDKDSAGLINDEEDKSPAKQSVLEERTSQEDVKSEREVAEKLANELEKSDKTVFVNNLPARVVTNKGDYKDLTKHFRQFGAVDSIRFRSLAFSEAIPRKVAFFEKKFHSERDTVNAYIVFRDSSSARSALSLNGTMFMDRHLRVDSVSHPMPQDTKRCVFVGNLAFEAEEEPLWRYFGDCGSIDYVRIVRDPKTNLGKGFAYIQFKDTMGVDKALLLNEKKMPEGRTLRIMRAKSTKPKSITRSKRGDEKTRTLQGRARKLIGKAGNALLQQELALEGHRAKPGENPLAKKKVNKKRKERAAQWRNKKAESVGKKQKTAAGKKDK O13742 VPP1_SCHPO SPAC16E8.07c; CHAIN 1..831; /note="V-type proton ATPase subunit a"; /id="PRO_0000119223" MSPSLFRSEEVSLVQLYLPTESARPIMSALGELSTIHFKDLNPDVVAFQRSFVREIRRLTDTERLLRYLHSEIDLNGIHVPDHNLPPSYESVLESSTIEDIIERITRLEARVRQLVESSQLLEARYLQQLEFANVLTKADAFFSKSGNTVDPLRNNYETSSIFSGEDDTTAPLIENALELGTTGTFDSEETSPQMNTTLDFVSGIIPTVKFQFLERILWRTLRGNLFIHQVRADDSLIHGAEKNEEKTIFLVIAHGTQILLRIRKISESLGATLFPVEEDAPGRTSQIQQANVSISDLNAVLENTRSALYTELTFIAEHISAWEAVLHKDKTVFQVMNLFNYDQNHKCLIAEGWCPTANLPMVQKTLRNISDLTDSQAPTILNVVHTSEQPPTYFRVNKFTEGFQSIIDSYGIATYREVNHGIVAIVTFPFLFAIMFGDLGHGAIMASVALMFVLYEKTLGAKKDLDEIVGMVFYGRYIVLLMGLFSMYVGFVYNDLFSKPMSIFSSRWVWPVKSEEAIARAVQVGTYPIGIDPTWHSADNNLLFMNSYKMKLSIILGVIHMTFCLFLSLSNYRFFKRKLDIYAVFVPSLIFLEAIFGYLVITIVYKWCIDWKAKDLQPPSLLNMLILMFLSPGTLEDQLYPGQKYLQVGLVIAALICVPWLLIVKPFVLWRRHSNEENKYQSLNSDLPNVDEADALMAVDSQEKQAEPFELGEVVIHQVIHTIEFCLGCVSHTASYLRLWALSLAHNQLSSVLWNMTLANGFRMTGIVGSIFVVILFGFWFIATCVVLVAMEGTSAMLHSLRLHWVEGMSKHFEGEGYAFTPFTFKVTAE O13744 RT07_SCHPO TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 157; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16E8.10c; CHAIN 40..259; /note="Small ribosomal subunit protein uS7m"; /id="PRO_0000310442" MLRLIKQPLFRCASSGHLMKESLVFIHQTRTFQVGKFTSNEKYNEKIEDINERSNPQWDNAGLENLLNQLQDSVEQSASDDFMGELEKKIEVENEEPPLMGTNLWPSPSSSIVGLIDRPFQVDSTVQHLVNLIMRDGKKAKAEKIVATALSIIQKETGENPIDVLKQAIAEISPLMKLVSAKRFNKSVEFPMPLKERQRRRIALQWILGECKSSSPKRLSDRIVKEIIAIRSKTSNCFKKKDHLHRMCLVNRGNAPVRI O13748 NTM1_SCHPO BINDING 64; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 69; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 111..112; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 127; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54712, Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13971, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138057, ChEBI:CHEBI:138315; EC=2.1.1.244; CATALYTIC ACTIVITY: Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54724, Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13973, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138061, ChEBI:CHEBI:138317; EC=2.1.1.244; CATALYTIC ACTIVITY: Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54736, Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138059, ChEBI:CHEBI:138318; EC=2.1.1.244; SPAC16E8.14c; CHAIN 1..219; /note="Alpha N-terminal protein methyltransferase 1"; /id="PRO_0000119291" MDPEKFYSDAIDYWNGVQPTVDGMLGGLGTGRIPQTDVVGSRTFLNRLNYRIGKIENLVAADCGAGIGRVTENVLLKIASHVDLVEPVENFISTAKKQLATKPCSFINVGLQNWTPEKNRYGLIWNQWCLSHLTDEDLIAYLSRCCEAIQEKGVICVKENVSSFEDTFDPIDSSVTRCEQSLKSLFKKANLVVVAETLQHGFPEELFPVKMYALVPHSS O13749 TF2B_SCHPO BINDING 20; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"; BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"; BINDING 41; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" SPAC16E8.16; CHAIN 1..340; /note="Transcription initiation factor IIB"; /id="PRO_0000119307" MNAPSFTGLPTSMLSVKMICSECREDPPNLVEEFSSGDTVCGSCGLVLGDRIIDTRSEWRTFSNSDEASGDPSRVGKVANPLLNGSQLDTTISSYDGAGAMLAKAQGRSVQVRGEKNLLTAYKEIGAMCDAISLPKVIADTAKQLYKRVDDHKALKGKSSQSIIAACIYIACRQGKVPRTFMEICTLTNVPKKEIGRVYKTLQRMLTEGGALHNSVDALKGHEYIQSSSTSAEDLMVRFCNRLMLPMSVQSAAAELARRAGLQGTLAGRSPISIAASGIYMISALMGYPKTPKEISEVTGVSDSTIRIAYKLLHAERKELIDPKWIANKAGNMDAMLPKP O13750 SUCA_SCHPO ACT_SITE 285; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222" BINDING 49..52; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222"; BINDING 75; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222"; BINDING 128..130; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222"; BINDING 192; /ligand="substrate"; /ligand_note="ligand shared with subunit beta"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222" CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_03222}; TRANSIT 1..22; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222" SPAC16E8.17c; CHAIN 23..331; /note="Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial"; /evidence="ECO:0000255|HAMAP-Rule:MF_03222"; /id="PRO_0000033350" MFKTQTTLLTSLRRFSSSSQLKNSKSLYEQTIPNLMINSDTKVIFQGFTGKQGTFHAQHAMDYGTKVVGGTNPKKAGTTHLGKPVFGTIEEAMKETKADASAVFVPPPLAAGAIEEAIAAEVPLIVAITEGIPQHDMLRVSDILKTQSKSRLVGPNCPGIIRPGQCKIGIMPSHIHKPGCIGIVSRSGTLTYEAVNQTTQTDLGQSLVIGIGGDPFPGTNFIDALKLFLDDPNTQGIILIGEIGGSAEEDAAEFIRAANASRSTPKPVVSFIAGATAPKGRRMGHAGAIVAGGKGTAAAKFEALEAAGVRISRSPATLGSLIVEELNKLKH O13753 VA0D_SCHPO SPAC17A2.03c; CHAIN 1..343; /note="V-type proton ATPase subunit d"; /id="PRO_0000119359" MDALSFNTNSGYIEALVRGYESALLEQHIYSNLSQCESLEDFRLQLSSTDYGGFLANQSKLTSSIISAKATEKLLDEFDLIRRQADETLSKFMDYITYAYMIDNIMLLLTGTVNGQDTHDLLERCHPLGWFETLPALCVATNVEELYSVVLIETPLAPYFKDCLSADDLDEQHIEIIRNTLYKAYLEDFYNFCKKIGACTADTMLPILEFEADRRAITITINSFGTELSKEERAKMYPSFGRLYPFSTSILARAENAGDVENACSLVKEYSDFFDQNSQKSLDDHFNEKEVELNKLAFLQQFHYGIVYAFLKLREQEIRNLTWIAECISQNQRDRALNIVPIL O13754 CNS1_SCHPO SPAC17A2.04c; CHAIN 1..358; /note="Hsp70/Hsp90 co-chaperone cns1"; /id="PRO_0000363376" MAGFQSSEVDPNTKNKNAEEMFNELNKVPFFMQSLEDVGDESENNVQLDALKALAYEGEPHEVAQNFREHGNECFASKRYKDAEEFYTKALAQKCGDKDIEIACYSNRAACNLLFENYRQVLNDCAQVLQRDSTHAKAYYRSAKALVALKRYDEAKECIRLCSLVHPNDPAILALSKELQKKSDDFEKRESEKKRVAQEKVIAAKTVLLALQERHIKTKTTEHPPDLGDAMISLSTFDDPKSELFFPTILLYPLVYQSDFVPSVSENCTPLELLKTVFQSPAPWDVHQLYNPDSLDVFATTDTLGLIKVGKNVPILKALTHPKVTLIDGLVQLHVVPHHLASDWISSWKKNKQENAKN O13756 VPS8_SCHPO SPAC17A2.06c; CHAIN 1..1272; /note="Vacuolar protein sorting-associated protein 8"; /id="PRO_0000372426" MQSKYGRSSLKIKNGDDTRTLRALSFSKDSVNSSSFDNEAASTTLGISTAIHASNRPFRQDEYSWNDCWMRWGQLRRVSSQLRELRFTMNDQPATVTSIAYQGTLLVAGTSSGHVLLNDWRTNDFQILKPGLSSNESVTLPVTSLAISNSKRIVCQGHAGGIIFVWDVSRKPPLQLFTINQHSEDSVLTHLVFNGNSDDVLLSTDHLGKIAVHEFYNLVINKHCTSWNLDMSKSNSLNLDSIIVDTSSISFEELHITGVKHFSFVVLQSLQSIQIVTLFPKTTLIYEFKYPAGIVSSACHSFSSSIVHKNGENTKLHAFFATAYNNNLRLYSVTFHKGYMSLQLMDRKKFAKAIWKLWWFPSSSIIIILFDDMELAFVNSMSLDIIGTSTILDKSLLRWDWYSNSLAAIGVSQTVFPFISSSLCISPRYMFVVNSETVSVGSFLMVSEQLQMLSERYGFFDSIKFGSYCVSNLSIFPKLLLEKTSVINLIMALYVKLLKSLARDFPARSPFEATSQKTNDYELEVQHLFTWTCELYSENFNTVISSFIIANSLGILPEIIEQIIPVFTRVGKVYVVLEALFDLILSQRFTNPSPQLQHHILNYLNDCKRLQDMDKLIPCIEYQSLDLDFITKFSRSKGLFDSLCYVSIYAFNDYSIPLVQFLNLLKSDIDSPSEETSINVEKGFHFLLYSLTGMKYPLGHSNNINDAYVVIHTLLKVIFSVVPLPFDVPVDNSVDFPYLRLFLEKHADDFFRCLEVAFDYPYFSLEKVTIAKKLLDTVNRQWILECISQLYEKKKSVSQSYYIFVSHVTANYSNQLLFSQSFYQGILDGLCNIDVPDDKREVVEAAIEELLTVYEHFDIATTLLSCWDHQLYQVILHISFKCGRYEDYIEAILALWKQKGQKHSFVSESSEALISLVFNNLQTINRFPGHRERYVSTLISHCGDLFAINHVCFVRNSLKYLLDDFTKVITKTFSIKSIRLQFLSLIIYEITYEQLSSWYRERTILSFLELVSFDQGDVKMLELLRLHPKLVRLQGLMEILNKNDCIESCIFVYRELAEYKLALSHVSKYIEKSMSVFDLEKSDDMTSRRIERLCLHLKTVVPLFEQCTKEVSAEDVTNFWLELVFTLLLVYIKLSLKGSINSQITFKDFQQELSLCIENLLDSFLSKTNSYKIALNTVLVRICEEASRNEHSDQYLRKLLLKLITDLYINHDITKECFLLWDMKQFYEIRSTLLQNASGVLVEDPKLQKNAKGQYTSKLKVYFSGLIEREDL O13764 PEX6_SCHPO BINDING 695..702; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P33760}; SPAC17A5.01; CHAIN 1..948; /note="Peroxisomal ATPase pex6"; /id="PRO_0000084619" MENRICTLAKPLPKLDESKQAWVSYLWLKKALPGFEEHSAYVYMTTNPTIAGRIFLPINNEDLEDGTVEISGYDNLLADALYISTIAPVKLDFVQLIVIDDNSQDQDAIIERIKGRNAILMESDFINQNILVQVCQPVRHGVVDSETKFVIERKDSFTFLASNEKNISSFKRGKTETDAELVIRPSKVHTEIQWCLQNCSLIHVPFELLFNVGKKNGCPISLRLSDGKNVYGIASIKSDTEHDSVQLSPSLHYFDEFNESVISEEGTEAFLVARGPSVGIASRISLRTIPTQSCFSEKLLKAANLCVVQQVKQKVFLQSKQIFCVPINSLMANSDSVDILELTRNTDAYIWYSVEEIDPLNTYNIYYTNEDTSIVLDTQLSHRLLPSLRKPLLNFVKVHPPSQKLLRFCRAFFDPQQVPGFNPFFLLHGNPFTGKTKAVEEVASLFSAPVFTISSYEFADATADHLEAKLDMFVQNVVKSPCAIIFVKDLDVLSISSDEGNIVPGSKSIQILLSKIDLVKSPQGRYIVIGTCHSIEKIPYEILSESFFELKFSELEMDERLELLKIYANNVIIDKRISLKDVALKTNSMSFGELECLPDHMTKAAVDRIKRTGYDNDSIILSGPIITEQDVDVSINRIRKEKSNTIFTVPKVNWDDIGGLEEAKTVLRDTLQLPLQFPELFSQGLKPRSGVLLYGPPGTGKTLLAKAVATELSLEFVSIKGPELLNMYVGESEANVRNVFEKARNSSPCVIFFDELDSIAPHRGNSSDSGNVMDRVVSQLLAELDSISKDNNKYVFVIGATNRPDLLDPSLLRPGRFDKLVYLGINKSEESKASMLRALTKTFKLDETIDLNEIAKNCHPNFTGADMYALCSDAVLSAIKRKTNEIDLLIQASGTDLSTEEFFKRNENQDSLELRITKEDFLTSLKKLRPSISEQELHRYEMVRHQFS O13765 DBR1_SCHPO BINDING 23; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:C4M1P9"; BINDING 25; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:C4M1P9"; BINDING 48; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:C4M1P9"; BINDING 93; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:C4M1P9"; BINDING 183; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:C4M1P9"; BINDING 235; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:C4M1P9"; BINDING 237; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:C4M1P9" COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P24309}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P24309}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P24309}; Note=Binds 2 divalent metal cations. {ECO:0000250|UniProtKB:P24309}; SPAC17A5.02c; CHAIN 1..478; /note="Lariat debranching enzyme"; /id="PRO_0000079796" MSYFARLKPPPAFLKMRVGVQGCCHGILDNLYILAEKRKVDLLIIGGDFQALRNVSDYHGISMPPKFKRLGDFFNYYNGRNKAPILTIFVGGNHEASNYLDELPYGGWVAPNIYYMGRSSVINVGGLRIAGISGIYSAMDYKKGRYEGLPYNYKMLKSIYHTREFDVLSLKSLQKPIDIFLSHDWPRGIEQHGDVAKLLRHKPFFRNEVERNDLGSPALEELLVELKPRYWMAAHLHTKFTAVVHHNSQEDDGKLSCSSKDVTSSGFSMKGLNEPSQERLPVEKEQNDKSDEEGSNNEQEEKQDKKQSTNRDLCRKESCKKEPSLSSSDQVTKFLALDKCLPRRSYFEVVEIEPVEIPDSGAPYMQYDSEWLSVLRAMHPFQSHTIEQDPPLPSLEVVKTLKRKEEIWVDENLVKKDKLGIPRNFCQTAPPHSRDITENMQPSSYINPQTVAFEILIGLKERTVDSPPPVKNPNEIVL O13770 YE98_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC17A5.08; CHAIN 21..210; /note="Uncharacterized membrane protein C17A5.08"; /id="PRO_0000010415" CARBOHYD 165; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRVITLSGITLFLLASLASAIELTFKLENQEKQCYYLDSFHTGEKTHFTYAVQSGGSFDVDYMIKAPSQKTVALGKKRRQADVFFTLEEKGEYEFCFDNHMSTFTDKIVTMEITMENELSLPALTRDEAKDYKKDSMQSTVLEISTALSEIDRVQNYFKTREHRNYSTVKSTQARIFWFSLAESIMVVALSALQVFIVKTFFKRSGRRGV O13773 UCP7_SCHPO SPAC17A5.12; CHAIN 1..697; /note="UBA domain-containing protein 7"; /id="PRO_0000071158" MDDLLDFNFYDKSTPSNQNNYSNNNSRTPSYSLPAPVAQKKNAQIPLKASKPEDPFANLFQKKTDNKISLKELERQKVGTPDSNSTPKSSNYDPFENLEILHQLSNTPRDKDAVIHDKIEENKRPISQPQVSASEKVTLKDLSLEPHQPVSLPAFENIGSETSIPFENHNEITNMNTAKDKLSSNEMYEKLRDLGFSDDQSRLALENSGSLEDAIEYILEKDNAKGQYREGEAYEAFSDSSAKTQFSDFQALSNQLKSQLFEKANDLWNIGRKKLRDAVEERRAVKDPSKPRWMDASHDFGREATPEILPKTPIPKRKPHKVPMNEKVSEDRITTNQSRSGNDESSLVDFLTSKSDNSSFNFPSDTYEGTENILETAYESTTARQVNNNKPGKSTVKKREEETLNNMVSALVEEQQSTGNELFRKGDFSQAIEEFTNSLSQLPAKHTKRVPLLSNRSLCYQKVGDLKTCLQDVDELVDIIGEEKGHGESIRDKSMNDYYVKNMVRKAQVLEQLEKYQESLNIWKDLIADGQISKLYIDGKHRCEAAISSHSSESHSKRTTQQPKSTPNHTNIKVKSERLQHVRMAQQKAEQLDEERSRLREPVQQIVNKWKEGKESNLRALLASLDTILWPECRWQKVSLSELVLPKKVKIAYMKAVSRVHPDKLPQQTSVEHQLIAESAFSILNHAWELFKQQNDL O13776 FT105_SCHPO SPAC17A5.16; CHAIN 1..925; /note="Ubp5-interacting protein ftp105"; /id="PRO_0000116710" MGGQESKLAFQRGIARLASQPDIPLDDEVWVSLWSVPESCPEVYDFFPPGLIREMRDHAFVNLEKLLLVLTSRLFALKNDKKFPNPETAPASEALNCIRLLTRIIPFLNEKLDLEEWHQKFWWSLRKKRNLPKENSELDLSNFQDDLDFENSISQKNEFSQKSPSVPLSPVSTFPASSISLDASSDVSAADVSVGGSSTIKEIGSIEETFTHEKTLMEELLDTVFRLLFCRGFTLPLSSPEQYAYIIWENGIGTTETQEKTTKELAFNRIEVLRLLLVLISKRLYRSSEVASHTLTYLTCVANKQLILVFLYSLINTTLRLRPDSWKASYSTLVPYNDSSIALSKLTSQILLLFLDHTPHETTVEYFRQRLNLSPGAAIENQYRLYFSRLQLQADYEFLVNELYRLLNAPVSAISAYISIVQKPNIAFPEIILFLWQAILYNKRFRAFLITSPYATEFLTSIQFYALRYREDNEHSGLVRICLFIVHYLSCEKVLCEKLNRNCMNAQSLMSSLGFSVPPMSYAEFLIISSFHISAVKRSPFSSLSPVILLTICNIAPFVENLSFVTCAKLMQLCSSLSSPRFLFRNPRNHLLLEYLLQAISSIVENKFSQNPNLSYSIIRLQQVFLNLNSMKLPAVAQTKSQPLVALNSEGSSDFESKSSDNTSLDGTPLQNTDFKKVATVEDDSPFDELDKFSSPFSSSSSRGGLSHISSRNVSISVPTVLQDVFSDSPLVLSRKLRGKIPENVSSSELIKKCASNPFGKDLEIDSNLFAPSNSWFNSWHSRLELDSILAIISQFSLPVYKKMNEELSTTDEAVKLLANSVLNDVHPRVPNFRYFIWSVPMNNWFQSLVWLYTLSFDEKGLMATPSLFTTSKVYKQHGNIMKVASPENSSNSMENATKSILDKLDLLYLQLPSSVNHDSSLRNK O13779 YF2E_SCHPO MOD_RES 105; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 152; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 226; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 241; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A2.14; CHAIN 1..617; /note="Putative metal ion transporter C17A12.14"; /id="PRO_0000201538" MPSNTSRSVPTGFYYKQNARMQNRPRFSDRKHSSKSKHRFPVDPSLQPDEADEGTRLLGNSDSDLLEPPSEHSSNGEDDKDINNPPSMPSSVCSSPKSPHRHYESDEDIENISLPESHPEDIQRKEFETENGKNTRDQPSPLAEVSDFAISSPHVYPKSANSHDSHYEQFANNDVTESAVDDHPATRKLSRDELYLPISPNNAQEPKFSVLDEWTKKMVANFEEYSVEDVDKRRERNRKLSEPLLVNGRYRVRDRWAQFRKSEIEKPYRFTFFTDELPSTIHSHEMWELVHDGQSFEDLFHSGGTWWLDVSCPKEEEIRVLAKAFGIHPLTVEDITLEEDREKVELFRTYYFVTFRSFNQLPSNSEYLKPLNFYLVVFRDGIITFHMNPTPHPANVRRRIRQLNGYLTVNADWIAYALLDDTTDAFAPFIEQIEDEVDTIDSMILSIHYDHVMEVKPQERMLQRVGECRKLIMSLLRLLANKADVVRGLSKRCNESWQVAPRGEIALYLGDVQDHIVTMVQNLNHYEKILSRSHSNYLAQISINMTLVSNETNEVLSRLTILGTILIPLNLVTGLWGMNVKVPGQDVPGLGWFFSILGSLMIFAISSFILCKWYKVI O13780 YEO2_SCHPO SPAC17G6.02c; CHAIN 1..324; /note="Uncharacterized protein C17G6.02c"; /id="PRO_0000116726" MYYDNAFGYIPAHWVTILAVILFSIAFILHVACLAFTRKWLVIVPIIGTIGELAGWACRLDASYNPDDYNAFLGQIIALIIAPVFYSAQAYVLFHHIVLLYGPRFSVLSPKLYGGIFITFDIIALILQAAGGGVAGGADSGSQLQTQGSQIMLGGICFQLFTIVVFSILFSIFFIALYTHHPIRPSTGRREPDVPYTRVRTMSCNCLALATFAMVVRSVYRVIELAQGWEGAVITHEVWFDIFDFIPMIFTSALLIPSLYPALERSKLPFTEKHVSSMEYAPSEYGPSEYGPSINDITNMSAVIYPDSFLAPKDPKKSFSSEEL O13784 RS24A_SCHPO MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250" SPAC17G6.06; CHAIN 2..134; /note="Small ribosomal subunit protein eS24A"; /id="PRO_0000137634" MSEAVTIRTRKFMTNRLLQRKQMVVDILHPGKANISKNDLREKLGQMYKTDASAVQAFGLRTHYGGGRTTGFALIYDDVEAMKKFEPHYRLVRVGHAEPIQKVARQQRKQRKNRGKKVFGTGKRLAKRKSKQQD O13786 PEP7_SCHPO BINDING 158; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 161; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 193; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 196; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 281; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 284; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 297; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 300; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 305; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 308; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 324; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 327; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" SPAC17G6.08; CHAIN 1..536; /note="Vacuolar segregation protein pep7"; /id="PRO_0000046857" MQNGKRRIGVRISSNLSNHSGTNLSTSAQSDSSNIVKATECPICGLELPNLSALNDHLDVTHFNDNEKIHKRQDSINSWLTRTLNGASALQMKAAQRLWRMEPYEQNGDSSGAVGLEATKLTDSLVVKNHWQPEVPDMVCHDPMCDKLLNFINGHIHCRKCGYIFCNFHSMYQIKLSIHATYDSENGFWCRVCRECYEGRPGYNDSNGLIRSRFQTFETFRKPLADKRRIEFLRLSKRMKKLEELWTSENVSMLDALLLNKAKRLEQSIVHWQDDSVVQICPECNNSFTLTRRRRHCRLCGRVICRFCVLEISLPQHPQPLLICMSCNQNYFRNVLYQTERSKSLGYIRHIEHLQVFRQAMVNYYRLYEDSLSELLSGEIITEATLKIVKDRRKKFLELCVKYDGTMKKIANHPSSNDAEEQFKQNVVNEAKRYLQETILRLQAIPYHLQVGQAWTSESERELEKKKEQVEKKQEELMQTRIVLEEQVFLVENMIEDAKAKRKFSEVETLLSSLAPLHEEIHSITEKIHDLDLFDI O13787 SEC62_SCHPO SPAC17G6.09; CHAIN 1..273; /note="Translocation protein sec62"; /id="PRO_0000206625" MDSSNVPVLKDEDKCKFSMRFTNFLKSRPELKTKPAILNGKRVYYFRVKRVLRFLTSEAYTPKKYKGFPEISSREEAIEVLKLLIMNSMLVRVDKLPPKQRKQKLVELQINRNQDFQDDMHYVWLYEPLPKRVMALAVLFALVVLALVLFPLWPMFMRKGAWYLSMGGLGVIGLFFVLVILRFFLFCITAVIVRPGIWLFPNLLADVGFCDSFKPLWSWHNSKSEVKKTRKSKKLSKKATSPAASATPEKSSTSTTSLKNLRHRNPTVEEVSE O13789 YEOB_SCHPO SPAC17G6.11c; CHAIN 1..636; /note="Uncharacterized beta-glucan synthesis-associated protein C17G6.11c"; /id="PRO_0000317219" CARBOHYD 291; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 378; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 429; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 464; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 489; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 616; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MYNVRGDLNRKTPSDGNVNEIGSMYASRDTSTSSFTNPTDSSTRLLYNNASNATFSSAALAAGVGGTRASGYTHRFSIRPSSQTYNRYPNGGNSAGSDMYSTSPQNNSIVDDIENINKLEAVAFAGPTAGESDFSLSREDKEIDDFLHYPLPAKDAKKLSYFVGGEGLMQLLFLLFLAAGTGMLFIGLPILTYTGHNSLASTRVTGITNHQFRILRLLRYGSLIDPDTPESAYTFDSQDLGTLDLVFSDEFNYPGRAFYDGDDQFWLATDLHYAATTDYEYYDADTPTTANGTLRLRMDAFYNHDLNFRSGMVTTWNKLCFKGGRIEVSASLGGSPYIPGFWPGIWTIGNLVRPGYLATSDGVWPYSYNSCDAGITPNQSDPSGISYLGGQRLNQCVCKGEDHPNVGTGRGGPEIDALEGTFGSGIPYNGSIYLETMPVVSQSAQYAPFDLYMYPNYDFVTIYNQSVSAMNGWAGGVYQQALSCASQLNNSWLSGNAYQKYGFDYKPGSGPDALISWFVGDEYTWTMRQPAVGQNGNIASRPVSEEPMIVVLNFGISPTWIYFYWYELTFPQTMYVDYVRIYQDSSDSSSVLGCDPEGFPTTEYIANHPKAYLNYNATSWSEAGYVRPKNSLMDGC O13796 RCQ1_SCHPO MOD_RES 56; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 61; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 63; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 110; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 111; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1142.01; CHAIN 1..656; /note="Ribosome quality control complex subunit 1"; /id="PRO_0000116835" MSSRALRKLQRQRQTELLEEALDSESDEDDEFSSTSGKKVVNVFEILEKENNAINSEAEKSVSEEEQDEPLVEGESPIVSTNKKAKNKKKKKKQQKKKKVTGKRDLDNQSSDNEKLEGLESSKNIDDDIDEIEKAAAELKLKYREQDQVEHVAGVEESATIPLDKELDEKLNKLLGVNISMLNPDLEIRKIFGRIVEKRSVNARHDNLRRKRHVLVQPQEGWPPLVRSGLGMKLTGQSQDLECFFEITQSRAYQEVQETFEYYVQTYDPNNLLMLLRSHPFHIDTLLQVSEIIDQQGDHELSAELVARGLYAFDSILHPRFNLATGATRLPFAIPSNRRLFLCIWRYLQSLQSRGCWRTVFEFCKALLQFDMSDPYAIGTCIDIYALRRREFAWIIDFANYLENSNKISDTPNMLYSSALAMFYVHGDTTDTRASMLAAFERAPYMLSELLDTLNISFTKSSIPSPQDPVQELHSAMYALYAKDSWSDPTVLAFINSILEKETVTLHDVEGQFAELTENLSRRVILLNEQSLRKFLPQRILQGTILSFDPLPPDTYLSESQVFGRDISRRIASFLSDYLSRAREVNENEEEPPAHEFDLPPAEQLLQQIESEVGEESEDGTPVMTRLRSFFGSLFTSTNSETEPAEESTEEMGQGD O13797 SGT2_SCHPO SPAC1142.02c; CHAIN 1..317; /note="Small glutamine-rich tetratricopeptide repeat-containing protein 2"; /id="PRO_0000363377" MSSNKVTAAIIDYLKQAITTGSISEEEKESLEVAAQCIQDSFKIKPEEIKPKSGDRLVAAFEEYEKLHPVEEDSTAHVNKEEAEKLKLEGNNAIAAKDYQKALDLYTKAIEIDPTSPVYYSNRAAAYNQLGQFENAVEDALTCLSLDPHHARAFGRLGRAKLSLGDAAAAADAYKKGLDFDPNNEVLKRGLEAANKQLNQPSDSSATSGADQARTSAGAAPDLGSIFGGGMPDLGSLMNNPAVMNMARNLMQSGALNNIMNDPNIANMARNFQSGGGMPDLSSLANNPQLQNLARNFMNNNNNGNTDNNNQGNPPPQ O13810 PROB_SCHPO BINDING 58; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 145; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 157; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 177..178; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 218..224; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; SPAC17H9.13c; CHAIN 1..402; /note="Probable glutamate 5-kinase"; /id="PRO_0000109767" MSPKSKSTNKTYTIVIKLGTSSICDEKTHEPLISNLSLIVETVVKLRKLGHNVVLVSSGGIAMGLRRLDLPKRPSKLSAVQAIAAVGQGRLISLWDTLFTQLRQPIAQVLITRNDIAERSQYVNAANTISELLHFGVVPIVNENDTLSVQEIRFGDNDTLSAITAGMINADYLFLLTDVDCLYTDNPRTNPDAKPILKIHDTSMVNANVSTPGSGVGTGGMKTKLIAADLGTSSGVNVIICRGSKPSSIFDIIRQESSDNKNESVELPLHTHFVAKKQGRIRDRHFWLLHGLKSHGSLEIDRGAFEAITRTNRAGLLPVGVTKVHGHFSAHQAVTVIYNGEEIGRALVNYSSTEIDLIKGKRSKEIASILGYNETEYVAYRDYLVVHGLNSHHDSQVSSDEH O13813 TOM22_SCHPO SPAC17H9.16; CHAIN 1..144; /note="Mitochondrial import receptor subunit tom22"; /id="PRO_0000076112" MVKLEEVVDETEVQNEQQTVIEKDQYIYAQEDVEESDSDESDFEGLEEETIIDRIAALKEIVPVTWRVKIADGAKTATTGLSKLAQFGGKSMWVISTSALLLGVPFMMSLEEEAQLTEYEKQIKDQRGANEVIAPGATSGALPQ O13814 MDM10_SCHPO SPAC17H9.17c; CHAIN 1..370; /note="Mitochondrial distribution and morphology protein 10"; /id="PRO_0000372307" MMSFNDYIFYEYLKKTNWNIHNLYCNLTQTADNILNFEIPSGVSCQLSSLTSSNFASGCKISAMPILNGSMSYVYTNVNLENLNRNITYNLQHFYEGYKHVDVPFVHYVNEFQDKKLPLRPTLLYGRMHLPSQHLDAIFATRLSPWLLFFIQGVNEIEDGVGDNLCFNWQYDTGKRCLEFVYESSGAMLGVRGLWNLNYRELNTKINMENKAPSNMRWSLGFETYYGVLTKCAGASLGMRLHSGPSHPYAPFILTCTLNPIVGHITSTFSTAEPRTKAFSAQYDFNIYSYESQLKLGIELWRSKQEMSQSTNDPTANSMSSLLKGTCSTSGDVSISWQARIRNFLLTIGTEAQLTKIDPLFFGVHFEYSK O13817 SEC7C_SCHPO SPAC19A8.01c; CHAIN 1..1082; /note="Protein transport protein sec73"; /id="PRO_0000120217" MTFRIPSSQESSNKSEKDTTVNSPNASSFSSFFKKSSQTYLSKRSEKLNEHNSKLKSSGSFTSNSQTDLSNSPSSKKKNIFYPIARAKHSFYFNHNWSSDLQQANSPVASYSSQSVSNDSNFPKDVTSPISTDLSGSNPSLKSPSSINSAKLRASRSFFRFPKWSRKSWNPDVNSTTSSPSEVGSLDKAGGPLNQQNENLSAESDNTILQNGTRKSSVKMSDLGKRIASLPVVKRPPIQFSISSDYIKPVDKSDQTSNVPSPSSSVGSLRLYRSPSIPNDVEQPQPQSSRSRPRSSTIPTQRTLERLRENRSSIFSFRTLRRDDDECVAQTIENSALFSDIKPNPTKFLSSVPELTADDTAESYLSKLRETVPYSRMIPVLAEKDHVTLNKALHLCMSGMEFENRPLDFCLRLFLLKSHLPKETQQIDRVINAFSKRYFECNPGMFSSQDQCYILVFSLMMLHTDVFNSNNKHKMTKQEFINLCDIDELAPEIMEYYYDNITFTPFVNLDDELLLIEKEKNEKYNFTSRKRLGLSPYTFTLENQLNISRPEISLSYDGKFISPGIKDIASLLNVRKLISSPAIIQLVSKRSHPMAFSNHFIGLPDNADPGLVDFSISMLGILPRCEKKRRSVGHNSYKEHLVLLTASRILFFRNLVWAKDLMAQKKAYERRYKNFTTTSSSFDTLQGIDTEAMEYEFPKIPPLVFTPPLEEFSPDTSYSLVNAFAYCDRDKKNVRNCSFTVIFRDGSEETLCAPTEESMIEWVAKINYISTLRTAGLRMPVSDSYHPKRDFSCYPKYMEEELAAIEAQMKQDMEIARARTIKTRIDQLETSITEFNKKLMVLQRNAKNLSTCAPLQPKTRVVILQALKKVDAKAQSLYLEIRKMESQLQVLRFESDLDKCISLESSNDIDDRPSSTSPSTLKNPSINSINRQTHDVEKESSDRDVPHLLDPDNNFNLKGNPENPSSTFFTPEILSPKVYSDNVKDEPVEDIFGFEDTSESSPGKPSQLRLQIEAFDDELADTASLGSVTTCLDQWQTFSDDTDSGFALNLYSSEDFRTDPYKEHDEFSMNSLSKWHSATSDN O13819 YMR1_SCHPO ACT_SITE 342; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10044" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; SPAC19A8.03; CHAIN 1..559; /note="Phosphoinositide 3-phosphatase"; /id="PRO_0000356185" MENIKVAKVGNVKFVNKGNELNGTLHLTAYHSIFSISENGKEIWTAYSMINNVKLCSNEKSFCIRIQCRDFMFFCWRFQSTEDAMDVYDTLQELMSINSINMLYAFYYMPSGDEEKLPSSWKSFLLENEYRRMGVGDSTQADGAGGNWRITKINENYSECHSYPQALAVPASISDSVIYYGCKYRSKNRFPTLTYLHKNSFSITRASQPLVGIRQNRSAQDEKLVEAIFATSIIPGKENLIVDARPSTNAMANIAVGAGSENMDHYRFAKKIYLGIDNIHVMRDSLNKIVNALKNTDISAAPPLIELLNRSSWLKHLANILQGAVLIVKTVHFRHAHVLVHCSDGWDRTSQLCALPQLCLDPYYRTIEGFFALVEKDWLSFGHRFAERCCHLPGKRIFTIDSSYSEEPPQSSPSSTLQYTFSTVRSALSGFSIDHSEKMMSPVFHQFLDCVWQIMDQFPNCFEFNERFLRRLLYHLYSCQYGSFLYNSERERAQASVSTHTRCIWDYFLSRKDEFKNPNYVPYDDVIMPDPSSLRWWSASFAQPDENMNIPSPSESPSL O13823 IMP4_SCHPO SPAC19A8.07c; CHAIN 1..289; /note="U3 small nucleolar ribonucleoprotein protein imp4"; /id="PRO_0000120243" MLRRAVRERRQFIYKRNQELQEAKLNEKRRALRKALEGNKELNKDLQEDSQLQKDYKYDESRATQEETETNLDDEYHRLGEREPKVLVTTSREPSSRLAQFAKEVRLLIPNSYRLNRGNIVVGSLVEAARANDITDIVILHEHRGIPDGLVISHLPYGPTLSFSLHNVVLRHDIPNTGTMSEAYPHLIFENLTSKLGKRVKTALSALFPPDPKDTTPRVVTFANTDDYISFRHHIYAKTGPKQIILSEAGPRFEMKLFEITLGTVDMVDADVEWKLKPYQRHKRDVLAE O13830 PTH2_SCHPO CATALYTIC ACTIVITY: Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; EC=3.1.1.29; MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 79; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19A8.14; CHAIN 1..205; /note="Probable peptidyl-tRNA hydrolase 2"; /id="PRO_0000120285" MKVPFVNFMISSFPAAVLVGAVVGFMIGRKYSVADASRGYSSKNANKASNPEKESPVSVSNDEDSESETELLDMLKGNSSLAALALAEGQTKMVLVVRTDLGMTKGKIAAQCAHAALACYKIASAVDPDLVRIWENAGQAKITLQAQTEETLELLQAQAMSLGLCARVIHDAGRTQIASGSATVLGIGPGPVSVINEVTGSLKLF O13831 TRP_SCHPO ACT_SITE 50; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 61; /note="Proton acceptor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; MOD_RES 381; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC19A8.15; CHAIN 1..697; /note="Tryptophan synthase"; /id="PRO_0000098725" MTEQIKKTFLKAKEENKNVLVTFVTCGFPNVDETIKIMQGLQNGGAGIIELGIPFSDAVADGPTICKGNEIALKNNITLEKVFETVKLARDAGVTIPIILMGYYNPIFSYGDAKTIQKAKEVGANGFIIVDLPPEEAVGFREECKKQGVSFVPLVAPSTTDRRMELLASVADSFIYVVSRMGSTGSSATGVINTALPQLCQRVRKFAGDTPLAVGFGVNTSEHFHQVGSVSDGVVVGSKIIDLILKAEPGTAATVVEEYCKYLTKEDPSAPVPKQFQSGGSVATAPPAAVVEPINEMYLPQKYGMFGGMYVPEALTQCLVELESVFYKALHDEKFWEEFRSYYEYMGRPSALDYAKRLTEYCGGAHIWLKREDLNHGGSHKINNCIGQILLAKRLGKNRIIAETGAGQHGVATAICAAKFGMKCTIYMGAEDCRRQALNVFRIRLLGAEVVPVTSGTQTLRDAVNEALKAWVEQIDTTHYLIGSAIGPHPFPTIVKTFQSVIGEETKAQMQEKRKKLPDAVVACVGGGSNSIGMFSPFKADKSVMMLGCEAGGDGVDTPKHSATLTMGKVGVFHGVRTYVLQREDGQIQDTHSISAGLDYPGVGPELSELKYTNRAEFIAVTDAQCLEGFRALCHLEGIIPALESSHAVYGGMELAKKLPKDKDIVITISGRGDKDVQSVAEQLPILGPKIGWDLRF O13835 IMP3_SCHPO SPAC19D5.05c; CHAIN 1..183; /note="U3 small nucleolar ribonucleoprotein protein imp3"; /id="PRO_0000132711" MRILKHHEQKLLRKVDFLNYKNDDNNHRDVMVMRRYHISKREEYQKYNIICGKFRQLAHRLSLLDPTDPFRLQYENLLLEKLFDMGILPSKSKMSDIENKANVSAICRRRLPVIMCKLRMSQVVSEATRLIEQGHVRVGPHVITDPAYLVTRSLEDFVTWTDTSKIKRTIAKYNDKLDDYDLL O13843 ALLA_SCHPO CATALYTIC ACTIVITY: Reaction=(S)-ureidoglycolate = glyoxylate + urea; Xref=Rhea:RHEA:11304, ChEBI:CHEBI:16199, ChEBI:CHEBI:36655, ChEBI:CHEBI:57296; EC=4.3.2.3; SPAC19G12.04; CHAIN 1..191; /note="Ureidoglycolate lyase"; /id="PRO_0000120561" MEAKKIYAQALTDEAFAPFGSVVQQKDDVKMVSANGGTAKKYLKVSESIQNYEKSSSASTRKGVWNFFSTHPSVHPANDEHAAFQISVLERHPFTTQTFIPMCRSSDEQAYLIAVAPNAPDGMPDWNQTQAFVAKGAQGVTYSAGVWHAPMVTIGKETMLAAFNYENGVAEDDCQVQSTESPIEVFIKIST O13845 RSD1_SCHPO MOD_RES 174; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 465; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19G12.07c; CHAIN 1..603; /note="RNA-binding protein rsd1"; /id="PRO_0000081876" MQLDAEALAEAPFRKQEVPQNQENQQKASSSFHESSLTSSTHSHPSNPPPPPTRLHDRSFKPVSKNYESEGRLTPPPVSMGYRYARSSKQSFQREDSGYNDDVVTNSSSHRTPRHHRRSYSPRSDYGSRSPSPHSSVDSHQSRSPVRSRDRDRSSRSSRSRHPSSRSRHRYDDYSRSPPYSSRHSRSRRRYEERSSRSSRAHDYDYEDLRDDDRSHERKRSRSRPRERSSKLSEEERDRRTVFVSQLANRLTSRELYDFFEQAGPVRDAQIVRDKISGRSKGVAYVEFCHEDSVQAAIALSGKRLLGLPVIVQLTEAEKNRKAREAAELARAASAEIPFHRLCVSNIHFNLTDEDVKAIFEPFGDIEFVHLQRDDQNRSKGFGYIQYRNPISARNALEKMNGFDLAGRNMRVCLGNDKFTTETTSSMLKRFDETLARQERSQPSQRNGGSSTYESQDYREAAPLSPTEEESRPITRDELMKKLARSEDISDNSKLVSEPEPPIRSRCALLENMFNPAEETSPNWVQELEQDVKEECDEKYGKVVHIAVVPNELGQIFVKFENADFAEKAITGLHQRWFGGRTIKASILPETDYYFKFPNAKTA O13850 COQ9_SCHPO BINDING 181..184; /ligand="1,2-diacylglycero-3-phosphoethanolamine"; /ligand_id="ChEBI:CHEBI:57613"; /evidence="ECO:0000250|UniProtKB:O75208" TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC19G12.11; CHAIN ?..250; /note="Ubiquinone biosynthesis protein coq9, mitochondrial"; /id="PRO_0000339135" MLTLRSACQLTTKNLGLHKCISKTVISALGRRGYHSENYETSKISGKKALILENALEHVPQLGFTEDAIVQGGQALGYSNLSKALFPSGPMDLISYFFLKQRYALSSLKPHLTTIPETSGRVVQLIWSRLQGNRDIVQHLPQMIAICTYPSNLRKSLSSLAELSDEILYLAQDKSADFQWYTKRAAISAIYSASELFMSRDTSPNFEATYNFVQHRIQHAKALNDLRNDVLEWGSFQLNAVRSILRSRGI O13855 RQT4_SCHPO MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 380; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1A6.01c; CHAIN 1..455; /note="RQC trigger complex subunit RQT4 homolog"; /id="PRO_0000116731" MEKWTKENVLKILPVDDESAAMITSTALAVDSSEAAKDYWISLLGDSAETIEFISDFNQKRFHSTHSGNSPSIMKNKKNVTPNNNIRQKNTATSSHPSFYIANNKQKGYDEEMYKVNPASRNKSQSNNISSHEKSSKTTKNVSPGVMTSDLIPEKKSVKHNNSSSNRIEGLADIEKAIRQIEISQNINKAERRVCNCQGRKHPLNEAAPNCLNCGKIICIVEGIGPCTFCDNPVISKAQQLELIQELKHEGSRLKQAANQKRKSKTVSSKNNFQRLQNSSLHSIFLDPKQLEQKAQEAEERKNVLLNFDRTSAQRTRIIDEAADFDPTSLASDTWASPAEKALNLVRMQKAMAKKEKKKKKVLSISLSGKKVVVDQKEASSESSDEDQDELDNLTKVEGQSHSHNPKAPVIRNLPRPIYHQDLHSSHVAVPESILNKINQKWSKVQDDDGMPSML O13862 RDP1L_SCHPO SPAC1B1.01; CHAIN 1..478; /note="Transcriptional activator protein rdp1"; /id="PRO_0000046815" MSEHSPEASSTYAQVTSNDELSSNKIYMNADQNNSRKKEMDGSLQNNGGRLQNVNPLGGNESMSAVATSAASSLPTAENGVSLNAASPTIHSNTPTVVSHPVMSGSELKGEESHNSPGTLNGTSVANASKQPNMPNATFRCDKCDMMFVKQSGLTNHKRTYHQVETVVIIGHRRYVWRRNENGRFQCVCGRQNWRRPVNFASHAKQCPSFLAMDPNNIPPEINKVSPHDDLRPLSDSRRRARRPHPSDTIPPGASMARSDPSQVPESNPSAAAAVAAAAVAAAANLTNGVNPPEVPRNLNSSLVDAAESLANVSQQQHHRHPFARQPDYSAHSIPRTAAPYAPSMNMFAQNGPNTSLLPTAMPSDVSISSSLQQQPIHPSYDSRFSKAPQGTDALAALGYGTPSSAATLCPLYRDTPAAIVSEKLHLRLANLRIAYCEDCREFISLNAALDHRRSHHQQNITGDLVHVYSDFLDFQNC O13865 PAN3L_SCHPO MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B1.04c; CHAIN 1..681; /note="PAB-dependent poly(A)-specific ribonuclease subunit pan3-like"; /id="PRO_0000372357" MDERRSSIFSTNIPCRNEQLYGRCPYIDKGCFFQHKNQDNAPASSKPPSATAIDPQNSGFSTKLSINSPSFTPLKLSKTSISSASNKESVPLTRPKSYSSALSSGKNGAAAQQAANSPKTVSLMTSSSKAANALQTHKSSLARAASAVPFSPSKATTVSLKESASLTSLSNNKSVSNLNSISGASSPSGSLVNLHSLTRSASFVPQPSVPNSGQLSNADMSRHILARFPPFFHNLNEQQQKTTSFFLADDHLKWFTYLTQEFYQFANIPKLPSHVLSYHSLIPRRMIVTVLPVLRYATSIYKVIDGNNGLPYSFVQLRDFTLLNDRNITNVSPWTKVDSPHVIKIREAFTTHAFEQKSIVFVYNYLPSCPSLYDLFFASPVFRKRTSSFYFSQPLKATKEVLWCFASQLISALYSIHSSGLAAKMVSLKNVLMVGKMRLAIFGLGIMDVIQEESTEPLTSLQRNDCRDVGLILLALATDTENVTLSTAKAHLTRLKTIVSTDASLVELIEVLIFNEELRIQTLLPTMLSYMVNNYESVLLMEDVYETYLAEQVENDRLLRLLLKLEFLDDRPEYVDDPDWSASGVYFVIRLFRKYMFQVQTIDDASKKPTLQSTTTPPRKLLNKAHLLSCLNKLDAGTDEQILLEDEFTRIIMSFKEVKTTINTAFMELERRCSNNLSVKK O13867 UPP1_SCHPO BINDING 33; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 42; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 76..79; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 86; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 103; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 111; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 132; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 138..146; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 138; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 202; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250"; BINDING 203; /ligand="uracil"; /ligand_id="ChEBI:CHEBI:17568"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 208..210; /ligand="uracil"; /ligand_id="ChEBI:CHEBI:17568"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 209; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998" CATALYTIC ACTIVITY: Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. {ECO:0000250}; SPAC1B3.01c; CHAIN 1..219; /note="Uracil phosphoribosyltransferase 1"; /id="PRO_0000120786" MSLVPEHGNVYVLNQTNQLKGLFTIIRDKTKPRSEFIFYANRIIRLIVEEGLNHLPVSSAKVTTAQNAEYEGVMFDGRICGVSIMRAGESMEQGLRECCRSVRIGKILIQRDEETHKPVLHYIKLPEDISKRYVLLLDPMLATGGSAICAMEILINMGCKQEQIIFLNVIASPEGLKNVHDRFPNIRIVTAVIDEGLDNNGYIVPGLGDFGDIYFGTKA O13868 ELOF1_SCHPO BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P60003"; BINDING 28; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P60003"; BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P60003"; BINDING 52; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P60003" MOD_RES 97; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B3.02c; CHAIN 1..107; /note="Transcription elongation factor 1 homolog"; /id="PRO_0000120949" MGKRKAKAKVKPKRRAPPLDTTFTCLFCNHEKSVSCSLDKQSGVGNLHCKICGQSHQCLITALSAPIDVYSDWIDACDAVANQAKEVDNINDQEAYSPEAAYEEEKE O13869 GUF1_SCHPO BINDING 65..72; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03137"; BINDING 130..134; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03137"; BINDING 184..187; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03137" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-Rule:MF_03137}; TRANSIT 1..44; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03137" SPAC1B3.04c; CHAIN 45..652; /note="Translation factor guf1, mitochondrial"; /id="PRO_0000091561" MSIFRLSRTFSLETCLKSSSFKIRWRFFSVSYASRKLASEDNKPSIQEVVRGIPQNRVRNWAVIAHIDHGKSTLSDCILKLTGVINEHNFRNQFLDKLEVERRRGITVKAQTCSMIYYYHGQSYLLNLIDTPGHVDFRAEVMHSLAACEGCILLVDASQGIQAQTLSNFYMAFSQNLVIIPVLNKVDLPTADVDRTLIQVQQTFDIPMSKPILVSSKTGKNVEQILPEIIQKIPPPKGSENAPLRCLLIDSWYNSYQGVIGLVRIMEGFIKKGGKVMSVNTGRKYEVQQVGIMYPDMTEVSRLRAGQVGYIIWNMKNIDEAIVGDTYSTIGSNVEALPGFSIPQSMVYVGAFPLDGSDYERLNDNIEQLALNDRAINVQKENSSALGMGWRLGFLGTLHLSVFIDRLKDEYGKELLITSPTVPYRIKYKNGREEVISNPNLFPTNHQGISELLEPTVDATIITPSEYLGDVIKLCESCRGLQKDCTYMSESRCMIKYQLPLAHLVEDFFGRLKGTTSGFATLDYEESDYVPADLVRLSIFMSGKSVDALCSIVHRSLALQRGREWIQRLKPLVPKQLYEVILQAVIDNRVVARESISALRKNVTAKCYGGDVTRKQKLLNKQKEGKKRLKSVGNVSIDKSVFYEFLTKKQSN O13872 VPS28_SCHPO SPAC1B3.07c; CHAIN 1..248; /note="Vacuolar protein sorting-associated protein 28 homolog"; /id="PRO_0000120957" MTEYYDLNLLEKETSEENNFHTKNQQVREDLSILYSILVALEQLEKAFTKDAVSTSDFNSTCELLIQQWESCFSDERVTQAFGSFEDFCSKYRLQCPRAIKRIQEGISDERSQSNSTFSNAISTTAEPSIAMNDTTPQTVNPTKAPSNPSASIAKSIAGLVQNFITTLDAIRLNFIAKDQLHPLLSELIVSMDDLTESLKIQVSCRNKLVQWLIKINNMNITDQLNDVEKRELLYDLEQAYAECYSLL O13876 YPT4_SCHPO BINDING 16..23; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 68..72; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" SPAC1B3.11c; CHAIN 1..234; /note="GTP-binding protein ypt4"; /id="PRO_0000121311" LIPID 233; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"; LIPID 234; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250" MDKESYDYLVKIVLAGPSGTGKSCLLQRFVKNQWDDQVSHTVGIDFASRIISVGMGNQQKRIKLQIWDTAGQEKFRSVARNYYRGAAGAVLVYDVTNKDSFEELSSWLSDIRAMAPSTICVVLAGSKSDLQNQRQVSTEEAAEFCSEKHISSAHETSSYTGSNVEECFLSVVSTIITRIELGEIDPQDQSLGIQYGDLSFRRPVHPSSTSNWWTSITNWDDLVRLERQTRSYCC O13878 UTP17_SCHPO SPAC1B3.13; CHAIN 1..806; /note="U3 small nucleolar RNA-associated protein 17"; /id="PRO_0000307923" MEGPNSMEVGSLEVKKNDKDPWSKTAYLGGRLVSKIPAVYSNDNKFVFLTYDTFIGIFSLITGDCINRIFFPNNLANLLPVAVLLSPENAFELYVIFQSGYVCVHDWSNSELLRTMEISTRVHAASFSGKLLFAVTDTPASDSASSQDRFTLYALSPSTSKEGSSILIPTFVSKFNEFLALDSSLRDNNLATVAVITTDKAIFSLNVPKKKRSQRWIHREHLFNMPQKLTNVSLCGSACAVSDDEGKIHVINDISNEKFNPQILHWHANPLNGLSWALNGEYLLSGGQEGVLVLWQMETSHRQFLPRLGSSILSIATSHDSDSYALHLGDNSLVVIRAVDLAEQIHVSGINSFESKYLTSTGPKNTSKQLQGLVQFSSVSPNGELLLMSSSSFNGHSVSVQEYDLTKDSTIRKFEAARYSYSSVSKNSDDATSLDNGHVGSVAVTSSRNGLYIATIDTWCTNIIDEQQRNVKQTALKFWQFDSVQKTWVLMTRIDNPHGNLEVVTALKMMTSSNRFITVGTDATLRIWALLPGSSAWKCVAIHHFANTHSQASIKQRYGFSKALTCSLDDSIIGFGYGSCMHFINSETLEEISTVDLPHGGQLENAQFLNAEHCVIISQRRLLVWNVISASVQWTLASKFTGLLASSSSGNDFAVIDFNSSYSRLIIFSPDSPKIQSIHIFKTLPVALHYLHGGFVVLDNKSIIHVYAGDLTTKIPSAQLSIDNTSRSLLGDFQKRNVPLLNLENPISGSQGLHYKRLTTDMIHNLFNVPSNSPVNMQAIYNTFSKMAVGEPMESLGTQIATLNTE O13890 SELO_SCHPO ACT_SITE 287; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q87VB1" BINDING 120..123; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q87VB1"; BINDING 144; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q87VB1"; BINDING 156..157; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q87VB1"; BINDING 208; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q87VB1"; BINDING 215; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q87VB1"; BINDING 288; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q87VB1"; BINDING 297; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q08968" CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; Evidence={ECO:0000250|UniProtKB:Q08968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289; Evidence={ECO:0000250|UniProtKB:Q08968}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q87VB1}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000305" PTM: Forms probably one or more intrachain disulfide bridges. {ECO:0000250|UniProtKB:Q08968}. SPAC20G4.05c; CHAIN ?..568; /note="Protein adenylyltransferase SelO, mitochondrial"; /id="PRO_0000121402" MSKKLKDLPVSSTFTSNLPPDPLVPTVQAMKKADDRILHVPRFVEGGGLFTYLTPSLKANSQLLAYSPSSVKSLGLEESETQTEAFQQLVVGSNVDVNKCCPWAQCYGGYQFGDWAGQLGDGRVVSLCELTNPETGKRFEIQVKGAGRTPYSRFADGKAVLRSSIREYLCCEALYALGIPTTQALAISNLEGVVAQRETVEPCAVVCRMAPSWIRIGTFDLQGINNQIESLRKLADYCLNFVLKDGFHGGDTGNRYEKLLRDVAYRNAKTVAKWQAYGFMNGVLNTDNTSILGLSIDYGPFGFLDVYNPSFTPNHDDVFLRYSYRNQPDIIIWNLSKLASALVELIGACDKVDDLQYMEQLHNSTDLLKKAFAYTSEVFEKIVEEYKNIVQNDFYDLMFKRVGLPSDSSNKILITDLLQILEDYELDMPNCFSFLSRNSPSSMENEEYAAKLMQACICLNPNNERVRNESVKAFTNWVGRYSEATKTQEDSSRLASMKKVNPHFTLRNWVLEEVIKEAYIGKFELFKKVCKMAACPFEDTWGFSKEEEDYLCYNTTPSKSQIQCSCSS O13895 CSN4_SCHPO SPAC22A12.03c; CHAIN 1..377; /note="COP9 signalosome complex subunit 4"; /id="PRO_0000120995" MEEVVHYFLEGNMPVAQFREALALHYTNEKELFEQAKRCLNICCGSNNFAKRNDVLFSLLDVAVSISSLELRKELISELYVPVQSLEEAPSEYLVSCCLQLATIYEAEQNFELLCSSLEAVEKHGHFENDLEQLLLLRIRLGDAYLKLGKAEKAILTVRTSIPLAFKVSNDQLLMELQLCNARALDETGQFLEAAKCYYRVLQYKVPGNELIYRENLCSVAQCLLLAIPSPIVLQFLQEISLQPSVREIPFYSLVEKYLKRKFIGKEDGAFLLPFLLPHQVIHMNRLIEDGRHFLETNILFLSEFFEVSSTSILAKHFKLSEEQVDTVVADMVIQERLNASIDQCEGYITFLPEYGKANNLPNYVNKIATVLQHYGS O13897 YF36_SCHPO ACT_SITE 116; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 179; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 206; /note="Charge relay system"; /evidence="ECO:0000250" SPAC22A12.06c; CHAIN 1..429; /note="Uncharacterized hydrolase C22A12.06c"; /id="PRO_0000316196" MKSATKSKILCIHGYAESGELFSVKLRALRERMADSVDFYFPTGPIELDKAKDELNGSGFDALSTVFSSSPASHRRGWWRINEYADTKQLEPTKAFEYLASYIKEHGPFDGILGFSQGTNLAANLAALVTIPKYQEYFSQPPFRFALFFSGYFRPLLMDGAVHATKLDLPTLHLLGKYDTVLSTETSTTLVRACKDAQVLFHPAAHQIPAPHAYVEPAADFIDFFSREDWPIISKHISLIVPTKKVNTTSAQTSLNNVEHDLISKIMSRSFKGGINVVVSDLQMFNEYKRIFGPKVLSLVVTDGQEPDTYSENVHYTPNFKGALAYLEAYQNSIGRIYVIGDKKLLTLGMLCRCTKRIIAITDAEDKFISQSSAQQVSGSLPFLEHSKEWLKAKSSQIRQWTGQSRLKHMSQDNSGEPVTMKLQMWERL O13900 SA114_SCHPO SPAC22A12.09c; CHAIN 1..481; /note="Pre-mRNA-splicing factor sap114"; /id="PRO_0000290652" MSSLMEFQDRNTTNNETEHQKSITDQSSSVPAGVILPPPAIREIIDKSASYVARNGPAFEEKIRQNEQANTKFAFLHANDPYHPYYQHKLTEAREGKLKSHATGLSTQKTSTLARPIQKPIEATIPAPSPYLFSEPLPSISSLDLDVLRLTARYAAVRGSSFLVSLSQKEWNNTQFDFLKPNNALYPYFMRIVQQYTSLIREPISSPEQELRENVRDPYSLLSKIQPRVRWQSHMESQKKKQKEEAEKEKLEYAQIDWNDFVVVEVIQFTKSDEHAKLAKPTNLADLQTATLEQKSAMFTMPDQNYTIEEAPPTAEPWEPISAPKKQEFGVSLPPSLASPEKGGISSTTSVSPAAQASPVLSTTTQPKVQKPVPKAFQPKVPMEISPFSGELVPATELEEHMRLKLLDPRWQEQRKVEESRKSTLNLENVNVAANMKRLVSQRTDLFDVQNGVEISQEEIERRKRAATQSAWGATPTNKRR O13901 YF3A_SCHPO SPAC22A12.10; CHAIN 1..386; /note="Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10"; /id="PRO_0000318106" MQLNRKQLKNLHNYKYSAIDNSLLSKYILKPYWWNQLLKVIPMSMAPNLITLIGLGFVVINILTMLVYKYHYEMDAFPSWVYASWAIGLFLYQSFDAIDGSQARRTGTSSPLGQLFDHGVDAINTSFEVLLTIELLQLDMFSSILTQFASLLYFYISTWEEYHTGTLYLSYFSGPVEGIVMVIGLFALTAIKGDSFWLKLHPTPESWGFVRSFLPYYTYGSCLYNFMAFALLLNVLQSLRNALQAVQKNNGSVIKALSGILPYFLQWMAVFSLYAKYPAFFEHHFLTIFCLNAFIFAYSVGVVIVSHITESPFPYWNVLILPFLVDAVDAYTFGVLKNVQTEYFFCYVGICIGVYGNFVAHVIAMITEEYGIKCLTIPSKPESKKN O13910 MPP10_SCHPO MOD_RES 268; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 293; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23C11.03; CHAIN 1..598; /note="U3 small nucleolar ribonucleoprotein protein mpp10"; /id="PRO_0000121533" MTELINSEPTLFLFPNKEDSKQLVEKAIEVFSNIKIPSTSPIQTIVTKGLDNWQIYNQLALAAKYALDDLPQVDVENEDEEEDSITSFQDEDDETSHQELSDNSEMNNRDDADDEFLGFSGPENLEDVDESSAEDVSGDEAEIMNEEGQQIEQKKDAFGLNDGFFDIDNFNKQTLALEEEAVEEGVLGDEDDGIDLLMDPDENMEDSEDESNGPQADSIMYEDFFGPKTAAGRRELKKKKAESKRKRTSKPDFKNDVQQNVIEENNESSDNEYATFDRVKKDLFASDEEDDVSADQLSSYERDKARLTQQIRELEAENVAKKSWTMMGEATSKGRPSNSLLDVDLEFETGAKPVPVQTEETTETLEDLIKNRIISKTFDDVPKRAPVAVTEFRPSELFELNENKSQRSLAEEYEEEFLKKSNADTYKSEADKKKEKEHEEIKALFSEVSRTLDSLASWHYVPPPPESTVEIVSNAPTLAMEDVQPTAASDTMALAPQEVYKPSNENREGETITRSGIAISSTEMDHQQKQARRRRVRRKHAEKRKQMAEKRRNSGTEQVVRQLSKSNVEVIGKGGERKKVASNSNKYHPIVSSNQLKL O13920 MDM28_SCHPO TRANSIT 1..85; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC23C11.17; CHAIN 86..485; /note="LETM1 domain-containing protein mdm28, mitochondrial"; /id="PRO_0000116675" MKYPRTHIQFPSMLRNRLFKTPHQTGFQWRLGAPATGITIRNQPIRSYSGLRGNFLIDKRLSPVKFNKYSPSDIVFYNIGSSRLYSTETPTPSKVKEAPKQVAAEETKPTTVVKKPSIWQRVKGGVLHFWDGTKLLGVEIKISSKLVYKMAVGYELTRRESRQLTRTLKDIGRLVPFSVFVVVPFAELLLPIAVKLFPNLLPSTFEDAKDKEAKKAQLRKTRNEVSNMLRSTLKSGKFTFSNETRESKEFRDFFQKVRTSGQSPSREELIEVCKYFKDDITLDNLSRAQLVAMCRYMNLNAFGTDPLLRYNIRHRMRQIRRDDRAIYIEGINSLSIPELFNACNSRGIRTQGLSPAKLKEELSVWLDMRIKHGIPSVILMLSNAFSYGYNEGTYDSRWDALQDTLASIPDELYHETVVDMPTKQVSNKERLEILREQEELIEEEAEHVAEHPDLAKKQTEENKATSKPAVSAKSPESNIPKNERK O13921 MSH1_SCHPO BINDING 747..754; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC13F5.01c; CHAIN 1..941; /note="MutS protein homolog 1"; /id="PRO_0000115180" MPTWRYIFSLRSKSSFTKTWVPFTQIRNSSKSPKVGQKPILQGALGPPLDFIRPKEKVTLPPLLKEVSFQQKKFADCVLLTKVGNFYEMYFEQAEKIGPLLNLRVSKKKTSKSDVSMAGFPFFKLDRYLKILVEDLKKCVALSEEVIRPVDDLSSKNMYIRSVTRVITPGTLIDENFMNPYESNYILTVVFDPNFFSSDISNQGTAEDKDCFADCKIGLSWLDLSTGEFFTQDSNLQRLAGDLTRISPREIVLDESLKSFTTHPIYSFIQERKYFLSYVENRYQSLDCWNKFLEKEIDPSFIKYCTKLEVTAGCTLISYIADRLQNSHPNIQPPIRVSLNEYMIIGESAMKGLEIRSSLYQNRYTGSLLHAINKTVTKSGSRLLTRRLCAPSTNIVEINNRLDLVEKFKLLPELCSKVINLLKKSNDTHRILQHLLMGRGNSYDLLKMADNFSITKEIHSLLSPLESSSAFRLLLLNMHPHDELKQLINNAVDENALMKQKINEEEETEVIAQEAEEILQDENAQVEIVKKSLSSEFDIRQSFKENWVVKSNFNNNLRKLHEKLQSLFASYDKLQEDLSKRLGKKATLRKSPAKLYYVHLKLSGNETIERFIKKFTQAVLFQSTKSTASFQLPGWTSLGMDLENTKLHIHQEEQRVLKSITDEIVSHHKTLRSLANALDELDISTSLATLAQEQDFVRPVVDDSHAHTVIQGRHPIVEKGLSHKLIPFTPNDCFVGNGNVNIWLITGPNMAGKSTFLRQNAIISILAQIGSFVPASNARIGIVDQIFSRIGSADNLYQQKSTFMVEMMETSFILKNATRRSFVIMDEIGRGTTASDGIAIAYGCLKYLSTINHSRTLFATHAHQLTNLTKSFKNVECYCTNLSIDRDDHTFSFDYKLKKGVNYQSHGLKVAEMAGIPKNVLLAAEEVLTLLPNTSKPTSMK O13931 ATP18_SCHPO SPAC23C4.11; CHAIN 1..60; /note="ATP synthase subunit J, mitochondrial"; /id="PRO_0000071698" MSFFGLKRYSTPILKPMLPFFLGGAIVFYGTVKLRDAMMDSAEYRNDPRNPKAGKYGSDH O13932 BET1_SCHPO SPAC23C4.13; CHAIN 1..117; /note="Protein transport protein bet1"; /id="PRO_0000206891" MGSRFGRRKERNGDMLPLYESQSPQHLDSLENENDERISKLTGKVKSLKELTMNIGTEITSSTKLMESMNDSFDSTKSLLSGTMTRLKNVSKNGGISIWMWLAFFCLVALILVLVRF O13933 ALG1_SCHPO CATALYTIC ACTIVITY: Reaction=an N,N'-diacetylchitobiosyl-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = a beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+); Xref=Rhea:RHEA:13865, Rhea:RHEA-COMP:19510, Rhea:RHEA-COMP:19511, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:58472; EC=2.4.1.142; Evidence={ECO:0000250|UniProtKB:P16661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13866; Evidence={ECO:0000250|UniProtKB:P16661}; SPAC23C4.14; CHAIN 1..424; /note="Chitobiosyldiphosphodolichol beta-mannosyltransferase"; /id="PRO_0000080257" MLVLKIVLFLSLVIWFNLKKRTDKKRIIVLVLGDIARSPRMQYHAVSFAKLGWKVDLLGYQHPGSSVGLFESHENIRFYPIPSLPAYLQPKNRLQFLFLGPLKVLHQFLALNWALFVRKPASFLFIQNPPCIPVFFIAQCLHILRGTKFIIDWHNFGYSILALKLGKQHTFVKLLKIYEKYMARGAYAHLTVSKRMKDVLQTWGMNPCYVCYDRPPNHFTPIKNEQKKQMSIKKIPCEYNPSSTKLLITSTSWTPDEDIYILWEALNEYDKTLDTPKLLVLITGKGPMKEEFSQYIKKHPLHKVRFCMPWLSIEDYPQVMACADLGVCLHTSSSGLDLPMKVVDLFGCGVPVIALSYPTISELVHDGENGLIVNDSKALSKKMQYLLTHANELNSLKLGALKESEYRWDDEWNKVIPPIVQGSN O13940 GLY1_SCHPO CATALYTIC ACTIVITY: Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48; CATALYTIC ACTIVITY: Reaction=L-allo-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:58585; EC=4.1.2.48; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; MOD_RES 226; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC23H3.09c; CHAIN 1..376; /note="Probable low-specificity L-threonine aldolase"; /id="PRO_0000121571" MSGSVTSTTTETRLCPSNQGSAKKYRPWNDFRSDTLTVPTDEMRRIMYEASDGDCVYEEDEDTRKLEVYVAKLTGKEAALFVTSGTQGNQLCIRSHLHQPPHSIICDDRAHIYNWEAGAIGLFTQAIVRPISPKNNVYITAEEIENKLILGNDIHFSPTGLICLENTIKGAVVPLDEVARISGLAKAHKIPLHCDGARLWDAAVASNVSIKEYCSYFDSVSLCLSKGLAAPVGSIIVGPRDFIAKAKWFRKAYGGGLRQSGMLAAAGLYSIQHNFPLLKQVHKYAIEVAEYAESLGIELEVPTQSNMVTLANINVAILCDEAKKSGIILMGPRIVFHIQITPDAVEILKNVLRRTVERQAVETHIVAKPGEFCVGY O13941 YEPB_SCHPO SPAC23H3.11c; CHAIN 1..629; /note="Uncharacterized beta-glucan synthesis-associated protein C23H3.11c"; /id="PRO_0000317220" CARBOHYD 286; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 373; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 455; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 480; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 513; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 607; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MEKGHSDLPRQPERVAQNPFLTFDQDSFPSSYGSSLNVSEQTSGSSSTSPLPQISCLLRKDDVPLANKELSRSLIHVQELSRYPPFYNQDHQHLGVPRSRVGSDVWKMREKSFLSPSQFSSIDLSWVYRSKEEDDDFHDPKSSVVSLMGEEDYLGWSRFCDLFFLFVLSLGIGLLFIVFPALTFTGNITPSKEKFDAIMANQITDHLFAHMRVPRTNLIDKDTPSTAYHRTGYNGRKYNLVFSDEFNKEGRSFYSGNDQFWEAVNIHYAATNDLDWYDPDAITTVNGTLAIQLDAFWNRDLNFRSGMLQSWNKLCLKGGIIEVSASLAGSGEHAGLWPGIWTLGNLARPGYMATTDGVWPYAYSQCDVGITPNQSSYDGISYLPGQKLPNCVCLNEDHPSPGVGRGAPEIDILEGSTEKLHPDDELDIGVVSQSGQFAPFDFFWLPNYDYLAVYNDSITHMNSYVGGPFQQALSGITTLNNTWYGGNAFQIYGFDYKPGEGTNGYVSWFVGPNYTWSMLGSAVGQNGNVGPRQISEEPMSIIFNLGISNNWAYYYFRDLSFPAVMYIDYIRIYQDPDDTNSHIGCDPPGYPTTKYIEEHPLAYKNPNATTWEMAGYTWPKNSLMHKCNT O13945 PPK9_SCHPO ACT_SITE 145; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 29..37; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 52; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SPAC23H4.02; CHAIN 1..532; /note="Protein kinase domain-containing protein ppk9"; /id="PRO_0000256816" MQTPSSASAESEKDSGNTYVGPWLLGRTLGQGNLAKVKLGKHFQTNEKVALKMVYNDELEDKDTWKRLQREVTILRQLHHPNIITLYQVFRVPKYTVLALEYMDTDLHSMVVKHNRLDECTTRKIFRQIVHAIDYCHLHRVAHRDLKLENILLNKDLVVKLTDFGLSNFMLDGSFLSTSCGTPHYAAPEVIQGRYYDGCDVDVWGCGILLYLMLVGEFPFEDVTISNVLSRVCKGIYTIPSFVSSSASDLIRQMLMVLPTSRIKVAEIMQHPWFIADLPTHSRLPSRTSSFSSKHRSVTFSPPDLAILFDPSITSPSSSVGQIPQPTDHSALSPSKPMSISGTESPNPDPASLCYSSYEDLYSATSWHSDMAESSGFLDPTDIPPIPSNVETLRSSLPQRHASFMNKVYNHPLSRPPAPNRLRSLRWHYGIQTAKNPIEVLRKLCEALLELGARFRPCDEESFLKENKYKVFSCITCHNSPVYLVIELFSIGPSASVIDIRFSSSDDSIKYTSSYSPMPFLEVVKQLILKIA O13946 TMEDA_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC23H4.03c; CHAIN 22..216; /note="Endoplasmic reticulum vesicle protein 25"; /id="PRO_0000237697" MMVSLKSSLFFMLALLTVVHALNFDIPAKTNPEPFCLREYVGEKNLVIVNLKTTGNMGDGQTLSMMITDSSGNTHSSIQNVLGEKSVAFDVDASAMLDICFLNTLTPGAIESEHKKRSVKLEFTVGADADDYSSLQKANNLEPVEADIRRARDFIEEIKGKIYYLQAREARFRNTNESTNERVKNFAYLTFISLFVLVIWQILYLRSFFQRKHLIP O13947 MTU1_SCHPO ACT_SITE 129; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 234; /note="Cysteine persulfide intermediate"; /evidence="ECO:0000250" BINDING 37..44; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 63; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 159; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963, ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215; EC=2.8.1.14; Evidence={ECO:0000250|UniProtKB:Q12093}; SPAC23H4.04; CHAIN 1..415; /note="Mitochondrial tRNA-specific 2-thiouridylase 1"; /id="PRO_0000121710" DISULFID 129..234; /note="Alternate"; /evidence="ECO:0000250" MRVSLFLQKQIIECSKAFQPHSTRLQWPKSQDKVFVAMSGGVDSSFSAYLLKSQGYNVEGVFMRNWLDEDSAPSGCPAERDWATVQKVCKKLNISCRRFNFEKEYWNLVFEPSLDLYENGLTPNPDVSCNRQVKFGALFDALKKHCENNVKGDWWLASGHYAKSVVNIETNESHMCIPTDKRKDQTLFLCTIRKEALEKTIFPLHNWTKENVKKQASSAGFKEIAEKQESQGLCFVSPNVGRKFRKFLQRYLNFSDRPIKVIAGKNVVGEFSGNHGIWSLTVGERCGLSLPQAQSEYFGRWYVWKKDIKNNALYICRGTNNELLMSKCIYLKDWKWCGTKLQNLEKSALSCFVRVRHQQPLQPAKVTWRNPESVKIHFQDKQRAVTPGQVIAVYVNDVCLGGGMVDTVEPEKDFD O13950 SRPB_SCHPO BINDING 44..52; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 65..68; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 87; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC23H4.07c; CHAIN 1..227; /note="Signal recognition particle receptor subunit beta"; /id="PRO_0000101229" MDGTSQAFKIIVATIIIGAIISTLGIFFTRKTIQKKLPAVFLIGPSDSGKTSLFCELIYKEKKTTVPSIEPNEAVWKYGAWLVDLPGHPRAKRWITTKFSGNYNVKAVVFVLNSATIDRDVHEVGLMLFDTILKCRKHHVPHLLIACNKFDLFTAQPAEKIQQLLKAELHNILEEKNLQLESIVSEDVDWESVADQIEDTDLKFLPGSVAKMSNIEEWISWMESALQ O13956 TSR1_SCHPO SPAC23H4.15; CHAIN 1..783; /note="Ribosome biogenesis protein tsr1"; /id="PRO_0000339127" MAHHHRSTFKAKKPFKSKHASKSSLKEKYKNEVEPHRSGPKNIVHTSTKADRRNTAKQIQLNKRTEVAMNNRIFGGKNGAPKVITIVPLCNNVDSWNVLTNLLRSIDPEASLPKFDKDSISYSTTIDRFKQNLLFLLPKREFYSLIDACKVSDYVIFVLSAVQEVDEFGELIVRTTQGQGISSVLSMVHDLSEVDSLKTRNEVKKSLQSFMNFFFSDQERVFAADVSQDALNVMRALCTSHPRGIHWRDSRSYLLSQEISYSNGNLLVRGIVRGKGLDPNRLIHIQGFGDFAINRIYEAPQGIQNSRGISMDEDTNLTGGLVELCSPTQEQDSLESLGPIIDDMDTDMDSEVGKEASRGVRLDDFYYFDDEEEPVAVAKRVPKGTSTYQATWIPDEDEESDQYSDVEDTEVIIEDQDNQEISNHVAEEKIDSDEEETIDDAKSEMFVDLSEEEEVRQYEEYRKKQKELQEELEFPDEVELQPNELARERFKKYRGLRSLYTSQWDADEYDPNEPREWRQLFKFENYRNLKNKFLKQPFIGEAKPGKAVYVELRNVPIEIFEYYNKPWNLLVLYSLLQYENKLTVSQFTAMQHSEYEEPIESKEELLLQIGPRRFMVRPLYSDPTASGASNNLQKYHRYLPPKQAVIASVISPIVFGNVPIIMFKKSSDNSLRLAATGSYVNCDTNSVIAKRAVLTGHPFKVHKKLVTIRYMFFNPEDVIWFKPIQLFTKQGRTGYIKEPLGTHGYFKATFNGKITVQDTVAMSLYKRMYPLPCELFKVTDIDS O13962 YE42_SCHPO CATALYTIC ACTIVITY: Reaction=holo-[cytochrome c] = apo-[cytochrome c] + heme b; Xref=Rhea:RHEA:22648, Rhea:RHEA-COMP:10725, Rhea:RHEA-COMP:10726, ChEBI:CHEBI:29950, ChEBI:CHEBI:60344, ChEBI:CHEBI:83739; EC=4.4.1.17; Evidence={ECO:0000250|UniProtKB:Q00873}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650; Evidence={ECO:0000250|UniProtKB:Q00873}; SPAC24C9.02c; CHAIN 1..216; /note="Putative holocytochrome-c1 synthase"; /id="PRO_0000121720" MQPEQLNQEEESKCPVPPEVRDAWLKSHGGKKPSEVHDTPHPTMLPTEREISTIPKVVTESDSGKEEKWIYPSQQMFFDAMKRKNWNPHPEDMKTIVPIHNAVNERAWQDILQWEQGWGSEKCGGPKLERFDGNVKKLTPKARILNLLGYNKPFDRHDWLVNRCGRKVAYVIDFYNGPTVNGTPSIYLDVRPKLSVHGAWMRVYRWTNEHFSQNSK O13963 MVD1_SCHPO BINDING 21..24; /ligand="(R)-5-diphosphomevalonate"; /ligand_id="ChEBI:CHEBI:57557"; /evidence="ECO:0000250|UniProtKB:O23722"; BINDING 77; /ligand="(R)-5-diphosphomevalonate"; /ligand_id="ChEBI:CHEBI:57557"; /evidence="ECO:0000250|UniProtKB:O23722"; BINDING 156..161; /ligand="(R)-5-diphosphomevalonate"; /ligand_id="ChEBI:CHEBI:57557"; /evidence="ECO:0000250|UniProtKB:O23722"; BINDING 212; /ligand="(R)-5-diphosphomevalonate"; /ligand_id="ChEBI:CHEBI:57557"; /evidence="ECO:0000250|UniProtKB:O23722" CATALYTIC ACTIVITY: Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557, ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33; Evidence={ECO:0000250|UniProtKB:P32377}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23733; Evidence={ECO:0000250|UniProtKB:P32377}; SPAC24C9.03; CHAIN 1..393; /note="Diphosphomevalonate decarboxylase"; /id="PRO_0000310441" MDKKVYQCTVSAPVNIAVIKYWGKRDVALNLPTNSSISVTLSQDDLRTVTTASCSEKFENDTLWLNGNAEEIFANKRLRVCVEELRKARLDLEEENDDLDKIGALKLHVVSENNFPTAAGLASSAAGYAAFCEAIARLYDLPWTPTQLSRIARQGSGSACRSLFGGYVAWEMGELHSGADSVAVQVEPVENWPEIRVAVLVASAAKKGVSSTAGMQATVASSTLFQHRIQNIVPQRIQEMKTAIRERDFETFAKLTMTDSNQFHACCLDTFPPIFYLNDTSRAVIRVVENINATAGKTIAAYTFDAGPNAVIYFLEENSEIVLNTLYAVTKNAEGWSKQYGSSPVTVDSAAANIVSSGISRVILTRVGNGPRVLTIDESLIDASGNPKFIGSH O13965 MUG70_SCHPO SPAC24C9.05c; CHAIN 1..730; /note="Meiotically up-regulated gene 70 protein"; /id="PRO_0000116696" MTVGTLSVVSSTASDTASHVSDTRKRQYQRDEALRKKIISELGKKSGNFESPVRKIRRNGEPGTVDSAALDPALTVHMQSLVTETAQLMAAKRQNCVLVVDDDEQLAGIVTATDIATRCVGAGLNARQTLIADIMSTSPLCITSDTRFDDALLLMIEHKFRHLPVVSDGGPDGSAGDEGDVIGIINMRACLREPLNRIARQQEAAQKLVEALEGAQEEIENKSVSGNTNSSSVSGNHAAEFLEYVESLKKKASGLEIMSLIDSSEEPFLVGTRTTVAEATESMARSGVSAVLVMDNGAVSGVFTAHDVVLRVLAAGLDPYRSSVIRVMTPHPDCALASLRVSTALERMIEGKFSNLPVVDESDAIIGMLSLFHLATAIEQTPEEEEEVFDQAENDAGIEPSNGFEDQQQQLLGNSNEVVENYDVNPPLPLNPLPSNTQQSESTYEYSARQLPKPPVQAWQNENLSSNNKPQEYVGVENDYNFSNNPPTAMSEQSFHPSVSQKPMDTPENGSNSFAASPYLQPYNSASQLAPSYVGSLPQYHGNPSFVEQALQDLVQPTDSASQIFPLNPQSPSQFTIKYRSIAGRVHRLRLDGINSVSDLRTAVEEREKEQLVTLTYIDDEGDVVELVSDSDLREAILLARRRGLPRLEVRGVAAFTNHLESSHPPISTVDSSIGSASVVEKGVANSIVDIHQPTAKADKGNSKKPIYIGIVSSSIVILAVSMWYLRRKR O13966 ACON_SCHPO BINDING 106; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 199..201; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 392; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 455; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 458; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 481; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 486; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 613; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 676..677; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; TRANSIT 1..32; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC24C9.06c; CHAIN 33..789; /note="Aconitate hydratase, mitochondrial"; /id="PRO_0000000546" MFCKISRAPARMGSRIFTQSTLRSFSCAPVAANIDAKKVAMSNFEKNKFINYQRIKDNLEIVKKRLNRPLTYSEKILYGHLDDPVNQDIERGVSYLKLRPDRVACQDATAQMAILQFMSAGMPEVAVPVTVHCDHLIEAYEGGPIDLERANVTNKEVYDFLQTACAKYNIGFWRPGSGIIHQIVLENYAFPGGLLIGTDSHTPNAGGLGMVAIGVGGADAVDVMANLPWELKCPKVIGVKLTGQLKGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVESLSCTGMGTICNMGAEIGATTSIFPFNPRMSEYLRATNRSAIADYAEEFAPIIAADENAHYDQIIEIDLNTLEPHLNGPFTPDLATPISKFKEAVKKNDWPQELKVGLIGSCTNSSYEDMSRAASICQQAIDKGIKTKSLFTITPGSEQVRATLTRDGQLDTMRKAGGIVLANACGPCIGQWKRTDVKKGEKNSIVTSYNRNFTGRNDANPATHAFVTSPDIVTAMVFSGDMNFNPLTDTLKDKDGNDFKFEPPTGAGLPSKGYDPGSNTYVAPSSVNVKDVAIDPHSKRLQRLTPFKKWDGKDMKGLKILIKAKGKCTTDHISAAGPWLKYRGHLQNISNNYMIGAINAENGEANKLKDQLTGEYKTVPNVAIDYRDHGIRWVTLGEQNFGEGSSREHAALEPRYLGGAAVITKSFARIHETNLKKQGLLPLTFADPAAYDKISPFDTVDIDGLTTFAPGKPLTLVVHPADGSAEWSTKLNHTFNKDQIEWFKAGSALNHMANMHKQK O13968 YE48_SCHPO ACT_SITE 199; /evidence="ECO:0000250"; ACT_SITE 266; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 197; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 232; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 232; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 267; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 295; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 565; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; SPAC24C9.08; CHAIN 1..596; /note="Uncharacterized carboxypeptidase C24C9.08"; /id="PRO_0000317321" CARBOHYD 118; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 466; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 541; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 555; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSTSNDPVVSSHDPIKQEKEQETDLEAQVEHKKRNERGNAFVGFLILIFVYYLLRGGSNDNDKQEMSHSPGSCMDSESAAVSTSAKCYIPPVLTPAKEPKLGDDVSGIDYIRSPEFFNDSLVRFQELLRIPTVCYDDMGDVGDDDRFDIFAVFQDKVRELYPNIFKKLKVEYVNTYGLLITLEGSNKDLKPLVLMGHQDVVPVNQASLDRWYFPPFSATYHNGHVYSRGAADDKNSVVAILEALEILAISDYKPEQTVIASFGFDEEVSGYRGALPLAHKLYERYGKDGVALILDEGGFTINLFGTLFATVCVAEKGYMDVHLKLKTPGGHASIPPPHTNIGLMSKLVTQIEEPFGGELTFENPFYTTLQCFAENSADMDDNLRQLIKSGDTEKMTDLFSKSRLYRYFFETSIAVDVINGGVKVNALPEETTLAVNHRVDASKGLKQVYDRYGGLLEEFGHEYHVNVTLFNGETVVEYEDAIGHIFASTAKTLEPSPVSPYDESSDAYKKLAGAIRYTFGDGTSVTPALMPANTDTRHYWNLTSNIYRWTPVSTNSTSKNSFNGHTINENMRYDAHMDSIEFFYNFILVSDSGEEA O13972 GLYD_SCHPO CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 243; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC24C9.12c; CHAIN 1..467; /note="Probable serine hydroxymethyltransferase, cytosolic"; /id="PRO_0000113515" MSSNDSIMLTPLKEQDPTVAEIMRHEADRQRSSVVLIASENFTSRAVMDALGSVMSNKYSEGYPGARYYGGNKFIDQIETLCQERALAAFNLDPAKWGVNVQCLSGSPANMQVYQAIMPPHGRLMGLDLPSGGHLSHGYQTDTKKISAVSTYFESMPYRVDPNTGLIDYDMLEHDAQLFRPKILVAGTSAYCRLIDYARMRQIADSVNAYLVVDMAHISGLVSAGVIPSPFEYADVVTTTTHKSLRGPRGAMIFFRRGLRKHDKKGNPIYYDLEDKINFSVFPGHQGGPHNHTITALAVALKQCQEPAYKEYQAQVVKNAKVCEEEFKKRGYKLAADGTDSHMVLVDVKSKGVDGARAERVLELINIVTNKNTVPSDKSAFSPSGIRVGTPAMTTRGFKEQDFVRVVDYIDRALTFAANLQKELPKDANKLKDFKAKLGEGEQYPELVQLQKEVAEWASSFPLADKW O13981 EMC1_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAC25H1.07; CHAIN 23..885; /note="ER membrane protein complex subunit 1"; /id="PRO_0000350761" CARBOHYD 66; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 302; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 397; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 502; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 526; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 687; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLRPLWPLFLTALFLNIYRAASVLIDEAGKNDFEISLLGKVNDLVYDTKNEYLYAVSQKGLLAKLNASNGDVIWRQSIAPETSQLNYNPVTNFIITVDKDYLYIWNSKNGILDRKIELADGKGKLFEVNKGFVYLNPHTRKFIELDLQASFSISIERDLQLDAISFLTYAEKNYVLFKRDGQFVLQALDHNYAVYGPETVLNVPENAQLLVTEKDVIIYSSNGVIYGIHVSMADISQLLIDEYKTFEWSSIPGKRHGYSITVDSQSTPVTYLFVIIDSEFVLIDEYIHEDTEALGYIHMEDNQTFSRVFAVANQIKFAPATVITIPNQLSRPVFRLFTFAEGEISAIVILDDGTFFSFSNTELVWKREEALAYAINPSILPTTLLTSYQKSIQDEENSSVSFLNRWYRHFNQLIDFLKHPHGFTSSSVLDDAFTTKIIIPTSTGSIFCLSSDPKQVHRILWRYDFNINPESVESWLLDISDEDPKFAFVHQWNDAFSFYILNASDGSVISQKSRDFKADEFYYVDNISKNLPNQIFAVKDYKVLPLTGDNSIFEKISQEANSIFVYTSETKVEGFSISADLTMDVQWSYNLAEGEIVIASIRRNPHEIVASFGRVLQNREVMYKYLNPNLFALFSKCKNDLVVYVMDSVTGSIVYQNKHQGIILFDKVYGVFSENWLVYSYQSDVPNLSTKIISVELFEGSHSNEKIDSNEIYSRHNDYRPYAFTKAYIFDREITTLGVTNTPQGITSRDVLLGLSSNQVAMIPQALLSPMRPVLRPNEKANDASFIPYEPIIPLNDDMVLSYNKRVYGVSQITSGITNFESTTLVLSTGLDVFFTRTAPSMPYDMLSSHFDKKQLMLTTFGILLAVLLTKPLVKKKQLNTKWYN O13984 WRIP1_SCHPO BINDING 9; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 12; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 24; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 28; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 129..135; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P55072" SPAC26H5.02c; CHAIN 1..504; /note="ATPase WRNIP1 homolog C26H5.02c"; /id="PRO_0000310280" MSGPDHVQCPVCAKTVTMNDINPHLDSHYSDSSGPSKPVSPFFKKERYKHHLETNVSSHQSATKFIEPEPSPTKKTKLTRRDTRPLAERARPKSLDEYVGQEELVGERGIIRNLIEQDRCNSMILWGSAGTGKTTLARLIAVTTKSRFIEISATSTTVADCRKIFEDSQNYLTLTGRKTIIFLDEVHRFNRAQQDIFLPMVEKGLVTLIGATTENPSFRLNSALISRCPVFVLKKLTRDNVKKILNHACLLESERLGSSMPNVETSIIDYISAITDGDARMALNALEMSIGMLRQGPLSLEDIKDKLVRSSALYDRVGDVHYDTISAFHKSVRGSDVDATLYYLGRMLESGEDPLYVARRMVRIASEDIGIADNSMLPLASSTFTAVQQVGMPEADVILAHCAVALALAPKSVDVYRSYNAVKSFLSSHPDAGRAEIPMHIRNAPTNLMKQLGYHKGYKYNPDYKDGLVMQEYLPDSIKGTKFYKLPIELKEDEEIKNLKTDTK O13987 YEG5_SCHPO SPAC26H5.05; CHAIN 1..1151; /note="Ankyrin and IPT/TIG repeat-containing protein C26H5.05"; /id="PRO_0000316206" MNLEFSFGNLIAKNTENSTKEEGTWEVNKLMKFSSEEGRSSSDDYMFSSPDFEKAGNGDAEMREFFNFDGLPDQGLNLPSIAPPSLSHASSPNLSNSQDEAECLPSDRQQDYINPSLHLNRTVFPTPQHSISDANFLANTVDQPLGDNPMFGESDVYLLKMDPMKQAPYEAGFNSVKSSGAIEDPLQFRQPITMLETPFNESINTLTPYAEDYAFSSLNTSAPPLSNKEYAFSVNHLPAINEHKWKSRVETNMLFELRIKSNDNQSVPFEYLRLPSWAHREDKKRSSKPQPLQPDPETVIHLVPTVLAGDKSSVVKTCCTRCLLRERKRNARSQATKDACMPNYTKLKAYERNMTDASPEEKQQFRIKLLNQFPKLEDIDEDRMIMVFTGPEYVRLQLDGNERVAHINARITCYSSHQSCPYFHIIWDLYSMSRLVDRLVFPEPVTVLDDHKSRNLTKSEKTGKSNSQQAPSNHVLSKSNTVPNLVTGFPTRSDNPPNEKRRRTSSSENSRALDIQLSASDSHSPNSKSTLKSVEGSAFSMSKSPSVLSMTTPSGVSPSISKNGFHVVRVPSDAAGFQQRQQQEEGVLEAHTNESAPIAPFPYCTDDFSFSVEEKSSVNNLLTQFDEVAKPDFVSTPIKENVDSSFINMTPPDVSHAPLISRIIPNKGSIMGGYEVTILGANFFNGLVCLFGDNPAAVTFSWSESTIIATCPPATNAGTVPVTFQNYNSSSEAPVMFTYEDNLDNELYKLTVQVLGLKLTGSIQNPLTLSKKLLSSWRDDFAQYITNSIKQPPNSESKGQSKKTLLHDSNMESLKSVISRIVKKDSNQSDDSVESTILAAFALVTDTTTPYLSDFSLVNESGRSLLHLTAACGLSNASTFLCNAGCDVNKRDALGYTPLHYASLYDHKDICVNLLSNGAKPDVIGASGKKPIDLSSSEPIKLVFKEANNEQAQSISRSLIKDSEGSINTNETLESTSIVNEIEESAVQTKSYSESMWNKTVTMFPSLQELPQNYMSEVPSMMQKAMLSTLKSISAIPDDVPPPYSEFADDTTAQAGSSKRDSAISEDPDHHKSVWWSLRWQSRLVGRGKSTALTPEETRAIQEQAKTLKKAGMDFMLFSFWLPALLLLSIFGLRSYAQMIGGYLYRCIIGI O13990 BGL2_SCHPO ACT_SITE 141; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O22317"; ACT_SITE 244; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:O22317" CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; SIGNAL 1..21; /evidence="ECO:0000255" SPAC26H5.08c; CHAIN 22..321; /note="Glucan 1,3-beta-glucosidase"; /id="PRO_0000011895" CARBOHYD 39; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 99; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 210; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 213; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 237; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 309; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 317; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MQFLSSFVFAALALLPLSAMAVDEAASEIASSTKPASTNGTLSFCLGVKHADGTCKYTDDYLADFEVLAPYTNMIRTYATSDCNTLEYLLPALAQSPYNFSAILGVWPTDDAHYDLEKQALMQYLPQYGVDHVRAITVGSEVLYRNDLPADVLAERIYDVRGLVQQKLGFDVPVGTADSWNLWAGGSGDVVITASDFIMSNDFPYWQGQNTSNMTNTFISDTLAALERVQSVKGTNNVTFWVGETGWPTDGPSYGEADATVDIASEFFQEALCNIRRKGIDIFFFEAFDEDWKGDSSSVEPYFGAMYSNRTLKYNLNCTSE O13994 KEI1_SCHPO SPAC26H5.13c; CHAIN 1..236; /note="Inositol phosphorylceramide synthase regulatory subunit kei1"; /id="PRO_0000341600" MALFRRPNWSALFEKIFIQKSFLGFCSLRVGCEIIIWFAIINKVSGLYGIVSLFQNSDASPWQVLMYVSSVLMLILFSWLAIHIPKSSVPHALILFYVYLIDFLLNVLFTVLFALSWFSKLVQSDSSSTEESADSDPSPSLLYLFFQAESIPSLLLLIFFASLKFYFVLITLSYSNKLIVDSGIRPQNLPPNFSGRVTRLLMKPYIMAANRSYLRNHTKRFTDSIELEQRLMDEVV O13996 YEI1_SCHPO ACT_SITE 221; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 245; /note="Proton donor"; /evidence="ECO:0000250" BINDING 99; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 137; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 138; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 177; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 190; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 219; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 221; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 224..225; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 225; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 245; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 249; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 312; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 360; /ligand="substrate"; /evidence="ECO:0000250" COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 2 calcium ions per subunit. {ECO:0000250}; SPAC27E2.01; CHAIN 1..491; /note="Uncharacterized glycosyl hydrolase C27E2.01"; /id="PRO_0000310320" MSLDKQIPIIYDFGENYEKNKDIWRRQCIYQILTDRFALDDHCTTAPSTGRMYLGGTWRGIIQKLDYIQSLGCTAVWISPIVKNIEGVTGYGEAYHGYWAEDLTQLNPHFGTKQDLTELVDQLHKRNMLCMIDIVVNHMAHAGDSPIDYSKYAPFNSPSHYHPKRFLHNYDDTWDCEIAWLGDEVVSLMDIRTEDQEVHNFFQNWIRDLIQTYHFDGLRIDTAKHVQKEFYPPFIAAANVFAFGEVYHGDPKFIAKYLEYIPSAANYPLYYQIENTFFPPKQSMNIFYQKAILEARATSMDTTILGNFTENHDVPRFLNRSTDYSLLCNTLTLLLFTDGIPIIFQGQEQMYAGGHDPENRDALWTSNYNQQNPIFQFLKKLIKLRQFLVDNVSGFTTELSNMLFVNEHVYVFRRPGVIIVVSNAGSNSDVDTSAEFSITERESLEFIDVLSGSQFSSLPTEDSSTISMNLEFSFPRVLVHRGLFHSMNELA O13997 YIH1_SCHPO SPAC27E2.02; CHAIN 1..280; /note="Protein IMPACT homolog"; /id="PRO_0000316614" MENNEEFQDELLALESIYPSCLLPISEQSFTYTLSIPDSSVRLNIQFPLDYPNSAPTVLDAYGIDKTLAEDVLLSVATGDVCIFSYMDLLKELVDIDAEQAAAERESKLQEESDKETPVMLNKSHYVAKTPEIQDEPWKPKFDWKESEPITDRKSTFMAHATRVYSTEEVREALEDLYMDKKVAKANHNMVAYRIISPNGNVIQDNDDDGESAAGSRMSHLLTMMSAENVFVCVSRWFGGVHIGPDRFKHINSSAREAVLLTDAAPSQKKGTEHGKKKKK O13998 OLA1_SCHPO BINDING 30..35; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03167"; BINDING 34; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 55; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 233; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03167" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC27E2.03c; STRAND 15..19; /evidence="ECO:0007829|PDB:1NI3"; STRAND 22..27; /evidence="ECO:0007829|PDB:1NI3"; STRAND 29..32; /evidence="ECO:0007829|PDB:1NI3"; STRAND 60..65; /evidence="ECO:0007829|PDB:1NI3"; STRAND 80..83; /evidence="ECO:0007829|PDB:1NI3"; STRAND 85..90; /evidence="ECO:0007829|PDB:1NI3"; STRAND 101..105; /evidence="ECO:0007829|PDB:1NI3"; STRAND 117..124; /evidence="ECO:0007829|PDB:1NI3"; STRAND 135..138; /evidence="ECO:0007829|PDB:1NI3"; STRAND 176..178; /evidence="ECO:0007829|PDB:1NI3"; STRAND 227..232; /evidence="ECO:0007829|PDB:1NI3"; STRAND 262..265; /evidence="ECO:0007829|PDB:1NI3"; STRAND 307..312; /evidence="ECO:0007829|PDB:1NI3"; STRAND 315..324; /evidence="ECO:0007829|PDB:1NI3"; STRAND 345..350; /evidence="ECO:0007829|PDB:1NI3"; STRAND 372..374; /evidence="ECO:0007829|PDB:1NI3"; STRAND 384..386; /evidence="ECO:0007829|PDB:1NI3" HELIX 33..42; /evidence="ECO:0007829|PDB:1NI3"; HELIX 68..77; /evidence="ECO:0007829|PDB:1NI3"; HELIX 93..95; /evidence="ECO:0007829|PDB:1NI3"; HELIX 107..113; /evidence="ECO:0007829|PDB:1NI3"; HELIX 140..168; /evidence="ECO:0007829|PDB:1NI3"; HELIX 179..197; /evidence="ECO:0007829|PDB:1NI3"; HELIX 203..205; /evidence="ECO:0007829|PDB:1NI3"; HELIX 210..217; /evidence="ECO:0007829|PDB:1NI3"; HELIX 222..224; /evidence="ECO:0007829|PDB:1NI3"; HELIX 235..238; /evidence="ECO:0007829|PDB:1NI3"; HELIX 246..254; /evidence="ECO:0007829|PDB:1NI3"; HELIX 267..273; /evidence="ECO:0007829|PDB:1NI3"; HELIX 278..287; /evidence="ECO:0007829|PDB:1NI3"; HELIX 294..304; /evidence="ECO:0007829|PDB:1NI3"; HELIX 329..336; /evidence="ECO:0007829|PDB:1NI3"; HELIX 338..342; /evidence="ECO:0007829|PDB:1NI3"; HELIX 352..358; /evidence="ECO:0007829|PDB:1NI3"; HELIX 361..366; /evidence="ECO:0007829|PDB:1NI3" TURN 44..46; /evidence="ECO:0007829|PDB:1NI3"; TURN 239..241; /evidence="ECO:0007829|PDB:1NI3" CHAIN 1..392; /note="Obg-like ATPase 1"; /id="PRO_0000356254" MPPKKQQEVVKVQWGRPGNNLKTGIVGMPNVGKSTFFRAITKSVLGNPANYPYATIDPEEAKVAVPDERFDWLCEAYKPKSRVPAFLTVFDIAGLTKGASTGVGLGNAFLSHVRAVDAIYQVVRAFDDAEIIHVEGDVDPIRDLSIIVDELLIKDAEFVEKHLEGLRKITSRGANTLEMKAKKEEQAIIEKVYQYLTETKQPIRKGDWSNREVEIINSLYLLTAKPVIYLVNMSERDFLRQKNKYLPKIKKWIDENSPGDTLIPMSVAFEERLTNFTEEEAIEECKKLNTKSMLPKIIVTGYNALNLINYFTCGEDEVRSWTIRKGTKAPQAAGVIHTDFEKAFVVGEIMHYQDLFDYKTENACRAAGKYLTKGKEYVMESGDIAHWKAGKR O14000 SYMM_SCHPO BINDING 329; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC27E2.06c; CHAIN ?..539; /note="Probable methionine--tRNA ligase, mitochondrial"; /id="PRO_0000374024" MLRKGICRLIHQVSESSKKPYFLTTPIFYVNAAPHLGHLYSLVLTDAIARFQNLKPDVSVISSTGTDEHGLKVQTVAQTEGVSPLQLCDRNSKRFADLAVAANTKFTHFIRTTNPKHQASVQEFWKTIQKAGMISFERHEGWYCVSDETFYPESAIQKVVDPATKQEKRVSMETGKEVQWSSEMNYHFLLSKFQSRLIEHYNKNPNFVQPSIFHTQVLEELKTGISDLSISRPKQRLSWGIPVPGNSQQTIYVWLDALINYISVIGYPWLNEKSSLSAGWPANMHVIGKDIIRFHCIYWPAFLMAAGLPLPEKILVHSHWTMNKVKMSKSLGNVVDPFWLIEKYGVDTIRYYLLKRGRLTSDSNFDIEELEKDEEHDLRRSLGVLLSRLQSKKLFISNEIQKQWHKKDDFTEYEDIVHELIELPVVCAQSIDGGCVYEVINLVQSVLRRVTKLFQLKEPWKLSDDSQEKIDTLMLVAHSLRISGILLQPIMPTKSTELLDQLGIPKNQRSLQNATNVFEPTEFTFHSGNNSHLFDKRTQ O14006 RT09_SCHPO TRANSIT 1..11; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC29A4.03c; CHAIN 12..271; /note="Small ribosomal subunit protein uS9m"; /id="PRO_0000030651" MFRSLAKLRCFASSLGLSSHKNIKSVPLIRNIHYIPDNPSYFTQNARFNEIYLHLENILKFAPKIIAAEEDVPKKWKTLEQYQKEFSDPKTTKVGYRKITRLLNELNEIVPEYRTEAVQKALEKFIRPDIVVKTTLKSQMLDENGMSITKGKRKSSKATVKMLPGTGKFYVNGSPFDVYFQRMVHRKHAVYPLAACNRLTNYNVWATVHGGGPTGQSGAVHAAISKSLILQEPSLKQVIKDTHCVLNDKRKVERKKTGQPKARKKYTWVKR O14012 RRP17_SCHPO SPAC29A4.09; CHAIN 1..203; /note="Ribosomal RNA-processing protein 17"; /id="PRO_0000352842" MDNTSLLTRGGEIYSRKKGKKQRLEEIVFDKEKRKEYLTGFHKRKVERRKHAQVQLEQQKREERLALRKSLREQRKRELAERLAFSKELNSSLENDEESSQQEDSSSKSDSEEESSMEPKTTEYDEDDKHVTVEIVEDDDDEEIAYPKEGFVTPRISPPPDVPLRPHKPKNAAKKKFRYESKFERTQDRRKEKIRRLKKKIRR O14013 RRN5_SCHPO SPAC29A4.10; CHAIN 1..556; /note="RNA polymerase I-specific transcription initiation factor rrn5"; /id="PRO_0000116649" MSSSINGLNESEGSTPLSTASIIGSSEQLYMTHDERYLDVLQQYEVETENKRDFDLEEEQWGVLSGSCVDGTYWSAEEKELFFQAVARNGKRDLDLIAYSIPSKSAVQIERYINALENELRWLRNHVDASVRSQCLLKYEDIPIAMEMSQNWIDWEEKIAERLLEGSNISGVETSHYNAQSVKNKTSNEDLFDTNEMRKISERFYHFDRQAPFPSNPLSAGATEFLLQIIKSKLKELIGTSIFLAESRFRKLEANNAFHRKPIIKNRDVVLSGKFLRFHRFNIPGFWKYLPTRQKMNVYKRNKRLKFQNYIHIMESDERQSKLKLGRVRARKTKNNENTMFFDSKEHSTDESDGNLGEHDVKRKVDSVPADETSINGFKKSVNQAEYPDNAQMFMDESVAEESLVEIDDSVEAYDMIQSKNYESFVWKYVLHLTDEMSTEDALFETIPLSNLLAQKRMKDKLKGSDVFTTLKITSKSLHNIDEHSDSDDEVQPICYYYKDPVVSHAPGAAEVVSELESGYVGLISYDLSNLPNSTEDPERKLAKPVSSWELSLPLK O14018 SYSC_SCHPO BINDING 238..240; /ligand="L-serine"; /ligand_id="ChEBI:CHEBI:33384"; /evidence="ECO:0000250"; BINDING 271..273; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 287; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 294; /ligand="L-serine"; /ligand_id="ChEBI:CHEBI:33384"; /evidence="ECO:0000250"; BINDING 358..361; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 396; /ligand="L-serine"; /ligand_id="ChEBI:CHEBI:33384"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence={ECO:0000250|UniProtKB:P07284}; SPAC29A4.15; CHAIN 1..450; /note="Serine--tRNA ligase, cytoplasmic"; /id="PRO_0000122198" MLDINLFQVEKGGNPEIIRESQRKRGADVGVVDKVIEMYKEWVSLRFELDNTNKSINRVQKEIGLKMKAKEDASELLEEKNSLTERKKNLIEQETAKNKEMLNVVSSIGNIVHDSVPVSMDEDNNEIIRKWAPEGVTVEKKNCLSHHEVLTRLDGYDPERGVKVSGHRGYFLRQYGVFFNLALIQYGLDFLEKRGYIALQAPTMLNKDVMAKTAQLEQFDEELYKVIDGDEERYLIATSEQPISAYHSGEWFEKPSEQLPLKYAGYSTCYRREAGSHGRDAWGIFRVHAFEKIEQFVLTDPEKSWEAFTEMINHAEDFYKSLELPYRIVAIVSGALNNAAAKKYDLEAWFPFQGEYKELVSCSNCTDYQSRNLEIRCGVKKMGDREKKYVHCLNSTLCATERALCCILENYQTPDGVNVPKVLQPYMGGKTFLPFTKELPKNSTSKKGKN O14028 MTQ1_SCHPO BINDING 124..128; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 148; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 200..203; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 200; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; EC=2.1.1.297; Evidence={ECO:0000250|UniProtKB:P53944}; SPAC29B12.05c; CHAIN 1..309; /note="Probable MRF1 mitochondrial N(5)-glutamine methyltransferase mtq1"; /id="PRO_0000353824" MRLPRITKFALYRENPCLLPLYHATRDPSLAKREWTWICKELKLLYPEISKHGLRKKIVNACQLRARNYPLQYILKSQPFGNIKIDCQQGVLIPRWETEEWVERVVDKLNRLERLKPLKILDLCTGSGCISSFVLANLRVPHTIEAVDVSKKALKLAVKNCDRAIAHGTVGKINFHQIDVLNEHERVESLLQTSHVLLCNPPYISDDDFAAQTDISVRKYEPKLALLAKNGGNEFYYKFSQYIKRMLQRNAKDFVPLSLIVFEIGSTHQAKIVKSLFDDTNWQANIEQDGAHQDRVVIITRKDRRLIDI O14035 YEME_SCHPO SPAC29B12.14c; CHAIN 1..590; /note="Uncharacterized permease C29B12.14c"; /id="PRO_0000317319" MKFSKPKFSMPKWRLTKEDFTPKGMWRNFKNFIVIEAKPGTTLAERFLTNEDLYPVPKSQRVWGPWNYVAFWLADSVNVNTWMIAGTAVESGLSWWEAWITVWVGYTIAAFILTIAGRAGAVYHISFPVLSRSSFGIWGSLWPILNRAVMACVWYGVQAWIGGECVTLMIRSIWPSFSHIPNTMAKSGTETYQWVGFFIFWLISNVAIWFPVYQIRHLFTAKSFLAPPAAIAFLIWALVKAHGAGDAIHAKTQLSTWNHGWAVTAGIISCLDNFATLIVNNPDFTRFATTPNAPIFPQLITIPMGFGITTLIGVLVGSASKSIYGENIWNPLDLLKSFLDHSNHHGVRAGVFFISTGLCLAQLGVNIAANTVSAGNDTSALCPMFINIRRGGYIASIIGICMCPWNLLSSSNSFANSLSAYAVFLSSFAGILIADYFVIRKGYLKVDALYTINPNEPYWFTYGINLRAFASYICGLLINVVGLAGAVGDKVPKAALTMNNIAYLLGIVTSFLSHLIICKIFPVTACGEKFLDERPEETDNYLLTLESTEDTISSYEETEGIPVKKVSYDSKEKSDDGKSGGIDIKESSVF O14039 RCM1_SCHPO ACT_SITE 350; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" BINDING 223..229; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 246; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 273; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"; BINDING 293; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01023" CATALYTIC ACTIVITY: Reaction=a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:47780, Rhea:RHEA-COMP:11911, Rhea:RHEA-COMP:11912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000250|UniProtKB:P53972}; SPAC2C4.06c; CHAIN 1..460; /note="25S rRNA (cytosine-C(5))-methyltransferase rcm1"; /id="PRO_0000317150" MDFYNHAANILSDLSKKKGSIKQLAFNSKKHDPKRTYALVCETLKYKPVLDEIIARSELLVLEKKLKENLARVLVHDLLMSKRGLSISNGPIKECILRHKTRLNAEFVKLKVKKGVKSHEELALKNPVSLPRWLRINTIKSTKDEVLQGLGLDKVSSIEELGPDKFYIDDCVENLIAIDPSFPIVENSLYKEGKVIIQDKASCFPAAVLAGLTGHVGDIIDGCAAPGNKTTHLAACFPKSHIFAFERDAKRVQTLRKMVGISGANNVTIEHQDFTLTDPKSDLYRNVTHILLDPSCSGSGIVSRQDYLLGNEQDVTEDTERLENLCSFQSTILKHALQFPNCRHVTYSTCSVHRLENEQVVCEVLSQEPDWKCNSLTKTLPNWKTRGIPEYCAQPSMAEGMIRCKPGAGGTIGFFVANLYHPQREQETFKMYKNDDDTKKRKRKKKKKEVKKKARIQGEE O14043 YEYA_SCHPO SPAC2C4.10c; CHAIN 1..166; /note="Uncharacterized protein C2C4.10c"; /id="PRO_0000304112" MTELHPDEQHVFLQCLNKMQKELDLSFERYERLFKTTQELQEKVKFSSSRFYNKDSTYSKDQGLAKESAALELQKLKQENVLLRKDLNNLEQISDCYAKGMDDIMKHVATYTATMNERMNACHKEYIKMYEALASERNSLYKINEQNVQSLNKVKEWLLKSLEEEP O14046 VATO_SCHPO SPAC2C4.13; CHAIN 1..199; /note="Probable V-type proton ATPase 20 kDa proteolipid subunit"; /id="PRO_0000071779" MSLFSTSLWTTTVMSIIVGLYMLFHNSGESFDFGSFLLDTSPYTWGLLGIASCVAFGIIGAAWGIFICGTSILGGAVKAPRIKTKNLISIIFCEVVAIYSLIIAIVFSAKINDINPAGFYTKSHYYTGFALFWGGITVGLCNLICGVCVGITGSSAALADAQDASLFVKVLVVEIFGSVLGLFGLIVGLLIGGKASDFS O14048 UBX2_SCHPO MOD_RES 371; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2C4.15c; CHAIN 1..427; /note="UBX domain-containing protein 2"; /id="PRO_0000211005" MDGDEASLVANFCAITNSTPEKAQEYLSVADGDLSTAITLFFESGGVTDVQSSYIEAPSQTEPVEEIRAPIAPTREVLVDPLADMSAGTSIMGNNFGFGGFPRMNRRQRRRMGIFDQSPSQIPFPSSNTEDSSEESDSSSRASRLAKLFRPPYDIISNLSLDEARIEASSQKRWILVNLQTSTSFECQVLNRDLWKDESVKEVIRAHFLFLQLLDDEEPGMEFKRFYPVRSTPHIAILDPRTGERVKEWSKSFTPADFVIALNDFLEGCTLDETSGRKNPLGAKSQKPVEAMSEDEQMHKAIAASLGNGNSTTESQGESSSQQAESHGVADDTVHKIDSAECDAEEPSPGPNVTRIQIRMPNGARFIRRFSLTDPVSKVYAYVKGVAEGADKQPFSLTFQRKSLWTSLDSTIKEAGIQNTALQFEFQ O14049 RS8A_SCHPO SPAC2C4.16c; CHAIN 1..200; /note="Small ribosomal subunit protein eS8A"; /id="PRO_0000122256" MGITRDSRHKRSATGAKRAQYRKKRKFELGRQPSNTRIGPKRIHEVRVRGGNKKFRALRLDSGNFSWGSEGVSKKTRIIQVAYHPSNNELVRTNTLTKSAIVQIDAAPFRVWYETHYGILMGSKGKKATSTPNPKSKHVQRKHSARLGDSKVDSALETQFAAGRLYAVVSSRPGQSGRCDGYILEGEELHFYLRRMAPKK O14053 UTP21_SCHPO SPCC1672.07; CHAIN 1..902; /note="U3 small nucleolar RNA-associated protein 21 homolog"; /id="PRO_0000051496" MPFAEKKRRTYENAVKPLRKSRIYAPFRSIGHVSNAVPFDIEARGTHFLVTTSVGNTFQTYDCEKLNLLFVGKQLDKEITCLKSFKDFMLVAAGSKIFAYKRGKIIWDIDVEQEHGTVTHLDAFGEWIIACTSSRHVYVWKHASKYSVPELHTTFLPNTNADITSLLHPSTYLNKILLGFSDGALQIWNLRVSKRVHEFQEFFGDGITSLTQAPVLDVLAVGTISGRIVIFNLKNGSILMEFKQDGQVLSCSFRTDGTPILASSNPIGDLSFWDLSKRRIQNVTYNAHFGSLPKIQFLNGQPILVTAGPDNSLKEWIFDSMDGAPRILRSRNGHYEPPSFVKFYGKSVHFLISAATDRSLRAVSLYQDSQSTELSQGSVISKAKKLNVRPEELKLPEITALSSSNTREKYWDNVLTAHKNDSSARTWNWKSKTLGQHVLPTSDGTSVRSVCVSCCGNFGLIGSSKGVVDVYNMQSGIKRKSFGQSSLSGKPVTAVMLDNVNRILVTASLDGILKFWDFNKGNLIDSLDVGSSITHAIYQHSSDLVAVACDDFGIRIVDVQTRKIVRELWGHSNRLTSFDFSDTGRWLVTASLDGTIRTWDLPTGHLIDSISTPSVCTSLTFAPTGDYLATTHVDQVGISLWTNLSMFKHVSTKALRLDDVVEVSAPSVSGEKGISVVEAALNVESNAEDEEDISYRTMDQLDPNLQTLSKLPRTQWQTLINLEAIKARNAPKEVPKVPEKAPFFLPSLKDQSEATVPKQPIATEISKPTAVASIKVSGTEFSTLLHGNDDDAFFEYLKSLGPAKIDLEIRSLDAYPPYEEFILFINIMTRRLSKRRDFELVQACMSVFTKSHEDVLLMHDTPEDTVPVFESLKAWESVHKEENQRLLDLVGYCSGILSFMRT O14055 SYYC_SCHPO BINDING 37; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250"; BINDING 164; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250"; BINDING 168; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250"; BINDING 171; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250"; BINDING 186; /ligand="L-tyrosine"; /ligand_id="ChEBI:CHEBI:58315"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; SPCC1672.05c; CHAIN 1..401; /note="Tyrosine--tRNA ligase, cytoplasmic"; /id="PRO_0000055675" MSLTPDEKYELITRNLQEVLGAKMIREILNERDISLYWGSAPTGRPHCGYFVPMMKLADFLKAGVHVTVLLADVHAFLDNMKAPMELVQHRVRYYEIIVKSILKSLNIPIEKLRFVIGSSYQLKEDYTLDNFRLAASTTEHTARRAGAEVVKQVASPLLSSLIYPGMQALDEQYLGVDVQFGGVDQRKIFVMAEEVLPVLGYKKRGHLMNPMVPSLAGGKMSSSAAANAKIDILDDPKTVNKKIRSAFCEPGVVEENGCLAFLKYVSFPAMELRGETEFVIDRPEQFGGRMVFKTYEEVEKAYKDLTLSPQDLKLGLESSVNTLLAGVQEQLKQYPDLDSILKAAYPDPKDLKKAMKQKKQDKKNAKKAGTTNASIAAESGAAPATESQTAESFKKLNLDD O14056 COX19_SCHPO TRANSIT 1..16; /note="Mitochondrion" SPCC1672.04c; CHAIN 17..112; /note="Cytochrome c oxidase assembly protein cox19, mitochondrial"; /id="PRO_0000122290" DISULFID 31..62; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 41..52; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MSFGAAGGSLPMTTREPPERGSFPLDHFGECTHVMKQYLECIKVKRENQEECRLLAKKYLQCRMDTGLFGKDDMKNLGFHGDENATSTSLSSSNDGNNNSNSSSSDNKTGGE O14057 GUAD_SCHPO BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 81..84; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 81; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 212..213; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 239..242; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 239; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 329; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3"; BINDING 329; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9Y2T3" CATALYTIC ACTIVITY: Reaction=guanine + H(+) + H2O = NH4(+) + xanthine; Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938; EC=3.5.4.3; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPCC1672.03c; CHAIN 1..527; /note="Probable guanine deaminase"; /id="PRO_0000122301" MDGHTCDVFVGKLIHTPSLGELEITDATVGVYNGKIVFLEKSMTPKTLEEAKSHHLLKEATIHKLKPLQFMFPGLIDTHIHAPQYPNSGIGIDVPLLQWLEKYTFPLESSLADLEEARQVYKRVVERTLSNGTTFASYFSTLHTPTSALLAEICYSYGQRAYIGKCNMNNLSPDHYCEKSAESSLEATRQLISYMSILDPKREMVTPIITPRFAPSCTEDLLSGCGELAEKHNLPIQTHISENTSEIELVKELFPERKSYADVYDYYKLLTPQTILAHAIHLEDEEIELLTKRSSGISHCPTSNSILASGLANVRKLLDSGINVGLGTDVSGGYAPSILIALRHAAMTSRSLSYVLGDPKVMLDLSELLYLATQGGAEVVSRGDQVGSFAVGKYWDALIVDLSAETHSCVDIFERDTWPVMLSKWVFTSDDRNLAQVWVNGRLVSGFEMKANLKNSTPLTNGVTSSGHQVFKELTQAHLLPRTQCVDTPPSCCGGHCCKEESCRTENCKGAYPANATVTVEEDSGMS O14066 IRS4_SCHPO SPAC1687.09; CHAIN 1..1379; /note="Increased rDNA silencing protein 4 homolog"; /id="PRO_0000116738" MDAIHPVSLRNSKRHPLLHSERNLSRRAVSPSISRSFFQHSNGSFPLFQNHRKSLPSAIYKSVDPYVDANPLDPLAAAKASFADFPEQDDSQSSTSPLSSKYHTKKNKQIFVEDSRRGGAASNAAAIAAKKSGYYERTSTRKRSLTVPTPRTSFPHHPRSRRFSLKNAAIATSYHKFKPLSSNSLSSSGMHFSASKQAFNSPLLQTFSPSPSVSPFSNPAVEKLKTSASKQAAEAQSLREFDFFTPTPEPSDKNLEKLKNGASKQASESQSLKNMESLSLARSSPILTSEKLKNGASKQAIESPPFRASEPLPSSNIIPNPAMERLKNGASKLAIESQPFKSAEPLSSAIPLPNPMSEKMRNGASKQAIMAQSSKINPLPPLTASISDPSFEKLKNTASKQAIESQSLMNSGPELLEPSISDPMLEKMKTDAGKQTVESLSLKSSDATIPKPSVSDLGVEKLKNDASKCAVESQSLMINDPSVSSTSFYNPNMEKLKNGAIKQAIEHQALNAAILNKTQLPYFHQSSSELPISASKRAALSQQTESASKSSSNISEMCDSHPPSNFSISASQQASKDRFSEATSSIDLDLSPGRSLSLASSKLSVKEAGARVYNRSVATPVMTPSNPFEISKSASQLASIAQVPVSEPAKTSEVNLKKSLSLASSKLSFQEAGTSLKEKTANVQHSPEVLNDRSLASLSASRHADAISSKSKQHTEIAQPAFNTTGTVLMKTKSNLSDSALSTPQHSDSVLFDITSKAARLASTCAKTDLHRKPRRKHKSFTLENYFGHNAEDESPQSDEVESQTPPSGYSENDIGGTDIYPFALQGAALAAAKDFSRREASLSDSQSAASMDMLPMKKKLSHSSASSTRSIKSLLTNANQKHIHSSINETDDIPTMAAHIVATGQKNKEKAPSFSNDQALDHLLGSAHKRIPSNKTEWSSSSLHIPSHNSFSDIHHRKIAAHAAAITAASEKLTPSIEETSYSSSKAHDASLSAATLVANKDKLIHAPTPQVLAPVLPKVSLPHRHSVSLGQIRGESEVEGDVFYDAPSDKEDLGSSNAPLDVPHGANRSSMDEVNGSKYDYSDGILDGSGQYTDSDMSDDENSLKDSQSSVLSFSAVPTKVLKFKLRDVLGSEYSPSPQLLASSSDVSGSSSAVRAAMKADKIFPAVHENPPPLKTKQSIAKPSPHTLRVPQKKHKHFYHRDDGKYKSGTNLRKSETVDLPQFFIDENRRKLYEGLWAANKGYLLSKSEYSKPNDLICNIVVRELWSRSGAPTSVLAKIYDLVDRHHTGVLGRDEFIVGMFLIDQYLKGRKLPLKVPDSVWLSSKRMGDMLWRLEKLQKKTDNKKPFFKKKKKKRKHLKKFFDFNTTAKVNEGAMTD O14069 RL28_SCHPO MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1687.06c; CHAIN 1..134; /note="Large ribosomal subunit protein eL28"; /id="PRO_0000122398" MSVSNDLIWQVIRDNNRFLVKRPEFGGIQFNREPVNVSGKNAQRFSGLCNDKAVGVQANSPRGVVLITKTNPKNAQKPAKLFRKDVIANASSRKTYKSIAGRIGRTGYRDDLVKVSVARASAILSSQRPKKTVA O14073 YEA8_SCHPO ACT_SITE 647; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 722; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"; ACT_SITE 755; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084" SPACUNK4.08; CHAIN 1..793; /note="Putative dipeptidyl aminopeptidase C2E11.08"; /id="PRO_0000122422" CARBOHYD 101; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 136; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 246; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 299; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 303; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 324; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 336; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 377; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 384; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 407; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 535; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 761; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNDFSFEDKGLISRSGFGSRHVRRVVKALALIFSLLILYLTISNVSDSPPKRDSLSLDDIVLQKYKPSYKQVNWIDSQGLKDTFLVKYGDLINIQDPYNLNKTLFSVSDLVYNGIQLDYDSYSISFDAKYVLVSVNKSQRWRHSSFAQYYLYNTETKDVNMLGQDNEHWTISLAEWSPTGHQLSFVYNNDLYVRKNDGNVQRLTYDGTVDVFNGLTDWIYEEEVLSSPSTIWWSPDSDKIAFLKLNESEIPTYHYPLYTAELDPSLPEFDYNKDMAIKYPKPGNPNPSVSLFVADLNSNASSNFSLWHNEPLAEPVVQNVLWVNTSSVLVQFTNRNSTCITARLLDTELKSIHTVKTECLEEGWYEVQQSAKMFPLNNSLVWENWSDGYFDILALDDYNHLAFIPFNGSSPIYLTSGAWDVTDGPIHIDGDFGNVYFLATLKDSTERHLYYVSLDTLEIYGITDNGEDEGYYSTSFSPFGDFYVLNYHGPDVPWQELRSTKDKDYCLSLETNSRLKQQLSSITLPSVEYGKLTFNDTTFNFMERRPRNFDVNKKYPVLFFAYGGPGSQQVAKLFRVDFQAYLASHPDFEFIVVTLDGRGTGFNGNAFRYSVSRHLGEWESYDQGQAGKFWADLPFVDENHVGIWGWSYGGYLTLKTLETQDVFSYGMAVAPVTDWRLYDSVYTERYMDLPQYNKEGYKNSQIHDYEKFKQLKRFFVAHGTGDDNVHFQHSMHLMDGLNLANCYNYDMAVFPDSAHSISYHNASLSIYHRLSEWIGDALGRIDPSTGVRQHRWD O14076 YEAB_SCHPO MOD_RES 167; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPACUNK4.11c; CHAIN 1..188; /note="Uncharacterized protein UNK4.11c"; /id="PRO_0000122440" MSSKLLSMKFMQRARGIDPKQAEEELSKNIVTDEHWSLAGKVDFLPQKMTRNVEYESGYGGLIEENDLESHSNEPNLVQGRASFGLFNKELGEENVDEKDVSKNEEVDVNGTKITDTSELTERERRKQELVSKKAEASRKMEVKAPAKESKKRKVNELSQDVISLHSPKESNARKTKKNKNKKKKKRN O14077 MU138_SCHPO ACT_SITE 71; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096" BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"; BINDING 72; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"; BINDING 149; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096" SPACUNK4.12c; CHAIN 1..969; /note="Putative zinc protease mug138"; /id="PRO_0000074429" MDGKPQVEVIVNGQVVPNLDDREYRLIKLENDLEVLLVRDPETDNASAAIDVHIGSQSNPRELLGLAHFCEHLLFMGTKKYPDENEYRKYLESHNGISNAYTASNNTNYYFEVSHDALYGALDRFAQFFIDPLFLEECKDREIRAVDSEHCKNLQSDSWRFWRLYSVLSNPKSVFSKFNTGNIETLGDVPKELGLDVRQELLKFYDKYYSANIMKLVIIGREPLDVLQDWAAELFSPIKNKAVPIPKFPDPPYTDNEVRKICYVKPVKNLRRLDIVFPIPGQYHKYKCRPAEYVCHLLGHEGEGSYLAYLKSLGLATSLIAFNVSITEDADIIVVSTFLTEEGLTDYQRVIKILFEYIRLLDQTNAHKFLFEETRIMSEAQFKTRQKTPAYQYAHVVASKLQREYPRDKVLYYSSVLTEFDPKGIQEVVESLRPNNFFAILAAHSIEKGLDNKEKFYGIDYGLEDLDSQFIDSLLHIKTSSELYLPLANEFIPWSLEVEKQPVTTKLKVPNLVRNDKFVRLWHKKDDTFWVPKANVFINFISPIARRSPKVSVSTTLYTRLIEDALGEYSYPASLAGLSFSLSPSTRGIILCISGFTDKLHVLLEKVVAMMRDLKVHPQRFEILKNRLEQELKDYDALEAYHRSNHVLTWLSEPHSWSNAELREAIKDVQVGDMSDFISDLLKQNFLESLVHGNYTEEDAKNLIESAQKLIDPKPVFASQLSRKRAIIVPEGGNYIYKTVVPNKEEKNSAIMYNLQISQLDDERSGALTRLARQIMKEPTFSILRTKEQLGYIVFTLVRQVTPFINLNIFVQSERSSTYLESRIRALLDQFKSEFLEMSDEDFSKHKSSLINFMLEKHTNLKEESSMYWLRICDGFYDFTRLEKQAEIVSTITKDEFYSFFINNIHYEGENTKKISVHVVSQRCEDEVYEIPNVTIIENGNMFKESMTLSKAAFPLKPFDEIDRSLLFN O14081 TPSX_SCHPO CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 145; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 149; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 150; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 177; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 189; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPACUNK4.16c; CHAIN 1..944; /note="Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 106 kDa subunit"; /id="PRO_0000122512" MGRILIAHLFLPSSVGFSFDTVPHDEVGSKFMQKEESKDWIADTPLDESAIVSEEESDDDSLLSDLPEEIDSTNAQSNIATPSPGTVAAAISGIQPPPKTPSSDSPSLENSLSNLNDLFKSRGRHMAFSKNDGTNLSLPPSRHQSPPPSSVLASQRHHRRHDSELEEFARRASRSLSFSMNGTPQRRMTFDAEAWKNVIFKIKPSSFGNASFYNAISAATRSKQFDDHLFVGTCGIPTDSLPDSLKERISHDYITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQIPDNPKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQDSEHLPHISDIVTRINSAYSNIASRHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKEQIDMQRIPAFTAQLIKEPYQNAQKRLILLYFEGTISTWGSQYHNVMTSLQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQRVPKLGIVAENGCFVRSPPKGDATMPVSKKEIAELWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAAMWAAKECCESVNNFNVPCSATIQNDMVVCRSNKVSKRLAAEDIYSANGGDYDFIFAASNDPDDDTVFSWMKNFKQSKKEVVPFTFSVCVSEHGNSTNADAESSGVFGFLQALEKVYSA O14085 SEC72_SCHPO SPAC2F3.02; CHAIN 1..192; /note="Translocation protein sec72"; /id="PRO_0000311764" MVAKQESVVAPQVDVSKWSGKELELGKKVNEYAKSLATFKYPFFIPPPYPPAKPNMALSTQVNKMKQTANEAFKRKKYEEAKKLYGLALQLALNRCTWEPSILTREEASVMLCNRAAAEIALSQFPEALADANAALKIRNNYGKCYYRKAKALEAMHRIEEAKQVVRDGLILAEPVTRNELVALWASYTEKD O14086 RPA49_SCHPO SPAC2F3.03c; CHAIN 1..425; /note="DNA-directed RNA polymerase I subunit rpa49"; /id="PRO_0000073954" MAGDELKGKKRKYRDSHSGDEKSVKILPLSESSLPPLVTTISGFYPPENTRFQLLKKSNQSNRDASLIGRTERVQFEAKNQSTATVEANYCLAVADKTGRVKKIVPAKYLNTFERNILALQEKDKFLKKKHGTVSGTVMEQRANLGLAFGTRKSQKAIMEESANRVKAETLGDVKDQLVSNVQKATEALPTQEDIAAAQAQDRPIPPVNVGAESIEDAYKLEDIIPKEEFSAIYIKPLLENPDERNWAKLLPYRHSLFINERFQRLLSIEEVDQKRARILYYISLLQAFLFSRRSVGNRETLRKKLADPPEILIDGLIKRFTQTTGIGSVQVSSREVDKIICYILVLCLIVDNYSTDVLTLANDLNVKTMKANELFRTVGCRIMAYTETQRMALGLNKTDAKNHKRAVLKIPLEFPKPRRGRARN O14088 YER5_SCHPO ACT_SITE 50; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q76L36"; ACT_SITE 111; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q76L36" BINDING 45; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 139; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 162; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 191; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 196; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 232; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 233; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36"; BINDING 237; /ligand="NADPH"; /ligand_id="ChEBI:CHEBI:57783"; /evidence="ECO:0000250|UniProtKB:Q76L36" SPAC2F3.05c; CHAIN 1..275; /note="Uncharacterized oxidoreductase C2F3.05c"; /id="PRO_0000310310" MLGSFVKLNNGLKCPQFAYGSYMVNRTKCFDSVYAALQCGYRHIDSAQMYHNEADCGRAILKFMEETGTKREDIWFTSKLNDLSGYKSTLSSIDASVKACGLGYIDLFLLHSPYGDRIESWKALEKGVEEGKLRAIGVSNFGPHHIQELLDSHPKIIPCVNQIELHPFCSQQKVVDYCESKGIQLAAYAPLVHGEKFGNKQLLAIASKYNKSEAQIMIRYCLQRGFIVLPKSSTPRRIKENGDVFDFEISKEDMEKLYNLDEDYHSDWNPCVSPL O14093 VPS54_SCHPO MOD_RES 483; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F3.10; CHAIN 1..949; /note="Vacuolar protein sorting-associated protein 54"; /id="PRO_0000339878" MERISSAPSISLGYPPTESSAHLAPSFSDSATSTLSFKSLLEDPVNPIRPVYTPTRTEITPVTLSPIPITPVREFQPYLHEISQEYARYSKQKRASLRRYLEKHGKLEGSMKESSINGSLLRRSSVSTILRPASESSYPNSNSETITYDIDDNVNPSSSLVDNFSISSVPSVFFQSDFNLDDPQIFDVVSEHIDITQTSDAPNSNRNLLLNNSMLQEKISWYLDTVELHLLQEIENASDSFPMIIDNLKQLKKETRDNVEETKHLLEKLTEVNVMCDRHMDAISSEELACHQLTQLKKVVQTLEDIYSEHKKVSEDVKDQRFLEAINGINSIVTQLKKKSTELNVDLLSLPSVKSLREEHKVLYHTVSQSVVQQFSKFLTSDMHKFSTILDSNELKDIYLSKNRLIPSVTKSLPSAMEFDADFLHEVDVCIDCLTLTDSLQAALTLYKTAVFEAFENLAQQYFTDGVEMRSVRKSSDLRRSLSAASLSSLSDSSRRSSSAANPFQSMSITEFAEMLTNIYFSSLECLRRIRSQIKVLIDILSKKDTKQYHLSVILNDLMATSSDVVTQQVTTINNLRFRVLDTYPPNNVIYLFSLHIIFHNELESLCGITQSSFIPTIMRQLLDWFKNFQRYSTQKLASSFERELWEAIPVEPSCQDLANRVFECSGNTPVEWTRLLSPEAEKEDENHRVHHVKVSEDCTATVSFGKQSLHIVRSSVTLLETLDDYGKLLAHFSRLAPEFQTGMLDMFRTLNSRVYQLILGAGTVRSSGLSKVLGKHIALASQTIALFQLSLNSMCRYLSRVTGTRLTNETNKLDQDFTVHHLQIHDKFVSLMRERVAISCSQIASLSWDIDSPHGYIIDLSKSLIKLYKVLHRYSQRDCVEVIPDVIRMFEDRLQLELTDIARNPSKWPGVRIDLSYFYDMMASKCGYAGDRTLLEKFERTPEQQEAA O14094 PPX1_SCHPO BINDING 40; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 42; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 116; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 116; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 138; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 200; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate; Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.11; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; Note=Binds 2 manganese ions per subunit. {ECO:0000305}; SPAC2F3.11; CHAIN 1..384; /note="Putative exopolyphosphatase"; /id="PRO_0000158600" MKLGRFLENGREQIRNLLLNASTVSSAPSFSFVSGNESADLDSCASSIVYAYCLQRKQLGRIVVPFFNIPRKELRLRPELSYLLNLASISSDDIVFLDDIVKLPKRIFSNPIYLVDHNSLDRKDLENFNGSIAGIIDHHKDEGGSLHADPRIIEECGSCCTLVCRYFMPVIRSLYDSKVSELHQTATNLAVLALGPILIDTGNLKNEKTTDTDVKIVNDLCSFVPKDWVRDEFFDTLKEKKKSCKGFSFDDLLRRDLKQYFPDGIVVNYASVGKGLDWIKKKRLGWEDELKSFAEVQNSDLVIVGLSLSKNDEFGRQLILYKRTERGAGLADSFLKLSKQNLGLEIIEEKDNGDLSMWNQRNSAASRKKVVPLLMDSVKQVASK O14095 PLP1_SCHPO MOD_RES 272; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 275; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F3.12c; CHAIN 1..279; /note="Thioredoxin domain-containing protein plp1"; /id="PRO_0000120171" MTSFPASHGFGPRKRGYQMDLTNVQPVENKPAWISMKSPLEKEIANEYEALKVTERKEDTQDYNEPELHNSNDPTVDLYADTYATQAATESDSELEDALFSQLDEFDDTAYREQRLEMLKKEFARVEAAKEKGHMQFLTVENEREVMDFTLSSKKVVIHFYHPDFIRCKIIDSHLEKIAKVHWETKFIRIEAANAPFLVVKLGLKVLPAVLCYVNSQLVDKIIGFADLGNKDDFETSLLEFRLLKSSAIDRLKEESSSNKSIYHDELQNNQSDDSDFFE O14096 QTRT2_SCHPO BINDING 307; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03043"; BINDING 309; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03043"; BINDING 312; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03043"; BINDING 338; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03043" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03043}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043}; SPAC2F3.13c; CHAIN 1..649; /note="Queuine tRNA-ribosyltransferase accessory subunit 2"; /id="PRO_0000135570" MAISSLSSPSGARVSSVTVKNKVLKTPCFFLPTSRGTVPHLTPDNVEEFDIPALYVGLEDCLDRLEASPILTNEGTIKKWIAAPSVQPTLLAPRRTSPLPSVSAGQSHINIVTASGAKKLTNDLYIKAVLKLCPELVIPLNDTPTSPPGVKRKPKIVERSVNWTTELLLALKATDAFNTTKVFFPVPDLDTQYLTPIFQFFQENQLANNIAGLAFSNNVNPLPADLVGLPRLSIQKFESPLEILKCIQRGIDIIVPDMITQATDAGVALTFSFPPPSKDVLNSKIELGLDMWDERFATDMEPLQSGCVCKTCRRYKRAYVRHLLQARELVAWILLQLHNVYAFTAFFQGIRASIQEGNFDEDVRKFEEIYMTSFPASHGFGPRKRGYQMDLTNVQPVENKPAWISMKSPLEKEIANEYEALKVTERKEDTQDYNEPELHNSNDPTVDLYADTYATQAATESDSELEDALFSQLDEFDDTAYREQRLEMLKKEFARVEAAKEKGHMQFLTVENEREVMDFTLSSKKVVIHFYHPDFIRCKIIDSHLEKIAKVHWETKFIRIEAANAPFLVVKLGLKVLPAVLCYVNSQLVDKIIGFADLGNKDDFETSLLEFRLLKSSAIDRLKEESSSNKSIYHDELQNNQSDDSDFFE O14100 ZDS1_SCHPO SPAC31F12.01; CHAIN 1..938; /note="Protein zds1"; /id="PRO_0000249236" MSSSSVSNTLSIETKSDPKDPAFVASQESTECNEHDTTQLSGSSSEPLENNSSLTRSTDDPSVEIRSKLVSPDNEANLLSDQNITISNENNNENDTTEEAETSSGNEAADDEDSSSDAQSSVPSFSEIHDGMSEEELDKERKTLTHLRRISLQGADDPEIPTDWSVAMSPPETEQDASTLFWVPANLHPELNPTGWKSFLDLQVKNLKSPTATDTSSSPLEHIRSLRRRKSLLSRQVKADDAVINYQDGSPIVEKAYLKRHRSLRLNELEHLESLARDPHRMVSLVDGMSNGSPEDSPLLVSPNHFLQRSSRTTIRRTGASIRTIHRGKTSTLSGNRSHSILQKPTDTSPLHKIEPISADELVESDDSRTSALSNSQNPSDDVENQSDQALEVLSLTNPPKIDNASADTTLHKETNKIDKLYVSENKAESAVASESSLSEGTLALKAPAPENKPEKSSTSKPPVPENKAEDSVVLKSSVPEDKSENSIASKPSATEGIPENAIALQSSVPENKAEDSVVLKSSVPEDKSEDSVPSKSSVLEDKHENSVEIDKKADDSLPSNNKTEGYTPSVVREEKNYSEPNASPSVIPPRVPTPVPGRTLSPKPTRIPTPIPSSLNVSLESSKKPEIFHERHIPTPETGPNKPSKNNILKSTQVPVTPKQKSSTANKGSTSSPSPPSSESKKTKRSWGRLFVSGDSDKEHKEHKKDKQKKKNDQISSSSKSASSFKKDRDKESIFGSLFGSKKKQTEIPPVSSSPPHNDAPPKAKPISAPSELPNTTSVAEAKCQTVTDDEGTDQQSDEKSTEPKTFIPDKDYYWSRFPICTERAIYRLSHIKLSNAHRPLFQQVLLSNFMYSYLDLISRISSNRPMNNVQQSTAKPIRKDINGQQRRSEFSAENVKNELENLSYQFGDQRKRNLNRKGSTIHTVSQNIQKVSKNAK O14102 SAP49_SCHPO SPAC31G5.01; CHAIN 1..335; /note="Spliceosome-associated protein 49"; /id="PRO_0000081957" MSIREDRNQDATIYLGNLDEKVTDSILFELCLQAGPVVNIHIPRDRVRNSHNGFGFCEFLHEQDVEYACQILNQVKLFGKPIRVNRASQDRGVNTLIGANLFVGNLDPLVDERVLYDTFSALGQLVKAPQVARDENGRSKGYGFVSYDSFETADAAIEAMNNQFLMNKPITVSYAFKREGKGERHGDIAERKLAAAAKKNKVAVTPQSTLPPGFSPATPAPTSAANTPATIAATSIPPVPNVPLVGATTAVPPLSIPNVLPFTAAQHFPGMPAMPMMNVPMGPGGAPLVPPPPPGMVMASPSPAAATIPGAPVMPNIPFYQTINAQNGYSQQQRR O14103 ROT1_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC31G5.02; CHAIN 22..232; /note="Protein rot1"; /id="PRO_0000333416" CARBOHYD 83; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 129; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MHLLYQIGLFTCLWLTQYVGAEIDNYDENLVGTWSSKSETVLTGPDFFDPLDEDFFEPELPGISYSFTDDGFFEEAIYIIKSNATKPQCPKGFLQWQHGTYAINDTGTLVLTPFVGDGRQLESDPCTSNFSVYTRYDQVETMEKYEISMDRYHGRYKLELYEWDGTPKQPMFLAYRPPKMLPTSTIAVNTIQTAAKRWTAPLVPLAQKHTNTIWWVGLGLIAIGSIGYLVVS O14105 RPE_SCHPO ACT_SITE 36; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P32719"; ACT_SITE 175; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P32719" BINDING 9; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 34; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 36; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 70; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 70; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 146..149; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 175..177; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 175; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P32719"; BINDING 197..198; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P32719" CATALYTIC ACTIVITY: Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate; Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121; EC=5.1.3.1; Evidence={ECO:0000250|UniProtKB:Q96AT9}; COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q96AT9}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q96AT9}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96AT9}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96AT9}; Note=Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250|UniProtKB:Q96AT9}; SPAC31G5.05c; CHAIN 1..228; /note="Ribulose-phosphate 3-epimerase"; /id="PRO_0000171594" MVQAKIAPSLLAGDFANLEKEVGRMLKYGSDWLHVDVMDAQFVPNLTIGPIVVKAMRNHYTKEEAFFDCHLMVIEPERYIDQLADAGASLFCFHYEATEKHEEIISRAHEKGMLVGCALKPKTPVEVILPFVEKLDMVLVMTVEPGKGGQSFMPECLPKVEFLRKKYPTLNVEVDGGLSLKTVDAAADAGANVIVAGTAVFHAQSPEEVISGLRNSVMKAQETKPWFK O14109 MAF1_SCHPO SPAC31G5.12c; CHAIN 1..238; /note="Repressor of RNA polymerase III transcription maf1"; /id="PRO_0000116721" MKFLELADLDTVNNALSFDADDCRIRGKCELYTTKSTNSDKKLFKAIENRCQEDLFALSSSKSPEYAFSLTQQSPFGPLDQSSSRRTFMYIVATLNASYPDHDFSSLQPTDFYKEPSLSRVVDSVNSTLNNIGRGRLSVNGIWEIIDRHINLSDCSVYSYTPDSDSDPYGDDALIWGMSYFFFNKNMKRMLYLSLHGLGKEVSGRNRYGNDDDSVFTPLADDAEPSDFDDDWVANMDD O14110 GCST_SCHPO BINDING 219; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 248; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 385; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC31G5.14; CHAIN ?..387; /note="Probable aminomethyltransferase, mitochondrial"; /id="PRO_0000010765" MNRSAALSILKRQSSTAASSSLKRTPLYDLHLKEGATIVPFAGFSMPVQYKGQTISASHKWTREHSGLFDVSHMVQWFVRGENATAYLESITPSSLKELKPFHSTLSAFTNETGGIIDDTIISKQDENTYYIVTNAACSEKDEANLKKHIENWKGVELERVQGRALIAIQGPETASVVQKLIPNVDFSVLKFGQSAYVDFKGVKCLFSRSGYTGEDGFEVSIPEEVSVDFASTLLADTRVRPIGLGARDTLRLEAGMCLYGSDIDDTTSPVEGSLSWIIGKRRRKEGGFVGSSRILKELKDGPSRRRVGFIVEKVPARHGSAVEVDGVEVGQVTSGCPSPTLGKNIAMGYISTGLHQVGTPAHIKVRNKLHPAQVVRMPFVETHYYK O14112 RS10A_SCHPO SPAC31G5.17c; CHAIN 1..144; /note="Small ribosomal subunit protein eS10A"; /id="PRO_0000116374" MLIPKENRKAIHQALFSQGVLVAKKDFNLPKHPEVGVPNLQVIKACQSLDSRGYLKTRYNWGWFYYTLTNEGVEYLREYLHLPAEVVPATHKRQVRPTAPRAGRPEPRERASADAGYRRAEKKDEGAAPSGFAPSFRGGFGRPQ O14120 MVP1_SCHPO BINDING 320; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 322; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 346; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250" SPAC3A11.06; CHAIN 1..664; /note="Sorting nexin mvp1"; /id="PRO_0000238601" MGDNVFLEPDPWASSSNWGSPVKPLNYKTAIGNSSIPLQYRNYWDVFQANNVLLFPEEESYSDIFHVPQDVMKEFFTLIESSSNQPLRQIQFFVLLALVACYQLGVPSTLEQIFKQRNVLPILQRFNPELFNRSSDNETPLFPNNSPPASTTALNLSSNIVPSINESKILEQEDDDVSNKSLPHAQQSIIRSFPDIQKQPKGFFSYPSSTVSSIAPSTLEAGNLHSQQPPKFSVDSSVDDNAITPRKPFSKIPNRLSPSTQPLLSNSRHSSFRLASSSTSFPASLEMNVDIDLEPSGYFFYRHNNYIISDSSNTREVLRRYSDFFWLHSYLMKKYPFRRVPLIPLKKFHSKCFNSKQFFRTPPPGLSDFVNDLSHHPIFSNDEVVRVFFTEPNVFKNWRRENQKRIDQEIEQFLVVPQSQVPDASETVKERLLKLNMSTTTAINNQLNIFRIFEKMIFTLQHFHEDFLRLQNSFNCLLDSGLYHQVFTSTFAQNESKIMSMASGHFYNIDSLLHQQNDAVKHTFLLGLSKEIKILISLRLLIERISEVFSTDLTKVRHTISNDENLLRETANSDESGRNRTFLNRSSKKRAENSLKSKKELYLKNLNQRYQIAHELEQELSYLQDYVFSLGNPYVEYCKQHVKLEEESLKIWHTLESDFSRLET O14121 NDH1_SCHPO BINDING 93..123; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 255..291; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9; CATALYTIC ACTIVITY: Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+); Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; TRANSIT 1..37; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC3A11.07; CHAIN 38..551; /note="Probable NADH-ubiquinone oxidoreductase C3A11.07, mitochondrial"; /id="PRO_0000337257" MLFSRSILRGMPKAGIPKSPLALSASRNLRLANSVRFASDAASSPKSTTSKWKILKRTTLGLFATAVVLYGANVYRFRHPDPHQPLPDPSKKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKSCYVKFYEAECTDVDADKKVIHIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPAETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTAENIHVEVKNPDGSKQEEVIPYGLLVWAGGNRARPLTKKLMEGSEEQNNRRGLVVDEYLKLKGYKDIFALGDCTHTAYAPTAQVASQQGAYLGQLFNKLGSLNFEKPSEDRHIALGDEMDSSTLISLANEKHASTKVFLPFKYSHQGSLAYVGHEKAIADIEVPWFGKQLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL O14123 NAH2_SCHPO MOD_RES 442; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 446; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 448; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 735; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3A11.09; CHAIN 1..759; /note="Probable Na(+)/H(+) antiporter C3A11.09"; /id="PRO_0000052406" CARBOHYD 699; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 713; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAWSQVEISKPHLAYAIIGGFTSLFMLCSLIIKEKLFLGEATMATATGLIFGPYVAKLFVPTSWGNTDYITEELARVLLVVEVFAAGAELPRAYMLRHWRSMFVMLLPVMIFGWLVSTGFMYALIPRLSFLESLAIAACITATDPVLASSIVGKGKFARRVPGHLRNMLLAESGCNDGMAIPFLYLAIYLIIEKPARHAGRDWVCIIILYECTFGCVLGAIIGVIARKMIKFSERRGLMDRESFLVFYFVLALFCGGIGTIIGVDDLLVSFCAGAAFSWDSWFSKKTEESHVSNVIDLLLNLSFFVYVGAIMPWPQFHMPHMDLSVWRLVVLAICILIARRIPAVLLFKSFVPDIINWREALFAGHFGPIGVGALYTCLVARAELEVHSTVPEPNDAIENPEIPNWYCIQVMWPVVCFLVLSSIIVHGSSIAFFMLGKRINTLALSFTRTRDSHFAFNLPRVRQGQSLPIKRVDALRSSANSIASSIRRRHPVNIQEDEDADISTVSLPEAAHLREERAESPRGGHYDAEEFPSEDYESRQPRRSNEEDREEEMNPGDETYLIGEDLVVEDSQGNIISHTSSRDANGPSIDEKLAQGDPKAKSFGRKFRSFLRRSYDTFQRNLHEPDDERQREPTLGHIESSIENHRPRYSRQNSESHLRENSVERRRREQVLTNIGDSESEDDNIPRPGIVPFYNENNESSSDTRNGLLSDNVSESRSRRPSRAPSAAVSSEGSPVEEDNEAQHRPNIRFLELTRAWE O14124 DPEH1_SCHPO BINDING 67; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 181; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 181; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 250; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 271; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073}; SIGNAL 1..39; /evidence="ECO:0000255" SPAC3A11.10c; CHAIN 40..409; /note="Uncharacterized dipeptidase C3A11.10c"; /id="PRO_0000314654" MVSDSKLELPLPVNQQKPRRRRILKVHLLIAALILSAVGYLGKGKWIWTPERKAHFVLTHFPLIDGHNDLPIYLRENYDNRLLNISLEHLPGQTDIFRLRQGHVGGQFWSVFVECPSLDSNSSLSWNRTGEYEAVTQTLQQIDVVKRMALYYPKTFSLTDHSGKVKFDFLRNHISSMMGIEGLHQIAGSPSILRQFYDLGVRYATLAHNCDNVFADAAVDGKRTNKGLSPAGRDIVREMNRLGMIVDLSHTTPETMHQALDVSVAPAFFSHSSAKGVYDHPRNVPDDVLIRVKETDGVVMVNFYPAFISPHPENATIDTVVEHIMHIANVTGSYRHIGLGGDFDGIDMVPKGLEDVSKYPDLFVKLAERGLSITELADIAGRNVLRVWKTTEDLGHSIHEPPLEWEDDF O14126 PRS6A_SCHPO BINDING 226..233; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC3A11.12c; CHAIN 1..438; /note="26S proteasome regulatory subunit 6A"; /id="PRO_0000084707" MSTLEELDALDQSQQGGSSNNEGLDGIEQEILAAGIDELNSRTRLLENDIKVMKSEFQRLTHEKSTMLEKIKENQEKISNNKMLPYLVGNVVEILDMQPDEVDVQESANQNSEATRVGKSAVIKTSTRQTIFLPLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMRKSKTLQYFA O14131 MU191_SCHPO MOD_RES 361; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3C7.05c; CHAIN 1..442; /note="Meiotically up-regulated gene 191 protein"; /id="PRO_0000278631" MSENVYLNEALNVVDQCFKTFFDKYTDRMGSAFACSGTIDKDHIFLVWSVAVYAEAMADSLRYTSKFERKFEHVFQALKKYWSPVFNACCAFHYFEGNDDVYYDDNAQVAIGLATAGYYTTNSSRRDHYVSRAESIISLIINKGWNQQRGGIAWHTRTTGPPWTNLNACSTSMSAVAALRLALALDDPNKKQHLVSFAWNCVRWIQENLLDENHIVCDGLSLKDGKWVLDKARFTYNTGTTMTAMSLLMGLGEFTKGLQDIEKLPTYLEDMARGALDTNGPLYDQSCNGSFKVWSDNTFFAQHLSEGLMTFSYAMPSSALAKPAQKMVLDQADFLMKYLRIPKEGLYYRNFGLYKLSPELTASFNKFFNANKQFQPDKDERIQQEGPVEQRPLCPTLIGSAGAARMLFSAAEIVNRNNPSSGESTTLPQPSHGKKDKDCVIS O14133 ATE1_SCHPO CATALYTIC ACTIVITY: Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg); Xref=Rhea:RHEA:10208, Rhea:RHEA-COMP:9658, Rhea:RHEA-COMP:9673, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10638, ChEBI:CHEBI:15378, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:78597, ChEBI:CHEBI:83562; EC=2.3.2.8; SPAC3C7.07c; CHAIN 1..391; /note="Arginyl-tRNA--protein transferase 1"; /id="PRO_0000351080" MVLDKLLYTGYNVSTECGYCKSGRKTEHFGLLAEKLSCEDYQRLIDLGWRRSGHYLYKPNGKTSCCSLYTIRLDSYNFKIAKEQKKAIKKWVKYVNGKPLKPMKSEISTDYLNNAFQTIESLGAEKYSVTMEPCTYTDEKFEVFKKYQMQVHLEKEEEITKKGFSRFLCNSPLFNEDKGIKYGSYHQMYRFQGRLVAVGVLDLLPHGVSSVYLFYDPDMSKFSLGRISACREIWLALECGYRYYYMGYYIHTCPKMKYKATYSPSYLLNPGTNKWIPIENFTSLWNTGAPKYISFGDENNSDIQTAVDYDSSEDSSQNEDDYTLFNRQLPGILSVNVAESLVSENFANIGNSTFPTRHVLSYFPQVKHWFVEINAAVGEEVAKSYTLVLSS O14136 PEX13_SCHPO SPAC3C7.10; CHAIN 1..288; /note="Peroxisomal membrane protein pex13"; /id="PRO_0000310479" METNQNEKGPSLPSYPAGGIMSVSNSNADTNQGVTQHPLANRIVNPNYYNMGFNPYSGFNSFIPSFNPFVPLETNLPGNGPISSLQVIESIVGAVGSIAQVLESTLMAAHMSYNTFVSVSENLNKLKSSIGAIFGIVSLLSRLKRLVLKFFKHSKIDEMNSQEYDVFEKEEGNHKNSIYSIVSSLAIILGLVGLPYAIIRLFKNIYEKEKQIQQAKIRKKIDSLEFCKADYEFMSRDPGVEMSLKKGDIIAILSKTDTQGNPCEWWQGRKRSGETGWFPSNYCSIISR O14137 G6PD3_SCHPO ACT_SITE 237; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P11411" BINDING 43; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 121; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 144; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 144; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 174..178; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 213; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 232; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 331; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 341; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 366; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413" CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; SPAC3C7.13c; CHAIN 1..473; /note="Probable glucose-6-phosphate 1-dehydrogenase C7.13c"; /id="PRO_0000337688" MVTFMVFGASGNLANKKTFPALFHLFKRNLVDRSSFYVLGYARSKIPIGEFRESIRESVKPDTESKQVFQDFIDRVSYFSGQYDQSSSYVEFRKHLESVEKKADSSKALRIFYIALPPSVYVTVSSHIYENLYLPGKSRLVIEKPFGKNYQSAVKLKEEVHKHWKEEEIYRIDHYTAKDMVNNFFTLRFANSSSIDAVLNRHSIQSVEIHMYETGGCEGRIGYYDANGVVRDVVQNHLTQIFCIAAMNEPKSASASDVRAEKVNLLKATRPASLKESMLGQYTTSEDGKIPGYLDLEGVPKDSKATTFAASTLHVDNDRWKGVPFVFVSGKRMKKGEVYIKYYFRLKDSGIFSDVKRRRYLILHVQPEEFVNLTCTINKPMTTDLQPIDAYASLNYNEQFKDLMKEKRDGYEILFEDAIRGDPTKFIRYDEVEYAWKIWDEILDSPKKPIPYPAGSDGPEGLEAYMKRHLGHE O14144 ERV1_SCHPO BINDING 81..87; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P55789"; BINDING 91; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P55789"; BINDING 120; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P55789"; BINDING 153..165; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P55789"; BINDING 176..177; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P55789" CATALYTIC ACTIVITY: Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PROSITE-ProRule:PRU00654}; SPAC3G6.08; CHAIN 1..182; /note="Mitochondrial FAD-linked sulfhydryl oxidase erv1"; /id="PRO_0000339121" DISULFID 122..125; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"; DISULFID 153..170; /evidence="ECO:0000255|PROSITE-ProRule:PRU00654" MVFGKRYRDKETGIIYDENGRPCKTCNIFSSFRNVAQQPNSSTVPEVKSNTQLESKQSSIDCNTNAIPDSVSFPRLPDVAELGRSTWTFLHAMAANFPKNPTPTQQNDMSSFLYNFSKFYPCWSCAEDLRIWMAKYGNSPRVDSRESLCEWICEAHNDVNERLGKPLFNCQVWSKKASELAD O14160 SYVM_SCHPO BINDING 559; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9; TRANSIT 1..90; /note="Mitochondrion" SPAC4A8.08c; CHAIN 91..950; /note="Valine--tRNA ligase, mitochondrial"; /id="PRO_0000352849" MFHFQRSFSSRKAHGLLSFKNRNYIHIEAPFDIAAIQDGWNIIRKHIHYPKPKSIEAPMFPILLPPPNITGKLHIGHALTITIQDALARFYAMHGYKVSFRPGTDHAGIATQSVVEKYLQKKGVYRNQLSKDELLSSIHSWQVKYQKSIINQLKSFEAIFDWDNIFYTMDQNRSEAVNEAFISLFNAGLIYRANRFVNWCPKLESAVSDIEVESQQINKPVTKYVDNTPVEFGWLYEISYQLEGSDNEQLNVSTTRPETIFGDRAIAVSPHDERYKKYVGRFVKHPLIDDLLIPVICDNAVDRHFGTGVLKITPMHSIVDYEIAKRHNIDCVSIMDKSGNLINCSKEVNGMNRLKARSKIVRLLQQRNRLVEQVPHSLILSVCSRTGDVIEPVMVPQWYLSVDSLKKEVLKSSNKLKLVPSLARKEWDSWFKKMGDWCISRQIWWGHQIPVWKILEEDKWIAAPNYEKALQLSVGKSVSQDSDVLDTWFSSALLPLSAFGWPKSKDIQPLPFIESGQDILFFWIARMALLCKYFSNELPFKEIILHPLVRDSEGRKMSKSLGNVIDPMDIINGVTLENMKKALLEGNLPISEVHKSSKQMEKAFPNGIPAQGIDIFRYGLFLCLHHEQRILLDMNSFSDAHRFVSKLWNLARYFNQYKDKENPLKLTDSQRQRISLLKMATYSKLHHAVEGVKESFEQRKFFNAADIMKNFLLNDLSSVYVELTRFDVKDSKSSAYEVYRVFSDILHIFLKLIHPIVPCISGVMLHSKIIPERKNSEFLSFPTSQQECLLVHDNQAEVVVQNAYDVLIQLRKLESPLNKSPSREHTVYISTSLEPLKYFYDAIEQSTNLKLKSISQEDTIDLMRNQTFILSRISSDTILLVPKKLYPSKRKKLRKNLDDLQKKLDKIQHTTSSSGYEKAPSYIKLKNCELQKDILVKIQDIKQALLNTEI O14169 PGC1_SCHPO CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = a 1,2-diacyl-sn-glycerol + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:32927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57597, ChEBI:CHEBI:64716; Evidence={ECO:0000250|UniProtKB:Q08959}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32928; Evidence={ECO:0000250|UniProtKB:Q08959}; SPAC4D7.02c; CHAIN 1..311; /note="Phosphatidylglycerol phospholipase C"; /id="PRO_0000116698" MAFNYSIANTVDDAAQSIAENTSSLATFSKPPLVIAHRGYKAKYPENTILAFQQAVKAGADCVETDVRLTKDEVVCILHDRNLNRVFGVDVDVRDLDYELDNGHFRTIQEPHEPLPTYEQFLHELTKHPGVNLLVDIKPVNDLLIIPRMVDAMLRVNSDLDFWKDKVSFCLWSHRFIPACDRYAPSIPLYHIGFNFAYAERHFVMHPRVKGVSMAVALFLLPHSQDFVDLVHAQGKQVFAWTLNTPSSIYLALIRGCDGLLSDDPVMARALSQGPIVTKSWHYFHYSEWLHMIYGFLRAQFVFFLLRTFVL O14171 YE54_SCHPO CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = a di-trans,poly-cis-polyprenyl diphosphate + n diphosphate; Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:19494, ChEBI:CHEBI:33019, ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763; EC=2.5.1.87; Evidence={ECO:0000269|PubMed:25066056}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q86SQ9}; SPAC4D7.04c; CHAIN 1..264; /note="Dehydrodolichyl diphosphate synthase complex subunit SPAC4D7.04c"; /id="PRO_0000123761" MGNLSGWFIHCPPLQWTLDQLETMMINTIKRGKVPQHIAFVMDGNRRWARQRRMETIEGHSSGFEALKSLLKVCLKLGVKEVSAFTFSIENFKRSKYEVDMLMEIAKNSLTQITAHGDLVDQYGIRIRIVGDLSRLQPDVLETALKAVEITKHNTKATLNVCFPYTSRHEIATSVQSIVKMAEDGTITPEDIDEDIFEKNLLIKDSLPLDLLIRTSGVERLSDFMLWQCHKNTEIKFIDFYWPDFSIWKFFPMLIQYQLQNQPA O14176 PRP40_SCHPO MOD_RES 688; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 689; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4D7.13; CHAIN 1..695; /note="Pre-mRNA-processing protein prp40"; /id="PRO_0000234563" MSAPPWQTSEYDETEGFTSNQEGPSAAPSKTVASDWHEVKTEDSRVYYYNSVTRKSVWEKPEELMNDFEKKLSKLAWKEYATADGKKYWYNVNTRESVWDIPDEYKAALVDEPEQQKKALSSKIKSNDNKPAVQSIQRHGPDVAAPSSQPAKDQSQQISQGSHKRTINFVQQKDKRQKRSNDYQHENYDTYEAAERAFFKFLDSHNVNPSWTWEQTVRELCDAKGYYVMKDPWHRKCAFDAYILNYLTDQSDAEKNRVTKIRKEFIEMLKSSDKIHSYTLWRTVKNEFSSHPAFNATSSETEQQQLFFEYKQKLLEDEKQLEKDRRKEALDDFCSLLRNMNFEPYTRWSVAQAKFDQDPRYTRNSNMKYLSKLDALVAFEDHVKHLEREYILDKQKQKKEKHRIERKNRDAFRALLQDLRVQKKITLRTKWKELYPIIKDDPRYLNLLGQSGSTPLDLFWDTIVDLENMYREKRNLVLDCLEVLQISVDDTSNIPEIIARLSEKLKDREESEAVTEDLIEEVVNRLRDKAIHKKAEEKRADERRIRRKIDNLRSAIKYLKPPISADASYDEIRPLISILPEFAALHSEEHRMAAFDKYIRRLREKRELEKQYQNRRGYYDVGKDESYLANSARPHSGYEDGRLEYSADLASKSNRNEINTMQDVQENSISHVTATQPAVKNIVDDAESSEEGEIR O14178 RM40_SCHPO TRANSIT 1..31; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC4F8.02c; CHAIN 32..279; /note="Large ribosomal subunit protein uL24m"; /id="PRO_0000116659" MRDLRKLIPRLRGPGTNVLKMKKPLPLHMRTKIREHLNKSDPTVKDDKSAKPELPFGKPADRVPFWHIFKGDYVYVHQGPLKGKWGRVVETNKYTNGITIEGVNVRSVKVPIFLLRNKPEDNQDPVIDIAHEVHYANVRLLAHAKTDAGEPVLIPVKLKKHSSTNLRSIIRPNIEGVQIHTIHLPRPKTEDKPKDPEGKLDTKNPVVSKVTWSPSLSEPPLPPFAIGDLRANWSRRLDRIWGYKKNNDDFTEIAKDLVRAETAAEDLIKKPISPNTYSD O14179 SDO1_SCHPO SPAC4F8.03; CHAIN 1..246; /note="Ribosome maturation protein sdo1"; /id="PRO_0000123765" MVISQPVGQIRLTNVSVVKYKKGGKRFEVACYKNKVTEWRNKIETDLDEVLQIHNVFNNVSKGHVASRQDLKKAFGTDDIDKIILEILQKGDFQVGEKERHHQMSSTYRDIVSHVTAMCMDPNSKRPYPASIIEKALSDCGFSVSTSKTAKSQALEAIKKLQEKNEIPIVRARMRIRIVVDVKQGKALRERLRSLADEIEEENIDDEYECIALVIPGNYKLIDELVRNETKNRGMVQVLDMSEART O14180 YDS4_SCHPO SPAC4F8.04; STRAND 96..100; /evidence="ECO:0007829|PDB:8EUY"; STRAND 122..124; /evidence="ECO:0007829|PDB:8EUY"; STRAND 147..156; /evidence="ECO:0007829|PDB:8EUY"; STRAND 158..165; /evidence="ECO:0007829|PDB:8EUY"; STRAND 171..180; /evidence="ECO:0007829|PDB:8EUY"; STRAND 197..201; /evidence="ECO:0007829|PDB:8EUY"; STRAND 229..236; /evidence="ECO:0007829|PDB:8EUY"; STRAND 239..250; /evidence="ECO:0007829|PDB:8EUY"; STRAND 253..255; /evidence="ECO:0007829|PDB:8EUY"; STRAND 260..265; /evidence="ECO:0007829|PDB:8EUY"; STRAND 269..281; /evidence="ECO:0007829|PDB:8EUY"; STRAND 288..292; /evidence="ECO:0007829|PDB:8EUY" HELIX 7..38; /evidence="ECO:0007829|PDB:8EUY"; HELIX 40..49; /evidence="ECO:0007829|PDB:8EUY"; HELIX 72..78; /evidence="ECO:0007829|PDB:8EUY"; HELIX 84..87; /evidence="ECO:0007829|PDB:8EUY"; HELIX 106..118; /evidence="ECO:0007829|PDB:8EUY"; HELIX 133..140; /evidence="ECO:0007829|PDB:8EUY"; HELIX 182..184; /evidence="ECO:0007829|PDB:8EUY"; HELIX 206..216; /evidence="ECO:0007829|PDB:8EUY"; HELIX 225..227; /evidence="ECO:0007829|PDB:8EUY"; HELIX 297..299; /evidence="ECO:0007829|PDB:8EUY" TURN 55..58; /evidence="ECO:0007829|PDB:8EUY"; TURN 141..144; /evidence="ECO:0007829|PDB:8EUY"; TURN 166..168; /evidence="ECO:0007829|PDB:8EUY"; TURN 284..286; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..306; /note="Brix domain-containing protein C4F8.04"; /id="PRO_0000120261" MGKIKNKIVRQQQYMKALHQKNKDKLERRKERAKEEEKDPEKKRLRLSENIPATIESKRVYDETIIEDKPDEELQAELKDDEFSAYFSEERKVPKLLVTTSKRASRKCYDFASELLDCFPNAEFRKRTGDIEVHEIAEAAAKRGYTDLLVLNEDRKKTNALTLVHLPNGPSFYFTLSNLQTAKEISNHGRSTGHIPELIINNFSTRLGMTVARAFQSLFIQTPQIQGRQVVTIHCQRDFLFFRRHRYAFREKSNMPDGIGTGLQELGPRFTMRLRMVQKGVWDRKEGEVFFESNAGEESDRRKFWL O14182 RT12_SCHPO TRANSIT 1..37; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC4F8.06; CHAIN 38..162; /note="Small ribosomal subunit protein uS12m"; /id="PRO_0000309557" MIRFAQYARYPVISRLMKPTVISPFQAQAFSSSSVMLKTLNQTIRNKEKRPEKTNKQSVALEGSPFRRGVCTRVFTVKPKKPNSAVRKVARVRLSTGRSVTAYIPGIGHNAQEHAVVLLRGGRAQDCPGVQYHVVRGVYDIAGVAGRVTSRSKYGVKKPKAA O14189 PP2C5_SCHPO BINDING 121; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 121; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 122; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 344; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; SPAC10F6.17c; CHAIN 1..444; /note="Protein phosphatase 2C homolog C10F6.17c"; /id="PRO_0000352809" MNFFTSAVGSKVFKRNNFKYVAIAASSIGLAAYHIRKDAIALDIPNSTYQHVSKNRVPPTDGDGITKRLKEFERTVTVNKDGIFRYDFNQVASNDPCEDDHVEVIDRNIDEGNWYFWGIFDGHSGWNTSLFLRQHLVPAVVRELQKCTASYYHQNACPSSLALDKSISEAFAKVDHQIVHEHVSHVFNNPESLQVAASLLLPALSGSCALLTSYSAKSKSLQVACTGDSRAVLGECTPDGSWEAIPLSRDQTGMNPDEASRLEVEHPGEEVLRNNRILGRLMPSRAFGDARYKWSQEISERLHREYFSASPIPVKTPPYVTAVPEIESITVNPKKHRFLIMASDGLWDTMSSEQAVQLVGEWADTVLGKTTNEKNTTQDDKQSWSLFKKTSKVIDDNAATHLIRHSLGGSDQRISALLTLTYPISRRYRDDITVTVIFFDEKTL O14190 ALG13_SCHPO CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-D-glucosaminyl-diphospho-di-trans,poly-cis-dolichol + UDP-N-acetyl-alpha-D-glucosamine = an N,N'-diacetylchitobiosyl-diphospho-di-trans,poly-cis-dolichol + H(+) + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:19507, Rhea:RHEA-COMP:19510, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427; EC=2.4.1.141; SPAC56E4.02c; CHAIN 1..162; /note="UDP-N-acetylglucosamine transferase subunit alg13"; /id="PRO_0000215603" MNAFVTVGSTQFDDLIRAVLKPEFQHCLVKHGINQLIVQYGKGKQAFGDPKSVAGLTILGFDYAPEIESYIHDASIVISHAGAGSILQTLRSGKRLLVVPNESLMDNHQVELATKLASMNYLVTCSTSNLVEGLEELYPKILTPFPKSDCSTFQKVMQDVAR O14192 AATR1_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P00509}; SPAC56E4.03; CHAIN 1..474; /note="Aromatic amino acid aminotransferase C56E4.03"; /id="PRO_0000308489" MAAQPKDLSHHLSVESASRKQSPLKAVALSKSSRNIKIISLAGGLPNPEYFPIREMDAEIPAINSWKKDSSNSGKLDTVSVPMSSSDSDVLPLSVALQYGQGSGAALLSQFLKEHTRIIHNPPYEGWNIIMTTGNTSCLDIALRMLTNRGDSILVEKYSFPSALQSMRPLGLSCIPIDMDQFGFLPESMDDILTNWDATSYGSPKPHVLYTIPTGQNPTGSTLSVERRKQIYTLAQKHDIIILEDEPYYYLQMDAYEGKPEAADKAFTNEQFVKELIPSFLSMDVDGRVIRMDSLSKVVAPGSRVGWFTAQPLFIERGLRAAETATQSASGISQGILYAMFKHWGQDGYLEWLKHIRYSYTLRRNYLLYAMDTYLPKSVCSYIPPVAGMFIWFEVDKSRYIHADKNESIPEIESKIHAEAVEEGVNLACGNWFVVDPRVNDKIFFRVTFAHAELEEFNVAIERFAGVLKNNFKC O14193 MUG69_SCHPO SPAC56E4.05; CHAIN 1..192; /note="SRP-independent targeting protein 2 homolog"; /id="PRO_0000278503" MANAAQKKLAAQNKHILTFMLAADLIVNVLFWILRFFVRSGLSKFSKFVYAFASISSGFLHYQLHRAAAPKYDARGSLLYVGQDLLQEGVTSYMVDYMYFSWILIFLAALTSVKVFAFYLLVPIFVVYKAAPLLKMLLQQLKNFKNQALNQPPQQQQQQQQQQHQQHATPSEPVLSKRQQKLRKKAAKYSRP O14196 MU165_SCHPO SPAC5D6.02c; CHAIN 1..300; /note="Meiotically up-regulated gene 165 protein"; /id="PRO_0000116653" MLEKGEHIEYPNTPPLHSPPESHTFSSQTDDSYFHKPSSTGLFATLVADTNSSVPSASRSPESIASSQSNDSAAIPSYRRKRRKVRKPEIVKPTLRKRGRKPKNISTLEHDKSKPVISSLIDEDANLSQIKARKSVLESRFSRLEEAFRDFYIKNLEKTEDLIRTDSHFVLNKELLSFRNDYEHRRKHYEKYSQCLNKQLDHFFSYKVTTVHKSYQRFATLLRRHLLDKTAKRYHDLCEKRPYKYITTDLLSPSLTCFASDILQTVPEYTSSQSSPVLLPATPSIVTNKQMMDDLTLCNV O14201 MUG86_SCHPO SPAC5D6.09c; CHAIN 1..304; /note="Meiotically up-regulated gene 86 protein"; /id="PRO_0000278568" MSSNPSRSNSRSKNGDLESGLKFVDNDHDSKDIEARNRNHFYGFRAEPIYDQTERLANQVAELQEQQKRLFGPSGADFEPNIHRLRYINYGNPAPFGLSAFAFTTFLLSLFNVNAGHVKVSNMVTAPAAFYGGLAQLLASMWEMASGNTFGGAVFGSYGCFWLSYASIFIPWFNIQNSYDDPNDFNYAIGLYLICWFIFTFLVLLCTVRSTLAFFSLFMSLDVCFLLLACAFLRTSDGSPNVVLIRVGGAFGIFSACAAWYNAMAGLATIENSFFTVPRAIFPWSLEGLGPEEANRRRMMADDK O14207 MMS22_SCHPO SPAC6B12.02c; CHAIN 1..1888; /note="Protein mms22"; /id="PRO_0000116662" MNSFLLLDHVSDSQDSGSEWSNTHGSLISQRGNEYDGITPATKEKNQNKLEILNNETTIGSTKSSVSSLPELNRNVSFEKSDQNLAETKREEENKRTEVFKKDAEHEAVVVKRDFRPRRPEQTRPYTYDFLRHQIEFKRIGLVPITVPHGFSSDRSITSKSSHKPVNVIVRNRASSRKPPLTSTHRFRRYGAVISDSDDDESNTEQDHSKESNLNTADNDLALSSTIEGKKTSTSKEALESESLLSDSDQSMTNISSNSTVSDLNLKTLKKRLRGVLPPSFLTLQEKKKLENRGVKKKTSLHKSVIEGEKIKGVARRKLHPRSTAKLSSELGNEISDSDNSISTPTPTDDSRFDTSEFLDSISRDNGWLKEDVVDQLWLPKRSLSALKKSSSLTSENPFQLNVAANAVSTIPVYRTTKTKMKKNRFKYVEVEKLPDLILESYGKKAPKFLRVFARSSSHIPKMIRRKRQMDSKKYFSFDKESDRQVIDQVLSDWYSGKHELVQQSHSYKKPSDSKSVGGNIFSVNSKKHSVNINAKTAANNGLSHLQNFSEELLKKRKLFSSLFSNNVSYKKSKKLKRTHTVHDKCQKVAKLDHYIRDNIELNSKEREHDCYEGTLAVPQVNTEIRKSSRKQKAQRFIRDDFDTVFFQSSSNPNYFTDVNPFWNIGIWSTTFNVITFRPGLSLPNNSFIKTQGLNSILQLDIVTHPFKSVYAFSCLFNIQDDVFKTFEKLKDTFETVLENLPYFTNSETVDLYNLLSFCSAFILHSQVSMGLVNLASSFLETYALVNDRVSSISGLNRSQLVEKIAVLFQTFQVVFYCEFELGNQQNINKVSWLASDLISKLLSAGQSGLLECYRNLRIQASDTTVIDTLFLESWSILNHILFHVYKKKYALWEQVNSFFDLQKKELSILEMEKIWYVIMTLNPVFQIGLNGTTHSPGNNSFWPLIIRVSESAFKMHKDGHNVKVVERYLRTVFLRIHFLISEWRWEDVAQILFLIFDFFSHRKFNDLSSEISEDTPTDFPDFVKSLDRPPNLHVTALDTCFVIYLKVILISISRLRQVDENTNSIKRIVSRLQPLHSRQYTRESPFSIKDFMSLEHTHTLLICLYWAAPENCRPSLNRIRDIVIVDNSHLKARLISLKAWLHLMKYVIKEGTDYELAQGMEWFNSILKVTFDEYLALFSNGTSVGEMQLAEYSKHQLENALIVAFHSLQDLIPNSSVYISRINVLVTEQSCRRILKDSHFFPPRVTLECILFLKKFLQYQSNTEPPKVTVVGSTSHDSQDAYFDSDVLDDNTLILEQEKFERKYEVAQILRTFVSPFLYQTISYLVGNDEDKENYIRILLLPLMECMAICASFAVEAKINDWSYYIDFGSESWERIRNTPLKRSLSTTFYSFLISYNDSFIKKHEEKVLTVWFESLGALDEDHAAQFTILLLQKNLKNPILLNLPISVKIEEISINYFKSVHLNLLTAVFCNMAKLYADAKTNGFASSQYLQSLFIHYLSSLLSSMQHSYETNGHSSDTHSLFVINSQRVVGDILQYCSQFANDRNLPALRYFMDSTKFPQPPERLEYTALRLRSYARKTLTNSASQNALFSFLKANFDVALLEQKQTETSNLLRLAMGFHNQNSSSKWDVEISSLRKFCVKELLLSYLGEGSLAAMFYSLLLLEGLSRTYNSFRRIYLQPYIQQLLCEEISVFVADLEKYALLYENKRPLLSGRIYYLISSFVAISMTNKTSGLPSSLICNLQNFLARIARDFLLELCWNIEGSEFPPPYNTVDCRSKFVKTIQQHCSADWYDNVTNIVHKSRKKKLVLPSQVEQEEEYWSGLMEVTIQIWKHDKGFLEPELDRFLNVICSYAPDMSGLPTKIKCFLDKIGYSWMTEENDFDIVLF O14212 YDT7_SCHPO SPAC6B12.07c; CHAIN 1..470; /note="Uncharacterized RING finger protein C6B12.07c"; /id="PRO_0000303898" MKFGHDFKRALENDMPPGWGEAAIQYKALKKCIKRFVFELSSLGLSAETISKLMAPTTVDPQQAITLSYSLGKEGHIVVPKIIINVNFDKLKTDKFAASMFKQLNASNMITTVRSNYASNVPSTPSDSTQQPPTNTLPSVSASSQSVETCETVDEDIDTQTMSSDMSEVQSMEISLNCDHEFFEKLTSELQSVEGLQREQRKILFNAIDILSHEISLIASPNSKKKYKSLYCWRKIFEIYMDSDIFISCKEADQSHERTPELAERHLKWFDDQVRLAKCLPSSSKHRDRILYAKFLELNESLLKVASFQQMNKLAVTKIMKKFDKRTSLTAQPLFFQVIESDPLLLVDNASKAICFSLSSKLFSIIPQLRDFECAICSNVAYKPVRLGCSHVFCLHCLIILQKQKVDFCPLCRAKEVMKADSRNIDHALMNFMKTYFPREIKEKFEENENDTFTPSSISVVSGQNNCVIM O14224 GDIR_SCHPO MOD_RES 63; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6F12.06; CHAIN 1..205; /note="Rho GDP-dissociation inhibitor"; /id="PRO_0000318108" MSVNNEVSADQHNPELEDDTFEHGPPVSLGEKKSLNEYMKMDAEDESLQKWKASLGITGTGYSPSNDRRTVVILKLSLLVDGRDPVDVNMEDAASVEQIRKKGFTIKEGSEFKIGVKFRVQHEVISGLRYVQTVRRRGFVVDKTSTMIGSYGPSETPYDFTSEPDEAPTGMLARGHYEANGKFVDDDKVVHHEFVWAFDVAKSWK O14225 TOM20_SCHPO SPAC6F12.07; CHAIN 1..152; /note="Mitochondrial import receptor subunit tom20"; /id="PRO_0000051549" MRRSVIIGSLLATAAVGYAIYFDYKRRNDPHFRKTLKRRYKKVHEAKKQEEKLATKKFDITVEEALQVVASTPVPSSAEEKELFFMQQVARGEQLFQQQPDNIKESAACFYSALKVYPQPVELFAIYERTVPEPIMNLLRAMQAKESIPSVE O14226 EXO84_SCHPO SPAC6F12.08c; CHAIN 1..584; /note="Exocyst complex component exo84"; /id="PRO_0000118985" MPDNPSSFEDEFMKSNHLSVASESIPNESQRQSPTRLRVGTSKTDDIYRQKRQTKHIISQNEVFLQPKFFDNQNFDAQSYLNDVLQDLSEDEFVSLYNKLLRIHMGVRKNLEKNFYKNLNEYVFISGEVESMTSDFKKFQSLLKTLETDIEGLNLVDHTHDPSDESIKQTVQRLRSSIEGLDEAFWEAPQRQLICEQYNWMLINIDNQRPKLLVNMLLFNDRLLVTTSHMKEVDFPAKQQVLYNWNLTEISISSIETYGPAGAEMLQKEKEVSLYKLSINHNNKTTLLAVHNSEERDYMVRQARHHQLQELENWSRKHDEDLEFSRELEYHTKSEQADMCSYTSFQVLCKNLDTQDILQAYAKQRNMVKEISMQFDHLDIQISLQEFTDAIRNLALIQNKLERGNLNELFAEFFADKLHNRKRKVTEILLHQLGFKGISLSHGKEIVRYLRSLGHEKEGQGVFMKSRTLLIKEKCLNVQLEKDTPNFIDACAFIVFRCLAQTTSSYLQLFELKKLDPAYRNWIFQQIEALVDLIENQYKHLAHDRSYTDAVSKIMTYNTELKEAKIDAMPILQRLFDVHSKDLK O14233 RNA14_SCHPO SPAC6F12.17; CHAIN 1..733; /note="mRNA 3'-end-processing protein rna14"; /id="PRO_0000238528" MNSDDNVEADASSNIIKDSPKIKEQENTSTVNESDVLATSTTASSGVKRKRLPNDLVGQLRDKIQENPNDISSWYALVEEYGSKGKHEELRETYEQMLRPFPYVPRVWVDYISSELAFNDFHAVELLFSRCLVKVLSVDLWTLYLSYIRRINPDGEGQSRSTITQAYEFVINTIGVDILSGPIWSEFVDFLRSGPANSTWEQQQKLDHVRRIYQRAITTPIHNIEKLWRDYDAFENSVNRATARKFVAEKSPVYMAARAAMRELSNLTEGLRVYDFTFERKYTKVERIAYSRWMNWIKWEQSDPLDLQHGTMLQNRIAYAFEQAMLYVPLCPQIWLDGFSYFLSISDEQRALQTIRRGMRYCPSNFVLHVRYAEHEEANNRTSEIRSTYESLIAALAREISQLDSKASSSSESSTDGNPQEKKLPEHLVKRKSRLVRQYSLAWCCLINAIRRTEGVKAARAIFTKARKAPYQSHEIYIASAMMEHHCSRDPVIASRIFELGMRHFGDVPAYVYKYLSYLIAINDETNARALFEKAIPRIAADEAKPIYQKWLDYESNYGDLNAAIALSQRMAVVYPQESTQAIFLSRYGLKDDAEEEERETKEAEKIRELSVRLNGGNGFPGHVHNNREDDEVSIASTSSKSNVEMEDTRLLPASLELANTQGASNPPTSALPTVPVPLPSIITEFLDELPAPQVITGPRIQPTKLIDHIIKSDIPFIRLRNANAHLKRARFN O14234 CCH1_SCHPO SPAC6F6.01; CHAIN 1..1854; /note="Calcium-channel protein cch1"; /id="PRO_0000311769" MSSSSNSDPSSSPDNTDFIPLKDNPKDTSSYINKKNPFVNDSFDSHDDSYLDNVNPFEYNVADDEDTISMTSDGVEFHNLGITETVDEQDKILSELQLAYPTVSRYSETLDKGLLNGDKTTKGDYTSLRRFRKPFLFDKLSPYFTHFFSEIYAAVLRVVGPPRANETPGRNLPFSPILRQIYNHPLYNIFIFVVIVLHAVLLMIRSDDPHDKSQTIDYLIIVIGILYTLEMLLKIYLFGFLYDGSSSFYDFINSYTKKTPRTMSYLRHSWNRVDFVAIVALWISVIGKKQQGIFRLFSMIACLRLTRLLNITRKTETILKSLKESSTPLVQVVSFNAFFGVMIAILGVQFFKASLNRQCVWLGDYGDQYLPTGQFCGGHWENGIKRAYLDKNGFPSNVNPRGFICAEKSVCRVVENPYSNTVSFDNFFNSLELIFVIMSSNGFTDIMYDIMDAEYFVSCLLFIISAYFLTLWLMSLVIAVVTSSFIDLQHSGKNQKEQKSVDKHLIRNKLCEKYLFYSNFIWISFIVAQFVTLCTQTYDQTSSTANRYLIFYACVDFLLAAEVILRFFAYLPDYRLFFRRYTNLVDIVLAVLNLVTLLPSIRKNPVAFGWLSIFAIARIYRCILLIPYTRKIAKLLFSNFKQLLNLMLFLVIVLFIASLCAVRLFQDLPNDGDSDDDAISFATTYESFLYMYQILTSENWTDVMFAIQARLAHLHLSWIPGAFFTLWFLFSNNVVLSMFIAVIQVNFAPSESDLKMEQLKMYLARLLRNYNPFQASLTLNALIKRNGSRKGKTVDESHYEWLYEDNIIKGFLRVTNIPPKEPLKPSLDTSPELSKYSLAKLSNNFKRFVMRDDPFSQAYFKRVIGIRWEKDMNLKTAAKDMQAAKAFVRIKQTEFLKNHPKYNDVFWVIKPSNRIRRFCQRLVMPGVNERYGGVEPYQWVYRVIQVFIYACILTAVIIECIATPIYERDHLLNDKQHAWFVWTEVAFATIFTIEAAIKIIADGFCITPNAYLRSTWNCIDFFVLVTLWINLYAVLTSHALLSRAFRAFKALRVLRLINLTQTSQRMFHDALISGFFKIFSAAVVSATLLIPFALWAKNVFGGLLYSCNDDNVLSASQCVLEYASTPNNWEVWAPRVWSNPPDYDFDRFPHALLALFEIASIEGWVDIMRSVMDITGFNNQPQTNASSGNAMFFVLFNLVSMIYILTLFIAIIISNYAERTGSAFFTAEQRAWLELRRKIKSMRPSKRPAIRPLGLRGLCYDFAVQKHGIWRRTFTGLYIVHLLFLLTIFYPCPIAYTYVRNSIFLILSICYTINICVKVYGLSFYYFFHSFWNMFDVVVTLGSLTCNIAILAKFENRSLTLLQTTLLVLVTVHLIPKFDNFDQLSKTVVASLPSIFSLIATWIVLYITFAIAFNQIFGLTKLGLNGGPNKNFRSIRNALVLLFTMTFGEGWNDVMHDYTISYPNCVNGDDFYNSDCGNKPWAYGLFIAWNIISMYIFVNMFITVVFDNFSYIHTKSSSFTNLQRNDFRQFKDSWAPFDPMVTGYIPKRNAVKFVLSLRGVYDFRIYRDEHTLRSIISKVQSKTGQQSVPMLENPLMGSEINLEALDQIIDTIDVNVVKERRNVLNSLCTEIMTLPGNVISFSNILMLVVLHKIVDHREAFPISDYIRRAYVLSELEKSIRMEKLLGLVETSIIRKTFLQHMEEKKKALENPFILLSEVSEILPETPIQEVLRQHNADPEQLLMSTRTPSVSDRSFSIVESTVPTIASGEGDDNHSVEDHLKVPTDNEPRRSPSLKEVLLRGSHSLHSNNDRTSFDIEAGFGTAESDFQFGGATEDINRIADRIDDYLDRDSFKG O14236 NOG2_SCHPO BINDING 317..324; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 361..365; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" MOD_RES 186; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 484; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 487; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6F6.03c; CHAIN 1..537; /note="Nucleolar GTP-binding protein 2"; /id="PRO_0000215815" MGTYKKEKSRIGREGANEKKPGNLRVKGENFYRNAKDVARVNMYRGGKAKYNAAGELVRAAEFQSSEVPKARIQPDRRWFNNTRVIAQPTLTQFREAMGQKLNDPYQVLLRRNKLPMSLLQENTEIPKVRVLESEPFENTFGPKSQRKRPKISFDSVAELAKESDEKQNAYEEKIEERILANPDESDDVMLAARDAIFSKGQSKRIWNELYKVIDSSDVLIQVLDARDPVGTRCGTVERYLRNEASHKHMILVLNKVDLVPTSVAAAWVKILAKEYPTIAFHASINNSFGKGSLIQILRQFASLHSDKKQISVGLIGFPNAGKSSIINTLRKKKVCNVAPIPGETKVWQYVALMKRIFLIDCPGIVPPSSNDSDAELLLKGVVRVENVSNPEAYIPTVLSRCKVKHLERTYEISGWNDSTEFLAKLAKKGGRLLKGGEPDEASVAKMVLNDFMRGKIPWFIGPKGLSSSNDEINSSQKVATQQTEGSDQDGEEAEEEWHGISDDGKADESESTKPVAEGSASESTDESAVDDNKNRS O14238 OST2_SCHPO SPAC6F6.05; CHAIN 1..122; /note="Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2"; /id="PRO_0000124031" MSSKSGLFLPLSSVITSYNENTNLSLKTIDAFLGFLVVVGGLQFGYALLVGTYPFNSFLSGFISCVGQFVITVGFRMALTQQELQSSSSKKKSPVVSPYKRAFLEFCFSSLVLHFFAVNFLG O14240 EAF6_SCHPO SPAC6F6.09; CHAIN 1..138; /note="Chromatin modification-related protein eaf6"; /id="PRO_0000086899" MSTPNSTPSEPPVNVSYYEQCKKELHEMIEKRQLLETSLIGLEDSIYRLEGSYLEKTSGTGNIIRGFEGLLKNNASNLRRRADYSESDRLFSLSSLSSPHTRSPAYDLDDSTETSRRRKRKNESDSHEGRRRSSFREL O14242 YELB_SCHPO BINDING 12; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 123; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 182..183; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 209..221; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 222; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; SPAC6F6.11c; CHAIN 1..309; /note="Putative pyridoxal kinase C6F6.11c"; /id="PRO_0000339162" MNTTKRILAIQSSVCHGYVGNRAATFPLQLLGWDVDAIPTVELSNHAGYPIVKGRTLSAEQILDLYKGVSAANPSGYECLLTGYARGIGSVKAIMEIVRSVKSKNKKAFWVFDPVLGDNGRLYVEESIIPLYREMLPFADLITPNGFEAEILSGMRINSIDTAFKCVECLQQKYKVPRVVISSFVVEENGVEKLYCIGSSIYSKSFFVLIPVIPGIFRGTGDLFTALMAAHIAESPDCTESLASIKEDKLKKSVEMALSSVHEVIQKTADRISALGVEEYHPAYAELCIVNSQNSIIAPSKLFEAVYYY O14251 TR120_SCHPO SPAC6G10.05c; CHAIN 1..1210; /note="Transport protein particle subunit trs120"; /id="PRO_0000374006" MEFDFFSFVAPSRVQSLVLPFGRVRRKSFSSYLQLLRRVSHIQLSDVPVATATRKSSSFNPLAFPLGRLVYNFLTSLDDQQALLEEFEYFRRVFVLIGIVDGSEEQEVEQLCSTLDVWRRRIPHALVAKCIVFNCPEDKENIFNAPNIIIGPRSDFSINSVMRSILCDITAELLEGFSSLEFSIHARSVILSPITDMPHLAPLQRKNSNASIHSLGSSSRPTLTRTPSITSRSVNSVTERSKSLSKGRIENQFGQLYLLAGRVPNALKHFSTAIALSKATGDFLWQGLSLELFTVCLVIMAHLHVDVQIPPNILSMFPSYNDRLNAFGPLKFDALLNFITEMRNVVDQLYQKSTLQPNDAVPGLCFSESILRYAHLLTVVYSCKGFNDNALDHIIAQAPIRPVKKATTYVPNKATICQWIMRAQGQHLNSLSIRERCRIYGAMANMLGSIGFSRLRVKMLRELVASLTPVLLETRRQNASKNGIHPEVIASHTAQSFKSTHYCNILPLISEICQEYGLLKTDGSLLNPELTKWGWSNLQFDVLNELISLCDSLSDYRSILLLISLFFLTSVQTASSSQQISMFKAFRKTYLFASNAGIHINAPYWDPFMITDLKFIGSSENAELIHQRLRNGLPKSIEKGPFIYNPFNRRQDQNQSKSVLVVDEQVAFSIYFRNPLSVSVEVQDVHLETKGVSAKCSHSTFTMRPLSIERTTLTVTPTETGELHIVGCRVKVFGCEPILQYVYEAKDKHKSLHVYLEKSKDVNAELRSLDTIDHLWTYFPFKKDLKTKSFDCIVIASQPKLSLAFQNLTSGKFNFAEYETGELVYVIENTSFVEASHISVLFEDSSSKAFEQAIADKSITADRLYELQFEEFNLPTFTVESSQPFSLSPGERREIHIKIRAKPNSQEGLILFESSVHKPEDTEFYVRRLRIPVSLNISKRVDLKQWSAFMDTEGDPSYCLVLLNFYNHFSEPLFVTVKTASTDESRSVLIKPKADNVILFRLKRFIMSSEEINLDIPNLSTKQFVLSSGFKKSIEDSYTMKKRFWIKEYFLKEVQASWKTDDNLHHGEIYLRNHILSDEMANNLSILPIRIQAWVSYDSEKVTTVCPREPFKLVLEFFGHADTNMRYKISWTQLNTQANTSSFNGLILDGPEEDIVCFNNSKCHVVIERNMFAYTTGMYNIFVRIFNEELQLLSQPVDLDEPILLIVDAK O14252 YE66_SCHPO SPAC6G10.06; CHAIN 1..376; /note="Putative oxidoreductase C6G10.06"; /id="PRO_0000353796" MSATSREGNKTKIGIVGGGIIGICTAFYLTEEQEYKKGELDIFIFESKEIAGGSSGIDSAILTKLCQNEIIQPLSTLALKLYEGLDKKFDGKKNWEYRTANSWFCKMKWDNTNVAKVPDTLQWLQRERMQKCSSIGSGNDFAMINPKLFCQFMAKEIEKRGVKFIFGSVKEVSKHHITYVPKQEAEDTIIKAQVHKTLVSAGPWTGYLLPFTGIAGLCIPIIHLSVGNFPVGDSIVVCCLNTMGNLNICKTTEIFSKNREQLIFMGTPKFHLLPKDSNRCFFNPFEIIELKEMTDLVLSENTKSNYLDASFKFLPTSRITGIPIISTTKSGVFVAAGHANWGITQAPATGLCMAEMLLGKEKTSINTDPFHLNLGE O14254 IDHP_SCHPO BINDING 106..108; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 108; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 113; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 125..131; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 140; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 163; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 283; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250"; BINDING 291; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 306; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /evidence="ECO:0000250"; BINDING 341..346; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 359; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; TRANSIT 1..26; /note="Mitochondrion" SPAC6G10.08; CHAIN 27..439; /note="Probable isocitrate dehydrogenase [NADP], mitochondrial"; /id="PRO_0000014425" MLEVRAAVKAPFKLAAAGRGFMNMRMASSKSFQKITVKNPVVEMDGDEMTRVIWKIIREKLVLPYMDIKLDYYDLGIEARDKTNDQITVDAAKAILKNDVGIKCATITPDEARVKEYNLKKMWKSPNGTIRNILNGTVFREPILIKNIPKYIPGWTNPICIGRHAFGDQYKSTDLVASGPGKLELSFTPKGNPSAKETYNVYEFNGSGVAMSMYNTDDSIRGFAHSSFQMALQKKMPLYLSTKNTILKKYDGRFKDTFQEVYESDYKQKFEELGLWYQHRLIDDMVAQAIKSNGGFVWACKNYDGDVMSDVVAQAYGSLGLMTSVLIHPNGRTFESEAAHGTVQRHYMQYLKGKKTSTNSIASIFAWTRGLAHRGRLDGNERLVKFANALEHACVRCVEKGIMTKDLYLLSKSPNGYVDTFEFLDAVKSELDSELVNIA O14258 ACE2_SCHPO SPAC6G10.12c; CHAIN 1..533; /note="Metallothionein expression activator"; /id="PRO_0000046799" MSLSYLSSSSQKSFESFRQEESPACNHSYQRDYETFGDSKHTSFSSFAPFENEVSLNQAVIPSPPSHLQNFQDQFDYSSVLKTPFNPLLEANSAYFLSNQISLPDSHSYASSFDASLSPPSSPLTCVSQIHTEQNFNNNDAFSLTNSQQAFSEIGYDASNWIDELDSQQQVLSFPEFDIPEIKTETCSNKDHLENFDYLSSSIPETSGPASSVLPSSSQLESFNEFMFLPSSPPGLDEINGAPSFEELNFQISQPSPAHPVDLSSPETAPNISPVSPFAQLVKLEPTSPQKPSFALDSSFSHLDVCRHTDNQKAFAKLSSPAEYVSEFEKFSSVCDHGLDISNANINNTLTQQFALSAPYESCIVTKKPEPCITVKEEEQLAPKIESADLSITPQVTEHDSKPPVRISYDHRCKTRKQSTRICRIPPETMASLYCGPEADGKYVCLYNGCNKRIARKYNVESHIQTHLSDRPYRCDLCKAGFVRHHDLKRHLRIHENGRPYVCECLKRFNRLDALNRHKQRNICVGGVDRRQH O14265 VATH_SCHPO SPAC7D4.10; CHAIN 1..450; /note="V-type proton ATPase subunit H"; /id="PRO_0000124201" MSNSDLELSNAASPPPVELDNSQVDEIINNVRCVAIPWQGYQRSGSLEENELQEIENLTGKPLSAYVKTAEEDTTAYSNLFLKLLSMKDTPDVVNFALVKLADTLLNSNKFLSAFGPAFYDFLEKDESYINYLDDDSKLLFARVFALCSSSSPCSVAKAFTLFLEYLGKLMQSLNPLTRLFAVQCLNGVLTLKAHRYALWAENTCSFRLAELLRNSIGDTQLQYYSLFCFWQLTFESHIAQDINKRFDLIKLLVQIIRSDTKTKVYRLVLAILVNLIDKAPKDTISTMLLEHVDKAVQLLQKRKWADEDITNYLDFITSTLDESSKHLSTFDMYKSELDTGILHWSPSHRSEDFWHQNAKRLNEDNYALLKKLFHIVQYNEDNTSLAVACHDLGAYIRSYPEGRSLIIKYGAKQRIMDLMSHPDPEVRFEALSTVQLLMTEVCFLSKITL O14269 YFPE_SCHPO MOD_RES 74; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC7D4.14c; HELIX 7..24; /evidence="ECO:0007829|PDB:7QUU"; HELIX 34..43; /evidence="ECO:0007829|PDB:7QUU" CHAIN 1..551; /note="Uncharacterized protein C7D4.14c"; /id="PRO_0000304073" MDAVEPSVEKEYKKIISFRDTVFEGKHQQFLVPNNVRLKFLRDRLHKSLKNFDSVKRKVEIANDEGNNKLLKSSPKAQTRDENTPSEFKNGGFSNRESMSENCFSKSSTNLPRLDINRDFNSLLNSQTKPEATGLMKEDITPVVNTSKQSSTGTQEESSKPEKSNKLLAKSTLSLYGNQAFNPSSVLPSNSSSTPKENKKNVNKETYQPNTFRRSPLKNDTGSVELSNLYMPSPPSSALPVSLVSAPSPPRATNVAVPCLKHLESSEQGNNLLINKAFTSPRLPSPPQSTRPSSTRFPSVPLSDEKNSIVSVKNEEPSVILGNQSPISDLHPYSPSWIPYPKELQSLQVNRIPELSLENNVMSTRDYKDIMPHPRPSAVLLDKPVSLDQTSHPFPHQNTYILPPGIRNSVDYDGTFLSRKSLPPYNGIHRLHESPSQFSNQSRYNWEPILENRSLLHLNRPPPIETHYSYESNNSSFSPYYHKRHRQISPYYPTSSVYGVYESPPHMSDSRISRQHMPLTHTTYEPSAPYYNDYELAEEIERRRHHSFYDY O14273 YET4_SCHPO MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 168; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 197; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 200; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 396; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 489; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 491; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 515; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 519; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 523; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC8C9.04; CHAIN 1..647; /note="Meiotically up-regulated protein C8C9.04"; /id="PRO_0000304022" MTTNPDIVKQTKNEIHQVTSRVQEKLDSKSTNAVEQNNNSSQASVTKDNKKKAAKRAKKKAAKKKKQSAAASASSTPVEEAQHAQEEQQEQTILQEPGFTQTIVEKDADQVDEPLEPIASSALGTVEPPTDNKPSASTSTAVPTTEARNTSITEPANSPSSSSSSASTKSTATTQSADYVVAEHFAPQRNDEQLGNSPASITSKPATTSAAQPSSKVEENMAKATSQPITTAEKEIPELKPIEPEAIMISKEINTTHDQAAATTTAAVASASTTATAESHAVADGIMNDNVLESIGENVQQETVFEDASDIPHADVIPHTTTVTVEEESPIALGQGGVTHEATTSARASASGIPGAFEEVQQTVQEDLPHPTAETVEIARFAEQPVRAQQPEQYESSVVQEATETVTDVGKGVSSTVKNEVNVPSTIPTESENPVAVGGTTAEHPVQEAVTAPTETAHDFSKETTTASKRVSKHDKASAEKHKVARKPSSTGQEPTTPSTPAKSAQSSKHARRPSKQASAPSSPGTTSAAVPGGKKSAIEAAAPIPTSADTVESKHAAGSGSATTIPSPGSATTKPTPGSATTKPTPVSATEEHAAGTTKPAPAAGATATAENETADGKAQTATDGEAAPKKSWFKRMKKSFGKLFH O14274 DTD_SCHPO CATALYTIC ACTIVITY: Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala); Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96; Evidence={ECO:0000250|UniProtKB:Q8IIS0}; CATALYTIC ACTIVITY: Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871, ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96; Evidence={ECO:0000250|UniProtKB:Q8IIS0}; SPAC8C9.05; CHAIN 1..149; /note="D-aminoacyl-tRNA deacylase"; /id="PRO_0000164632" MKAVIQRVLNASVSVDDKIVSAIQQGYCILLGVGSDDTPEDVTKLSNKILKLKLFDNAEQPWKSTIADIQGEILCVSQFTLHARVNKGAKPDFHRSMKGPEAIELYEQVVKTLGESLGSDKIKKGVFGAMMNVQLVNNGPVTILYDTKE O14277 RS5A_SCHPO SPAC8C9.08; CHAIN 1..203; /note="Small ribosomal subunit protein uS7A"; /id="PRO_0000124538" MATSSLTPGVSLDENGSIKLFNKFPFEGVEVKDISLVDYITIGNGQPLPHTAGRFQTKRFRKARCFIVERLTNSLMMNGRNNGKKLLATRIVKHAFEIIALLTDQNPLQVLVDAVAACGPREDSTRIGSAGTVRRQAVDVSPLRRVNQALALITIGAREAAFRNVKSISECLAEEIINAAKGSSNSYAIKKKDELERVAKSNR O14279 RR14N_SCHPO MOD_RES 80; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 83; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC8C9.10c; CHAIN 1..154; /note="Ribosomal RNA-processing protein 14-N"; /id="PRO_0000373875" MTEVEERINAWNDGFEELLSYIPAKLYYREHTANQWKQKKSTLEEKKERRKMKFSLDGLVNDADDDSQKSSKWEQSSTMSDDTDVSDRHAESMSQIRGKLASKIQDLREKRKAGDLNQKRQNKRPVENEKDSQKGSGKSKVQKKKHKASPRAGF O14280 YETB_SCHPO SPAC8C9.11; CHAIN 1..84; /note="Uncharacterized bolA-like protein C8C9.11"; /id="PRO_0000316212" MVNAQQLELLIQNTLEPTHIEIQDMSGGCGQNFEVIIVSPLFEGKSTLARHRLVNHKLQEVIKDIHAFTQKCYSPAQWEALQAK O14284 OXR1_SCHPO SPAC8C9.16c; CHAIN 1..188; /note="Oxidation resistance protein 1"; /id="PRO_0000058121" MFNFTRQYSVKDGLITDELASHIVENLPARYASAETWKRIYSLQHDGASLQTMYLACEKEKARSGHPKGACILAVRDTDGDVFGVFIPDYLIPAPHYFGSEETFLWKYFPPKKYVHYPFVGNSNFVAYCTKSFLAFGGGNGRYSLWLDGSLEYAYSSRTPAFENNPLSYRGCPDQRIQIVDIELWVLE O14293 YF19_SCHPO ACT_SITE 270; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008"; ACT_SITE 304; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008" BINDING 247..252; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" MOD_RES 248; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 501; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9E9.09c; CHAIN 1..503; /note="Putative aldehyde dehydrogenase-like protein C9E9.09c"; /id="PRO_0000056595" MSTKLVDHVEITVPTGKTYIQPVGLFINNQHVDSVHGGRVKVYSPSTEKLICEVADADEEDVDIAVKVARAAFQTDAPWRKFSSAQRGRCLSRLADCIEQNLEYLASIETLDNGKSITLARGDVQAAADCFRYYGGWADKDYGQTIETDIKRFAYTRHEPIGVCGQIIPWNFPFLMCAWKIAPAVACGNTIILKTAELTPLSALCLTKFVPECGFPPGVINVLSGDGRRCGNAISSHMDIDKVAFTGSTGVGRMVMRAAASSNLKKVTLELGGKSPNIVFNDADLDSAAVWTNYGIFYNSGQVCCAGSRVYVQEDVYDEFIKRMVAKAKTLKVGDPFAEDTFQGAQVSKQQYERIVSYIESGIAHGAKLEIGGKRHGNLGYFVEPTILSNVTEDMAVGKEEIFGPVLAVIKFKTIEEAIRRGNNSTYGLAAGVHTNNITNAIKVSNALEAGTVWVNCYNLLHHQIPFGGYKESGIGRELGSYGLTNYTQTKAVHINLGMDSPI O14296 VPS24_SCHPO SPAC9E9.14; CHAIN 1..231; /note="Vacuolar protein sorting-associated protein 24"; /id="PRO_0000362997" MQTVRSYFFGPTPQEQNRKWQSIIRKEQRQLDRQVYHLKAGRKKAEVQLKQLAKQSDITNMRILAKEIARANRHGKRLAESKALLGSLSLQLNDQMAMLKIQGTMQSSTKIMQDVSSLIRLPQLSETMRNLSMELTKAGVLEEMRDEMFLPVEDDEELMDLADEDEEVQEILTKYNVIPAPSEKAADAATHREQSLKQALPSLSNGIAKDSTEIDEEQLLDIRDKLDALKS O14300 OXA11_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC9G1.04; CHAIN ?..374; /note="Mitochondrial inner membrane protein oxa1-1"; /id="PRO_0000020358" MLHFLIRPSTRCAGSPHFNSTSSFLRKRLQSKTILSKRLGFQFRPSSTNVLAEVSTATSGFNPSWWPYALIQNTAYTINVYAGAPWWVSIILTTLGVRLALTPVMIASFRNSTKLSVIQPEMKKELEAIKTAKLDNDQLALNQHSIALRGIYLKHNVNPFAIFILPLTQSAVFFSFFYAIRKMSRLSVDGFTTGGLAWFKDLSIPDPYCILPIINAGLMFSGMQMNRANTASTIGNSTNWRTFFFLCCLLSPLLTAKLPAAIFMYWIPSSLFNIVQGYILKNPVVRSKLGFAPLPSIIEKQPSGFTLITNPIKSLKEFYKGVRDGFKTQYEQLQKDVSRRAVATTSASTIRPNSHYKKLKELNRSKKNSKKQSN O14301 YE85_SCHPO SPAC9G1.05; CHAIN 1..595; /note="Uncharacterized WD repeat-containing protein C9G1.05"; /id="PRO_0000051495" MSSQLKSTWAPVPSTKPSQPCKIGTDFKGERIVYPANKAIIIREIEKQENCFQYNEHTAPTTVARFSPSGYYVASGDNQGNVRIWDCAGEDKILKNQVTAISGRITDLDWDGDSQRIIAVGEGKERYGHAFTADSGNSVGEIFGHSSVVNAVSLRKSRPFRAATASDDNSINFFHGTPYRFNRSLRVHSKFVYDVRYSPNDERFASAGADGKVYVFDGKTGDQVYEIDAHKGSIFSISWSPDSSQFVTSSAGYSCKIWDANTGSLIREWLSSDKKQLVGTVWPTKDLIIVVNSKGNLTYLNPSDCKVIDTIYGHQRSITAATLSPDATHFYTASYDGTVLSWDIGKQKAFPLVGESHTNQVMQMIMADDHVITIGMDDTLRVIDIKQGCFAKDNVFPTGYQPIGVCSVEDCLILVTVSDIQVLRSLTGVSTAKTIYQPSAVASHPLKSEFCVGGEDCCVYIHTLEKGELCEVAQCKDSTAPITCLAYSPDGKYLACGDASGKVVLYDANSREVITSRWAFHTGRILGMSWNAKSTHLATASLDTNIHIYSVERPMKYIAMKNAHSLGATQVEWVSENELLSTGSDAAIKVWSVTF O14306 YE8A_SCHPO MOD_RES 195; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9G1.10c; CHAIN 1..1191; /note="Probable inositol polyphosphate 5-phosphatase C9G1.10c"; /id="PRO_0000316865" MASRQGFSNVNEDEPELPPSVLSLKSKFESLSTGDLTNLDEKTAKRRTVKGCKNGTSEPNVFKARPIPPPRQVSSTIGSSTGRKVSGSIQRLASNFKNPSNPHADVSKIDRLPSDSSESHVATPSSPTISNSFVSVSPLLKRPQQKGPEISFQSSVQSTKGNDLMKHDDTNNHQIPPPKPNFSSKAGSSSPISVSPLKNVKAYISQSPTHSEASSVLSSEEEEENVINSSKSVPSFDLHDPFSQTFGKECPISTAPPVLNIGDRSLETPPPIPSPRPPQPVAVEAIQQSRAVISQQLPLHVSPRKPPKPPLRKVSTQRSSSPIENLATKSDASLVTGLQSSPYTHIAPASEMSLIPEKPRLPPRPSHTLSELSSPALTSENLSSKPSPLFPPPPPRVKSLATNKPVSMPVSTEQSDPSVAASSSSSSQLDVVLKGSIPDTSSVRRNPPCFVNGVESINVDFEARIFDVSGDRLVLAGNGGLRVYDTVTGLCHWHMPLGDTKVTSLSFKSSPENYSDDGRFVWFGTRDGMLWEVDVQNHHIVTKKSVSNCPITYVMVYKNEMWTLDDMGKLYVWQEDEIMGLSIQSTPHSIRTIPHATHAMVLDNRLLWVVVGKSIYVYDPSTSENESASVLAKPMTPPGLIGDISCGTTISNFTDLVFYGHVDGKISIFSKTQYRFLELITSSSFYRICSLVGVGNTLWAAYTTGMIYVFDVSESPWRLLKSWHGHKASHNGATTILGIDVNSVWKAKRLQVVSMASSVVKFWDGLMMGDWLATEMRSRFPEYSNFTDVSILICSWNAGASKPSDLDSDTIGASMIPMMIRDNGYPDIVVFGFQELVDLENKRLTARSILSKSSSKGGSSNSANISSQYRLWREKLESEMMRVSSNDDYQVLVCENLVGLFSCVFVKNKLQSKIRMLQSTTVKTGLGGLHGNKGAIVVRFLVDDTSYCIVNCHLAAGQSNKAARNNDLATILDNASLFPENDETDQLNTFVGGGDGSLIMDHEVCVLHGDLNYRINTLRPKALDLIKKNDIKTLLQSDQLLVERKRNAGFRLRTFTEPEITFAPTYKYDVHSEQYDSSEKKRVPAWCDRICYRGSPDYISAENYTRYELKASDHRPVSALIHSKAKMVNAQSQGSTWDVVKRKWIEYADEFKRKAKITYVMNYTSVSYQTAEQYLSGNNWNVQNALKQVSS O14307 TRM61_SCHPO BINDING 114..116; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q96FX7"; BINDING 135; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q96FX7, ECO:0000255|PROSITE-ProRule:PRU00952"; BINDING 140; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q96FX7"; BINDING 167..168; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q96FX7"; BINDING 186; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q96FX7, ECO:0000255|PROSITE-ProRule:PRU00952" CATALYTIC ACTIVITY: Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220; Evidence={ECO:0000255|PROSITE-ProRule:PRU00952}; SPAC9G1.12; CHAIN 1..364; /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit trm61"; /id="PRO_0000256175" MVFADYKQRVENGDLAVAWIGRNKLIPLHIEAEKTFHNQYGAFPHSEMIGKRYGEQIASTAKQGFIYLLQPTPELWTLALPHRTQIVYTPDIALIHQKLRITYGTRVIEAGTGSASMSHAISRTVGPLGRLFTFEYHATRYQTALQEFREHEMLIDVGGNTHLTHRDVCKDGFLDTEVKVDAIFLDLPAPWEAIPHLSNHVNHDKSTRICCFSPCIEQIQHSAEALRELGWCDIEMIEVDYKQWAARKSRIVHIDEAIDRLKEVKRRRIEGFERRKMRREQNLSSDAKVEDQDNDSMLGENKSSVSTETALKPVTNKRIREGDGNYEWTDVARVDSNLKSHTSYLLFAVHLPSQLDKQNQETGP O14308 SWC4_SCHPO SPAC9G1.13c; CHAIN 1..437; /note="SWR1-complex protein 4"; /id="PRO_0000076344" MTSADIRDVFELPPPEIGNKQKSKTPTERRPEGISRELYSLLGENSAPLAIYQKKFKEKPKVSHKAKNWVRQPFSISSRKDDFTLHHWVLKSEVDSEASYKFEKFNVPLFIIDYTDEEYQNYLKDEDWNKDETDYLFRLCKDYDLRFFVIADRYDNEKYKKHRTLEDLKDRFYSVSRKILLARNPINSMTAAQSSLLNTMEYNKEQEVIRKKYLIGLASRTPEEVAEEEALFIELKRIETSQAKLLSDRDEVLRLLDEQKGDGGIHEYHTSAGMSSLIQDMINSQRTKNKVEEAIVSSSAPSSGVSSVLNTPTRPHALSTPRIRYGPQPTDPQFGITWHEKLHPGTFVRSQKIPAIKASLSQRVSSVMTELGVSSRLIMPTAKNFEKFVELQNSIVSLLELKRKVDRLSQETEIQDKLSRKRSASPDGSESKKHISQ O14311 SPT3_SCHPO SPCC61.02; CHAIN 1..307; /note="SAGA complex subunit spt3"; /id="PRO_0000072165" MTETGRTSKYRVEIQQMMFILGEVQDPLPETTQLVEELIRGQVMEMLIQANELALRRGSRSITVEDLFFLIRHDRAKVNRLKTYLSWKEVRKKAKEQDANPADTKDLFEEVDSKTRSMNAVAMPWEVKNMFTEPVPETEEFEEDNDTMEMAYATRQRLKMADERTKKMTREEYVHWSECRQASFTYRKGKRFREWCGMSILTDTRPDNDIVDILGFLTFEIVATLTEEALAVKDRMDRIQNSSGSGGSHAAHHPKNCSLFDGLTEGRTPLQVSHVLEAFRRLQIPDKTHTAMRSFHGGLVKSRVYLI O14323 MCP4_SCHPO SPBC16E9.08; CHAIN 1..355; /note="Meiotic coiled-coil protein 4"; /id="PRO_0000096290" MEPCEDKCKRGLSLNFFEEDGPSLRLNSDSLDFLARDFKVEGMSQDNFDQKTKLYITEESLQKEVNIFLTKIYIRESEREPPQSHNSVFQLLSKIRNSVPNVSAFRNNLSILSKELSFFSFARHIHNRRLCWAEFIYCIRRGIKAIFKTTVQFLPTRLAKIFEKKASEVLKDNLLQTCNSKREGEVCDVKEPAVASSESSDCFNDMQELNNIVDLRDYSNSRFQQNRLLDRNLKGWIQGESEKALKGRRTTKRNDKENYNYPDFSNDNELLFSLATLIVENNPKKENIIPKYYLRYLQRLSRTEINKEIIEIEKLELEVVQFQMSIANLINTQVEVTNTIEELGLRCRPLPNENE O14324 YB79_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPBC16E9.09c; CHAIN 20..215; /note="Uncharacterized membrane protein C16E9.09c"; /id="PRO_0000316580" MKLGIFGLLLFTFFFQSQAVHFYFDGSKPKCFLKDMPKGMMVTGIVKAEQWNNEANKWVTSNNIKIRVQVDETFANNHLIYKNDLRSNEAVRFTTTNEGTHRICYLSTSDGAWFSSTKTRLHVDLASDDKYNLIASSEDEAKDLTDRVAALNTRLESILGEQMLQRSREMTFRDTSESANSRVVRWTIVQIVVLLVTCIWQLSHLQRFFVKEKLV O14325 YB7A_SCHPO BINDING 215..222; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 533..540; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 97; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 120; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16E9.10c; CHAIN 1..779; /note="Uncharacterized AAA domain-containing protein C16E9.10c"; /id="PRO_0000310279" MRRSGTSLSRDLERKIHERLVSLKDTIQQTEIEEWPVSTRRAIQFVQERDMSLRRIKKPILEKVVEKVLDTLKAEVEEKLASSQDLVLVDSDMEEQSDSNLMEVKDTNVINKSITSLWSSPNLKEIDGEDEKKSVGQESITGSAKRKDRRSKTNGSKRQKAEANREPPSDISLSDIGGLDDCINELLELVAMPIKHPEVYQYTGIHPPRGVLLHGPPGCGKTMLANALANELGVPFISISAPSIVSGMSGESEKKVREVFEEAKSLAPCLMFIDEIDAVTPKRESAQREMERRIVAQFLTCMDELSFEKTDGKPVLVIGATNRPDSLDSALRRAGRFDREICLTVPSQDAREKILRTMAKGLKLSGDFDFRQLAKQTPGYVGADLKALTAAAGIIAIKRIFNEISPLNKLDLNSDPRFNELDSDMALDSNDSLPLDHSSIIQRYLNAHPDPLSPEELEPLAICPQDFIEALAKVQPSSKREGFATVPGVSWNNIGALKSIRVELQMAIVQPIKRPELYQSVGISAPTGVLLWGPPGCGKTLLAKAVANESKANFISIRGPELLNKYVGESERAVRQVFLRARASSPCVIFFDELDAMVPRRDDSLSEASSRVVNTLLTELDGLSDRSGVYVIAATNRPDIIDPAMLRPGRLDKTLLVDLPDAHERVEILKTLTKQTPLHEEVNLDVLGRDERCSNFSGADLAALVREAAVTALRSAVFADIASNEPEITQHSALEPIRVTNADFELAFKNIKPSVSDRDRQKYQRLAKRWSSASTNDAD O14326 PUB3_SCHPO ACT_SITE 754; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; SPBC16E9.11c; CHAIN 1..786; /note="E3 ubiquitin-protein ligase pub3"; /id="PRO_0000120334" MEQGAKRVRFYIVAADGLSKRDLFRQPDPFAILTVDGEQTHTTKVIKKSVNPYWNEGFEVTVKPSSVISIRLFDQKKFKKKDQGFLGLVSFRMREVGSFRSNREVSLTRPLKKSSTTNLSVLGNLVLKVAPSKIRAPAGNHSSTTANRTTSTPTTTTARTTRTTPRPTATTNTSNQSTSNSTRNGTSAATSNGTGTGAGTGASHRSSPVTNRQTNNTSALSNSNAHIMSSFEDQYGRLPPGWERRADSLGRTYYVDHNTRTTTWTRPASSTNPVHNTSSDSQRLNHQNRHLPDDSNPSLMQSDSGNDLPFGWEMRYTDTGRPYFVDHNTRTTTWVDPRNPLVRPNGGSSTVGSLMQPQSLSHLGPLPSGWEMRLTNSARVYFVDHNTKTTTWDDPRLPSALDQDVPQYKCDFRRKLIYFRSQPGMRPLPGQCNVKVRRDHIFEDSYAEIMRYSAHDLKKRLMIRFDGEDGLDYGGLSREFFFLLSHKMFDPIYCLFEYSAVDNYTLQINPHSSINPEHLNYFRFIGRVIGLAIFHRRFLDAFFVVSLYKKLLRKKVSLADMESIDAEFYRSLKWVLENDITGILDLTFSVEEDHFGEVRTVELITNGENIEVTEENKKKYVDLVTEWRVSKRVEQQFNAFYSGFVELVSPDLVNVFDERELELLIGGISDVDVEDWKSHTEYRTYIATDPVIKWFWEIIAGWKNEDRSKLLQFATGTSRIPVNGFRDLQGSDGPRKFTIEKAGTPDQLPVAHTCFNRLDLPDYPSKDTLHEKLSLAVENTVGFGNE O14332 REM1_SCHPO SPBC16E9.17c; CHAIN 1..402; /note="Meiosis-specific cyclin rem1"; /id="PRO_0000080419" MNSNNKRVALQEISNYVSKSLNVKGWVNAQVREISLQNGCSPSDKHFPSQSWHGISSIEESQIQKDYDSFLASPLEEEIVFTEKQLLVDLDVCSISNVQSPNCSVSEFGIAIEESNDNCAEEDEEEELQMRYSADESVSVEYAKEILSHMEKLEIRFMPDYRHMSAQPYYVTEMRASVINWIVGVHTCINLLPESLFLSINVLDRFLSLQNVPASKMKLCGATALFIACKYEEIHPPTVKDLEIVLEGEWIGEDICGMEKYMLMVLQYQLGWPGPVSFLRLLTIVNKWESQLRIMIKYFLEVSLVEQRFSSLRASQLVATCAYTGQSILQEENWSNTLPQITGYDYMSLVSYVHLLLKCLENPFDHHYAIYSKYATPYFHGISRQVHDWIATNTNLMAMDGS O14336 MUG80_SCHPO SPBC1D7.03; CHAIN 1..461; /note="Meiotically up-regulated gene 80 protein"; /id="PRO_0000278613" MSFPYQHTSRSQVQPPLAAPGLSMFAPVSSSNSANSASSVAALLSHAPMYGLGQRRPSFLPGVSVPDTLSVRSGFSIPSSSHHPSAVPSLLSQHRLQQPQPRLYPSAPLNYYWPSYQSVPSAAPPPPSQQRYMPDSAVAYNPNQDQFGNSVNVSAACNNVSAPLIANNCAPSFYQSRHPVADVPVTNNTATTTSETDNTIPGNLNMPSVANVQQRISPVCKTNMEDQEETVYTGGVAAKLDYKMDQMVEYLSIMTCKLYARFLNNAQMHSLANSLPGLVFSFRKVVTQILTSTRLPRASCLLALSYLSDRLDAASQTTDFVNQWTKESLFFQICALLTTALILANKFLDDNTFTNQSWSQVTGFRTALLNSFEQDWLASMSWNLSPGPRGQKAWEWWSASYSLFTSSNATYSGEQKTYSPTTLSTNAPPSPSSGRSCSNCNYYYPYTPVGYYPVYNRYAMT O14337 RM07_SCHPO TRANSIT 1..18; /note="Mitochondrion" SPBC2F12.02c; CHAIN 19..287; /note="Large ribosomal subunit protein uL5m"; /id="PRO_0000030544" MLGIRKNIRISVNFLQRRTITVKQKLGKNRPLPGWDPNSEYFRPGPTMLNRLQEHLHDTILPDVLAASYRHDIDTALSTDEHTQKDRLPRWIGDNPYYKNRPPQKMRGNKPLLPVKESVNPKNLPSISKVVVSTMHKEALVDKTQLLSTMMAFRSITGLQPEIVYARKDVSPWKLRSGVPVGVKVTLTGESMYTFLSILSELVLPQLHDFKGLSPTSGDQTGNISFGLPSEVMPLFPQIEAVYEMYPHSLPGFNVNITTNSKDTRLARFFVSSLIPFTDGNKEGYVG O14338 YB33_SCHPO MOD_RES 261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 263; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 265; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 268; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2F12.03c; CHAIN 1..891; /note="Uncharacterized serine-rich protein C2F12.03c"; /id="PRO_0000116497" MSAIDSCEHTVSWKLCEQKYNEATTLLSKLKKLLGNFKENCTSVVVDGHKKPRSESRKKYDAKKQHQSSHFATPVKGVESSEPTEKKKRNKEALWLRARQKKWKEIFELCQKITSLLGGTILIDVSFSMEKDVLTYLWMRVHYQVISFFKHRIYEASTQHDPELLSSLVTMHIQYLNSTIQFYTTLIAIIGELYHLQCLSPLTSFFTSCVTPKTILESPLRKQGSHNWKTSTNSQSRLAALFSSIFEDSCLEVDSVKRLLSGSPSSSSSPLKKDSSSNSLTYEPALTDHKPQYLVLCVYRSLIYIGDVHRYLAEVRSPNVPDYQVSRRYYVMAANVAPDYGVHFHQLGLIEVADARSSSRKSSSGQSSSLKGNVNVEDKRLIQALPAISFFFLSSISPNNVAASSAKTSLFIALKRCFGKTNDGSNPCLYHKESSAISLFLRLYAIAFSNTDADYIQDSGPLFKRVRFLLSESLKSGLFSESSLLQMTYCALAARVLAPFIGFSDSGEHGESYPNLKLATQTTTMFFEVLSDSVNSQLPLQALTSGVSSKKDGNFDDLVERRQYGSLSSNAVLMPMLLPLCVLTSSCLQNGDVWLTKDIRTGLSQIFNRLSFFLENTNQTAPDDSVLVRCSSKSIGLLFFFPLVKVCGVPRDTLQWLYFSNHYPFNEEGKGPQVDDSDALITIALDSLYVLLNMRAKSTPNSTSFSSPPTPHRSPFSGQAFTGMGLSNYSLMSSSSFPSAQSSPTSPFLSGTPSIANQSSSIASLQFGRMVDSLVGPVQPIPAQTTGCSVHSLQQRTFSNESPRAVDSGFSRTSTPFSESTSSYPLVSGNLSSCETHLNGSPQNGHLQGERVLFRPLRSPALNTFSTPATEPPEHLVLSELLKKMVNISNN O14339 RL17A_SCHPO SPBC2F12.04; STRAND 5..7; /evidence="ECO:0007829|PDB:8EUY"; STRAND 14..24; /evidence="ECO:0007829|PDB:8EUY"; STRAND 79..82; /evidence="ECO:0007829|PDB:8EV3"; STRAND 111..121; /evidence="ECO:0007829|PDB:8EUY"; STRAND 144..152; /evidence="ECO:0007829|PDB:8EUY" HELIX 11..13; /evidence="ECO:0007829|PDB:8EUY"; HELIX 26..36; /evidence="ECO:0007829|PDB:8EUY"; HELIX 41..52; /evidence="ECO:0007829|PDB:8EUY"; HELIX 71..76; /evidence="ECO:0007829|PDB:8EUY"; HELIX 86..105; /evidence="ECO:0007829|PDB:8EUY"; HELIX 169..181; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..187; /note="Large ribosomal subunit protein uL22A"; /id="PRO_0000125344" MVRYSASPALETKCAKARGAYLRTHFKNSREVAFTINGMSLKKAFIFLDNVKEHKQAVPFRRFNGGVGRTAQGKEFGVTQARWPVKSVKFFYDLLKNAEANAEAKGLDMDKLIIKHVQVNAAPKQRRRTYRAHGRVTAYLSSPSHIEIIVAEEEEAVPKANDTVSRVSLKQGAKARNLAARKAITAA O14342 CATIN_SCHPO SPBC2F12.12c; CHAIN 1..517; /note="Splicing factor cactin"; /id="PRO_0000116498" MAFRDSTRDFNRSRPEKRHASRSSSPRSFRPSNQNARANYNLPRVRDAMKEEERSRETKEMQEREFLRLQQLRRAIIRLKNDRSKPIDKLLVSVYLMPGPEWEENGEKNSIDFGTVDMFDPLSVIQSYKAEDLEEISRNIGDIQQLETNQCRLTYWKYVKMLVNSRMEHNKVGQFSRGLKVVAGEVQRILAPKSFEQLEQLEAQIQKKLKSNVPLDTDYWVDLLNSLKSYKAIAYLKKTFNEELQIRKNKLDNEEWDKAFSDAKKLSNMKDREEKLYIVPIDPKPILRAQAIPRRIQPEEQADYEKELNDHVNIVKSSTYIPISIPTQKQKPTLPKNSNLINEDEFSIANRARLEREYLQSDDAEEQEMLGDYVEGQTRVVNENGVTLKKPHYFNRVLLGFEWNSYNQAHFNEAHPPPKAVQGYRFNVFYPDLIGTGRAPTYRIERTRRKNKSDTTDLQDDVCIIRFIAGEPYQDIAFSIVDKDWDYSAKRDHGFKSSFDNGVLSLHFRFKKLHHRR O14346 HACD_SCHPO ACT_SITE 145; /evidence="ECO:0000250|UniProtKB:P40857"; ACT_SITE 152; /evidence="ECO:0000250|UniProtKB:P40857" CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377, ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134; Evidence={ECO:0000250|UniProtKB:P40857}; SPBC19C2.15c; CHAIN 1..208; /note="Probable very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase"; /id="PRO_0000116858" MSKILKIQYLKLYNVISCFLWMSVLLRTGLIWGITKDTAVVFHETNTLVRWVQTLAIAEVFHSIFGLVSSSPLTTIIQVASRLYLVWGVCYPFSYVIEGSPIYLSMIIAWSITEIIRYAFYAFNLNGDIPAFLTWLRYNTFLILYPIGAGSEFLLVLKSRIAAQYVWSLNKLLWPILMSIYPPGLYIMYTHMLAQRRKISKRAAARRT O14348 NC2B_SCHPO SPBC30D10.02; CHAIN 1..161; /note="Negative cofactor 2 complex subunit beta"; /id="PRO_0000317090" MNDGFADDELSLPKATVQKMVSDILPVDLTFTKEARDLLIECCVEFIHLVSSEANEICEKEAKKTIAAEHIIKALENLEFKEYIAEALEVAAEHKEQQKNREKKSSKFEQSGVSRDELLRQQEELLSRARERFKNQNIAHDNHTTTAIPVPTASETETKEN O14349 ISN1_SCHPO ACT_SITE 147; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; ACT_SITE 149; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:A0A144A134" BINDING 108; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="allosteric activator"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 147; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 147; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 149; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 149; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 155; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 183; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 333; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 341; /ligand="IMP"; /ligand_id="ChEBI:CHEBI:58053"; /evidence="ECO:0000250|UniProtKB:A0A144A134"; BINDING 365; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:A0A144A134" CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000250|UniProtKB:Q99312}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q99312}; SPBC30D10.03c; CHAIN 1..405; /note="IMP-specific 5'-nucleotidase 1"; /id="PRO_0000084255" MASRYRVEYALKQHRKDDFIEWIKGLLSVPFVLQAGTPSQKLVTREKEQETLERYAVILRDVEKLIEAHIQIVSEGGSYSQLKMLVPSITIFWTPLPLVKAMYALEPKLCLAKRSFVAPSFNDVRAILGGAQLNYLADNGLDMVSFDGDVTLYEDGQPLLPDNPVISRLIQLLSRGIYVIILTAAGYPSRTGQEYTDRFSGLLQAIEDSDLKDGQKRKLHVLGGESNYLFAYDPLHGLQWVDADSWMLPVMKTWPHDEILEILDTAEETLRSCIQGLNIDAKIVRKERSVGFVPSLGQKLRREQLEEAVLETQATLQIRNFSVPFTAFNGGNDIWCDIGDKKLGVLCLQHFFNISHPSRCLHVGDQFLSAGNNDYKARAAATTVWVSSPHETIEFLDYYFSFLKK O14354 MG101_SCHPO TRANSIT 1..35; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC30D10.08; CHAIN 36..270; /note="Mitochondrial genome maintenance protein mgm101"; /id="PRO_0000045818" MQTMLGKPALQYFGKLSRYLYKNGEPINIWVYSRNSSFSVIPKNGLLSPKITQRFYQNSSIQYQKDKNIYEPKENLEEKELSEGFLDESRLEIPEAGHNWEKSFFGLSSQPFSKEICDLLTAPLEVDDIEIKPDGILYLPEIKYRRILNKAFGPGGWGLAPRGNTNVTSKSVSREYALVCHGRLVSVARGEQTYFDPEGIATASEGCKSNALMRCCKDLGVASELWDPRYIRVFKRENCVEVFVENVLTKKRRKLWRRKEDKFSYPYKEV O14355 YB49_SCHPO SPBC30D10.09c; CHAIN 1..217; /note="Uncharacterized membrane protein C30D10.09c"; /id="PRO_0000315969" MQLLMLEQISLASSVVATTVLVAPVLSTIINLLTNFGQRIFIAADSSKSTSMEFLSTIIGAGYPIYKTYLLLELPSKRSQLLPKAFQLRNEEHKSIEEERRRLMAYWCVYGCVTAAESILGRFLSWVPFYSTSKIVFWLWLLNPRTQGAAFIYASYISPFLSDHKAAINNFLEKLVQFTTRQPLVLNAWALVKSLIDKLPKGDVEAPGSDADTKKSK O14357 GPI1_SCHPO SPBC30D10.11; CHAIN 1..653; /note="N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein gpi1"; /id="PRO_0000087557" MSTTTMNIASAPIEVKRIYWPKSTISYTDSGYLVGWKYSTNDLIVVTTITSYQSFANFLVDYCKNQDQSVDIKSLCILGTFNCSADILPGDKYEIDCWIKVQQSTELSHPRVFDSASTPLKINLHIIYYHPPQPRKMQFLSLEPLSLLLLKDSFINKSNPEYESMQHQQILLKKLKLHFPRRKENSWKRSLRSGLIELLNQSFEVRMLTHENNNKKNSYVFRLFDRVSSSTFYFFNSLFAYFIILLRIINEVILLAINYRPIPLSYNMMDIFVSARQVDLRLQQACFWPVQYMKLWVFRKSKRVAIEDYKEYIRFYNNLWLVANDMIFGITMSSFILENLHLVVKLIENITFEYAIKNVRSMVIWLVDTPAGLKLNNDICKFIMKLSVWVIDVWSNFLLHCLPWTPFLVQVVAISGFGGASLMIALISDFLSVMTIHIHLLYLASSRLYNWQLRVIYSLLQLFRGKKRNVLRNRIDSYEYDLDQLLLGTILFTVLIFFLPTIYVFYAAFALTRVSVMTCLAICETMLAFLNHFPLFVTMLRIKDPYRIPSGLNFEIVSFEPLKQDGFATLYLNCNSKPMSLGSMFEHYRKLARRLISHYLSKTTLISLLVGCPVPAIPAEQLYNIQYAMLPTKRISIRKLRDLLFHQKKFPYD O14361 PHA2_SCHPO CATALYTIC ACTIVITY: Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51; SPBC30D10.16; CHAIN 1..272; /note="Putative prephenate dehydratase"; /id="PRO_0000363369" MSASKIAFLGPRGTFSHQAALLARPDSLLCSLPSFAAVLEALSSRQVDYAVLPIENSTNGAVIPAYDLLKGRDDIQAVGEVLVPAHHCIIGKSLENVQKILSHPQAFGQCSKWISANVPNAEFVSVSSTSQAAALASKDITGTIVAISSELCAVENQFNLLVKNIEDDSNNRTRFLLLRSGGFQDDLSPLKEKSLLQFYLSHPKKLSAVFEVFAAHKVVITNLVVRPSCKFPWTYIYFVECLGMEKHLIDRVGKYCDTFTFMGSYTNQISYF O14363 RL1A_SCHPO MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC30D10.18c; CHAIN 1..216; /note="Large ribosomal subunit protein uL1A"; /id="PRO_0000125840" MSKVSPANIRSSVETILKGSEEKKRNFTETVELQIGLKNYDPQRDKRFSGTIKLPNVPRPNMSICILGDAHDLDRAKHGGVDAMSVDDLKKLNKNKKLVKKLAKKYDAFIASEVLIKQIPRLLGPGLSKAGKFPSPVSHSDDLYGKIIEVKSTIKFQLKKVLCLGVAVGHVDMAEEQLAANLSLAINFLVSLLKKGWQNIGSLVIKSTMGKPYRLY O14369 SCE3_SCHPO MOD_RES 49; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 50; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 61; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 71; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 197; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 250; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 251; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 252; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 347; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC18H10.04c; CHAIN 1..388; /note="Probable RNA-binding protein sce3"; /id="PRO_0000081900" MGPKKSTKMSLNAFLGDESFGSTNWADDIDDLPALPQDRTTSTYRATPSSADAGYNAPSSTFESVRSPPESRREGGMGSGYQRDAIPIPSEPPFTAHVGNLSFDLTENDLGDFFGEGVTSIRLVIDPLTERSRGFGYVEFETADTLSAALALSGEDLMGRPVRITVAEPRRSFAREERSTGDWVRRGPLPPAEPAESPFGKRRTNSGRFRDPARDPSDRVREEPREWVRRGPLPPRESSERPRLNLKPRSSSNVNTEATPSATTTTSSKPKRDPFGGAKPVDNTSVLQRVEEKLAKRTQSFRREDNANRERSTSRKPSADKAEKTDKTDAIAEKVSDIRLGDGEKKSSETDSEVAATKTPATEDAPATNAGEAEEEEGWTKIGKGRKH O14388 RL27A_SCHPO SPBC685.07c; STRAND 9..13; /evidence="ECO:0007829|PDB:8ETC"; STRAND 22..29; /evidence="ECO:0007829|PDB:8ETC"; STRAND 40..48; /evidence="ECO:0007829|PDB:8ETC"; STRAND 55..57; /evidence="ECO:0007829|PDB:8ETC"; STRAND 69..75; /evidence="ECO:0007829|PDB:8ETC"; STRAND 80..86; /evidence="ECO:0007829|PDB:8ETC" HELIX 59..66; /evidence="ECO:0007829|PDB:8ETC"; HELIX 90..92; /evidence="ECO:0007829|PDB:8ETG"; HELIX 98..102; /evidence="ECO:0007829|PDB:8ETC"; HELIX 104..124; /evidence="ECO:0007829|PDB:8ETC"; HELIX 128..131; /evidence="ECO:0007829|PDB:8ETC" TURN 17..20; /evidence="ECO:0007829|PDB:8ETC"; TURN 77..79; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..136; /note="Large ribosomal subunit protein eL27A"; /id="PRO_0000126090" MVKILKPGKVALITRGRFAGKKVVILQAIDQGSKSHPFGHAVVAGVERYPLKVTKSMGAKRIARRSRVKPFIKVVNYNHLMPTRYALELDNLKGLITADTFKEPTQRSAARKTVKKTFEEKYQSGKSAWFFTPLRF O14399 UBL1_SCHPO SPBC12D12.08c; CHAIN 1..78; /note="Ubiquitin-like protein 1"; /id="PRO_0000114889" MLIKVKTLTGKEIELDIDPNDKVSRIKERVEEKEGIPPSQQRLIYAGKQMADDKNAESYHLEGGSVLHLVLALRGGSC O14400 GPDM_SCHPO BINDING 69..97; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1223.03c; CHAIN ?..649; /note="Glycerol-3-phosphate dehydrogenase, mitochondrial"; /id="PRO_0000010433" MFSIFKRRSVQAALAASGLVGGAVFYSDFIKRPAPSHFNPQFTPFTKSLAPPPSRETLLKNVEDISKFDVLIIGGGATGTGVAVDASTRGLNVCLLEKTDFASETSSKSTKMAHGGVRYLEKAVFQLSKAQLDLVIEALNERANMLRTAPHLCTVLPIMIPVYKWWQVPYFFVGCKIYDWVAGSKNLRASTIFSKETTVAIAPMLDDSNLKASCVYHDGSFNDTRMNTTLAVTAIDNGATVLNYMEVKKLLKSKDNKLEGVLAIDRETGKEYQIKATSVVNATGPFSDKILEMDADPQGEPPKTAQFPRMVVPSAGVHVVLPEYYCPPNIGILDPSTSDNRVMFFLPWQGKVIAGTTDKPLSSVPTNPTPSEDDIQLILKELQKYLVFPVDREDVLSAWCGIRPLVRDPSTVPPGTDPTTGETQGLVRSHFIFKSDTGLLTISGGKWTTYREMAEETVNELIKDHDFGKALKPCQTKKLILVGGENYYKNYSARLIHEYHIPLRLAKHLSHNYGSRAPLILELYSKTDFNKLPVTLADKEVFAPSSDASSDKSVSYASFDEPFTVAELKYSIKYEYTRTPTDFLARRTRLAFLDARQALQAVAGVTHVMKEEFGWDDATTDKLAQEARDYIGGMGVSSDRFDVKQFEVK O14423 CBH1_SCHPO SPAC9E9.10c; CHAIN 1..514; /note="CENP-B homolog protein 1"; /id="PRO_0000126134" MPPIRQAVSLAEKKAIRDYYNQSAHRIPQKEVTEWFRKTYNKDLSQSTISEILSPKYSYLDDGSVRLGDIKKIRAPKFPLLDNAVYEWLQQREVEGLPISGDMIKQAATRFWSKIPAYASLPLPDFSNGWLDKFRRRHYIQQSAVNQALESIKFEVFREYPVHIQEFIRPYAQKDIFCVGGTSLFWKLTPNKQNLDYQEIQGMKRGKAKVSLIMCCNADGSERLPLWIVGYAQNPRSFEQCGIFPKSMNFEWKWNGRASISPIIMEEWLRWFDTRMQGRKVLLMLESNDTYQFGVESVRRFKGGFQNTSVFRIPEKTLDIKSPFEQGIVDTFKANYRRYWLQYSLNQINILRDPLKAVNVLKAIRWMLWSWNFGVSEKTIQASFLRSGLLGPHSEAEGQGMESYQKAIMEIGNLISSKGSEAVKQINEYIRPSEEDETKLHQDAVDTVAAEFLEERRFESDEEEDVEPQISNVEAAMAFEVLIKYFEQHENGDPSFVLDLYRRQRVIAPNNLIA O14443 GPN3_SCHPO BINDING 13..18; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9"; BINDING 173..176; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9" SPAC4D7.12c; CHAIN 1..276; /note="GPN-loop GTPase 3"; /id="PRO_0000255594" MVKVAAFVCGVASSGKSTFCGALMSYMKSVGRSCHLVNLDPAAENFEWEPTVDIRDLISIDDVMEELDYGPNGGLIYCFEFLMENLDWLNEEIGDYDEDYLIFDMPGQIELYTHVPILPALIRHLQVTLNFRPCAVYLLESQFLVDRTKFFAGVLSAMSAMVMMEVPHINLLSKMDLLKDNNNITKAELKRFLNTDPLLLTGEINETTNPKFHELNRCIVQLIDDFNMVNFLPLESGNEESVSRVLSYIDDATQWYEDQEPKDPDRFEADDLEDDE O36016 PTPA1_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPAC4F10.04; CHAIN 1..325; /note="Serine/threonine-protein phosphatase 2A activator 1"; /id="PRO_0000226103" MQVVDEKTILELENERFDESSQFKTPEKLIVEASDMTAFRQSKAYYRIFDFLQRLNIASVGVNDYHVEYSTRVEKLVRILCRVKEITKTVPPASGRHRFGNPAFRIWHEKLRDSASQIMDIIIPDSLSKAKVELLDYFLGSFGNSQRIDFGTGHELNFLGFIKGLDLLGLLDAADYKAIALYITHVYLEVCRELVQTYRLEPAGSHGVWGLDDHFFIPYIFGSAQLADKASSSIIKPDAILNKKIVDEKANSNLYFSAIKFINVMKKGPFYEHSPILYDITAVPIWSKVNQGLIKMYDVEVLSKYPVVQHFHFGNLFPFNPLVAK O36017 LIPB_SCHPO ACT_SITE 182; /note="Acyl-thioester intermediate"; /evidence="ECO:0000250" BINDING 83..90; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 151..153; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 164..166; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; SPAC4F10.05c; CHAIN 1..219; /note="Probable octanoyltransferase"; /id="PRO_0000062908" MNKIQHISFITKKNPLVSYERVGALQNRFVQHYLNYKANKVEQPPKPTIITSQVCPVYTLGRRESSINFTKGFPKAKVVKALRGGQTTFHGPGQILAYPIIDLKSFGLSPREYVSRLEQAIIATCKSFGIEKAHTTKNTGVWVTENDKIAAIGIHLRRNITSHGLALNVSTDLKYFNYIVGCGLYGKNTTSFKDQGVFTDLKSVEKVLVNNLDSFLMSK O36025 MPD2_SCHPO MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 318; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 320; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 509; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 604; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 637; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 775; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 829; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 838; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 840; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4F10.13c; CHAIN 1..992; /note="GYF domain-containing protein mpd2"; /id="PRO_0000339406" MNSEASVFSNMDWSQLAHSLHKKANNSSSSTTGAFPQLTSFTKPTATNGVDSPTSSHIDPSVSAKLDSQRKLSLKSGNMWDSLNAPSELTSKNPTVSSTTSSANPAIVSNGGSPFYKNPVVANNPSSTFDMSTNLFNSKNANTSFTNAFSNEGISPGFLRDCFPSSNSITTGTASPKLGSPFNHINRPVLDRSPSSFSQSRSAVSGNMNPGVGTLQQPQRAGSDTFPDLNTSSSNQPGGEPNVASANTHSLEILSSSAYHPSGSSNGISAGLTQSVASPVGQVDNLADFSQSPLRRGPSRFPTNSNVPVGNSMSIRDTDSPLNILVDKAKAKASIKENASQPVAPSASQREHSAVNSPAAAMSPSTAMFSSEAFPQHLASLIPPALLHWLYKDPQNNVQGPFTGVDMHQWYRAGYFPLGLPIKRLEEEEYYSLAFFIRQVGNQLEPFLVPLSPVTVQNASWNAQGTDLPLSNYLPESSEQNRGGNKHLELYPSTAEVSNVRNDESKANSLSEISYNQQSECRSSELNVNEDSANQKEESALGTSDNSDMYEKENTPIHHNESLNQLSKDLGSISLSEETKQEKPSKLKETVESKRLSTGVQKQSPAASKEIPVTSGSQTTAPKPSPWKSLPPKHLPSLDETISREMSIASSEALPQVEKSNSDQPPVAIPSTSKTGSPWAKVSDVSTSMAQEIQRMEKQNENLKSKVASNPVSQTSTNAKASTPALASGSIWGSPSVINAWANKPAALKSPLIKKNIQQAELAQNKQQSSVTTASPRSNALNANTPKAAAPSSNVTMKNVTSILETSTFEGEDTWSVVGPGGKIVNQQSPSAQQTTRSPSKVSATLNAGNSQASTSSKLQQVVSMSGHSPDFLAWCKISLKGLNEGVNYEEFLDMLLSLPAENNVETFEIISDSIYANSTIMDGRRFASEFTRRRIADLTGKDGQQSNNKSQSELGNSSGAWSQVVRNKPKQGTEWNSAFKVVTSKKNKKRV O36030 YEKI_SCHPO SPAC4F10.18; STRAND 3..9; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 16..21; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 31..47; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 50..52; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 55..65; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 70..75; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 80..82; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 97..106; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 111..117; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 120..127; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 137..146; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 148..150; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 151..161; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 164..172; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 175..182; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 187..193; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 196..204; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 207..213; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 234..239; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 252..254; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 256..261; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 267..271; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 275..281; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 285..288; /evidence="ECO:0007829|PDB:4GQ2"; STRAND 306..310; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 319..321; /evidence="ECO:0007829|PDB:4FHL"; STRAND 328..333; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 338..343; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 351..355; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 360..365; /evidence="ECO:0007829|PDB:4GQ1"; STRAND 369..385; /evidence="ECO:0007829|PDB:4GQ1" HELIX 26..28; /evidence="ECO:0007829|PDB:4GQ1"; HELIX 218..222; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 240..242; /evidence="ECO:0007829|PDB:4GQ1"; HELIX 293..298; /evidence="ECO:0007829|PDB:4GQ2"; HELIX 386..388; /evidence="ECO:0007829|PDB:4GQ1" TURN 129..131; /evidence="ECO:0007829|PDB:4GQ1"; TURN 214..217; /evidence="ECO:0007829|PDB:4GQ2"; TURN 262..265; /evidence="ECO:0007829|PDB:4GQ1"; TURN 334..337; /evidence="ECO:0007829|PDB:4GQ1" CHAIN 1..391; /note="Uncharacterized WD repeat-containing protein C4F10.18"; /id="PRO_0000316556" MTLSSNQYQLPLNVRPYTTTWCSQSPSCSNLLAIGHDTGITIYCASEEQTPGSTGLTLQELFTIQTGLPTLHLSFSSSCSYSENLHDGDGNVNSSPVYSLFLACVCQDNTVRLIITKNETIITQHVLGGKSGHHNFVNDIDIADVYSADNRLAEQVIASVGDDCTLIIWRLTDEGPILAGYPLSSPGISVQFRPSNPNQLIVGERNGNIRIFDWTLNLSAEENSQTELVKNPWLLTLNTLPLVNTCHSSGIASSLANVRWIGSDGSGILAMCKSGAWLRWNLFANNDYNEISDSTMKLGPKNLLPNVQGISLFPSLLGACPHPRYMDYFATAHSQHGLIQLINTYEKDSNSIPIQLGMPIVDFCWHQDGSHLAIATEGSVLLTRLMGFTRL O36032 GLRX1_SCHPO SPAC4F10.20; CHAIN 1..101; /note="Glutaredoxin-1"; /id="PRO_0000141610" DISULFID 25..28; /note="Redox-active"; /evidence="ECO:0000250" MSSVESFVDSAVADNDVVVFAKSYCPYCHATEKVIADKKIKAQVYQIDLMNNGDEIQSYLLKKTGQRTVPNIFIHQKHVGGNSDFQALFKKGELDSLFNTA O42648 YF98_SCHPO MOD_RES 314; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 315; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 316; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC10F6.08c; CHAIN 1..341; /note="HMG box-containing protein C10F6.08c"; /id="PRO_0000339416" MENPPYHVSISKSEEIKYRQKCKDLKARIQEIQKGNQELLSKYEVIRRAVKRGRLERAILMEQLELQSEAKSREFGQRSEPSPPPPPEGIKIKISTKGAGNPSAKKLKISTEETSDTNVALNNTSEISHKSSNNSQPKDASVNDTDADFEQQNQVVQSKDEKITNTDPIPSPIITNLKTESSKSSGAKKATSNAKITDTMLFNHFSSIQKPKLKAEGSTLKGQALKKTLEDTWNNLTEEEKKPYHEGLLAAREKAREARRRRSAQNSAKLEKEKAKEKQKDKDQEQDTVSDKNQIDEIEKGQKEVDEEPVSEPTTSPILPPKNQEPIRMGGFTVVNRSSNA O42656 RIC1_SCHPO MOD_RES 293; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1851.04c; CHAIN 1..1052; /note="Guanine nucleotide exchange factor subunit ric1"; /id="PRO_0000116843" MYFLHGTPQRIQLSSRAIQICRIPKVSFFVVLTETEILIYQIRPLTLISKITKSQNLFERHGKNKKIAVNSEYGIIAVATEKNYVAVYHFTLNASKPVLTPSPYLTRYDDGPGEIFGPIKCEIQYKLAMRYGGGLKCLEIQRDSIVYAADSAPIIQVSTLETTDPNKLWKVSSKQYDLREVTWFLDHSSLISRLYFDVKIDTFFWMSTDGRVYANIGVSSNTNTKSLFGLCVHNPVDLNKSDNDKDINEDLESKLREKKATVLSTNARFSLLYVGTADGTVYAYEIRDFGRQYVQTHSFKYSASSGKVNHIATTGDGHQVMVGYDDGWATLSPYLNLCCASSETEYFNFGLSCGFWDRDSSSFYGLGSKNFSSTGEAEGTGLSTPIIAESLKENDEFFAMEKENVDIQYLSQNDNTNDVLYSITDSKQFISTIYILPFLKSTIVSSVQSTLQVCGAQTSDRLYISKSYEFCSSVKNNFGIDFWDQVEYPQPYVASEWPIRYVSIKDDGSLIAIAGLHGLAIYVCSKKTWFLYKDANMEQLISVTCPMIWCSQFLLAGVVCESNFELHLYKAKGPLDDRENLAKLSFTSTIVTMSVCDEYSLVVYTADNFLHHIRFDINELGRLELDYLTSVNFAPIFTTPSRVRSITLLLPKDLANIQPSDLLFYAVLLVLINGKLVLLSLKKQHSKELLYQCSMLAGDVEFYFINGSQEIPSLFHSIWIMTGKGLKLWLSFSEILSSVLINTKNLIDGLPKFLNTSKRVSLENFHRLSVEDLRSPSFVYKNGVDCNFDNTHLAKLIKNVNISEKFQKECIDLESQGCLLTVLSNYGLLLTAYTQGHKNLVNKMEYAHIQIGVYPFLPEIVRALLLLDKREQAIDLVKTYGHLHYINFVLEKLLSSSLLTYNSSQRDKLLYEVSLLFKDLQEFTTFKIVLGCLRKTEAEYWPMIFKYFGEPKDLMKKCLETEDVKSAAECLIIWQIHQGSASCASTFLSIYEMALKIKNWDVCTELSSYLVSLDPEKRLLKTALELLDEGPDSKDIRLYDQFNNLMKEVDKY O42662 MTL16_SCHPO BINDING 54; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q86W50"; BINDING 83; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q86W50"; BINDING 106; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q86W50"; BINDING 155; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q86W50" CATALYTIC ACTIVITY: Reaction=adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:52808, Rhea:RHEA-COMP:13573, Rhea:RHEA-COMP:13574, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.346; Evidence={ECO:0000305|PubMed:28525753}; SPAC27D7.08c; CHAIN 1..385; /note="U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase"; /id="PRO_0000339418" MPIYILIERSVKNGRIDFWNEDAIRTLGKAILDRDYSLRVEFPENRLCPMVPNRATYIRYIHDLLSSTSGQKDKKRIIGLDIGTGASCIYPLLGCRMYSYDFVGTEIDKFSFETAKSNILQNNMESQIKIVLRSKQDCLLPDTEGMEEFTFVMCNPPFYEHEEDFINFKQNPPSGVCTGVYHEMVTEGGEVGFANKILTESKKRKGIQWYTCMFGKKSSVPAVVDKLREQNISNYGIYELALGKTKRWIICWSFQAMRPHNELIRPSSTSLSKYFPHKVLQNWTLDPELCAQIDDILQKFLDDNKIPWSKKGSVLEISTKSITWSRKARRISKSQTSVSSLEGQMKCELNVIDNQLQCKWIEGYDYNVYESFCSALARALRDNKK O42668 TPR1_SCHPO MOD_RES 930; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 932; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 959; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 961; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 964; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 998; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC27D7.14c; CHAIN 1..1039; /note="Tetratricopeptide repeat protein 1"; /id="PRO_0000106375" MEGFTLETHASRIIEVPLLGQEDQSVEIDCSSLPSDATELCEILVNEQAPREFWTKFAHEYYIRGLREQAILILKSGLETLKDSESLCILNANIAAIYLSMAREAMLKKDTDLRDEQLRNVRTYLEAANNIDSKSEINVLLHGIYRILLNPTDKESLENAARCFDFVLQKSGGNILGFLGKARILYAKGNYRSALKLYQRALVSNPQFKPDPRIGIGLCFWNLDMKTDALSAWTRVQQLDPKNTVVDTYIGLYYYDLAFQNVNNDSFVQNYGKALQHIQRAFKTRNNDPVASSILERYVYSKKNYEGCIKLAENVIQNSFSSSLIADGYYWMGRAYHQMGNNEKAMASYQKAKAADDRHLLSSVGIGQIQILQNDLTSAKLTFERIAEQNQSCFEALVVLGCLHASDSKPDLTKARMLLDRAFNLVGSSKLPRVVDSDLYITQARLWEKEDTKKSLGFLTRALDFLESAHMSVGPELLNNIAVLQYHLGLIPEAHGNIIKAKSVLPDANPELSLLLDYNLARCEEELGNTSVASEAYVSILEKHPSFIDARIRKCLLQLSNPNEETFKEIRHIMNADSQNLEVRAFFGWYLSKQKRRPVEDPEVRHCSQTLRHWHDDIYSLVQLGNAYMRQAREFRVHNDREKLKRQKLYIKAIQSYDQAIKFDPKNAHAAQGIAIILAQNRQFSKALLILSKVREAIKDATTLINIGNCLAELKQFSRAIEVFETVYSSTGESDTYGVLSCLGRVWLQRGRESKNVDYLKESVRYATLALEKNPENPSLLFNVAFVQFQLCELIRQKPENSRTVEDLNFAMQQLDASIETFTKLVSVEHPPYSPTSIEQRAKMAKNTTKRQLERAIQAQIEYEKSVAAKLEDARIQREKEKARRLAEEEALLKEKQERERQLQEERQKMQEEVLEWRKSQQKASEDDMSLSDDEEKQSGKKKKKDRKKRKSKSKQESSDSGVSEDDEIPLSDARNKTKKRRVNRRVISEEYTFDQDSDAEGNQEEEVSRTIEEKQDNDITDNQDDNKELNLFSEEDEE O42699 RL19B_SCHPO SPCC1682.14; CHAIN 2..193; /note="Large ribosomal subunit protein eL19B"; /id="PRO_0000347281" MANLRTQKRLAASVLKCGKRKVWMDPNEISEISNANSRQNIRKLVKDGLVIRKPNLMHSRFRIRKTHAAKRLGRHTGYGKRKGTAEARMPSTVVWMRRQRVLRRLLRKYRESGKIDKHLYHTLYLEAKGNTFKHKRALIEHIQRAKAEANRTKLIQEQQDARRARAKAARQRRAKAVEEKREQIYTAAEKIEE O42700 TAL1_SCHPO ACT_SITE 132; /note="Schiff-base intermediate with substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2; MOD_RES 268; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1020.06c; CHAIN 1..322; /note="Transaldolase"; /id="PRO_0000173573" MSSLEQLKATGTVVVSDTGDFESIAKYKPQDATTNPSLILAASKKPQYAALVDAAVDYAKAKGGSINSQIEIAFDRLLIEFGTKILAIVPGRVSTEVDARYSFDTQTTIEKARHLIKLYEAEGIGRERVLIKIASTYEGIQAAKQLEEEGIHCNLTLLFSFVQAVACAEANVTLISPFVGRILDFYKAKNNRDYTAQEDPGVVSVSNIFNYYKKFGYKTIVMGASFRNVGEIKELAGVDFLTISPALLEQLNNSTDAVPKKLDASKASSLNLEKVSYLTDEPKFRFDFNNDEMAVVKLSTGIAAFAKDADTLRTILKAKLEA O42706 RL21B_SCHPO SPAC959.08; CHAIN 1..160; /note="Large ribosomal subunit protein eL21B"; /id="PRO_0000149681" MPHSYGIRARTRYTFQRGFREHGQIRLSTYLKTYKVGDIVDIKVNGAVQKGMPHKYYHGKTGVVYNVTQSSVGVLIYKVVGNRYMEKRVNVRIEHVKHSKCRQDFLDRVKANEAKRKEAKAQGKTVQLRRQPAPPATAHFVSTENNEPVTLHPVAYDTTI O42707 YOC5_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPBC4F6.05c; CHAIN 20..384; /note="L-type lectin-like domain-containing protein C4F6.05c"; /evidence="ECO:0000255"; /id="PRO_0000316861" MKFCSLFHVLSFCCTLAYAVPKSQFLQLHSLSNAIPVEWKWYGSVDEDSGYVYLTSKDSNEARSGSLWSTSVLRQVGWQLSTSFVAHVSENENTFFAIWYTSAVGSEGPVFGASDKWDGLLISQEIDQTGKIFVRGYLNDKSFELAQFTDPDLPPFAKCTIESSPEALNNIILKYGDQSGLELFVNDKPCFQVKDVILPQGYYFGVSSQSTSAKDLVALSNLNILPPDTSNNENLNPTSNTKQSVGDNTSPQTVIDTEGLNAIKADLAKLFNLVESQRQKMDSLHFALTNALERLNDISSTSQFPSERFNALEKLLHDSLSAQSSTADGTSKHLAEFEKEIKKAMGNAYSPYNLTNFMVFLLLGAIVSYGIMLVRRDRRRHKYL O42846 RL34A_SCHPO SPAC23A1.08c; STRAND 8..10; /evidence="ECO:0007829|PDB:8ETC"; STRAND 21..24; /evidence="ECO:0007829|PDB:8ETC"; STRAND 30..33; /evidence="ECO:0007829|PDB:8ETC"; STRAND 52..54; /evidence="ECO:0007829|PDB:8ETC" HELIX 59..62; /evidence="ECO:0007829|PDB:8ETC"; HELIX 67..70; /evidence="ECO:0007829|PDB:8ETC"; HELIX 82..106; /evidence="ECO:0007829|PDB:8ETC" TURN 45..47; /evidence="ECO:0007829|PDB:8ETC"; TURN 75..79; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..112; /note="Large ribosomal subunit protein eL34A"; /id="PRO_0000131843" MAQRVTYRRRLAYNTRSNRTRIIKTPGNNIRYLHIKKLGTIPRCGDTGVPLQGIPALRPREFARLSHNKKTVQRAYGGCLSANAVKDRIVRAFLIEEQKIVKQKLKQLSSQK O42847 YFH9_SCHPO SPAC23A1.09; CHAIN 1..121; /note="Uncharacterized RNA-binding protein C23A1.09"; /id="PRO_0000310810" MRPAKSVEGYIIIVTGVHPEATEEQVEDLFADFGPVKNLHLNLDRRTGYVKGYALIEYATLEQAQKAVDEKNLSLLDEKLEVDFAFLEPPERAPRPSISTRSRSQSPEVQHRDRDVAMAEP O42849 SYFB_SCHPO BINDING 346; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="shared with alpha subunit"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"; BINDING 352; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="shared with alpha subunit"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"; BINDING 355; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="shared with alpha subunit"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"; BINDING 356; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="shared with alpha subunit"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00816" CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A5K464}; SPAC23A1.12c; CHAIN 1..589; /note="Phenylalanine--tRNA ligase beta subunit"; /id="PRO_0000127022" MPTISCDKEELYKALGREYTTQEFDELCFQFGIELDEDTTNDPERSPSERPSLKIDIPANRYDMLCLEGIAQALNVFNRRMATPQYKLLPSTTSLTISPETSEIRPYAAAAILRGVKLDPIRYQSFIALQDKLHANLCRNRTLVAIGTHDFSVMEGPFTYEALKPEEINFVPLNQTQEINGSNLLEFYKDSKHLSRYLHIIANSPRYPVILDAKRRVCSLPPIINSEFSKISVDTRDIFIDVTATDKTKLEIVVNMMTTMFSCYCEEPFTIEPVNIISEHNGCTRVTPNLNPTCFKADIDYLNEACGLSLPEDEICHLLTRMMLTAKPNPNDSKTLLVYVPPLRADILHQCDIMEDLGIAYGYDNLKHTYPAHSVTFGKPFEVNRLADIIRNEVAYAGWSEVMPFILCSHDENYAWLRKTDDSKAVQLANPKTLEFQVVRSSLLPGILKTVRENKNHALPIKIFEVSDVAFCDYSRERMTRNERHLCAIFAGLNSGFEQIHGLLDRVMLMLNTKRIMNPKDSDAVGYWIEAEDDSTFFPGRCAAVYYRKDFGTAGIRVGVFGVLHPLVLEKFELTSAASAVEIDLTLWV O42852 SEC20_SCHPO MOD_RES 97; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23A1.15c; CHAIN 1..226; /note="Protein transport protein sec20"; /id="PRO_0000232410" MADVLNALEEKVVELQQSESVEVIKRHFREFRKIWETARVELEYSSIQLDSVLRYEKAVQEYIRLNRRYRNKIASGEPWLPIAQEIGKIVDEEEITSPSDGSLQKRSMDNSGSWQSDDIYLTSASQVTAAMRDIHAQMVQAVDMSAENAMELSSSTNLLETLQEKYFGVEDVLYTSKRIIKSLKLSDRSDYFLVVSGFGFFIFVVVYLLFKRIVWPILSMFLWFLR O42853 RPAP2_SCHPO BINDING 83; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"; BINDING 88; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"; BINDING 115; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"; BINDING 119; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00812" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; SPAC23A1.16c; CHAIN 1..197; /note="Putative RNA polymerase II subunit B1 CTD phosphatase rtr1"; /id="PRO_0000317210" MNKKSILKKPKNAQSTQEKQLITWSKSLIDEARSRLQYDFFALEWIEKLVDPVSLETLEEARKYLRKSDYDQVVKERKLVNLCGYPVCPYEPKQQTRYKLEDSGMKVYGGLNYYCSKDCFLKSCQYMVELSDEPLWIREDAREAMKQHLDPRQDEAFRKELENKKIEDVRLLLQALPVGYKAKVGEIVEHPLANEQS O42854 YFHH_SCHPO MOD_RES 1258; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1261; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1266; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1379; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1380; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23A1.17; CHAIN 1..1611; /note="SH3 domain-containing protein C23A1.17"; /id="PRO_0000303941" MSSFPTRVVALYPYRSSFSDDLEFDPGQVIDVVSNLDGDWYTGTYVDSDGNRKIGSFPKDFTEPAEDAVFVERASEMALHQPTPTSAVHSRNSSLGYAPSITRSIKSISNNTEHLGADTESYLSANDFIDSTSEALTKIVDVDTLSAPFGNDSNSRPHSLKNVEKLHTFSAPYTISEETPSCSTENDSLPLTATHTITGGEDAATGAAVTNTTTTHITTSTNTSTVIPSNPNSVFLVDCTHSQCPTDLPNIATTQHSLRYLDNASASAITVLERTHPAASSTMATESSHQSPSADSQAEELSKSQRVAKDDDPFVVSNTANSDEPASSSKPAKPLTDLNRAFSQRLNLDPQKPGKSQGEISEQEEDEYDDAESDEMHSPYSTHEPESEPEDQDEPSEKDDENKDVEEEQEQEQEEEQIDPEEAKRIALRERMAKMSGGIGMHVFGLPGLAAPIGRKNTLRRTPAKSSEEAKSTTNDSSPPKDSSSTSTQPTEQSNAQQAPSPKEEERPLPSEPSQNQPAEYRDTPDTPRNIMPLPGLMSADQPIKVTEPSNDADKAIVAEGPNNEEETKGPVIPETQETSEQQVHKTPSPEKQKVLSPPPIITNFDKETLASNEAHEAVPQKPSAPQVTRLMAPQDSSSVVTPSPTSLLDPARAVRKVIDGIDPPKEAGAGATADVESAANSPITPPRTWHSPDFTSKSFEPIERKLPSRISEVTEDSIDEDKQNEVDPSTSARALPPPGLRFGKVDTLASLAHDDLDDLPAVPRIFSPPPLPKTPSGEFGDNEFMFPKKSNRVRGHQSRPSTGSQLRNVVPVSIVTSGGRPALPDEMASPSSSIGHPLPSPPPADFNSLNVDFYEPHSYLESPAPEPQPSYEEESFNATVIHAPTPSTATFQGHPTISNVATPPLKQDVTESKASPVADASATHQSSTGLTQEITQLGSNMRLPTKLTRPSNDGRKASGPRPAAPPSIPPPLPVSNILSSPTSEPPKDHPPSAPLSKPVSTSPAAPLARVPPVPKLSSKAPPVPLPSADAPPIPVPSTAPPVPIPTSTPPVPKSSSGAPSAPPPVPAPSSEIPSIPAPSGAPPVPAPSGIPPVPKPSVAAPPVPKPSVAVPPVPAPSGAPPVPKPSVAAPPVPVPSGAPPVPKPSVAAPPVPAPSGAPPVPKPSVAAPPVPAPSSGIPPVPKPAAGVPPVPPPSEAPPVPKPSVGVPPVPPPSTAPPVPTPSAGLPPVPVPTAKAPPVPAPSSEAPSVSTPRSSVPSPHSNASPSPTSSSMASAAPARTSVSRSKSKAERHETSTSSRKSSKSGEHHHHHNEGHADSSSTRTSLAHQDSRKSLHRHLSRSSSRASKKPSIVSTTGPFNESFSAKPVEPCASEKWWLNSTAVPKSVVQMNDSVLYMIKEGITGQDKKYKSVHILFPDYSQTVLTATFNPHNQNITQLSQLQLAPPAQPSKARLDEEYACYGSTILKKARAYQGSMVGDGSAFTFVNSVMSILAHNLEPINKQTFGGVIYKNVGNVTVQQIGEIRPGDIVTFDKAKFSGQKGTLRSKYSLEVGKPMHYGIISEWDVSKLKIRVLEQGRESKKVSVASYKFGDLKSGEVTVWRVMRRSWLGWN O42857 NPR2_SCHPO SPAC23H3.03c; CHAIN 1..409; /note="Nitrogen permease regulator 2 homolog"; /id="PRO_0000339459" MEYSEEGWMDQADSFPPRLLAIFFALFDPLQGPIVACEAPAGSVTNVDGGKNCLLPFETISDYVIPKRELCNKTITVCTNHYQVIGHPISIIGSNYERNALIFNMCMIFHEEEDSACYIPLVKRLARNLEVLEKQIHYISDLNKRPVIFSVIEQILEDMNNFCECMIQLDDQNSINIKLFPVFPSPPTVKSFHVPILTAQLDLLMDKNWDMTVQKVYPFINGINSVQRIAELANVSYRSCQKCMEHFLYYGCLIIADIFQFHNIYAMTTNAPNLLQDPDFQRECTAYVSTNSSNAKNVTFATIFKLYCSLRQGLRVKDWMNENKEIFKGLDVRRLISFGTIKGLIYRVHKYPYLERRTMRNNLTEEEKKLLGLLDGKHHFDELCVTLKKSPKVVNEMIAGLGDACFIYV O42858 SWD1_SCHPO SPAC23H3.05c; CHAIN 1..398; /note="Set1 complex component swd1"; /id="PRO_0000051250" MNLELLDPFSIPDYPEALTTTLKHGHATSIRFSTNGYHLASGLVNGSVVIWDLSTFSVSRVLTGHTRAIQSVCWSSCDRFLLTASRDWKCILWDLRDGSIVYQVVLSAPVWSASLHPHKINTFVASLLDESPQLIIVDDGIPKHKYLPTNPDIDENYSDRRNRSKHVTLVSFFHPSGEYILSGTSKGWFHVIDASTTKIRSSHRITSQSIKQIRLSFCKRFLIFNSTDRVIRTVSIQDLDNPEVEHKFQDVVNRLQWNSCGFSQTGEFVFATTYQMAHAIYVWERGMGSLVKILEGPKEELVDVDWHPVFPCVASVGLDSGSIYIWAVEQKESWSAFAPDFQELEENIEYEEPEDEFDIHDETGKSEEEEYFTSVVKILPHDSSAEQPFVMPPTLSSS O42866 FABG_SCHPO ACT_SITE 137; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 151; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 155; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 13; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 34; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 115; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 151; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 155; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 184; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 186; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; SPAC3G9.02; CHAIN 1..236; /note="3-oxoacyl-[acyl-carrier-protein] reductase"; /id="PRO_0000374026" MRKVLITGGSSGLGKRIAQIWSQKGHQCHIVGRNEFHLKETLQSLSVAKGQQHTLTIADVQSDMKNLKSIFESVEIDTVVHAAGVLQSSLCVRTSEKEIDSIICTNLVSAIKLSKMAILEWFRNKNSERDRLILNISSRLSTYALPGTSVYAASKAGLESFTKVLAAEVASKGIRVNAISPGYVDTPMLSSQIRAIAEKKVPIGRLASTDEIVDACTFLLDNRYTTGTILPITGGL O42870 SYFA_SCHPO BINDING 330; /ligand="L-phenylalanine"; /ligand_id="ChEBI:CHEBI:58095"; /evidence="ECO:0000250|UniProtKB:Q9Y285"; BINDING 372..374; /ligand="L-phenylalanine"; /ligand_id="ChEBI:CHEBI:58095"; /evidence="ECO:0000250|UniProtKB:Q9Y285"; BINDING 412; /ligand="L-phenylalanine"; /ligand_id="ChEBI:CHEBI:58095"; /evidence="ECO:0000250|UniProtKB:Q9Y285"; BINDING 414; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="shared with beta subunit"; /evidence="ECO:0000250|UniProtKB:A5K9S0"; BINDING 438; /ligand="L-phenylalanine"; /ligand_id="ChEBI:CHEBI:58095"; /evidence="ECO:0000250|UniProtKB:Q9Y285" CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A5K9S0}; SPAC3G9.06; CHAIN 1..499; /note="Phenylalanine--tRNA ligase alpha subunit"; /id="PRO_0000126827" MSKLEALQVFLLEKLNEKNEIPNTSHLEFDGKKLGPQEAQSAILSLAAKNMIEFSRHEIEIYNLTAEGENICANGSHEAKVYNEICASMSGLNIGELKKKLGNSAGIGQGRAFKLGWIKKDGDKLVKNTDSITDETPKVLSEIKEHGTISDSKTLTDLKKRKLVERNKIMYFSLRKGPNFSLQIEKLNTDLTAEMITSRSWESAKFKSYNFAAEGIPPAGGCLHPLMKVREEFRKFFFELGFEEMPTNNFVESGFWNFDALFVPQQHSARDAQDTFFLKVPASTDKLPDPEYVARVKATHENGGETKGIGYRAPFSLEETRKLVLRTHTTAVSANMLYKLAQNGFHPAKYFSIDRVFRNETVDATHLAEFHQVEGVICDRNITLGDLIGFLEVFFGKMNVKNLRFKPAYNPYTEPSLEVFSYHEKLGKWVEVGNSGMFRPEMLEPMGLPKDVRCLGFGLSLERPTMIKYGVADIRQLIGPKVNLDLIEASPAVRLDKEE O42873 PDC4_SCHPO BINDING 30; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 119; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 396; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 419..421; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 451; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 452..453; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 478..483; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 478; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 480; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 484; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P06169" CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2; Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1; CATALYTIC ACTIVITY: Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06169}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P06169}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|UniProtKB:P06169}; SPAC3G9.11c; CHAIN 1..570; /note="Putative pyruvate decarboxylase C3G9.11c"; /id="PRO_0000316039" MSSEKVLVGEYLFTRLLQLGIKSILGVPGDFNLALLDLIEKVGDETFRWVGNENELNGAYAADAYARVKGISAIVTTFGVGELSALNGFAGAYSERIPVVHIVGVPNTKAQATRPLLHHTLGNGDFKVFQRMSSELSADVAFLDSGDSAGRLIDNLLETCVRTSRPVYLAVPSDAGYFYTDASPLKTPLVFPVPENNKEIEHEVVSEILELIEKSKNPSILVDACVSRFHIQQETQDFIDATHFPTYVTPMGKTAINESSPYFDGVYIGSLTEPSIKERAESTDLLLIIGGLRSDFNSGTFTYATPASQTIEFHSDYTKIRSGVYEGISMKHLLPKLTAAIDKKSVQAKARPVHFEPPKAVAAEGYAEGTITHKWFWPTFASFLRESDVVTTETGTSNFGILDCIFPKGCQNLSQVLWGSIGWSVGAMFGATLGIKDSDAPHRRSILIVGDGSLHLTVQEISATIRNGLTPIIFVINNKGYTIERLIHGLHAVYNDINTEWDYQNLLKGYGAKNSRSYNIHSEKELLDLFKDEEFGKADVIQLVEVHMPVLDAPRVLIEQAKLTASLNKQ O42875 SYWM_SCHPO BINDING 21; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9UGM6"; BINDING 27..30; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9UGM6"; BINDING 165; /ligand="L-tryptophan"; /ligand_id="ChEBI:CHEBI:57912"; /evidence="ECO:0000250|UniProtKB:Q9UGM6"; BINDING 177..179; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9UGM6"; BINDING 225..229; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9UGM6"; BINDING 228; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04803" CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; Evidence={ECO:0000250|UniProtKB:P04803}; TRANSIT 1..16; /note="Mitochondrion"; /evidence="ECO:0000250" SPAC3G9.13c; CHAIN 17..361; /note="Tryptophan--tRNA ligase, mitochondrial"; /id="PRO_0000314631" MAKLPKITSLLPHSRVVSGIQPTGIPHIGNYLGSLKQWVQLQEEAARTPFSKCFFFVADLHALTVPQDPLKFRQARLDMLAALLAIGINPQKSTLFFQSDVAQHSELAWLLACSTSMGQLNRMTQWKSKLHLHDHDDLSFLDASATSSTRFNLGLFSYPVLQAADILLYGATHIPVGKDQSQHVELTRSIARSFNSSYKEKILTVPDIILNSSSSIMALCQPEKKMSKSDINSKNYILLSDSTGEIRKKISRAQTDNIKGITYGDSNRPGINNLINIFAAISDSTPSDIAQANASCSNAEFKEKVSSAIIRCLQPISTSFNEWRQNRELLRDIAKKGAEEAVAEASSCMHKLKTLTGLSVY O42878 INVX_SCHPO ACT_SITE 18; /evidence="ECO:0000255|PROSITE-ProRule:PRU10067" BINDING 15..18; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 34; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 75..76; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 149..150; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 202; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 288; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000255|PROSITE-ProRule:PRU10067}; SPAC8E11.01c; CHAIN 1..508; /note="Putative invertase"; /id="PRO_0000169868" MPVRPCIHFTPPEGFMNDPNGLVYSNGKWHLFFQWNPTGNQAGNQHWGHAVSKNLYKWKLLPTALAPGDDHGLMFSGSAVIDKTNSSGFFESGFFSRKSVDPEERIVLIYTTHYDNRETQNIAYSLDGGITFIKYKKNPILDIKESQFRDPKVFWHEESRAWIMVVVLAQKYKVLFYHSLNLRDWVKLSEFGSAGVLGYQYECPDFVRLPIEGTDEFRWVLIVSINPGSSINGGSMVQYFIGDFDGQTFTPIDSASRILDCGHDCYATQTFGNAPDGRVISISWASNWNYTNDVPMRMKHRGMFTIPRELTLCYTHLNQETRGLVLRQRPVNLHHLYYPDSLPAPLLLNRVCEFPTVWTSATVFYLAVSIPKSIVLESPMEFLCLTWSTTPDVETSKEYFELGYRFHDGAVYVERGVCSSSWKYPLYPERCTSSVPPSSYEDNYILEIEAVVDHSIIEVYLQGGIMCLTNAYYFKGDEPLQYYYLRVPTGASLAKSGMQPLLNNRPHS O42881 APTH1_SCHPO ACT_SITE 116; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 170; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 203; /note="Charge relay system"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniProtKB:Q12354}; SPAC8E11.04c; CHAIN 1..224; /note="Acyl-protein thioesterase 1"; /id="PRO_0000316195" MTAKLNSVIINPSVAHTATVIFLHGLGDSGQGWSFMANTWSNFKHIKWIFPNAPSIPVTVNNGMKMPAWYDIYSFADMKREDENGILRSAGQLHELIDAELALGIPSDRILIGGFSQGCMVSLYAGLTYPKRLAGIMGHSGFLPLASKFPSALSRVAKEIPILLTYMTEDPIVPSVLSSASAKYLINNLQLKCLDRPFEGDAHSLSSESFMAMYKFTQTVIGSP O42885 YBN1_SCHPO MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 14; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 292; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC8E4.01c; CHAIN 1..572; /note="Putative inorganic phosphate transporter C8E4.01c"; /id="PRO_0000050479" MAFGSKILNIGSKSDEYNDDAVPLDQVEEGAQERRYYLGLTKREFKLMMLAGVGFFLDSYDLFIINLVTPIFEYLYWGGIEKGPTGKGHYPSGIRGLVNASANIGNIFGQLLFGFMGDFFGRKFVYGKEMVIVIIATVLVIAMPKSIHSPLSKMMWVFCWRWLLGVGIGGDYPMSAAITSERSKIKRRGTLISLIFAFQGFGTLAGAIVTIILLGCFEHPLNREGHYHKLEGVWRLQFGLALVPAIGVLIPRLIMKESKSYENSKALNSAEGKDPKAFFNTDDEDNMKKSSSHGDSEVVEASDRYANQADAADAEVDNIEKQFAAVTTPENSSGFITYFRQWRHFKHLLGTSVCWFLLDIAFYGVNLNQSVILKNIGFSTGTNEYRTLMKNAIGNLIIAVAGYVPGYWFNVFLVEILGRKWIQLQGFVITGLMFAILAGRWNEISTGGRFACFVIAQLFSNFGPNSTTFIYPAEVFPARVRGTAHGVSAALGKCGAILASLLFNFLTGVIGYGNVMWIFCGCMWGGILFTLLLPETKGRDADEIDRLELFYGKDGKVQCDSKWKSWYFNGIF O42887 SPEB2_SCHPO BINDING 206; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 229; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 229; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 231; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 233; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 331; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 331; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 333; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" CATALYTIC ACTIVITY: Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145, ChEBI:CHEBI:326268; EC=3.5.3.11; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; SIGNAL 1..22; /evidence="ECO:0000255" SPBC8E4.03; CHAIN 23..413; /note="Putative agmatinase 2"; /id="PRO_0000002092" MFTYQKIIQLALLLSGVCGALASIDTDSHLSPKVLEKLRPTENLAYEDDSLDDDTWRSKRWEFDYQYSGISTFAHLPHVRCLVEQSEDFDIAIIGVPFDTAVSHRPGARFGPKGIRSASSRQMAIRGFNPSLNVNPYESWAKILDCGDIPVSSYDNQLAVRQMTEGYIDLLSRKATASPASNNLKTAGLAKDGIFHPRLITLGGDHSIGLASLRALGHFYGNVSVIHFDSHLDTWNPKRYYPSYWHSDRADFTHGTMFWMASKEGLINNGTSIHAGLRTRLSGTDYYDYEEDNRVGFTFIEAQEIDEIGVNGIVERIKQVVGDTLVYLSIDIDVVDPGLAPGTGTPETGGWTTREMKSILRKLDGHLNLVGAEVVEVSPPYDDRAESTSLAASDFIFEILSSMVKHPLYDVKK O42897 RPN3_SCHPO SPBC119.01; CHAIN 1..497; /note="Probable 26S proteasome regulatory subunit rpn3"; /id="PRO_0000173826" MIDDQRDMQVDSVNQEENVDSGETKQNTVTEVPRTVLQDVEANIAALMQATKQRDPRLVYRSLRTTSNICHRLNADVLGQLIKKYYSFDNSLKNELLELIDMPQNGDDSSTSITNGNGNTIFPEVDMYLQLLLSMTLYYNEKYEVGAEYIKKVIARLQSYDRRTLDQIAAKLYFYYILFFEKCNRSVECRNTLLSVHRTASLRHDSETQAMVLTLLLRNYIQFNLYDQADRLVSKTSFLTNASNNLAIRYQYYLGRIRAIQLDYTTAHEHLVSAIRKAPNTVYAVQFLEAVYKLHIVVQLLMGEIPERRIFRQKSLEKTLVPYLRISQAVRIGDLCAFTDALSKYEAEFRFDGLYTLICRLRHTVIKTGLRMISLSYSRISLRDVCIKLGLDSEESAEYIVAKGIRDGVIDASIDHSNAFMASNEAMDIYSTEQPQQAFHERIQFCLALHNDSIKSMRYPMDAHKSELEGVEEARRRMDKEMAEADLDDDEPDLGEF O42898 COMT1_SCHPO BINDING 56; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 78; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 86; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 106; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 107; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 135; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 162; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 162; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 165; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 190; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 191; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 191; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; SPBC119.03; STRAND 74..79; /evidence="ECO:0007829|PDB:5ZY6"; STRAND 101..107; /evidence="ECO:0007829|PDB:5ZY6"; STRAND 128..133; /evidence="ECO:0007829|PDB:5ZY6"; STRAND 157..161; /evidence="ECO:0007829|PDB:5ZY6"; STRAND 186..189; /evidence="ECO:0007829|PDB:5ZY6"; STRAND 232..240; /evidence="ECO:0007829|PDB:5ZY6"; STRAND 253..262; /evidence="ECO:0007829|PDB:5ZY6" HELIX 11..20; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 24..30; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 34..43; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 58..71; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 85..95; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 109..121; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 135..147; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 165..167; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 168..177; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 192..196; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 198..203; /evidence="ECO:0007829|PDB:5ZY6"; HELIX 208..217; /evidence="ECO:0007829|PDB:5ZY6" TURN 125..127; /evidence="ECO:0007829|PDB:5ZY6" CHAIN 1..266; /note="Probable catechol O-methyltransferase 1"; /id="PRO_0000318148" MPHMEDNGSEKEQLFLQHIQNLPQERLDAIRGHPELVLKEIDEFTYPDGSGVRMCIGDVKGGFIVGKIRERKPKIMVELGGYLGYSAILFGNEISKIPGGRYYSLEVNEDYAKIAYELVKLAGLDEIVTIMIGKACDSLVELQQKLLHKDLGFQALDMVFIDHWKDLYVPDLRVIESLNMIAPGTLLVADNIITPGAPEYHKYVNMSPEERRGYQAKVRNVNGFDFIGRWDLIYKTETKEFEGVIRNKHRKDAVDVTECVGYAKKD O42906 GPN1_SCHPO BINDING 15..22; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9"; BINDING 18..23; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9"; BINDING 178..181; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9" MOD_RES 311; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC119.15; CHAIN 1..367; /note="GPN-loop GTPase 1"; /id="PRO_0000315977" MTDKEKKPCAIIVVGMAGSGKTTFMQQLNAHLHSKNKPPYILNLDPAVRNLPYEANIDIRDTINYKEVMKQYNLGPNGGIMTSLNLFVTKFDQVLKILEKRAPTVDHILIDTPGQIEIFQWSASGSIICDTLASSWPTCIAYVVDTPRATSTSTWMSSMLYACSMLYKAKLPLIIVYNKCDVQDSEFAKKWMTDFEEFQQAVTKDEGMSSEGATSGYMGSLVNSMSLMLEEFYRHLDFVSCSSVTGEGMDDFLEAVKAKVKEYEEEYVPEMERMKEIQRQTKERQKEAQLSKLMKDMHVSKDKEDVGLTVSDAEDEYNGELVDPDEDDGLTAEDREDMIKQYRVALGISDDISDEKLLEMLTERMKQ O42908 PREP_SCHPO ACT_SITE 94; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q5JRX3"; ACT_SITE 167; /evidence="ECO:0000250|UniProtKB:Q9LJL3" BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q5JRX3"; BINDING 95; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q5JRX3"; BINDING 192; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q5JRX3" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q5JRX3}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q5JRX3}; TRANSIT 1..30; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC119.17; CHAIN 31..992; /note="Presequence protease, mitochondrial"; /id="PRO_0000178015" MNYAKLSIAFSKKTIKTHNCRLFQRWLHVGDKVHDFRVVDTKKVPELQLNYTRLKHEPTNADMIHLDREDPNSVFSIGFQTPAENDEGIPHILEHTTLCGSNKYPVRDPFFKMLNRSLATFMNAFTASDFTFYPFATVNTTDYKNLRDVYLDATLFPKLRKLDFLQEGWRFEHADVNDKKSPIIFNGVVYNEMKGQVSDSSYIFYMLFQQHLFQGTAYGFNSGGDPLAIPDLKYEELVKFHRSHYHPSNAKILSYGSFPLEDNLSALSETFRPFSKRELNLPNTFLKEFDQEKRVVEYGPLDPVMAPGRQVKTSISFLANDTSNVYETFALKVLSKLCFDGFSSPFYKALIESGLGTDFAPNSGYDSTTKRGIFSVGLEGASEESLAKIENLVYSIFNDLALKGFENEKLEAILHQMEISLKHKSAHFGIGLAQSLPFNWFNGADPADWLSFNKQIEWLKQKNSDGKLFQKLIKKYILENKSRFVFTMLPSSTFPQRLQEAEAKKLQERTSKLTDEDIAEIEKTSVKLLEAQSTPADTSCLPTLSVSDIPETIDETKLKFLDIAGMKAQWYDLAAGLTYIRLLLPLKNFPESLIPYLPVYCDACLNLGTHSESIGDLEHQIRRYTGGISISPSAVTNNSDVSKYELGIAISGYALDKNVGKLVELINKAFWNTNLSNTDKLAIMLKTSVSGITDGIAEKGHSFAKVSSASGLTEKTSITEQLGGLTQVKLLSQLSREESFGPLVEKLTAIREILRGTSGFKAAINASPTQHEVVEKALQKFMKSRGVNQQTQTKSTSKERNGINSIKTYHELPFQTYFAAKSCLGVPYTHPDGAPLQILSSLLTHKYLHGEIREKGGAYGAGLSYSGIDGVLSFFTYRDSDPIRSLSVFDEASEWATTHEFSQRDIDEAKLAVFQGIDSPVSESQKGMLYFVDGVTDEMLQNRRKQLLNVSANDLKAVAKKYLVNPKKSYTAVLGPKSEKQLPTWVIDKFES O42910 PPR7_SCHPO TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC16A3.03c; CHAIN 30..658; /note="Pentatricopeptide repeat-containing protein 7, mitochondrial"; /id="PRO_0000116511" MRNCVSPLLFAWTKHLRLREFKIPFPNRLVVRSLNQLSVHHEKVTGCRPRQASSDELHKYSKSASNEAFLSSFAENQLFHKCLPSSAGAVLSENDLMYIIRKVSEVYADNKTEKVTVPFDKHKNPFLIYVKKRFAECFDKNPDLCLIVYSKLEVETLAKITPIWINVAKKNKKEDFLVELCLRFLERFRSCNLTEQAILYQNFRENWWSNIKLPQNLKSLYVELCLVYHFHNSHLGMDSSTVSNLKRFCFSESLGHIFAPLRFQNQQLPLQHVYAFLFSIAYRDNQVDTAHFLYKQWSRAGMGPLPKDAFIKFVQLLSKNRNWVLMRDIVQLEEYNSYLLDHRIVSAFLKPLSEKGNYKDILSLISVWQHSVWRPSLAYLQVVYSFSMRALLVNRQYSSAFAFFWKIDPYIRNERLVSQMLQAASQLHYHDLILYVINTYYSGNIMKNLGNKDLICITQSSPPCNISGIKPGSLKLSPTTNTVLAKSICYWLNDAMALLFLLENQLNCKHSLFQRKSLIILLNGILNCPHSSYDLQFRAVSLLTGRIRLNVDFEVSVLASQLVFFVKHRDFKRTLITMKAISKLQKNFDVRIWNYWLVALIQQKLYSRAVKVYSKLICSSAVRNDTTRSLIRLIPKSYFKSYPLLKESETEKKTNSAL O42912 TAD1_SCHPO ACT_SITE 91; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00240" BINDING 89; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"; BINDING 96; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250"; BINDING 144; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"; BINDING 201; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"; BINDING 204; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250"; BINDING 357; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250"; BINDING 363; /ligand="1D-myo-inositol hexakisphosphate"; /ligand_id="ChEBI:CHEBI:58130"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855, Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34; Evidence={ECO:0000305}; COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250}; Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; SPBC16A3.06; CHAIN 1..388; /note="tRNA-specific adenosine deaminase 1"; /id="PRO_0000316215" MEEFTLDRNSNVGNLIALAVLNKFDELARHGKPIIRANGVREWTTLAGVVIQKKMENEFICVCLATGVKCTPAGIIKNEQLGSVLHDCHAEILALRCFNRLLLEHCILIKESKKDTWLLEVADNGKFTLNSNLLIHLYVSECPCGDASMELLASRLENNKPWNLTVDSEKLMRGRADFGLLGIVRTKPGRPDAPVSWSKSCTDKLAAKQYLSILNSQTSLICEPIYLSCVVLYKKVIVKSAIDRAFGPFGRCAPLAEFGEKDNPYYFHPFTVLETDENFLYSRPLNQAEKTATSTNVLIWIGDKMQCTQVIHNGIKAGTKAKDVEKSQTLICRKSMMNLLHQLSQSLTNEKNYYEWKKLNIKRCQQKQILRNILKNWIPNGGNEFQWI O42915 UFD1_SCHPO SPBC16A3.09c; CHAIN 1..342; /note="Ubiquitin fusion degradation protein 1"; /id="PRO_0000194988" MFGGSFFSSDDDGFSMMSQLRSAFHNNVNQRFDTRYRCYPVAMIPGEERPNVNYGGKVILPPSALEKLSRLNVSYPMLFDFENEAAEKKTHGGVLEFIAEEGRVYLPYWMMTTLSLEPGDLVRVINTDIAQGSYVKLQPQSVNFLDITDHRAVLENALRNFSTLTKSDIFEILYNDQVYQIKVIDVQPDDSRHVVSVVETDLVVDFDPPIGYEESLQKNKQQNIAGVQGTMVTKIGYDELVRQGDSNLMKGTGTKLNGKEVAEVPKINLLDVEKQECPAPLILPLGTYFFGYPYKAPSIEEDSKKDPNLFKFEGAGTSLRASRKTNGTMGKGSSDDPIDIDA O42924 EAF7_SCHPO MOD_RES 193; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 201; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16A3.19; CHAIN 1..272; /note="Probable chromatin modification-related protein eaf7"; /id="PRO_0000310359" MSSRGTRSSTAAEQKRQEDVNKESNMNDSVTEWSVLEETLLLKAICRGLRPVGIEKNFYMIGILREIRDGCKRSTIKAQDVWNKLGTLYNLKEFEELEAPGNEEVKAKEKRIKSPDVKDFKLPKDILKVKEKSEKPLETSQKVEIETVETKPGEPEVKQETNLQKEKKESKVKLESKEEKISRNLRSSSRSISPVTEQPQSPKIQPVIPEKKEKSEKKESSMTLRKRSVSPSSQNTARSPKRMATEPIEPASSPAASNQAIRRSSRSRRPPT O42926 VP13B_SCHPO SPBC16C6.02c; CHAIN 1..3131; /note="Intermembrane lipid transfer protein vps1302"; /id="PRO_0000065879" MLEGLLANFLNRLLGEYIENFDATQLKVAVWNGDVTLRNLQLKRSAFRKLELPISVQYGLVEELTLKIPWSSLKNKPVEIYIVGIRALASMEENVKSQSEVDPHQVLESKRRQMQLWEASQIGKAETAYDPKTQTFTESLITRMIDNIQINIRDIHIRFEHLPVSNVVPGGYSFGLLLSEFSIESCNEEWTSTFVETESQTIYKLCSLRGFGIYSDETAECIDKTDINELMNTFQALITDFQSREKDYIIAPVTGMAKVTINKLPTPEIPRFLSQISFRGFDVSLNDSQISCGMSLAHELQDVMSKLAFRKRIVGNVSLDTPLDYLRFIFQKTLHDIQQKHYARSWPAIKAFCEKRRNYIKLYKKKFLAVQLSADESKELDVLELNLDISQLKLFRSLAYQEIKNEGFEPQPPKQQGWGSWMWNSFRGASDENGEVTDDQRKTVIDAIGLNDSIIESAHVGDLQSNTSLFDVRLEVPSGKFSLLKYPKKENVISLELLNFFSQFKCNKKDYSFVANLGSLKMYNDDRNFLYPRETSNKEIETTSPSIFTLSFERSSSDDNDTDTLGINLRALEFFYDPNLLLRVKGFQSSLFANDNGRKLVRLANDAVTDFTSQTVQNLQEYLNEKRKLNVNFQFQTPLLIFPEDCNNPESFSLFVDAGFISITSQNVETNDKESNSESETLYHLIYDRYRVSLESARLLLGPLNELKNESNKINEEYYLMNELNTEIFIQAQRVPTPQYPRIKVEGNMPCLSFILSDAQFRILNNLASTMLKDGKASDDDDNGDWRPESSESLDSHESEYKLNNTPSEQSVKVSHFFEFNMKLGEVTLILCREDSQTKRNSMVSVNFAKLLLSFNQFEDNSHLRMSINSFHINDMLSKSSRDNNRQLMRCYAPDSVDAENTPVIVEIKSVKAGENQSETNTTVDFLCANGDFYLAKFSILTLIEFLPSFAPPPSNDKQSTPQVSNSAAGKMELNFKIHKIGLRLLENYESKPICIDLLALDLSVNSTKGISEVESRVDKIQVMAWDHEKDEIVTLIDSKQDSLFDLKCKMQEGWFIHSPNPSTDVNIKMGSFTMLCHKQPIEEILNYASNFGHYKAIVQSVKYLAETGTHQVQQGTNVNINLYISNPIFQIPLTLENGSSAMVEILPGSFSLKTPSWLPNLTLNLESKSTTLRTIYYSKDFDEKGNQITVLDDLNISLDGSIVQAVDSAITNYAIDLHCGISELLIHLSQAQYLILLKLASNLPEMLSIANAFSANVDAPSVMTLLSEELYSIDTVNDAISNLSQNSSFDMKFGLHFPKISLNLYDGTFITPENSLSPLSNFTLNEIRAEGSYDLKTGASALIKMASLAIEDVRSEKSRYFSNVIIPSTDTESQLQVSFQYKPDTSSILLEGDIFKSMYVLSLDHLLSIYYWFGQPLMEKKLESPDDVQSLQAESSVSTPAVTAASEKSISLSVRFDIRNTSLVFVADASKSTSQAIVLRTDQISLVKQLSYSLTVQKMGMFVTRMDKLDDGIQILDDFDIGFGLVQDCSENKSFSATLDLDRLLFRISVYDLLLLQSIAQASVSVISSYKDKSSSISENMNSGDYGQQILNASNIAAVQQKAEQTATTLLTVLGHDSLISEEFTINSAGIQLILISDAHCLPVFDFTIENFNVLVKDWSTNLSATTSLTLHCNAFNFAKSHWEPVIEPWTFSTTAIMKDGMHEVNINSDDIAQISLTPMMVTDVHRLIKFYLTNQENNIEKRPEGYPYVILNQTGYNLSIQYGNLNSSEMQSLSLPSGKCVPCRFESKEVLTSRMSSKVQDVATKVRVSFDSTWYPVDEVSVHQEGSFLYELKPRIDQRTFLLVTVVLLESNIKQIILSSPYSIVNRTKEVIEVVCNDRSGHRQSSVIKIDPNETGYVPLDLACLYPLRIRPVSKLGFLWSNQIVDWHSLNKSPLQYLTCESTSTSWKHNLLVFARNLMDGSLQNDYPFLQLNILPTLQIENLLPYEINLRIIERSSGNDWRSSLSPGDSLPILHTDSKSFLLMGINVPDLDLQPVDLPIIYTPISSGQDVQTSALLTASDKQDVVKLILKYEKLPGTNYVSKVMIYPPYVIFNHTDLSIQVTSSSPNSIRYTIPSGSYSNDIKPYFYSFDESGRKNRAMISIDNGTSWSADIGFDTLGSSSQVEVRKTNESDVCLLGMSISESSGKFCLTKSVTFTPRFVFKNHLDCTVSLREFGSSKVLHLPSNELIPMMYFSNPQEIALLLSLPSSNNHWTSPFLAQNVGIVHLKAFEFDDDDNNMSTTLLRLCVTLEDATFFVTITKEDKAWPFRLKNCTSREICYEQKRPDPESVDSRFLQGSRSMKYALNPGEEANYSWDFPILKSKLLQVEVGKAIHDLDISSVGQLEPWHPTELDQKIRIHPEVKVDSLTSLVTFNEIDLSKPKLPSRTNSNVKGSIVEQKFKLVLQLKGFGISLIDKKYEEFAYATLKNFTFRFDDSKDLNTFGMSLGWLQIDNQMLDSVYPIALFPTMITQEVKQDDPQLLQLRFSVLKDSSFNILYIKYASLLLQELSLEVEDRLVLTLLQLLYPSSDVSKDSASLSKNAFADKFEIPDLDADVYRSNVFFETLHLQPTRLNISFETSYESDQPAVKSSNPTLDFMTGILISTLGNIHDAPVQLNSILLENARGTLSEMANRVASHYKQQVGYQIYKIAGRADFLGNPVGLFNNVASGVFDMFYEPYQGFLLQDSQSFGDSFARGTSSFMRKTIYGVSDSVSKITGTISKGLSTMTMDPKYQNSRRRFRSRNRPKEAVYGVTAGANSFYDSMSSGFKGLKKPFTDPKNNSAGKFLKGFGKGMLGLATKPAIGLLDMTSNVSEGIRNSTDVRTNPEIDKVRVPRYVEFGGLIVPFKPYESLGKYMLSCLDDGKYAFDEYLYHAEIQNVDILYISTKHFIITGSNYIVKIAVPVKQISGLRVSEHDLNSSCLFTFAVFWQRCESLFDCEYLSTPNLELFVKEKKKPIMSITMSDSSAYGEELMRERFEHLLKAYEKMALMVAEQEEFNAKIEDMALKLLSEKYDNEAYQAELFYRLSNCVEKVLHNKISITDLKTEYEEILEQTLKKECKAYERSCIENVKLKKRTEQATAYYASSSSEP O42931 PRS7_SCHPO BINDING 220..227; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 90; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16C6.07c; CHAIN 1..438; /note="26S proteasome regulatory subunit 7 homolog"; /id="PRO_0000084718" MPPKEDWEKYQKPVDTEEENDKNPPPLDEGDIELLKSYATGPYARELAAIKEDTEAVLKRINDTVGIKESDTGLAPISFWDVAADRQRMSEEQPLQVARCTKIIENEQSAEKNAYVINLKQIAKFVVSLGERVSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQKVVKGNQKFSSTADYMNMSS O42932 QCR6_SCHPO SPBC16C6.08c; CHAIN 1..214; /note="Cytochrome b-c1 complex subunit 6"; /id="PRO_0000307212" DISULFID 157..204; /evidence="ECO:0000250|UniProtKB:P00126"; DISULFID 173..190; /evidence="ECO:0000250|UniProtKB:P00127" MSFWKNLFTSAFTPISAEADELIKEDRKQFEENTPSKKNFETQSPDEPSPKTTDSTGARDANLSLKTQEPIVSADDAKGAQGKGADEKEEKKETIQPPEEVKTEPPQPEEKEGKEAKEPEEPPKEEAEEPQEGGEEEEEEEEEEEITDPLEKMTQECMDAPDCKEVKHHFEECTARVTKKVEQGDKSEDCIEEFFHLYHCARDCADPKVFKVLV O42935 RL32B_SCHPO SPBC16C6.11; CHAIN 1..127; /note="Large ribosomal subunit protein eL32B"; /id="PRO_0000131144" MAAINIVKKRTKPFKRHQSDLFKRVGESWRKPRGIDSCVRRRFRGTISMPKIGYGNNKKTRYCMPNGLKAFLVRNVSDVELLLMHNKTYAAEIASNVSARKRVEIVEKARALGVKVTNAGAKVRSQE O42937 COPB2_SCHPO SPBC16C6.13c; CHAIN 1..796; /note="Probable coatomer subunit beta'"; /id="PRO_0000050917" MMRLDFQRKLLSHTERVKAVDFHPTEPWVIASHYNGQVGIWNYNTQTLVRSFDINDVPIRACAFIARKNWFVCGSDDFQVRVYNYNTGEKVTQFEAHPDYIRALVVHPTQPFLLTSSDDMTIKCFNWDMSWKCVQTFEGHSRYVMSLAINPKDTNTFASSCLDGTVKVWSFGSSVANFTLQAHDRGVNYVNYYPAGDKPYLITAGDDNLIKVWDYQTKACVRILEGHTNNVSFAFFHSKFPIIISGSEDGTVKIWHTLSYSLIKSYNFSLDRAWCIAQNKDNGLVTVGFDNGLITFSLGRDEPSVTMDSSGKVVWSNYNEVMSAMIRPAKEQSDLTDGSLISLSVKELGTTELYPAVLKHSPNGRFVSVCGNGEYIVYTALAWRNKAYGKALDFAWSADSNVYGSRTSDRSIVIHKNFKESNRLDLSYSCDKIFGGFLLGVVGSDFICFYDWDTGILVRKIDVKPKGVYWNDDGRFVILACDDDFYLLGFNAEMFYSAVESGTADEEEGVADSFEALADVSESVVNGKWVAETFIYTTTAARLNYLIGDQTYKIANVESSFYLLGYIPRDDRIYLTDRDMNVVSYSFNLAIIEYQSLVLKGDLEAAQGLLEQISETDRPRLSDFLSRLGYKEAALELSGDSVQRFELALDAQRLDIASQIAQELDDPLKWRSLGDAALNAWDFVLAQECFEKGKDYGSLVLLYTATNNHEGLKELSQLTKSTKINNTAFICSWLTNQPAECVNILTSTQRYPEANLFAATYCPDEVKNVLPEWKVDLTKNQKERIADSLGDLELKN O42943 YBP8_SCHPO BINDING 108..115; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 423..430; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" MOD_RES 50; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 53; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 54; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 55; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16H5.08c; CHAIN 1..618; /note="Uncharacterized ABC transporter ATP-binding protein C16H5.08c"; /id="PRO_0000310286" MSSKSASKLKREAKKAERLAAKGESVKPSKKNGTKNGKDKEVDGVTKDLSELSTSDPIFERSASGVLTSQPMSRDIKIDSYTLSFHGRLLIENATIELNHGQRYGLLGDNGSGKSTFLESVAARDVEYPEHIDSYLLNAEAEPSDVNAVDYIIQSAKDKVQKLEAEIEELSTADDVDDVLLESKYEELDDMDPSTFEAKAAMILHGLGFTQEMMAKPTKDMSGGWRMRVALSRALFIKPSLLLLDEPTNHLDLEAVVWLENYLAKYDKILVVTSHSQDFLNNVCTNIIDLTSKKQLVYYGGNFDIYMRTKEENETNQMKAYLKQQEEIAHIKKFIASAGTYANLVRQAKSKQKIIDKMEAAGLVEKPEPPRQFSFEFDEVRKLPPPIIAFNDVAFSYDGNLDHALYRDLSFGIDMDSRVAIVGKNGTGKSTLLNLITGLLIPIEGNVSRYSGLKMAKYSQHSADQLPYDKSPLEYIMDTYKPKFPERELQQWRSVLGKFGLSGLHQTSEIRTLSDGLKSRVVFAALALEQPHILLLDEPTNHLDITSIDALAKAINVWTGGVVLVSHDFRLIGQVSKELWEVKDKKVVKLDCSIEEYKKSMAKEVQSRDTTAKVKHLI O42944 OMH2_SCHPO ACT_SITE 271; /note="Nucleophile"; /evidence="ECO:0000255" SPBC16H5.09c; CHAIN 1..372; /note="O-glycoside alpha-1,2-mannosyltransferase homolog 2"; /id="PRO_0000316584" MRISRLLIRVLLGFVILFITYILFPSIPKALVNTLNVYKLEERLNYYNDRLLDGNLKSKELENATFVTLARNADLYDLIETINIYENRFNSKHNYPWVFLNDEPFTRTFEVVMSRLTSGPTYFGVVNSSEWDIPKWIDMDIAHSNWNRLSREGVLYGGMKSYRQMCRYFSGFFWRHPLLDPYKYYWRVEPSTKLLCEVNKDPFRQLRLLNKTYGFVITLFEIGQTVPSLWNSTLEFIEKYPETLAKNNLWEWISDDNGKKFSHCHFWSNFEIADLDFFRSDSYRKYFDFLDKKGGFFYERWGDAPVHSIALSLFLDRNKLHYFDEIGYSHAPLLHCPRKGRCFCKPEEIDLSSNSSCIARFINLTNEDYDEL O42948 YBPD_SCHPO SPBC16H5.13; CHAIN 1..1026; /note="Uncharacterized WD repeat-containing protein C16H5.13"; /id="PRO_0000343432" MDWVALSKSCKTHLLDEGLDVSSIHCFDQYLIVGQCSGQVMVFDVSTDNHFTLIQTFIAHKHSVSSIVCLPFEADGIVDLSIITLDESGLLCQWLLKTCDRRATLQLCDGLCLKLFRLNNNFLAVTGTFLKIYLIRISNFQIVATWTGHEDWPILFPFKDEALLIPVAYSDGSVSLWSVDWSALTFKRNSVTKADVKPTFGKVIDVVPADCISSNYALYVYSDAVVLLESHEKFIASYSLAEITSVFVLADGTACIFTLSSSTLLKLHQSPEPHFELISKYSGDFPWKSCTILKSKPVSLCVYPEKITFNWLTEGTVDSCNLCKLSNTAAVSYAYTDSLNLFLGTTSGLVMFSLFDWYLHNDPAPLYSFTRVSGIVTYMKIFETEHSRSILVVATKTGKAYFYQQLQGERWRFLCERALQSSSITKIIHAKKSLSSGSSGLFIFMSLDGSLCALDESYNLLSYLPSDGAQVETLYSFPDLDQIYVAYDNFQLLNWDVVDQKCSEGNYSDIIDSSFISIGTFDKSNLPTLYHGSCALLTDNLVTVFLDAHDLVLNLNFSNENYIEKTYIDEFLDFIQPPFLNSDIEMEHQLLGTVFDQSSLHLGVGKPDGNAILRFDTEMKSIINTAPNCSALLLYLYFSLMVPLCKYDGLSDTKLTEGILLKLKDLKTVDYSISVLSYVWNNSGKVMQGIIKSMLSRTLELISPEELQRLIYYYFEFFTTTGGEYYLKKEVQHSLYILSLIVSLRPSAFDVSQLKFLSSYLLQKSESMDYDLTAIRLLSNGFSVFSKHIDPAKFIYNLVLSSLENTKDLDDKNSILYRSIVDVSVSNAVLLLTCLCDEVYEQMKSNLRSVILKVVSLAIENTQSEFSLFNQLITEKLLPILYSSRSVEEVHDVTNAIATQFPFACFDSKVEKYSYIDDGDLVVYEIAKRRKVVSKENAECDIQVLSASPSGDYFVGVSATQKECIIWKYSQDFVKFLNLSTPSLTIRKRILLQTNKTNEVEIPEVLWISQSSAEVHIGSTFAIIDL O42951 PABC_SCHPO CATALYTIC ACTIVITY: Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate; Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; SPBC19G7.02; CHAIN 1..231; /note="Putative aminodeoxychorismate lyase"; /id="PRO_0000339123" MEESNLFETTLYDGELFLLPSHLQRMKASAKSLGYSWPGEQYIENKLREAVQDTSMARVRWELSKAGDVTVQIVPIQTLEKAPYTLILDKQPSSTEKNPSCINKMTNRAIYIEAMNRNDAQYSKAQDVLLYNHQGFVTEATIFNVAFHRNGQWITPSLKHGLLSGTMRKNLLENGSIHEDDKGLLQKDNLKNGEQVLLFNSFRKVCKGVLIIQPEKACELLKKKDSSEKLS O42962 COG5_SCHPO SPBC19G7.14c; CHAIN 1..411; /note="Conserved oligomeric Golgi complex subunit 5"; /id="PRO_0000116762" MEFRYDFSDYKKSDFDPKAQAERVLISVHADSDVNEDKEVARKRLGYALKEVERQITDLIVHEETTLTKNVSSSLNAQSYLQDIEGKLEQLMLVYERIRSLVVIPSENLGPLHEAIVNLHSTYMTLYWLGEFFGIQAKLFPLFQGSINENEKLSRYYQASLLLQESDQLLSRFPLMKRQSSVSLLLKLNITNRSRIIKETSSYLLSQEDQLSFSVNSNGFTNACSVLYMLDKYLLEQDLTRLLSSRIQKAIIQFDSIFQLSPTTRRLLHNSTDPSAANSTIWSKFEDGWYQISKIGAQCVFWERSLQKANICNPDYPNLLEYFQMQPNFILDGATICIYFFKELAISISSKMQMLDRRDPILLRVFRSDFQRVTHIVEQAIARSSSEIVNKDTRECSIVMNSLRVLAPKNP O42964 IWS1_SCHPO SPBC19G7.16; CHAIN 1..428; /note="Transcription factor iws1"; /id="PRO_0000083363" MSEEEKAELENMQVESEAKTSENDQTIDTKVDVADVTTHVDEDLDNKEEALDFSEDELSDLDENQFENFDESKIGREAEEPTIYNLPTFKKKQEPNTIEENLEVPRKVRKEQKPRRRRGKRSSTVDALNDELNELGENEEEVLTEQKQLDPTLAAKKELDLQMDAVLKPTRTKKRSNEDNLEQMADDEVLRLREQMRLAALRDAELNSEQLPATEKLKMLPLVDAVLRKTHLYDTILDNNVLDSVRMWLEPLPDRSLPALNIQRSLMDILTKLPIQTEHLRESKIGRIVLFYTISKKPEPFIKRIADNLVSEWSRPIIKRSANYRDRAVGVASFNPEVFQTRRRRDLAAAESNDDAQASRTGRTVIPRSIDSRYQVAPRVRLNPTAMTIAGRMKPADTEQVRKLKAKMKAIRSKSSKKSGVSIEGRGL O42967 YB92_SCHPO MOD_RES 566; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1E8.02; CHAIN 1..603; /note="Uncharacterized ubiquitin-like protein C1E8.02"; /id="PRO_0000310777" MSEYRIRVTTVDQKVGIFQVPRTKTVLELKELIAVTFEAPADRLKLIHAGRVLRNETPLEEILHDATDLVTFHLVIAVFNSTSTTLPSATSSSVPQSRTSELSSTNSIPTPRITSLNPEELSRRERAQRLLQTYNSFHGSGLGGLFPNIHRELESHGFSLPTHEQSSPVAESLDNSVSSALSPHLETLRRRNLSIHHQHIQAHEMAQESLETRNPGNISSSSAPLASDQSPTVSSNHIHASGNLALGSNSGLNPRSPNSFSSPLDNPALHTVDSTNVNGSLSPLSNSSSINQVHQNETHGSTISVPNPNLSQMGPSHSSSVPSNLSPNPAQNENPSTTSIPSINNQPFPSGLSASNSNFASSSFIPQSVPQLLPIYYQTIFYNGNYYLQQLPSASPPTMFRDHSFAPLVSPSIVSPYGVLENEETGECAFLFSPNASQPHFQPRAPTFGIPRNVRSLFTLPFFHTIRNIERHFRLFIRLALFCVLTTYNVSLSQTILLTSIMSVVFLLQTGALAPFINDNPLIQSGMRHIRNLQDEYRRRRNRTAQRVVEIPNETQTEDEQDGTNTPDNRADAEERELTRSQRIYRTVVRTIVAFALSFVPRA O42971 APC10_SCHPO SPBC1A4.01; CHAIN 1..189; /note="Anaphase-promoting complex subunit 10"; /id="PRO_0000174015" MAQIRQEALKKQKSETQKSTEGFVDIGNLAQWTCSSEKSGFPIRLVRDDNIDTYWQSDGSQPHTIHIKFVKRVSIKYVSMYLQYTLDESYTPSTLRISAGTGFQDLEIVTTVQVEEPTGWVHVPVGDFGRNGLLDVHLIQIKILANHQSGKDSHVRLIKIYAPEIEQPAIAVDEIPYTSLQFISRNQLR O42975 NRDE2_SCHPO MOD_RES 970; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC20F10.05; CHAIN 1..972; /note="Protein NRDE2 homolog"; /id="PRO_0000343144" MPSNHNTSVPKFSSFNSVKAKKNPITKSNKKYRSSHDQVSSNHAKSSFPSHRSIQSNFAVDTKGEKQNLLYGINKRPVPKYHRSSSSVYGSAPLLRIVKESKEGITLNKKKSLEIKYDEERSFDEKENDESEFEDGQQGFIPLLVNRNSDPSEKSTFSLNILKAIKETDEEIKKNPGKARLWIKMCEYQERLLFDEFRRSNSDDIKGKLKIENNSRSVKLSILEKALKEVKGCDHEILVSYYLQLGSEEWSKEETNQKFEEVLIEHPGYLNLWMKYAEYFTGISEFTFNDCLNMFSKCFKFLKQKLSDRKSCKERESTDVTSNFEVEEAILHLLIRLCDFLKNCGYYELAWSIFQANMELCYFYPRYLEKKLDSTFFESFSKFWNSDTPKFSEENARGWCNVLDDESSQQNQNFSSEIGIFQTVKLWYLNESKFDTNPPPRSTMSCRKLSGIDDPFRYIVFNDIQDFIVCFESETIAFAFKYKFFAFCGVPLFPPGISTNSWFASYDKGIYNLLFGMASSESFINGQIAEKNSFQFPCSILPSYIDLFISLMSFKNLNFKLFDYNLAHHVKESMERAFHQLVFSADDEYLASVYLIYLKQMETKNLSEEKPQVNKIVKKILKKYDSSVSVWNTYAQLEHLSGAFTMAETIFKTIFQIHASQLRYIDNLNVYKNWAFRKLLINDTEGCLVIIKCLLFPGDKSLTSDNNRASEMLFGMLENCASKEELLYVCLIYTIWTHCTDMDSMDNCVYLCIQKFESYGWGASSEMECYFSYCSLIFYYQATTLQFYNLPKVRPFFEKGVTLFSANTAIWEVYIFFESKLRQENKPKIRAMKILKSASNAVVTACWYLFYVAVQQIEPTNSQYFLRTLDITLNNEKLKSVAKFWRIYLKILNLRLNGTEWVSAITTKALASCPCNKGVCMDVIDLLLKKEMESRAIICYIIMLEKGFRVHNEIRRDVLKFERGDELILSPN O42979 PSL1_SCHPO SPBC20F10.10; CHAIN 1..243; /note="PHO85 cyclin-like protein psl1"; /id="PRO_0000374022" MSLAFTLLTSKDNTDEDEEHLELSSFNQEKLLEMISVFLSRLTRLNDSKQEATESDQIPLSPTSLKNPCLIFSAKNVPSISIQAYLTRILKYCPATNDVFLSVLIYLDRIVHHFHFTVFINSFNIHRFLIAGFTAASKFFSDVFYTNSRYAKVGGIPLHELNHLELSFFVFNDFNLFISLEDLQAYGDLLLSWYRQNGQNYNPTDVSCSIESPISHTPQQNQQDEQPRRPIMDRRLLSSHSIG O42984 RS17A_SCHPO SPBC839.05c; CHAIN 1..131; /note="Small ribosomal subunit protein eS17A"; /id="PRO_0000141544" MGRVRTKTTKRASRVVIEKYYPRLTLDFQTNKRIVDEVAIIASKRLRNKIAGYTTHLMKRIQRGPVRGISFKLQEEERERKDQYVPEVSELEVDRVNVDQDTKDMLKSLGYDQIPVRVLAPAPQERFRRRQ O42991 RL16B_SCHPO MOD_RES 193; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC839.13c; STRAND 6..11; /evidence="ECO:0007829|PDB:8EUY"; STRAND 33..37; /evidence="ECO:0007829|PDB:8EUY"; STRAND 43..46; /evidence="ECO:0007829|PDB:8EUY"; STRAND 91..93; /evidence="ECO:0007829|PDB:8EUP"; STRAND 103..105; /evidence="ECO:0007829|PDB:8EUY"; STRAND 136..138; /evidence="ECO:0007829|PDB:8EUY" HELIX 17..29; /evidence="ECO:0007829|PDB:8EUY"; HELIX 39..41; /evidence="ECO:0007829|PDB:8EUY"; HELIX 48..60; /evidence="ECO:0007829|PDB:8EUY"; HELIX 77..87; /evidence="ECO:0007829|PDB:8EUY"; HELIX 94..100; /evidence="ECO:0007829|PDB:8EUY"; HELIX 111..114; /evidence="ECO:0007829|PDB:8EUY"; HELIX 126..129; /evidence="ECO:0007829|PDB:8EUY"; HELIX 139..144; /evidence="ECO:0007829|PDB:8EUY"; HELIX 151..185; /evidence="ECO:0007829|PDB:8EUY"; HELIX 188..191; /evidence="ECO:0007829|PDB:8EUY"; HELIX 193..195; /evidence="ECO:0007829|PDB:8EUY" TURN 67..69; /evidence="ECO:0007829|PDB:8ETC"; TURN 122..124; /evidence="ECO:0007829|PDB:8EUY"; TURN 145..147; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..197; /note="Large ribosomal subunit protein uL13B"; /id="PRO_0000133789" MSEFQKVVVIDAKGHLLGRLASVVAKQLLGGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFQKAVRGMLPHKTARGQAALEHLQAVEGIPPPFDKQKRVVVPAALRVLRLKPGRKYCTVGRLSSEVGWKYNDIVAKLEERRKVKSAAFYQAKLAKQKKIASAKEASPVNQKLSQFGY O42993 FKBP_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPBC839.17c; CHAIN 1..112; /note="Peptidyl-prolyl cis-trans isomerase"; /id="PRO_0000075304" MGVEKQVISSGNGQDFPKPGDRITMHYTGTLTNGKKFDSSVDRGSPFVCTIGVGQLIRGWDEGVPKMSLGEKAKLTITPDYGYGPRGFPGLIPPNSTLLFDVELLAINDKKA O42999 TOM7_SCHPO SPBC27B12.10c; CHAIN 1..52; /note="Mitochondrial import receptor subunit tom7"; /id="PRO_0000046766" MQISEESKERLVKVFNIGKTVTHYGWIPLILWLGYTQSNPKPQLMRVINPLA O43000 LIZ1_SCHPO SPBC2G2.01c; CHAIN 1..514; /note="Pantothenate transporter liz1"; /id="PRO_0000121370" MALLNRLAKTFSPYYGLNKVEQKLLIKIDWFILSYCCVSYFINYLDRSSINNAYLSGMQEDLKMHGNELQDINVVFTCGYIIGQLPGSYALQRVPARLWFSVMNILWGLMTIFSFAVHSVRALMILRFFMAVAEASTFAGTHYILGAWYKESELCKRAGIFSASGLVGTMFAGYLQTAVHSSLNGKGGLSGWRWLFIIDGILTIPLSLYGLFLFPDVPETTKAPYFTEQEKELSFKRLPARPKKKPLTLKAIKDIVRSWRIYGLCILWIFSGETQAIAVNVLMGQWMKWSNKFSVAQINNYPTVITAVGVVSTLGASVISDKLAGNPRWPFGLFLCVITTVSATILLAWNVPDGAKFFAYFASGCTYAGQAVWFSWANDICRDNDQERGVVVFLMNMCQNIWHIWWAPIMYPNTDTPRFIKGLIGLLVVGGIVFVSSCIVSYMQIRDKRIKRSIQDAKDFDDVFTEHESLELKKIGKNDEESLNTTNAVKEISSPGLVITRQRISMPKETNAQD O43002 SC61B_SCHPO SPBC2G2.03c; CHAIN 1..102; /note="Protein transport protein sec61 subunit beta"; /id="PRO_0000157259" MSSTKASGSVKNSAASAPGGPKSQIRRRAAVEKNTKESNSGPAGARAAGAPGSTPTLLKLYTDEASGFKVDPVVVMVLSVGFIASVFLLHIVARILKKFASE O43003 MMF1_SCHPO TRANSIT 1..?; /note="Mitochondrion" SPBC2G2.04c; CHAIN ?..162; /note="Protein mmf1, mitochondrial"; /id="PRO_0000036210" MLRALGSRLLVASRPAAYRSFQQSLRPVPRFFIHKMSTKTPINSPKLSSAGPYNQAIKANGVIYCSGQIPVANGKVIEGTVGDQTRQCLLNLQEVLTEAGSSLNKIVKVNIFLADMDDFAAVNKVYTEVLPDPKPARSCVAVKTVPLSTQGVKIEIECIALE O43004 RL16C_SCHPO SPBC2G2.05; CHAIN 1..197; /note="Large ribosomal subunit protein uL13C"; /id="PRO_0000133790" MSEFQKLVIIDAKGHLMGRLASTVAKQLLAGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFTKAVRGMLPHKTTRGNIALKNLQALEGIPPPFDKQKRLVVPAALRVLRLKPSRKYCTIGRLSSEVGWKYKNIVSKLEERRKIKSAAFYQAKSANQKHINVAKTKSSVNEKLAVFGY O43010 NMT_SCHPO ACT_SITE 466; /note="Proton acceptor; via carboxylate"; /evidence="ECO:0000250" BINDING 51..54; /ligand="tetradecanoyl-CoA"; /ligand_id="ChEBI:CHEBI:57385"; /evidence="ECO:0000250|UniProtKB:P14743"; BINDING 185..187; /ligand="tetradecanoyl-CoA"; /ligand_id="ChEBI:CHEBI:57385"; /evidence="ECO:0000250|UniProtKB:P14743"; BINDING 193..197; /ligand="tetradecanoyl-CoA"; /ligand_id="ChEBI:CHEBI:57385"; /evidence="ECO:0000250|UniProtKB:P14743" CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723, ChEBI:CHEBI:133050; EC=2.3.1.97; MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2G2.11; CHAIN 1..466; /note="Glycylpeptide N-tetradecanoyltransferase"; /id="PRO_0000064247" MDNENNKNTKNSQQDSSFSEGGIRELLDRLALRSLIEKEEAAAPPKTYEDFKFWKTQPVPKFDDECTQEGPIDPNTDINQVPREPYRLLKEFEWATIDVTNDNELSEVHELLTENYVEDATAMLRFAYISEFLRWALMPPGYVKEWHVGVRVKSSRKLVAFISAVPLSIRVRDKIIKKCAEVNFLCIHKKLRSKRLTPLLIKEVTRRCHLENVWQAVYTAGVLLPSPVSLSRYMHRSLNWKKLYDIGFAPFPLGSTEKKETAKYHLPPNTQTPGLRPMELKDVPAVQSLLSQYMERFELAHLFSEEEVRHWFLYTDKVSSGPVVWSYVVENPESKKITDFFSFYSLPSTVIGNPKYKDIQAAYLYYYASDSCPKDLSSESQLAFVERCKLIVNDALILAKKFHFDVFNAVTVLDNNLFLKDLKFGEGDGFLNYYIYNYNCPKIPGGIDASKSVDYSRPSGMGFVMI O43012 DCTD_SCHPO ACT_SITE 248; /note="Proton donor"; /evidence="ECO:0000250" BINDING 246; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 273; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 276; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=dCMP + H(+) + H2O = dUMP + NH4(+); Xref=Rhea:RHEA:22924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57566, ChEBI:CHEBI:246422; EC=3.5.4.12; Evidence={ECO:0000250|UniProtKB:P06773}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q12178}; SPBC2G2.13c; CHAIN 1..322; /note="Deoxycytidylate deaminase"; /id="PRO_0000310830" MPTVGLTGPLCSGKDAVVEYLETKHGFNAIFRLPQLNEDGEYIYRTGDLVLGSVDDLISYLTPRWRERFVINGIHSPRLLSALLKRPFFLLVYIDAPIMLRFNRYKTYSSLANTTLEEFCSIQDAAAFQSDNAGTRHRALANLLINNDSNIKLHLWEKLQKADLLNPNRFRPSWDSYFMEMASLAAKRSNCMKRRVGCVLVRGNRVIATGYNGTPRGATNCNEGGCPRCNSASSCGKELDTCLCLHAEENALLEAGRERVGNNAILYCDTCPCLTCSVKITQLGIKEVVYHTSYNMDSHTASLLQAAGVQLRQYIPPENSIF O43014 MPI_SCHPO ACT_SITE 284; /evidence="ECO:0000250" BINDING 99; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 101; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 126; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 265; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate; Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527; EC=5.3.1.8; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC2G2.16; CHAIN 1..412; /note="Mannose-6-phosphate isomerase"; /id="PRO_0000314774" MYRLKCDVKSYGWGKVGHESLAAKLAEAGYGFEVDPNTPYAELWMGSHPSGPSFVMQTGKPLSELLTPETVGEKVYKKYGKQLPFLFKVLSINKVLSIQAHPDKPLGKQLHKTNPKEYKDDNHKPEMAVALTEFDALCGFRPVKQIEQFLDSIAPLREFVGEEAVRQFKGTVKQDERKALETLFNELMHKDEKRIQEFTPQLVQLAKSDANNFGGTEYGGKAFSDLIIHLNSQFPDDIGLFVTPFLNYVRLHPGEAVFLRALDPHAYVSGNIIECMAASDNVIRLGFTPKFKDIETLVNNLTYQTADAKSQLTQPVPFAKACGSGKTLLYDPPIEEFSILQTKVSPGQKQCIRGINGPSILLVTEGSGILNGDKGDVASISPGFVYFISANFPLTISATSEPVVVYQAFCEI O43026 G3P2_SCHPO ACT_SITE 152; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10009" BINDING 13..14; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 35; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 80; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 151..153; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 182; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 211..212; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 234; /ligand="D-glyceraldehyde 3-phosphate"; /ligand_id="ChEBI:CHEBI:59776"; /evidence="ECO:0000250"; BINDING 316; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PRU10009}; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 153; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 154; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 182; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 184; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 192; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 203; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 209; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 211; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 237; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 241; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC354.12; CHAIN 1..335; /note="Glyceraldehyde-3-phosphate dehydrogenase 2"; /id="PRO_0000145581" MAIPKVGINGFGRIGRIVLRNAILTGKIQVVAVNDPFIDLDYMAYMFKYDSTHGRFEGSVETKGGKLVIDGHSIDVHNERDPANIKWSASGAEYVIESTGVFTTKETASAHLKGGAKRVIISAPSKDAPMFVVGVNLEKFNPSEKVISNASCTTNCLAPLAKVINDTFGIEEGLMTTVHATTATQKTVDGPSKKDWRGGRGASANIIPSSTGAAKAVGKVIPALNGKLTGMAFRVPTPDVSVVDLTVKLAKPTNYEDIKAAIKAASEGPMKGVLGYTEDSVVSTDFCGDNHSSIFDASAGIQLSPQFVKLVSWYDNEWGYSHRVVDLVAYTASKD O43027 RGA6_SCHPO MOD_RES 141; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC354.13; CHAIN 1..733; /note="Probable Rho-GTPase-activating protein 6"; /id="PRO_0000097314" MTLNPSTLNNGTLGDLKEHKDVVLSSNAQTDEKRFEEPSLEVGGSLAKVENGLSTSISSSASNLEGQQAPFFTKQNSCLSRFRELAQTYNIHEINLEEYVSQIKEVKQSLYSDDSVFNESKSSSPPDAHTDKYFTPCGSPTKLIHSTLLEERDTPSSLEHVSFYLQESAVSEVRFDKPSNNGPLGRSSLNLSSLSHELQTSQDSPSLSATNQLSSSDTLEPLQYPPSSFGSQRQFNASQDSPKRSPSKGSWSSILRRPSLTYSPKRQSTGLHRRSLTNYFKFPHRNAHQHNAIAHNPSVFGKPIGDLTSDPTNLCKFTFPTPECAPPSLLLPHIFAQCVHFLSLNALHVPGIFRISGSGPVIKAITEYFYSPPHFWLDETSEIFKRIGFPSYIDIAAVLKRYIMLLPGGLFTHKDILNLLVPLYVDSSRVKVPIDIRNEMAALCFSQIDSYVRFSILCSLLALLHQIATRTQELENGMENTKDSTLMKPEALGIIFGPLLLGNSSTDLSKSCPSGNVNDLMRFETEKARVEAKIVEGLIIHWPEVLLKINSLDIPNCFSDVGLTDQVAIFTPAVPKEDSPEQIPENVNASEESYPNVKHISKLPLINDSSDNESGNQENDDAVANESTKVVVDNQQPQPKISTVSDTAVPSMSFANNISSRSVISAATDSKPSTRTSPPFVNNTKPIVAKSPVTVTASSETNKKSQKINKKASPRVSLWTKLFGKFRSNKKKS O43028 VAC8_SCHPO MOD_RES 548; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 550; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC354.14c; CHAIN 2..550; /note="Vacuolar protein 8"; /id="PRO_0000256217" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000250"; LIPID 4; /note="S-palmitoyl cysteine"; /evidence="ECO:0000255"; LIPID 7; /note="S-palmitoyl cysteine"; /evidence="ECO:0000255" MGNCLSCCEKSKDEQYEPLLADREREAVADLLSFLEDRNEVNFYSEEPLRALTILAYSDNLDLQRSAALAFAEITEKDVREVDRETIEPVLFLLQSPDAEIQRAASVALGNLAVNAENKALVVKLNGLDLLIRQMMSPHVEVQCNAVGCITNLATLDENKSKIAHSGALGPLTRLAKSKDIRVQRNATGALLNMTHSYENRQQLVSAGTIPVLVSLLPSSDTDVQYYCTTSISNIAVDAVHRKRLAQSEPKLVRSLIQLMDTSSPKVQCQAALALRNLASDERYQIEIVQSNALPSLLRLLRSSYLPLILASVACIRNISIHPLNESPIIDAGFLRPLVDLLSCTENEEIQCHAVSTLRNLAASSERNKRAIIEANAIQKLRCLILDAPVSVQSEMTACLAVLALSDEFKSYLLNFGICNVLIPLTDSMSIEVQGNSAAALGNLSSNVDDYSRFIECWDSPAGGIHGYLVRFLSSEDSTFAHIAAWTIVQLLEAGVPRLTAFIQSSDDIIELLNDIVARDANNGEYEDGEGDVILLSGRALHLIEQDTDS O43030 FES1_SCHPO MOD_RES 18; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 20; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3B9.01; CHAIN 1..287; /note="Hsp70 nucleotide exchange factor fes1"; /id="PRO_0000285401" MEKLLAFSTQLQAQGNSSNSPPDPKDLDPSVLDHIFGANPADEMRKAMDAIEDPSVPLDQKEIAFDNLEMLVEHIDNANNLVPLQLWPRLLKQLESPESTLRRLAAWTIATAVQNNPKSQQALIENDGLKILFGALKKEDSDETKNKVLYAITSELKLNEAGIALLDKIPNSWEMLIEILELKHSVMTKRVIFFFYALLIQEDKSKQIILQKAHEFQIPEKVYQFSLEHSVDEDCVTKSLHTLYLFQKNKVSVANTNELLKSLVQFKSEFPEIFTVDEWKAFHEALE O43031 SPP2_SCHPO MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 275; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 277; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3B9.02c; CHAIN 1..381; /note="Pre-mRNA-splicing factor cwf28"; /id="PRO_0000218527" MKRKAVLEAFSDSEDEDEKKLKGPQLITGFSAEEGVHYQNETIQRIHEKKRAPKIIHIASDENWMEKRKARFKKKETEVHEKPSQLPDSGLNYGLNIRVASSSAADNEIVDWKANNSNEKAQNKIATNKESTDILPEEVQLVLNDLNDDVKSANSANLQPITTNVVNEKDAYRKDIDELPEPSNMKDYSEIPVEEFGAAMLRGMGWNGQLSSKDAFDVNQRPTFLGMGAKPVDSELTELDIWKNPKKTMFLPVKPLESNSALNSQNEHTEVQKKSNSIDNLTPSSELFRKRSRDNNLSRESSVSSKHLDYNSRNYNKRDRDPDRTKYREYHSERRKQHRTDRYSDDYYQGRSYSYKKRSHRSDRYTERENPDRSYRSTRTL O43032 SRPR_SCHPO BINDING 349..356; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 437..441; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 498..501; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPBC3B9.03; CHAIN 1..547; /note="Signal recognition particle receptor subunit alpha homolog"; /id="PRO_0000316024" MIDLFAIVNKGGIVLWKKTNSLVNLKCLQVLFHEAFLSEQRTVNNTVTFDRYTMQYQEATQYSIVFVVVFQDLKCMAYSQSLLNSAHNIFLNLFKEKLEDRQVPNEAEVEKLFAPIFNRKSAQLENETDTKSLPVEANNDNSARKKNEYEMKKKGAQSKQTNAPKKGKKQLRKWDDQITEEEQAALNYSSQASSASQTVDNSQLSSIVGNNNKFQKTGSGDVIISDLEMDPNQTISNKSASSAFSLFSNLIGGKYLKEEDLSPILKQMQEHLTKKNVANSIALELCESVKASLINKKVGSFDTVKNTVNKAFRDRLTQILTPSTSLDLLHSIRSVRKNENRPYTISLIGVNGVGKSTTLAKIAYWLLSNNFRILVAACDTFRSGAIEQLGVHVKNLQSLKGSSIELFAQGYGKDSSFVVKNAVEYAKQNSFDVILIDTAGRRHNDQRLMGSLEKFTKATKLDKIFQVAEALVGTDSLAQAKHFQASLYHRPLDGFIISKVDTVGQLVGVMVGMVYAVRVPIIFVGIGQTYSDLRTLSVDWVVDQLMK O43041 TRS23_SCHPO SPBC3B9.12; CHAIN 1..132; /note="Transport protein particle subunit trs23"; /id="PRO_0000357022" MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVLFTEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH O43042 RM03_SCHPO TRANSIT 1..26; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3B9.14c; CHAIN 27..326; /note="Large ribosomal subunit protein mL44"; /id="PRO_0000314100" MSFISRSTTTFRRSISMKDYARVRWYSNSGKSLIENILSSKIAISKVYTLKKRIGLPESYPMKVLVQALIDKTVVQNPQYSNEKLWSIGKVFGDFYVLEYIKCKYPRLPEEAVHGMQNGWMGSKALSQLATIWGLEVQRREEGLQESFGKVLAKRADPEMLRKPGEIYKDEAARRAILAILGGVYLHQGFNDTKKFINDHILSKQLDPRTMLQLQWPRRQLSRLCKRLSLKEPVYRIIAETGRKSREPVFVIGAYSGHHLLGQGQASSLNLAEQQAAYNSLISYYIHSPPFRQLPSDYLEVNDGKIPKASEPYTSIPLVSHGQLVI O43046 VATF_SCHPO SPBC3B9.18c; CHAIN 1..120; /note="V-type proton ATPase subunit F"; /id="PRO_0000144811" MSSQSYRERTLVSVIGDDDTVTGMLLAGTGQVNENGDKNFFIITQKTTDEQIAEAFDDYTTKRKDIAIVLINQFAAERIRDRIENHVQAFPAVLEIPSKDDPYDPEKDSILRRVRKIIGE O43047 GRPE_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3B9.19; CHAIN ?..223; /note="GrpE protein homolog, mitochondrial"; /id="PRO_0000013045" MLGLGRVFSSAVRPRTLIRAPINKRSFLWYSTEAAKEEKPAEEKVAETENVDVKELQSKLSELKSKYEAKDKEVAELKGSIRQSLADYRNLENRMKRDMEQTRAFAVQKLTKDLLDSVDNLERALSIVPEEKRNNRESNKDLVDLYEGLAMTESNLMKTLGKYGLVRYDGIGEDFDPNIHEAVFQIPVEGKKPNTVFHCESKGFQLNGRVIRPAKVGVVKGDD O43049 PPT1_SCHPO ACT_SITE 279; /note="Proton donor"; /evidence="ECO:0000250" BINDING 217; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 219; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 246; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 246; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 278; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 327; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 404; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; SPBC3F6.01c; CHAIN 1..473; /note="Serine/threonine-protein phosphatase T"; /id="PRO_0000363378" MAKEALELKNEANKFLKEGHIVQAIDLYTKAIELDSTNAILYSNRSLAHLKSEDYGLAINDASKAIECDPEYAKAYFRRATAHIAIFQPKEAVGDFRKALALAPSDPAARKKLRECEQLVKRIRFQEAIHNTEPPSPLANINIEDMDIPSDYDGVILEKQITKEFVEDMKERFCQGKKLPLKFAYSILRDLKELLEKTPSLIDIPVKGDETLVICGDTHGQYFDLLNIFKLHGPPSPTNKYLFNGDFVDRGSWSTEVAFTLYAYKLLYPDAVFINRGNHETDDMNKVYGFEGECRSKYNERTFNIFSETFSLLPLGSLISDSYLVVHGGLFSDDNVTLDQLRNIDRFSKKQPGQSGLMMEMLWTDPQPAPGRGPSKRGVGLQFGPDVSKRFCEANGLKAVIRSHEVRDQGYEVEHDGYCITVFSAPNYCDSTGNLGAVIKVKEDMELDFHQFEAVPHPNIRPMAYANGLLSGM O43051 NOP14_SCHPO MOD_RES 190; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3F6.04c; CHAIN 1..827; /note="Probable nucleolar complex protein 14"; /id="PRO_0000137161" MGKNGSQLKNLKSSIRQANLGTRPNNKKSRTRSTESHEDRQAKVQKIQSDFNLFDRQFTKRKFDVGGRRVKGTEGKPGVSRGVGEELRRRTIGAELKKRNRSGAIIDRRFGENNPHLSVEEKMLERFSREQQRRSKRELYNLDAEDVLTHGNRPLSDIDSFEEPGFGLDEGEELNDEVVRRMHFGGFEDSDAENEKEGEGAHKSKREVMSEIIAKSKHYKAERQAEKERYEDEREKLDEQMEDLQSFLSDYKKASRKSGIKTQRPIISDGDARYDSFVREMVFDKRAHPTERTKTEEELAQIEADRLRELEDQRISRMEHYQEDSASEAGSIEDEQATDNVFGFGKGLEQENEEEWNGINEEAEESEDEESVNSDTSFVDDEQLKVEEQPLVGSAIKNEGSEKASLAYTYPCPTSHVEFVQLLKGLDYKDYPTVVSRIRTLHHVKLHPDNKSRLENFSVILLQHILHLTRQPMISMELLEHLTEHLHSLAQQFPSALGISFISVVEGMRKRLAKSYVYPEIKFPEISDLLFFNLTGSIFPTSDKKHIVVSPVMLTMAESLSQSPADSLSDVCKKLYIANLFLKFQSYSHRYVPEVITAVSQALYLLYPNFISIVPGTFALPDSLKEKQNLFAIQDISLDEPQRLSLYELEELPTGLLQSSILFITLNLIEMAIDIYFKEQAFIEIFVPIMDMLQLYSLKKELLSKRLSEKLLSTLQAVSDSIESAKANRKPLALQSHRPLGITSQVPKFEEGYSLDKSSHDIDPERAQLNKLRAQHRDAKKGAIRTLRKDARFIARERRQEQRAKDQAYNEKMRKLENRLQHFDPAV O43061 MU136_SCHPO SIGNAL 1..34; /evidence="ECO:0000255" SPBC4C3.08; CHAIN 35..372; /note="Meiotically up-regulated gene 136 protein"; /id="PRO_0000278627" MRLYFSAFRHPKRLGLCLLITLSIILLGWQCVLLYNHSPEIQRSVYTLTGLAPSSKMAFVTMLTVRAANGENEVENTQQDWYYNSTRLLVHRLVKFKPTKSKYPVVVLAMKGIDQWKLDQLQEDGAIVKVVDPLYAHEVVDDVNDIALLDSRWSMMFTKLRVFEMYEYDRICFLDSDILPIKKMDKVFDVHQLSYSKDSVLFPPTLFYKPRRSIFWRRFTEEFAAYGLTRDDLYPYVFAAVSDPGMWHETPPPFKDYFNAGLFVFKPLKAHYKRLMALARFPKLYDNANMMEQSLLNFAYNSAGAFPWESLDWTFNGLWARKNDLPYLKAVHGKHWQPEGSLGYDEDTSKLWWDAFQEMQTYHDQQRNADLY O43062 YGT9_SCHPO SPBC4C3.09; CHAIN 1..376; /note="Uncharacterized protein C4C3.09"; /id="PRO_0000372363" MNFFKRLRLHTRLLLRSKFVLISLILLLNLGLLLGIQIYRDPAFPGSLISSAAYEFGLHKHGPYYNDNVDDLKRYTFMGLLTLPTSEHDVYFNATRVLVYKLKHHPETKSKYPVHVLVMKGVDEWKIERLRLDGAEIIMVDQIKTEDLIESGLSIGMGSYRYQYMFTKLSVFEQTQFDKVCILDSDLLVLKNMDDIFDTPYVYESPAEPDMFSFPIFKKPDDEEDYQFSDNFDAYGAPRSEFYPYLLGACDDRNPGHATPPEESETFNAGLMLVHPSSLHMHRIKKIARYPYMYDDARMMEQSLLNLAYNKYGWFPWTRLDFSYNGVWVTEEDLPYLRAAHGKFWEYDNTEFPQILTAEWHKAFGELLAFHDYVVE O43063 PSB1_SCHPO ACT_SITE 25; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; SPBC4C3.10c; PROPEP 1..24; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000026641" CHAIN 25..226; /note="Probable proteasome subunit beta type-1"; /id="PRO_0000026642" MATTVKDTMNVDINAIKKGEIRMGTTITALRYKDGVILAADSRTTMGAYIANRVTDKLTQLTDNIWCCRSGSAADTQTVADLLKYYLSMYRIQFGHDPSVHTAATLASEMCYQNKNMLSAGLIVAGYDEKTGGDVYSIPLGGSLHKQPLAIGGSGSAFIYGFCDANFRENMTQEEAVEFLKNAVALAMERDGSSGGTIRMVILNKDGMERKFFAIDTANPIPVFTH O43076 SHQ1_SCHPO SPBC8D2.13; CHAIN 1..451; /note="Protein shq1"; /id="PRO_0000302828" MITPKFELRQDEEFVYLDVHTPYIKAKNVEIDAFNNEVNFCIAPYFLKLELPGNVLDDDRANASYDISSGFVHIKFPKETPGEVFPDLDLLTTLLVNQNKEPVKKPLIEEVEDTPSPSTSQNASKDEEKEVKIDWQNIHFDDPDFDWGLLQRLDDEKMQYTSTSQYGFNNQYSGLLKYNALVGNEINQIPEPERTPPSTRSEIRVQLEDEKFDAEHYMADFYDREMIDEILHYIPDYIGEFLLVQQGKSDRLLEFTSEEKEALAKLPKRSYLIDNPKNVYLCLVPLIFAYAYDNRTTLGDPTIESCWNIGTLSSTISCLDTNFLAIKDIFIACIRRSLAYPLYRNWDLALTCWKDTHAILSLGKRWILRVLLRIRNLFEHHDVYYIYNAIVLNDYAYWIQTANDNVLAALAYQVSECTITKEETNWPLEEIEANVQETIIASDEESESIEK O43077 MDE3_SCHPO ACT_SITE 150; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 27..35; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 53; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC8D2.19; CHAIN 1..559; /note="Sporulation protein kinase mde3"; /id="PRO_0000086318" MSNESIYSVLDLTQVIFEDRYLVKQKLGDGSFGTVYLAQRKEKNGLYETVAVKKLKNSSKPKPKHELLKLRESLALRKISKHPCLIDLLETFMDPYRNIFLVMEFMDCNLFQLFKRRQGRLFTKETAFNILLQIISGIEHIHKHGFMHRDIKPENILVKRISPKPISSRYSIKLGDFGLARPSVSSDPLTEYVSTRWYRAPELLLRSGSYNHSVDLYAFGCIVFEIYSLKPLFPGRNETDQLNRVCEILGNPGIDELDTLHYWSQAKELAKRLGFMLPPTKPYPIQKLLPQNCPEGHAKMIPCLLAWNPDVRPTAKYCKEVFFPLPPSASKSNSVPQKISNPKVEQNLGFPISREDKKSTRRVGWLKKNLSEFVSSVKSVFPDSHGSQPHVKTEKPINAKESTGHLANPIASSNVPAISLKPGELHESVFFSENEQIDYLLTSIDYLPSYKPPSNGSNIAINAFNETVGDRIPSSKDILITEKIPFKKENEIRDSIVPSCSQPDESNKEGVASCLLLQKSGMEMTSVLEYSTPNPAEVQNICNDHAKFETSKSLHLSSP O43080 NAA38_SCHPO SPBC947.03c; STRAND 58..63; /evidence="ECO:0007829|PDB:7L1K"; STRAND 65..67; /evidence="ECO:0007829|PDB:7L1K"; STRAND 69..77; /evidence="ECO:0007829|PDB:7L1K"; STRAND 84..89; /evidence="ECO:0007829|PDB:7L1K"; STRAND 111..114; /evidence="ECO:0007829|PDB:7L1K" HELIX 48..54; /evidence="ECO:0007829|PDB:7L1K"; HELIX 106..108; /evidence="ECO:0007829|PDB:7L1K" TURN 55..57; /evidence="ECO:0007829|PDB:7L1K" CHAIN 1..116; /note="N-alpha-acetyltransferase 38, NatC auxiliary subunit"; /id="PRO_0000304083" MALHYFLQYDVQILCIALMFSIFRVCISTAIDFTSPKLDEFSLIMENGEILLTSWLNRSVHIEIFDERKFIGKFLCTDREGAAILSNTTEYNKGFSRALGLVVIPGKHIKSFSVRA O43082 RR14C_SCHPO MOD_RES 75; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC947.07; CHAIN 1..233; /note="Ribosomal RNA-processing protein 14-C"; /id="PRO_0000356272" METTEGKNDLRAKLAEKIQTFRSQRKATEKVDRALLLQRRKEKAKARAEAKKLAKKESKAKQESKVAAYDTGNSSDNIADEENDNHKSTITYGTLIVGDDKFSNGKLKVAGKKRGPTDVFGALKHLEAKKRRIESMDEEKRRKIEESDKWHRVLLQAEGKKLKDNEQLLKKSIRRKEKEKKKSSDAWKERKDNEKKAMLMRQQRREENLKKRRESKKSKKGKAPKKKKPSKKK O43083 HPC2_SCHPO MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC947.08c; CHAIN 1..338; /note="Histone promoter control protein 2"; /id="PRO_0000373989" MSLLSGDQRIICLEIPLQGKENVHINFAKEVEKLYGPSVQENSKKNDLSDSADSEGESTHVDEQQAANGAADGTQTIKKKKRKRRYADEYYDRTDPFIDDAELYIEEKAAATKDGFFVFSGPLVAEGDTVKIERSKKTKKKKKTSLSNATHPAPAVSAVVASADASFDDSRDIESEDEQPLRTLSIEMAAKNALKEAKRENAKVPKDVSKKEAKTTKSKEKATKKTSSSVPKQSTGENTKKAVKLETPLTSTPPIPPLSEPKHSPATVNEHISPPSALTNPSTEELKPSTSLPIDQGNASVVSKPTQQVSIVLSQNASLPVDEHQAEPEKSIPTSSIP O43088 RBA50_SCHPO SPBC947.13; CHAIN 1..452; /note="RNA polymerase II-associated protein rba50"; /id="PRO_0000374018" MENHRSVFSNVIGDIVEKPPKQLVEVKRSVQRHARGFPAVSRTLPKRESKSMSAYKEKMLRKNKESPGLEGKGNLDDQGIDEENRVRLERMNDLEIEGAQEEIRATIRDDLLEMLKKRAFKKKAERELAQRKDRSSQVNTPDLSQRPSDDSFLSNEKLRSSEKLNRNLQSVLSSEAVDSSSGSPSPPMALSQAEIRSRQTKRVMFPDKAEELTKIFSLPTLAPIKGNEEDDASEDAKHSPKKHSPALSDGTTSNDGAPLEFDTTHLPEKQVTLDPNDPSFYEQLHDKYFPNLPVDEKQMQWLHDPSPAENSYHPSVESLHAHEIRFGFKGEIITPSQSQTIPVNEGLHHHGDAPFSAGYTLVELAHLLRSSFPTQRCIAIQTIGRIIYRLNSGEFREVLSPELHTLVEDAHIYELLAAAASDQVKHLTVRSLAIEALWLCSQSQHGSSRSAV O43090 NDH2_SCHPO BINDING 92..122; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 255..291; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9; CATALYTIC ACTIVITY: Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+); Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; TRANSIT 1..35; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC947.15c; CHAIN 36..551; /note="Probable NADH-ubiquinone oxidoreductase C947.15c, mitochondrial"; /id="PRO_0000337258" MSVSKARLQSVVRLSRTVPYSKTMVRSFHVSCAVKNSGNVPTPRNKSFFSRALEMAEVTSSLSMLGAVALFQSLRRLNNSSPKGKSGVPKKNIVVLGSGWGAVAAIKNLDPSLYNITLVSPRDHFLFTPMLPSCTVGTLRLPSITEPIVALFKGKIDPSNIHQAECTAIDTSAKKVTIRGTTEANEGKEAVIPYDTLVFAIGAGNQTFGIQGVRDHGCFLKEAGDAKKVFNRIFEILEQVRFNKDLSPEERARLLHITVVGGGPTGMEFAAEMQDFIDNDVKDMFPELQKDIHVTLIEAAPGVLPMFTKSLITYTENLFKNLNIKIMTKTVVKDVNEKNLIVQKTNPDGSKAMQEIPYGMLVWAAGITARPLTRTLMSSIPEQSGARKGLIVDEFFRVKGVPEMYAVGDCAFSGLPATAQVANQQGAWLAKNLNVEGKKFALHERIQALEKQLGEKEAPSQVAGLKQQVEQLKLEPFKYHHQGALAYVGDEKAIADLKLPFMKKMLPLQGIVGHTFWRLAYLNELISARSQFMVLIDWLKTRLFGRYDAKV O43092 OXA12_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP4H10.03; CHAIN ?..409; /note="Mitochondrial inner membrane protein oxa1-2"; /id="PRO_0000020359" MFSVIGRGIKFSSKSHYSVSCFLIATQGAKIRQIHTHNTFFKNFSFAKLGRNQRTSSLIKIHNSSTSFPKSRSEKVVYTPSLPLSSSVLASFSFLPHNILQNGLNTLHIWSGLPWWASIAACAVAMRIAVFPIMLKMMKTSAKLAIINPKVAEHMSVLSKAKAEGNSELMMQATTQIQNLYKVNNVNPLNLLSAPVFQGILFISFFYALKTMAGVPVEGFTDGGFWWVNDLSQPDPLHIFPVANGLLMLLNIELGSETGSNKVAMSPSMKKFFRFLCLASPLFTMNFPMAIFMYWFPSNVFSVFQGAFLRSSTIRHKLGLPEVPSAMPVPNAQNESFVKSFTDIVHGVQEKGKYPQASEILDATRFLKTDTNNEQKPTNNSTITKATTLSDNSQNDKSSSVTKPTEKKD O43120 UAP2_SCHPO SPBC1289.02c; CHAIN 1..367; /note="Splicing factor U2AF-associated protein 2"; /id="PRO_0000082003" MSSQPFWDERIHRWRCLGSEGNELIYIDEEQTWKDYDPNSLKMNKAGSTGAEVSDVTAEATEGKESSNGEDRHTKRLYESTSAEGYPSGSRNKKSKSENSEASPAPVINKAVYIQGLPLDVTVDEIEEVFKKCGVIAKNIDNGTPRIKIYRTEDGTPKGDALIVFFRSESVELAEQLFDDTEFRYGSGQKMRVQKANIDYKKEKTVNKDVGGALKKKALRLRQQQMQQISSWDDVDEEVDDKRKKRFNKIVVLKHIFTLEELDKTPELLIDLKDDITEEAEKCGRVTNVVLYDKEPDGVVTVRFSNNEEAEACVRLMQGRYFDGRVVEASIYDGKVRFQKSGKHTLDDEEDEEKRLEKFADWLENSN O43125 CSH3_SCHPO SPBC119.05c; CHAIN 1..296; /note="Protein csh3"; /id="PRO_0000079396" MDHKNYLNHVIRGIYNDFQFLVDEGVVERSALDWVHANIHLQDGPASPVTAPAAQPVESSVPLPLPKRKSSVEKRAGSVASAVAAMSLSQNSGEKRTPEEPRKLPGVPAPQKQSEASSVNSSTEKLPPPPSYPGPNTAHKNVERVLAMYDFPGPDAGDLGFHAGEVIIVLEHVNNDWWRGELNGKEGIFPSNYVRLLEDSAVKAQPPPPPPQQNYPPAASSSAPPMQYQQTAYPPQQAPYPPVQAYPQAPQQPIVVAQPTEHKHSSTFKKIGSGLGSAFVFGAGATAGADLVNSIF O59667 HIS2_SCHPO CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide; Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, ChEBI:CHEBI:59457; EC=3.5.4.19; CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31; SPBC29A3.02c; CHAIN 1..417; /note="Histidine biosynthesis bifunctional protein his7"; /id="PRO_0000352786" MALLPFFDLTNFESDASEELGWLKYVGRVQTRVFPQHFKDNLEKVRKISETIDVIVDTTAELGPEACVNLLNAGALAILVNEEMLNELADISPNRLVLKTDTTDIGKIEKLSQVAGSIQWIGSAENYPPDFFERASKIIHKAVMPEGGGRTLYLEFPEQPSMEVLKSFSVHSVVPVLSSSFLTVKPAEEPKKLSLADLILISANTDREDGLFSTLVVNELGIALGLVYSSKESVAESLKTGTGVYQSRKRGLWYKGASSGAVQHLIHIDVDCDEDCLRFVVYQTGKGFCHLDTLHCFGQASGLCQLEKTLIDRKNNAPEGSYTARLFSDPKLLRAKIMEEAEELCDATTKENVIWEMADLMYFAITRCVGSGVSLNDISRHLDLKHRKVTRRKGDAKVAWQEKLKDKGGVANTSYTA O59671 ELOA1_SCHPO SPBC29A3.08; CHAIN 1..263; /note="Elongin-A"; /id="PRO_0000058505" MYSLKDLCIQVAQKHVHDIDDIGDCPFELVKPILEKARPEHLIDLEEKSPHLKVDTQPLWKDHVLRDFGLELQKRTILNNIDDWRGLYGKLKKKRNAHYNVASAKLRSAYTKLEQSKQNKRIVPLEREPRAARPPKRPRPMSNYCPKSSLMARAKSDFLKKASATRHIVSATSSSRSFPQLHPLGRSSSNATNTSTKRPLTSNTYPSIPLPPKSFTSQNFKSFNAVKTQPSSSSSPSISRPTSFPMSFFPNPSRFSSQVPKRI O59675 RS9B_SCHPO MOD_RES 89; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 179; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC29A3.12; CHAIN 2..192; /note="Small ribosomal subunit protein uS4B"; /id="PRO_0000132702" MPSAPRKQSKTYKVPRRPFESARLDAELKLAGEYGLRNKHEIWRVALTLSKIRRAARELLTLDEKDPKRLFEGNAIIRRLVRLGILDESRMKLDYVLALRIEDFLERRLQTQVFKLGLAKSIHHARVLIFQRHIRVGKQIVNVPSFVVRLDAQKHIDFALSSPYGGGRPGRCKRKRLRSQQEGGEGEEAEEE O59677 RT23_SCHPO BINDING 200..207; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" TRANSIT 1..54; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC29A3.15c; CHAIN 55..476; /note="Small ribosomal subunit protein mS29"; /id="PRO_0000372636" MLPKFRSRSSIIKNTERISNILSGGKLTVCGSKLGGLYTFEKCTFNKYYSSSQYQHTGRPVGGNIHSSSNQQRQKNSEAPRINEIPPSTSSVEKSTTIPNSSVVLDHLLNEGENTLEEVKPSEIHPHMSWSSKSEGKMFKIPEELLNKLNGFGALEKQKKSFSFFTSASLLHRKITTELVNVLQRSKDQGTKDGRFLLDGAPGSGRSIALIQAELFALSQPNFIVLPVHNCEGWVNSTSSYGYDEQLKLWVQPDLIKGFLTSVMKTNSDKLKKLKTFESHELLQNECIPAGTDLLSFLHKLIASSNAPKSLEIFLQELNNNTKSNSNMKVLLVIDNISILSVVTKYKDKKNNFLPPKDFYFINLLFKYISGSLTFNRGTVLAATSSQPRVSTPSLDIALGVAHRNPYKSSDETILDSLQSVHILNMEPYTLDESRRMMEYLVSSNVCLEKVDNYLQNHVLSGGNPRKFFDACTRLA O59678 RRS1_SCHPO MOD_RES 34; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC29A3.16; CHAIN 1..166; /note="Ribosome biogenesis regulatory protein homolog"; /id="PRO_0000185378" MSAQIENSIPLDFDLGNMAAFDISPLDETKLSGSEKESFLFSLSRDNVQQLVNKMISLPKERTSDGVLLQLPETVTPLPRAKPLPKPKPETKWQRFARIKGIAPKKREGRLVFDEASGEWVPKWGYKGKNKELETQWLVEEGEKEKKLTSKQVRNTSKKIKRSRRH O59679 GEF3_SCHPO SPBC29A3.17; CHAIN 1..525; /note="Rho guanine nucleotide exchange factor gef3"; /id="PRO_0000255583" MSNPRMFQSRGKRVVSDSLPIANSTHTLEDTLKLRPDWTIALSQHETETRSTRTSCSTTTESTIAMRSKQKAIISVLEEFRDSEAAYVHDLHVAQRYYADRLSDRVKKSEWKDVFEIFLVLCKQASLFEIEMHKSLNDEINYILDDQDACLKPKPSVAQLFLSWLPKLSAVYGRYCVIQENIGKKVEKWMKNSSISEYLQECDSMAKIESNSWNLDSFLVKPVQRFLKYPLLLNQLYRSASLGIISDYVLLGEACHKSEIASQRMNELKRRRDIIITALDSVSNSQEVLLLSTDSIDKKIAKLQNSTNIFYVPEHEPILAFVHQLSSSYTNLLNLRSAICDWLKFSRYHYLKFFTFVEAYSVFCKDTKSADKWALISVALDNIAKGAVLRLTEQCQTSVLRPISNGILFFRNPLCVTDVWIKKATAFSKRRQSQVFEEDLESFPLLSNCLLEELPLFLEMARNVTDECILAFAQIQATFYDTIQKVLEPVVAKFNLTDHQDIPSIESIMDFTSLRSSMESSPKSK O59682 SPTC1_SCHPO CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000250|UniProtKB:P25045}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P25045}; SPBC18E5.02c; CHAIN 1..509; /note="Serine palmitoyltransferase 1"; /id="PRO_0000309453" MSYSYPFFDDVYAYYNQTVTFFGKALDVLPGSPIVKRYIKSSYQNDPLRTFIEFLLLVFAAYYVLRKPRTSPDNNYVEFTEKEINELVDDWKPEPLVAELTDVEKLELKSIPVLESVHLHTKLIDGRPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQELEDDFVKHNRPLTRRFIITEGISENYGDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAALPASLAVAAYEAISILSRDGGSMLNDLRSKSALFHAKLSRNKFFETSSDIESPIIHLRFKDKDISHDKQVFLLEEIVELCIAEGFLIARAKRVESLERVKVQPSLRICISTGHSAEEIEKLALLIKEKTEIVFDKHKVINQV O59683 IF2M_SCHPO BINDING 178..185; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 226..230; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 280..283; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1271.15c; CHAIN ?..686; /note="Translation initiation factor IF-2, mitochondrial"; /id="PRO_0000014482" MAFLSACTSWRHVHNAGFTFITKFPFVRNVHKLSYHISPLSSRFSLADISVKENNHPNGPQLRLQTHFFHSSSPMHATKGFRFPKSSTPLTLPAVLSVASFANLLQIPTRRILRDLNRLGIKDVFPEYLITYEYSSLLAEEYGFDVQEAAAYSAPSPKSLNSKKDSGPLRPPVVTLMGHVDHGKTTLLDAFRKSTIASTEHGGITQKIGAFTVPFDKGSKFITFLDTPGHMAFEAMRKRGANIADIVVLVVAGDDGVKPQTVEAIKHIQSADVPVVVALTKSDRPGTPIHKIYEQLLNNGIQVEALGGETQIIPISAKTGKGIPELEAAILTLAEIMEIRASPRDPFQGWIVESSVTKGVGSSATVVVKRGTVKKGMYLVAGKSWCKVRSLVDVNKKSIKQVLPGQAAQVYGWKDLPIAGDLAYEVKSESEAKRILSDIYRQSNEQNFYELAESQNEQRVSALAAKKSGPAAIQEETSVSKSFNIIAKCEDTGSMEALSDYLKPLQFGKVKSRVLYTGVGPVTETDIERAETSDAIIISFGVSVPKATFRLAEKHNVKLLFHNVIYHLMDDVRKLFALRLPPILVQRVTGEAIISAIFDIKAKRAVVHVAGCRVTNGTIEKSHKIRLVRNDKIIWSGEIDSLKHLKEEVTSIKKGRECGILLKNFDEIVTGDKLQTFVEEYKPPDF O59698 YN41_SCHPO MOD_RES 99; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC36.01c; CHAIN 1..580; /note="Uncharacterized transporter C36.01c"; /id="PRO_0000173448" MSESSVNADTPKNTNDVLNGAYQSATTEPEGQYRSATDNPSLYQVPTHGSLYRNLSNSASAYYPANGNMNSREPANELSDISSLAEKGELEPPMAKLLSDPDFQGKQFPTVEAPELFIFELAPDSPSIALNWTFWRKMKTTSIYAYASLTIAWGSSVLSPASATLAKKYHIGMTTSLLNVSLFMLGYCLGPICWAPMSEITGRKTPLYIGLFLFSVFQIAVATAQDIQTIMICRFFGGYGACVPLCVVAAAFADMYPNRYRGTAITIFAAVIFVGPLVAPIVGGFLTKSYLGWRWTEYITSFMGFLSIILIYLFCEETYLKTITENKVQEYREITGNQLVHARSEEESLSARDIIMNYLLIPLKMLATEPIVFLVSLYCSFVYAIIYLLLEAYPVIFQEGRHFPLGVSALPYIGILVGVFIGCGINCLFEPWYFRQVIKAGNKPAPEARLPPMMIGSFLFPAGIFWLAWSGYYTYVHWIVPTLSGLLTGAGILLIFLQCLNYLLDAYLFRAASVFAANVIMRSAVAGGFPLFAVQMFHNMGVGWAGSLLGFIATALIPMPFAFFFFGKKIRAKSKMTAQF O59699 YN42_SCHPO SPBC36.02c; CHAIN 1..577; /note="Uncharacterized transporter C36.02c"; /id="PRO_0000372792" MSSTPTAEELALQNTVSQSASAHPELYHTVSHASNNSYQLPQLSRSATSNFSTSARFAARYPTTAGESFQNLTPVNSNPSNQNSKTEPNPDDVEKCIQDPLLQVFPVVEEPERFVFSIDPKSPLIAVNWPFKRKLKTTCILAYVALCSSFASSVFAVPAEAITTVFHISLTVSLLTMTVFLLGYCSGPIIWAPLSELSGRKPPILIGMLGFGIFNISVAVGKDIQTIMMCRFFAGFFASAPLTVVAAALADMYSNKYRGTAITLFSAMVFDGPLVSPIVGGFLTKSYLGWRWTEYITSFMGFFALIIVYLFCDETYSKAIIQGKAKEYRAITGNYFVHAKSEEEVLTLSDIAKNYLLVPMKLLFTEPICFLITLYSSFVYAILYLLLEAYPIIFGEKRHFSMGVAELPYIGLLVGVFIGSGINIAFEPWYYRKCLAQGGKPDPEARLPPMMIGCFMFPAGIFWLSWSGHYSYVNWVVPALSGLATGCGILLIFLQCINYLIDAYLFRAASAIAANTIMRSAMAAGFPLFAVQMFHNMGVGWAGSLLGFIATALIPMPFVFFFFGRKIRRMSKMAVDF O59700 YN43_SCHPO SPBC36.03c; CHAIN 1..538; /note="Uncharacterized transporter C36.03c"; /id="PRO_0000372793" MYNNNSSTSSDSSNSEEKANAQHASSTDSTSEHTDPAVADEGFPAEQYQSADLEKQQLLIEEGPGGFPYITNPERFYVSLEPSDPRLAVNWPTHVKILHVALLAFTTLTASWGSSVFSAAATIFAAKYHIGLTVALLGMSLYVCGFASGPILWAPISELVGRKIPLIVGMFMFSIFSIAVAVAKDVQTVMICRFFSGFCASSPLSVVAAAFADMFDNKTRGPAVCIFACITFAGPLIGPIAGGFLAKSYLGWRWTEYITSFMGFFSTLCLLFMKECYSRTITEQEAARLRVEYNNNFIRAKSEEEYIDFKALAKRYLAVPFVLLFCEPIVFLLTLYMSFVYGILYLLLEAYPIIFAEKRHFSLGVDALPYIGLLVGVILGAALIAYFQGYYNRKLDANGGKPVPEARLPPMMIGSVLFPAGIFWLAWSGYYTHVHWIVPTLSGLLTGCGILTIFMQSLIYLIDAYLFRAASVIAANTIMRSLVAAGFPLFAVQMFHNMGIGWAGSLLGFIATALIPIPTLFFIFGKRIRLMSKNTVNL O59704 ELP1_SCHPO SPBC36.07; CHAIN 1..1253; /note="Elongator complex protein 1"; /id="PRO_0000339337" MKNLVTHLHHVFPNVNGSIKALAFNSISDKIYVVCGLDNENPGIEIYEISENDDVSKLVEFDSPSFVSDNGDIDEIQSMQFLGEPMAICLSLKGGDIVMVKVDPSPEEAPWEIIGNVENGIVASCWSTDEQVFCIITGGDTILFMTKNFDIISETSLSDADLNEFNKHISVGWGRSETQFRGKRVRAKLRDPTLPEKIDEGKLSDVDDGKTYICWRGDSQYVSINRLEKGPRRAIRVYSREGLLDSISEPQDGQQSLLSWKPSGSVLATIKSDSSDNSSKVIFFERNGLRHGEFSLRRREDEKYTGLAWNVSSSILAVSTENSVMLWTTGNYHWYLKKEINIPQNALISWHPEHANTLYITGKNHIEKVVFDLKYVTEFSTSPNDFGLIPVIDGSSLLVTPLSLCNIPPPMCRYKLSLDYNVQMTSINATSDMLFAADDRRLTAFTFNSQEDIAKFGEFDISTYAEGLNFKSLLGLSGNQVLLLADGTNNCSKFFVFQCDEDNESLKLLASESFESCILNASYCSEMLFFQTSSGKLISYNLNVKSIESISLSFPKPCSDFVVVPVHETFVPIGLTSYGRLYAEQRLLSTGVLSFFCTERFVLFTTTKNLLKFVHLVSTVDDLQVVEDDAVDRHDERCRVVERGSKIVASMPSKMAVVLQMPRGNLETIYPRIMVLDGVRTYIKALKYGDAFKVCRTHRLDLNILFDYDPDLFLKNIPVFVDGLYRVDYLDLFLTSLKPENVTTGMYSDTSKSQSQQSVTTIDNKVNLLCKIIREHLTSKYGDTHFQAIITSYLCESPPKIEAALGMISGLIKAQSETVDLAIEHMCFLVDVNMLFDHALGLYDLKLALLIAQQSQKDPREYVPFLHEFQKQESLRRKFNIDCYLKRYERALGHLKEMENAFDEFKNFTIQHKLYPRALELYKYDKEAQKEVLIIFAQYLRENGKSNEAAIAYESVGKISEAIEAYKSAGMWRECLSILQQTTNSEDLIRETAEDLASLCIEKREHCDAGSINLLYLSNPREAVIQMCKGSQYSEAIRIARATGDSSIYKDLLISVLGESFGEASELVADFRNQIKSQTERILVLREKKKEDPISWMEGTMEDQTPDDISLASTSLSTNRSLYTQYTKSSNSSKMTRNTSKNNRRLERKRARGKKGTVFEEEYLVNSLRRLIARVEEIRPEVHRLLEALVRCNMTTQASELQRNFANVIGTIGEKVIPILSVPVSTFETALGEQPQAPVVPNVKPFEKLSILI O59705 COG2_SCHPO SPBC36.08c; CHAIN 1..191; /note="Conserved oligomeric Golgi complex subunit 2"; /id="PRO_0000339334" MTEKDADSGSDLVDAFLSDAYLNTEELRKDGPFSPDEFLVSKRFLGLDGLVNELSRLFEQVNNELMLLVKDNYQDFVHLGSRMKSGNTKVSTLISSIHRSEEQLKNSKQSLIGHSTEIQNNLKHKQDVENEKLIASNLLLLDQILKFLKSNDSSHPLWLESLNNAQRLCDTYKDHPWVQSISPTLINYIKH O59709 GIT7_SCHPO SPBC36.12c; CHAIN 1..379; /note="Glucose-insensitive transcription protein 7"; /id="PRO_0000185392" MGVDLSDINDSLFKLSDKLSNDLAKQRNLCIVKEPSFSIEEHIKCFTTCINTYKPFSCLKHANWALLLAKKKSDTGLIGYCQSLRGLAYYLLEQYQSSAICFGFALKHLKKEDLTKWQVQLDSMLTIVHEQQNQDTSSLIPDECPNIPELEAAKIEGDEEFLNMSLKAPEGQIEKNEEKLSNRIRYDWSQTSFSLNIDIYAKKVKDEDVSLLMEKNTLKIEIKLEDGSIFSLVLDPLYEEIVPEKSSFKLFSSKVEITLIKKVSEIKWEALVKSPANNSVNVYAKDSNHSSASGNTKNKAKDWDSLAKLADLEEDEPTGEAALANLFQNLYKNADDDTRRAMMKSYTESNGTALSTNWKDVKSKTFETKPPQGMEPKKF O59711 LYS9_SCHPO BINDING 9..12; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 32..34; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 54..55; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 75; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 97..98; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 98..99; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 124..126; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 125; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 174; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 223; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:Q9P4R4"; BINDING 244..246; /ligand="L-saccharopine"; /ligand_id="ChEBI:CHEBI:57951"; /evidence="ECO:0000250|UniProtKB:Q9P4R4" CATALYTIC ACTIVITY: Reaction=H2O + L-saccharopine + NADP(+) = (S)-2-amino-6-oxohexanoate + H(+) + L-glutamate + NADPH; Xref=Rhea:RHEA:10020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:57951, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349; EC=1.5.1.10; SPBC3B8.03; CHAIN 1..450; /note="Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]"; /id="PRO_0000316856" MPSILLLGSGFVAHPTLEYLSRRKENNITVACRTLSKAEAFINGIPNSKAIALDVNDEAALEKAVSEHDLTISLIPYTYHATVMKAAIKHGKHVCTTSYVNPKMAELEEAAIKAGSICMNEIGVDPGIDHLYAIKTIEEVHKAGGKIKSFLSYCGGLPAPEDSNNPLGYKFSWSSRGVLLALRNSAKFYENGKLVEIDGKDLMETAKPYFIYPGYAFVCYPNRDSTVYQERYQIPEAETIIRGTLRYQGFPEFIHCLVDMGFLDETAQEYLSPEAPALPWKEVTARVIKAESSSEADLIKKISSIHKFKDEDDKKRILNGLKWLGMFSSKPVTPRGNPLDTLCATLEELMQYEEGERDMLILQHKFEVETKEGKRQTRTCTLLDYGVPNGYTSMAKLVGVPCGVATQQILDGVINTPGVLAPNDMKLCGPLIDTLAKEGIRLEEEIIDEE O59712 YBH4_SCHPO SPBC3B8.04c; CHAIN 1..867; /note="Uncharacterized transporter C3B8.04c"; /id="PRO_0000303946" MKFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDEETRLLEHERRSPDDRFMFALDKELQGIVEFYAPKEKEIADQYGRIKGEFETYENEYMSQGNNINYPTPERLQKSSASRKSGRMARSQELPRITSSNREIYLNGQTSDGGYAAPAISRAESTAIQPSEPHDVDTSKNGLSKKQHSEAQPEVQGNDDEVEEEDDDDDDEDEDEDEDEDNNNNNRWLLIEQYPSDIVAYENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKTLGSSLRESYMKRVNQAYPFLPATGKTLSKRLNIVAEWYAKLCCQGDTFVAIRRLRGHLREYVAWERNTIWREMMAMERRTQAARLSGLKPVAADEKESEQPPYFTIKTKFGVFRIPRCFFNSTIATLITIIVIFILLLSFPVIDNREQNNCLALLVMVSLLWATEAIPLFVTSFLVPFMTVFLKILRDENGSPLSGKESTKVIFSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAESDFAKILIVGIALASNVGGIASPISSPQNIVALQNMDPAAGWGEWFAVSIPVSLLCIFSIWFLLSFGLLKDEHITLAKIRSTKDTFTGVQWFISIVTIGTIVLWCLERRFDEVFGDMGVIALVPIIVFFGTGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVSSLNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLADPHPRLFVLASGMMCSLAMALPTSGFPNMTAIMMENEAGKRYLKVSDFLKAGIPATLISFVILLLIGTPIMRALGF O59725 MIC60_SCHPO TRANSIT 1..38; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3E7.05c; CHAIN 39..550; /note="MICOS complex subunit mic60"; /id="PRO_0000372365" MNRQLRTVKSCFSLQKTHQYRSFWIQSSLRALPPDVKQNKTEPIPFVPKPEEGSSNKSNSSKFRKRFLLLFLLGITGYSCSVVYCFKDPNFYDYFAEHTPFGKQVLYNVEQSWIGYKYLGGNRIKVDDSSPKLKQNSNNISKKQNSSRNDDTKVKKDTTIERPESLVVEIVDLPSEVTKDTAEESVWKDIGLDQETGLSVTAIPIITETLDHAHEQEIKDQSLRFESSLNEANELHGKLSKIQQEQEHLFEQRLREKVSEMESKLEALLIARDEKWQSAFESEKLRLQKLHEARLQQELFKLASVFESKLKNELTEQAITLEKLHLQSIKAQVEQERGSRLGRLQELRNSFQQLQELVRVVLHENGRVTRLVDVSNTLDDLNKDMRFHKLSEVRQHVNTLKEATKDDELAALASRVIEKIVDSGPILDKEELQTKFDTLSKEIYKTCFLTTESGFFGHLKSIILSQLPAAVFKSPDIVSVKKTLEDARSHLLKDDLDGSVRALLSLSQWPRALSRDWINACRRRMELQQAIEIIKASATLSSQLEDAQQA O59729 SLPI_SCHPO SIGNAL 1..25; /evidence="ECO:0000255" SPBC3E7.09; CHAIN 26..659; /note="Uncharacterized protein slp1"; /id="PRO_0000363387" CARBOHYD 94; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 111; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 128; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 142; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 393; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 415; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 495; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 504; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MVKRRLSAFGNAFLIYFIIFRLCCCSPQTSHWCKYPALCLKSPDTHNENLVCDAYLSVIATKSEEKEASNPTTWDFTPTNKYQEPSFHTKTSLNGSDTISSNFLSKYEYSNGTSTSEFIDSISPPLVNETSTISSSKKLEQNYSVTEVIDTNIITSSSVTLPISEDGSSTSAAATIDSNIDEKTVAFSEEKRFNFASTDCAAAVIKTNPEAVGSSSILTENKDKYMLNKCSAENKFVVIELCEDIYVDTVQIANFEFFSSIFRDFKVSVSGKYPKYESSWMELGTFTALNLRTLQSFHIENPLIWAKYLKIEFLTHYGSEFYCPVSLLRVYGKTMIEEFEEANEDFLEQKVNDGSAIKADEIRKPQESPIFVDEEDTDVQSKPVRKNPSVELNSTDTLLSSTVISKSLSTVVIGNETGKSESYPATSTRSFNDISPSSSSSYSTAQISTFPSNQESIYKNINKRLSTLEERKKAFDEIVEKILTNYGKHNAKNMNFTQLLHELNSTLQLEISKLSKSVVKPSLFALQAKLELLSAENEYFQSQITSLYQESSFQKRLLMLQLTVLIVLTVYMAVSRLPENLPTTRSSSNNPIEASRPPFSRDEQDISKANDFRVSASSAVYTVGPELLQRKKRDPNTSIRSIHEREQDKIIHSRSHSVC O59733 SYF2_SCHPO SPBC3E7.13c; CHAIN 1..229; /note="Pre-mRNA-splicing factor syf2"; /id="PRO_0000072379" MDSPSHSREARVEKLKKIREQMRKSSHENRKEVVQEHSRMRIDPALERRLERKRMEAEEELAKIETEEEGGDFERRRAWDWTIEESEKWDQRLRKKKQTIQNVAFSDYHSQASKDYNRGIRDLKPDYEKYDKDKKEEKSKSRSVALYDEAERLDWVSNKPDKEHVERLVESIKKQDQRRLKNTKRRGTDEEDHITFINERNRKFNLKLQRFYSKYTKDIKEDLERGTAL O59736 LEU1_SCHPO BINDING 54; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P9WQB3"; BINDING 262; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P9WQB3"; BINDING 264; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P9WQB3"; BINDING 298; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250|UniProtKB:P9WQB3" CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13; Evidence={ECO:0000250|UniProtKB:P9WQB3}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P9WQB3, ECO:0000250|UniProtKB:Q9JZG1}; SPBC3E7.16c; CHAIN 1..584; /note="2-isopropylmalate synthase"; /id="PRO_0000140445" MKSTFEAAGRVAKGMLKDPSKKYKPFKGIQLPNRQWPNKVLTKAPRWLSTDLRDGNQALPDPMNGQEKLRYFKLLCSIGFKEIEVGFPSASQTDFAFVRHLIETPGLIPDDVTISALTPSREPLILRTIEALRGAKNATVHLYNACSPLFREVVFRNSKQETLDLAIKGSKIVTAATKNALESKETNWGFEYSPETFSDTEPDFALEVCEAVKGMWKPSAAQPIIFNLPATVEMSTPNTYADLIEYFSTNISEREKVCVSLHPHNDRGTAVAAAELGQLAGGDRIEGCLFGNGERTGNVDLVTLAFNLYTQGVSPNLDFSKLDEIIRITEDCNKINVHPRHPYAGNLVFTAFSGSHQDAISKGLKAYDERKAVDPVWKVPYLPLDPHDVNSEYAAIIRVNSQSGKGGVAYLLKTNCGLDLPRALQVEFGSIVKDYSDTKGKELSIGEISDLFYTTYYLEFPGRFSVNDYTLSSNGPQSKCIKCVVDIKGEKKDTPSRVVIEGVGNGPLSALVDALRRQFNISFDIGQYSEHAIGSGNGVKAASYVEIIFNNTSFWGVGIDADVTSAGLKAVMSGVSRASRAFAK O59737 GYP1_SCHPO SPBC530.01; CHAIN 1..514; /note="GTPase-activating protein gyp1"; /id="PRO_0000312835" MESQSKKSSALKTLSSLWNGSSSATSDPVTVLDRSRTHHHRGRSTSSKAQPFRLDDSVYSDQPPKDHISLARSITRPESASESKIYAPSARSSLSLEAVVGKKVSAKFAKYLSQTDDDWGVSNIKASKSLPRMARSTTPNSSSRSLFPQNGVDTTTSRQKLHSSGRFPLPAKLAHRSVEVEVAESNALVSRIKKFSRILDAPIVDLNALRTLAWNGIPSEHRPIVWKYLLGYLPCNASRREVTLKRKRDEYNAAKDSCFNTNTEPPPLDQTIWRQIVLDVPRTNPSILLYQNPLTQRMLERILYVWASRHPASGYVQGISDLVTPFIQVFLSEYIGDKDPMTYDIALLDETNRNDIEADAYWCLSKLLDGIQDNYIHAQPGIRRQVNNLRELTLRIDEPLVKHLQMEGVDFLQFSFRWMNCLLMRELSISNIIRMWDTYMAEGVQGFSEFHLYVCAAFLVKWSSELQKMEFQDILIFLQSIPTKDWSTKDIEILLSEAFLWKSLYSGAGAHLKR O59739 BAG1B_SCHPO MOD_RES 144; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC530.03c; CHAIN 1..206; /note="BAG family molecular chaperone regulator 1B"; /id="PRO_0000088880" MSFFTQLCSMDKKYWISLAVLSVTVLISALLKKRATETEDIVVVHYDGEKLNFVLRQPRLNMVSYTSFLRRVCNAFSVMPDKASLKLNGVTLKDGSLSDQNVQNGSELELELPKLSPAMQQIEAYIDELQQDLVPKIEAFCQSSPASAQDVQDLHTRLSETLLARMIKLDAVNVEDDPEARLKRKEAIRLSQQYLSKLDSTKNQNK O59744 YN28_SCHPO SPBC530.08; CHAIN 1..815; /note="Uncharacterized transcriptional regulatory protein C530.08"; /id="PRO_0000310391" MDNESHSQETESKILEGAKVATRRRRVTRACDMCRRKKIKCDGLRPCKNCKAGKLECTYHMPSSRKSSFSPEYVENLESRVRYLETLLKKNTNFDLSSNSPSFLFFLREQKFQATNELENMSPERKVIFTSMINYGNLFVDAKHGTRYFRGGSSIHVLIQHLIRRLPGDFEICEPYSAYPLGNKNIQFDDNDPEYQFFTPTPRFSIDFMVSSVDPREIQLPGIEEALCITKAAVSYVSGIVFYTTYADFPKKIRLLYSGNYQGNFFPLFLSILCVGYYHHLLNNPSNTELQSLIKKYSFYSERLVKSADNFTIESIQCLLILSIYRYCRTEISAAWYYMKLGLNCCLRLGLHRNITEGFTEEQIDSRRRIFWAIYCYDRQLCTLFGFPLGVRDEDIDQCLPVTPKFPSVTEIEANARLFFFHGVKLYKISSRILTKLYSPNSRNVTKKHISYAVIQDLEQLLDGFYNSLPRVFRAEQPGEFQANHFFYNLQLVYYSFRMLIYRPLLHYLEADSPAMQALKVPDRQTAFTLACKCVDSAIVCVQNLSHLSKGLKRTLDRYYWTTVYCGFSTIVTLIFAALLTKNTNLLIHISVARESIEALAHECVTRRLLPLIDKMRESLMKILESNADGYKQMSPTKAPQVFESESNVPINNGPQQSIDKESNSNTQLPQVETEGQQQSVFDGNIGTIPYQAYNMNEDSFIDINTLSSMLNYHTQAVSIHHPSFYISRSDVPLEEEFQIPNELLAVDPVAESMQENSDIINEAFGLVDPDVSDGKSRESSSLNNSTPFNPTVNIDPASILEHFSQNVMKDSQNS O59745 YN29_SCHPO SIGNAL 1..25; /evidence="ECO:0000255" SPBC530.09c; CHAIN 26..296; /note="Putative mannose 6-phosphate receptor-like protein C530.09c"; /id="PRO_0000316243" CARBOHYD 64; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 81; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 93; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 96; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 143; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 44..87; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"; DISULFID 147..183; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"; DISULFID 163..195; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" MRLLTCLINVLAGLTLFSQFQRAFGLTITRRGFKVQESDEEPFCALHHPNTGEYFDLSGLIRDNTSEKGDYSVNGYDFGTNFSINLCHPVVSNLTNYTVEGDVSSEDSIGGFFTVEDDDLYSIGQAAYKPYFRGKKLIMQLDNGSLCPKSNHIRMSTLISFTCNRDPYTAPSVITYVGNLNDCAFFFEWKTIHACPTVKKDSTLNPVSVFLLFCAIAFLAYFVGGFVYQRVVLNARGLRQIPNYEMWRSLFGFISDIVIILYSSILSILPSSITRMRGNRRNIDYVEDALIDDIDT O59746 YN2B_SCHPO MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC530.11c; CHAIN 1..819; /note="Uncharacterized transcriptional regulatory protein C530.11c"; /id="PRO_0000316609" MLENSTAVHGVRLSDSPEDPFLRKRLASNTQLNQKKIRFTENENDLSPERAQKEPVSIPHGRYTWSTSPDTDSSHLPSTPPTVDIPFHHPHTIHSPTFTLSVSPDSQSSSATHQNDYISSPHADFSFSPPASKIQSHEPLNDMAAVHPLRPSHVSGPLSPPEPKAASVDHSINPAYNASFRLPDGPLWTEGSENLPSLDIQLQLAHIYFIYAHGQPYVLFHRDSFMEALKSQRLPPVLVLAMCAVAIRFWQTDKYDKNELFEQWFNRASAIAMANFDKLDLVYVASFVMLSYVCAATSKYWMFAGMAIRMVVALHPNKTPNLPYYDRPDSPLPFEIRVQLTRRLFWDCFMLDRLNSLYCNTQFLNLEDIHVPLPMRETLFMYKAHAVTETLTGKPSSPDSFTNANPTTAPIVSRNAQDNMGMLAYMIRMVSIWGRVVRCLKSYSQKQSNPYPFWHAKSTFKQLDQELYEWEKNLPNRLRYSRQTLLSYHMMGQGGQFACLHLIFLQIHLYVHRYAASISSVPFSHVKSPPTVFENQSAVLASQCANAICRIIQDCTELSISLAAPFTASSAYLAGTVLLYHYITRGSEVQASKAAVHLPIAKRHLAQLSVYWPALGMYAKALDAIAFHQGALVTPSVPPVIATVSKTNTTNTGVQQRGNVGVTTTGSILTQSSPALPVQPVPLAYSKPAPTTKSSLTELAYNTNVSLPPRSPGTGSLAAGNLPNEKAPSLMTMVNGGPVPGDIGEASIPVVQNLQPSTAHVDPESDLGRVIKICDWYQSPSSDVLLSKPLQLNSSEEMEQQCIDLSRHNTLLNLSSYGI O59761 TYW1_SCHPO BINDING 97..101; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"; BINDING 187..221; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"; BINDING 357; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000255"; BINDING 361; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000255"; BINDING 364; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="4Fe-4S-S-AdoMet"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine; Xref=Rhea:RHEA:36347, Rhea:RHEA-COMP:10164, Rhea:RHEA-COMP:10165, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315, ChEBI:CHEBI:73542; EC=4.1.3.44; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250}; SPCC1020.08; CHAIN 1..688; /note="S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase"; /id="PRO_0000281834" MGYSLGYIGEHWEEYRAVLYIVLLLPVLIHFLIRRKTQLSNSDKSSEKKDEVKKQREVKRFKRVGKRGKIGSPSSSIRKQNDTIDWKNSPLCVFYSTLGGTAERYAKQVHEELSSLLQRDDIQLLNLDYVDLSEYFVSCPENAIYLVVLPSYEIESSIDYYLSSLQESFSDFRVPKDPLHGLSGYAVFGLGDMENYPGDKFCYQAIQADKWIKKLGARRLAPLGVVNTQLAPTAQIDALLQWTRSVAECLKNGTLLKIGNTDSLSSDVMDVEDMGSMMAKAKAEAALPVGTKEMVSTESPTYKALTKQGYSVVGSHSGVKICRWTKSAMRGRGFCYKYSFYGIRSHLCMEATPSLACANKCTFCWRHGTNPVGTSWRWKVDPPEMILQGILKAHYAKLKLMKGVPGVLPDRYEEASRVRHCALSLVGEPIFYPYINEFVSMLHEREISSFLVTNAQHPEALRNMGMVTQLYVSVDASTKQSLKSVDRPLFKDFWERMLTCLEILREKRQRTVYRMTLVKGFNMEQIKEYTELIRLGVPCFIEVKGVTYSGNSDQSPLTMKNVPYYEEVIDFVKKLIEYIDIHLQDLGVRYEIAAEHAHSCSILVAQTAFKKDGHWHTHIDYPKFFELIRTKKDFGPFDYMASTPDFAMFGNGGFSPEDTRFHRKKKTQTSKPISATISETATISEAAA O59762 GNR1_SCHPO SPCC1020.09; CHAIN 1..399; /note="Guanine nucleotide-binding protein negative regulator 1"; /id="PRO_0000343431" MDNCVNSFEDQKDDLVHKKKSQNFGYVCGSINLGTNVIAQSPTKPLNFFHSSRWSPDGSTILSLTEDQCLNCWNVPFSDLSKKADGPLNFSKHLSYKYQSPETVYSYSWYSRMKLDDPSSNLFAVSSRDQPIKLINFTTGKNKASYHMIDHQERYQGSHCLQFTNDGEYLIAGDKNCLHHFNIRTGCKEPVMTTVTHGYKVPLWEFSLKGIQSCFSLNPMDSKTLAVGTYSNRVGIYNDCGRRPCQLEFSIERGNGVTHLQWCEDGEKLYVGSRCSDKIEVWDIRYVRDMVYALEGHRGDTNQRILFDTDKKDEILAGGTDGSIRRWRNKDLVEETHVTGNYDLTVNTVQANPINMQIKCVCYGNRIYKYEKDESEEEDESKEKDLWTGTVSALQVWMD O59768 VCX1_SCHPO SPCC1795.02c; CHAIN 1..412; /note="Vacuolar calcium ion transporter"; /id="PRO_0000352843" MIERLKIAKNRLEAMNSFNFPAQDRHERAPLLGSEYDHSMARQLSLLNVVGMTKSVLMSSYFNLMLVFVPIGLIAGWFEWNAKSVFILNMLAIIPLASLLSFATEQLSIISGPTLGALLNASFGNAIELIVGVLALKRGELRIVQSSLLGSILSNLLLVFGMCLVTTGIRREITTFNITVAQTMIAMLALSTATILIPATFHYSLPDNANSENALLHVSRGTAVIVLIVYVLLLVFQLKTHKHVCHDPSEVEEETEPRILGLRSSIAMLAIVTVFVSLCADYLVGSIDQLVEEVNISKTFVGLVILPVVGNAAEHVTAIVVSYRGQMDLALGVAIGSSIQIALFLAPFLVIVGWIISQPLTLYFESLETVILFVSVFLVNYLIQDGATHWLEGVQLLALYAIVVLAFFYYPQ O59770 PSA7_SCHPO MOD_RES 104; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1795.04c; CHAIN 1..253; /note="Probable proteasome subunit alpha type-7"; /id="PRO_0000124101" MSSIGTGYDLGLFFSPDGRLFQAEYAYKAVENASTCIGIKCEDGVILALEKVVTSKLLKPRVNNRIGSVDRHIGIATTGFIPDGQHIVKRARDEATSWRDNYGSPIPGTVIADRLGNYVQLFTCYSSVRPFGVMSFVATYDSEGPHLYMVEPNGVYWGYNGAAAGKGRQVARNELEKLNFSSLKMKDAVKEAARILYATHDEENNKEHEIEMTWVGVETNGIHTPVPDELLQEAEAYARRIADGEEEDIAMQE O59781 GEM1_SCHPO BINDING 10..17; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 57..61; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 113..116; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 197; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 199; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 201; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 208; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 317; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 319; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 321; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 328; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 428..435; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 459..463; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 527..530; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /ligand_label="2"; /evidence="ECO:0000255" SPCC320.04c; CHAIN 1..630; /note="Mitochondrial Rho GTPase 1"; /id="PRO_0000239339" MKEVRVVICGDQGVGKSSLISALIQEDNVTSIPKVFPIISIPSNPDSNDDVSLVLVDTQSDSNEREYLAAEIKKANVICLVYSDNYSYERVSIFWLPYFRSLGVNVPIVLCENKSEDLDNYQGLHTIEHEMIPLINEFKEIEACILCSALEKINVNELFYMCRACVIYPITPLWDAKERTMRKATIHALSRIFFLIDKNNDDLLSVDELNSLSEKCFSKNLSIEDASEILSKVKEICPEGVYEGQLTLPGFLAYNRVQVENGKQESTWGILRAFHYTDSLSLDDSYLSPKFEVAPGQIVELSPKGYRFLVDLFYQFDRDNDGALNNEELSALFRHTPGLPEIWVSSQFPNSTVLNEHGYVTYNGWLAQWSMITLFDYKTTLAYLAYLGFDTDGRGHNTDALKVMRKRVSQNRKVSKYDRNVFLCFVVGSKSCGKTALLSSFINNNTNRLTPNTVVNSVEFQSTQRYLVLSEIGETDLDILAEPKSLEACDILCLLYDSSNPNSFSFIANLLNLYPDLQKIPCVFAATKADLDRQQQRYPVQPDEFTKQLGLPSPTHISTAAIWNTSKEFFIQLAESAQYPASSIIRIPEEDSNKTNYQLVAALTAFGALLLSVGGSLTWKIIKHQYYSKK O59782 SULH3_SCHPO SPCC320.05; CHAIN 1..667; /note="Probable sulfate permease C320.05"; /id="PRO_0000303897" MSSPSENHLLGPKTSFIDNRTSTSRPLHEIPSYQSLARRSSTWKRANIPQQKPSLVRRINYYIPVLHWLPNYSLRNIIWDVLAGCSTACLSVPIALSFAQTFLGVPPIYILTGTAIGPILYCLFTACPLISIGPEAGMCLLIAENIHQRVLSKADVPQETAILVTGLIAFIAGIINLAAGLFRLGFLDALVSPVLLRGCILSISMIIMINQGSVFFGFSGVKYKGSDFPIDKLMFLIRNMSKANIYTTILSCITISLLIGCRNLKSKLSAKYPRIVSIPDAVIILLLGSFLSKKFDWHSNYGIAILGEIKTTILLPKLPLPEKNKLHFITQSLQTGVMCSFLAFIDTVIAVKAISLQTNNLIRSNRELISLGAANIGSSLFCGLPICGGYLRTKCNIMSGARTQVATIACSVLILLATFFIMPVFSTVPTCMLASMVVSLGVSLFADAAVEIFKLARIRVWWELGIIFSIATCTMMFGLETGIIFGLSITVMQIIRHSTRSRIMFRSPTSNGTAEFILEDAASTLSHRTNPSSTAVESAPRILVVRIPEPLFFANVSQLEDRLNRLEKYGHPRMHPGETPYRRIEDIEVVVFDMVGVSSIDSSALFAFQRILKEYVEHQVEVHLVSLDPQVLHIFEKHGLLDLIGGYDHVQDSIKKVDALCDIELGV O59787 SRP72_SCHPO SPCC320.10; CHAIN 1..561; /note="Signal recognition particle subunit srp72"; /id="PRO_0000135237" MSNHEEEIEELAQRIGKIEVGDTKSDIYQKVLNLIDIERYEHALKIIEKYLGETDAVYERAYCAFQLGKEDFSLEDKQFLQHLQAQKAYRLSDFSKALKIYEHLENDLPEQRADIRVNMLAAASQLPGLQLNNAVSLDDQDSVFNLATRYLTIGDWNQAIELLSSSLEKLENSDSNSEDHKSQINLCRLQLFFAYLQAGDNEKASKESLKISKDCLDETSQAIFVNNLISMSIDNPYISFRDLHGTNLEKALSSLLASQKKQFIRNLALLDMAVGKQRSVRKEKKRNPEESIYFSTILLREETKSLISPKKLPGYLENLFKSDSDNIVVALLLMQHKISNGNFRGALSIYQKLRTSLEASQSLSVLYSPGLVGLGDALHYKIQSTGFKSQLLHEAANYWRKQQSCEAKLLLCTRSLLAHLDERAPVSTIQDDMSVIDDLLQWKGPISELVSCKVAALCYLDKEIESGMDKYLVPTKDLITGIDVDDIEIRGVPVSAAIGPIKRSVEANSSNSSKKTRKRRKPTPKSFNPKATPDPQRWIPKRDRTNVKIKSKGKSMQGGVA O59794 RL17B_SCHPO SPCC364.03; CHAIN 1..187; /note="Large ribosomal subunit protein uL22B"; /id="PRO_0000125345" MVRYSAAPALETKCAKARGAYLRTHFKNSREVAFTINGMNLKKAFIFLDNVKEHKQAVPFRRFNGGVGRTAQGKEFGVTQARWPVKSVNFFYDLLKNAEANAEAKGLDMDKLIIKHVQVNAAPKQRRRTYRAHGRVTAYLSSPSHIEIIVAEEEEAVPKANDTVSRVSLKQGAKARNLAARKAITSA O59796 VPS3_SCHPO SPCC364.05; CHAIN 1..910; /note="Vacuolar protein sorting-associated protein 3"; /id="PRO_0000314772" MSDIELHESAIPKELDSPVTTIALYNNHLYFGTEGGDVFLYNFSNFQLNESPELVKKISLVSKSRVNRILAMPFLGAVFIHHGSFAEVYKEDDLTQLYPSISFKGLVEFCHPGQRIDEKSTYLIVTNTHLKLISFQKDGIILVKNELKYPNIQTARVNGHIVCLVTENSFELLDILTFDTTPLFPIIKYDSENNGLMYKPMIVLHSNEFLLITGSPKDAIGLFVDSQGNVTRSTLTFSFYPKHVFSTSHYVFAISSSSLQIIDINTLSLVKSINLKDDESFSFISRLTSVHFCDRQIFSKFSAVNTASTSKTSDTIERASFSKPSFIFLTNKSWGFGAEAHFMNKLEFSITIGDIEAPLRRVSKRLRNPKKYGITNDVAYLQSAYLEQISALQYWKQGQYENSLSLLETSKIDPRVVISLYPDLYHSELSYIAFQGVISFRKSILSVDDTVANVLKSNELFRDTDQYTQRQMIEITKENAYIMLMRYLKNYKKNTSISEYLLSSQRDVMLAVEHSLLLLYLNMDDLAAGTKNAKELLESGLTGVEDIKDVLIQKKEYYLLSVLLATVRDHDGVLQTWKKLITGDYEDRRFNDGLIKIREYLVNDIEPSTFWEFTTWLCKHDATEGTRVLLDKTVSGSISAEDVLEHLDSSQDDVLIDYLVKSNSVTHRALLLKLCVNKLLGSLLDHNDFKNRLETAIETFRELPCMEKPTYAQYLEQLWGDMSDFSTHLSFYYLCSINLMENVEEESIDKIKDILFDIHVDNLYLFPQLEHSFYKRKKNYEKALSVLVTNIHDYKGGEAYCLQIDDVYPQCWCNLLEKCISTGDGCSDFIKELLYRRPFSYTLSYVCEQIPDHWNLNLLADFLCILQKRNAERLNESQTRLTLEKSLSQNLEELFMAINRRNVALGKNEI O59797 YCO6_SCHPO MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 20; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 24; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 26; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 59; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 90; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC364.06; CHAIN 1..393; /note="Putative nucleosome assembly protein C364.06"; /id="PRO_0000185661" MVENVNINNKRAGKMSAAPTPHNTPSGTSAPNFGAKAPQVNTIDEGDENLEAIDGKLGSLLHLTSEGVSELPEAVQRRISGLRGLQKRYSDLESQFQKELFELEKAYAKKYAPIFKRRSEVVRGADEPTEEEIKKGEAADENEKKEPTSSESKKQEGGDDTKGIPEFWLTAMKNVLSLSEMITPEDEGALSHLVDIRISYMEKPGFKLEFEFAENPFFTNKILTKTYYYMEESGPSNVFLYDHAEGDKVDWKENADLTVRTVTKKQRNKNTKQTRVVKVSVPRDSFFNFFNPPTPPSEEDEESESPELDELLELDYQIGEDFKEKLIPRAVEWFTGEALALENYDGFSDLDVEEDEDDVESSSNEEVSDSDEEDSDSKHTAHGQQNAAECRQQ O59801 SKI2_SCHPO BINDING 302..309; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPCC550.03c; CHAIN 1..1213; /note="Putative ATP-dependent RNA helicase C550.03c"; /id="PRO_0000310785" MSSKLVDAINEVAVSNKDKIELDGIKDDSFDGHLSITEATYDVDTFLKPSPALSKDWIRKLQKKWDREITYKGLYEYPETLARTQIRFQRHGLEGKIMGYKEVPELIEDLNSKNSSSFLRKPSSKNEFVRGSTSNIPFLADDSDVDAIAGEPSVKMALYGEDGLLQVPPGFSRGLSMTATSTTDNLNDEFDPEKWDTKKVKSSNRNFVTIHELNEHLKNVNSKHSEIDDLLPDKRSIVSLPPSTLNLHKQPDYAHVVDSSAPIENFQQLVPEMALDFPFELDNFQKEAIYHLEMGDSVFVAAHTSAGKTVVAEYAIALAQKHMTKAIYTSPIKALSNQKFRDFKHKFEDVGILTGDVQVNPEGSCLLMTTEILRSMLYRGADLIRDVEFVIFDEVHYVNDLERGVVWEEVIIMLPPHVTLILLSATVPNTKEFASWVGRTKKKNIYVISTLKRPVPLEHYLWVKQNMFKIVDQHGRFLMDGYKSANDALKKPDKPVIAKDNKNSARGRGAARGRGVQTNMMRGRGSAKSVERRDANTWVHLIGHLHKQNLLPVIVFVFSKKRCEEYVDTLTNRDLNNHQEKSEVHVVIEKAVARLKKEDRLLPQIGRMREMLSRGLAVHHGGLLPIIKEIVEILFQRGLVKVLFATETFAMGVNMPAKSVVFSGTQKHDGRNFRDLLPGEYTQCSGRAGRRGLDVTGTVIILSRSELPDTASLRHMIMGPSSKLISQFRLTYNMILNLLRVETLRIEDMIKRSFSENVNQTLVPQHEEKIKSFEEKLSALKKEMSDVDLKEIKSCLLSSESFKEYTKKMHFRAITTANGKRIFKDGRVIVFQQLDFTRTVGVLLGTSIRTNASDCTLEVAYLNPQNNLKRPSDLLAFADAFNDVYDNAIFDESNQFKYGLINLSGIERVCNTILRIDSGGIRDRRGGAFRKLSEQFASIKKFSDLLFEEVNWSKVRDFEFCEAFEKRNFLQNKLSGNPIISTPNFLTHFALAYQEYELESNIDNLSSYISDQNLELLPDYEQRIKVLQELGYIDAERTVLLKGRVACEINSTSELVLTELILENSLADFSCEETIALLSAFVFDEKTEVEPTISPHLQKGKEMILSVAEKVNQIQEHYQVLYFNEGNDFESQPRFGLMEVCYEWARGMSFNRITDLTDVLEGSIVRTIIRLDEVLRECRGAARVVGDSSMYTKMEECQNLIRRNIVFCPSLYM O59802 GPI2_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705, ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198; SPCC550.04c; CHAIN 1..324; /note="Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit"; /id="PRO_0000372382" MDEVCAAPAPKKMVAKSLVLNTFRKASVKEVVELKKPWKKVLWRKQDYPDNFIDESFLNGLQRNVNIQVTDFWSLVADSLPVSQHLSSVVIFASVFVSIYRNQLSCALVGFVSNVSAVAAFILWDFVLRKPCNNRTFPNYMGIVKSCILIVLTLAGLSPILMSLTKSTSPDSVWAIAVWLFLANVFFHEYTTETIRPHVRLHNSLSTNAALSASVVLASRLEKSINVFFFILFAVHWFALFPIFRKYIHVFSFYADMLMTLVLIISAYIALNAVASVVIAFVFLSLIFFISFICPIWFIKLQRFKNEIHGPWDIALPKLGPSKG O59804 CH10_SCHPO MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC550.06c; CHAIN 1..104; /note="10 kDa heat shock protein, mitochondrial"; /id="PRO_0000174921" MATKLKSAKSIVPLLDRILVQRIKADTKTASGIFLPEKSVEKLSEGRVISVGKGGYNKEGKLAQPSVAVGDRVLLPAYGGSNIKVGEEEYSLYRDHELLAIIKE O59805 YJV7_SCHPO ACT_SITE 132; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 207; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 231; /note="Acyl-ester intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4; SPCC550.07; CHAIN 1..533; /note="Putative amidase C550.07"; /id="PRO_0000316202" MTIDWRQIAAKYCAHRDGSIPEPFKIKTLPKDTVLNVTKIPSECGLLTPKEIELTEKYDATALAEMIKDRKVTSVELVTAFCKRAAIAQQLVNCVNELFYEEALARAAELDEYYAKTGSLVGPLHGVPVSVKEHISIKNHTATASFLAKANIIAEKDSDLVATVRKAGAVFYCRTPQPQAIMHLETSSNLTGVTVNPFNRKLTPGGSSGGEGALLGIKASVLGIGSDIGGSIRSPAANNGLFGLRPSTLRLSRKGCQGAVSGQETILGVVGPLGRSVRDMNLFMKACIDSQPWLDDASLLPMPWRSVAPPKTLKVGIMRSDNVVNPQPPVARAMQMAIDQLSKNPDFDLVDVEPLDHKYSWDLISEMYWLDGGKVYYDLFNKVGEPILPLTEWIMHQPNVKPHDITAVWKLTAARDEYRNRYLKHLQAYGVDVLLTPVGPSPAPKLGEAKYWTYTSVWNLLDLPAVVFPVTTVDPKLDVKDESYIPMNEQDAANYETYSPEDYLDAPVSLQLVGKRWQDEELLAALDKIVSML O59808 BADH_SCHPO ACT_SITE 271; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008"; ACT_SITE 305; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008" BINDING 249..254; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8; SPCC550.10; CHAIN 1..500; /note="Probable betaine aldehyde dehydrogenase"; /id="PRO_0000056531" MTIDLNVIQSDIISARRAPENSLFIDGKFVSPIEPAAKPIPLINPATEEIIGTCANASAKDVDSAVENAYNTFRSGIWAKWPGKQRGLVLRKIAKMMREKRELLAGIDTINCGKPTPYALFDIDSCADMFEYYAEVAETDNPTVKVPLPNNPGFCAFEKRFPRGVIGVITPWNFPLKMALWKLVPAIASGNCVVLKPSELAPWSCLEFALICKEAGLPDGVLNVIIGSGKESGAALSCHPKIAYLAFTGSLATGKKIMHAAAENIVPLTLELGGKSPLIICEDADLSLAIPSAAFAIFFNQGEACTAASRLIVHESVADEVLGGLVSEANKLIIGNGLDPQVTLGPVVSKTQFEKIVSYIQSAINEGCKCVVGGLPRSEQKGYFIPPTVFTNVQTHNKIWREEIFGPVLAVKTFHTNEEALELANDSEYGLGSGVFSTNPKTLEFFSNNIEAGMCSLNNYHVVTHELPWIGWKHSGLGVGLSKHGYNEYMRLKQITQYVG O59809 IMA3_SCHPO SPCC550.11; CHAIN 1..1029; /note="Probable importin c550.11"; /id="PRO_0000303894" MSLVEHFDATLSADPNTRTKAELSLKQLEKEPSFVLAVLQLLSSQEISLPTQQAAVIYLKNRVSRSWSSIDDAPSPLDIPEEQKALFRQNILPVLLQSPMSTRSHLMAILNIILSTDFPEYWPGFSEYTSNLVHSTERCEVYAGLICFHELAKVYRWRLDDRQRDIGPLVAALFPTILQLGQGLINLEDNDSAEMLRLILKTFKSVIALELPPELLANDMILSWIQLLLAVVQKPLPESLMSLEPEVRQSHVWHKCKKWAYYSLNRIFTRYGEPSSLVGDSANKYRAFAKNFITNVVPNILETYIQQTILWTQGQLWLSPRVLYFLGCFYEECVKPKSTWALLKPHLQLLIGSFVFPQLCMSEEDEELWELDPVEFIHKYIDIYDDFNSADVAASRFLVKLASKRKKYTFMGILSFASDILNQYAASPPNEKNPRQKEGALRMVAAVSNSILSKNSPVAGMMQDFLVAHVMPEFTSPVGYLRSRACEMINRFSEIDWSDKSQLLNAYQAVLNCLQDNDLPVRIQAALALQPLMRHLEVHDVMTAHVPIIMQNLLFLANEVDIDALSSCMEEFVSSFSHELTPFASQLAKQLRNTFVKLMQETMDESTTVDDFDSLVDDKSIAAIGILNTLSTMILSLENTVDVLREIEAILLPMINFVLDNNIFDVYAELFEIIDGCTFASKEISPIMWGVYEKLQKVLKESGIEFVEEATPALSNFITYGGKEFASRPDYIAVMVDIIMQVFNSEHLAVNDRVSACKLTELLMLNYRGLLDQYVPAFIEVAGNLLLVTEKPTSQTYRVFLLEVIINALYYNPSMSLGVLEMHQWTLPFFALWFENIPSFTRVHDKKLSLVAILSVISLGAQQVAVAIQDSWGNIMKVMITLLNTLPEALAARAELEKEYDGETFNLSGSGWNDGIDWEADDDEGVDDFAVEYGGPDLGGEISADVVDDFDEFEHFQGNYLLDEDPLFHTLLDQVDPFSLFQEFMVHLKDNSPVTLQDLVKNLEASEQQSLQRLVTEKPSTLAVASDKT O59811 REI1_SCHPO MOD_RES 150; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 155; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC550.15c; CHAIN 1..463; /note="Cytoplasmic 60S subunit biogenesis factor SPCC550.15c"; /id="PRO_0000310843" MSTSFACTTCTVAFNNAESQKIHWKSDWHHYNLKRKVASLPPLSAEVFAGKILSIQKQNEEVQKKAEFYQNCEVCNKKFYSEGAYSSHMASKKHRDNLSKFQRNSRIKKLQSEDASSIASSTLSMGEPVVDSEIEEEEDLASQLTSRAISLSNLSLHGRESEPSKTELATSIPQSNEASKSHLFTQEPTPEEIEAELARRSSQRLSPRDCLFCAASFSSFDTCKKHMKASHSLYIPEREYLVDEPSLFDYLAEKISIGFTCLTCNREFKSLEAVRAHMQQKGHTSIAYDTEDEQLELSDFYDFTTSYPDYAVKQDETVVEEDGSSGEGDWEDVSDDSDNSSLDSLEMGRVPIADEYELHLPSGNRVGHRSLSRYFRQNLHSSSTAVGDGASIHQNVARRAMSGNARAYRQAVETSIAGVRDGRKNYSASHIKSFQDQRRREEFANKMGIKNNTKKHFRDALLQ O59812 G6PD2_SCHPO ACT_SITE 238; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P11411" BINDING 42; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 146; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 146; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 214; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 233; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 332; /ligand="D-glucose 6-phosphate"; /ligand_id="ChEBI:CHEBI:61548"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 342; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413"; BINDING 365; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P11413" CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; SPCC794.01c; CHAIN 1..475; /note="Glucose-6-phosphate 1-dehydrogenase gcd1"; /id="PRO_0000337687" MLSIIVFGASGDLATKMTFPALFALYVRKIIPEDFQIIGYARSKLSQEAANKIVTAHIPIDDTVGASQKALNTFVEHYKYVPGTYDKPESFEMLNSIIAEKETAPASECTRIFYLVLPPHLFAPVSELIKSKAHPNGMVTRLIVEKPIGFDYKSADAILSDLSKHWSAKDTFKVDHFLGEDMIDGFTAIRFANSMFEPIWNREHIESVRVDFREDFGCEGRGGYFEGAGILRDVVQNHLLQLLTLLCIEEPKSQDAEDIIKCKVDFLKSLHPVSKEDIVYGQYTKSANGKVPGYRELDGVADDSEVSTFCALQLRSEAPRWKGIPIIISAGKGLDRDYFEARITFKRREGGMFPTVDSSNVLVLRVYPKEFIALKGHIKQPGFSRQIVPVTLDVKYPEAFPDTWIHKAYEVVIADAINGKHTHFISDDEVRTSWKIFDDVLDTTGDLSPLPYAFGSHHGPDATLEFFKKRNLEWD O59817 EFR3_SCHPO MOD_RES 210; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 726; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 729; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC794.08; CHAIN 1..798; /note="Protein efr3"; /id="PRO_0000270783" MWLLFRSKHKKLVLRCFPSGKLGETEPNGSPLAYLSYYAASNSSKLRKVAHFLGSRVRHSYYHKRDNEVIIGLKICKTLVQKCRDNINVMASEVVNMLLVASSSKNLEVLSACVDCFATFCDNSGKGSPATFGNEFHSAFNNLVNSFFELSKGIDCVDPQQSKMLGLKAFHALTACKFAGTEGGMRYQPHFAIHCVLINSWSESDQEKKSFIDLVRSTAKSYKPLPPSSTGVSLPEHDEAGDNIDVAIKKLCIRILFNIYTQTDPLFMAESTKSLIHFFAAKSDTPVNLEYISVVLNQILDWTPVELRHSIFFCCLRCLSSSRIVNSETNVMVPYMIYSILNSKNSISGLSVIDVLRDLGSHLINAVNSFDADDQTWYNMCESPSEKLPRRLYLLLVCITCLTKHQYYDEEFADVWREIDTLANSETSSAIQMVALTAFHKLQNEKLNTKKESSAPLSLVTDFLLHSWPKSAERLHTSQSPFVRIKTAEVFYEFLCFLRPSLINFDTILRKSAITSFSVLWDFIYETSWHIERWLKVFSVQSEFYILKLIIQRLYQLYGPVSVTAVLPAMYRGLRPFENDPPRCIAEAVTAYYIIYIGENLKITTLQSSGRKWLDSLSSSLPSSLLNRGSSTHSWEKLTNASTEEVMLPLDMVVNELLEKSPKVFPEDSRLLFAEQSRHPKYTDIIQKLKKPSREKSFTSSSEYSLPFISPASDYQQNPLLHATKSLVSIHQQSQRGEMVSTLKQALSRPHTASTVVRSPSEINLTRQTSNRVPLLDMLNLNRAMSPTPIQSPPYVRT O59819 UGPA2_SCHPO BINDING 108..111; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 110..111; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16851"; BINDING 122; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 185; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 214; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 215; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16851"; BINDING 243..245; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16851"; BINDING 245; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 387; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3" CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885; EC=2.7.7.9; SPCC794.10; CHAIN 1..499; /note="Probable UTP--glucose-1-phosphate uridylyltransferase"; /id="PRO_0000185764" MLHRRIHFKSQSTLDFDSVAVSISASTMKNELDKLVLNSRVSDKKTFGIQMDNFFALYRRYLLHTVKGYECDWDSIRPLGPEDMIDYGDLPLCKNAGKYLNRLAVVKLNGGMGNALGVNYPKAMIEVRDNQSFLDLSIRQIEYLNRRYDVSVPFILMNSYDTNDETCKVLRKYAGCKIDISTFEQSRYPRVFVDSQLPVPKAAPSPIEEWYPPGHGDIFDALVHSGTIERLLAQGKDYLFVSNIDNLGASVDLNILSHVIDNQIEYSMEITDKTKADIKVGILVNQDGLLRLLETNQVPEQHREEFMSDKVFKYINTNNVWLYLPAVKRVVENRELNLDIMPNIETVYYNNEPARIIEFTTAIGSAISQFKKTEGIRVSRPRFISVKNSSDLFLVRCDLYNVDHGSLKIEESRLGFPPPVVRMSNEFKDIAELFCRIPYMPSMKDLVSLSISGNVYFGRNVILKGNIVIVASENTILCIPSNAVLENCVVTGNCKIMEC O59826 KCAB_SCHPO ACT_SITE 67; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P62483" BINDING 33; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 62; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q13303"; BINDING 67; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q13303"; BINDING 167; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 193; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q13303"; BINDING 222; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 223; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 224; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 225; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 233; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q13303"; BINDING 243; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 301; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 303; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 307; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 310; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483"; BINDING 311; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:P62483" SPCC965.06; CHAIN 1..344; /note="Putative voltage-gated potassium channel subunit beta"; /id="PRO_0000310339" MASATTHFQPKNVPFRFLGRSGLKVSAFSLGGWLTYGNEGYDVEHTKNCLKQAWDLGINTFDTAEIYSNGNSETVMGKAIKELGWDRSEYVITTKVFFGAGTKLPNTTGLSRKHIIEGLNASLKRLGLPYVDVIMAHRPDPSVPMEEVVRAFTQLIQDGKAFYWGTSEWSAFEIEHAHHIATKYNLIAPVADQPQYNYLTRDHFEKDLLPLQQIYGYGATVWSPLKSGILTGKYNDGIPEGSRLSTTFTSLAGQLQTPEGKTQLDQVRQISKIAEQIGATPSQLALAWTLKNPYVSTTILGASKPEQIVENVKAVEFIDKLTPEILKKIDEILNFTPLEIQYRR O59827 GST2_SCHPO CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; SPCC965.07c; CHAIN 1..230; /note="Glutathione S-transferase 2"; /id="PRO_0000185985" MAHFTLYSHAGGPNPWKVVLALKELNLSYEQIFYDFQKGEQKCKEHLALNPNGRVPTLVDHKNNDYTIWESDAILIYLADKYDTDRKISLSFDDPEYYKLIQYLFFQASGQGVIWGQAGWFNFFHHEPVVSAVTRYRNEIKRVLGVLEDILKDRDYLVANKYTIADLSFIPWNYNLGGLFGEGKFSFKEEVPQLDFEKEFPKAYAWNQRLLARPAVKATFEELAKAKEQH O59829 YCU9_SCHPO ACT_SITE 45; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 118; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 150; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" SPCC965.09; CHAIN 1..272; /note="Probable nitrilase C965.09"; /id="PRO_0000315967" MKANIACVQMAPKVCDVKHNLQKMSSYVHEVMESNPSTNLILFPELITSGYECGNTFTQIAEIAGEGPSFKTMSNLAAKYHVNIIYGFPEKEEKQSNIIYNSCIYITENGNLGGVYRKVHLFDTERKHFKKGSDFPIFETSFGKLGVMICWDTAFPEVARIHALNGADLLVVATNWENPYSDDWDLVTKARAFENCIPLVAANRVGTDEKLSFFGHSKIIGPTGKVIKALDEEKEGVISYTVDLDDAKPLRKNYYTFFEDRMPDLYKRLLSP O59833 YCUD_SCHPO SPCC965.13; CHAIN 1..537; /note="Uncharacterized transporter C965.13"; /id="PRO_0000372788" MSILNVIRSHHDVEPQNVEEEPPLTGQTIVTEDKLETSAKDKKHESPSMSEDEEGSVENVDAWDLTKALMSIDPNHPAHPHKWPLWKKLFVATVYTFLEVYVIWSSTACINFFDIYQTNWHCSIQVSYLVQSLFIVGNAFGPMLLGPMSDIFGRKWVYVGSLILYIIFQIPQALAYNLPMMAINSAIAGAFGSSALANVASSMCDIFTPETVGFGISLFVWGANAGASIGSPIGEALYDHWRWFYWMNMIVGGFFVILCVLCPETLPVINIMNYSSTTGEKTVQVSTLAKAKSAVVRTKFVLSTAFKLLCTEPIIMALGLYNGFAYGLIFLYLDGLFPVFVDNYKMGYMGANLTYLNFLVGVTIVVMLQPIQNWLYRWDKRRHGGVARPEARFLISLLTVWFFPAGLFWFAFTSDGRISWVSPLIAGGVLGVGDPQLWLAMINYITDSYPSVAGSAIAAFTLPSFAIAAVLVHLGIIMFDNMTTTWAMATLAFISLSLVATIYVIYFFGHLIRKHSRLAVTQQALQEAHDAKVLPEV O59865 RS24B_SCHPO MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250" SPBC17G9.07; CHAIN 2..134; /note="Small ribosomal subunit protein eS24B"; /id="PRO_0000137635" MSEAVTIRTRKFMTNRLLQRKQMVVDILHPGKANLSKNEIREKLAQMYKTDSECVQAFGLRTHFGGGRSTGFALIYDSTESMKKFEPHYRLVRVGQAEPIQKVARQQRKQRKNRGKKVFGTGKRLAKRKSKQQD O59866 OSTB_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPCC338.15; CHAIN 20..437; /note="Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1"; /id="PRO_0000315923" CARBOHYD 275; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 289; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKSALCIALALTWSLLVQAARQTVLAVADHDIGGYSTFLQSLTDRDFDVKTSYIKDESAKLFEYGERLYDNLILLSSQSKSLGPVFSPKSLLEFVQSGGNLFVVAGSQLPEGIRELGRQLDMFLAERQSVVVDHFNHAEGSDDIILLDGISENPYIISDETRAAGPILYKGIGHYLGPNPQTQPILRGNPTSYIYNTKTEAEVSKNPWAAGTQLFLVSVLQSSTGERVGLSGSIDMLKDEYLSPQSPSFSKSNFLFARDLTNWVFQRKGVLQATNMTYGKVAEPLESRNASCYRIKDEMIFSIDISLLEDGQQTPYVADDVQLELIMLDPYYRVNLVPVPSDSQTSQHYEAVLVAPDHYGDFTFKIEYKRPGLTPIEEKSTFTLRQFFHNEFPRFLPHAYPYYASCFSVLGAFLLFCGIWLLQKPAKPVVPSAKKQN O59932 GHT4_SCHPO SPBC1683.08; CHAIN 1..557; /note="High-affinity hexose transporter ght4"; /id="PRO_0000050412" CARBOHYD 357; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGRTLTSVLVVFISMAGWLGGADTGSISGILGMRDFQSRFADRYNPITNSYSYSAWRQALLTGTVNAGCLFGAMLSSPFTEAIGKKYSIAFFSGCYIIGQILLVTAVPSWVQIMVGKLFTGLTIGALSVLSPGYQSEVAPPQIRGAVVSTYQLFQTCGTLIAACINMGTHKLRKTASWRTSFGINILWGIFLMVGVLFLPESPRYLIYKGRDEEALRIMCQTAELDPESEIIQTNFNTIKSDIEMEMAGGKARWPEVFGKEVRYRTVLGFLTMLLRELIGNNYYFYYATQVFKGTGMTDIFLPAVILGAINFGTTFGALYTIDNLGRRNPLIFGAAFQSICFFIYAAVGDRKLIYKNGTSDHRAGAVMIVFSCLFLFSYCCSWGPMGWVIVGETFPIRYRSKCAAVATSGNWLGNFMVSFFTPFISNSIGFKLGYIYACINMTSAFQIFLMAKETKGLTLEEVNELYESDIKPWDSYKYVRQIESRRIHFSKEEEKREREKSKGYRGQEERFIENADGADNDDSSASSESFASAGAHSRSVFPRRSNVSEESHPTWV O60055 UTP20_SCHPO SPBC56F2.04; CHAIN 1..2493; /note="U3 small nucleolar RNA-associated protein 20"; /id="PRO_0000316028" MKAAAQSNSKNYVFLPFSKRVENLKIDVAHKIPRAADLEDEDVESYFISCLRKWEDLNLSTHYVNFLRSVTPYSQSLPQIVYHQKTIFDLIVQYAREGDSLSLQPILELLTQFARDLALEFASYIDQTLELLCILVQNNELEVVDWSFHAAAYLFKYLRKILAPRLIHTYDILSPLLGKEKQKSHVTRFTAEALSFLCKTVSYENAIEFTGHVLLDLNDHYTPQYHEGVVILFSRIIQGVDTSIHFKGKAFFEILLRSEIYTLPRSKSVIIPVLISTIHHCTSDSFNELEKLIISKITGEPLLYINLFKATLVTRKGSRVSDYPSFFKAYLQIPNLVSWENIESDLSVLIFEISALLFVYPQISDLMPHTVRIISFLQQGPLHLFFSFVDVVKQLNMQRYDSFIKPSLPKFISSLVSDESQKSLAILESVLDNSVPVPVDVASVSLNHFVYCIERLQIVSPSYEDIISLWSSLMIIISSSLGSDEIYKACLLFLRKLEDVSSESVLLGDICGIVLHLLQRKVSRLFLDSSYYKPILDSLLGVFGFLADSKVFLESIRPFFGTSYDFCSSYTSLMDRLINNLSRGLTSLRAASIDLIIALCKSLQKNEVLQSLSLVKKLSELPFDPSTSRDASVLLRNLSAKSSALEKDTRRVVLHALLGLTITRFTPLWPDLSRTAASIVTKEVEDEFLAIIYSWLSLPSPPSGLLGPTDTAVFVKPDLSLEKLPTLEINTFNCPAISYFETSFDECFSKFASSDNYIIGNLLKTNQEDLSNLPTFRSQALRVLNELPEIASRNINVLDNYLFSLQHGFDLNTEWARPDVYLLLGLYSKFTGIKEFVNRDARKEFFLWALTINDPKVQKLVLDIILLYSEEAITTYEENLRNLLDDKKCRDELITFLFVDYADSKIQDIHRPLLMPVVISILYGKMVSKGYGGQKNQAARRSTILSALGNMQVEDLQILVDIMLRPYNGLEVKLNANNNLEIDTGNIPSLTLRRQIGFLTMTEELLLQISSKLSSVAPKILNAVLYNLVVSDDQISSQEAFENFEVKMAYTVRQLSLKVFLLFLKSCSDVDFKPYNVFIYTAFVVPRLDRFADENTQSVSNLMKIFRCWFENEAYLDSVLEFSSHILTALLNTASHTAVKLPVLLYILDTLNLVITHLQSEESESQLREKILANLVMPNITLIFASLSNILKNPQFCNNNRVMDGSVQALSAVSEYMSLDIDSSPLLNLLVSFLRKPNRLVPSNVKSNILVLLCKLLPTNTKWLHASISQTNDFDTIMHLYTSMVDIKARQHLNDLLKIYSTIDDNLIFSSVFVEEINSISKKRLDEPDFERRLSAFTSFNEKHFSLISDLAWLPVLYNFFFYVQDAEELAIRASASLGIKRFIESITMNDASNQFKIDVFVKFIFPFIKNQMKNKNELIRQEFIGLLSYSIKSLTMVDAISDMQPLLYEGDEEANFFNNILHIQLHRRKRAMKRLVNVCAIGVIRSGNISQIFLPLLENFCLGNDTVQTLLDESVITIGEIIKWAHWNQYQAILKRYVSLLKNNAIDQKVVVRLITAVVSALRPLDDAVASYTNSEMNIEQFDGQKKKCVLASSLPSEERFTEVLTNDFFPTLMLYLHIRDESTVTLRVAIALSIVQLVALLPEEEIVLRLTPVLIDTCHILRSRSLESRDATRKALAAISKFLGPKYFSFIISQLQTSLKRGYQLHVLGYTVHYLLLAIEDVYPYGSIDYCMDSLAQIFVDEIFGEVGVEKDSEDYKSNVKEIKGNKSYDSYEIVARISSFDSLSTLLRPVKNVLFETNVPKSLRKVDELCRRLSLGIVANKQSASQSSLIFCYNVYEFVVKEKETVAALKQQENDGYRSAPNFFLENSKKLIRFTFDVLRGVSNKHKELLTARNMAAFVPLIGESLLSSSEEVQISALRFLVLLLPLKIDQVFSGSSVFTSQAVKYIQNSPSTNTELCQASFKFLASILPYENVKIKESTINYLLERVGTDIQEPDRQGVMFSLVRAVIARKIMTPELYKIIDLIRDMMVTNHTKSTRQTCRHLYYSFLLDYPQGKTRLSKQISFILKNLEYEFAPGRESVMELLHLILNNFSDALLKEYHQGIFIALVMVLANDSEPHCREMSAELIKLVYQRADNENFNLIRQLLSHWTSVEKAGKNLVRVSMQLFGLLFETFGFERMEEVHLFTKVFERVLSTTISHPEEATNEWELNYFGLQSWLKLVLADPKKSCEKEFSKIWESMRYLILFKHAWVRLSVSRLFGHFFAIIGDSNFGKLSLGIDGVVFSLDFVTQISNALQAQLRSPVLSEELGMQVAKNLIFLTRWFNSIRSSDDSPFLEIFRRMRKTLKKQTIEEYSINKKYLMQWFASVIHVFSGEELQPVLSEIIAALYRYTELQEAERKSQQELADLVTESLQVLQEKVGATVFARAYQEVRNAAIEVRRERREKRAIEQVVAPEVASRKKIRKNERKRENRKQKTNHHRMVNSIFKNR O60058 AFG2_SCHPO BINDING 320..327; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P32794"; BINDING 589..596; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P32794" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P32794}; SPBC56F2.07c; CHAIN 1..809; /note="ATPase family gene 2 protein"; /id="PRO_0000310282" MSVAIKFTVKINDGSLRRQQTRHVFLSPAALNRLKLSPSQVIYLKHKGGEAVGITQSVKGNGIGPFEILISPLLAKWANLKAFQRVNISQYVHPLKEAEGIKIVASLSSNNEPIPESLIRKELLEIRYLHPGMIVMGESPMNMAKSGSKNLSSENMATEIFEINSGLSAQSGTEVGSSQSSPSVNESEPKATEDLDELSPGSYKVKEIHIRSPSNLIEAISDMSLDEPRIYKFTAASSMEIETPDLLKLPHEDRTQSAYNQGSEETQNFDGPPSAVTFSSIGGLQAQIAQIRDIVELPFQNPELFKFFNIMPPRGVLLYGPPGTGKTMVMRAVAAEANAQVFTIDGPSVVGKYLGETESRLRKIFEDARAHQPSIIFIDEIDALAPKRTEDVSEAESRAVATLLTLLDGMANAGKVVVIAATNRPNSIDEALRRPGRLEKEIEIGIPDKSARLDIIKLLLSGVPNEINDAQLEDLASRTHAYVGADLAAVVREAALRAIKRTISLQKDTSGLDIFGAVQMDDLEFALSSVRQSAMREFMMESPNVHWSDIGGQEEVKQKLKESVEWPLTHGETFSRLGVRPPKGVLLYGPPGCSKTITAKAIATETGLNFIAVKGPELFDKFVGESERAVRQVFQKARQASPSVIFFDEIDALTANRGEDNSSDRVVAALLNELDGIEALRNVLVLAATNRPDMIDPALMRPGRLDRLLYVGPPNFEARKQIVKIQAEKMKFAEDVDLDLIAEKTEGCSGAEVVALCQEAGLIAMHEDLEAKEICQAHFKTALLALRKAITRDMLEYYASFSESVTSIS O60059 YG58_SCHPO MOD_RES 102; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 104; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 105; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 482; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 486; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 488; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC56F2.08c; STRAND 1..5; /evidence="ECO:0007829|PDB:6NX5"; STRAND 26..31; /evidence="ECO:0007829|PDB:6NX5"; STRAND 38..43; /evidence="ECO:0007829|PDB:6NX5"; STRAND 67..71; /evidence="ECO:0007829|PDB:6NX5"; STRAND 428..430; /evidence="ECO:0007829|PDB:6NY5" HELIX 13..20; /evidence="ECO:0007829|PDB:6NX5"; HELIX 33..35; /evidence="ECO:0007829|PDB:6NWW"; HELIX 45..55; /evidence="ECO:0007829|PDB:6NX5"; HELIX 110..113; /evidence="ECO:0007829|PDB:6NY5"; HELIX 115..123; /evidence="ECO:0007829|PDB:6NY5"; HELIX 131..143; /evidence="ECO:0007829|PDB:6NY5"; HELIX 161..176; /evidence="ECO:0007829|PDB:6NY5"; HELIX 182..191; /evidence="ECO:0007829|PDB:6NY5"; HELIX 196..199; /evidence="ECO:0007829|PDB:6NY5"; HELIX 205..215; /evidence="ECO:0007829|PDB:6NY5"; HELIX 218..228; /evidence="ECO:0007829|PDB:6NY5"; HELIX 229..231; /evidence="ECO:0007829|PDB:6NY5"; HELIX 232..236; /evidence="ECO:0007829|PDB:6NY5"; HELIX 241..250; /evidence="ECO:0007829|PDB:6NY5"; HELIX 255..265; /evidence="ECO:0007829|PDB:6NY5"; HELIX 266..268; /evidence="ECO:0007829|PDB:6NY5"; HELIX 269..274; /evidence="ECO:0007829|PDB:6NY5"; HELIX 278..284; /evidence="ECO:0007829|PDB:6NY5"; HELIX 285..288; /evidence="ECO:0007829|PDB:6NY5"; HELIX 294..302; /evidence="ECO:0007829|PDB:6NY5"; HELIX 304..308; /evidence="ECO:0007829|PDB:6NY5"; HELIX 311..322; /evidence="ECO:0007829|PDB:6NY5"; HELIX 328..339; /evidence="ECO:0007829|PDB:6NY5"; HELIX 342..345; /evidence="ECO:0007829|PDB:6NY5"; HELIX 349..359; /evidence="ECO:0007829|PDB:6NY5"; HELIX 367..375; /evidence="ECO:0007829|PDB:6NY5"; HELIX 376..378; /evidence="ECO:0007829|PDB:6NY5"; HELIX 379..382; /evidence="ECO:0007829|PDB:6NY5"; HELIX 388..397; /evidence="ECO:0007829|PDB:6NY5"; HELIX 402..413; /evidence="ECO:0007829|PDB:6NY5"; HELIX 416..418; /evidence="ECO:0007829|PDB:6NY5"; HELIX 419..426; /evidence="ECO:0007829|PDB:6NY5"; HELIX 431..439; /evidence="ECO:0007829|PDB:6NY5"; HELIX 447..463; /evidence="ECO:0007829|PDB:6NY5"; HELIX 472..476; /evidence="ECO:0007829|PDB:6NY5" TURN 21..23; /evidence="ECO:0007829|PDB:6NWW"; TURN 61..63; /evidence="ECO:0007829|PDB:6NWW"; TURN 192..195; /evidence="ECO:0007829|PDB:6NY5"; TURN 290..293; /evidence="ECO:0007829|PDB:6NY5"; TURN 469..471; /evidence="ECO:0007829|PDB:6NY5" CHAIN 1..661; /note="Pumilio domain-containing protein C56F2.08c"; /id="PRO_0000310365" MLYVSNLPVGTSSSAIHALFSAYGNVKDIWMLSPDNSAIVSYESLSSAIVARDALHNRPVFENHGPVQVMLAKPSSNYEPGNITAAVSPPASTSSKDGVVCSPTSTGASQLLKSRVDILEVARQFEMRINLDIVDSMIASAIENNKVATEILPPVETLRSRQFEASKLREIRKNIDSGFYTQEEIEVIARSMLDDVAELSSDYLGNTVVQKFFEYCSDPIKEAMLERIAPYLAAIGIHKNGTWAAQKIIDVASTEKQMDLIVKHLRPYTALLYFDQFGNYVAQCCLRFKYPKNTFLFEVMARHCCEIGQSRFGARAIRACLENENATFEQQALVVASIIINSHLLATNSNGMLLLTWLLDNSFFRNRHRLLAIHLATHLHTTCTHKLASTLIFKLINNKQEPESRNLLLKNLFFSEKDNVLTYILQDQAVGPSFIHKVITYPSIGREFLAQFHLVIKRVLINIHAQPNAVYCRLMEEVGMTSKSISPSLSGISAPSASVDSSASRLARDFGSLSLSSNSLLGSLGGLESTPAYPSYPSHIPLGTASLPLKGNLYQISRSDDIKSGAPVLDTSSLVNPTLAKSASLNNSSLLNPSSSLLRREVPAGKLTMPAYPYTTQLMNHTAGADYGLPRLSSKLPQVFPGNYPRLQQSLFPRQGELRFN O60061 ALG5_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl phosphate + UDP-alpha-D-glucose = a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117; Evidence={ECO:0000250|UniProtKB:P40350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15402; Evidence={ECO:0000250|UniProtKB:P40350}; SPBC56F2.10c; CHAIN 1..322; /note="Dolichyl-phosphate beta-glucosyltransferase"; /id="PRO_0000311759" MVVYIVLYTCLAGFILLFLVYYYLTHSHCPRKQLEGEETCVFIENGQKKSLTLEKWSTSDNIQITVIVPAYNESKRIGNMLQETVDHLEKYYRSSSSAGQRRWEILIVDDESKDTTVNAVLEFSNKLDLRDHLRVCSLKRNRGKGGAVTWGMLYARGQYAIFADADGASQFSDLELLFKNMPPGPRGGVVVGSRAHMVNTAAVVKRSFIRNFLMHCFHKLLQILGIREIGDTQCGFKLFSREAYQSIFPRMHVEGWIFDIEVLTLARFFGLPIIEVPITWHEVGGSKMTLLKDSISMAIDLLVIRLNYTFGIWERPSAKRIT O60063 NAM9_SCHPO SPBC13G1.01c; CHAIN 1..327; /note="Small ribosomal subunit protein uS4m"; /id="PRO_0000132707" MKGKFRFSLKRGLLRPSWNKYNIYNIARKQLPALNNRTLYQKKWNAKKETRSYHGPQLREYQLKNAFRPKLEGVISSLDNKLPIPFMNQTYAFLESRLDMSIHRALFASSALQARQLVLHGKVHVNGKPERRAYRQLLPGDLVTVDQKSVMNCVSASSNNTPSIQDGKQTEQVSSKDGENEKKKDNDDDLFEQTSNGKLPSINETISNFVPKPFMSLMAFIPAYLEVCFRTCSFVYVRDPVARPGLTEVPSPFPEDLHALAYTYYIRSRNMRQGAARCQARRLIPQKVRDASFYQGPPELYKKRNVSPKEAFSHRYPVRQGKLTKLV O60064 YBB2_SCHPO CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527, ChEBI:CHEBI:58409; EC=2.7.7.13; SPBC13G1.02; CHAIN 1..414; /note="Probable mannose-1-phosphate guanyltransferase"; /id="PRO_0000311772" MISSAVILVGGPSRGTRFRPLSFDVPKPLFKIGGREMIYHHLAALSKIESVKDVFLVGFYDESVFKDFINEVASHFPSFNRIKYLREYNCLGTGGGLYHFRDQILKGHTSNVFVMHADVCCSFPLQELLNVHHEKKALVTLMATKVSKEDASNFGCLVEEPSTGRVLHYVDKPSSYLSNIISCGIYIFDASIFDEIKKAYERRLEEVEKQLRSLDEGMEDYLSLETDVLAPLCSDSSKAIYAYNTPEFWRQIKTAGSAVPANSLYLQKAYHDGTLPKPDTEAEIIQPVFIHPNAIVSKGAKIGPNVSIGARVRIEDGARIRNSIIQEDCEISANAVVLHSILSRHCKIGKWSRVEGSPTLPSQHSTTIMRNSVKVQAITVMGADCIVHDEVRVQNCLVLPHKEIKVGLVGEIVM O60065 PEX14_SCHPO SPBC13G1.03c; CHAIN 1..286; /note="Peroxisomal membrane protein pex14"; /id="PRO_0000372384" MREDLLRNSVEFLREKTVLDAPDVKKIEFLKSKGLTAEEIQEAFKLAKNPLFPSYPRFENTSNFVSRDWRDWFIMGVISTGFAWSAYSLVKKYIAPMFRAPSQNAYEADKNALDAKFLEAHKILENLDEQTRKLSERTEKQQDELDIALDDLEETLNTLKRTSENRDREIARISQDVYTMSTITLPQSLEQIKKSQEEALQNLSREISSLRCLQTDSKKDDTFATTSNSSIPVLENPLDTSEGFQTKKVGTASLPDWQISMHNEASKNIDFNDIDPAESYVAEDAY O60066 ALKBH_SCHPO BINDING 142; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 149..151; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 194..196; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250"; BINDING 205; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"; BINDING 207; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"; BINDING 235; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 261; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"; BINDING 290..296; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250" COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion per subunit.; SPBC13G1.04c; CHAIN 1..302; /note="Alpha-ketoglutarate-dependent dioxygenase abh1"; /id="PRO_0000066669" MLAGNMEQANVFRLEEKRYKCRADTIPDMSEVLDPNDPQSFGFEALVEIKPRVFSFQKAPGLLILKNYVSSELQMQLLKSIMFTQIQDPENKTNLSPFYQLPLGNDSIWRRYYNGDGESIIDGLGETKPLTVDRLVHKKLRWVTLGEQYDWTTKEYPDPSKSPGFPKDLGDFVEKVVKESTDFLHWKAEAAIVNFYSPGDTLSAHIDESEEDLTLPLISLSMGLDCIYLIGTESRSEKPSALRLHSGDVVIMTGTSRKAFHAVPKIIPNSTPNYLLTGNKAWDGWISRKRVNFNVRQVRPSR O60067 TAPT1_SCHPO MOD_RES 94; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC13G1.05; CHAIN 1..649; /note="Endoplasmic reticulum membrane protein 65"; /id="PRO_0000328879" CARBOHYD 215; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MGSNTSPGQADPLESENESSLTSRFLPNKRDGGKDNESVIPEKEEPDLNEPVLAVPLPKSRYALTKRSSSSEYPRRSASTSAKKNVIPITRSYSTTFFSKTNDQPTVTGNQDKPISRLRASKLQIQNFWNYICFELLANDTVPANPIKEKHVENFLATPYAIEKTFLFGWFVSVDSFLYIFTLFPIRVLISFFTLSRCIFQGLFSTFFHRNSSPNRSLPRSRKIDLLKLLLIFSTSILIRKIDVSRLYHIIRAQASIRFYVLYNVLEIADRLCCALGQDVLDCLFSNHILSFNFWNPAGWMTFFYYFAISLAYMVLHTLVLLYQIITLNVTVNSYSNAVLALLMSNQLVEIKGAVFKKFEKENLFQLTCSDVVERFQITIMVIIIFLRNLAELYTTSSLDQPLLTFKRLKTLLAPFFWVIGSELFVDWLKHAFIIKFNYIKPSIYSRFTDVLCHDYVASGAQLTQTVTGCSQQVARRMGLPVLPLVCVFIRTSMQTWSMFRSTHSMKQEIAKSIGTIFPTKDNYVYYLPNKEANTYNAGKEASWETLLLSVVRGKSGIAFLFFMAIMLKLLLGKAILAITQSRYESMQQREEKINSWERERKANNFFRGHIEIDKKTKDFLNNSKDDLPVPKSPLLTLERYAMHSKRIW O60069 SWF1_SCHPO CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; SPBC13G1.07; CHAIN 1..356; /note="Palmitoyltransferase swf1"; /id="PRO_0000212992" MDFFYKYLALVAIASLMVFILLFGQIPKLKYTVIGKLNRFFMVTIPYHLHVLDSRYADGRCSAAMRSLSNYVLYKNNPLVVFLYLALITIGIASFFIYGSSLTQKFSIIDWISVLTSVLLPYISLYIAAKSNPGKIDLKNWNEASRRFPYDYKIFFPNKCSTCKFEKPARSKHCRLCNICVEKFDHHCIWINNCVGLNNARYFFLFLLCTIQLLFHSILRLGYHFNALRDMRQYPSFLRSWWFAIKSEGELGSVFLISLICSVLVLCLLGYEFFLVYAGYTTNESEKWSDLAHLVKNRKVYMYYENGSQLLALDKDASNDAILVTSMSQIDNIYDNGFYNNFFSLVFPYRHLYSTT O60071 YBB9_SCHPO MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 156; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC13G1.09; CHAIN 1..449; /note="Uncharacterized protein C13G1.09"; /id="PRO_0000186119" MPKAPKTKLHHAPLYKDIAESSESGVLRQKPSKQKKSKESNTGNGFLDAKTSKKILQLAREQKEELDEEENGKPSQISAFISNGHQKDTLENPAIESSYEESEHARNVSDSESITSQEEEEYEELEIDDADRDLFDRFLPTVSGEEGDLTEEKTTSLSDLIMQKINEAEARARGEYIPSAEEEENALPPLPPKVIEVYSKVGVLLSKYRSGKIPKAFKIIPTLSNWEDILYLTRPDMWTPHACYEATRIFISNLKPVQAQHFLTVIILERVRDDIRENKKLNYHLYMALKKALYKPSSWFKGFLFPLVQENCTLREAAIIGSILQKVSVPVLHSAAALLRLTEFDLSGATSVFIRILLDKKYALPYKVLDSLVFYFMRWKSLERPLAVLEHQSMLVFAQRYKFDITPEQKDALLEVVRLKGHYSIGPEIRRELLNSASRGEEIPVEMEY O60073 YKT6_SCHPO MOD_RES 194; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPBC13G1.11; PROPEP 195..197; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000396673" CHAIN 1..194; /note="Synaptobrevin homolog ykt6"; /id="PRO_0000206778" LIPID 193; /note="S-palmitoyl cysteine"; /evidence="ECO:0000250"; LIPID 194; /note="S-farnesyl cysteine"; /evidence="ECO:0000250" MKLYSVSILRFDPKPVQLLCTASDLSSFSFFQRSSIGEFMNFFTKTVAERTNPGQRQDVEQSNYVFHVYNRSDGLCGVIASDKEYPLRVAYTLLNKILDEFLTKNPRTKWESGAVTLSFPELDTYLSKYQDPKQADTIMRVQQELDETKDVLHKTIESVLARGEKLDDLIQRSDNLSTQSRMFYKSAKKQNSCCIIA O60074 DID2_SCHPO SPBC13G1.12; CHAIN 1..200; /note="Vacuolar protein-sorting-associated protein 46"; /id="PRO_0000315899" MSNLEASLFQLKFAAKSLNKQSLKAAKEERAEREKVKKAITKGNSEIARIYASNAIRKQQESLNLLKLSSRIDAVSSRLQTAVTMRAVSGNMAGVVRGMDRAMKTMNLEMISQVMDKFEAQFDDVNVQTGYMNKAMGSVTAVDTPQEDVDLLMQTVADEAGLEFNQNMNNNLSVPAASVPTPAAPVEDDNLQERLRALRS O60078 TYR1_SCHPO BINDING 5..34; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=NADP(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADPH; Xref=Rhea:RHEA:21640, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934, ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.13; SPCC1494.04c; CHAIN 1..431; /note="Probable prephenate dehydrogenase [NADP(+)]"; /id="PRO_0000119207" MKETFQVGIIGFGDMGRLYAEYISKAGWRVNVCDRPENYESIQATYGNGGYTVLKDGFQVSRTSDYILYSVEAEHIDKVVALYGPATKVGAIVGGQTSCKAPEMNAFEKYLPEDVDIISCHSMHGPKVNPKSQPLVIIRHRASDEHFEIVNEILSCFKSSVVYLSAKEHDRITADTQAVTHAAFLTMGLAWHANNQYPWEINRWCGGIENIKMNLSMRIYSSKWHVYAGLAILNPEAQRQIQQYASSVTELFKLAISGKAKEYEDRIRNAGKFVFGENMDRNSSGLLLSDELLDQYSISNIPKDESKRNSHLSILAIVDSWSKLGIHPQNHMICSTPLFRLWVGVSEYVFRHPGLLDSCIYTATKHNDFSPDDLEFVVAVRSWSECVAAKDFTTYKKRFLETQEYFRPRFEEATRVGNAMISKLLENLQKM O60080 DBP9_SCHPO BINDING 58..65; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPCC1494.06c; CHAIN 1..595; /note="ATP-dependent RNA helicase dbp9"; /id="PRO_0000232345" MEKSGGIREESSEKTFSDFNLDPRLQRAIHKCEFEKPTSVQSETIPLALEGKDLVAQARTGSGKTAAYLIPILELLLKQKQIDENQRGIFALLLVPTRELAQQVYNVLEKLTAFCSKHIRFINVATNSSDTVQRPLLLDLPDIVIATPSRCVVHVASGVLPLDKLKFLVIDEADLMLSFGYNEDMKTLSRSLPRGTQSFLMSATLSKNIASLQKLVCRNPFILAVKDKEASGKLTQYVVKCSEQDKFLLAYILLKLRLIKGKILIFVNEINRCYRLKLFLEQFGLKSLVLNSELPVNSRLHILEQYNKGLYQIIIATDESGMMGEIEELENNVDFVEEEVISTDQPTLDKMKDQENADVNDESILAAAKDKSKKKKRVKQDKEYGVARGLDFENVACVLNFDMPSNTKSYIHRIGRTARAGKPGTAMSFVVPKSEVGKHKPTSLESCKKDESVLRRLEKKQISLQPYSFDKNQIDAFRYRMEDALRAVTTVAVSAARAAELKQELLISEKLKSYFAENPDELLSLTHDTVSSVRLGHTQRHLRHVPEYLLPKGMQAVNKDIGFVPFKKNNRRKVFKSRKNPKHRHDPLRSMKRKS O60081 THADA_SCHPO SPCC1494.07; CHAIN 1..1502; /note="tRNA (32-2'-O)-methyltransferase regulator trm732"; /id="PRO_0000372374" MDLSVIKAASLDLESLPSQPTVSSFQQLRETFIQSKSEDWYLKNGLFFRYYSFLKSSLENATLDGPSQVACLDTISVWLRRIFNACKQDPEISKYVWDTMELKFWTNLFSLPANKISIPGLTGVQVAVKDVFSKSLQLYLLVCPSEDIKNDFLLDSLKHALHWDRHAKVVCTAIQLLVKVTGAEAVFAFQPDFFEQSLKLLKDYSYAQAISSTILTVLTLRFKSLSEETEDREEVETKWMNIWCPIILYEFYGNDRQVQAGMSSFLIPSLLGVSPGITVKFLSRLQNYPNVSKDARDAACLYALKIAKDSKIIKNLDLVKEHAFVKTLFKHPDIKIQLACFRLIALCPNVSSPLSFEDFDCLESNIEFSFNVLDPDSRQILLKSMQDFFIRLRASCHSIARTMRSRHSDKVALSGLLDRAMQFLTSFISVCKKHLYPTCNYQQVLVSLSFLDTLISFGLDDNVESSSIREAQHDFPFSMVIIDRDLSRLMIDRLKDPYDDIRNLCLKILLSYKSLPGFISDSDAYFLFNHGLELLNAVRSHECDGGAKTIYLCNHFMEKSVPGSVLANTKVILNRLKSNIEHAKTSLLEAAVNCPLQGYLIQLTYIFQSLSPTIVKNDNESWKNIVMELIKASETIWGLIKDVLCDDSPEGNLPDGEGEGGIVSNLEDTPAQLILSYSWRSLKETSSLLTVLLTKCLSLFDEEFTPFTLNYYGELMMTWLWEIRHRGAFTSVYPCFIEYCSFLFECNKHEISELPDPWLHKNLSVIQEKSSFITRRSGGIPLSITAILVAGKDKREQLIEQTVISLISIAKQPVEQKNIAGQFDLPQVHAMNTLKTIFTEHRLSSVSVEYLEPAIALSIEGFSHELWPIRNCSVMLFTALINRAFGSKKPKDAVNLGNNKGLSTKMFFSKFPTLHDYLLRELEVSVASLSSNDQPSTGLYPILNMFSRLQYAQPYGNENEWTGLSQFEPLIFKCTASRICKVREIASLSLTCLLDCSKMTTFIVSQLKGVAGLQQNEIHGKLLTIRAVLSCFFSKLTLQQVQEFYEVVPLAFINCFLEFTSSKTSFYAKKLFLEVLNSYFMSNTDSNAKRLQQLRRMTMDYCKRMLLDRKANVTNVFNTIGLPIHQQMAATIFLENLKEFSVYCDAHSIGFLVSKLLHYEFYEVQLTTLRSIVDSPRKKIIVNNPEILQALIKLTPRNQWSQVRALALSLLSDSLNSTSYRLLGISCSDMVSNILSNECLPIKESFIVLLGSCIKQLKTENFLEYKVTFAKWVEILLSYSNEYQPFSSRKAALDSIIHFDLFNAESTAEAFSFEFYILYLLLGDFLNDDDEEIRSLAANHAYQVLGTSAQCVTEIWNLWKLRTKATFGGQHDFQHCINKRLILEDGCELASVQLDNALSRNCSLFERERQNLYYSDNQKLEDLLFYASYPNEKLKDWATDGINAILSRFEDVSRDGPLGKTSDPNVWFTIYKIIRIAEHVHLPLDRVHSLMNRIDGHPSFCQ O60084 TIM44_SCHPO BINDING 90..97; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC14C8.02; CHAIN ?..427; /note="Mitochondrial import inner membrane translocase subunit tim44"; /id="PRO_0000034318" MFLSRKITKNARTIVQCQRFFQTSIFSQNAAPQSPIKVFMDTFRAELKKSQELQDSVKALQDSSGSLSESDTFKKARDAYEKARSGTTAASSFTGKTVGKAGAKIGSYAQKAWESAPVQLSKKVISSTANTVATGVDTATKPVRETAFYKTIKQTMSDGSTSSRYGFYADKEQRKKLREEFERRNRMFASSARIQPNEDVQSVVVHSNPSWKNKVEQIKNESRLVRKIQELKKSYQESEHPIVSSIRDMADSISGVWSRMFSETEASQVMRRFKEIDPSFNTEHFLQYLREYIVPEVTEAYVKGDKEVLKTWLSEAPFSVYETTTKEYAKHGVVSVGKILDIRGVDIMSQRLLQPNDIPVFIVTFRTQEVHMFKDASSGELVAGKDDRIQQCTYASVFTRVEDELDNPETRGWRIVDFARARAVDYF O60085 MAP2_SCHPO BINDING 179; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 199; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 210; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 210; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 279; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 287; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 312; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 407; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175"; BINDING 407; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175" CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Note=Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. {ECO:0000255|HAMAP-Rule:MF_03175}; SPBC14C8.03; CHAIN 1..426; /note="Methionine aminopeptidase 2"; /id="PRO_0000311766" MTSATTTEATAKDLQEKLSLKENDVVEDDGKVEENDAAEEGASNGEKKKKKKKKSSKKKKTPQEQTNPPTVGLSKIFVNKKYPVGEVCDYAEDNLWRTTDEEKRALDRQNFDQYNDLRRAAEVHRQARQYAQSVIKPGMSMMDVVNTIENTTRALVEEDGLKSGIGFPTGVSLNHCAAHYTPNAGDTTILKEKDVMKVDIGVHVNGRIVDSAFTMSFDPQYDNLLAAVKAATNKGIEEAGIDARLNEIGEAIQEVMESYEVEINGKTHQVKSIRNLCGHNLDPYIIHGGKSVPIVKGGEEIKMEEGEIFAIETFGSTGRGVVHEDMECSHYAKIPDAGHIPLRLPRAKALLNTITQNFGTLPFCRRYLDRIGESKYLLALNNLVSAGIVQDYPPLCDIRGSYTAQFEHTIILHPTQKEVVSRGDDY O60086 ILV6_SCHPO MOD_RES 34; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC14C8.04; CHAIN 1..289; /note="Probable acetolactate synthase small subunit"; /id="PRO_0000317338" MFARRCGRLANRFVRLKSTSATSPITYKALHANSPLPRCRIIEPPRATVPEAVSNIIMSTPFNRVQRPKRHVFNCLVQNEPGVLSRLSGILAARGFNIDSLVVCATEVENLSRMTIVLRGADEVVEQAKRQIEDIVSVWAVLDYTGTSMVERELLLAKVSLLGPDHFQEHFERSEKVAESTNAKAKSDGEGVMNANAALQLRASQLAAINQLTTLFHGRVADISTETIILELTATPDRVDNFLSLLRPYGVLEACRTGTSAMTRAPHSNEVTEEAEDDVEVEEVFLPPG O60095 TGCE3_SCHPO ACT_SITE 214; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 382; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P80035"; ACT_SITE 408; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P80035" SPBC14C8.15; CHAIN 1..460; /note="Probable lipase C14C8.15"; /id="PRO_0000312661" CARBOHYD 308; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 457; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTLNGNIMKYCLEKGEILISFLLIALESMFRICTVILPSPLRNWFYEQSKKVYSYFLPELLVDDNANKLTDARDTIDLCALHGYDLEEHFVRTTDGYLLGLHRVYKKKKGKIEELNYLPPVLFIHGLMMNSESWVCNLKKEDAIPFALVEQGYDVWLGNLRGNKYSIKNIKFSSQNPKFWDFSLDSIAIFDIPSIVKYILSVNSFDSISLVGFSQGAILAFAALSIDTELRNSVRAFIALAPAIAPKKYSGRTVKSIIHANSQLLYLMFGRNSMLGSAVFWQAVLYPPVFAKIVDLFLRFFLSWTGKNISETQKIVAYSHLYSFTSVKCFVHWAQITRRKVLQMYDDSPGFKPSYYTNLNRIARYPIENIRLPITLVYGSNDNMVDIETLKTQLPPLSQCIQIPNYEHLDIIMGDTKKDIVIQQVVEQLNHVIAGDYFESIKEEFGLDTELVDGVMNHTI O60096 RT35_SCHPO TRANSIT 1..66; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC14C8.16c; CHAIN 67..315; /note="Small ribosomal subunit protein mS45"; /id="PRO_0000372637" MRNSVEFSQLGLKTAFNLSQNKTYTSAVKKQFFSTGAFLSNGGNIDLNKHTQKNIDSKYVACNSRSVTPPNDVASSVSKNTLRHKQRLMMAQWLMSPEVQKAKSSSSGNVGLGPNTNQPFPLNPFFKPPRPISHSLRMKITDEYLQGASIEVLARKFNTSPQRIEALIKLRRINDEFEEKKKPILHSYNEVMEKMLNACTKPEMMQFNDGNDIPLRSNPVSLWKSLPEGETFTPQEAAKILKWPSIEELNMRQNATHFHKTSDEHKDLNEDEELISSSPSEVGKRVFRLIDLSTGNVYRRDTGGDIYVKRKKSTT O60101 PGK_SCHPO BINDING 24..26; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 39; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 63..66; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 122; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 169; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 217; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 310; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 341; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 370..373; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; MOD_RES 75; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 76; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 172; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 173; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 183; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 260; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 299; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 328; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 351; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 373; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 387; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 390; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 412; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 413; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC14F5.04c; CHAIN 1..414; /note="Phosphoglycerate kinase"; /id="PRO_0000145889" MSLSTKLAITDVDLKGKNVLIRVDFNVPLDGDRITNNARIVGALPTIKYALEQQPKAVILMSHLGRPNGARVAKYSLKPVAAELSKLLGKPVKFLDDCVGPEVEKACKEAKGGEVILLENLRFHIEEEGSAKVDGKKVKADASAVEAFRKSLTSLGDIFVNDAFGTAHRAHSSMVGVDLPRVSGFLMKKELDYFSKALENPARPFLAILGGAKVADKIQLIDNLLDKVNRLIICGGMAFTFLKVLNGMKIGDSLFDEAGSKNVESMMAKAKKNNVEVFLPVDFVTADKFDKDAKVGSATAEEGIPDGWMGLDCGPKSSAKFAEVITTSKTIVWNGPAGVFEFDNFAKGTKSMLDACVKTCEAGNVVIVGGGDTATVAKKYGKEDALSHVSTGGGASLELLEGKALPGVVALSSK O60104 MED7_SCHPO SPBC14F5.08; STRAND 211..214; /evidence="ECO:0007829|PDB:5N9J"; STRAND 219..222; /evidence="ECO:0007829|PDB:5N9J" HELIX 18..22; /evidence="ECO:0007829|PDB:5N9J"; HELIX 25..37; /evidence="ECO:0007829|PDB:5N9J"; HELIX 56..64; /evidence="ECO:0007829|PDB:5N9J"; HELIX 192..195; /evidence="ECO:0007829|PDB:5N9J"; HELIX 223..248; /evidence="ECO:0007829|PDB:5N9J"; HELIX 250..252; /evidence="ECO:0007829|PDB:5N9J"; HELIX 253..314; /evidence="ECO:0007829|PDB:5N9J"; HELIX 322..334; /evidence="ECO:0007829|PDB:5N9J" TURN 215..218; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..376; /note="Mediator of RNA polymerase II transcription subunit 7"; /id="PRO_0000096392" MEPNEGVQLFSAFPPPPPYYKLFTRENIEKVISNMEKEAKHEDDANTLQPKTEEEIESLAKLFKKPSCLTSGTYQMFGDTWRLDEAIPSLKEFGIPELYKDIKDGEDEIEVVEYDPKSNAIVGTSFTRVHDYDKNSPIENEKILEDDQHTAMKEKDNESDKTMKDVEEKTEPSLKKEEEDIQMKEPLDSQDTGAVSASSVNEGFRADQKSKDGETSDLIKIPRRAYELRFLSRSLMLNFLELLGIMAKAPEQFPSKVENIRVLLLNLHHLINDYRPHQSRESLIMLLEKQLKHEESQVELLRTHNRQMTETLEKYKSLDFNMEKEGDVIQQLKSSIKKPLSGAEDEQKSRSMFSKNDEKLKKSLELMEDVIKRDLS O60109 PPB_SCHPO ACT_SITE 115; /note="Phosphoserine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10042" BINDING 68; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 166; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 168; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 306; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 311; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 315; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 352; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 353; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 456; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions. {ECO:0000250}; SPBC14F5.13c; CHAIN 1..532; /note="Alkaline phosphatase"; /id="PRO_0000186165" MASERDPLLPVHGEGPESPSRRNWKTWIKHGILLILVLSTVIFFYFFSSHKSKGTNEKPKFVIMMVSDGMGPGSLSMTRSFVETLNDKEGYRLPLDEHLIGSSRTRSSSSLITDSAAGATAFSCANKTYNGAVGVLDNEKPCGTILEAAKEAGYLTGIVVTSRVTDATPASFSAHAANRFMQDLIAEYQVGMGPLGRSVDLLFGGGLCSFLPKSTYRSCRSDNLDLLKYARKKEGFQILLNRTDFDELSNAQLPLLGLFSDYHLSYDIDYQPEVQPKLSEMVETALDVLLNATNEDTSKGFFLLIEGSRIDMASHNNDPIAHVYEVMEYNRAFEIASAFVEKNGGSLISTSDHETGGLTVGRQVSKKYPEYLWKPQVLSLALHSIEYLASAIVNHNQNTLLPYIEQFVLPAIGIPDPNPKQIHDIYVARHNIFNLINVLSDIVSVEAQIGWTTHGHTAVDVNVYGVGEVTEHLRGNMENIEIGQFMEIYLNVSLSDVTEKLKDAPIHGAPDRPSLVETSFSDRLVGFGADLF O60110 OCA3_SCHPO SPBC15C4.01c; CHAIN 1..282; /note="TPR repeat protein oca3"; /id="PRO_0000353838" MSNSILKVPDQNPQEIVALFSQQEAYAKLGKYKDEIWDVYQKVFIAALTTGETVLAKKCWNRLNDRFHKSPRVEGLYGMFLEATASEKDAMSYYNSKLSEDPTHTVIYKRKLALLRSMGQTKECIQGLINYLDTFYNDLEAWAELADIYVSVEAFESAIFCYEEMVLLQPFEPRLFARLGDLYFVLAQSNATNYWFSLKHYCRSVEICEEYFHGWFGISKCCQQLLELSRTELKRLLSKVNEKISDTFPDTESVRQLYQLSLKKSDLFAQKQPKLKALLEQC O60114 YG65_SCHPO BINDING 654..661; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPBC15C4.05; CHAIN 1..1428; /note="Uncharacterized helicase C15C4.05"; /id="PRO_0000310783" MAKKKSKASNSARGYATTSIPSRSASSPANKNQVKGEKNNKTQKVEPKNAFKVENQSNDIGVDTVDAFDHLLLDKTLPTIDAETEVIKNTSLSNSKSFLHSWQTDIRLRKNDNVLGLTEDEIQQILKTFRDSWKSSLKESYAFSNRSSFSLRKRYLWTTFLSLKGMGFEESEIFGAFSSIPIVSIDEYITWMITENLINSEPSNSSFSYEVQPSNYTTFCRMLDEPLPANNPVQSNSRLVPLMKDFSNDIKHTPNKETQPSNQVDDSLKSKDSKPLTMSEVLTQLPEDDIPFDDPFDLTSQYVKVKLKMLRLQIANKKNSEEFSTLNLQLESITSQYLFSSKEAEIVFRKSRIEFMNKLKALQQKLENERIVEEIKKNGIQEDSQSTDDSSKDDDNNSESNDMSPHNDAETRADDDAYLMGDLFNQEEEDIQDTENDLLNANYTLLPLTTDKSGTRPSTTLQYELHKIGSNIKAEFKTMPIGKIGYQSTCFVRCSTGQKTFSDLKTVLPTATLAADYISMIVLFRLMANFTKISLQTFPKSFKEVYGKFSAEKQNTDLAEDAKISEKLDSIIKSKELETPTSATTSKLMAPMDNIGKFSGFERPPETLLNKWRQQLESESAEKFKVFRNQLPATMFRETIIDAVNNSQLLIISGDTGCGKSTQIPAFLLENSTKNGKAVKIYVTEPRRISAISLANRVSQELGGNPPSARSHELVGYSVRLDSKCTPLTPLTYVTTGTFLRLLEVGNEIESVTHLIIDEVHERSIDSDLLLIHVLHLLKQHPHLKIIIMSATLNAEKFQLYFEGSNLITIPGKTYPVHRFYLEDILSQFGNDKSFGNAAGQDVIEEDDYETDQQDASISNKSAEDAIVEMNLIPAWYNEKAINYGLIVYLLKYIFTEGDPKFSKCVLVFLPGISEILRVKSLIEDMPMFRNHRKFCIYMLHSTLSSAQQQSVFNIPPKGCRKIVLSTNIAETGVTIPDVTCVIDTGVHREMRYNSRRHLSRLTDTFVSKANAKQRSGRAGRVQEGICYHLFSKFKHDTQFLSYQTPEILRLNLQEVVLRVKMCQMGDVQDVLGKALDPPSSTNIIRALEKLHQVGALSENEKLTKLGKFLSQLPVDANLGKILVLGCFYKCVDAASSIVAMLTIGSPFRKSVDNEFSANKARLSFAKENTRSDLVLMYYAYCAWREICLSPLGPDEDSFAKEKYLNLEALSMTESLKIQLLSELKDMKLLGASDVDTCKSLKRSICRRFAVIPKEHDINSGNAEILCGVIAASLYPNILRYDYEKRQWSTLSTNKRVRILDVSVNNRSELPNMPSKFVAYTNMMSSTRASEYVNETTMVTLRQLLMMCGLKVENRVSVGQAKLDNFTVYFENVYVSASLSILRRFIETSLNEFFAEPDKRLLNSHLEVIVNIVSRLNYGTKFQKRLKD O60116 RBSK_SCHPO ACT_SITE 262; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215" BINDING 11..13; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 41..45; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 146; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 190; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 229..234; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 256; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 258; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 261..262; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 262; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 292; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 295; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 297; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215"; BINDING 301; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000255|HAMAP-Rule:MF_03215" CATALYTIC ACTIVITY: Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+); Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216; EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_03215}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03215}; Note=Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate. {ECO:0000255|HAMAP-Rule:MF_03215}; SPBC16G5.02c; CHAIN 1..318; /note="Ribokinase"; /id="PRO_0000080093" MINIVVLGSMNTDLVMRTKICPSGGETIHGEPDGFSTGNGGKGANQAVAVARLSNPADTKVSMLGCVGDDAFGVEMLSGLKKDGVNVDNVKKIENKSTGVAMIIVEETGENRILLSEGANGNVDTAFVKAMEQRISTCNLLIMQLEIPLEAVEIALQIAHKHGVDVLMNPAPAIPLSHDMISYCAYLVPNEHEAAILLNQADSPATLENVDAYASKLLSFGVRKAVIITLGSQGAYYKSANGESALVSACKVKAVDTTAAGDTFIGAFSNSIAHGQPLKDSLEFAAKCSAITVQRKGAASSIPSLLEVDGSFNLKKNT O60118 RM23_SCHPO TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC16G5.04; CHAIN 30..157; /note="Large ribosomal subunit protein uL13m"; /id="PRO_0000314627" MSTLNGQTALAYAKVWHHVSAKNVPLGRLASQIATTLMGKHKPIYHPAADCGDVVVVTDCSEIGISGRKLENHKYYSHSGQPGHLKEWTMEEMAAKRGHKDLLRRAVGGMLPRNKLWDRRMKRLYIYDGAEHPYKANIFRSYHNPVSSQIAKELFSK O60123 KEX1_SCHPO ACT_SITE 175; /evidence="ECO:0000250"; ACT_SITE 367; /evidence="ECO:0000250"; ACT_SITE 427; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; SIGNAL 1..21; /evidence="ECO:0000255" SPBC16G5.09; CHAIN 22..510; /note="Pheromone-processing carboxypeptidase kex1"; /id="PRO_0000314765" CARBOHYD 51; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 392; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 416; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MISKLLKIVLLTAGVIGNTLADSRIHEQYLVKAFPNEPVDYEGRMHAGHLNQTDQLDGDLFFWMFESVKPEYEHRSILWLNGGPGCSSEDGSLMEVGPFRLDDNNTFQLNPGRWDELGNLLFVDQPLGTGYSYSLAKDFQSNNEKMANDFSIFFEKFLEEFPERANDEWFIAGESFAGQYIPHIAAKLKEKNLVNLGGLAIGNGWINPLSHYETYLNYLVEKGMVDFESELGQYLHHSWAECLLAFDKIGSGSGDLSKCESFLGDILYMVSKEPGKACMNMYDISLESTYPTCGMDWPYDLSYLTEFLSTREAMTSLNVNLEKVHDWEECNDDVALQYAREGIESSSKLIQDLVSTVPILLFYGENDFLCNYLSGEKLTRSLEWNGAVGFQNQSAQPFYLPGYSDQPSGSYVSSRNLTFARIVEASHMVPYDHPNEMKTLITAFFNNDFASLPSVPKPSPDLGNGNYKWLYLGLIPVALTIIILFSIYLCRRFGLFGLSKQRYQPISPTP O60125 BAG1A_SCHPO SPBC16G5.11c; CHAIN 1..195; /note="BAG family molecular chaperone regulator 1A"; /id="PRO_0000088879" MSEKTSTVTIHYGNQRFPVAVNLNETLSELIDDLLETTEISEKKVKLFYAGKRLKDKKASLSKLGLKNHSKILCIRPHKQQRGSKEKDTVEPAPKAEAENPVFSRISGEIKAIDQYVDKELSPMYDNYVNKPSNDPKQKNKQKLMISELLLQQLLKLDGVDVLGSEKLRFERKQLVSKIQKMLDHVDQTSQEVAA O60127 PTF2_SCHPO SPBC16G5.13; CHAIN 1..126; /note="Pdp3-interacting factor 2"; /id="PRO_0000116769" MDEIQESSCNEKLSDEDLAAEFVEFTDNIPIEIYRSLRYIRKYENFFAKENENLNTAARLVCDCPISEVPSAKQKLADSLFTSHEYLRQTSAEANKLYENVLASYKHLCEKIKYLEADNPLYVPAP O60128 RS3_SCHPO MOD_RES 32; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 106; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16G5.14c; CHAIN 1..249; /note="Small ribosomal subunit protein uS3"; /id="PRO_0000130331" MSAAFTISKKRKFVADGVFYAELNEFFTRELSEEGYSGCEVRVTPSRSEIIIRATHTQDVLGEKGRRIRELTALVQKRFKFAENTVELYAEKVQNRGLCAVAQCESLRYKLLAGLAVRRAAYGVLRYVMEAGAKGCEVVISGKLRAARAKSMKFADGFMIHSGQPAVDFIDSATRHVLLRQGVLGVKVKIMLPEPKTRQKKSLPDIVVVLDPKEEEPITKPYTVINQPVEAAAAAGQEVVAEQETAVAY O60130 YH7G_SCHPO MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16G5.16; CHAIN 1..827; /note="Putative transcriptional regulatory protein C16G5.16"; /id="PRO_0000310383" MSSGDVSRRQRVSRACDECHRRKIKCDQRRPCSNCIAYNYECTYGQPFKRLRHAPEKYIEFLELRLKYLRGLAEESDPNLKLPSFLAPPNDKDSPVNQSPWKRSDSSKRSSSQDEFESLFDRYGQLSLKDDGKADFRGSSSGFVFMKNIHQNIARNSTVPNPVQESNSSSSQPDPLSFPYLPPTPAEDEHKKPPLKIQLPPYEEALSIVSQFFMNDHFLVHIHHPASFFEKMHMYYKTGKTDNNFHFLLVATLCLGYTYMPDESPSANYPYHEAYEYYYYIRSSFSWEDSYTIEVVQILLSVALFALFSSRLSQAYTFTNNALLCCHELGLHKDFSDVLTSHESRLSKRVFYSVYVLACYTSTIVGLPLSIEDVDIDQSLPNSFDFTLENDQVPPRLIASECTSLEVFIQHITLSRILSHFVRKVYPVKSPSDSHCKVSLPAVRDHEEKLTYWWKNLPSYLKMSEVPKFSPKWIQAIILELKFRQIELIFYRPFIHSISTPIDNQNGSPMKPANFALKCAQSAERVVFLLQELAKSPNTPKLFFNLYSGYYALMTLTYCATLTKDDANKSNNFITKARLGFHCLQMIYRESTYYSTIMEAIKNLLIAYDMNSSGTENLDATPDVTGQLPNNFSQRTSNIPREFPQAQIFYSDAPYPGYYNPAQFQNAPTNFPMPTYGGRTQDQSYPRQNGYPSYSDGNVYPHDRVMINYGSSMPTANGFYVPNTYSPVPFPYNTSYPPYMSPTSNMPQAFQAYSQYPYQHPPFPLSEQMLPLPTSGVMMAPGAAKSGMPYPFIQPPSMTNQVAYPTVRDGSNNSPDHPSSSNSKRTE O60137 SWD2_SCHPO SPBC18H10.06c; CHAIN 1..357; /note="Set1 complex component swd2"; /id="PRO_0000051252" MTTVSITFDLLSSMQPRKWLKNQNFVGEITSLSFDDSGELCLASCTDDTLQLYNCISGKFVKSLASKKYGAHLGRFTHHSNSLIHASTKEDNTVRYLDVVTNRYLRYFPGHKQTVTSIDVSPADETFLSASLDNTIRLWDLRSPNCQGLLNVSSPVVAAFDATGLIFASVSERKYKISLYNIKSFDARPFQDIPLTFLPPHVRIANVEFSTDGKYLLLTTGNDFHYVIDAYSGSELLRVPSKVSTKTQDGNLTYYASACMSPDSKFLFTSYDNEHLCMYQLPELKQTVNSDHIVNSFTEMGLASTTPTSNSHSTENPLAIIPSSTSKNLLPETPSIVRFNPRFSQLVTAHSGVIFWT O60141 CWC16_SCHPO SPBC18H10.10c; CHAIN 1..299; /note="Protein saf4"; /id="PRO_0000358864" MQGFNMGKYIPPEGPNAKRKFDKLRNVIRFEMPFPVWCNNCENIIQQGTRFNAVKKEIGSYYTTKIWSFSLKCHLCSNPIDVHTDPKNTEYIVASGGRRKIEPQDINERPAKAENDEKVPSDAIEALETQLTQQKSEKHNSSVINFIYEKNERLWSDPFVSSQRLRKQFRERKKIEKKQEAKDLSLKNRAALDIDILPPSSSDKDKALLLLDNELGKNKFIRKLDYRRTLMPSSRTFSTFAKFAETSFAKKDPFARKFVPSEKLRSEQRKFPTENLKGEKILEDNSVSLVNYEVSDDEG O60142 PPR2_SCHPO TRANSIT 1..33; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC18H10.11c; CHAIN 34..432; /note="Pentatricopeptide repeat-containing protein 2, mitochondrial"; /id="PRO_0000316604" MQFIKRTFPRRAFVDLLLNRFCLREFATTYSVSVSNARKLVRKRLLIADALKFKEQVNNLNEFRNKKTKSSLIRNDGFKLAKNVSSLLQKESLEKALHLLYERSNAKKTVAYNLVLQYHLAKGHYNAAWSLYNDMKKRQQKPSDHTYSILLKGFCDAIEKNKQGNFSKLREYSEKVTASALKESNNVTSNLHHIRIISKCSLKLKSMVLVSMIIPSIKQTLDFYSGSQILRLLNDFSMFNPEQREEVLKMGTNLWNYFVLECQKKGIAVDESLICSFVKLLATSNSPQVRNVGLNILTKVMGLEYQIFEDSNLRYPLPPYCDCTSRSLVTALQVIRQIQNGDLLARYWKYFEESHKFDLNLQVYHEKLRNLVQQGQAAECLNTIKRMSHNGPFPTQQTFLIVLSLCKRPKFYSYTKSFLDLAKKLNVPVEAT O60146 YNSG_SCHPO MOD_RES 9; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 64; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 270; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 271; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 901; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 936; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 939; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC18H10.16; CHAIN 1..1050; /note="Uncharacterized transporter C18H10.16"; /id="PRO_0000310954" CARBOHYD 175; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MARLLTKSSQVFDFLADRLSVRKSRRFWETQENLESSTPLLQEPQQSYRSNSFNELPPLSRSVTFAENEQPNEAVKLGTFEGCFIPTTLNVLSILLYLRFPWIIGEAGVLKTLLMLFISYAVGIFTSLSISAICTNGMVRGGGAYYAVSRSIGPELGGSIGLIFYVGQILNTGMNISGFVEPIISIFGKESGTISQFLPEGYWWVFLYTTCVLAMCCILCCLGSAIFAKASNALFVVIILSTISIPISSIFVHPFKDPSLLVHFTGLKWSTLMKNLASAYTENEKGTGYESFKSTFGVFFPATAGLLAGASMSGDLKAPSRSIPKGTISSQATTFLLYLLVILCVGASVTRTGLLLDMDVMEHISLHPLFIISGILSSGAFSSFMGIFGAAKLLQAIARDDLIPGMFFFAKGSSYDDIPYVAIGVTYLITQISLFWDINMLSSMITMTFLLTFGFINLSCFLLRISSTPNFRPTFRYFNRRTTLVGTILSFGVMFYVDRLNAFISFLIAGILVVVIYFTCPPKNWGDVSQGIIYHQLRKYLLQTNKARENIKFWRPQILLLINNPNRSENVIRFCNSLKKGSLYILGHVIVSDDFQASMDDLRKQQRLWHQFVLDRGIKAFVELTIAPDEVWGIRGLISSAGLGGIRPNIAVLTFINTNYRRHRIYSGSSFSLENTSEESESDSKKEFVEHDILPVKWVQILEDMLVGSVDVMVTNGFDRLNWPKRKGEKQYIDMFPIHRISGVGSEVNESTPTFATNFETYTMVFQLSWILHTASDWKQGCRLRLITLVEFENEIEAERESMHQMLETFRIKADVVVLCLAAMNLDAYRYIVKNEHVRPSKSSELENLLKDDSWWQEEKKRRGNTVDSLGPIRFPRRMSGYNFRSASFDKSAPPLSVPLSFRLGPHMHSVKSFETESSFGNRSLSPKQENRRTYSDSTIESSLMPNVVREDSSSDRLAPKKKIGRDYSKEKLTFNDLSSRSQYIIMNEIVLKHTKNTSVLFTVLPAPLADTHKSFRKSEEYVDDLLIFMEGLPPCALIHSKSLTITTAL O60149 VPS38_SCHPO SPBC18H10.19; CHAIN 1..474; /note="Vacuolar protein sorting-associated protein 38"; /id="PRO_0000372371" MSLELPGNYRLSRLKSIQIRNVQEIQNHSKFAINTTENLWKRDVQLKRAISEGTIRIFISLHVQSKKLPVYITETSGNANHIFYVDEKVTEKLQKYRHEEYFIVRTWCSSSSHAFKLHKEWKILRYDSNFRYIGNDPVFAVCHIRNGLLCEFNDGVYIYTTSQSSDIMRQTSFPKSASTYSIDRRKDGYTIQKITRILKLAECIDEMHIAKHEIRAHFQEEEFQQIRLMHKRMLLRDEKIDELAKLEHLWQKQINSITQMRTKFDKTKSWLSSKRNTLNKSKESLQKDEAEYVELANSLKTKVETNIEIRILMAHAIRMHVSHLSKIYPIQPSPGNHDEFTIRNLRLSFEPDKINNVEMAASIGFLAHLLQTLSKYLEKELAYPILCASSRSSILDTLTPDIPTRIFPLYPATRPIELFEHAIYLLNQDVNDFLETFGLPIDQSMDILRNFKKLLQFILSGQHLSFVQVTSTAP O60150 YNSK_SCHPO MOD_RES 12; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC18H10.20c; CHAIN 1..361; /note="Uncharacterized protein C18H10.20c"; /id="PRO_0000372372" MPLKLALPRSTTPKDPARCTLDIRMESPPLVFLGSPETSSGALASGILKLTILHQPFIKVHTLKLQLIKRITVLHPAISHCSACAGSKEVLQTWDLAANTTYRPGTQHWPFSWLFPGSLPASVSNRYIKLEYYLEATLCYGTPEGGISPSKPEVLKFPLQLKRAAIPSPDTIHKRIFPPTNLVANITLPSTLHPHGAALMEVTMTGFAQNDGNDWKINRVTWRLEEHMQFSCQPCERHRDLVKPRPIEEKRILSTQDLQSGWKFIDNQMFLSTQINTSSLREPSCDVEIPAPFSLKVSHHLIFETIVNRKKNVAGNNMGNARILRVSVVQPLTTPAGLGISWDEECPPVFESVGPAPPAYT O60155 PRS1_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215; EC=6.1.1.15; SPBC19C7.06; CHAIN 1..716; /note="Putative proline--tRNA ligase C19C7.06"; /id="PRO_0000317133" MSVDSLVSCLEQLITDDLKLVEHQEVSNGATWASALQSTKDVPSHALTKTIVLKPKTAKSQTVVPIILAALETTSTPSGIAAKAVGSKEARMAAADLVEEVFGIPPTDVGIFSVNKENASKVHVVLDAALIQHNGLLAFHPSSSAKTVFVSPAAVQTYLKSVGVNPIIVDFSAPGSATAPSKPAAQKKKAEPSKNDAAIENAALIGITVRKDADFPNWYQQVLTKSDMIEYYDISGCYILKPWSYSIWEAIQGWFDKEIKKLGVRNGYFPLFVSSKVLEKEKDHVEGFAPEVAWVTRAGTSELDEPIAIRPTSETVMYPYYAKWIRSHRDLPLKLNQWNSVVRWEFKNPQPFLRTREFLWQEGHTAHMTLEGATEEVHQILDLYARIYTDLLAVPVIKGVKSENEKFAGGMFTTTVEGYIPTTGRGIQGATSHCLGQNFSKMFNIVVEDPNAEIGPTGERPKLFVWQNSWGLSTRTIGVAVMVHGDDKGLKLPPAIALVQSVVVPCGITNKTTDQERNEIEGFCSKLADRLNAADIRTEADLRAYTPGYKFSHWEMKGVPLRLEYGPNDAKKNQVTAVRRDTFEKIPVPLNNLEKGVSDLLAKIQTNMYETAKAERDAHVVKVKEWADFVPALNKKNIVMIPWCNTTECEKEIKKNSARQVNGDEPEDEKAPSMGAKSLCIPLEQPSGEDAIIEGTTKCAGCGNLAKVWGLFGRSY O60156 SEN34_SCHPO ACT_SITE 206; /evidence="ECO:0000250"; ACT_SITE 214; /evidence="ECO:0000250"; ACT_SITE 245; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16; SPBC19C7.07c; CHAIN 1..284; /note="Probable tRNA-splicing endonuclease subunit sen34"; /id="PRO_0000109467" MEDEKFPISYVHGKFLVFDVQAVEVFRKNYHILGTLVGTLPQLPQQNVFLGLPMELSKEEAFYLIEKGISYIVDDTKVHKQLLENTTKDDVKQCLKKRQSLAYDQMIAAKKKENEKKIEIMKKLGRTLPLDPLNYDEHDSFDLSWIPVDTVTTRIAEKSSMNDDFHKEEDVFENLDINRYLMFKSLVDTGFYLNPGLRFGCQFVAYPGDALRYHSHYLVNSYKWDQEIPVLFLIGGGRLGTAVKKTWLIGGSNDRNINMNGEKSKEELLLLPVRHFSIEWAGFG O60161 UTP4_SCHPO SPBC19F5.02c; CHAIN 1..710; /note="U3 small nucleolar RNA-associated protein 4"; /id="PRO_0000307921" MDIHRCRFIDYTPSAITAMAFSHKSGQNDSMPNNLLLAVGRASGNIEIWNPRNDWCLKTVLYGGVDRSIEGIVWSTGEEELRLFSIGFSTTITEWNLHTGKPLVNQDSNAGAIWSIAICDETKTLAVGCDDGSCVLFDISGGPGVIEFKRVLMRQTSRILSLDFQTKDHLVGGCADGVIKVWDLSTPNSAIISRMQVDRARKGEAALIWAVKSLRDGTIVSADSSGAVKFWNGKFFTLSQSFKLHLADALCLGVSANGDMVFSSGIDRKTIQYSREGGKREWVSNSFRRFHSHDVRCMAVFECKSLDVLISGGMDMMLAVIPVRQFNRKNHRMISAVPQRPRMAVAPKARLFMLWNDHEVLLWRIGSPGYRFLLKIVLADEENISHAAISPDGELIAISSVLRTKLYQLQYSDENVKVETVEDSFLSNIGASLLSFTVDKNKLILVSNDSEIFLIELSRLDSRQLEVFELSQPTSKKIAPRQRSNVSSMCDGICSIAVSSDGDYFAVADTVGNIFCYSLSNLTYSELPRVNTYVRAMAFRPDVRGRLAVATAGNQVYEFDVQSRKLSEWSKNNSTNMPKEFSQLLDKAFGAFFDSKHPSRFWIWSANWVSFFDLNLQLPAPRAAGKRKIEMNATVDGNLNDKKLANANSNGISNYGTGDSRCFWITHKYRPMLLVGSVGNSELLVVERPIADMLMSKSMPASFYEHKFGS O60162 YG23_SCHPO MOD_RES 46; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19F5.03; CHAIN 1..598; /note="Uncharacterized protein C19F5.03"; /id="PRO_0000317230" MVQFEANEKQFKLRREDCCLTIDRESGAVSFEPDELKPVARSKENSVTLFGSIKLKKDKYLILATEKSSAAQILGHKIYRVHKFEVIPYRNLLADDQDELDLYNLLQNHLKTGPFYFSYTWDLTNSLQRSCTDEGKASPILRSDKRFFWNEFASKDFIDLIGAHSEVSLFITPMIYGFITSASTIVKGRTITLALISRRSKQRAGTRYFTRGLDENGNPANFNETEQITIVSDEKSEVTYSHVQTRGSVPAFWAEVNNLRYKPLMVANSASMAAAAAKKHFDEQISIYGDQVVVNLVNCKGHELPIKQLYENVIRRLDNPHIHYHYFDFHKECSHMRWDRVSLLLNEIQPELEEQGYTTLDTQKYRVLSRQNGVVRSNCMDCLDRTNVVQSCIGRWVLTNQLRKCGIIGATHPLRSVIPLDNIFCNIWSDNADYISLSYSGTGALKTDFTRTGIRTRKGAFNDFVNSAKRYILNNFYDGARQDAYDLVLGQFRPDVNFRYRLDLRPLTIRCVPYILLACLILFFMTLFSRSSSTILPPSILLILTFLGIVASLYYCFAHGLQFINWPRLLLPSFLRSDMTPEGRVFVINRQLASKHKV O60167 YHC3_SCHPO MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 287; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 414; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 417; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19F8.03c; CHAIN 1..649; /note="ENTH domain-containing protein C19F8.03c"; /id="PRO_0000303952" MSPSKWLLTYERAVKKATKVKLAAPKYKHVEIILEATTEDPETLENVIQALCERLKEQSWTIVFKTLIVFHVMLKEGAPNTTIVALSQRPRILEVLKASSLLAQGKNIYNYSRFLSERAKQYGRLGVDYAQVGDAPKKKIREMKLENGLLRNVEGIQAQLRRLIKCQFVAEEIDNDIAITAFRLLVGDLLVLFKAVNIGVINVLEHYFEMGHHDAAQSLRIYKTFVNQTEDIINYLSTARSLEFVTKFPVPNIKHAPISLTASLEEYLNDPDFEENRKQYLQNKSGSPVEETAILNRKPTLRKKKSIPKKQNESSSTIQKENTVQQEASSSEEEAVKSLPETQRTTSRIETQEEEIKEEEMEGEEEEEEEEVPNYESENELEDKVGDLSLSLGVASSFVDEMLRERNNLSAEGTSASPSLDKKSESTNIVQPIPSHPNDSLNPFYNSSSPTYHPQPIPPQLQQVQLLSQMAGNQMANIQYTMNGMQQTGASPNTALNISQVNMYAQNNPVNPSTTNPFQNFLRQPSYQGMQFEQQQPTTIPLQPNIPVLNQQYPVMIPAMEDSRGPLPSPAHIMYPEGSPGFIQHSPNGFTHGHSASPVNIGQKLDVPERPMSTPYTASKNPFSTRELAEPTDLARNSISTESKNPFRS O60168 LCL3_SCHPO ACT_SITE 104; /evidence="ECO:0000250|UniProtKB:P00644, ECO:0000255|PROSITE-ProRule:PRU00272"; ACT_SITE 112; /evidence="ECO:0000250|UniProtKB:P00644, ECO:0000255|PROSITE-ProRule:PRU00272"; ACT_SITE 152; /evidence="ECO:0000250|UniProtKB:P00644, ECO:0000255|PROSITE-ProRule:PRU00272" BINDING 109; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250|UniProtKB:P00644, ECO:0000255|PROSITE-ProRule:PRU00272" SPBC19F8.04c; CHAIN 1..230; /note="Probable endonuclease C19F8.04c"; /id="PRO_0000312663" MQESQYKEKAIIGTGLITTSIGGFFFLRRFRRISNASTIPKNYLNNSTVENRKYKTMFGYVTRVGDGDNFRFYHTPGGRLLGWHWLRKVPCSRSDLSNETISVRLAGIDAPESAHFGKQEQPYALEAKEFLHNKLYHKSVRIIPLKIDRYARLVAGVQYYPIPHFFWKKDIGPQMIRKGLAVVYEGSDGVFCPTKKECLLALEIVAKKKKLSLWSQGKKLILPSVYKRGV O60171 TAF10_SCHPO SPBC21H7.02; CHAIN 1..215; /note="Transcription initiation factor TFIID subunit 10"; /id="PRO_0000326090" MSDINNNEPAENIEQPKQEPEDGNNSMSVDEQPETSSTNLPTGDNLAPMSVESPAHLNNEDSPKSDDSRERHGSNYVIEPHLELRDMAKDKTLENFLAQMDDYSPLIPDVLLDYYLSLSGFKCVDPRLKKLLGLTAQKFISDVAQDAYQYSKIRTGSSNASSTTFGAQNFGAGGASGIGSSGRRGDRGKTVLTVDDLSAALNEYGINLKRPDFFR O60172 PPA3_SCHPO ACT_SITE 69; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P07102"; ACT_SITE 341; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P15309" CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000250|UniProtKB:Q01682}; SIGNAL 1..18; /evidence="ECO:0000255" SPBC21H7.03c; CHAIN 19..463; /note="Thiamine-repressible acid phosphatase SPBC21H7.03c"; /id="PRO_0000311718" CARBOHYD 98; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 324; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 439; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 458; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MQLCIISLWFLAAFIVNADNVQFEDYESNFFFKEHLGTLSPYHEPYFDGLDSAFPETCEIQQVHLLQRHGSRNPTGDVTATDVYSSQYLNNFQEKLLNGSIPVNFSYPENPLCFIKQWTPVIDAENADQLSSRGRLELFDLGRQLYQRYYKLFDSYVYDINTAEQERVVESAKWFTYGLFGDKMYEKTNFILISEGKAAGANSLSMYNACPVFKDNNFHKNATDAAHAVWRNIFIEPIVNRLAKYFDSSYKLTINDVRSLFYICEYEIAIKDHSDFCSIFTPSEFLNFEYDSDLDQAYGGGPVSEWASTLGGAYINNLADSLRNVTNPDFDRKVFLAFTHDSNIIPVEAALGFFPDITPQNPLPTDKNIYTYSQKTSSFVPFAGNLITELFFCSDSKYYVRHLVNQQVYPLIDCGYGPSGTSDGLCELQAYLNSPIRANSTSNGISIFNTECQARPTNVTIYF O60173 DBP7_SCHPO BINDING 185..192; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC21H7.04; CHAIN 1..709; /note="ATP-dependent RNA helicase dbp7"; /id="PRO_0000232259" MADEPLLLNFVVDNAQSRKPEALKSSRRWTDRARDRKRQKRNSNESSKSTVKRNSGTNGASTDYKNSQKEKVINPVFDPRKPAHELKGNKRDNTFVTSLFTGDDSEHFSQDVGQNLEDNQISNIGTTKEASNAPIKTTNFAGVQLDTQLADHLNNKMNISAPTAIQSCCLPALLNTDDKDAFIEAQTGSGKTLAYLLPIVQRLIRLPKNLHTRTSGIYAVIMAPTRELCQQIYNVANKLNNNPLSHWIVSCNVIGGEKKKSEKARIRKGVNILIGTPGRLADHLENTEALDVSQVRWVVLDEGDRLMDMGFEETLTKILSYLESQSSIIKKDLSIPSRKVTMLCSATMKDTVKRLSDSALKDALYLKSSIVEETNDGYSQAPEQLLQRYVVVPPKLRLVSLVALLRSHVRSYKKIIIFLSCSDSVDFHFEAFRCAINADEMEEAVKEKPDSEGDIISNAPALRIDGKSNVYRLHGSLSQQIRTSTLNLFSSSEDSGSHILLCTDVAARGLDLPNVDLVVQYDAPFSTDDYLHRIGRTARAGHNGAAIMFLLPKESEYINLLKSSVSANILEQPNGPSGLLSAGFSQGKTNTNDWQDRATEWQLELERFILENEPMRNIAKRAFTSYVRAYATHLSSERSIFNMRDLHLGHIAKSFALREAPGKISGANSSKPRKQGGSVDKGKSKSSKDIAALMHRKAMEHYSTEHNIG O60178 NTA1_SCHPO ACT_SITE 43; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 121; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 155; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" SPBC23E6.03c; CHAIN 1..286; /note="Protein N-terminal amidase"; /id="PRO_0000314759" MKFGCVQFFPKLGKVNENIVHLRQLLDQHSEALQSVKLLVFPEMCLTGYNFKNSESIQPFLENVTSNHCPSIQFAQEVSEQYRCYTIIGFPEFQNSNGISTLYNSTALISPKKELLNVYHKHFLFETDKSWATEGKGFSFEPCIPELGPISMAICMDINPYDFKAPFEKFEYANFILRELEHQQMVSSNVSRPIICLSMAWLVSDDKVIDASLPDIKNLHYWTTRLSPLINSNTDAIVLVANRWGKENDLNFSGTSCIMELSQGRAILHGVLKAAENGIVVGELEK O60179 UTP10_SCHPO SPBC23E6.04c; CHAIN 1..1649; /note="U3 small nucleolar RNA-associated protein 10"; /id="PRO_0000186206" MASSLQKQLKNIQSNNVLKINKIRRAPSLLYDPKVAADMDLEEIYVTAVSGFHELAVHEPRLLYFEKTLLGEQSVQVDRVLLNRTENEKIDLECVQILRLLAPFFTEKNALKVLEWLIRRFSIHEYVSDEFILSFLPFHDHPFFARILGCSKPKSRPLLFLENAIKMPVTLSRADIVHALSRDKEFFAMFAQFVQNTAESHNMYPELARFWAGTMMEVLVAWHSSNEDPNVLLDRFFLRVSYAVSYVSSIDFQIAGFMLLSSIAASLPLSPSIIPPLVSAITDRLSFDNIKPALICVGHLLQFCSSFEFDHEQLEKLESFGASSLLIELSQEHRLDEFFVSYWVSLIKSRKQKDKKRLISLLDTSISQIRVTHEQAKFLLSVIPVNQDFKALQSYRRILDSVIQPERKEGKLDNLINTLQDKKKSSTFSKKDREVLLKKISEIDSQTSFEQCLAYADSAADLDSSVFISLLSKFGDKIPFLLFCIANGSERIIILSLIELRKTIEENKDVDYQIILPVVLYSLQSKDTEVRSRALNLILTFLELRNENLEFSIIYGMDDNDNKNLRWLSPVETKYYCSDLLLDRSSEIGLDGTYLFSYIPERLFTEKKPKNASKEIAVTSFLSSHAACSKLSNVRVLLLEILTRVHGKVEDAKMQILLPRLEQLSEFNSEKFKTVSKREVEALVNCFNHTSFTSLLSFLSSNIVLSQAICRRIVEIQSHLKDPQRLEFVKAVISQDEQPHYYVDVLDSIKIPDTVFKKLIGSVRLVKEKNPAIAKRKRIDSHIFDGDVQRLTRILELLETKNAASYPKLASPLFEVLNSVIALKEDIVSSNYLLQLLLGLLYEMIGASPITELSPSIRIDTLVGCIRSTNNPQIQNKALLLVSALANAAPEAVLHGVMPIFTFMGSTVLSRDDAFSIHVIEQTVKTVISALIRLGKDFDSSLLVSCFVNAFPHIPQHRRLRLYRLVLQTIGSNRFLSVVLIQFAEKMLLAKSTNVVAIHDFCLTLVQSFSVADRIGSINQCSRFCLKSLEEQSNSDSNGKAVSLIKLDELPMDVDLATLGSLRVKVLELISLVSKAKNFAFDLAKIMENSVDSFVEIQAGLFESIKLLITLSQQSSNEMELGHVYVALRSVIHLLPNELFCTVLGKLLHDERALLRRKALSIVQQRVQQGSKVSALTALIPDVTYNISNYSDEETTQLAMDCLAVMAKRFSASPELFISPIEVVSGPYGLKNSARDVQVSAIVCITVLTNTLAARILPYLADIVNYSLSILDDARKDPEGDLLELACFSMMIDFFKVLPEFSSSYVEPTIKCALASDRAFEHDAIGELLFETIANFIPTRLLMKSIFAAWPECARLGSTAALRLLELIELALQNSSRSAIGTVYKSIFKFFLDSFDSRRSLLFAEDVDNVETQAVNVFLKFVMKLSDTTFRPLFLHLHSWALEDLYETDPSGIVSRQTFFYNFLTIFLDTLKSIVTNYYAYVLDDTIELLSSKDTNSEVRHLVNSSLVSAFENDTEEFWMVPARFGKISPVLIEQIQYAPLLDDKVLVKAIVELASVASSSDNFRSMNTQLLQYLRSSNINARLLAIQIQTQLYGRLGENWISTLPQSVPFIAELMEDDDDQVETATAELVRIIDDRLGENESLQDYLT O60180 ARX1_SCHPO SPBC23E6.05; CHAIN 1..417; /note="Probable metalloprotease arx1"; /id="PRO_0000148997" MELDPSDSNSRVVDASQFSKYRDAGALVSKAFHQVASRCVPGASTREISSYGDNLLHEYKSSIYKSQRFEKGIAEPTSICVNNCAYNYAPGPESVIAGNDNSYHLQVGDVTKISMGLHFDGYTALISHTIVVTPPPQPGMGPYIGPGADAICAAHYASKAVANLLATNNSDDPITGSRLRKIVDDIASQFRVSVCPGSRIRRISRFLVGQPTIDRLEEDQNTKHAVEWPAPEEETRKADVTNSLDPANVLSTELNTWHVMPKEAWLIDISMSSQPISSLKEHPDLKPTLYIHDVNVSYMLKLKASRSLLSEIKKEKSVFPFHFGSLSSERNLLGLRELTDRHILVPMPVLISSPSNVIAREELTVITQPNPSSDLLCLTVPTPPSYVKSDFSLEDGTDAALICEGINVNIKSININV O60181 RIB3_SCHPO BINDING 27; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q8TG90"; BINDING 27; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q8TG90"; BINDING 31; /ligand="D-ribulose 5-phosphate"; /ligand_id="ChEBI:CHEBI:58121"; /evidence="ECO:0000250|UniProtKB:Q5A3V6"; BINDING 82; /ligand="D-ribulose 5-phosphate"; /ligand_id="ChEBI:CHEBI:58121"; /evidence="ECO:0000250|UniProtKB:Q5A3V6"; BINDING 140..144; /ligand="D-ribulose 5-phosphate"; /ligand_id="ChEBI:CHEBI:58121"; /evidence="ECO:0000250|UniProtKB:Q5A3V6"; BINDING 143; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q8TG90" CATALYTIC ACTIVITY: Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830; EC=4.1.99.12; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Magnesium or manganese. {ECO:0000250}; PTM: S-glutathionylation is reversible and dependent on a glutaredoxin. {ECO:0000250|UniProtKB:Q99258}. MOD_RES 56; /note="S-glutathionyl cysteine"; /evidence="ECO:0000250|UniProtKB:Q99258" SPBC23E6.06c; CHAIN 1..204; /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"; /id="PRO_0000151828" MLASIEEAVNDFRDGKFLIVLDDETRENEGDLIIAGCKVTTEQMAFLVRHSSGYVCVPMTGERLDSLEIPMMVDNNEDRMRTAYAVTLDYANGTTTGISAHDRALTTRQLANPEVTSPREFNRPGHIVPLRARDGGVLERDGHTEAAVDLCKLAGLPPVGAICELVREEDGLMSRFDDCISFGKKWGIKVITIESLKSYIKGRM O60185 MTNA_SCHPO ACT_SITE 235; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03119" CATALYTIC ACTIVITY: Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533, ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_03119}; SPBC23E6.10c; CHAIN 1..359; /note="Methylthioribose-1-phosphate isomerase"; /id="PRO_0000317330" MSLQAIIYNEDKLLVLDQLLLPYERKYISVSNVEDAFAVIKKMQVRGAPAIAIVAALSVAVGLKHLSEDADAKEYVINSFEHLKQSRPTAVNLFETAKFMQGIALQEGKNCRNKIIQEAERMLVKDLEDNHNIGTAGRKFLLQHYKDKDKLTVLTHCNTGSLATSGYGTALGIIRSLHESGNLEHAYCTETRPYNQGSRLTAFELVHDKIPATLVTDSTVASIMHKIDAIVVGADRVTRNGDTANKIGTYNLAILAKHFGKPFIVAAPFSSIDTSLASGSQITIEQRPPIEMTTITGPIITDSNSRNLEDPKRVRISIAAPGIDVYSPAFDVTPANLITAIATEKGFYTQQTNNKYDFS O60188 UTP6_SCHPO SPBC244.02c; CHAIN 1..488; /note="U3 small nucleolar RNA-associated protein 6"; /id="PRO_0000374010" MAEKVQYYMEQSVPELEDLLEKNIFNRDEINNIIKTRRVFEEKLARRQVKLNDFLSYIQYEINLETLRAKRHKRLNITGKITISDYAGPRKVLFLFLRATNKFFGDVTLWLDYIHYAQKIKAVNIVGKICVAALQKHPNNAELWVVACDHEFSINANVSAARALMNRALRLNQENPVIWAAYFRLELSYMTKLFARSQILTGNISSKTENITNGVSEDTIGSLSSDTIQLPMVSMEEFLGSSSSEVRKNDSDLNISDDIGNISSKEQQTQKFANVLLQIILNSRKNLSLQNYVGFFVSVLDALFECFDVPVVQYMYQENIIGICNEHFEHFKNESGEIYGVLLHRWCFLEIFIKLRGAYPSNDSGISGKGIFGLKKNDPRITSMVLTDPGFVDDLQAIVEKYQSISSDFQIPFKTKKIFYSFFVKTLHAISSSSAAESSIALALHMLVINAFQSMEKLKILTFDDSLQEIYKEAQIQSGTFMSNATLS O74172 RS25B_SCHPO SPBC3D6.15; CHAIN 1..88; /note="Small ribosomal subunit protein eS25B"; /id="PRO_0000192890" MAPKKKWSKGKVKDKAQHATVFDKSIIDRINKEVPAFKFISVSVLVDRMKINGSLARIAIRDLAERGVIQKVDQHSKQAIYTRAAASA O74173 EF1B_SCHPO SPCC1450.04; CHAIN 1..214; /note="Elongation factor 1-beta"; /id="PRO_0000155041" MGFSDLTSDAGLKQLNDFLLDKSFIEGYEPSQADAVVFKAVGVAPDTAKYPNGARWYKQIATYDLATLPGTAKEVSAYGPEGAAAAEEDEIDLFGSDEEEDPEAERIKAERVAEYNKKKAAKPKAVHKSLVTLDVKPWDDETPMDELEKAVRSIQMDGLVWGLSKLVPVGFGVNKFQINLVVEDDKVSLEALQEELEGFEDYVQSTDIAAMSKL O74174 VATG_SCHPO SPBC1289.05c; CHAIN 1..108; /note="V-type proton ATPase subunit G"; /id="PRO_0000192915" MSAQTNSGIQQLLEAEKVARNIVEKARQHRTQRLKDARLEAKREIDEYASKKEEEFKKSESQASGIYSQAEAESKKQVQDTFASIETSSQKNSDKVVDAILSITCNVK O74175 RL13_SCHPO MOD_RES 177; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 180; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC664.05; STRAND 22..24; /evidence="ECO:0007829|PDB:8EUY"; STRAND 73..75; /evidence="ECO:0007829|PDB:8EUY"; STRAND 123..126; /evidence="ECO:0007829|PDB:8EUY"; STRAND 135..137; /evidence="ECO:0007829|PDB:8ETC" HELIX 28..45; /evidence="ECO:0007829|PDB:8EUY"; HELIX 77..83; /evidence="ECO:0007829|PDB:8EUY"; HELIX 87..90; /evidence="ECO:0007829|PDB:8EUY"; HELIX 91..93; /evidence="ECO:0007829|PDB:8EUY"; HELIX 106..121; /evidence="ECO:0007829|PDB:8EUY"; HELIX 128..130; /evidence="ECO:0007829|PDB:8ETC"; HELIX 149..152; /evidence="ECO:0007829|PDB:8ETC"; HELIX 168..172; /evidence="ECO:0007829|PDB:8ETC"; HELIX 176..187; /evidence="ECO:0007829|PDB:8ETC"; HELIX 189..199; /evidence="ECO:0007829|PDB:8ETC" TURN 46..48; /evidence="ECO:0007829|PDB:8ETC"; TURN 63..67; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..208; /note="Large ribosomal subunit protein eL13"; /id="PRO_0000192936" MAIHVKGQLPNAHFHKDWQRYVKTWFNQPGRKLRRRQARQTKAAKIAPRPVEAIRPAVKPPTIRYNMKVRAGRGFTLEELKAAGVSRRVASTIGIPVDHRRRNRSEESLQRNVERIKVYLAHLIVFPRKAGQPKKGDATDVSGAEQTDVAAVLPITQEAVEEAKPITEEAKNFNAFSTLSNERAYARYAGARAAFQKKRAEEAEAKKK O74306 RL5B_SCHPO SPBC11C11.09c; CHAIN 1..294; /note="Large ribosomal subunit protein uL18B"; /id="PRO_0000131453" MPFIKAVKSSPYFSRYQTKYRRRREGKTDYYARKRLIAQAKNKYNAPKYRLVVRFSNRFVTCQIVSSRVNGDYVLAHAHSSELPRYGIKWGLANWTAAYATGLLVARRALAKVGLADKYEGVTEPEGEFELTEAIEDGPRPFKVFLDVGLKRTSTGSRVFGAMKGASDGGLFIPHSPNRFPGFDIETEELDDETLRKYIYGGHVAEYMEMLIDDDEERYQKQFSGLIADGIESDQLEDIYAEAYAKIREDPSFQKSGKDAAAFKAESLKYTQRKLTAEERKERFNAKVIEAGRA O74308 YOG2_SCHPO SPBC15D4.02; CHAIN 1..547; /note="Uncharacterized transcriptional regulatory protein C15D4.02"; /id="PRO_0000310392" MEYHPSSQSPQVNPGMESQQGGYTYTYQQPAPPNSLHLQHPSILTRLPPLSSSVVSPSLASLPPFTPTSTYHSIAALTPPSYPQSSSAPSNNSYTIVPSPHDPSNAYSMHHVLQNTAPQSVPSPSPIEMVPPSPPKTGSNNSAPVTGKTVQSGNALNNSGLVKRQARKRTKTGCLTCRKRRIKCDERKPICYNCIKSKRQCEGYTHFPRPSGTFTASRRIPVSSLLSEPAPHGLAGQPTHPTFLYYIQSVAPSLCLWDACHFPPLSPYSSFSSIYWSSTVPELALRNPNISVALYAFASAKRHLTDDAVAFARQARVALTNITTTDSLLILVLLAVTQLYIPKSDIQLFNFAVDQVVKFDASLMTSPSDEIITYLLRRMFIRQVVLAGIVKPLASGLNPLPLLKCDLPPATTPTAVLDESLFHLGLRKLCHEKGLEPEFTKWSKNCPIDKADLPRLALLMIHAVFTSPVSLAQWVELILQNPDPTPAIHIARACLLAVHGVVDLGDLQMKVEKCVQSCEERQLQATISNFSTEVAQTNSSALAIGCQ O74310 ZNG1_SCHPO BINDING 68..75; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 127; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8VEH6"; BINDING 129; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8VEH6"; BINDING 130..134; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 130; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q8VEH6"; BINDING 218..221; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P53729}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P53729}; SPBC15D4.05; CHAIN 1..411; /note="Zinc-regulated GTPase metalloprotein activator 1"; /id="PRO_0000343521" MDFEIENESEIPQLVDVEEVNTQPHSETLSVPTVSSNNDIDSFEQQSDFLLVDHDSTLDPVPVTILTGFLGAGKTSLLRSILENRNGKRVAVLMNEVGDSGDLERSLMEDVGGEELYEEWVALSNGCMCCTVKDNGIKALEKIMRQKGRFDNIVIETTGIANPGPLAQTFWLDDALKSDVKLDGIVTVIDCKNIDNILKDESDIGFIQISHADCLILNKTDLISSEALSVVRQTILKINCLAKIIETTYGRLDDISEILDLDAYGNENTSNLEWSIQRSNDSNINCSTCLDVDCQHLHSLDTHSLDISTHTFKLPPLMSKEVFQQFLQWVRHTLWSCLEEGEDEEFMIYRSKGIFNKDDGSWYIFQGVREVFEIMPLSEKPRAFLEKDIHPEIILIGRNLHRISPFVVGNQ O74314 MET7_SCHPO CATALYTIC ACTIVITY: Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate; Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661, ChEBI:CHEBI:58161; EC=2.5.1.48; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 427; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000255" SPBC15D4.09c; CHAIN 1..610; /note="Probable cystathionine gamma-synthase"; /id="PRO_0000114780" MSANISYLVNPPTEVGSSIPADTEHAISVTLPTWKSNVGYEEGDPNVTTKMKSGYPRFFISAHVKDCISIIKKFPEIEILKLKDYDMFLYPSLSVAKQSAAFLESKGPIDSAEVIIYDATKGLRKHLDSIDRNRKYTEEIHIPQVYSVLFPSKYFGIAKQFWQHTGDGISSRRAAAFLHSYKKIQSISEFLVAQRSISHLKSKSRSRYASHPDLQALNTWMTNEGNQANDEMEDVSLYLEERYGRNLDLSLATAAKLVLRRRIAGTLKDEVDLQKALPKEGSQYLREVKGLSHDDVFLFPTGMSAIYNTHRILRLVLDDSRKSVCFGFCYVDTLKILQKWGSGCYFYGLGNDEQLDEFEKRLESGEKVMALFCEFPSNPLLNSPDLVRIRKLADSYDFAVVVDETIGNFVNVEVLPLADVVVSSLTKIFSGDSNVMGGSMVLNPSSRYYSRIKDAMKALYEDLLYDEDALTLERNSRDFAERSQVINHNAETICNLLYQNPKIKTLYYPKYNTSKEHFEACRRENGGYGGLLSVVFHNPEDARQFYDKIQVAKGPSLGTNFTLASPYAILAHYQELDWAGENGIDRNLVRVSVGMEPSEHLKNVFINALS O74315 AMO1_SCHPO SPBC15D4.10c; CHAIN 1..475; /note="Nucleoporin-like protein amo1"; /id="PRO_0000064588" MVVCKYFLQNRCRYGTNCKNQHTVPSNGQNAFSKVNVFRPENGRPPIWVQRRLKRSDLDNLLPNRRMKDINDDLKNAKPQWPFTGYSVVENLPSIYEGDVSPEELRWWAYQAKATNNMQAYEQRQKQLMDDVEAKAAAVKRSPAAAFDEMRNKLVGKTNYKSIFDKSTSNSTVTSNQFNKPTQNSPFNSFSNNNNSFNNNQQANDIFGAPTTSAFTSQLNASPFSQNTSSNSFTGSNPVQNNPSSFGSSSFGSATSGPSAFGGISQPNSSFVNSGQGIPNSSFSSFSQVASGFSQSQNVNDPSSIFGPTVASGFGIQNQPQQSAFQNLNTQFSLPNNSQPVFGHTSLTQPVNPNGFTVQPPATFMQQPQGPFVPPNTTFESPFANVTSKISASGFSNDNPANKNIIQTPMFGSSNTIDGPINPIGASSIQTLDDQVEMSNSNQNLAFPPEMIQQFEAQDFIPGKVPTTAPPPQFC O74319 TAF73_SCHPO SPBC15D4.14; CHAIN 1..642; /note="Transcription initiation factor TFIID subunit taf73"; /id="PRO_0000234562" MAQSSYSSGNSTSDLNKIVLDYLFKKGYSRTEAMLRLEISSVGAIPEEQQDWHIGASETYVQVYILLRDWIDGTLDLYKPKLQKVLYPIFVHSYLDLLQKNDPEMAIYFFESFRIEHEVLHGYDIRALAQLKIASDVEEIEIAQLYRKNKYRINFTRSTFDLLVQFLFENEVNGSGIIIRLLNQYIDIKITMPQVEGKEDPNVQAVYEMDEAKNEQTIISEQEGIPGHSEQLLDYNKQSIQLGLRPLSEEVVTTLKNLLEVKDKDVEGRNEALNKILHPAKNLVELLTEKENLINESTLESPSDPPLPPTKMKDIDYFVSLLESEQNSLILGKNATDPSVFMYTMHNTLSAVNCAAFSDDASMFALGCADSSIHLYSSTNNGPQPLVGSQNEPLQKSSLIGHTRPVFGVSISPQKEFILSCSEDGFTRLWSKDTKSTIVKYAGHNAPIWDVQFSPFGYYFATASHDQTARLWDVEHAAPLRVFVGHQNDVDCVSFHPNAAYLATGSSDHTTRMWDVRTGGTVRVFNAHHSPVSALCMSADGLSLASADESGIIKVWDLRSSNQHVSFVKHSSIVYSLSFSYDNKILVSGGADTDVNFWDLTYRNNLSDGEQSPLLFNFKTKNTIIQNLSFTRRNYCLALSSS O74322 RS12B_SCHPO SPBC1685.02c; CHAIN 1..148; /note="Small ribosomal subunit protein eS12B"; /id="PRO_0000122339" MSTEGDHVPQAEEVIETVEVVEEETGSSPLSVEDSLKEVLKRALVHDGLARGIREASKALDRRQAHLCVLCESCDQEAYVKLVEALCAESQTPLVKVADPKILGEWAGLCVLDRDGNARKVVGCSCVAVTDYGEDSVALQTLLSSFAA O74323 SEC11_SCHPO ACT_SITE 47; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P15367"; ACT_SITE 104; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P15367"; ACT_SITE 129; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P15367" CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89; Evidence={ECO:0000250|UniProtKB:P15367}; SPBC1685.03; CHAIN 1..189; /note="Signal peptidase complex catalytic subunit sec11"; /id="PRO_0000314115" CARBOHYD 114; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MQKLSFRQGLAQILNLLLVLSSAYMGYKTLSFVTDCESPVVVVLSESMEPSFQRGDLLFLDNRNPSFDEAKVPSVFEKIIYGSPVGIGDIVVYSLPDRPIPIVHRVVKLYESENQTHLITKGDNNKIDDVAMFPKSINYLDRENHILGVVRGYFPYLGMITIWLTDYPILKYIMLGGLGLLTLIQKEEQ O74326 CID11_SCHPO BINDING 106; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 108; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; SPBC1685.06; CHAIN 1..478; /note="Poly(A) RNA polymerase cid11"; /id="PRO_0000256154" MELLTFTCCPFEGQMQQKKRRFDANLVQLQESEHRNDQINETVDAELTNECWKLYMRLKPSNEEVSRRQQFVDKLRTILSTEIKDAKLDLFVFGSTENNLAIQQSDVDVCIITNGSKYLNSTCQLAQLLYSYGMKQIVCVSRARVPIVKIWDPQFDIHCDLNINNDVAKINTKMLRLFVSIDPRVRPLGLIIKYWAKQRALCDAAGSGTITSYTISCMLVNFLQTRNPPILPAMLDLMSNDDNKMFVDDIVGFKEKATLNKTSLGRLLIDFFYYYGFSFNYLDSVVSVRSGTVLNKQEKGWAMEVNNSLCVEEPFNTARNLANTADNPSVKGLQSEFQRAFRLMSENNACERLCKICEEYQFLDITNEANYGNTNTPFNTAYESFGCNHTVLPEAAAYPKPYYPPQITLSDGGNMNFLYYIPDESNHQSYENKANRDSDFQGQTSLTQGSAPPWHYIPCQSWLVWYPSEDASNPASGN O74329 RS29_SCHPO SPBC1685.09; CHAIN 2..56; /note="Small ribosomal subunit protein uS14"; /id="PRO_0000131031" MAHENVWFSHPRKYGKGSRQCAHTGRRLGLIRKYGLNISRQSFREYANDIGFVKYR O74330 RS27_SCHPO COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P35997}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P35997}; SPBC1685.10; CHAIN 1..83; /note="Small ribosomal subunit protein eS27"; /id="PRO_0000149065" MVLAVDLLNPSHESEMRKHKLKQLVQGPRSFFMDVKCPGCFNITTVFSHAQTVVICGSCASVLCQPTGGKARLMEGCSFRRKN O74340 DCA13_SCHPO SPBC1A4.07c; CHAIN 1..436; /note="Protein sof1"; /id="PRO_0000316545" MKVKTITRGTSLTRLNDQDPVKRNLDPSLHPFERAREYTRALNATKMDRMFAAPFLGQLGRGHQDGVYSLARDTKTLIDCASGSGDGAVKLWDASERCERWTSKAHEGIVRGLVFSNQGDVLSCASDRYVYMLNKQDGKVKRSYLGDSSLLDIDTSKGGDLFATSGENVSIWDYSRDTPVTKFEWGADTLPVVKFNYTETSVLASAGMDRSIVIYDLRTSSPLTKLITKLRTNSISWNPMEAFNFVAGSEDHNLYMYDMRNLKRALHVYKDHVSAVMSVDFSPTGQEFVSGSYDKTIRIYNVREGHSRDVYHTKRMQRVTAVKFSMDAQYIFSGSDDSNVRLWRARASSRASIRSTREENRLKYLDSLRERYKHIPEIRRIARHRHLPTNVKKAAEIKREEINSLKRREENIRRHSKKGAVPYEKERERHVVGIQK O74341 TCPG_SCHPO MOD_RES 250; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1A4.08c; CHAIN 1..528; /note="T-complex protein 1 subunit gamma"; /id="PRO_0000128330" DISULFID 364..370; /evidence="ECO:0000250" MQSPVFVMNTNGNRQVGHKAQMSNIQAAKAVADVIRTCLGPRAMLKMLLDPVGSVLLTNDGHAILREIEVAHPAAKSMIELARTQDEEVGDGTTSVIILAGEILAAASPLLDRKIHPVVMIRSFKQALEDALSIIDEITLPVNVDDNAEMFRLIRTCIGTKLVARWSDLMCHLALRAVRTVASTSNGRMEIDIKRYARVEKVPGGEIESSCVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEYRKGESQTNIEISKDTDWNRILEIEEEQVKRMCDYIIAVKPDLVITEKGVSDLAQHYLLKANITALRRTRKSDNNRIARACGANIVNRLEDLREKDVGTGCGLFYIDKLGDEYYTFLTGCKNPKACTILLRGPSKDIINEVERNLQDAMAVARNVFFHPKLSPGGGATEMAVSVRLAEKARSIEGVAQWPYRAVADAIEIIPRTLVQNCGANPIKALTELRAKHAEGQHSFGIDGETGRVVDMHEYGVWEPEAVKLQSIKTAIESACLLLRVDDIVSGVRKHSE O74345 UCP3_SCHPO SPBC21D10.05c; CHAIN 1..601; /note="UBA domain-containing protein 3"; /id="PRO_0000065714" MSGRRNETAIRELVQSVSGNNLCADCSTRGVQWASWNLGIFLCLRCATIHRKLGTHVSKVKSISLDEWSNDQIEKMKHWGNINANRYWNPNPLSHPLPTNALSDEHVMEKYIRDKYERKLFLDENHSTNSKPPSLPPRTKSSSQSSPMASTSTSKSRYADSLSTLHDMGFSDDSVNTHALEETNGDVTRAIEKIVQHGSSKPQKPSTLTSTKSTIKLVSARLKKRNKNLSVHFEDGTKPGDAYEVTGDTRAASPTLNPFEQMMAMTNQGMSVSPGVETTSSPFFTAPVEPNQPLQPLRPSMTGPVPSSMGSEATLNMPSTYGIDSNLYTNSNSSSIVQNPLQPARTGPAAINYNYTTNYSVSSPSVTNPFFDVGSSTQNASLMGSTGYPSSANNVYYENSYQGVGTSMSDNYQLPDMSKLSLNEQPAAPSNSNSQYMNTSMPTLDSTNMYGQSNQDPYSMSNGVYGSNYSAQPSTMQMQATGIAPPQPNMSMQMPMSMQSTGYQMPMENTWVDYNGMSQQGNGMQPATMNYSNSMGYDTNVPADNGYYQQGYGNVMMPPDASYTGTGSYVQPMNQPSGGMGAPADSSKADSYIQRIMQGKQ O74346 MAP4_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPBC21D10.06c; CHAIN 24..948; /note="P cell-type agglutination protein map4"; /id="PRO_0000353808" CARBOHYD 31; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 32; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 57; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 383; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 436; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 469; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 491; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 522; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 553; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 568; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 598; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 921; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNSYAILLSLFFSFERLLTLANANSLYSPFNNSSFVDSDTSFSDLSRNGLLSLLDSNTTSASVQTIAISQTDNAASCIPSASLLSSSVVLYSAKETVTVSSYWSLVSTSVTGTVYVPYTSSVACFPYATSDAPNPIPRGDSATSTSIAPTYSASDSSATTITSSSPSTSIIGTGSTDTSVSSTLTYHTPIASPTTSSNSDNEYTVDVITSSSLSSFVITNVDSTTTSVINYIGASTLESSSLTNTVSPTESTFYETKSSTSSVPTQTIDSSSFTSSTPVSLTSSSTSSSGSSQDSTTIDSTPSTIATSTLQPTTSSPITTSAPSLSSALPTTYPSSLSTEVEVEYFTKTITDTSSIVTYSTGVETLYETETITSSEISSIIYNFSTPISGSSFPDGFKPINPTSFPSLTSSTKKIPSTTLPTSSKMITTTTPSVSNNTQSSFLIISTFTSSYEHSEPFKVSSVPLTSNNFSSISHSSASSLPITPSSYLSNTTLHSSVQSSQSSQFTVSVPSSTQSYSTSSNFTTPITISTSLSSFPTTIVSSSFQYSSLSSNVTTTNAQSSSLSSSNSSALTHISSSIVSSGSSSALSSSTIVSSINSSSSVFISSVSSSLQYSSSYVTETTTSGSVGFTTTIATPVGSTAGTVVVDIPTPSWVTETVTSGSVGFTTTIATPVGSTAGTVLVDIPTPSWVTETVTSGSVEFTTTIATPVGTTAGTVVVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLIDVPTPTASSSPFPSCNTQCTNENSFRIQVINDDIYPSYVHLDSNNYAIAAARGDSDGENVFIYDSDIKRIVSCCGVKPIYRLDQDDTEGYSFEIYKDNDGQLQFKYPLNDALYPMELLTLTDGRIGITTNLTLYKPYYLNNVENERAANVVLRALEY O74350 BDC1_SCHPO SPBC21D10.10; CHAIN 1..299; /note="Bromodomain-containing protein 1"; /id="PRO_0000310329" MNIAQEVAVLQYLDIQQENPNAPNEELFNRTAESSLLLEPIEQDQLKDLVEEWMHDSNKSDSKLLSNQVSQNDNDARKNLRKRLRNDVLKDLAEEIQGCEKKLESLYEEVAKAKAKAVEDQLALEEADKEAKKAKTEAPVEAANKSLRSRKKTPEIAAPANIEPEVAPTTKTPKKRAALSNEEKQSLKKFQSAMLPMLDNISNHRFGAPFSHPVNRKEAPDYDSLVYKPQDLRTLKNMIKEGNITEVDELYREVLRIFANCKMYNGSDPANAMSIWGDECFRYTEELFDIYRQASTRSQ O74356 YH16_SCHPO BINDING 134..141; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC25D12.06; CHAIN 1..585; /note="Putative ATP-dependent RNA helicase C25D12.06"; /id="PRO_0000351075" MKCCPASILDRFNAIKVINVMGLRLNGRSVPWLLQTRKFINITSPRYTAGRPVILNENQLIRYLPNYTNKGDEEVTRRKKLHEPNGPKFHELPLNQNILDGLSTNFAEYKNSTPLQQRIINALMKSGVSFIVRGWNGSGKSFGAMLSTLSMYFEALKFLKHNPVAGKPVQSGCQVLFIVPNDNLAAQYQFWIERLLHGITEKEELQHIYKILTLTPASLDSFQNRPPYIGITTFPNLQHCIKKNQPILKQFTSQLQLLIVDESDLVIPDHGRSRRLSSPEILADKIFLSSFIQLCKKNLRINMDDENVGGMGIHSQLHGKGSIPTMVFMSASNSKNGVNYLSRYITDQLGIIGIDRKHQWYWNLTSTPSVFHYLIKAQAEPKTTKVTLTNLPYEFVRFNNSMHSIGDNNFSYNNSEAVLQIFAQSVPRILNIEAKKSKLENNILKCVMIVLPKEFNPHSFCNQYKGFAVGNRFWQCRTLSTESLNFSTNLNNVVFVANPSEIRGLHLPSITHIFHLWSTFSGVAYQHIAGRLGAMGQTGKIFNFIIPDYYKSNDFKKTDFRRCILFMLQRVGIRPKSYEFDDEHF O74358 APC13_SCHPO SPBC28E12.01c; CHAIN 1..135; /note="Anaphase-promoting complex subunit 13"; /id="PRO_0000237684" MDSNYNYVHMNKPGVVLFASDWLKDRLPVDDVEVRVEHLPPVTEDEMTIQHSSANLILMKNKQLRHEPAWKDLELEDLVNAFAFIQGSSNAEGKNTIEDNFETDPFKSVKEAPMAPFLEANRRHQGEHASMRYFR O74359 MUG60_SCHPO SPBC28E12.02; CHAIN 1..663; /note="Meiotically up-regulated gene 60 protein"; /id="PRO_0000278492" MDSHVLAFPIPDPSTPPPEEASLYASKCDYYESDIYSQIRRLTEEKCIETEKELPVNIKLHVKHKGMSISSSRNELVVTVSGNYKNVYTAKIKILQAIPKILISKLVLEEPLENLLFDEDGYVYEDTMKHLDKITEITGAKIYIMHRSMCHDIDFQLRTDSGFSNRLNEQQSFYQRHLESTRHEFSCQKNAENSFFIVFYGDYCSVEHARIRVLALMDEIRGLSVVAIATSVSFQPILVGKAFSSTAGMKATESINIYTLPFCSDSIPRLQTLPALNSSKIIITGEEEKLQRLEEAFYYAEEHLKLFTHVTEISFVKLFEFLAYEMDELRLIMEENSSFIRFPEYFKEGGETSPENSKVKIYSSSIANSEKTALRLAKLASKYVQGKTQFGVEDNEDFLRVAGSWRRASTIEKGVSSSELSSIVSSTGSIVETNGIGEKMSFSPLKKLSIPPTEFVAQIAIICMASGVEMLLKTNGIEYFGQENTVPIAMDKASKIFYKFGQSQWHQILLEAPTKDQDFISGKKNGKLDKVKQQCRFNLKNGDILFCPQSTSIFTVDIYSDELERVIKGMNTMLLEFPAEMHFYVPEEIHKKLIGFRGEQIQRVTKLYNSYIEFSTTPFDCYGHNVLIRTPSKFSENLWAVRSLFIKTAEGLGYDIPKYLFAN O74362 ESF2_SCHPO MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 53; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 54; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 88; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC28E12.05; CHAIN 1..334; /note="Pre-rRNA-processing protein esf2"; /id="PRO_0000285379" MSTAEQLFGAEEEEKYVDQDLSEDEEDERFLKAIRSSRSTKPVVDVLKVKSESSADELEERDAHLDRFRRDSTFESETSDHEDFSGGSENELDEETTKNANSIKKISLEEVEKQRKAIKRSGVIYLSRIPPYMAPNKLRQILSQYGKIGRVYLTPESSAKRAQRLRNGGNKRVMYEEGWIEFESKRVAKSVAELLNTNQIGGKKSSWYHDDIWNMKYLPKFKWHHLTEQIAAENAARESRLKVEIEQGRKQLKQYMRNVENAKMIEGIRKKRSERDTLNVSTEFPEETKDLSEDTKPSKQARRFFGQKSIVSNRNMPTDNAKQQKVENVLRRVF O74364 ADN1_SCHPO SPBC30B4.03c; CHAIN 1..391; /note="Adhesion defective protein 1"; /id="PRO_0000350969" MVANYASMMYHNGSNILGYGVLRLLQYNEQLMSGWESTMKDDIGYWRRFVHDFYTEKGTFRYNIDYKDSPNQEPKLFELSYAALPRFLYLSYCGKLKKMSFLLGNTKEFAIPNNGYFVESSRASILYQYQGGVQVIVSGHLRAHFFRAPLLKLDSLEFSAVGHSEYLLRELMTNASLALSQSRPPQNQIQHDGVKSEDPSSESVNINSSSSLLPDSPVNEYGLEPHIMRFMEITETISGMRDLIAFTLAQRSGPTSALHKFATALQQQHQMQKSTSSNIPYANPAPSGFNGSPRNGDVASLASNYRYAKQPPTMPANAISQANRLLDQNNIPNMDPSILPQSMPIASVPPYSLQGIKRQGTHSPMVEGENPNNNPNFYSSDMLNAQKRTKV O74366 TFB4_SCHPO SPBC30B4.07c; CHAIN 1..297; /note="General transcription and DNA repair factor IIH subunit tfb4"; /id="PRO_0000119273" MDEFQTLKQNASWDISEDANDTPSLLVVILDANPASWYSLSKKVPVSKVLADITVFLNAHLAFHHDNRVAVLASHSDKVEYLYPSIAPEQKVAEVDPTKEANTYRKFREVDDLVLSGMKRLMSSTDKVSRKTMISGALSRALAYINQVQNKNTLRSRILIFSLTGDVALQYIPTMNCIFCAQKKNIPINVCNIEGGTLFLEQAADATGGIYLKVDNPKGLLQYLMMSLFPDQNLRKHLNTPNQANVDFRATCFCHKKVLDIGFVCSVCLSIFCEPRVHCSTCHTKFTVEPMSKKLHT O74377 SULH1_SCHPO SPBC3H7.02; CHAIN 1..877; /note="Probable sulfate permease C3H7.02"; /id="PRO_0000080186" MSFIKKIKHYFADPADLPQDEAPDSVPGLVPPPSNFVPVYPEPTYSDTVSKKGTIVRVVRHTASKLTKHGDSSQSLSTLPNNDISVGEYVEPLPSVPGWLKQNIFSHFGTRLLHYLRSLFPIMNWLPRYNWNWLVYDFIAGITVGCVVVPQGMSYAKVATLPAQYGLYSSFVGVAIYCIFATSKDVSIGPVAVMSLVTSKVIANVQAKDPNYDAAQIGTTLALLAGAITCGLGLLRLGFIIEFIPVPAVAGFTTGSALNIMAGQVSSLMGYKSRVHTNAATYRVIIQTLQNLPHTKVDAAFGLVSLFILYLVRYTCQHLIKRYTKFQRVFFLTNVLRSAVIIIVGTAISYGVCKHRRENPPISILGTVPSGFRDMGVPVISRKLCADLASELPVSVIVLLLEHISIAKSFGRVNDYKVIPDQELIAMGATNLIGVFFHAYPATGSFSRSAINAKSGVRTPLGGIFTAGVVVLALYCLTGAFYYIPNAVLSAVIIHSVFDLIIPWRQTLLFWRMQPLEALIFICAVFVSVFSSIENGIYTAVCLSAALLLFRIAKPSGSFLGILKIANKFDDDENSIDVVRDIYVPLNQKGMNPNLTVRDPPAGVLIFRLQESFTYPNAGHVNSMLTSKAKTVTRRGNANIYKKASDRPWNDPAPRKKKNAPEVEDTRPLLRAIILDFSAVNHIDTTGVQALVDTRKELEIYAGDEVEFHFTDINNDWIKRTLVAAGFGKARDATKYTSRSIEVGSAAPLRDIETPMAPGNSRIVMPSSVRVRPFDEEEAIESSIPAIVSEDGADSDTISVSDDKDKKVEGHRPSQDPTFSHHEYYPVISTTYPFFHVDVTSAVVDIQYRHVLDVNYKPKIVTNEVENENIEHSDGAA O74378 ODO1_SCHPO BINDING 305; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 404; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 404; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 437; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 437; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 439; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 439; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:Q02218"; BINDING 669; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:Q02218" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:Q02218}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q02218}; TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3H7.03c; CHAIN 40..1009; /note="2-oxoglutarate dehydrogenase, mitochondrial"; /id="PRO_0000315629" MLRFIPSSAKARALRRSAVTAYRLNRLTCLSSLQQNRTFATQPTDDFLTGGAADYVDEMYDAWKKDPNSVHASWQAYFKNVQERGVSPSKAFQAPPLLDYADSYTALDSSLINGNNYADIDVGIYMKVQLLVRAYQSRGHHLAKLDPLGINVNHNRPSELTLEHYGFTESDLNRTIHLGPGILPNFREAGRKTMTLREIVETCEKIYCGSFAVEFTHISSRKRSNWILSHLETPTPFRYSHDQKIMIFDRLSWADSFERFLFTKFPNDKRFGLEGCEAMVPGMKALIDRSVDEGISNIVIGMAHRGRLNLLHNIVRKPAQAIFSEFRGTQDPDDEGSGDVKYHLGMNYQRPTPSGKRVSLSLVANPSHLEAEDPVVLGKVRAIQHYTSDEASHEQSMGILIHGDAAFAAQGVVYETFGLHALPGYSTGGTVHIVINNQIGFTTDPRFARSTPYCTDIAKSMEAPIFHVNGDDVEAVTFICQLAADWRKAFKTDVVVDIVCYRRHGHNETDQPSFTQPRMYKAIAKHPPTFKIYTQQLLQEKTVSKAEVDAQEKRVWDILESSFESSKNYKSDHREWLSNPWVGFASPKDLMTKILPSYPTGVNIDTLKQIGKALYTLPEGFDAHRNLKRILNNRNKSISSGEGIDMPTAEALAFGTLLEEGHHVRVSGQDVERGTFSQRHAVLHDQSSENVYIPLNHLSPNQASFVIRNSSLSEYGVLGFEYGYSLSSPNALVVWEAQFGDFANNAQCIIDQFIAAGETKWLQRTGIVLSLPHGYDGQGPEHSSARMERYLQLCNEDPREFPSEEKLQRQHQDCNIQAIYVTKPSQYFHALRRNIHRQFRKPLVIFFSKSLLRHPAARSTIDEFDEKHGFKLILEEEEHGKSILPPEKIEKLIICSGQVWVALSKAREENKIDNIAITRVEQLHPFGWKQMAANISQYPNLKEIIWCQEEPLNAGAWTYMEPRIYTILKHLGRDLPVRYAGRPPSASVAAGNKQQHLAEQEQFLNDALL O74379 RT26_SCHPO SPBC3H7.04; CHAIN 1..220; /note="Small ribosomal subunit protein mS42"; /id="PRO_0000316038" MSFQQRFARALDVGYKNFLSKDAVRNIFAYDNHLRGLVQKECKIHQTPYRVPSDLMVQSASDPARANLFNYSSQLVNHDFFFSGLISPERPSADADLGAINLKPGIDASFGSFGELKSQMVDVGNSVFGDGWLWLVYSPEKSLFSLLCTYNASNAFLWGTGFPKFRTNAIVPLLCVNLWQYAYLDDYGLNGKKMYITKWWDMINWTVVNNRFQATRIESL O74381 POF9_SCHPO SPBC3H7.06c; CHAIN 1..467; /note="F-box protein pof9"; /id="PRO_0000119976" MAKSPFLELSYDILLEISTYLDYKDIVHLSETCKSLSYVFDDKTIWHRFCARVQGLTNVVPVVDDNYKRPYAVWKDRGYAYSWGQQIRNYLGRVVNTNQYPRDRPGALTGKDVRSTIQVQVGGYGMYLLNENGNLYVTGVPNNVGPELMRDLEPIVKIHAGREFCLALGETGHLYQVSLKTRICLTDEQNMLSAYRGRIANFKSGWDSHSAYVPGIGFLVWHTGRESEAQLFQPEASMKEFVLNDYVHCAGFLVYTVASPQKKGAVFRLDLDQATQHTLGRELKRFASHDPHQGWHLAGSFETFTCLSDDGNTVYMGHANTKQVDDDPVIHDFLQNRGIKQLAHGDHHHLYLTSDHSIWSWGVELRYCGCLGLGSLHLQEQTSDPSIVSDPRTARNIVSIPHQIHFSGTCYSVAAGGWQSAALAISESVLPEVNVPPITTFSIIRPSRVPALRFLAAPATRTLERDG O74382 SERB_SCHPO ACT_SITE 82; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 84; /note="Proton donor"; /evidence="ECO:0000250" BINDING 82; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 84; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 91; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 127; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 170..171; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 217; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 240; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 243; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247, ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; SPBC3H7.07c; CHAIN 1..298; /note="Probable phosphoserine phosphatase"; /id="PRO_0000156884" MVNAAIVVSSNRPNVLEQISSLFRDGKTRSLGEQWTLVSGQLKGTFEDAKDACNRISATENVDCNCLSEATFSTKKKLVVFDMDSTLIQQECIDELAAEAGIQKEVATITSLAMNGEIDFQESLRRRVSLLQGLSVDVINKVIGKITFTPGAKQLCHCLKQMGATLVVASGGFVPMAEYVKGQLDLDYAYANVLEFSDDGKFLTGKVQGAIVDGQRKASILREKREELGLNKLETMAVGDGANDLVMMAESGLGIAFKAKPKVQLLADSKINLPSLQNALYLLGIDEQQQKKLLENKN O74385 ELP6_SCHPO SPBC3H7.10; CHAIN 1..249; /note="Elongator complex protein 6 homolog"; /id="PRO_0000351069" MSSLHEHLRPIPEPFSLTLLLGTRETPVTFLFHYYLYHALKAKESTCFLTFSKTLDEHAISMRKWGMDIKTKKNFFFIDGFSMLFAPISKPSKVQAPETKNHIKSVFAPVIQCVEENDFEFENSTIIIEDIDILQSTHALDSTKIQQAILELRKCFSRVIVNVTLGAPLPQQKSLGSSIGHMATRCISCRPLTSGSARRITGFLRLSRMPNHFRSGICETPEDDDKELLYEVTEAGAKVYSKGQVTLQL O74389 MU176_SCHPO SPBC3H7.14; CHAIN 1..406; /note="Meiotically up-regulated gene 176 protein"; /id="PRO_0000278519" MPSLNQEETPKKTKNPYRKGHSRRQSRHSIPSDELNSNSSKSLNNDRISRTIENSLQKETNSDNKIKKLSKTKSNPTNPKSEEDPSQICQSFDESNIITPSKYLFPLSKDYSPNEGLFQTDMNEKNPHDLWNPTVPMAYLSRSLQGLTISKINETEQKFPLSSVHAYVEIGEGMFSMEIVTEQLRLLGATVHASLQMTEENPVSHAVLYDCSQETLKKISSAQVPIVCVSPKWVLACYSSKYLVDEEMYLVDPQDILQTKCLQTDDSELLNPLDPFTDTQMIQDPSDAFFFDTQAENLEPFVNGSPDSHCFNADSFLDQTLSDDYEFGLITCSDSNESSMSNDAQRENNPETISQISLSPTADLFSSFKITTDLEMTHLESAKKKYLAYKPLIGSPLKKKVSLIDF O74391 RL25B_SCHPO SPBC4F6.04; CHAIN 1..141; /note="Large ribosomal subunit protein uL23B"; /id="PRO_0000129482" MSVGKAKGAQKTVQKGIHNKVARKVRTSTTFRRPKTLELARKPKYARKSVPHASRLDEYKIIVNPINSESAMKKIEDDNTLVFHVHLKANKFTIKNAVKKLYSVDAVKINTLIRPNGTKKAFVKLSADADALDVANRIGFL O74395 STR1_SCHPO MOD_RES 5; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 41; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4F6.09; CHAIN 1..612; /note="Siderophore iron transporter 1"; /id="PRO_0000084879" MRLKSFSTTLDTLRRRFNDSSSEEDKLEKNIQDETSIKEVSLQDAKQSDEKGVEEKVFNDESFSIDVAPKPEDELSGIVKARYLTEHSSRISFYICYFSIFLLFFAISFQAECYYSLTAYATSAFAGHSLLSTIAVANNIISAAIKPPLARLSDVFGRLEAFLFSLLLYLVGLILMAASTNVQTYAGGSVLYNAGYTGVELIMTIFMADTSSMANRSLVLGISYLPFVVTIWIGPRVAQEFYMHSTWRWGIAVWTILIPACSIPFLAVYSYYQFRAWREGALKGTLTINPVELFKKLDIIGLILMTAGLALVLLSISLASYDTGKWSDAKFIVMIIIGGLCLIAFVLYEIFVASFPALPFRLMREPTIGACCAMSFLFYITFYCWDNYYYSFLQVVHYTSITAAGYISYTYSFTSCATGFFLGILIRLTKRYKWYFVASIPVYILGQGLMIRYRGEQYNWGYQIMPQIIVGIGGGVIANLLTVAVQTVVSTENFAIVTALVSTVTPIGGAVGSAISGAIWNSVMPKRLEKNLPSDLKDQAYTIFESLTVQLSYTRGTDARNAIILSYSEVQKILTSVATGFAGAMIFPVWFVANPRLSTVKTHIFDSKESKV O74396 VPS91_SCHPO SPBC4F6.10; CHAIN 1..572; /note="Vacuolar protein sorting-associated protein 9a"; /id="PRO_0000316571" MDYPSFHEDPTKDESTVAEQRKGQSNEEKPLIDLNDSLDEQRNAYNEHCKNHDQQPSQQVRNMEDEANQYEQTDSSSDQEVMNEKQSLDKENRNDNIPHENNPGQQEINEPIFDFHMFLEQLRSSSAEPVAKYLKSFLSEFTKRRWTVNYQVKLIRDFLKFINEKIEQYEPWASGSQAEIDNAKEGMEKLVLNRLYTSLFSPEIAKSGIPLSSEHSDDVEEDRVLSEKMELFQWITEENLDIKKQKSSSKFFKLAADELRRINDYHAPRDKIICLLNCCKVIFSYLRNVVKEESADMFVPILIFVVLQARPAHLVSNIQYIQRFRSPEKLTGEVMYYLSTLMGAMSFIETLDCSSLTITEEEFNAQIEKSIKKMEERKLSEKSESKTAVNENATYKDPVLSRGLSSSIDVSTGVALVNLPEELENMKYLQIDTPESKEYPRSTRPRASSHSGSFTTDSGKRSRRNSNKYVGSSDRPPYRVSRAYSSSATHSPIVHEEQPVDDGLQQNDDLREATTASLETAEAERLQAREKAEAITALRAMFPAFDSEVIEVVLNAQQGRLSSSIDSLLEMS O74402 HSP78_SCHPO BINDING 139..146; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 539..546; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255" TRANSIT 1..36; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC4F6.17c; CHAIN 37..803; /note="Heat shock protein 78, mitochondrial"; /id="PRO_0000372309" MNILPKSIPIRIQSLRRYQGSLKTSLRALSTRPIFEKRLLAETPFSIRPSNASVLIAKRSPKFGWKQVRFYAANPNGGNFRMDLGGGRKQGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRGEVPESMKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAEGKVILFVDEMHLLLGFGKAEGSIDASNLLKPALARGKLHCCGATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLPDKAIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKAKTELEQARIELERTQREGNYARASELQYAIIPELERSVPKEEKTLEEKKPSMVHDSVTSDDIAVVVSRATGIPTTNLMRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLFDTDKAMIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRKVDFRSTLIVMTSNLGSDILVADPSTTVTPKSRDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVNVRLDEVQQRLNDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDVLDGELEFKANKLEPQSTSHED O74407 SYDC_SCHPO BINDING 287; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 331..333; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 331; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 339..341; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 502; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 505; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 509; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 551..554; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12; MOD_RES 282; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 307; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1223.07c; CHAIN 1..580; /note="Aspartate--tRNA ligase, cytoplasmic"; /id="PRO_0000315951" MSEMEKQVENLSLEAKNEKPKEVILGEDGKPLSKKALKKLEKEREKEQKRKEREAREAEEKKKREANEIDYSAGKYGDLPLNRSTARPGRTYTQISDISAKNDGQTVLLRARVYTSRLQGNKMCFFSLRQKYDTIQALAVVNKDTISKQMVKWCGSISLESIVLVEGIVKKSPEIIKSATVQDAEIHISSIYVISPIKKNLPFLVEDAGRSEEQIRESEENAAEGDSKFVRVNLDTRLDNRVLDLRTPTNQAIFDIQAGICQAFREFLLSNSFNEIHTPKMSGASSEGGSNVFKIQYFKTDGFLSQSPQLYKQMLIAADRERVFEIGPVFRAEDSNTYRHMTEFTGLDLEMAFNEHYHEVMEFIEKLFLYIFKTIREKYAKQVAVVRQQYPSEDFILPDADRIRFHFKDAVKLLKEAGYRKQLVPGQKVPEDEEFHYCEDPEFDDFSTPEERALGQIVREKYHTDFYVIDKYPSSVRPFYTMPDPEDPRYSNSYDFFMKGQEIMSGAQRIHDPELLVERMKALGVSPDVGLQQYIDAFAIGCPPHAGGGIGLERVVMFYLNLPNIRLASSFPRDPKRLLP O74413 AROC_SCHPO CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; COFACTOR: Name=FMNH2; Xref=ChEBI:CHEBI:57618; Evidence={ECO:0000250}; SPCC1223.14; CHAIN 1..395; /note="Chorismate synthase"; /id="PRO_0000140703" MSSFGTLFKVTTYGESHCKSVGCIVEGCPPGMNLTESDVQVQLTRRRPGQSNLTTPRNEKDKVQIQSGTEFGVTLGTPIGMLVLNQDQKPHDYSDMDNYPRPSHADYTYLEKYGVKASSGGGRSSARETIGRVAAGAIAEKYLLEAYGVEIVAFVSSVGKIAIPLHETASSAILDPEDDTFESPITAEYLKFLNKITREEVDKTTVRCPHAATAAKMAERITRARDNHDSIGGTVTCVIRNVPTGLGEPCFDKLEAKLAHAMMSIPATKSFEIGSGREGCKVAGSKHNDLFYRNADTGKLGTLTNNSGGVQGGISNGENVYFTIGFKSPATIGVEQSTSRYDGSDGVLAAKGRHDPCVVPRAIPIVEAMAALVVMDAVMIQQSRIASRNLLPNAQ O74414 YJL1_SCHPO BINDING 8..15; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC14G10.01; CHAIN 1..236; /note="Uncharacterized protein C14G10.01"; /id="PRO_0000173042" MLILGLTGSIATGKSTVSREFQEKYHIKIIDADVLARKVVEPNTPCLIKIQKEFGNEVLHEDGTLNRAKLGQAVFQDAGKRSLLNSIIHPAVRLEMLKELLRCYVRGYSIVILDVPLLFEAKMQFICWKTICVSCDKSIQKQRLLARNPELTAEDAENRVQAQMPLELKCQLADIVIENNSDLETLYENIHNVLPLITPSYFFTLLCLILPPLQITLQVIAFVSQKKKVSEFRKHI O74417 YJL4_SCHPO MOD_RES 123; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 131; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 132; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 258; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 310; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 436; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC14G10.04; CHAIN 1..497; /note="Uncharacterized protein C14G10.04"; /id="PRO_0000304026" MSQVIQYSEADLLYLSKSPLIKKPENLPEWILPEAMKADRERHIRQEKEMKRHDDDGRQYQSDRKFAKSKHDDIILGPPKLSFASSNENGRSVGRHDDLLSLGNVYNGVASLRYRNGASVSRSSSIGHSGSTAPWSSVGRHNRKKDNEHRDEMEGLEKVMKQRAGNTGPLVANSTEEFEAWKRMMKASSGEAGAGNVITPGVTSTTGAPSGKASLSRAASNSSTSARAGISVDSLFGKRSAAQAMATVVPSVSTPGGTPPRFASPALTVESMVHAAPSTTTSSRFSKFFNGLAGPETSKTSTPNMSNNPSPRVANTVVSPAPIPTIGSATIDKDAEGFQRVLAMLGRQASSTTGSPKVALSQMPQVNVNPSNQDLASVKQPSGFSPPSAVAPPPGLGNHNFSNDDSSFFRSLMTSDTRSVPPPPGFSTNAPKAVKSPEISAPPGLYRGLSSGASIPSAPPGFGYQQPSFPYSPGFPPSAYNQNRTGYGFPDTSRPPH O74418 SNUT3_SCHPO MOD_RES 121; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 140; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC162.01c; CHAIN 1..244; /note="U4/U6.U5 tri-snRNP-associated protein 3-like protein C162.01c"; /id="PRO_0000374005" MSSSRSGEHRRNYAQGRNYESSRSRGDQRDRDYREYRRNYRDERSSRRYEDSQRRDYSPARRRDRYERHRESVREESPRRPVEHERNWQPELKHGRERFRERDYEGRRDRKERRDGVSPFSPEGEGLERKREHEKLQAPSPKEEEERPVDQGDKMDGVKEDKDGSLEVGKSHDAMTRTKSAEEEIVEQEDEATAEMKRIMGFSGFDTTTGKKHGDVGQVYKQKKTKYRQYMNRPGGFNRPLDNE O74426 PPK33_SCHPO ACT_SITE 151; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 36..44; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 59; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPCC162.10; CHAIN 1..338; /note="Serine/threonine-protein kinase ppk33"; /id="PRO_0000259483" MGNSNSKSVKNDKENFEDPNATNFESVSQFKIRNVIGKGSWSTVFVVKHRQTKQRFALKCINKKKHDEHKIKKLRNEVLLLQSLNHPLLCKFYSEFEDETKIYLVTDLMLGGDLRYHISQRKFNESVIRIWMVELVSALIYIHSKGVLHRDVKPDNILLDEKGHCKLADFNVAAKVHTSSSPSKSNMTVGRVGTPVYMAPETLIHAVSYKESDWWSLGITFYECLFQVRPFPNHLLINWIRASEEEKASSADRLSSALHISRDKKLTTISKDARSAVMAFLEMDIKKRLGHSSKKLQTHPFFCSISLETVSKGNLTPIFRPKSGKVYVDPILDLEATF O74431 ATC9_SCHPO ACT_SITE 619; /note="4-aspartylphosphate intermediate"; /evidence="ECO:0000250" BINDING 1015; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 1019; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; SPCC1672.11c; CHAIN 1..1315; /note="Probable cation-transporting ATPase C1672.11c"; /id="PRO_0000046352" MASPKMIRSKRSTSSIASKNSLNSYLASSLMSHDSIFDGPGLGTSIPSSVSSFHHQTLRPSSDASVSQFSMDYLQSEYNLNRYNDGESIAASRDYQSLLRDNGSGVYSDEEEITEMMLEELNIHPVLRRESVGEAAGLSEDGCCQILYLVEEDLEVGIAGYKTNKSRYRLYQAICLLTLGLAYLIFRWLPKYFIRFVGTREPLATADWLTIETQWGELSKLDIQIQPYENSLSSIFGASIRVAAPEGTENDPFIENFRYVNYRYMKLIFHPLLDRFLIQQDWKDPRWIRDTSVVKEGLERDAINDRLCIFGENLIDLELKSVSQLLIDEVLHPFYIFQVFSIILWSMDSYYYYAICILIISVVSILGSLIETRKTLRRMREMSRFTCPVRVYRDGFWTSISSTDLVIGDVFEISDPELTIFPADALLLSGDCIVNESMLTGESIPVSKIPATDQSMKELFSFSKNIPASLCKHFLFSGTKIIQVRKPFVNEKEEGASLAMVVRTGFNTTKGALVRSMIFPKPTNFSFYRDSFRFITAMFIIALIGFVFSSINLLTLGVPIATIIIRALDLITIVVPPALPATLTIGTTFAISRLRKQGIFCISPQRVNVSGKLDLISFDKTGTLTEDGLDIMGVSVIEGSELGDLRSNSGNLCSKDLLSNDSPSNLLYTMATCHMLRYVDGELVGDPLDIKMFKFTHWSYSEENFLNKKMSSEQAEDAAYVRTQQLIPPTVSPPWNSPSNNYTESDLELGIVRTFEFVSQLRRMAVIVKHGKFKKMDAYVKGAPEIMPSICKPESFPANYQEVLDYYTHNGFRVIACASKQLENCTWAKAQRMKREQVECDLDFCGFIVFENKLKSTTATVIRELNDARIRTVMCTGDNVLTSICVGKRCGMLPEDGYVFLPRFDEESESADEASRQLVWQAIENNEIFLDPHTLRPNVDFADHEPVSIELARLKDFHIALTGDVFRWLVDYAPLNVFHHILLKAQIFARMSPSEKNELVSCFQNLNYCVGFCGDGANDCGALKAADVGISLSEAEASVAAPFTSKWFEITCVLDVIKDGRAALVTSFSCFQYMALYSAIQFITVSILYTTNSNLGDFQFLFIDLVIILPIAVFMGRSRPYHRLAHKRPTANLVSKRILSPLIGQIVLICIIQYITLRIVRREPWYIPPPANSSDTNITNSDVTALFLISCFQYIFIGVVLSIGPPYREKVWRNYSFTAVVVVLLILTVKLIRLQNHKNFFMKLFQLTPTSKSFQNFLIFAGVIYYLLAASGQNYIFISMTNFISHLNNRLLNRRTKVSKKLYKRLFADLQNEQV O74433 QCR9_SCHPO SPCC1682.01; CHAIN 1..67; /note="Cytochrome b-c1 complex subunit 9"; /id="PRO_0000193557" MASSTIYNIFFRRNSSFYATIFVSAFFAKIGFDVFTDSVWKRANAGLTWDEVKPRFLNKDEDAEDDE O74434 MU174_SCHPO MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1682.03c; CHAIN 1..626; /note="Meiotically up-regulated gene 174 protein"; /id="PRO_0000278518" MLLKVSSCEPLVPIKQWIHTSQLDLSDSSSLVADLLYNIIKFNFSGLEDKRAIFTGYESIKRYTIGNEMFLQLAKDGFALPVSMSYGLFLEETDTLELRALPRSEGLHRGCEVLVLRLDSPNELKENIREWSSKFMNSKASQKQQMLSPETMQKVDLAGRASPRYQANDSWISKKRNAPLSSISQYANMPENYALNTKKSKISNENDTIFKANFQQNKYESLHAKQISASDLSLHQEFVSASIVQQPELNSLLTSQSKNSTPSESDSSSSESSSSVSDSSDLSSTSDSSSGDESSDTARQSSSDTISSNNVSVSVSLNTANEFSFPQGTFKAENEAVESEVAPSSSTPPTVEEISYLHYDEPSQYYFSSPSKLSSETTKVHRGCENTEKPSEEGKNFTTPLSDSVESENTWSNTLRSSVEDDNTGVSDDNKKSKLNAEFDGHVNNISVRPPGSGSSATKARNLRRKKARILKRLMQESNDTFSANESTVVANVPDSYLTKNDEEDSASLASLKVAPKYVSHPVSLSSNSFHTEFPIGSLMRFTVMDLNPVTCTPEISEKTGRVVDCSEEKVKIQLDLGDRLDLKFDVNGEVIRNRYGTTPDEELIEGIATYEWSSLSNVHKLELTN O74436 SRP68_SCHPO SPCC1682.05c; CHAIN 1..597; /note="Signal recognition particle subunit srp68"; /id="PRO_0000351070" MDPHVKLSTSLVIIAFRYLPNNFNDSRLGCDNLSTVGLCLKNGTGEVLFSGLIKQMANFYIFPLLLEARSDHFYEGNEYIKYLSHRIHGLRKSLHITQRGGKPKSSVDKRYAEILLFNADRAFQQFVFLRSSQRRHALRRLKRADQFGKELVSFTNAFDCNDHIFYLEAIAFAKYIEGTLNYEKRDWEGSLSAFSISRLSFLVLQNKIDTLAEHEKSVLGELQNQIDSNLRYVAQRTGLQNQTKSLDILMLSSIPKDEEVIQHVNSVDSEILQMTGDEQDSLQTITVIEWRDQRVKIEHPDVVLALYAIHDVKNSPGTIDSKRDRLLAAWARAEEITKSVLDNTGLEDEQKFQTLSICYTYLAYNVVLLRIQRDLAVENDSELVASQAQLRSRQSLYDSIIKNIEIAKELPGIARDTGMTAQLEAQISLAKSKRCQAIADAYQAQDKLASLAMCVRAASYLQQVNDILRNFEEKPHLIAFDIIPELKKDEKELKKKILLLQSLASMGNINQPPKNLSLVETLDSYQTLAELEPSWNLTDADIRAIPAKPLFFDLAITYLGQQTSFDKKKAQPEKPVTSVSKEPKQKNKGFFSSLLGR O74440 RPN8_SCHPO SPCC1682.10; CHAIN 1..324; /note="26S proteasome regulatory subunit rpn8"; /id="PRO_0000213950" MPPAVSSETSTIVPQQVIVHPLVLLSAVDSYNRSAKGTKRRVVGILLGQNNGDVVNVANSYAIPFEEDEKNASVWFLDHNFMESMNEMFKKINANEKLVGWYHTGPQLRPSDLEINNLLKKYIPNPVLVIIDVKPKSVGLPTNAYFAIDEIEDDGSKSSRTFVHLPSSIEAEEAEEIGVEHLLRDTRDASVGTLATRVTQQAQSLQGLGQRLTEIADYLRKVVDGQLPINHAILAELQSVFNLLPNIFSGPVVSEQALESEAQRAFNVNSNDQLMSIYISSIVRAVIALHDLLDSLAASKAMEQQDIKPTVQNGEVSANAEQKA O74444 MU122_SCHPO SPCC1682.15; CHAIN 1..749; /note="Meiotically up-regulated gene 122 protein"; /id="PRO_0000278572" MYRKWDLCITRHLLPYIEHSVIPIIALLVLSLIFYILYICFGTTSYILSGIILGAYVNSLFHNNHSVILNIKHPELGEPLKPYQTPLPPELEAPLQLLISKLTQHYINGWYKHVSEDPSFIREVQSTIEYIMRQFYAYVSSQESSHIIYELLKNAISTTTLVLSDLNHFRSKKIPLTEFALRYPESAVSKLLDQASIERTLRAQASAMIVKFSRPEDSACLPLHCLLREVLAMQVFKRITTHCSSPRFVNRCIILYFSSSEDKSDCLAKKNYVNKCLMAKALKDYPVHTNIDPDAGKLSFDDAFYEAHIELHYQFLKEASLNTLIKDKKMLKFIITVRPVHLHVSPWVVYRRYRGFKTLYYLLKKQSARNGRAVPSFPVWRGNTYEKFREGLYFFIEALLHDSHFATNVDVRKFFAKSMRSHPLVDDIYNGFDVDKKHQSSSVPTLPNLTNISRVLSNKTSKSAKPKRSERTGLLSHQSTLAPEPLSQQRDSFELCTTGYRDTGSCTSDDEDSIHEPYRPASTQPTENPPAMPDHNGSPTTEPPKPNAFELKEERLKEIISGGFALVDELCSLNSKLWFFRKSVLTIMKTTVLHGPGRFSAQVERMLKNQIYDKLSNTQLVGDLLTSLILNVWPDEKKAMESHSTRAHRRSTESKISFDSEADSLFEEASKSVPEDPVSVFCDEESDESLRLRAEKTLVENALSENFTLMLGQSTSEESLKIIFELLQEPQFVQGFLAHLLSNALRSII O74445 PRS10_SCHPO BINDING 173..180; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPCC1682.16; CHAIN 1..388; /note="Probable 26S proteasome subunit rpt4"; /id="PRO_0000084736" MSERDTALEKYKSYLLQHREWDSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQIIGEVLKQLDSERFIVKASSGPRYVVGCRNNVDQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKVADLKKLEGTIDYQKL O74446 SIF2_SCHPO MOD_RES 135; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16C4.01; CHAIN 1..382; /note="Sad1-interacting factor 2"; /id="PRO_0000097758" MSNRIGPQRSTKTAAKLRLLPSTEEFDDFRRQDTGREVYSQIPQIEGSTAKRDAEHLGKRHREFLPRVTAYCTCDTFRVDLLFKFFQSRRSSHKTRPKQFDECIYSPYSYNNEETTDLLPDTLESSRGTLNRESSQESLQSIFEESGLDRNQPLFREVFCFTYGVVVLWGYTIDEEHRFLRELGRFEIEKLKIEDMEVEEFNYYITTLYQPRIFNDFIALRDASNYMIRLSISHAIAQSVKISLFEELVNETIDATKDTPQMIAETGRVNLKREEIMMAVGQLFILRININLQGSVLDSPELMWTEPQLEPIYTAARSYLEINQRVALLNQRVEVIGDLLSMLKEQITHTHDESLEWIVVILMGLLVLIALFSIVVDWKLFQ O74450 POP3_SCHPO SPCC16C4.05; CHAIN 1..201; /note="Ribonucleases P/MRP protein subunit pop3"; /id="PRO_0000337991" MKKKQTKVKQTVKLVLRNPLSISWPIVDANTQEKLAQTLVQWLPASHKDILDSKLTVGLNSVNELLERCCQNAKDVTQPAVVFILHDQDSMLVTHMPQLVANANFYGSSKCRLVPLGFSAQALIAKKLGLSRAGAIAVQDDSPLWKYLKDLVMNIEEPQARWLSENPEYEVTKVEKIITSQKENQGTKKEGKNEKGNEFKK O74451 YCG6_SCHPO ACT_SITE 96; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 154; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a uridine in tRNA = a pseudouridine in tRNA; Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; SPCC16C4.06c; CHAIN 1..413; /note="Putative tRNA pseudouridine synthase C16C4.06c"; /id="PRO_0000316610" MHSLLRPSRFSANQSVLCLLQRHRVFFSSISVKPRKRMVYCVVSYRGTGFAGLQYNANVKTIQDTLFQAFARVGAVVQVNADSPKKIRMCSAARTDKGVHAIVNVLGLKVLDNQPLPHVVNLVNDILPPCIRVWKMARTFNSFSPHTVCDSRVYEYWLPVSSLLTPRPCTLEAYVIAKASEKAFPINETLSHLANLSKQDCVANSLSEPFRLSKPKLDFLKHACTMFRGTHRFHSYTTEKGFSDASSRRFLLDVRVDNLHIDKLNRQWVKLIFHGQSFMKHQIRKMVGILIHLTRTGWNAQVLLNTFNNSYRIRIPRAPAEFLLLNQPIFQAFNKKCSRFDHEPVEWSCAQKGIDQFAHSFLRTPMFDCFISSESFQSFFILQKQFQLFQDLALLTSFDFLEPSSRRDILGEK O74452 SCW1_SCHPO MOD_RES 191; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 193; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 196; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 216; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 218; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 231; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 302; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 325; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 370; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16C4.07; CHAIN 1..561; /note="Cell wall integrity protein scw1"; /id="PRO_0000081901" MFVGSPSAIEKPLSLSSKTKVGDETEFTEDALRGSSLVPTGILNGDDECHALHMSPQAIHSQAGKAESDGLPTYASVEKSTTPIGRLLSNLNGGLASAPPKVGFGFPRYYALRIEDLPRDLTPREFLCTFLFATNVVSVELNPVSVDNEVAHGLAVFSSRDAAASARDTLLSSDVYSACSMIILDNYRKGSQTNLSDETEGSESSVSFNRLSRNHSPTRPLLGNRDLFRRSSNHVSASMPTANHSESAYRHSKTPLGDSTFQAPNNGGSLHSDRLWSSFPVSYPLTLANVLAKDEVGSPTWSPTPSKSSTNLRQDGVPPILRFNSLSINTNVARNYLSSEKGYSAHTQNSSAQSPHPRVFSANSAFSTTSPPPLTPSTSRDYPFSASTISPSTPFSAYSSSHGIHQRIPASTPTNTNPADQNPPCNTIYVGNLPPSTSEEELKVLFSTQVGYKRLCFRTKGNGPMCFVEFENIPYAMEALKNLQGVCLSSSIKGGIRLSFSKNPLGVRSSSSSHNNHNGNVRNLHSGSMNNYNTDSLLNHTGGHNEVHASPSWGNNLMYGK O74457 NAT3_SCHPO CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-[protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254; Evidence={ECO:0000250|UniProtKB:Q06504}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-[protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254; Evidence={ECO:0000250|UniProtKB:Q06504}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein]; Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254; Evidence={ECO:0000250|UniProtKB:Q06504}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein]; Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254; Evidence={ECO:0000250|UniProtKB:Q06504}; SPCC16C4.12; CHAIN 1..180; /note="N-terminal acetyltransferase B complex catalytic subunit naa20"; /id="PRO_0000310295" MTDTRKFKATDLFSFNNINLDPLTETFNISFYLSYLNKWPSLCVVQESDLSDPTLMGYIMGKSEGTGKEWHTHVTAITVAPNSRRLGLARTMMDYLETVGNSENAFFVDLFVRASNALAIDFYKGLGYSVYRRVIGYYSNPHGKDEDSFDMRKPLSRDVNRESIRENGENFKCSPADVSF O74461 MU123_SCHPO MOD_RES 180; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 187; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 189; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 191; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16C4.17; CHAIN 1..235; /note="Meiotically up-regulated gene 123 protein"; /id="PRO_0000278622" MERLATRSSHDDPYSRSSLPTSNAINSNHESNGSTFSYVQSLRRAKATVWSDIGRVAPLHSSPSIKSSSQNGKSSSKGLGGMRSRVFSSQHHGVYHTRPASLHSRTMAPQHTILTPRLSATEGKDDDEDELVISTSNTAPTYISMIESSRASSTHSGTAPSIMGMSIHSRADSRAETTQSDGFESRSGSPTHDIQSYLVNRRSSSSESSDEDSAEEGMKRLVITNMGDNDEFDSD O74463 YQC1_SCHPO MOD_RES 343; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 344; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 483; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 489; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 495; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 499; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 502; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1739.01; CHAIN 1..547; /note="Uncharacterized protein C1739.01"; /id="PRO_0000116888" MSAASSAIPKRSDPRLLDQKKSAKSTLPKNTPENGVSTVKNLQHVPCKFFRNGTCTAGENCPFSHSLETERPICKYFLKGNCKFGPKCALSHALPGNTNLPNGTSTNTMASMAANGGASSVASKQMGANQISPSLSSKTMKNPADKANNTTATDVRGNTATSPYFPFSRSPGRHSGNSTINGMMTTPNFLSSGVNSRSVDEFNNSSSGFPSSLNGIPIASPPLATSPTSFSLASSASSTNLGGSKGLLFQQMTSENNRDYFSRRPTLLNTYGNRCSSTDTLSSLSRLTSQDPLKASLPLQSPPLAPKTGVSLSRPRLTLDQSLGNLSLGSGINQRRQVPRSNSYAGAFPSVVSASLPTKVDLNHQMDVSDEEQRFLSTPLGSFDESILGSSPINRLSSSFKQYTSSLKSPGLSTRTSSTMNSLNSSRFGAYFSKSRYVEGSGSMSTTPLATSVNNSYKLPSGFSVREEAVFSSPTTEGSRPVSLARLKSEPIFRSDTASPETIAGLGDTKNDPVVSTNNSVSRITVANSSPPWNSTVEEETPFQMDD O74464 RM22_SCHPO TRANSIT 1..22; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1739.02c; CHAIN 23..249; /note="Large ribosomal subunit protein uL22m"; /id="PRO_0000310372" MKYINQFMKISKGFLVPSSTIGLNSKTYHYKFPLLSFVREFSNGSYLRESAQNPANLGSQKGSDIFSMLANQKDDSNRQQKEERVKERPRSRISFKKQETMDPSYTLQSMVLRSSLKKVGALCRQIAHKPFYHALLQMKMSDKKISKYIATALVSARENAVREAGLDESTLYVDQIWVGKAKYLKKLITMGRGGRAIERSPRVRVTVVLRDERALLRDLQRRQQRLERKKVWTPLPNRPIYLKSNFFTC O74471 COX13_SCHPO TRANSIT 1..31; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1739.09c; CHAIN 32..130; /note="Cytochrome c oxidase subunit 13, mitochondrial"; /id="PRO_0000006126" MSMMNRNIGFLSRTLKTSVPKRAGLLSFRAYSNEAKVNWLEEVQAEEEHAKRSSEFWKKVTYYIGGPALILASANAYYIYCKHQEHAKHVEDTDPGYSFENLRFKKYPWGDGSKTLFWNDKVNHLKKDDE O74474 WTF21_SCHPO SPCC1739.15; CHAIN 1..329; /note="Meiotic drive suppressor wtf21"; /id="PRO_0000193233" MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPPNTHRENNPSRSTDNSSPFLIKLLISFTPIYVLNVLAICYLTYKDAFFKDYGAAEWTLFGFWCLVCTLALIFLTYFYETWVKAVKVTVISLAKCVKVISIGLFNIRREMMIIIWILWLIICCILFVYIKSGDLILNKALICSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVLLLQSGIVLVLNGTMFLRGKHFERIGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILGGIGNAMMGLANAIRGANDNNDIPLGEMDVESEV O74477 MCA1_SCHPO ACT_SITE 214; /evidence="ECO:0000250"; ACT_SITE 270; /evidence="ECO:0000250" SPCC1840.04; PROPEP 1..?; /evidence="ECO:0000255"; /id="PRO_0000333668" CHAIN ?..425; /note="Metacaspase-1"; /id="PRO_0000310335" MSYNSNPYNGGQYPPYNTYTRPNYSPNNGSQSNNTVHQYQPPRMPPPSTRPQTDGNSNQIPMENVGHISLSSANSHAYAPPSGPPPNTGANSYGNPNYSGPQLPNTQTQSYNLAGGGNFQYQYSTCQGKRKALLIGINYLNTQNELQGCINDVMSMSQLLIQRYGYKQEDMVIMTDTASNQRAIPTRQNMLDAMRWLVSDAQPNDALFFHYSGHGGQTKDLDGDEVDGYDETIYPLDHQYAGQIIDDEMHEIMVKPLPAGCRLTALFDSCHSGGALDLPFTYSTKGVLKEPNMLKESGMDVLHAGLSYASGDIMGAINNVKNIFTSATNGFNNNALQYSRQVKFSPADVISLSGCKDNQTSADTSVNGFATGALSYAFREVVTQNPQLSYLQLLRGIRQVLSNKYSQLPQLSCSHPLDMNLAMVL O74479 ATPO_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1840.06; CHAIN ?..216; /note="ATP synthase subunit 5, mitochondrial"; /id="PRO_0000002655" MNHIFRRSIPITARLPSLGIRSLATATASAHPPVQLYGLDGSYASSLYTAAVKESKLDNVEKALNKLSGVLQQRPEFEQYISSPWLTREDKKILVSSLTQMTGNEPLLKNFYNVLLDNHRLYLLTRIQKQFSTLMRAKRGEIEVKITSATPLDSKILSRLESRIAKSKYGKGKLLVSNKVTPSIIGGLIVEIGDNILDVSVGSRLNNLNKLLSEPI O74484 MPG1_SCHPO CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527, ChEBI:CHEBI:58409; EC=2.7.7.13; SPCC1906.01; CHAIN 1..363; /note="Mannose-1-phosphate guanyltransferase"; /id="PRO_0000068740" MKALILVGGFGTRLRPLTLTLPKPLVEFGNKPMILHQVEALAAAGVTDIVLAVNYRPEIMVEALKKYEKEYNVNITFSVENEPLGTAGPLALARDILAKDHSPFFVLNSDVICEYPFADLAAFHKAHGAEGTIVVTKVEEPSKYGVVVHYPNSESLIERFVEKPVEFVSNRINGGIYILNPSVLDRIEPRPTSIEKEVFPAMVNDKQLHSFDLEGYWMDVGQPKDYLTGTCLYLSSLRKHKPEILAPASSNIIGNVLIDPSATIGKNCKIGPNVVIGPNVTIGDGVRLQRCAILKSSRVRDHAWVKSSIVGWNSTLGSWSRLENVSVLGDDVVVNDEIYVNGGSILPHKSISANIEVPGTIVM O74485 CUE3_SCHPO MOD_RES 386; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1906.02c; CHAIN 1..581; /note="CUE domain-containing protein 3"; /id="PRO_0000310343" MSENVISSSKNVVSKLLYVKDEYWPSVAPAATELISKLINAFWCQTLNGQLVEEDEGERNCIFLFDRCLKTEGCLKKIGPVTVMQFLACFLLSSQNHAYAWSVCRQIPSDDMAFKFTKCFQNSQQFRDANFCKLVLVWTVCQCVSSTVYYPAILDLLPVLSDLVKEMEKDPASLQAKENEFWLKKLIQTSLHHSSDNSLVFYLEMLLDSLDLRNCIYVVFEDEALFRRLKDIGNPEIRMMLDSGLRDWRKQRSGRSSSHVASKGINKVVNINPGDVKSLIELFPQLSVEEAVEHLSASLGNIDAACESVITSSLPEELDSSTHSPIYTKPNVDSMHKQPKKAIAPLSLSSSVTAVISNRTSDKKTRSTVAEEDDITHLNISPDRLYLNKKPEDLNFWKKSVPETDKSRVLNLLAMAEDDEYDDTYDDLDTTGPVDSGVGDDDPEASSKDAHDFQKFINQTLYDFYQQNPEVFDQKARKSKERADLLAKLDNSLTHEQIEGWRRMFTTDSKFAEAVKKEVTFGSGNTNIGSLRQTKFKQSNYTPPELNDGSRQHRPSRPSKNPSLKKKKYVRTKPKKASNEK O74489 QOR_SCHPO CATALYTIC ACTIVITY: Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone + NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; EC=1.6.5.5; MOD_RES 191; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1442.16c; CHAIN 1..329; /note="Probable quinone oxidoreductase"; /id="PRO_0000339115" MSNLLVQVSKTGPSSVLQVITKEIPKPAPNGLVIKNAYAGLNYIDTYLRTGLYTAPLPYIPGKEAAGVVAAVGDKVEADFKVGDRVVYLTPFGAYAQYTNVPTTLVSKVSEKIPLKIASAALLQGLTAYTLIEEAYPVKTGDTVVVHAAAGGVGLLLCQMLRARNVHVIATASTAAKRRIAIKNGAEIACSYEDLTKVVADYTNGKGVDAAYDSVGIDTLSSSLDALRNGGTMVSFGNASGAIDAIPLKFLSARCLKFVRPSLFGYITGHAVFEGYVSRLWKEILDNNLNIAIHHIFKLSEAKEAHDAIESRATTGKLLLLCNEDLADA O74490 IST1_SCHPO SPCC1442.17c; CHAIN 1..271; /note="Vacuolar protein sorting-associated protein ist1"; /id="PRO_0000274480" MSRLQIQLKLAASRIEILRQKEEALAKQARRNVALGLKSYSPALAKARIEPLIMQDIYIELLELLQVDVEILANRCVVLEKRAFNDSMSFKSSLYHVMAAAPQLQIKELRFVHDFLVKLYGKEFARLSDPDLATNDTAFYQLLYPPIPKDELVEAYRKELIRTYFPNDYPKEANKDIPSSAEADTMLNLESSENREQPTSLKEENTQEDDEKVNGNLANISKRAEPQNNGSTNASSLQSSNYLPTNPTLTHSNKAPSFEELAARLDRLKHL O74492 HIUH_SCHPO BINDING 16; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 57; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 121; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072, ChEBI:CHEBI:58639; EC=3.5.2.17; SPCC285.04; CHAIN 1..124; /note="Probable 5-hydroxyisourate hydrolase"; /id="PRO_0000050605" MASNPPQPQGPALTAHILNTMSGIPAAGVQVALFKLNESPTPSQQFIATTETNANGRVTSWNVDLSTVESGIYTFRFETGAYFDSLGVTSFYPYVEMAVRINKGQHYHIPLLLAPYGYTTYRGS O74495 WTF18_SCHPO SPCC285.07c; CHAIN 1..372; /note="Meiotic drive suppressor wtf18"; /id="PRO_0000193230" MKNNYTSLKSPLDEEDELKTDHEIDLEKGLLPEYNSEEEGTLPLYSDISKLANPVPEDSSTGPTEIANPNVERRQEFKDSHPNIYFLLRLLISVLAVSVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPILFIATFCFFETWTQAVAQCIKVTVIFLAQCVKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLEGIGNAFGGIGNAIGRIGNAFRGANDNNNNIPLEETEAESEV O74496 COPD_SCHPO SPCC285.08; CHAIN 1..240; /note="Coatomer subunit delta"; /id="PRO_0000316200" MVVLAVSIVNRGGKAIISRQFREMSRVRVESLLSSFPALVSEKSQNTTVESDNVRFVYQPLDELYIVLITNLQSNILQDIDTLHLLSQVVTSICSSLEEREILEYAFEIFTAFDEATSLGYRDNVSLTQIKTYLEMESHEEKIQEIVSRNKEIEATEERKRRIKQLELQKKEAARRAAQNLPSADAYESIGYQTVNTTFATSNVEDESAMESYHAAAKASSAPKAKGMQLGKKKNTSLLY O74498 UCP10_SCHPO SPCC285.11; CHAIN 1..427; /note="UBX domain-containing protein 10"; /id="PRO_0000314760" MSGSRKQEAIDELRNSLDVPADTAQSVLESFNWDVQEAIESLTGESSRVDRNSKLGLSFGVFQSVFSLLFSGLHKLWMILSRVPLISTFIPIFGTTKRVLSPADTANKLVQNLEEQYGTEHIDFFTDGGYMEALTRIKRNYGVALLFFTSSKNDDSETFSRSVLMNQELKEFLNRRNILCWTGDVCEDEAFRGSRQFHCTKFPSAVLVMYSPQLSELVVAAQLHGCLDSSSIITNLTNALAKHLPSLERFRSEREAREAARELRRQQDNAYQASLARDRERQAFARAEEERLAKEKEEREIVQKKKKQYRAWLASNLPPEPSSEDEPARLSIRFPDGSRAVRRFKKDDTVESVYNYVDYMLFEKEEPEEFGRATSSSNPVTPPSDYKHDFHFQLYSSLPRALLKPSVAISTNKAIFPNGTVVVELDD O74510 BQT3_SCHPO SPCC594.07c; CHAIN 1..255; /note="Bouquet formation protein 3"; /id="PRO_0000304117" MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL O74512 WTF14_SCHPO SPCC663.02; CHAIN 1..229; /note="Wtf element wtf14"; /id="PRO_0000193228" MENNHHLAKDSLDELNPKRGKGEHETQVSQYTVVEEATIPQSLVKTSRPADHKVMEASKVADTRTAWSTKIPAVLLPVFVINIALFKYLVFANFSTKDRVLFGLGNGGINIFSMWLLLATYETWFRSIKEVIVACGAGIRSFPQKRGVNMLYAILKLTFVNAFAIPLLMFFRSHFEQWRLGCPLVERVIGVMLNVAYFIIEIENPGLFTRVFNKYCDCLFAIRDILNRN O74517 SAF1_SCHPO SPCC663.11; CHAIN 1..278; /note="Protein saf1"; /id="PRO_0000372375" MLSKRGLNPVQAESRKKKKREQIKVREERAKRHEERLSHRNMSQMERQLSELTQLESSQALNAHDKQLLQNLQRDMAIMKKKNIHGHRVGRVESDKTKEAERQHKPRKPFIPKNPKRSIYYDPIFNPYGVPPPGMPYREKEELSSETDESVIDIPLPSEEYPFEDPKPREKKNKSFKPKHHKKQDINASSAQPKSTTTTEAAANTKDIEEETMIEYSAQPVVRDLRQEAAQFLPAAFQRQKLAKGQKIGQPDRDVSSQVQEDKDEEIDNFYKEIGGYL O74520 YCPE_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPCC663.14c; CHAIN 22..687; /note="Uncharacterized membrane protein C663.14c"; /id="PRO_0000372621" MKLILLAYFAVLSNILSSVEGRVRYSKRPNHKLGTAEYAECMSNAPIVFNRFDASYYTRNLSVVFNILGYSSVDANVTFDIIVEAYGEQRARFTFDPCEINLNTVCPVARDTAITTQGILPVSPQDVQMIPKIAWGIPDFEGLVRFRMYRSEDIAASSIDNSTPLACMIATLNNGHTFKNKVVKALSGTALALSIAGVLGFYVIGMEHSTYLTRQVFINSVPSLQHMGELLQCIAFTGAIGITQPKVLVAWASNFAWILGFITNKEIENSLESFRKHSNGNLSSPKIGGVHRRDAVATNPQSPIPGFYHGFQGLATEVGTLTTNLFTLTLIWFLISLAIAGGIVIIFVLIIKFLRQTRIIAKSSCDYITRYWFRVLFNACMRWVLVCWPVLVTMIIYQFTLREAYGPVILAALLLALLFGLFLWLTIKVIRVITTSGLSNEDNPETLISDPKIYTWWGWLYLDLKERRWLYVYACFAHYFSFALVLALVQQFAKIQTILLFVIEIISFILLAVFRPFVGFKNSFCVFLVALTRVVSFALLIPIAFDLAIIPKVIIAIILIIIQGLVFSFMALWSLWNFITMLGTAWPAISYTVPWLRRLIDEYQRQLHIDFENPAVSASEKLSTEEIIPQESNFEEPSTTKKEGNVDTKEDGNDDVFSLVNASPMRPASTIPSHSCDNGINEMQRTV O74522 ADN3_SCHPO SPCC1494.10; CHAIN 1..964; /note="Adhesion defective protein 3"; /id="PRO_0000116893" MADFMDIEPSSHSAKASQYESSAPASSSLGNSHPNESLDYYIYDYFVKHNFEEAAQAFLRESKIQIPKSSSSTAFSPSNNNAPSPFPPKNSSLASPSKISESISGDRLYNHMSSAPSPNKKEETNVVHANEDISLDKRQSFGSSSLPPSEVSINVPEGFLVEWFNIFWDVFSARVSRVNSTPIQLYDPSTQRQMARPMSNLQASQPVPSSTFSRSAVVPNPSLPLNPSVLQGQVMNNPTIPKGTPSTSIEGAKTSIPPSHAMQNPHNSFPASADRLQKNHPVQSSNFNPYTPAPSITVPPNYIPNTAMMGPSYSSFGDTDPRTYPAGMGPNPTAARNGFYPPTPAQIHQLKAQQQHLQRQSKQMSEPAPINMKSNKDQQLQYVDFRGVGSGADLQKQQWNKSTSAEGLQPNGLVMRNFGDVRHQKLPTSSPPSQHPPVGQIPSQYLPYQAGLKVPGNTPIPVKQVGGMPLQSPLPVSMKPSADDHSRATPTRSVEAPTLPSYAPRHPTQANGSRYMNPSTSRMTPQSPYMQNYYRPHAQMQDQNNMMSYMLSQQKAMEIAKSREMAIQRNTQTLSSGNQPPQQSGPNPNEFSMSMDPANMQQGNHALSDYHMQLMLLEEQNKKRLMMARQEQGTGSLSPQSYMNSRYSVDVGKEHMSMIPNQTAPMIQPNVPVSANSPAQANTPAADSTKSGTIQPTNRNGEGLSYSPHQQFSPSAPQAEKLSRSMSPFVSQQQQLNQPVSNKPDGLTQNKEVTGMPLNKEELTNPAFPQSRTSWMMPQSFDTSSLNAPGAKDSSSFSSLHAQPGKSGIATMGVADNTIRTTERSTFSEIMKDSPSAHASPGAKTSPNASRAPEPTGGTNSISQDTTQSLQMQSNSVNSSSMVDASKSKEKSGGDTSALDSNAKNEPTAAKPISKLEDDALFNDSAGNAFGFSSKTDSNVEMLNDFDFESFLNDAGADSASVYY O74524 PROD_SCHPO CATALYTIC ACTIVITY: Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039, ChEBI:CHEBI:132124; EC=1.5.5.2; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC70.03c; CHAIN ?..492; /note="Probable proline dehydrogenase, mitochondrial"; /id="PRO_0000025805" MRAFRLASGVLRNRKVILGIGAGSLITAGNIKIRNDSKFDAFFAKGFPDELQHRSLFSVLRSAFVYEICSRAWLVKLSLGAMSLCDVFHLSFLYNPFCRYTFYKHFCGGETPQAVMATMDTLQAAGITSCLNYSREVDLDGDMDVNKIASQGVVPPQVPVPSEKNQKVLRQIADKAFESNMHIIDMATYKPGTVCAVKLTPFINPLVLQRYNSILNQYPVESACNYLEHLKSPELSTYEVSELKKFWEYADKLCQFAKEKQIPLFIDAEQTYFQDCMHAVTVDLMRKYNKEVAIVHNTYQLYLKKSRKIMDDHIKKCVAEGWLMGAKLVRGAYLNSEPRFLIHDTKAETDKDFDSAVEAIIAAAAKFAPGDPASASDPIASRKGKWGIMVASHNKKTMFESVNLAETKKVDFTKTSFYLAQLLGMADDITYALAYSQRNQQPNFCIVKYVSCGPISEVLPYLVRRARENIDALDRCKEERAYYRQALRRRIF O74531 POF7_SCHPO SPCC1827.08c; CHAIN 1..361; /note="F-box protein pof7"; /id="PRO_0000119974" MSTVEDQLSLELETVNKDILLKKALLHYKDAIKSEREGNLGESLNKYRLAHKVHEDVESIYRRLERLQLCKRNEEEEMLNSDASEAMLTVSSVPSPTLTENESVNESVVPNILKLPDEVLLVILENCIRDLHDLRYLSSIALTCKHFAKALRADSLYRSFCYCSCEQKEWQQSIKSIEEELVEKYQQSWKTLFLKKPRSRFDGCYISVCRYFRPGTSDTSWNQPIHLITYYRYLRLYPNSTCIVYQSSNEPNDVVRNFSVQNTSLFSPMSSSPMFSNGNVALTGSWSMTPSGEMLIVYPASQTYTYVQKLQVRGIRLKWISFYSIHNYTSFTNEMPLTHNRDYVFSRVYSYTADSESLKRG O74535 CPSFX_SCHPO SPCC74.02c; CHAIN 1..710; /note="Cleavage and polyadenylation factor complex subunit C74.02c"; /id="PRO_0000351430" MDNWNSVRNVSSDRQTSKTSENPPHTSNEYSGKPEFINLSPDLEENLDEKLMSAFPGLEPHVFQHSQSPLSHKDASLLATMPSVASSNPSLISSGSSQTGSPSQSLSSNKEPSSPGISPSNDSQSQNTNHTSISANPYVNNPSHTSRNPDSGSSLNTASHEVPSSKSDVNVQMLARLKSKSRQKISSSDPLEDLRLTLTECLNPINIVQAPKECAAILVNLMSNITQDDQKLVFLDLLKSKVGNSIYSQLVDGGRKLFLPKLRNWFVSAIRSKHDELIHLILLVLANLPLTTEKLAEVKFGKPILIVKKKSTNSVIRQLAENLSELAEKSFTIEQNRENEKSSTKNDSTVSSSAVVMAPAGPAMAPSASNKPSASSTTKSSNSKSKKKVTSISGTSFFKNLASSTKPTSASSSTKAPLTKQQTNPSTPLSSIMAGLKGREKEKDKDSGISSENVSNNREELPSFRKRSSSSRQSEEIASLQAENAVFSSDPASNDEKTGNKKRKKKSVSWKPDNDLVQVKFIESLNEEGAASVKTPHIYGNARDMDRQEARVAFGSHVEDDVENEIIWYKPVPIKFEISKDEIHPRGYKCGGNERNLTPEATSEIEREKNESKDISTFNIILDLPVIREFDDSRPPAHIKLVSSDTQATTELGFNGLVQQVSENNTNAYSATSNSQLSSIFSNLSSSISDASSNVLQNPSLSIPNYSNAI O74538 RL27B_SCHPO SPCC74.05; CHAIN 1..136; /note="Large ribosomal subunit protein eL27B"; /id="PRO_0000126091" MVKILKPGKVALVTRGRFAGKKVVILQNVDQGSKSHPFGHAVVAGVERYPLKVTKSMGAKRIAKRSRVKPFIKVINYNHLMPTRYALELDNLKGLVTPTTFSEPSQRSAAKKTVKNTFEEKYQTGKSAWFFTPLRF O74546 OMH3_SCHPO ACT_SITE 276; /note="Nucleophile"; /evidence="ECO:0000255" SPCC777.07; CHAIN 1..378; /note="O-glycoside alpha-1,2-mannosyltransferase homolog 3"; /id="PRO_0000316585" MGIPKSSIYFCILLFCIISFYLQSSKDGPKELKVKYVFLKKATAKQRGESSLTDSDYFPKQPNMNATLFMLCRNRDIKDALVSIQSVEDRFNHRYHYPWTFMNDAPFTKEFITATSKMVSGDATYVQLNNEEWGIPINIDLNRMLKSIRDMTDDKVIYGFSLSYRIMCRFNSGFFYRNKALSHYDYYWRVEPGVEYSCDIPYDPFRKLSDENKAYGFVISMTDYYETLPSLWNVTRDFIHQNPQYLAQNNSLDFIVNDHQGLSGDYNLCHFWSNFEIANLNFFRSPAYTDYFAHLDKNYGFFYERWGDAPVHSLAASLFLNKSQIHYFEDFGYYHLPWYHCPTDVQSHATARCLCDPTGTIDYLPFSCAIKWLENINS O74549 UBC12_SCHPO ACT_SITE 105; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine.; EC=2.3.2.34; SPCC777.10c; CHAIN 1..177; /note="NEDD8-conjugating enzyme ubc12"; /id="PRO_0000082499" MRKIWELKKKEAQKEKNASGISPAQIRIQKDVTDLEIPSTMSTSWPDPIKLNVLHLEIRPDEGYYKGGKFKFRIQIDDNYPHDPPKVKCLNKIYHPNIDIEGNVCLNILRQDWNPVLNLNSILVGLQFLFLSPNAEDPLNKEAAADLHKDPQGFASRVRTAMKGGLVNGISFDNVMA O74561 YCZ8_SCHPO BINDING 728..736; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q12494" MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 585; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC970.08; CHAIN 1..967; /note="Uncharacterized inositol polyphosphate kinase C970.08"; /id="PRO_0000318136" MQNAPKCYLPNSRKGRDVNFHDRGPETLKCLYDESEDNNNFTMHSESIGPKSLDSLSPRRLSNYSSAVDPRTTSLEDVPRLILTRSNSQEQTPLRTHTPVEYMSDSIHKSLADLQLGGSSYSVAESPVPVLQSSAVSEADDMASAHSAHPSRKASRSLRLFESSTSNNLETGNSTNTALHNVSSPLESVSERLSKSGSPSVGAQHDLDEVISEKDTSLSRRSSRGRSSAPKRRKDSGSSKTTATYIPHNPSKKSSQHLPLLPDASFELERSVSRSYQSPASTPRSSVSSVSSSPPEDHPFFHWNVDYPVTVRLEPFKHQVGGHTAFFRFSKRAVCKPLTRNENTFYETIEACHPELLPFIPKYIGVLNVTHTITKTEENDSTTEYVNTESSSKTPAPHKHTFNSCYQKKDYGYIPEVSVEQNRHIFPEWMLPDKRSHSYGSPKSLHHKSSSAGERPVSPTFVADIPPKTPWGTTLINRKLREEVLREVFAPKHARRRLGTRFHSRSSHRPSVFRDNSVAFGQLDNGNTSSRARDKDADPNKSLSCSVEDKHYDLHSAVAEENEEVDEELLNVPSNNQGKSYRRFSSDAVWEEPESNEFPRVSGTMEDYDSRESTGHTIKELRSTPNSHGTVPDDSIFAMDNEENSELPPPLEPAEIGDPFRSVNDPRRVLSLPHMASADEDHRIPASDNQNNNNNDANALAENSESQHSTQIERYIVIEDLTSGMKRPCVLDVKMGTRQYGIMATEKKKASQTKKCAMTTSRVLGVRICGMQVWHPWLQSYTFEDKYVGRDIKAGEEFQHALMRYLGKTDDDEDNSHLLVHHIPTIIRKLEQLEQIVRFLKGSRLYASSLLFLYDGEPPPSDKSSKEKVKPREIDIRIVDFANCVFAEDKELLAKATCPPQHKDTYDRGYVRGLRTLRLYFLKIWKEAKGMQIAERGYEDSLSNAYDELGGLMSYSNDDDSCGETST O74690 SNU13_SCHPO SPAC607.03c; CHAIN 1..125; /note="13 kDa ribonucleoprotein-associated protein"; /id="PRO_0000290662" MSVNPKAFPLADSGLTQQILDLVQQASHYKQLRKGANEATKTLNRGISEFIVMAADTEPIEILLHLPLLCEDKNVPYVFVPSKAALGRACGVSRPVISASITTNEASDLLPQIQAIKLAIEKLLI O74729 PPIH_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPBC1709.04c; CHAIN 1..173; /note="Peptidyl-prolyl cis-trans isomerase cyp3"; /id="PRO_0000232959" MSTEPVVFMDIAIDGRLLGRIKIRLFSSIVPKTAENFRQFCTGETLGVNQKPIGYKNSTFHRIIQGFMIQGGDFVSGDGTGSATIFNSRTFPDENFTLKHDRPGLLSMANAGKDSNGCQFFITTVPCDFLDGKHVVFGEVIEGYDIVKEIESTPVGANSRPKSNVAIVECGEM O74732 ERG27_SCHPO ACT_SITE 180; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 203; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 207; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 16; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 44; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 50; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 75; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 203; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 207; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 236; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" CATALYTIC ACTIVITY: Reaction=3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-methylzymosterol + NADP(+); Xref=Rhea:RHEA:36379, ChEBI:CHEBI:1949, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:136486; EC=1.1.1.270; Evidence={ECO:0000250|UniProtKB:Q12452}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36380; Evidence={ECO:0000250|UniProtKB:Q12452}; SPBC1709.07; CHAIN 1..338; /note="3-keto-steroid reductase erg27"; /id="PRO_0000371806" MSFRKYALITGSNSGLGFGIATRLLQFYQPRLQDEPEVFTVILTCRSREKAEDACRRLKEFFPDRKIRLEYVLLDLSNMASVEAAVQDIATRFPKLDFVYLNAGAWDLEGIQWLKAIFSTLINPIQALTHPTFYKETAGRVSNDSLGYIFESNVFGHFYLKNRLAELKVLRSSTKVVLTSSLVAEKKSLDFEDLQCFHGEQPYQSSKRLLDVLHYAELEKGLPFEQYLVHPGLCTTNMYETFLGPILVMCAKLGFYICRLLGSPWHTISPYVAAFAFLWTALHATKEDQSIKWGAAVTRFGHERVLSTPVELILPSEQEKALEYMTKLYQEWKKKLVS O74733 CFT1_SCHPO SPBC1709.08; CHAIN 1..1441; /note="Protein cft1"; /id="PRO_0000290635" MSTIFQDLVDSTVIKNAVQGQFTSLVSNNLVVSKVNSLHLFEIEKIQKDESSFPLDDSLQNEFSTSIIDESQAFMETNMHLIRTNEQTTYVLRLVSQVKVFGTITEISALKGKGSNGCDLLIMLTDYAKVSTLEWDMQSQSFVTNSLHYYEDVKSSNICSSHTPTQLLVDPDSDCCLLRFLTDMMAIIPYPANEDLDMEEAAIENSKISSSYAYKPSFVLASSQLDASISRILDVKFLYGYREPTLAILYSPEQTSTVTLPLRKDTVLFSLVTLDLEQRASAVITTIQSLPYDIYASVSIPTPLGGSLLLGGNELIYVDSAGRTVGIGVNSYYSKCTDFPLQDQSDFNLELEGTIAIPLTSSKTETPFVVLVHTSGQFFYLDFLLDGKSVKGLSLQALDLEINDDFLKSGITCAVPAGENLVFLGSQTTDSYLLRWSRRTTNEEVRLDEGDDTLYGTNDAEMDDMLDIYETDESVGSKRKIAYENGPLRLEICDVLTNIGPITDFAVGKAGSYSYFPQDNHGPLELVGTAGADGAGGLVVFRRNIFPLIAGEFQFDGCEALWTVSISGKLRNMKSRIQAQYSNPELETYLVLSKEKESFIFLAGETFDEVQHSDFSKDSKTLNVGSLLSGMRMVQICPTSLRVYDSNLRLTQLFNFSKKQIVVSTSICDPCIIVVFLGGGIALYKMDLKSQRLIKTDLQNRLSDVKTASLVSPDSSALFAKLFTYNETLNAKGQIANGMNDSASETDLDIQPNHKTSNNDQMGYDQSVSADDVPEVDNTIVTEKNVSNLDQESLEKHPILFALTDEGKLKVYNLADFSLLMECDVFDLPPTLFNGMESERTYFNKESSQELVELLVADLGDDFKEPHLFLRSRLNEITVYKAFLYSNTDKHKNLLAFAKVPQETMTREFQANVGTPRDAESTMEKKASSSVDHLKMTALEVVGNHSAVFVTGRKPFLILSTLHSNAKFFPISSNIPILSVAPFHAHHAPQGYIYVDENSFIRICKFQEDFEYDNKWPYKKVSLGKQINGIAYHPTKMVYAVGSAVPIEFKVTDEDGNEPYAITDDNDYLPMANTGSLDLVSPLTWTVIDSYEFQQFEIPLSVALVNLEVSETTKLRKPYIAVGTSITKGEDIAVRGSTYLFEIIDVVPQPGRPETRHKLKLVTREEIKGTVAVVCEVDGYLLSGQGQKVIVRALEDEDHLVGVSFIDLGSYTLSAKCLRNLLLFGDVRQNVTFVGFAEEPYRMTLFSKGQEALNVSAADFLVQGENLYFVVADTSGNLRLLAYDPENPESHSGERLVTRGDFHIGNVITAMTILPKEKKHQNAEYGYDTGDDFSCVMVNSDGGLQMLVPISDRVYRRLNIIQNYLANRVNTIGGLNPKSYRLITSPSNLTNPTRRILDGMLIDYFTYMSVAHRHEMAHKCGVPVSTIMNDLVELDEALSYM O74734 RRF1_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1709.09; CHAIN ?..244; /note="Putative ribosomal recycling factor, mitochondrial"; /id="PRO_0000372618" MFRIISKATLFQDSQRFHTSILSPRCAFHNGGILHKKAKDKDVKHDHDPEFANSFNKMLKSFEAKMQLVHEKLAKRFQEAVVLPSQGNFTQLEALFIPSKSIKAPTPSRLLREIAAVSQKGSQQIIIRPFEDVDIKNILKAIEDSRYPFVANKLNASTIEVKPQRTTLESRQQLAKVLEGYAKDSREQLSAMRTELKKEIAKNKKSKAWTSDDCYKAEAEMQTAFKNAINLLDSGLKSALKKVI O74735 ATX1_SCHPO BINDING 11; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"; BINDING 14; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00280" SPBC1709.10c; CHAIN 1..68; /note="Metal homeostasis factor atx1"; /id="PRO_0000314752" MKYQFNVAMACDGCKNAIDRVLTRLGVEDKSISVEKQEVIVTTDKPYELVEQTIKKTGKEVRSGKVLE O74738 SET10_SCHPO BINDING 234; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" SPBC1709.13c; CHAIN 1..547; /note="Ribosomal lysine N-methyltransferase set10"; /id="PRO_0000303949" MEKLLHEALQNGCKLHKSVEFIQSRDDNACFGSYIAVAQNDIAPDQLLISCPFEYAITYNKAKEELKKLNPNFESCNPHITLCTFLALESLKGIQSKWYGYIEYLPKTFNTPLYFNENDNAFLISTNAYSAAQERLHIWKHEYQEALSLHPSPTERFTFDLYIWSATVFSSRCFSSNLIYKDSESTPILLPLIDSLNHKPKQPILWNSDFQDEKSVQLISQELVAKGNQLFNNYGPKGNEELLMGYGFCLPDNPFDTVTLKVAIHPDLPHKDQKAAILENDCQFQLSNLVFFLPKSPDKEIFQKILQCLAVVTASSLELRKLTAHLLTGDLASYVPSLRGQIKSLEVLLMYIDSRADLLLKSNPQVSPTSERQVWAKIYRDSQINILQDSITYVKNYMEESLQKTYKPLPNLLQYLILNSISIFLLQHPLFAPLSHAIESLYGSTDAEALVATDEQDILMILICVYCLSISEKLPFSISMLVEGYPAVANPEGVEVFEILDEMFFQQFTNVFGESKHFNKENVSWALQLVNDESLDFSGFTFIIAHN O74740 CFT2_SCHPO SPBC1709.15c; CHAIN 1..797; /note="Cleavage factor two protein 2"; /id="PRO_0000339461" MLNYQCLETDSYCGTSHIELDGIHIYIDPGSDDSLKHPEVPEQPDLILLSHSDLAHIGGLVYAYYKYDWKNAYIYATLPTINMGRMTMLDAIKSNYISDMSKADVDAVFDSIIPLRYQQPTLLLGKCSGLTITAYNAGHTLGGTLWSLIKESESVLYAVDWNHSKDKHLNGAALYSNGHILEALNRPNTLITDANNSLVSIPSRKKRDEAFIESVMSSLLKGGTVLLPVDAASRVLELCCILDNHWSASQPPLPFPILFLSPTSTKTIDYAKSMIEWMGDNIVRDFGINENLLEFRNINTITDFSQISHIGPGPKVILATALTLECGFSQRILLDLMSENSNDLILFTQRSRCPQNSLANQFIRYWERASKKKRDIPHPVGLYAEQAVKIKTKEPLEGEELRSYQELEFSKRNKDAEDTALEFRNRTILDEDLSSSSSSEDDDLDLNTEVPHVALGSSAFLMGKSFDLNLRDPAVQALHTKYKMFPYIEKRRRIDEYGEIIKHQDFSMINEPANTLELENDSDDNALSNSNGKRKWSEINDGLQQKKEEEDEDEVPSKIITDEKTIRVSCQVQFIDIEGLHDGRSLKTIIPQVNPRRLVLIHASTEEKEDMKKTCASLSAFTKDVYIPNYGEIINVSIDVNAFSLKLADDLIKNLIWTKVGNCEVSHMLAKVEISKPSEEEDKKEEVEKKDGDKERNEEKKEEKETLPVLNALTLRSDLARAPRAAPLLVGNIRLAYLRKALLDQGISAELKGEGVLLCGGAVAVRKLSGGKISVEGSLSNRFFEIRKLVYDALAVV O74741 DIOXL_SCHPO BINDING 30; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 205; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 263; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC1709.16c; CHAIN 1..297; /note="4,5-DOPA dioxygenase extradiol-like protein"; /id="PRO_0000316041" MASSRLLDWMSRMRSVPQLERLIPALYLAHGSPFLMLPQSSDDEVFSNDSKLGGLHYQFLEQLGPFLLEKFRPKGIIVFSAHYESRGSVEVYSRDDENPLFYDYYGFPDYLYQIKFHSKGSKRIADQIISALKEYQIPAKTVSGDRGLDHGVFVPFKIMFPDGLNIPLIEVSMHTLDPMQLYKVGQALQSLRKEYLIVSGGLNIHTFEDLSAFNEDTAADGYKEFQLDILKAIETDKQNDRLNKLLGLQLHPYFRKAHPREEHFVPLYVAAGLGSSGKSKVVCDLYGAVSAFFGIDE O74748 TR852_SCHPO SPBC1734.07c; CHAIN 1..618; /note="Transport protein particle subunit trs85-2"; /id="PRO_0000343162" MESNLSAKGIFQHASANASGELFQEPVTEDLEKVMQSKGLYSMEELCSIIQEAYAPRVSVLCSRDADEFAMRKGYPKGFWELLYPFGDRIRGKVNRRGMNGEMLTLENLNLHFVPIDALESHLSEASFPSLRSVLCERYPGLVSPEPPSDYSFGVHYKNVERWAWTLAHEGNYQMPLPVYVRQLLTGIPITPFETFSHPVAHLVVVTSHNPSPFESLRSLINSIPYLSLPAFVFNDINYLFVYVHDEDQHDLELSMAIFDTMKQTFGDCGYFLRLHSQKATLDYEHTVPFPTSSWLSAEERLHLLSNTDTEIRLLFESDNESLRRLSSHIAFNGIVSYLDKCVRAWDDQYASPRRGITGKLLFASRKYLSSSNASTNSNYFPSSNAYRPFSPEAYLRKLADYSFMLRDYSHANQIYEIASRQYENDGACLYSAASLEMIVITEHILHLKMPYMSLTNTLRINEYMQSAMLNYLNKSFNSYYHAARCFLLLGQFLSCLPAPKVDDAANWNAGLLYSKRLGPVGRAMIFQQTHTLFKSLSYLKTESTDPFSNKRTRKAALWCVLTADAWLRCRIPFRAKPFVEEAKLFYGKIDWKDLKECVAALDEVEVSKQPASNIPSS O74750 YEA4_SCHPO SPBC1734.09; CHAIN 1..316; /note="UDP-N-acetylglucosamine transporter yea4"; /id="PRO_0000339147" MIASALSFIFGGCCSNAYALEALVREFPSSGILITFSQFILITIEGLIYFLLNDVQSLKHPKVPRKRWFVVVVMFFAINVLNNVALGFDISVPVHIILRSSGPLTTMAVGRILAGKRYSSLQIGSVFILTIGVIIATLGNAKDLHLHVESMTRFGIGFTILVITQILGAIMGLVLENTYRIYGSDWRESLFYTHALSLPFFLFLLRPIRSQWNDLFAIHTKGFLNLPSGVWYLCFNTLAQYFCVRGVNALGAETSALTVSVVLNVRKFVSLCLSLILFENEMGPAVKFGALLVFGSSAVYASARSKPKTNGLKKND O74754 ATPG_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1734.13; CHAIN ?..301; /note="ATP synthase subunit gamma, mitochondrial"; /id="PRO_0000002690" MLRQTLTQASRMRPCISVVGFRGFHASSPCEATLKEIEQRLKSIKNIEKITKTIKTVAQTKLTRAQRAMEASNKYYRVSDEVFKEAGTKAPEEGKTLMVACSSDKGLCGGIHSSISRLIRRELHDPKTFENTSLCILGEKVRTQLLRFCPESFYLTFAHIGGASPSFEEALQISSNILEHAKDYDRIVLVYNKFASAVSFETVMKNLYTTKAINESPNLSAYEVSDEVHQPLMEFAFANAIFSAMAEAHCSEMSSRRNAMENASKSAGDMINKFSIQYNRQRQASITNELIDIVTGANSLA O74755 PST3_SCHPO SPBC1734.16c; CHAIN 1..1154; /note="Paired amphipathic helix protein pst3"; /id="PRO_0000121543" MDVMNVPVDSERDNPGDKVETQSDKNHLPKASPSQSQSPVNTSLHNGDGKDNGVATEPVENKQILSERSVTRDDYEKGKTIVSSLALSSISGKDGSISSQNAEGLSSSSNRPLDVNDALSYLELVKYYFSERREIYNRFLEIMRDFKSQALDTLGVINRVSELFNGYPQLIEGFNTFLPSGYKIEVQLDSSNTSVVRVGTPMHPLPQQGVQSTLPVAPSNEDQRTMESTSPTDSQPQPSAPNLVSSTENEKPRVDFNYAIAYMNKVKARYPPNSDTYMEFLGVLRTYQKAQKSIFEVRARVAEIFKDSPDLLEEFKLFLPDNVDSTEPSTPNVQKSPNRLPPVGNFSLPPSAPVREKRNRPAHSAQISRSISKTSRMYRQTAEEPLNSYSLHVYPQKITAPTSPYAATQEELLAFTTIRQHLPDTLAFHKFLELLHLYREKLLDKTELLNSFSKLVRNDNLTLWFSEFIRWSDNPILVKNEPVDERVYLPETFECISLTYRKLPDSWKQDKCSGRDDLDNSVLNDDYISVAPKPSHVKNIMHHENQYLQALQLVEDERYDYDRVLNTTESAIKILANFCEPTIHEHLETALQELERSKRIIKNALIIVYGKEHANLALDTLFKKLPTAAPVLLKRIKTKDQEWRRSKREWSKIWRQIEKKNAQAAFDDRYCRIEGRDRRGLSYSRILRDIDDIYQRQKHRIDGAKLGFQFTQVLCDSLIFLNILRLSDAQLTNSSFYSYADKGRISAVLKALLSQFFGIPLPREALETNLASENIESVKKHRDGLSKIFIRPESADNSNNTNVSFQTDETQTEDETMSDIHPDDVENHSKSKFLGEESKNIIGYNFFGNATMYVLFRLICVCYSRLEHIKLFVESSTIYASSTGGYENILNICEKYLKGSCSRLEFRKYLQKFNNETCYMICSIERLLKVIFYRIHEILLDPKLGQLLLLFESDGANSVTTPREQMVYRNHVESILAPESKIFNMRWYPLEKRLCIQQLLPADLTMHDFENPAKAFMYYVDSYAISHITEGVDLMQVKMPFLRRSLQRISQQGYLAGRGSGRLHSLFNEHFCKSNLQLFFSTDTYVIFFEPNTENVYINSYNLWVDQSSQSKKQNRTTNWRRWLESDEGWRKSKANTDIKFFSETTLDQCIEAM O74759 NTO1_SCHPO SPBC17D11.04c; CHAIN 1..767; /note="Mst2 complex subunit nto1"; /id="PRO_0000303918" MQTFRLTSTGRNILRPDELAFQPREEIPYKSFHPDLQIDEPLEILEGDHTQYAGLRDSLVTYKSENSYVLKALLNAKIENVKPVGVQTENINPQEKKFGYKTAKQLDWSPDEYFKFVAIHPYSKTSFPVSYDLDELDTMWLTYYNEFQLSSNSEWENVSKEFLEIVLTIIEREWLYLEAWMPKIEPVRVEDELDGRCVICNEAECENSNAIVFCDNCNTSVHQNCYGIPFVPEGQWFCKKCLLAPHEVICCAFCPDRDGAFCTTLDGRWCHTICAIAIPEISFHDTSRLDLVRNIASIPKSRWKLVCCICKLRWGTCVQCSDKNCYAAYHITCARRAGFFYKIYSHSASYDSVDMETYCDKHTPPDYLNGLMKRLFPLAELYYKRMATDVPLNFQATKAPDFVPEGPWKSHPLPAFIVDKVTKVLLSYNVKRQDLPSIVTDICKFYHMKRRSRKDAPLLKSQLLMDSLENLPVRASKDRVRSLEVAKALQDQYQSLLTLVESTAKRQLLKCQLSNLRKKFLNLNYFPAQRLLQDTLVKIIDLDVDGLFNMPLDNGWIGWVELKRQVFSYQIGSISSLEKKLEPIWDVDGVIQCIDDMEQLTAMVQFAQKTEGEVKKLFIKAKIYFESLSLDERGNLKVPSLGINGLEYDNWPGLNELEMSQLDIPSQGNLKSLHDFIEGLDLNEKIGKFPISMFQNQVAQFSTIEIPKMSGRANGMHNFHSEDVTGQSNHALPNSVTKKNGTKQPYTKNSLPFNERITRSKAKKNYS O74762 RPN2_SCHPO MOD_RES 952; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17D11.07c; CHAIN 1..965; /note="26S proteasome regulatory subunit rpn2"; /id="PRO_0000173807" MTMVYSDNTSIITSAGGLMALLDEQERELQVHALLKIYEFIDQLWPEISDDVTKIEVMYEDHSFPERELAALVVSKVYYYLGEYDEALLFALSSGPKFLHDKNSDYKETLIFKCIDMFIHKSAELYKNPKADPLDERLSGVVEGIFQKCYAKNEWRHVLGIAIEAHRLDIIEYILNADKETDLKPYVLELAMTVVLDIEFRNRLLRLLLSSFLTETEPDYFSVGKCVVHLNDASVAAKLLMKLSSQNDDKSLLTAYQLAFDLEDSAPQEFLNSVMDLLPSPSVANSEEDANADSKKEDSSPCGYIIRILSGEQTVKYDREFLYAHNNTDMLILNRTKDSLEARNSVFHNAVTFANAFMNFGTSSDSFFRDNLSWLSKANNWSKFTATAALGVIHRGYYNQAMNILRPYLPEEDAPSSSTYSEGGAFYAMGLIHANHGRGVTEYLREQLKHTEDEIVQYGLLLGIGLTGMASRDETLYESVKTILFNDNAVAGSAAGISMGLIMLGTASSAAIDEMLQYAHETQHEKIIRGLGIGIALIVYGRQQEADGIIKELNNDLDPTLRYAGMFATALAYCGTSNSKIVRDVLHISVSDVNDDVRRAAVCALGFICFKDPNALISTVELLVDSYNPHVRYGSAIALGIACANSGSNAALDLLSRLVEDATDFVRQGAMIAQAMILTQHNDQLNSKVSGIRKHFEQVINEKHEDALAKLGATLAQGIIDAGGRNVTIALQTATGSLKLSAIVGLTVFLQYWYWFPLTHFMSLSFSPTALIGLDKNLNAPKFSFISNVRPKLFAYPPKSVQPTAKTVQKVETAVLSTTVKAQARAKRAEREKASKGSNDDEMKIDKKTTEEKEATPMEMDEEKSQDISINGNSKKEEPKSETLENFTRVVPAQLPYISFNLNGRYYPVRKFTGGVLMLIDRESDKAPDLIELNRDAVPASADTEPGEQEASPPEDFEYPFDDDD O74764 SPB4_SCHPO BINDING 45..52; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P25808}; SPBC24C6.02; CHAIN 1..606; /note="ATP-dependent rRNA helicase spb4"; /id="PRO_0000232332" MSFQSINIDKWLKNAVAAQGFKKMTPVQANAIPLFLKNKDLVVEAVTGSGKTLAYLLPCFDKVTRRDTDETGLGALIVAPTRELATQIFNVTKELLAYQPDSLDGGKKLVADMYIGGKGTLTNDLASFREKNPSVVIGTPGRLNEMLSHISSKHLEILILDEADTLIDMGFQRTLQSIISQLPKQRRTGLFSATMNDTVSSFLKIAGLRNSVRVSVTVTSKKIDTRTPSSLAIQSLVIPPIYKVQCMIHLLCTIEYEKAIVFFSSCASVEYFNSLFLTYKLPFEIVALHGQQVQSNRSRNFEKFKKSNKKTVLFTTDIASRGLDIPNVDFVLQLDPPLDPKSFSHRCGRAGRAGRAGVAIVLLNDGREEEYEELLRVRKVPITRIDTPIEALDLSRLKVLTHELRKIVSKDRDLYDKGLRAFVSHVRAYTKHHASFIFRIKDLDLGQLATAYALLHLPKMPELKDTEISENIFKKFDIDYATIPYRDQVREQARRRRLEVEKTEPKKLARPAKIKNEAWSKQKEVKEKRNTRREKRKSKKEFLKAQKNEASNNLKQEIVSKAGAQETENDDLIDEESDALSELEEDYRQLKKSKKRKNQASFGFSM O74765 SYPM_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215; EC=6.1.1.15; Evidence={ECO:0000250|UniProtKB:P39965}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC24C6.03; CHAIN ?..425; /note="Probable proline--tRNA ligase, mitochondrial"; /id="PRO_0000314630" MLQHLRNRASIEVLGKAIRKYNVPESANQLLIDMGFIQPSMPGIFQYLPLGLRVQNKICDLLHISMRSLGASAISLAHLSSKEIWEKSGRWQKTGSELFRLHDRNDREMCLAPTHEEDVTRTMATIIDSQKQLPIRVYQIGRKFRDELRPRGGLLRGREFMMKDLYTFDIDKASAMKTYEDVLQAYHTFFKEVGLPFVMVKAATGNIGGNLSHEFHYRHPVGEDVIYTCPSCHYSTNSEMLDLSKTSSDISCPNCNDQLTSTTAIEVGHAFYLGKIYSSKFNATVEVKNKQEVLHMGCYGIGVSRLIAAVAHVTKDAKGLVWPSSIAPWKVLVVPTSDNHIQSAETVYDATANVVGFDNVLLEDRQNRAFGYKMRDAELIGYPFVIVVGSRFQEEGICEIIVRSSGERYKLDKDSLHQVLLGNFL O74766 PUT2_SCHPO ACT_SITE 298; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008"; ACT_SITE 332; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008" CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88; MOD_RES 391; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 394; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 396; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC24C6.04; CHAIN 1..548; /note="Probable delta-1-pyrroline-5-carboxylate dehydrogenase"; /id="PRO_0000056502" MSQFAEFKLPAIKNEPPKHYGPNSADREGIVKAYKELEAELPVTIPVIIDGKEVETNTIGEQRCPFEHKKVVARYHRAGAKHVEDAIEAALRGKKVWESLPFADRSAIFLKAAHLISTKYRYKLMAATMIGQGKNIWQAEIDAGMEIIDFLRFNTKYASELYASQPPENTPGVWNRMEYRPLEGFVYAITPFNFTAIAGNLAAAPLLMGNVVLMKPSDHAVLSSYIVYQIFREAGLPAGALQFIPGDAVEVSKVCFNHPEFAGLHFTGSTAVFRSLWGTIGENVANGKYRTYPKIVGETGGKNFHLVHSSAEIKSAVVNAVRAAFEYQGQKCSALSRLYVSKYAWENGFRDELTKQVKSLKVGAPLTDFANFVGPVIHQASFNKLKKVLESAASDSEIEVLAGGKADDSEGFFVEPTVLLSKNPKHDIFVNELFGPVLSVYVYEDDNLDAVCDLIDTTTPYGLTGSIFAQDRVVVRKLTDRLRNAAGNFYINDKCTGAVVGEQPFGGARASGTNDKAGSGMILSRFVSPRSIKDTFAYADSVLYPSNF O74767 COPE_SCHPO MOD_RES 262; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC24C6.05; CHAIN 1..288; /note="Probable coatomer subunit epsilon"; /id="PRO_0000193855" MFSWEASLSNELYFVRQYFYSGNYTKLFEIDTTSMSEKGLELTEIYMARAKLALGESLESIQSILTQKTPGSAAILALAGEGNMELIIDQHGNSDSVVQTLGAIFQIKNGSFDDAMDLLKKSVENLEAVALQVYIHLREHKIEAAEQTLKQALDWADEEIVLQLAQSWIKIVSGGVESYNDAFYVFEELNGTDSNPMTLTGMACADICLLRPEEALSSLKTALDSQPNYEEALSNMTTAITDLGPDAPSQAKNILSSFTNSSTLKLNDHLNEKAQEFDTFSTQFLSTA O74769 BHD1_SCHPO SPBC24C6.08c; CHAIN 1..367; /note="Folliculin-like protein bhd1"; /id="PRO_0000223944" MDVVFALGHFCEAEGPSIIFCTQKLHRSTVSKFFEHPTSKRSIGVTENGNDSPEAFKNELDNRNNADSQSLQSSTESLFKADSEDYLCKKVSKGPESPRVNSFHNSYSRNQSPISRKSSCVTCSTVLPLEFSVPDVQPRLYTNSSTNPDVLYMSSQHPHTQQRYSTLKRLMVRCLSCEYSTLSEASDSMSNPLFFGDQDNGYVISQSFSLRDPSARGGLRRYAIIATCPNQLDLILRYSFISEKFLHIVQFLRISSFNTKNDYSSSRSKTTASSSNGTFASPSFNISSLSGSSNIGTAPSYEISSSIGANVSSLAHTQRLPSFSFLRRRDDIGEGRSLVDITCWDGIFVGLHSSFSWILEVWDLLVV O74772 CWF14_SCHPO SPBC24C6.11; CHAIN 1..146; /note="Pre-mRNA-splicing factor cwf14"; /id="PRO_0000193901" MPRLRTSRTKRPPDGFDEIEPTLIEFQDRMRQIENTMGKGTKTEMLAPIFQLHHQRSRYIYDLYYKREAISTELYNWLLKQNYADGNLIAKWKKPGYEKLCCLRCIQTAESKFGSTCICRVPKSKLDKDQRVRCTHCGCNGCASCD O74775 SIP5_SCHPO MOD_RES 127; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 128; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25B2.03; CHAIN 1..554; /note="Protein sip5"; /id="PRO_0000333442" MGNTIGKERQENDEELIQHLVQLVDGGFLDPQGVYSSAPAYKTNIVRKLMLERRLMPFYKGLDSYSKDWPADKVVEVVEKALGPHKSALLHCAIRQSRSLSVGNTRSLKRDSRGSSDHLLTRNRSNSTPGSISADYRTTAITTIYANAMECPICFLYYPSNFNYTRCCAQPICSECFVEIRRAEPHLPTVHANEPTPNEFDLISEPAKCPYCMTERFGVIYKPNPKLTPFSFNNNPDTLPSNIAPMGTLSKSSLPLHHIPWPPNQHIKFAHDDKNVVSTDFIHPDWQYKLERARRRALRRAANATLLNSHLLETGPANANANHNTDLSHDPTSHGGPRRTLSSRRQHYLANVEQLMLAEAIRQSLLDAQSNDSTNSLPSTEVSQPDSTNISNEQEIVQPQPTHTTNVALVEEINRPDSVESAITASSSIDTGNENETQEVNSDSLPQFVHQTMTQTNFQESSPSVAADETRVHNVDEYIEQQDLDELIHSPIASTNPFLADQFARSETVDLNAHICSPALSVSDDGVTATNKTQSSFPSVYEHQLKSNELERGH O74776 MTG1_SCHPO BINDING 70..73; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 155..160; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 207; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC25B2.04c; CHAIN ?..328; /note="Mitochondrial GTPase 1"; /id="PRO_0000280264" MAFVARQTFEYQMPSTWYPGHMNKTLKRLKNLTSSNDIFVEVRDARIPLTSRNYVMEDFLNKKNRIIVYNKCDLADTFHTKAKVSKHRIQNLAQQFQNVECWFKETSTPEKSAFITPYVSKAPYFAKELLRLIRTLVDQASANGRVYVYFVGMPNTGKSSILNSLRNVALRKSKSAIVGNYPGVTKRISEIVRLFNDMDVYMLDTPGIMTPSITKPEDMLKLSLVGCVKEGIVHPVTVVDYLLFHLNRIDPSLYSKWSLPTNDVDEFLQNTAYKARKLTKGGFDENFVSNYVIQQYRIGRLGRFQLDTIDKNELLIRLHNEQNKKNAK O74777 KRR1_SCHPO SPBC25B2.05; CHAIN 1..327; /note="KRR1 small subunit processome component homolog"; /id="PRO_0000050121" MTEVESSTENNVIVNKNKRYRRDKPWDTDDIDHWKIEPFTKDDSKESFLEESSFATLFPKYREKYLREVWPHVTRALDKFGITCVLDLVEGSMTVKTTRKTFDPYSILDARDLIKLLARSVPFPQAVKIMQDGVACDIIKIGNILRNKERFVKRRQRLIGTNGQTLKALELLTQCYILVQGTTVAVMGGYKGLKEVRRIVEDCMHNIHPIYHIKELMIKRELAKDPTLANESWDRFLPQFKKRNVARRKPAKIRETKEYTPFPPAQPPSKLDLEIESGEYFLKKEEKERKKRAEKKEQQKEKKKEKEKERMKAFIPPEESSKKRKRD O74778 BTB2_SCHPO SPBC25B2.06c; CHAIN 1..284; /note="BTB/POZ domain-containing protein 2"; /id="PRO_0000278358" MSMNSSTEISQEPSIMKPVSSISSFVFNAGFLQGTFSDTTLIIKGETYHLHALFLGRSPVLLQKLIENNPKGDVHYTIEVETEDPYVTKESCLFVLSTLYCDSPRIPAEVNVCSVLAVSDLLGLDTLAFEASSLIEKSIRPETMESVIRFLDPNFEGLERLKMGMYPRFTSGLFNKAIQVMYNTLVSNWNTEYARLLCNLPFEVIKDLLESDKLTVGASSMARYKLANEIVKMRASFRKQNHIEGKGDESVVLAFDEGSRGIQLVHIAPGAESRRKIWKATSVR O74779 MU164_SCHPO SPBC25B2.07c; CHAIN 1..517; /note="Microtubule-associated protein mug164"; /id="PRO_0000225610" MPGSPSQEPLAEAESNMLQRLEQLQMQTSNILKELHSTSIFTDSTTSQLHNGGENSVMDTEESSAIDKLSASLQQVNISSPSVPTSQSRVTQGQSLGNTQISNPTSKTNNVRAKARNIRNPSQRLRPSTSLARLSNNAPRIPKEASLHENSISSKESPSVTTSKHVATITKPSTSSIARMSSNARIAAIPRAKSSMAVRSPSRLGNGPNVRSPKVGFNAKSDDSPVVKSPGSNDKPSASPRISVRSLGNSSVVRPPTRTSTTRPLSRVNVTNASGSISKNSTSPSKVKVNASTKIVRPVSAAQTVRPGSRIFRENSASNTQRPNVSATSNSTVRVASSLAVRPVSRNAQARTPSRLEQREVNVKNSSAKIVRPGTSLGVRSPSRIQSTLSSRTTTGNVRTKAANIVRPSSSINRRPPSSINQRPPSNLRILAPSRSRATIHERPSSSILHRHAHSLTSSSFSTKTLATTKEIQNSPTLVESSTVVHHDPSYLQNQTSEINDTNHSSHSSPLDLNRMI O74781 SYRC_SCHPO BINDING 146..151; /ligand="L-arginine"; /ligand_id="ChEBI:CHEBI:32682"; /evidence="ECO:0000250|UniProtKB:Q05506"; BINDING 160; /ligand="L-arginine"; /ligand_id="ChEBI:CHEBI:32682"; /evidence="ECO:0000250|UniProtKB:Q05506"; BINDING 359; /ligand="L-arginine"; /ligand_id="ChEBI:CHEBI:32682"; /evidence="ECO:0000250|UniProtKB:Q05506"; BINDING 363; /ligand="L-arginine"; /ligand_id="ChEBI:CHEBI:32682"; /evidence="ECO:0000250|UniProtKB:Q05506"; BINDING 387; /ligand="L-arginine"; /ligand_id="ChEBI:CHEBI:32682"; /evidence="ECO:0000250|UniProtKB:Q05506" CATALYTIC ACTIVITY: Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215; EC=6.1.1.19; SPBC25B2.09c; CHAIN 1..618; /note="Probable arginine--tRNA ligase, cytoplasmic"; /id="PRO_0000151663" MATSVDQISKSLSTLGLQDLPVFREADIHHNPVDVYRSYISSELSKINGVDVSLIYPALETSISKDSADLNLPVPRLRVKGKPQELAQKWAEAFPKDLVEVTANGIFLRFNFNGPSLTKLILPIIWEQRENYGRNESGSGKVAVIEFSSPNIAKPFHAGHLRSTIIGSFLANLHESQGWKVHRVNYLGDWGKQFGLLAIGYKKYGDEDQLKSNPIRHLYDVYVKVNADATEEDEKIQKDKAEAESKGLPYTPPLSLHDKAREFFKRMEDGDEESLKVWARFRDLSITKLKDTYDRLNIHYDEYDGESQVSLELMNKMVDELRSLNLIEEDGGALLIDLSKHDKKLGKAIVQKRDGTTLYLTRDIGTAYKRYEKYKFDKSIYVVSSQQDMYFSQLFKIFELMGFDWAKKCVHINYGLVQGMSTRKGKAVFLDDIMEVAKEEMHKVMQKNEEKYAQVENPEEVADIVGKTAIRIQDSTGKRINNYAFDWSRMTSFEGDTGPYLQYAHSRLSSVRRNVNYTDEEIMGANLELLTEPDAYDLVRLLGQYPDVLKNAFRFQETSTVVTYLFKLTHAVSKLYDILWVRGRERDIQLARLALFGAAKQVLNNGMTLLGLTPLERM O74782 YGBA_SCHPO MOD_RES 44; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 48; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 98; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 102; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25B2.10; CHAIN 1..307; /note="Universal stress protein A family protein C25B2.10"; /id="PRO_0000312662" MSESAPAGSKEGVSFGNLPRPEPRTSKDQQKLSISTDVKKPSHSAPVTPVRSARSSMEQPTFRPVAKNSVTVAPARAAGFCPPQFEEYHHGRSHSLVSPPPSPHFLKRISFDTFNNKAATDFSLTLKTQHQAYKWTRTSRTFLCGMDGNSYSEVAVDWLFETLLADNDEAVVLRVIDPSSKLAEDLSDEQSYRSLAEHIMAGILKKVDDDKAVSIIVELVVGKPQDMILRTIHVYSPDSLIVGTRGKALNSFQSLLSSGSVSKFCLQKSPIPVIVVRPDRKRVRSKNKRLKDKTRKSYMEILEKSGR O74783 POF2_SCHPO SPBC25B2.11; CHAIN 1..463; /note="SCF E3 ubiquitin ligase complex F-box protein pof2"; /id="PRO_0000119972" MRVPNEVCFNILSYLEADELRCKSTVCTSWRNFIIPTLWEKVVFQNEAQLNNFFDTLQYSKDVSYYFRYLRKLNCSRVRKFLTDKHLMLMTLATGISRLNLSGCTRISEPLIGKLLYQNLNLVTINFSNIFSLPANILEYISDNCPNLKALNIGNCGLVEDTGMVQIIKRCPYLNRLIIPNCRKLTDVSLQILSEKEDLIELDISGCEGFHNADTLSRLVSRNRGLKELSMDGCTELSHFITFLNLNCELDAMRALSLNNLPDLKDSDIELITCKFSKLNSLFLSKCIGLTDSSLLSLTKLSQSLTTLHLGHCYEITDIGVQCLLKSCKNITYIDFGGCLRLSDIAVSAIAKLPYLQRVGLVKCICLTDLSVILLSGSFSRNLERVHLSYCIGLTAKSVSYLMYNCKTLKHLSVTGINSILCTELRSFSRPIPDGINPSQVPVFCAFTKVEIDLFREFIRNRI O74788 IML1_SCHPO MOD_RES 738; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC26H8.04c; CHAIN 1..1496; /note="Vacuolar membrane-associated protein iml1"; /id="PRO_0000301778" MAITLNLWTHESSLFPNDAVLNYDLVPSAKPGDIFEIRAQNGDEIALQHNHSSTGKLHAKREKEPVYLMPSPLTDDLKRRHPNLQLSVVSHISSLLNIKNREPVVVKICEDKTNLEAEHVVIFFRDQFISRSDMWKLFRELCGKCVYLKQRVSFIGDVPGEIRCIWRKGKKCHSAYISERTKPIFRSESARFLIFIQMSEEMWHFEEDGELNYNKAIDGFLPDLFSFWRDLGTHHLVSIILFTRVEYSHHGPMCVWQPRSQKNSEKGSSIYPQNSFNASIDNEGGPYEDFFKVVVDNVSSRDWQPVLANLKLELAKFRQDVIVRKIKDENGREIEYICGRMTGSQEGNFLEVINMAVFQFQSDYIDRDLSRTGTSIIIVTPGTGLYEVNEKMLHLTSKSLLNTVVGMDIVSLGKVPLFLTPIVRYKNPVKNKKRSQLTSRISSSVSPSNVIPNSLTSSVSNFSVSSFLNNLKEDTEWLYTFPIGCNISFYSTTEMRSLRSPWENLMREHQFEPTAKMHELQMMGVLEAESAKISIPLLQSDPLLKGSVFSEEVQEDYDERQFTGEAAVSANDVLSSSSPRHFSSHTPVNVDKSSYLEMNGHSLSTVISGKESISSFGAKVDDLKSTSKESARQFGKSALTERLQKLAGNSSNVSSSLQTSSSNKSSLLTKKSSFPALLKGFLALPATVTTSANPLGFKSTIQRPIPIKNNEDSDSCKAFSQAPPIATKKPPTFLKPNSPEYAKTVIPKSSTNLENEYQTPWKIIQNPFKLKETTADNDPVSLRWEHLYMKVQDVRKFNWLSMCTPGALPLTFSYFPSEEELNDKFEEYTYTIGIDPEFTQMNQQELLAEMICQRLSRGYQIVVNPAAAVSYSGNPKANKAGTITDFSRSVNNQRNGHLTVGSDAVCLSLGDSQFHRLSCDSVGYNIEVKRYVKKVSGQGKMRYDYNFWSKNECKYVKSNITFSANDSANYNWNYVDQLICGFETYLPDSVKYWRARFVLLPMSTTSTHVFQKYQLLDHADALSDEEFRVEGIYKLSELLYKGKIDPMNDSNNKTPNTSPAELLGIKFTTLPMAQYIHSELEALRLDSSRNEQSLFMPNKRLDCSADLHTIAKEIQGPGGPKIDDITWHYRIYENCFLGSEFVSWLANTFIGINTREEALKYGNKLLSLGLFDHALKKHPLLDGYYVYRISPDYSIKPVSNRPYRSWFSRKKDSGQKHLDNKIITESEAGPSRLELSRRILFNADVEKKNGKSETVTVHYDLLHNPASCYHIRIEWLLATASVIEKLLQSWSRILERYGLKLVEAPIHEIAAVGELNPFDQVSIISLALDPPPIPERAPLVNDPVNYSKNWWNVKILEHFDFILDTEAASTFPKSITAVYSWGKPNFRYVQYIHRTGTVLVQIDDDQRFLWLPNRLHNSKVSKLSFTKSNKSTLNPNLKETAEELERKFREFCSNKDELDQFYGIVNHASDDRRSIYSSASTHASNASADDASNVNV O74792 SNF59_SCHPO SPBC26H8.09c; CHAIN 1..515; /note="SWI/SNF global transcription activator complex subunit snf59"; /id="PRO_0000373987" MEEEDITLEHSDDLNKEESGESNRVNIEEPEHHDNSNKESTNLDDLNMLEEPKYHDNSNKESTNLDDLNMLEEPEHHDNSKKESTNLDDSNMLEEPKHHDNSNKESTNLDDLNMSEEPKHHDSSNKESTNLDNSNMDESENQKNFKIEEPKPSGDFRNEGPKQCDDSKIEKPELHVNSKIEEPIHRIDSEHNEPEYHTESKNEESEHNTKSIREEPIHHVDSKNEEPVYSKIPEKMGDEFSENSLSKSDSAVKQEGNLLIHPNNSLKDTAPSKCKEPPVDEALSKKEISDDIAQITSVTPITEKIEDKDKYISEVIDTYGKLADGFEYRAKTFCLEGRGKVLYMLGTECSRLLGFKDSYFMFHKTPSLRKVLTTQSERDQMVEMGLLASNFRFRQLSIVPARQMFLAFGARILMKGTIDPESHKALIEKNISWADDEYYHMDVMANGSTRSSSVKLELKSMDNQNSPSPFQGKDILTLAQGASFYNSKVMRTRNLRKEARLSYYTKLRGVNRSVS O74794 CCHL_SCHPO CATALYTIC ACTIVITY: Reaction=holo-[cytochrome c] = apo-[cytochrome c] + heme b; Xref=Rhea:RHEA:22648, Rhea:RHEA-COMP:10725, Rhea:RHEA-COMP:10726, ChEBI:CHEBI:29950, ChEBI:CHEBI:60344, ChEBI:CHEBI:83739; EC=4.4.1.17; Evidence={ECO:0000250|UniProtKB:P06182}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650; Evidence={ECO:0000250|UniProtKB:P06182}; SPBC26H8.12; CHAIN 1..377; /note="Putative holocytochrome-c synthase"; /id="PRO_0000121716" MTSSETTTDHPRTGKCPIDHSKFARSNEANPDAYINGIKKDQQSSSWWNSLWSRNTDVASEPDVAMLHKKPSTVDTHDHPLANPPPGCPMHKASNENSTGFFSNLFGREKQNSEATPAVQPPATCPMSNSNQKPAGVSEVLTGVDSKQQSYVPEGCPVATPKRGWFNWFGNNDDQKQEAYEVDKSNMMYKNIPQTAVDDQVVGLETTRTTSSIPKVDGKNWEYPSPQQMYNAMWRKGYRDSGENVPIMVQVHNFLNEGAWSEIKAWEREAGENTEPKLLRFEGNANKRTPRALWYMMLGRINPNRWGSGEGPFDRHDWYVQRKDNSIVRYVIDYYEAPDSADGKPVFSLDVRPAVDSFESVALRWKHWRAMRQMQQQ O74798 ALY2_SCHPO MOD_RES 653; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2D10.04; CHAIN 1..658; /note="Putative arrestin-related trafficking adapter C2D10.04"; /id="PRO_0000303890" MRGELNIPALSRFGKSISASLHHQNGSSRDDNDSNPYENRSSNSGLNRRNSVFGLPSSGLSSRLSKPSLSSINNSNNSSSNTGGNVLPNPALTPVRNMSNKPPLTWSPSSANLFGTSKVTSIIGNNVSDVVPPVIKKALASSHGGGMSLSIVLLEPVLYLAGFDLNECQIENPALLRGALVLRVAKPANIRGISLSFTGRSRTEWPEGIPVKGHDTYEDKVIISHNWKFYEPTMKDADAPQHGADVARLVGEQLPLPSSAAASLRGYSVFAPGEYTYNFDLAIPNCFPESVEAKMGWVRYFLEATVERFGTFKSNLNGRTPVQLVRTPSPASLSSSELINISRDWDERLHYELQVSGKSFRLGEVVPITFRFLLLDKVRLYKLSISVVESSEYWCRSRKFHRVDPKRRVLLAERSAKHQNTDNLFETPDEGDGLSSAVFNFNVALPTCLVKERDRLTFDTTYKYIKVRHRLKALLVLSIENTENPEKRKYFEINIETPVRILSCRCVKDSTLLPPYESSSQGDNQVLLPCPCRLATTHVEPTEVTAFTTQSVLASSAPSAGRPAAAQISRPAQLFRIPSTNPPPFDGDVCPPACNTPPPNYDELFDVLSSISIQDCETDRANDDTILNNRVRRSGTIREEAPHRSLSRTVSRSFEIPR O74802 HIBCH_SCHPO BINDING 141; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 166; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 189; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 197; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888, ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4; Evidence={ECO:0000250|UniProtKB:P28817}; SPBC2D10.09; CHAIN 1..429; /note="Small ribosomal subunit protein mS47"; /id="PRO_0000311721" MGLKLNISNDLKKSGFMLRQSLLKTSVSNFLSLNASSTMSRAFIRNPKFYSTSSNDTVLYESKNGARIFTLNRPKVLNAINVDMIDSILPKLVSLEESNLAKVIILKGNGRSFSSGGDIKAAALSIQDGKLPEVRHAFAQEYRLSHTLATYQKPVVALMNGITMGGGSGLAMHVPFRIACEDTMFAMPETGIGYFTDVAASFFFSRLPGYFGTYLGLTSQIVKGYDCLRTGIATHFVPKHMFPHLEDRLAELNTSDISKINNTILEFAEFASSSPPTFTPDVMDVINKCFCKNDTVDIIRALKEYASNTSALAEFAKSTVKTLYSKSPTSIAVTNRLIKSAAKWSISEAFYYDHIVSYYMLKQPDFVEGVNAQLITKTKNPKWSKSHEYHFKDLENYFKLPSEYNNGISFAAKGRRKTPLWNYKTYPYL O74807 CENPS_SCHPO SPBC2D10.16; CHAIN 1..110; /note="Inner kinetochore subunit mhf1"; /id="PRO_0000304030" MMEEERFKAEIFHVTQEVCNRTASELTESESRNVIVDELFCVGVTEMVWEQIRVLAKDIEAFAEHAGRKTVQPQDVLLCCRRNEGLYEIINNFHKESIKSKKKKKENSTT O74810 UBC1_SCHPO ACT_SITE 89; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPBC2D10.20; CHAIN 1..217; /note="Ubiquitin-conjugating enzyme E2 1"; /id="PRO_0000310742" MSDNRSRRIAKELADVQQDKQAGIQVWTINDDISHLKGMFRGPEGTPYEGGYFVVDIEIPIDYPFRPPKMNFDTKIYHPNVSSQTGAICLDILKDQWSPVYTMKSALISLQSLLCTPEPSNPQDAQVAQVYLQNYQQFVRTAREWTSSYAAAPAGVDLDAENTEFGGIDPNIITNLQQFGFSTELIVRVLQREHIKSQEDLKDYPNGINGILDQLLH O74814 YJ03_SCHPO MOD_RES 372; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC337.03; CHAIN 1..387; /note="UPF0400 protein C337.03"; /id="PRO_0000268706" MALTPDTVSSKLATLNETQESITGIAHWVMFHKRYADEIVQIWLEALYESSSNKKLLLLYLLNEVVQQSRVKKISEYIDAVSPYVVNSVADAYASVPASIKTKIKYVFDVWCQRGIFSKEILLSLQERFNNAENSGHSNYYPVGPPEWAPYTRLMTQTSLYAKSAHSTKTVVDALYKSYLEKQSDYSELLDNYKKQLNKASESCKGNYQACIESRSTLITSLESLIEEQKKLLSEEEESLKSVESIISNLENKESTTATSTLTDAGFGDKSSTAGKHNVETTSPPSSSPNSDDAYSPQVDSYSPSINSVPYTSNIVENPSEDNLSPLPPPASGPYSQEEEETSLFKSQRKEENEEESKELPEDSDIYGKDSSPSSDDSSAAGLYGDS O74815 PPK27_SCHPO ACT_SITE 231; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 108..116; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 133; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPBC337.04; CHAIN 1..413; /note="Serine/threonine-protein kinase ppk27"; /id="PRO_0000256825" MSEKKHSCEEKSLQLYPLSNKIRHVNPNISALPSETDISESLTNDLTKLEISNYAPFNRDLETFSDLIFGLTNIQKKSLYSLQLGRSRGYALYSDENEKYLWSINTKITSTEQREVLLVKSNNKKFDTSIVLKHTHLSSKSQNEKKARVKVFRQEIWALKTLSHPCVVQLLNYYVSSAELILVENYCMGGDLYHYTKKHHSDFSLEFVGRIFSELVHTVAYLHSKCLIHRDLKLENILLTQPYNVIKTIDNWKNYPNALIQISDFELSIFVDSKNHLVQSSCGSQEYAPPEVYMGIAHDGFRADAWSLGIVLFALLEGRLPFDSYPTLDPENVRIKRYVQRLVRCDYTWHLCKSPFKRSTGNTNDNDDPSWRFRLFVKKLLKNRDQRSTPTELLKDFNKHGNFTLPLLENVTI O74818 ECM14_SCHPO BINDING 248..251; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00730"; BINDING 248; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"; BINDING 251; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"; BINDING 323..324; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00730"; BINDING 377; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"; BINDING 378..379; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P00730" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; SIGNAL 1..28; /evidence="ECO:0000255" SPBC337.07c; PROPEP 29..148; /evidence="ECO:0000250|UniProtKB:P38836"; /id="PRO_0000453256" CHAIN 149..497; /note="Inactive metallocarboxypeptidase ecm14"; /id="PRO_0000310336" DISULFID 317..337; /evidence="ECO:0000250|UniProtKB:P15085" MAYNKSLKSLVFILLASQIVFVLFLCYGKSSRELGVKWNSDIRSWMTSYVGFNGETAAISEEQLIWAEKIPDYNEEIVVRLHLEEENNLSDILQKAQSQNLDIWDYNFDHVDLRLKEENFDFWKSQYRSDILINNLTETLFESIVPDTTNSPFSTEAFLQAVENGHLNHEMFTSFTDIFFKSYQNLESINSWLRLMASLYKDLSELVPVGITAEGRTILGLKLNGRHPSDNGEKIRNKKVIIIQGGSHAREWIGIPSVCYAAWQLLAKYDSDGHVRKLLDKFEWIFIPVLNVDGYEYTWSNDRLWSKNRQPLNNSECFGINLDANWAFGFNGNIDPCSNEYGGLSPFQANETMALFNLITESLSQEQKKVVGFLDVHSYSQSVLWPYAYTCDLFPPDTENFEELAIGLVKELHRVNSRYYTYQQACIPYDGFHKHYLPGTAIDWVYFAADVAWPFNIRLRDMGDYGYLLPAKQIVPTAKEFFAMILYYGEFIAEYAF O74820 ERG28_SCHPO SPBC337.09; CHAIN 1..136; /note="Ergosterol biosynthetic protein 28"; /id="PRO_0000193907" MSQILAMLPDSLVAKWNVVVSVAALFNTVQSFLTPKLTKRVYSNTNEVNGLQGRTFGIWTLLSAIVRFYCAYHITNPDVYFLCQCTYYLACFHFLSEWLLFRTTNLGPGLLSPIVVSTVSIWFMAKEKASILGIAA O74821 DRE2_SCHPO BINDING 185; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 196; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 199; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 201; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 244; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 247; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 255; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115"; BINDING 258; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255|HAMAP-Rule:MF_03115" COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|HAMAP-Rule:MF_03115}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03115}; SPBC337.10c; CHAIN 1..288; /note="Fe-S cluster assembly protein dre2"; /id="PRO_0000324871" MSSSVLVLTSPGFASKEESLKKVFDLIDNGASRELQMIDRVQSQLVNLPINRYDSVIAAIDDGAWSSTLGPILSQAFASVHPGGTLRVYSTADEADESFEMTALLSGWLIESKSPWILSRPNQVEAVPIKLSNKNGQSASKNKILDFLKSDKENLISGDDDQELIDEDELLDESAHDNVLKVPECKPEPGKKKRACKNCTCGLREMEEHESSKTSAQLEAVKLTDTTEVDFTEKLKSKNAVSSCGNCYLGDAFRCSGCPYIGMPAFNPGDTVILAENRDKMSWMADDI O74823 YBJC_SCHPO SPBC337.12; CHAIN 1..376; /note="Zinc finger CCCH domain-containing protein C337.12"; /id="PRO_0000314103" MNEQQLLENIASLAGAINQYKNEKEPTQVLDAAKANKNTRSYPYSVSRNYSFILNKSNRSKSTAASPPYVIPSTSSNADDANKEPEKQSTSDYVSRKNRHMQLIKKNILEHDLQARKANLESYRAKLEKEYKTLAENKIQQRLSDGTKQLVTIDGLQYITGVSDTKWLEFVSAKGQCPKYLYWNNKSYLLKKKRFLKEVGNSPSAVYCRYYNANGICGKGAACRFVHEPTRKTICPKFLNGRCNKAEDCNLSHELDPRRIPACRYFLLGKCNNPNCRYVHIHYSENAPICFEFAKYGFCELGTSCKNQHILQCTDYAMFGSCNNPQCSLYHGAVSADVPEQTEAPISKTAGSINPEDSGSEIGSNSLESNLDFISV O74825 RPB4_SCHPO SPBC337.14; CHAIN 1..135; /note="DNA-directed RNA polymerase II subunit rpb4"; /id="PRO_0000073983" MPRAIFEEDAAQLKLGPEFENEDMLTVSEAKILIETVLAQRARETNGEIPMTDVMKKTVAYFNVFARFKTAEATYACERILGNRFHKFERAQLGTLCCEDAEEARTLIPSLANKIDDQNLQGILDELSTLRKFQD O74828 ESF1_SCHPO MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 121; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 506; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1734.01c; CHAIN 1..682; /note="Pre-rRNA-processing protein esf1"; /id="PRO_0000352844" MGKKQTKPINAKSRSESNVVADPRFQSVHSDPRFSRLKRGNFKVKVDERFKSLKEDKDFKTTASVDRYGRPLNQDKATKEIDRLYELENEGSSSSSESSEITDNEEVASASSKSTKSEELTDEESEDEEVYDPARGEGIISTSESSDESDAESETEAQPEISELAGIEPEENIPRGSETNRLAVVNMDWDNLQAVDLFVALSSFCPPGGKLLKVSIYPSEFGKSRMAAEHVQGPPRDIFTPADNQPSSAELHEAQKFGFDNNESDQDEEDALIEEDLGNEFDMVKLRQYQLERLRYYYAVVECDSVRTAKVIYETCDGAEYETSANIYDLRFIPDDVTFDDDESREVCTKAPEKYEPRDFVTDALQHSKVKLSWDAEDPHRKDLIKKAFTSQDIEDLDFSAYIASSESEDEDVDVIRSRYQKLLSGDADDFQANSNPFEDDDKLEGANGEMEVTFTSGFDVDNNANSSEKDETTIEKYKRKAAERKQRRKELRQLKKTKDDEGEGSDVDLGFDDPFFKDKDASRNNKKNKKGKHTQIEDPTAASKEELENLVREDENDSEQLDHFDMKSILKAEKFKKNRKLKKKASNLEGLQEGFEADVSDPRFAALYTNHNFALDPTNPHFKRTKTVEKIMDESRKRRSNQLEQTQDGKPELKIKKRKAEKGDQRQELDRIVKSIKRSGK O74829 YN2F_SCHPO MOD_RES 31; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC530.15c; CHAIN 1..516; /note="Uncharacterized MFS-type transporter C530.15c"; /id="PRO_0000084888" MAERTSESSSESASFDLEKQQSNHHDRYQSSVSSELEESLKKYPVISNPQDFIVTLDGPDDPDLAVNWPLAKKLRNVAVMGSACLCAGFGSSIFSGAVPEVMVKFHVCRTVALLGISLYVLGFASGPVVWAPMCELFGRRRPMIIAVFIFCIFHIAVATAKDIQTVMICRFFCGFFGSSPITTVAGSFSDMFSARTRGLVIAVYSAIIFNGPLMSPIVGGFIGKSYLGWRWTSYITAIMGFTAFTSMIIFHRETYTRTITEIRASKVRVLTGNYCLHAKSEEEPLEFSYFFHKYFTFPLRLLIFEPILLVVSTYTAFVYGILYGLLEAYPVIFGESRKWRLGVESLPYLAIFVGVCIGCSSVALFQPYYFKKMDENKGRPVPEARLPSMMIGCIVFPIGIFWLAWTGNYPWIHWIVPTLAGSFIGFGIITIFQQTINYIIDCYSGCSASAIAANTLLRSSFGAAFPLFTTQMFNNLGIGWAGSLVGFVAVGLIPVPFMLFLYGPKLRQMSKHCLKD O74831 FRDA_SCHPO CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; TRANSIT 1..?; /note="Mitochondrion" SPCC1183.03c; CHAIN ?..158; /note="Frataxin homolog, mitochondrial"; /id="PRO_0000010134" MQSLRAAFRRRTPIFLKPYEFSTNVFGLRCRYYSQVRHNGALTDLEYHRVADDTLDVLNDTFEDLLEEVGKKDYDIQYANGVITLMLGEKGTYVINKQPPAHQIWLSSPVSGPKHYEYSLKSKTWCSTRDEGTLLGILSSEFSKWFSRPIEFKKSEDF O74832 PT127_SCHPO TRANSIT 1..12; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1183.04c; CHAIN 13..524; /note="mRNA degradation protein pet127, mitochondrial"; /id="PRO_0000352804" MLIYKKKNFGRRSVYNLKKCLHKGFQINSCNIKAADNVLHSKASAFEKVNVVDKESIGNLQHHLDTVLPKKKFQFLRDPKTNDYKWDEYLSKILPVDKFNFGLLSKFRPPSEDEQLQKVANSIGAEFVGSTSSLTGLMSQLHFFISKWKFPNFSDLSKGFYISPNERNFTRLCRSASSVHISYQNGLYCIDKDKSLTKEPSVNIILMNVGKSLETFFTVDKDQFLLYKKPPSSNGVLKPLKDVFQYGRCSSLLVRSQLDCYDKKIPESGVFDLKTRAVFGVRMNQTQPELFKSYKLTHYYGNRISFEREYFDLIRSAFMKYSLQARLGYMQGVFVAYHNTSDIFGFQYIPLVAMDRAIHGSSEIGEAEFNLNLQLLEKILQYATSIFPKRSFRVMLSTTEDVPNPPLKVYLEVADDKENRGFDLLDGQKNLEAKTVSPSNFCALEVCALQFVNGVHKSVVKHLDEKETWSIKYHFRKPRDQDNLLRNYIRLRDDIKRRESKISNPPESLLHDYYACSEQYYKRN O74835 RRP5_SCHPO MOD_RES 1391; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1394; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1684; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1686; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1183.07; CHAIN 1..1690; /note="rRNA biogenesis protein rrp5"; /id="PRO_0000314629" MAGNKRKRSNASEGSDSQGNERISSLSANEATQDFPRGGASSLTPLEYKEAVLEAKKDFMESASGTAELSKKTRPKKKGSKKSSKSELDNEENLKVHIQSLRYKNITPGSLILGQIAQINTLDLAVSLPNCLTGYVPITNISDKLSDRLDSIDNHAEDNAATEEEDGLNQIPDLMDLYKVGQWVRVSVTALGSENTTKTGKRHIELSLKPQDANGSAPEAADFVAGSMIQAVVSSIEDHGIVFDIGINNYTGFLSKKHINDFPFVEGQSLLCSVISKEDRIFHLSLTATSTKALEVMPSVQAILPGDYINVLVTDIKESGVIAKYMGVVDVTSDIYHSSPVKGEDLEDKFQLAKSVPARVLFVIPGDPPKIAVSFLPHVLTFNFATPNTPHPDQLDIGFIVNAAKVTYVSSSLGVFCDVGVPEISGFAHISRLSDKKVAGISPNSGPYKVDSTHEARIINYSYVDNLYILSFQQSVLNQQFLRIEDIEVGQFVDGTIAKLIPQGIVVTISEGINGLVPSTHMADIALQFPERRFKVGSSVKCRVLSTNVLRKRVLLTLKKSLLNTDLPLIYDYEQATPGTQTVGTLARIFEDGAIVEFYNSVRAFLPVSEMSEAYIRDAREHFKVGQTLSVTIVSCDPENRKMRVGCREQSWDAKRLERFENIKAGSVLSGIVLQKTEDSVIVDLGDKVTGVITLGQLCDGDLNKCSKVMNKLRASTKLAEVLVLRKDTSKKLISLSLKKSLVEAAKENRMPINITDLKEGIKYFGFVRNATTFGVFVEFCDGLVALVPKAYISEEYVPVPSAVYKPQQSVTCVCLSVELSQEKAFMSFKPLAQKQEKAVEFMESKYDIDNPVDETIKKTYDYVAGKITWAVVTSAKASQLNVDLAANVHGRVDVSEVFDNFGEIVDPNKPLKRFHKGDKIRVRVLGIHDSRNHKFLPISHRVSPKQFLELSVRPSILNMEPFSMKEPQFKKGDEVTGFVNNVSKECVWVSLTPSVNGRIPILDLTTDVKELNSLQKHFFLGKAIKCYVVNAEDSITLSAIGPLQGFENLTPGSRLVGKVTNVNEAGAILQLPGHMSGRVSRIDMFDDYDILPETKFTRNNLVGVCVLSVDVPNRKVALSARNSRTQSQPVEIKDKEINSVDDLKIGDICRGFVCNVANQGLFVTIGHNLIARVKIGELFDTFIKDWKPHFHVNQLVKGSIVGIDNDSKRIEMSLKQSKIKDSSEITKTFADIAVGSNLDGTVVKVGDYGVLIRIDGTDNIVGLCHKSEIADAVVLNISKLYSSGDKVRAHVLDVDSEKRRIALGLKSSYFDSDSDISMSDNEEDVEMRSEDQSDTSESEVGSKDDVQSEEVENLESAGDEDEEEEPSALQANGFDWTDGSTVFDKLADDTEDSEDEEDEEPKRKKSKSDRFDDEEKDLDEIPSTAADFERQLLSSPNSSLLWISYMAYHLNLNELQEAREVGKRALSTINYREEDEKLNVWMALLNLEVAYGTEDSLKEVFKEACAYCDALIVYEKLCGILIKGGKVDLADEYMQLMLKNFKQVPSVWIQYATFLLNNDKAEKAHGLLERSLQSLPKSEHVGIIEKFAILEFKNGDPERGRTIFEGLLSSYPKRLDLWNVLIDMEMKQDDPSIVRRLFQRLLALNLSTKKAKFAFKKWLAYEKNIGDDEGAEQVKRRAIEYVSESHSEN O74836 RL1B_SCHPO MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1183.08c; CHAIN 1..216; /note="Large ribosomal subunit protein uL1B"; /id="PRO_0000125841" MSKVSVASVRSNVEQILKGSEEKKRNFTETVELQIGLKNYDPQRDKRFSGTIKLPNVPRPNMAICILGDAHDLDRAKHGGVDAMSVDDLKKLNKNKKLVKKLAKKYDAFIASEVLIKQIPRLLGPGLSKAGKFPSPVSHADDLYGKITEVKSTIKFQLKKVLCLGVAVGHVEMSEEQLIANIMLAVNFLVSLLKKGWQNIGSLVVKSTMGKPHRLY O74837 PMP31_SCHPO MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1183.09c; CHAIN 1..109; /note="Plasma membrane proteolipid 31"; /id="PRO_0000193985" MSNVTLSDFLLIVLSFFVPFIVVGIRRGFCTADFLINICLCALGIPGIIHAIYIVIKYPRTVRLDIENSPNDPLVRYTPNPEHAVSPHSGPAPPSYSSLASNDNKHQSP O74841 FAD1_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2; SPCC1235.04c; CHAIN 1..265; /note="Probable FAD synthase"; /id="PRO_0000100690" MDELERVYQSIKNIFTHSAPSEKLVGLQNRLSISLRFIEYAFETYQPERLAMSFNGGKDCLVLFLLCIYYLKEKYKEQAQAKLSNIPFVFVRPRDEFPEMDDFVNECQSKYRLNIIKISLPMKEAFCKFLKEHKHIQAILIGIRRLDPHGLHRIAFEVTDKGWPKFMRIQPILDWSYTEIWDLLLETNTKYCSLYDRGYTSLGGVSDTSPNPALKNPDGTYSPAYLLSDGSLERAGRNNTVPFSRTNSRFLYDSGASSYASSEVS O74857 RPC4_SCHPO SPCC18.07; CHAIN 1..330; /note="DNA-directed RNA polymerase III subunit rpc4"; /id="PRO_0000351044" MRKFTPKFVPRRKNGPVEEKDVDERVKIEFDVESQKKWKASRPKPEIKLTASGPFALGPNASSSGTGRPIGSVYVPPPNVKNEEKDDALSKLAASSGHDEGHDEDMVDILKLRELNGQEQGKTDIGGKDLLVPIITDRMLPESNDEKLKHHAESAIHTTVINKEDEEQERVALDLQSLAQHLGLTEQEGMEDHFKDQMVLMQFPDKLPRFMGDADVDPVWPSSEVKEEEAGEKTDVEEKKDPDKHGRENGNIDDLTSLPYPAFHPPAGQIGVLRVHQSGKTTLEMGGVNFVVQSGSDCLFLQEIAVVDYDSKRIWNLGSFERRMIVSPDF O74858 SYKM_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000305" SPCC18.08; CHAIN 19..531; /note="Lysine--tRNA ligase, mitochondrial"; /id="PRO_0000315954" MISRGLLSKGILSIIKRKNTGNLIPHVYYSEYHADIEERRKALGRLGISLYPSVTSDASTTTIPVIIEKWRNKITKSEIAMVRYTVCGRISSIRYSGSKLAFFDVLYGNKKLQVVFNKKNIGTEEEMKGKFIPRLKALQKGDCIQCSGNVGRSGSGELSIYATELPKLLSPCLHPIPVKLTNYEKRFEKRFVDMMSNTKSLELLEKRYRIIESIRKFFSERGFLEVETPILSHHFGGATARPFITSDIHKLPLTLRCAPELWLKQLVIGGMNRVFELGKNFRNEGIDATHNPEFTSCEAYCAYLNLEGMKKLTEELIRFICLTINGNLQISGQTVDLEKGFEVIEFIPALQKELNVELSPLDNSENCRKQLISIFKRCEIMLPKTCTVAHLLDKLFDSLVLKYNTSSPKFVINHPEVMSPLAKSDIKLYGAVEQRISKRFELYIGGYEICNAYEEENDPVAQYHKFQAQKYDRLQLGDDETPAPDSDFVHALEYGLPPTAGWGMGVDRLVMLMTGQSKISEILPFGSLRYV O74860 YQ9A_SCHPO BINDING 19; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 130; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 189..190; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 218..230; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 231; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; SPCC18.10; CHAIN 1..340; /note="Putative pyridoxal kinase C18.10"; /id="PRO_0000339163" MTFPNVKFIGNKRVLSIQSSVSHGYVGNRSATFPLQLHEWEVDVVPTVHFSNHLGYGATRGSACIPEEVHDLLNALLQDNGIVYDAILTGFVPNHDIIQVIFDCVLAYKKDHPKVLWLLDPVMGDQGKMYVDTNVISTYKAMIPHAFAITPNAFEVEILTDIVIHTQMDAKRGLEKIYQLYGIQNAIITSFEVEESPGTLFCMGYSCEHGKPQLFLYQFPSLSGVFTGTGDLFSGLLLAKYREELDKRKHQQSDETKQTKRPTVLACAVGQVLSCMHTVLVNTKTYADEILLEDPKIASDEFLLSNARELRLIQSRTALLSKKSIYEAEFLPGFEEGEDV O74862 UTP23_SCHPO SPCC18.12c; CHAIN 1..260; /note="rRNA-processing protein utp23"; /id="PRO_0000339874" MRQKRAKNYRKLMHTYQLLFGFREPYQVLVDADFLKDLSQQKIDIQAALARTVQGAIKPMITQCCIRQLYSKSDELKQEIRIAKSFERRRCGHIDEALSPSECIQSVVNINGRNKHRYVVATQDPELRQALRSVPGVPLIYMKRSVVILEPASRATLLEKHNKESVQMGMSKEEKLLLSGKKRSANELAIDDQDTKESTDLAGTEDSAPKANKKRKGPKGPNPLSIKKRSSKNHTTDEPTLPVNIIGDVGERKKHRRKRK O74863 TRM82_SCHPO MOD_RES 413; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC18.13; CHAIN 1..421; /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit trm82"; /id="PRO_0000051294" MSEQRVFKHPCQFLTWNSKHNYIVCCSGPYLLGFSCSTGEKIFEHCYRDNINEKHREAAAYGEAIRQVAFSKDYSRMATVSEDKCLRLWDSTQPDKIELLYQKNIPKRCADLCFAGSNEIVFGDKFGDVYCVDENWFTTSEVTEEKKSNVVEGKQEPVNNDTLKDSKLQKLEPIMGHVSILTQLIVAQNPQNSKEEIIITSDKDEHIRISRFPNAFVIEGFCLGHEDFVSRMSLYDNRTLISGGGDNHVFVWDLENFKCLDAFDLRSAFSTYLSLNQPMVVSVILPIFKRQLVAFACEGMAGLIFAKVTPEKRLLFHSALKLSGPVLDAVLLDTDTDQILISLDSSFTFGACFECVKFDEGNAAVLTKPDVIKRIESDGLISTEKPFCPLAQIHTLRKNHSKFIRSVETGTSSPSVESKDN O74864 RLA0_SCHPO PTM: Phosphorylated. {ECO:0000250}. MOD_RES 302; /note="Phosphoserine; by CK1"; /evidence="ECO:0000255" SPCC18.14c; CHAIN 1..312; /note="Large ribosomal subunit protein uL10"; /id="PRO_0000154785" MAISKESKAQYFEKLRSLFEKYNSLFVVNIDNVSSQQMHTVRKQLRGTAELIMGKNTMIRRAMRGIINDMPELERLLPVVRGNVGFVFTNADLKEVRETIIANVIAAPARPNAIAPLDVFVPAGNTGMEPGKTSFFQALGIPTKITRGTIEITSDVHLVSKDAKVGPSEATLLNMLNISPFTYGMDVLTIYDQGNVFSPEILDVSEEDLIGHLLSAASIITAISLGANYPTILSVMHSVVNAYKNLVAVSLATEYTFEGTEQTKAFLADPSAFVVAAAPAAAAGGEAEAPAAEAAAEEEEESDEDMGFGLFD O74865 DPH7_SCHPO CATALYTIC ACTIVITY: Reaction=diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + H(+) + methanol; Xref=Rhea:RHEA:42656, Rhea:RHEA-COMP:10172, Rhea:RHEA-COMP:10173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:79005, ChEBI:CHEBI:82696; EC=3.1.1.97; Evidence={ECO:0000250|UniProtKB:P38332}; SPCC18.15; CHAIN 1..326; /note="Diphthine methyltransferase"; /id="PRO_0000372416" MSETGIIPKSTDYTDWPADVCKYSQVFEDVLVVGTYMLDESTKLRHGKLVLYDTKEDVLKRVFDMHCDAILDFKWSPHDASVLAVAHSTGHVSFYRHQFRAELMFLRGIKVADSSVLMLSLDFSDSGKELAVSMSNGSVLIIDIDSGVIKNKWKEHDYEAWTCHYSRQDNNLLYSGGDDAALVCYDQRIPNSCIWRDIQVHHSGVVSILSRAPFGPYIATGEYGDFMHTLDTRNIGKPLFSANLGGGVWRLEHMETTENYHKVLGILMHRGAQVLRISNDFSSIDASKRIFKEHESMCYGGDWRHTDGLLATCSFYDKRVCLWEDI O74869 NIC1_SCHPO SPCC1884.02; CHAIN 1..408; /note="High-affinity nickel transport protein nic1"; /id="PRO_0000194003" MNSMSEYVKPRKNEFLRKFENFYFEIPFLSKLPPKVSVPIFSLISVNIVVWIVAAIVISLVNRSLFLSVLLSWTLGLRHALDADHITAIDNLTRRLLSTDKPMSTVGTWFSIGHSTVVLITCIVVAATSSKFADRWNNFQTIGGIIGTSVSMGLLLLLAIGNTVLLVRLSYWLWMYRKSGVTKDEGVTGFLARKMQRLFRLVDSPWKIYVLGFVFGLGFDTSTEVSLLGIATLQALKGTSIWAILLFPIVFLVGMCLVDTTDGALMYYAYSYSSGETNPYFSRLYYSIILTFVSVIAAFTIGIIQMLMLIISVHPMESTFWNGLNRLSDNYEIVGGCICGAFVLAGLFGISMHNYFKKKFTPPVQVGNDREDEVLEKNKELENVSKNSISVQISESEKVSYDTVDSKV O74873 SC231_SCHPO BINDING 56; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 60; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" SPCC31H12.07; CHAIN 1..759; /note="Protein transport protein sec23-1"; /id="PRO_0000295471" MNFEEIEERDGVRFTWNVFPSTRIESSRTIVPIASIYKPLNERPDLPPVLYEPVTCKAPCKAVLNPYCHIDTRAKFWICPFCLQRNMLPPQYKDISNTSLPIELLPEYSTIEYTLPRPPQLTPVFLFVVDVCQDEENLQALKDSLIISLSLLPPECLVGLVTFGTMVDVYELGYTECSKSYVFRGSKDYTSKQIQEMLGLPTSNVSPVALQQARSFQGSAAPSRFLLPIQQCEFQLTNILEQLQPDSWPVANDRRPQRCTGTALNISVSMMESVCPNSGGHIMLFAGGPSTVGPGTVVSTELREPIRSHHDIERDQAKHVKKALRFYEGLTKRVSANGHAVDILAGCLDQIGIMEMKSLASSTGGYLVLSDSFTTSIFKQSFQRIFGRDSLNNMLLGFNATMEVLTTKELKISGLIGHAVSLNKKSQNVGDIEIGLGNTNSWKMCGISPKSTYAIYFEVATQSASAPQGDSRGLVQYLTLYQHSSNTFRLRVTTVARAFADGGSPLIVNSFDQEAAAVAMARIAAFKAEVDDGPDVLRWTDRMLIKLCQKFAEYRKDDPSSFRLSSQFTLYPQFMYYLRRSPFLQVFNNSPDETAFYRHMLNHEDVNNSLIMIQPTLQSFSFEHPGGVPVLLDAVSVKPDVILLLDTFFHILIFHGDTIAQWRNAGYQNQPEYQNLKELLEAPRVEAAELLIDRFPIPRFIVCDQGGSQARFLLSRLNPSETHNTTSMYGAPPAHAILTDDVSLQTFMSHLKKLAVAVS O74875 YJ83_SCHPO BINDING 104; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"; BINDING 127; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" MOD_RES 68; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC330.03c; CHAIN 1..145; /note="Uncharacterized heme-binding protein C330.03c"; /id="PRO_0000310346" MLSIFKNLLGTSEEDGTTQEANSKDTKGLKEERKRKKRKNKYKIPPGHTQQDWDALVASGKNLSGVESPISVTAEELAKHCSPDDCWMAIRGKVYNVTAYLPYHPVGPKKILKHSGVDATKPYLKHHDWVNEEELLKTSFVGYLV O74879 NOL10_SCHPO MOD_RES 531; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC330.09; CHAIN 1..634; /note="Ribosome biogenesis protein enp2 homolog"; /id="PRO_0000337683" MSLKVQNPNNVRVYTVSGEGVTQRLPNWISKRKLKKDYALSHRIELLQDFEYPEASNRIKCTRDGKYAMATGVYKPHIKVFDFAEMSLKFERHTDAENVQFEILSDDWTKSVHLQTDRTVDFHSQGGIHYSTRIPKYGRDLKYHYPNCDLYLAAAGDEVYRLNLEQGRFLNPLKIESAQIDSPTGGVNVIDINPMHQLLAFGTDAGSVEFWDPRDRSRVGILEIPSTVPSTPYSDNSRSVTALKYRNDGLNVAIGLSDGATLLYDLRSSSPYMSKDQGYSMPIKSLHWMDSALDGTARVLSADSKIIKIWEKDTGKPFSSIEPTVELNDVCPIEGTGLILTANEGSPMHAFYIPSLNPAPRWCSFLDNITEEMEENPAPTIYDDYKFVTKKELLNLGLDHLVGTGVIRAYMHGFFIDNNLYEKARLIANPFSYEEHRQKIVKERLEKQRASKIRSQNRPKVNAGLASRLSYQENKLRKKTGVTDGPSILEDERFKNVFTDKEFEVDEDTLEYKQLHPSRSEARGLTAAEESEEEKEHTKGIKFSSDEESLSDMEEENETFDALVDRRKTEQQVSNEKTPQETIRSTPSGMEMTFKVEKKKKSKPVNRDEDSTSGKKKQVTQGRRSASKNVFRNM O74881 BTB1_SCHPO SPCC330.11; CHAIN 1..1347; /note="BTB/POZ domain-containing protein 1"; /id="PRO_0000278357" MSHLLFAYYLCNDIRSFQNLLKQDDSKVKEPRKGFSEKSGQKLRINQKDRYGRTVLHIAVSENKNSFVRSLLQHKGIDVFVQDEESGYTALHRAIYVGNLEAASLLLSKDPSFRSLRIKDKEGLSPFQFLSRVLSSTIHPVLDLPIIGNELYGFGTNVNNTLGIANGKEPSSPERVFLLKNQTESPTSGQLFSRDKILDVQASKFHSVVLTDEPSQNVYVCGIGAGGRIGFNTDVQYNFIPIPGIIHKVIQISVSHTHSLALTKFGSIYSWGKNGSGELGLSNDELKKDDPIQITPRRISAFKDYQIIGMAAGKSYSVAWTDTDIYSWGLNNGQLGISDHISVVSTPRRVAGLLSPVIHAVCTTRATICLLQNNSIIAFCNYNQVKLPFNVDFGSSLKVTKHPLSLTRFNVRKLLASENKLAVLTELGEVYEFDMKLLLDRDSTSSKNSTRTSFKFTPLWIFESSDLAALDIAWTADNSLILCTRNGTCWKRELRSKKREKSSSSPYSRGPYKYNRIENLQMVVGVRASASGSFFAIRNDYLPPPIYKPSNMLIDLLRSLLPYDHLLHVRQPRLIPPEDEDGVPIFDEDRAASSNEMQLLFEGSIPILTSYENYKQSFSDVTIYCGTSMFHSHKFILCARSSFLRKLLLQKKKSSVSNIIYIEEITQSHSTIRVEDIPPLAVAILLHYLYTDTLLSPWHLDSRFSPLKENLSKLANLLELPHLAEVLPFSVSRQPLLSLTNDILQLYNNFYVLCEETMDTVIKLKDGELKAHGLFLSLRSEYFSSYFQFVSMESNSFDIPITVNLSHLTVEHMSIVLRHVYSDLKVELFDDLKESDFHNWLETMFEILSIADELLFLELKSIAQQSLLRFLNLKTLPTLMDLSLSYHAEELYSRCIDYACHNIEFFLEANRISEWDGFHLKKVAQRLTELLSDQRVHLPSSKIANRLLIRDPVLMEKRNYELKVLREYLFSQESSQLWDDSPYRSIFEDRRCSTSAVILESGIVPSSNQSDSLNKEDAEEKSPKPNVVNVTSITKTAGASVEIQNNIESASSGGDKTQLNGPGADQPVTATITFDKTSPWRNRENLSHNNNTTRASLRELLEQEKADASTTTVLSDSRFMKAPTKKSQREKKKELSKQVPISKTNVGHIDIELGKSNHSNPWSVATHQRGSFSSSTGVKKSFNGILREAAREEGSSQVIYQESKKRISNGSPTSWNLLTKPSPRSASLPKNSQPLSISEIMTEQKEEIESQKRRSSFRKTIEEIQQEEEFQKWWEEESLRVQKELGILKTERDTSTNRKQGQASKQPQRRHRKEKDSKVSESTAEFKSLPIDIPRTTHKKGKARAVK O74882 SDH3_SCHPO BINDING 138; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_note="ligand shared with second transmembrane subunit"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000250" COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=The heme is bound between the two transmembrane subunits. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion" SPCC330.12c; CHAIN ?..180; /note="Succinate dehydrogenase cytochrome B subunit, mitochondrial"; /id="PRO_0000041773" MFATRSFCLSSSLFRPAAQLLRPAGRSTLRNVWRRSIATEHLTQTEANSRLASQRVHRPNSPHLTIYEPQLTWYLSSLHRITGCVVAGTLYAFAMGYLVAPLAGYSLDTATISGLIQQVPTWIKVPAKFVISYPLTFHIFNGIRHLIWDTTKELSLKGVYRTGYAVLALSVLTSGYFAMI O74883 RPC5_SCHPO SPCC330.13; CHAIN 1..242; /note="DNA-directed RNA polymerase III subunit rpc5"; /id="PRO_0000357058" MSFSEDQAMEEAKLRNDETEEQDPVVRTYPVFFSPGLRNNLLLNQFPLRPKNRTYSDANGEAPIDVRVKPKTGWMEVDVPIPTTKYYNEDKAMKYGNGKKPIQTQTLSGRLQKPRTNLMVGLIRDGQFHIVPLRGLTQLRPSMKHVNEYTQKLKAAAGPSNSSSGTSTPRGPIRAVQVTAKQNTEAPKVSTTHIVRATEEEEWVELDCRPERESESILKQLECPIEHQPNECAAVDEDYSFI O74884 RL24B_SCHPO MOD_RES 50; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC330.14c; CHAIN 1..149; /note="Large ribosomal subunit protein eL24B"; /id="PRO_0000136892" MKVEVCSFSGSKVYPGAGRLFVRGDNKVFRFVNKKSESLFLQRKNPRRLSWTVLYRRMHKKGISEEHAKKRTRRTVKHQRGIVGANLDVIKEKRNQRPEVRAAARAAALKQRKDKRAASESEKKAIKAKSAASSARGQAIKNAKVAARR O74888 BXI1_SCHPO SPCC576.04; CHAIN 1..266; /note="Bax inhibitor 1"; /id="PRO_0000316210" MPANYQSVPQDDPSVPNLAQAPPAYSEYNESATENPAVDQFKNTTPVAECAKSIRMAFLRKVYAILTAQLFVTSLFGGIFYLHPAFSFWVQMHPWFLILNFFISLVVLFGLIMKPYSYPRNYIFLFLFTALEGLTLGTAITFFSARIILEAVFITLGVFVALTAFTFQSKWDFSRLGGFLYVSLWSLILTPLIFFFVPSTPFIDMAFAGFGTLVFCGYILFDTYNILHRYSPEEFIMSSLMLYLDFINLFIRILQILGMLQNNDNN O74889 SAC31_SCHPO MOD_RES 841; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC576.05; CHAIN 1..1024; /note="SAC3 family protein 1"; /id="PRO_0000316863" MEKRNETGNNRLKRSNNRGKSKKDWKDASVETTPRETSVDEDNTSVFEDVEAQDSRQKRFSSTLEGNRFEELRSLREKEREVAIQNGLIDDPTKPRQLDEAVTFVGTCPDMCPEYEREQREYQNNLERWEINPETGRVDKNLAVKAFHRPAAGNEQALPSDVRPPPVLKKSLDYLVDKIVCGPDPLENTHFFVRDRTRSIRQDFTLQNCRDLDAVACHERIARYHILCIHQLCEKKQFSAQQEVEQLRKGILQSLCEFYDDLRKVKIRCPNEPEFRSYAIITHLRDPDVVRQSQILPIEIFDDQRVQLALRLSALAQKNNERVGHILPRNTEACPNLYTRFFKLVQSPAVTYLMACLLESHFMSIRKGALKAMRKAFMSAHANFPCGDLKRILHFDTVEQAASFSRYYGLEVSDDNGELSINLNKTAFFNDSKPDFRQLFSQTLVESKLQNRSFADIINGSRYNIDRVSPNTAFSTNIPLSLPFANKEPQPIAGFKKNTPETSVVSKNLSTFNGKFNVNAPVFTPRSFPTKPFSATDISSVQPTNLPNGSTNGTETFIPPVQNSITSNKEAVKPIKNKPKPISFESLSAVGNLIISDSLSRIVRQILQNLYTEWVHEKTNLVFATMFRTIFREVLLDGIASEVYLKSLKKHAISQISVRAHHSWVKKQEKMMLEMREKNRQEKYFSVLNSVVKAESSNITRLPIKRTFYGDTRNLDKASEKLRAEHDRTRRLWKPVLMDSLFSNLQKFPVYEDWHLLIFNASTSSMMKTWLCAKFSLKETNKTSFWHSSYNLFNRQYHVDMPDNVSDLPQTRLCYGACVYNVGLLDEEKRKDLANSDLNSSPKLIQGNDSRSAHESSANKLFSFVHDISRLTITKLPLLLIFWSDSNLDMQGITQKYRFLELITSTWSAISSIHVLTITNDRDMDLEHSLKVLLDNVTVEKSPFAQLEELEVVRKKREAEIEASSKTVKRLASNNKFLTDSNVEGLLEAPTSLENSLVEDDKWASLRQKIKAARDLLKKVETFY O74891 COPZ_SCHPO SPCC576.07; CHAIN 1..190; /note="Probable coatomer subunit zeta"; /id="PRO_0000193829" MNLTLYAVNAFLILDSSGKRIFTKYYAPPHLKEGEGGVFNSVKEEKTFEKGLFEKTWKTQNDILTYDGKLVVMLTVMDVIFYIVGGMEENEVMLYECLRSIRDALELLFKYVPDKRTLLENYDQLVIVVDETIDDGVILETEPALIAARVTKGPVSEAQAIVSDFKEMGFMNSFQKAREKITERILKGTF O74892 RS2_SCHPO SPCC576.08c; CHAIN 1..253; /note="Small ribosomal subunit protein uS5"; /id="PRO_0000131683" MAESAPRGFGRGGRGGRGRGRGRRGAKRDEEKEWVPVTKLGRLVKAGKIKSIEEIYLYSLPIKEYQIVDYFLPRLNDEVMKVVPVQKQTRAGQRTRFKAFVVIGDSDGHVGLGIKCAKEVATAIRGAIIMGKLSIMPIRRGYWGTALGDPHTVPVKVSGKCGSVTVRLVPAPRGAGLVAAPVTKRFLQLAGIEDCYTQSRGSTKTLGNFVKAAFAAASLTYGILTPNLWAERPFGQTPIEEYADILMQTEKKY O74893 RS20_SCHPO MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC576.09; CHAIN 1..118; /note="Small ribosomal subunit protein uS10"; /id="PRO_0000146691" MSQVAKDQKEQQIPSTVHRIRITLTSRNVRNLEKVCSDLVNRAKDKQLRVKGPVRLPTKILKITTRKTPNGEGSKTWETYEMRIHKRLIDLHSPSEIVKQITSIHIEPGVEVEVTIAQ O74894 PRS6B_SCHPO BINDING 175..182; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPCC576.10c; CHAIN 1..389; /note="26S proteasome regulatory subunit 6B homolog"; /id="PRO_0000084696" MNSTEEIDLYNRWKALERQLEMLDLQEGFIKEDCKSLKRELIRAQEEVKRIQSVPLVIGQFLEAIDQNTAIVGSTTGSNYVVRILSTLDRELLKPSASVALQRHSNALVDILPPEADSSISMLRPDERPDVSYADVGGLDVQKQEVREAVELPLTQGDLYRQIGIDPPRGVLLYGPPGTGKTMLVKAVANSTAANFIRVVGSEFVQKYLGEGPRMVRDVFRMARENAPAIIFIDEIDAIATKRFDAQTGADREVQRILIELLTQMDGFDQGANVKVIMATNRADTLDPALLRPGRLDRKIEFPSYRDRRQRRLVFQTITAKMLLSPEVDLDTFIMRPDASSGAQIAAIMQDAGLLAVRKSRGVILQSDIEEAYARAVKPTDMEQFAFYK O74897 SWC5_SCHPO SPCC576.13; CHAIN 1..215; /note="SWR1-complex protein 5"; /id="PRO_0000212510" MTEKLIDFGLEQEEEDTEFVPGDSTDTESSFSDADSSEEEFVEEKEASQVQSTKSKIATSESEDVTLKNIAKKNKRERNDKLIPQQSNESEAIEKPVQSTTEVELKTNELAESNSSVAVEGDENSYAETPKKKHSLIRKRRKSPLDSSSAQKVLKKNKLNTLEQAQQNWSKYIKEQDIQDELRIANKDGYVERQEFLAKTRAAHEEKIREMKKLP O74898 DPH5_SCHPO BINDING 9; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 84; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 87; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 112..113; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 163; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 221; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 246; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA-COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314; Evidence={ECO:0000250|UniProtKB:P32469}; SPCC576.14; CHAIN 1..283; /note="Diphthine methyl ester synthase"; /id="PRO_0000156145" MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLHTLVLLDIKVKEQSWENLARGRKVYEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAEHDIGPPLHSVVLVGRDVHDLELEFLRAYAVNLENFDRVAKTYLEK O74899 YQEH_SCHPO MOD_RES 55; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC576.17c; CHAIN 1..525; /note="Uncharacterized transporter C576.17c"; /id="PRO_0000372795" MNDTNDVMHVHSESISPKKNDLDIELGESVVEPHLSNNSIAKLDTYELEENEDISDYAYKLAGISNEHPAHPQNWGWWKKAYIVLLSTSLQMYVFWTPNFYPGVQDSVMELWHLSSQVSLLGQSMFVLGVALGPLFLGPLSDLLGRKLVYIGSLIIYVCFCISCALARNYAQLVISMLIMGVVGSTALGNVAGAVADVLGDEDSNWGMYMFIFMCSVASVGSPMGTGVAENPKLTWRWLYWIDVIVGGFFIILFVFTPETLPAIVIQRYEQKRQGLPVSWFPQFSLKKLAKDTYFVFFMAIKIFFSEPIVSSLGIYNGFVNGLLYFFLQAIWPVYFSIYKMSDMAASCTYMAAMPACVILLWFEPLQCWLYKRDKRKHQNRLRPEARFIMTLFYVWGFPIGIFMFAFCSKVHIHYIVSLIGLTIFNIADYHIWQAMLLYVTDAYPNVSASAVAAFELPSNLGAVGFIHLSALMFSRMNVHWATAVVGFASLPLIALIYALYFYGDRIRARSKLASQRVPINTAAH O74904 RL35_SCHPO MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC613.05c; STRAND 9..11; /evidence="ECO:0007829|PDB:8EV3"; STRAND 117..121; /evidence="ECO:0007829|PDB:8EUY" HELIX 5..8; /evidence="ECO:0007829|PDB:8EUY"; HELIX 13..35; /evidence="ECO:0007829|PDB:8EUY"; HELIX 42..71; /evidence="ECO:0007829|PDB:8EUY"; HELIX 80..82; /evidence="ECO:0007829|PDB:8EUY"; HELIX 88..92; /evidence="ECO:0007829|PDB:8EUY"; HELIX 96..99; /evidence="ECO:0007829|PDB:8EUY"; HELIX 104..112; /evidence="ECO:0007829|PDB:8EUY" TURN 72..74; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..122; /note="Large ribosomal subunit protein uL29"; /id="PRO_0000130551" MALKTFELRKQSQENLAEQLQELRQELASLRVQKIAGGSGSKLSKIKTTRKDIARILTVINESNRLAAREAYKNKKYIPLDLRQKKTRAIRRALTPYEQSRKTLKQIKKERYFPLRKYALKA O74905 RL9B_SCHPO SPCC613.06; CHAIN 1..189; /note="Large ribosomal subunit protein uL6B"; /id="PRO_0000131110" MGRDIYKDETLTIPEGVSVDIKARLVTVKGPRGVLKQNLRRVDIELKKQGNTIKFIVWHGSRKHNACIRTAYSIINNMIIGVTQGFRYKMRLVYAHFPININLTENGTVVEIRNFLGERITRVIKCLPGVTVSISSAVKDEIIIEGNSLENVSQSAANIKQICNVRNKDIRKFLDGIYVSERGNIEELE O74906 BCD1_SCHPO BINDING 9; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 12; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 21; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 24; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 29; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 33; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 37; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 43; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" MOD_RES 294; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 296; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC613.07; CHAIN 1..345; /note="Putative box C/D snoRNA protein SPCC613.07"; /id="PRO_0000173561" MSENRLGICSTCQKNASKYRCPRCDSRFCCLECNLEHKRLTKCSGERDPATFVPKSKLVNHLNSDFNFLSGVERLINRKENGSHQVSNRAERNRLQLKRSLERAGINIKFAPPSNKKRRLNRTHYDKKSHLIKWSIEWCLHESSTSKDLTDEASENTIITHSHPESEPLEKIFRKLVEENSEMNSQVSKANIHAPDDMQFMIKSRKSRSKGFIYKKIEPSNSLSSCLRNSFVFEVPTIHVFTSTTQVHTESSYETSSSEQSDDSSSSSSCISDSEESSSDDELNELSNEKKANSPTQNVDTSSKLSSVKFQNEDDEDRRKNSDGSEASYSLPPLFGSYFQKQGQY O74940 NADE_SCHPO ACT_SITE 45; /note="Proton acceptor; for glutaminase activity"; /evidence="ECO:0000250|UniProtKB:P9WJJ3"; ACT_SITE 114; /note="For glutaminase activity"; /evidence="ECO:0000250|UniProtKB:P9WJJ3"; ACT_SITE 175; /note="Nucleophile; for glutaminase activity"; /evidence="ECO:0000250|UniProtKB:P9WJJ3"; ACT_SITE 359; /evidence="ECO:0000250" BINDING 357..364; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58359, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.5.1; SPCC553.02; CHAIN 1..700; /note="Putative glutamine-dependent NAD(+) synthetase"; /id="PRO_0000152247" MERYVTIASCQLNQWAMDFEGNRLRIIDSIKEAKRQNASLRVGPELEVTGYGCEDHFLESDTYYHSWEMLCSIIHDPDCQDILLDIGMPVMHKAMRHNCRILALNGKILLIRPKIWLCDDGNFRESRWFTPWLRPRVVETHYLPTFVAKSLNQTTVPIGDAILQCNETVVGVETCEELFTPNSPHIDMALDGVEIFINASGSHHELRKLTTRVNLIQNATEKCGGIYLYSNQRGCDGGRLYYDGSSMIFANGKMLAQGHQFSLKDVEVISATVDVDTVRSYRFQPSHGIQGVTRPSYERIHVNFSLSSYQQDYDIYRKPTDPIEVTIPLPEEEITFGPACWLWDYLRRSHAAGFFLPLSGGLDSCSTAVLVYSMCRIVCKAMEEDDAQVLSDVRRIVGDPSYSSTDPKKLLNHLFYTAFMGSEHSSKETRSRAKELSSLIGSYHTDVNIDTMTSAVVKLFALVTGKTPQFRSNGGTNAENLALQNIQARSRMLLGYLFAQLLPWVRGYSGSLLVLGSSNVDECLRGYLTKYDCSSADINPIGGISKTDLKSFLRYAKEALDLPILQEFLDATPTAELEPTTESYVQSDEADMGMTYAELSVFGRLRKISKCGPYSMFTQLMHQWGDRLSPSQVAEKVKRFFHYYGINRHKMTTLTPSYHAETYGVDDNRYDLRQFLYPSWTWQNKKIDALASKFEQHQRK O74941 PEX1_SCHPO BINDING 379..386; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 647..654; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P24004}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P24004}; SPCC553.03; CHAIN 1..937; /note="Peroxisomal ATPase pex1"; /id="PRO_0000374017" MRCIVSYKSLRSCLVNVPELLLESISEPVQNYAVQAVVCKNDIKKTFYFGISGIPSQFSFEIDSTYAHTLKLAENQEINLSIIDCTHEIEQLEIEPVTSNDWEIAERNAAWLEENLLVQYRVATTERFIIYLPSGTFIQFQPLKLIPSSLCGRLLRTTEVLITPKPNTSAIEVKENRKVNLRCVVENRLLPDSVTADSPALCVFLPLNFPDRPDVVYMDGGNLKSTIVCQCVSCPFQIPGHFFISKSLALSYSIKTGFKFQIWKAHNPPSSSKFILEQKGLPPESNLSSELVAAKLKNSYLMDGMTLKLVDIAVSYSVSGLSGVVKNPIQDIKITSDTNVPVNAGIRNNSPRLSMQPFPHEFAQVRNAVFLHQNIYINGPKGCGKSNLVHSLFDYYSLNSIYFQMIVSCSEIDRSSFAKFQSFWNNVFIQAERYEPSIIYLDDVHCLISSSNENGELGFVEEREIAFLQHQIINLKRKRKIIFIGFGEEFLTFSENLVLPLLFQIKIALPSLAVTRRKEILTTIFQENFSDITMDSIEFISVKTEGYLMTDLVLFVKRLLSEAFVEKIQNGPKHLMNKGLIEKTLKDFVPLQLRKAKFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSINAVDPSQTTSSFTNLTTESKRNASMLALPPESRYNQNMQSMSDSKSVVIEDYMLMEALKKNSPSLNSEEFEHLSNLYRDFRSKLFEPELNARNTDVGSKTRQI O74942 CYP9_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC553.04; CHAIN 1..610; /note="Peptidyl-prolyl cis-trans isomerase 9"; /id="PRO_0000358863" MMDGASPVDRDVSPVGLPKKRIKQNHDQVFLHNLPDAPRYTKSYMHNAEIYKCFPTKSNYILSVSYDGYVKFWHKTPNGVEYIKEFHAHNAMLLSAELSQDERLFITGADDKSLKVFDVESIDLVNIIDLEFLPKAICCFNSPSLKTSLIAVSSAESPLIFFFESGGDGEVLYTVKKHTAPVHCLRYLSTLDCFLSIDIGGMVEYWSPEEPFQKPDTAELFNMKSQTDLYIFKKQKSVPTSLEVSHFENFWSTISYPDCKVRVFDTKSGRAILELDENPSNAAKKVEALFEKEDTESSYYMSHVELGRRIAIERDIEKHGLTVGTTAIFDESEKYLLYGSIVGIKVVSIDNGTVVRIYGKDEAVRFTRLSLYQQAPKKSNLPSLDVIASNNPLVEESFQKDPTLFATAWKKQRFYLFSNMSTKFTLSDRDVYNEQVLPVTNNEGRQENGNILLGKAAIIHTTQGDISIKLYPEEAPKAVQNFTTHAENGYYDNTIFHRIIKNFMIQGGDPLGDGTGGESIWKKDFEDEISPNLKHDRPFTVSMANSGPNTNGSQFFITTDLTPWLDGKHTIFARAYAGLDVVHRIEQGETDKYDRPLEPTKIINISIVYT O74945 RIA1_SCHPO BINDING 26..33; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 100..104; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 154..157; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; SPCC553.08c; CHAIN 1..1000; /note="Ribosome assembly protein 1"; /id="PRO_0000315632" MPVIPPEKLVSLQKNQENIRNFTLLAHVDHGKTTLADSLLASNGIISSKLAGTVRFLDFREDEITRGITMKSSAISLFFKVISQNDEKRVEKDYLINLIDSPGHVDFSSEVSSASRLCDGAFVLVDAVEGVCSQTITVLRQAWIDRIKVILVINKMDRLITELKLSPIEAHYHLLRLVEQVNAVIGTFYTGELMQLADNDEVISDEGIYFAPEQGNVVFASAYDGWAFCLDQFSEFYEKKLGLKQKALTKCLWGDYYLDPKTKRVLQPKHLQGRRLKPMFVQFVLENLWAVYESAVSNRNLENIEKIIKALNIKVLPRDIKSKDPRNLLLAIFQQWLPLSTAILLTAIREIPSPINAQANRARKVLSSTPHYEMIDPDITLAMESCDASKEQPVLVYISKMVAFSERDLPNHRRKQLSAEEMKLIRSKLSESIESGINTISIEENVSSTNSDNLEGSTTDMDDDKDILIGFARIYSGTISVGQEVYVYGPKYDPVNPEKHITKVTVESLYLMMGQELVYLETVPAGNVFAIGGLAGTVLRTATLCSSPNGPNLVGVTQQMEPIVRVALEPVRPFEMNKLVTGLDMLNQADPCVQIAVEENGEHVIMCAGEIHLERCLKDLRERFAKIEIQASQPLVPYRETTIATPDLLAKNKELSIGFVTATLPVGGVTIGITVTPLSGSVVDFLLKHSKTIENVSSNFSKKNRNVVVSESLTKSMEEVLTPEKFYERLSKLLEEENSDLGELKNHLDSIIAFGPKRVGPNILFDKTKKMRDFRRQSDETKLIPSDLSEYVVTAFQLITHQGPLCAEPVQGICVSIDQFDISDDSEDSKLLTINNPQIPGQVISVVKESIRHGFLGWSPRLMLAMYSCDVQATSEVLGRVYGVVSKRRGRVIDEEMKEGTPFFIVKALIPVVESFGFAVEILKRTSGAAYPQLIFHGFEMLDENPFWVPTTEEELEDLGELADRENIAKRYMLNVRKRKGLLVEQKIVEKAEKQRTLKH O74948 T2AG_SCHPO SPCC553.11c; CHAIN 1..109; /note="Transcription initiation factor IIA subunit 2"; /id="PRO_0000194052" MSQYYELYRRSSIGISLTDALDDLISQGKISPQLAMKVLFNFDKSMTEALAEKVRSRLTFKGHLDTYRFCDEVWTFIIKNPSFRFDNETVTSNKIRIVACATRDSSANR O74952 SYFM_SCHPO BINDING 115..118; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 143; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 150..152; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 157..159; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 271; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 296; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC736.03c; CHAIN ?..429; /note="Phenylalanine--tRNA ligase, mitochondrial"; /id="PRO_0000316581" MFPHRVSHLSKLFSRRFPNWKRKVQTDSWSNVPEHIHSKIGRNLFQKEGHPICSLRQLLEQQFQKFEMNNVQKESPIVSVETNFDSLGFPKTHVSRSKSDTYYMNNKTCLRTHTSAHQPEEFSRLAKEGFKKNGFLITADVYRRDEVDSSHYPIFHQMEGALVWNRNDTAKMKNDLKKVALSPSLKSMVDDETTALETHNDMQDIYSLEETKFVSQHLKDTLTTVIHDLVSLAPSISSGAEQVRYRWTYDSFPFTKPSFQLEIDWKGKWLEILGCGVVQDRLLKGAGLNNYIGWAFGIGLERLAMILYGIPDIRLFWSLDERFSKQFLPNKISTFKPFSKYPACFKDIAFWINNDFNPNDFYEIIRDVCQDMVESVNLIDQYTAKSGKTSLCYRVNYRSMERSLRNEEIDKLQEKLRNRVANSLRVELR O74955 TSNAX_SCHPO SPCC736.09c; CHAIN 1..231; /note="Translin-associated protein X homolog"; /id="PRO_0000352756" MEEEFLSFKNFLQEDQDKREKIIRLSREITIQSKRMIFLLHQTSSSDGFPLPKDFDRTSIFEKKIHKELESLKRELAGLNADKFSSACTHGLQEYVEAVTFKFWLQTGTLLSCKDSSFRISINFIDYVLGVCDMTGEIMRFLVTNGSKFSVQQLTQQVKFLRGLHKNCSEIEHLPSKVKSELQQKLSVMENSISKVEGICYSKILREADKRYLNLEVDTATPPEEKRLRST O74967 VPS25_SCHPO SPBC4B4.06; CHAIN 1..175; /note="Vacuolar protein-sorting-associated protein 25"; /id="PRO_0000362145" MRVPSIYNFPPFFTRQLNDNTWHSQKAAWQMWILLWCRENRQTSITINPELLESSLLHNSTIHRTLPLSVFREIVEDMVKQNLAEWTEKRNPKDVFWVYWRSISEWGNMILKWLSDMGREGSICTFYELQEQYKEVDCLDEVLLHKVLELLMKKGNIELMKGSSGKYSGFKVLKA O74968 RU1A_SCHPO SPBC4B4.07c; CHAIN 1..249; /note="U1 small nuclear ribonucleoprotein usp102"; /id="PRO_0000338448" MDPQTNSHQEVQQPSPKETDSQTPSETLYIRNIEEKIRLTMLKRILEHLFGSYGKVIDVQARKTLRMRGQAFVVFDNLENASRALKDLQGYPLYGKPMMIQYSKSKSDIIVQRESPEEIETRKKDRKNRREMLKRTSALQPAAPKPTHKKPVPKRNVGAERKSTINEDLLPPNKVLLLQNIPQEVNADVLTQIFEAFSGFQEVRMVPGRRGIAFVEYDSDREATVAKNGTTGMSLSGNQIKVTFARKAS O74974 UTP25_SCHPO SPCC1827.01c; CHAIN 1..652; /note="U3 small nucleolar RNA-associated protein 25"; /id="PRO_0000372381" MAIESDLDGASMDELAGKSYEALLYLMNKNKKRKPEKKDDKEKSSKKVQKKNKVIESLNEMEVEMEDENENENDEQEAIQYYINVESQDADETLHQEAQDSSEDPFHQHFDYDDSEVIKNSIAAYDEGKLCKSIEESKLGVSQSFFPDVTKRLPCSCLSEIKNIDDLGLKQRILDSYKKQKPSGQLTSMQIELAKAMFNYQDVFFTNMSMKSHKLGTSLLALHALNHVFKTRDRVLKNSARISQNPELEFRDQGYTRPKVLILLPTRNSAFEFINLLISYSGTNQVENRKRFDNEFSIEKEVISEKKPEDFRYLFSGNTDDMFRLGVKFTRKTVKLFSQFYNSDIIVASPLGLRLAIGNKGDKKRDLDYLSSIEIAMVDQAHALVMQNWEHIECIFDELNGLPKEAHGCDFSRVRPWYLDQQARYMRQTILFSQYNNLDINSFFSHYMSNIAGKVKFRSLLHGVLNRLGYKVTQTFVRISVDSIIKVPDARFSYFTGSILVQLKKYSQSGILVYIPSYFDFVRVRNYMDEEGINYSAISEYSSVSDMTRARNLFYQGRTNIMLYTERAHHFRRFDFRGVKAVVMYGPPTNPQFYVELVRMPMRTISEGNLDSDAAKCRIMYTKFDSICLEGIVGYQRVSNMCHGKHEVFEFL O74975 PCY1_SCHPO BINDING 109..117; /ligand="CTP"; /ligand_id="ChEBI:CHEBI:37563"; /evidence="ECO:0000250"; BINDING 147; /ligand="CTP"; /ligand_id="ChEBI:CHEBI:37563"; /evidence="ECO:0000250"; BINDING 147; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 176; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 193..194; /ligand="CTP"; /ligand_id="ChEBI:CHEBI:37563"; /evidence="ECO:0000250"; BINDING 198; /ligand="CTP"; /ligand_id="ChEBI:CHEBI:37563"; /evidence="ECO:0000250"; BINDING 221..225; /ligand="CTP"; /ligand_id="ChEBI:CHEBI:37563"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate; Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975; EC=2.7.7.15; MOD_RES 315; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 319; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 323; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1827.02c; CHAIN 1..362; /note="Probable choline-phosphate cytidylyltransferase"; /id="PRO_0000316623" MGEEGIKINDTHKRRIDEVEPSEKEDNVERQTKKYNFEIDEPEEQEKKDEKEDDKEESPSKSLEEISQSVSPVEEEPRDVRFKELSTPFSYPINDPPEGRPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITPEFLEEHKIDFVAHDDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRNLARGVNRKELNVSLFKKNELDLRHHIKVLRDTLRNHWVSTTRDLKADIKSFLSMATTDYQLQKNPLHGSSEPSSPGPTGFLGGINRWMQRRSSSHYDLPRVGNEIAASSSSATEENH O74983 MMS2_SCHPO SPCC338.05c; CHAIN 1..139; /note="Ubiquitin-conjugating enzyme spm2"; /id="PRO_0000082599" MAKVPRNFKLLEELEKGEKGLGESSCSYGLTNADDITLSDWNATILGPAHSVHENRIYSLKIHCDANYPDAPPIVTFVSRINLPGVDGETGKVNPHKIDCLRHWKREYSMETVLLDLKKEMASSSNRKLPQPPEGSTFF O74985 NAT1_SCHPO SPCC338.07c; STRAND 271..273; /evidence="ECO:0007829|PDB:4KVM"; STRAND 340..342; /evidence="ECO:0007829|PDB:4KVM"; STRAND 361..364; /evidence="ECO:0007829|PDB:4KVM"; STRAND 479..481; /evidence="ECO:0007829|PDB:4KVM"; STRAND 648..650; /evidence="ECO:0007829|PDB:4KVM" HELIX 11..22; /evidence="ECO:0007829|PDB:4KVM"; HELIX 26..31; /evidence="ECO:0007829|PDB:4KVM"; HELIX 34..36; /evidence="ECO:0007829|PDB:4KVM"; HELIX 44..56; /evidence="ECO:0007829|PDB:4KVM"; HELIX 61..71; /evidence="ECO:0007829|PDB:4KVM"; HELIX 78..90; /evidence="ECO:0007829|PDB:4KVM"; HELIX 94..107; /evidence="ECO:0007829|PDB:4KVM"; HELIX 112..124; /evidence="ECO:0007829|PDB:4KVM"; HELIX 128..141; /evidence="ECO:0007829|PDB:4KVM"; HELIX 146..158; /evidence="ECO:0007829|PDB:4KVM"; HELIX 162..174; /evidence="ECO:0007829|PDB:4KVM"; HELIX 185..201; /evidence="ECO:0007829|PDB:4KVM"; HELIX 203..214; /evidence="ECO:0007829|PDB:4KVM"; HELIX 215..217; /evidence="ECO:0007829|PDB:4KVM"; HELIX 221..234; /evidence="ECO:0007829|PDB:4KVM"; HELIX 238..251; /evidence="ECO:0007829|PDB:4KVM"; HELIX 257..265; /evidence="ECO:0007829|PDB:4KVM"; HELIX 278..287; /evidence="ECO:0007829|PDB:4KVM"; HELIX 297..300; /evidence="ECO:0007829|PDB:4KVM"; HELIX 302..305; /evidence="ECO:0007829|PDB:4KVM"; HELIX 308..324; /evidence="ECO:0007829|PDB:4KVM"; HELIX 330..334; /evidence="ECO:0007829|PDB:4KVM"; HELIX 335..339; /evidence="ECO:0007829|PDB:4KVM"; HELIX 343..355; /evidence="ECO:0007829|PDB:4KVM"; HELIX 367..369; /evidence="ECO:0007829|PDB:4KVM"; HELIX 378..393; /evidence="ECO:0007829|PDB:4KVM"; HELIX 397..409; /evidence="ECO:0007829|PDB:4KVM"; HELIX 414..427; /evidence="ECO:0007829|PDB:4KVM"; HELIX 430..442; /evidence="ECO:0007829|PDB:4KVM"; HELIX 448..460; /evidence="ECO:0007829|PDB:4KVM"; HELIX 464..471; /evidence="ECO:0007829|PDB:4KVM"; HELIX 482..489; /evidence="ECO:0007829|PDB:4KVM"; HELIX 493..505; /evidence="ECO:0007829|PDB:4KVM"; HELIX 509..529; /evidence="ECO:0007829|PDB:4KVM"; HELIX 533..540; /evidence="ECO:0007829|PDB:4KVM"; HELIX 543..553; /evidence="ECO:0007829|PDB:4KVM"; HELIX 560..578; /evidence="ECO:0007829|PDB:4KVM"; HELIX 582..584; /evidence="ECO:0007829|PDB:4KVM"; HELIX 588..596; /evidence="ECO:0007829|PDB:4KVM"; HELIX 601..630; /evidence="ECO:0007829|PDB:4KVM"; HELIX 658..666; /evidence="ECO:0007829|PDB:4KVM"; HELIX 670..672; /evidence="ECO:0007829|PDB:4KVM"; HELIX 678..689; /evidence="ECO:0007829|PDB:4KVM"; HELIX 693..705; /evidence="ECO:0007829|PDB:4KVM"; HELIX 712..725; /evidence="ECO:0007829|PDB:4KVM" TURN 8..10; /evidence="ECO:0007829|PDB:4KVM"; TURN 37..39; /evidence="ECO:0007829|PDB:4KVM"; TURN 288..290; /evidence="ECO:0007829|PDB:4KVO"; TURN 356..360; /evidence="ECO:0007829|PDB:4KVM"; TURN 443..446; /evidence="ECO:0007829|PDB:4KVM"; TURN 472..474; /evidence="ECO:0007829|PDB:4KVM"; TURN 530..532; /evidence="ECO:0007829|PDB:4KVM"; TURN 554..557; /evidence="ECO:0007829|PDB:4KVM"; TURN 651..654; /evidence="ECO:0007829|PDB:4KVM"; TURN 667..669; /evidence="ECO:0007829|PDB:4KVM"; TURN 673..675; /evidence="ECO:0007829|PDB:4KVM" CHAIN 1..729; /note="N-terminal acetyltransferase A complex subunit nat1"; /id="PRO_0000311768" MAKVQLSPKEITLFRTALKCYETKQYKKGLKAIEPLLERHPEHGESLAIKGILLHSLGNTKEGYDNVRLGLRNDVGSGVCWHIFGLISRADKDYVQAAKCYINAHKLEKNNSSLLRDLALLQSQLRQYKALADTRNALLQDNPGVRANWSALAVAQFLRGEYASAYKIVDAFESTINQGVPVDTQEESEAMLFMNLVILKKDGVEDAYKHLLSIEKKVLDRVAFLETRAEYELYLSKMEEAKSTIYLLLDRNPDNHQYYYNLQRAYGYEDASGKVLDSAEWLNLYSQLAKRYPKSECPTRLPLEKLEGDEFLTHVDLYLRKKLKRGIPSVFVDVKSLYKDTKKCKVVEDLVSKYASSLSTTNKFSEDDDNSQIEIPTTLLWTYYFLAQHFDHVGELEKAEKYVDLAIDHTPTLVELFMTKARISKHKGELQTAMEIMDHARKLDLQDRFINGKCAKYMLRNDENELAAKTVSLFTRNEAVGGAVGDLADMQCLWYMLEDGKSFARQKKFALALKRFSTVFKIFDTWADDQFDFHFFAFRKGSLRTYLDLMSWEDSVYDDPSFREAAQGSIEIYFALFDLPFAKYSPKLPDFEKLSSGEINEEEEKKIYKKLKKDLSKRLERAEKLKEADKSRAKSEDGMPVKYDEDPLGENLVATSEPLKEAQKCLEKLLPYGDKNPSAYILAAQLYTRLKNFDTASKYLEQAKVILGQNDPTVISTEKFYNSIKTQSN O74988 COX5_SCHPO TRANSIT 1..20; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC338.10c; CHAIN 21..186; /note="Cytochrome c oxidase polypeptide 5, mitochondrial"; /id="PRO_0000006096" MYLSKIICKKVPMKLLCTRNAATVSAAATNALQKEQPSGEAMIARPRLVDLDKRWGIMSQEEKDGLITDLYARQKQPWTTLSIEEKKAAYWIAFGEHGPRAFSHISQKTVFWGTVAGLTIGVVLFGLIRTQAAPSPRTMTREWQEKSNEYMKENKINPISGEASEGFKGRGQISGGIFSPSEKDKK O74990 COG4_SCHPO SPCC338.13; CHAIN 1..738; /note="Conserved oligomeric Golgi complex subunit 4"; /id="PRO_0000339132" MDISINDCTDISQIKQRFHDLQVESQRTDEKLERLLSDAQPTEKFNSLIKNMAERLVLFVGQIEELKDAFCNTTIVSEEVIERIKSVDREQNRIKECLLFVRQVRDFKECLQDLNRAMHHQQWEKAADLVHRASSTSPAIIEGKFAHAVVPTAEQPLAPMDTLKEITESLHTLFWREFHKAARNQDQKEITRYFKLFPLIGKEKEGLEAYWHFFGGIIASKARATLDEPPTHALFFAQAFTGLVEHVASIIRAHTPLVQKYYKAKNTITVIEKLQGDCDRQGSIIVNTMFDVRRIDNLVSSIASYKYILLHAKLKNRAFVSDQKELERVSLQTLHPILNEMSAIVSKWNISKIFISRLVLRLSQSDGTSNDPSVQDNLICASIFNSSKMELLLKKQLLPSLLQLETYYFRRSIETSLELEEYYTKVSPWMSSIVDDVMYVTKQVFQRAFFTVSSLFFTRFVNESLIPILRNDYYVYLSHNLLTVCNIIKAQFQRLKNANSIPAKQVENYITLVNSASLSKQYLKSIVDGVSSRLEEVFAFAKDQKLVKKSIDNFLQLTVNFENLCKTSFNMYFPIFLLPRIEQCIDDSFDGINYVLSYEDYTKETEHERLVVTRLRSVWDRVLLLEQFTPENQLSLRSMACEKAASYIENLILYKIQWNDYGAMALENDISSLITIFSNDQANLRHSFERLQEILILLVWESDSTAPEQLINDLNLQLLSIDIVSAIMEKKANVQGED O74992 YJZI_SCHPO MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC338.18; CHAIN 1..117; /note="Uncharacterized membrane protein C338.18"; /id="PRO_0000304071" MTEQNIDIKRELKDESPIGQSPHLENDGRPSLMSRYSYSSIEEVSKEGYQWFKHQSVFLKFSLIVLLFSLMFSLTFGSLLGLISLALGFPSVGYRYVLLPILNALLNRLRLNSSGLK O74994 RNG3_SCHPO SPCC613.04c; CHAIN 1..746; /note="Ring assembly protein 3"; /id="PRO_0000097380" MTHELSSTPQIDLLNDILKNSVESNVFSDYQKKQIVTLILKSKISTAIVLLSPKSTAASEWNYLCNLQDLHECVLCVDTILPANLQTIAKRIFSLVLLPPLNDWCKQLRDAFLRFVSQPSICPTDFPLKLFFLSTVGIELLIVNEKIIPQKTQKYLLYELFSSPSSITANEIARLCQEANNRNYLLQSLTSATDARRAFLNNPNYRLLSAIIFQDGPSNLAFVLAKDCVLLARQPETIPVSFERMSSLLLMCLPSHPDFISPEFCHEWTELAERNGLQEEWLNILNTACNFKECRAIIHKECSEFIKDNHTSRVAILISMKLAFQYQLSQVIPTLKLLLQSKVYDSVLLEALRQSSTLGPVKQLIADDSCLLNNLSKLLLDTNISPLDASSIATIIYNMCKFKITKSEHERELNQLRNMAEASKTIDYKEDETAPTERRIQKILEYDILSKLFSAAKHYNSLNGLLAMILVHMANYKLARRKLVQIGALKFLTRQCFIQTQDSNAAFALAKILISVAPHSIFTKAFPSNRAIHPMSKLLSTNSADTEYPILLGKFEVLLALTNLASHDEESRQAIVQECWRELDELIIETNPLIQRATTELINNLSLSPYCLIKFIGDKDSDFENTRLHIVLALSDTEDTPTRLAACGILVQITSVDEGCKKILSLQNDFNYIVRMLTDQDEGIQHRGLVCICNIVYSKDQEIFNKFIKTPKAVETLRTYITKQAALKELQHEALVMIDSRLQGSK O74999 RAD7_SCHPO SPCC330.02; CHAIN 1..563; /note="DNA repair protein rhp7"; /id="PRO_0000363002" MSSGSRVRGPNSALTEFLRSQGINASALGRARPPRQSEESAGQSTGTESEVIQTPTSVEENNEDENSMSTTTIEIPVVKRRNLRNQKKKKKTDEEAEDNEDTFSMNSRAGFSYKAREHTGKLDFCAHCNCRFTITPYSKYSNSEKGWLCYPCSRGAEDRSVPELRTRKRKALTRKKVAAATMDEEISVPKLQDLCIRVIAEYINDIEAFGDIGQVNMDKISQIISKNRSLNDTTVKLFLSGGQTELKLYDCSKITADSLFQIAQYCPNLQTLHLTYCGQMQDQVLHFYADHLTELTDVSFQGAFLVSSSEWINFFKKRGSKLISLELTDTARIHVSVINAIVDCCPNLISLNLSRIFYLDDECVRLLAGCRNLVSLKIESPGGIINDGSILDVLNQIGSGLHTLSLSGCTKLTDEVLKQGIGPCCGRLKHLNLSGLELLTDDEASIVFGEWKIQSGLETLSLRRCLSLGDKTVRAVLVNSGHTLRTLDLNGMSFVTDEALQYIVNFPLPMLKALDVSWIRGMNDKLVCDFESKKPTLEKLLVWGDNHVLMPSNRLLLIGREVQ O75002 MOG1_SCHPO SPCC1840.01c; CHAIN 1..190; /note="Nuclear import protein mog1"; /id="PRO_0000215202" MVQLFGGALCADFPPKFLDASVLRQIPDNQEVFLQDSKENLTVIIELLEKIEKPFDGSVAAYHFNSIAFDNDASQRVIWRDKSLGEDDFEGMRSEKASGSSVQGCQRVLEKGKRNPESATNVAIFVNVITLIDFQTDIVISVNAPLPNTSSVPSSVENIPPSDQSIVRAALETIQRVTRSLVLVDKTVFA O75005 SYV_SCHPO BINDING 655; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9; SPBC1709.02c; CHAIN 1..980; /note="Valine--tRNA ligase"; /id="PRO_0000035838" MADKGCEAAQSKDSSAPGSGEPRPKTEKELERERQKAAKLEKYHAKLAAKKAKEEARKPKLDKKAKIASPVAEYVEKTTPGEKKVLQDLDSPALKSYNPKAVESAWYDWWVKSGFFEPEFGPDGKPKKEGVFVITSPPPNVTGALHIGHALTIAIQDSLARWNRMLGKTVLFLGGFDHAGLSTQSVVEKKLWYTQKKTRHDYPRDKFVDIVWEWKEEYHNRIKNQMSRLGGSFDWTREAFTMDENLSRAVVETFVRLHEENIIYRANRLVNWCTALQTTLSNLEVENVDVPGRTLLKVPGYDEPVEVGVLTSIAYAVEGSDERIVIATTRPETLLGDTAVAVHPQDPRYKHLHGKFVKHPFCNRSIPIICDDIIVDMEFGTGAVKITPAHDPNDYEVGKRHNLEFINIFTDDGLLNENCGEFAGMKRFTARVKVVERLKELGLFVGTKENPMVIPLCGKTSDIIEPVMKPQWWVNQKEMAAAAAEVVKSGEIEIAPDMSRREFIRWMENIQDWCISRQLWWGHRIPAYFVNLADEPSQDRSEGRYWVTGRTLEQAEEKAKAAFPGKSFTLEQDEDVLDTWFSSGLWPFSTLGWPKDTSDYENFYPTTLMETGWDILFFWIARMVMLGLKLTGKIPFKRVFCHALVRDAQGRKMSKSLGNVVDPIDVIEGISLQALHDKLLVGNLDSREVEKAKKGQRLSYPKGIPQCGTDALRFTLCSLTTGGRDLNLDILRVEGYRKFCNKLYNATKFALGRLGSNFVPNKTADLTGNESLVEKWIFHRLNIAAAAMNKNMEEMNFLQATSAVHQFWLYELCDVYIENSKYLLSDGTEVQQESAKQTLYTVLDNALRLMHPFMPYVTEEMWQRLPRRPGDKTQTIVKAAFPVERVDYSNEIAAKYYESIITVVHSTRSMMAENGIKSDAVVYIHPDEEHSKLITSESASIQSLIKKCKTLSIVDNTFDSDKCVKNEVLEGSTIFLERNN O75006 SEC15_SCHPO SPCC1183.01; CHAIN 1..768; /note="Exocyst complex component sec15"; /id="PRO_0000118958" MDIDVLEFVDKIASIESAGDTLDRLPQLISLACEKGQETQVYERLNELASKSAIRVEQLSAENNQDFSKSVNQLSVVRSELRSLQSLMADLNTDIQASGRDLQNMKQQLNSLSTSERFLTKYHNLVRSCMQVLHQVQYSQELLSKKQYLPTLRICSEISEVHLKRLDGLGMYSTIQQYIVTTKEAICSAVMEDLHEWLFSIRQKLPLVGKSCSQQIDEARRRWAREYKEDLVNLSSKTSISLELYLLEMMDFSPLDNEIVKISFEPLYICLQVHSYLGLLSSFRSSFERDRRRQQEFLAPKSLTTLDMAVVSEWLNSIAGFMIVEYYILQCIPNFRSYEEVQNIWTIICEKLVETILSVAFTEQSTTTIIKLKNQIVLLMHTMERFGFSVESLRNLCVELIDAFGGALILKHSVFFEEAFEKDVYAPMIVETQEEYDHYIAPYWNFPSEPFPRTMSFSKMCPLCCTTLSKFVRHFFMFLNDSVILATEVNEKAPRFYRRFILRSLVDRLKSLYPKLALSQMSQLVKNFYAFEDPLLQIEKSLVLNKPIHQIGAEASSSNNVKSTELLEGLANARKSALHEIFVKINLKIDDFLGLAEYDWTTTQVRKDVSGYLQEMVTYLQTMYLESLAGLPKHDKSYVYLETLDHLCTAMVDLLSDPSIRKVTTAAAEGFKLDVEYLESFAAQVPDQSIVNADSFIELRQCANLLLGDNMEEYLDTDKFMRDFNRLQPAVAIKFLERHINNYSANPLSNDRPKRRAIEILIATLKKR O94238 RL14_SCHPO SPAC1805.13; STRAND 12..16; /evidence="ECO:0007829|PDB:8EUY"; STRAND 25..31; /evidence="ECO:0007829|PDB:8EUY"; STRAND 33..40; /evidence="ECO:0007829|PDB:8EUY"; STRAND 49..52; /evidence="ECO:0007829|PDB:8EUY"; STRAND 56..62; /evidence="ECO:0007829|PDB:8EUY" HELIX 53..55; /evidence="ECO:0007829|PDB:8EUY"; HELIX 71..80; /evidence="ECO:0007829|PDB:8EUY"; HELIX 91..103; /evidence="ECO:0007829|PDB:8EUY"; HELIX 107..121; /evidence="ECO:0007829|PDB:8EUY" TURN 20..23; /evidence="ECO:0007829|PDB:8EUY"; TURN 84..89; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..134; /note="Large ribosomal subunit protein eL14"; /id="PRO_0000132042" MEGFKRYVEVGRVVLVTKGEYTGKLAVIVDIVDHKRALIDSPCSEFPRQVIRYGSVVLTHIVMKLPRGARSGIVAKKWKAQDVCNKWASSAWAKKLEAKKVRSQLNDFDRFAVMRLKKQRREQVNVAVAKALKA O94241 ARP6_SCHPO SPCC550.12; CHAIN 1..401; /note="Actin-like protein arp6"; /id="PRO_0000089119" MGLPPKTIVLDNGAYHIKAGFAGGKVVEIPNCLTRSKDGNRLFLGNELANCNDFTTLQFRRAHEKGYLVHWSTETAVWDLVMRNVGVMEPSMADYSLLLTQPVFTMPSIEHNTIQLVFEEFQFDAYLPCTPAELIPWDHGSFTMNQEDAYTGQHGECVLVIDSGYSFTHIIPVIDFSVQEQAVKRVDVGGKLLTNYLKEVISYRKYNMMEETYIVNEIKESVCYVSQNFKEDMEICHEKPRSKLEICYALPDYSTGKHGYIVRDINQKIEQQVLNLSNERFMIPELLFSPSDIEIREAGIPEAVMQSVTHFPENIQAMLLENVVTIGGNCKFPGFHKRLSSELRSLAPANWEVKVFEPSDPICFPWKKASHMPLEHWNANKITRSEYSEHGANIMTRKRRI O94242 SYDM_SCHPO BINDING 192; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 238..240; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 238; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 502; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 509; /ligand="L-aspartate"; /ligand_id="ChEBI:CHEBI:29991"; /evidence="ECO:0000250"; BINDING 554..557; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12; TRANSIT 1..30; /note="Mitochondrion"; /evidence="ECO:0000305" SPCC736.06; CHAIN 31..611; /note="Aspartate--tRNA ligase, mitochondrial"; /id="PRO_0000315952" MVLSRLPACLLPLVGTKVSIQGWLVATSRQVSKSISFHQLRDTHGTILQLLSTDKIILQQKREPLVSSTDFSQQKSTSVMRTLSSIPPESVVQVTGKLQRRPEHDRRPGNEFELHVEDVKLLNVAKNLQLFPGDEKPGMRIQLANRHIQLRAPKYNSYLRQRSRLAYQVHSFFNDREFCEVETPLLFKSTPEGAREFVVPSRLNPGKFYALPQSPQQYKQILMASGIGNYYQIARCFRDEDLRFDRQPEFTQIDLEMSFVDKPHEIMEVVEDLLVRLVSFAKGITLAKPFQHITYQHAIDKYGSDKPDIRFELPLKNITSLLPKQDPLISTEILVYNDLSHSLSNAESRKLCEAVGENVVVTSIREHSQLQTWVKKLPQLRQLPIVAEELNQKLQIGINSIVFMTNRPKYLVSGTTPLGKLRLLLHELLVKKKALPELDKDLLKFVWVVDFPLFSPTEEKNQSITSTHHPFTAPHWDDVHLLEKKPLSVRGLHYDIVVNGIELGGGSIRIHNPDIQRFVLKDVLKLPENRYATFEHLIRVLSSGCPPHGGIALGFDRLAALLTNAPGIREVIAFPKTSSGADLLIGSPSAIPEEMLKDYNVAITRQTQNRN O94246 GSH0_SCHPO SPCC737.06c; CHAIN 1..287; /note="Putative glutamate--cysteine ligase regulatory subunit"; /id="PRO_0000310836" MIQNEKKHLILYTGDVTKNLKSGIWNASRIKSNLELVKALENVKLTKFTGDGDENLKKNIKVLVPVNEKPQKLDGKQEEYEIIVKLFFLDGENIDIKKREETLSQVFYNLHMLFGIDFVSTLVVSFPHITFLKESGNSSSNEIYDSIDEIPPQEIQSWVDTWKLLEEKVGEGKIGTLGVSEFGVNELQRLISSVNVVPESTQINIGQNCKLPNDLLNFADRHHLKLFFHSDPSALLSESEITSVIHKACPEIPNPARVDWVIRYTILTRHTAVIHQKGYIVQSTYTE O94250 GLO22_SCHPO BINDING 63; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 65; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 67; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 118; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 139; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 139; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 148..150; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 178..180; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 178; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 250..253; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16775" CATALYTIC ACTIVITY: Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925, ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6; Evidence={ECO:0000250|UniProtKB:Q05584}; CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione + H(+); Xref=Rhea:RHEA:25245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=3.1.2.6; Evidence={ECO:0000250|UniProtKB:Q05584}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q16775}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775}; SPCC13B11.03c; CHAIN 1..256; /note="Probable hydroxyacylglutathione hydrolase SPCC13B11.03c"; /id="PRO_0000337690" MSFQILPIPMWVGTQDNYAYLLLCEETRQAAIVDPAEVNVVMPILKKKLKNKEIDLQAILTTHHHADHSGGNLNLKKEFPHVTIYGGSDQNGVSHVLQDKETLRIGNVQIEALHTPCHTRDSICFYAHSSNEHAVFTGDTLFNAGCGRFFEGTAAEMHIALNAVLSSLPNNTVIYPGHEYTKSNVKFASKHLQSEALNHLEGLCNHNQFIAGHITMGQEKQFNPFMRVTDPELQKHLGLNDPIKVMDELRTLKNQG O94252 YOR2_SCHPO SPBP8B7.02; CHAIN 1..261; /note="Uncharacterized protein P8B7.02"; /id="PRO_0000304122" MNDEESHISVLPVMNKQTSLVLQNLKEETENQLKELEKKRSQLHKEEQINLQLVYAINDLRSKTKELKAENEKEDTFLNSFNASGDLTANKKIQLREQSRKLEESLLSYHKKVKEMEKQHRSASSKLELAKLSAQQLQTNVNVLRSQNNPEILQDMISETKDCRSLIAEQLLQSASLLNDFQNDSDRIAKNHSSLIDTSRAHRVSLTNATKNYTHIFDSLLTFTRHDSEDVSTSVEKLTSKKISELEKLFADYCSIEDAFD O94255 CAN_SCHPO BINDING 163; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 165; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 219; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 222; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; MOD_RES 111; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP8B7.05c; CHAIN 1..328; /note="Carbonic anhydrase"; /id="PRO_0000311757" MLPPFGALTTTKIPLPKTILQSTFNQIKSSSYSIIAAPRLTSRFIRFPCNYNSCLQSISFSSLGRKRLFFSSSQLLEKSDKKKKMPDRLKRRIEEIDHQDEIIDREASTASPVSGAGKIDQNGEIKDLLERNLTWSQQTSRKYPSFFTATKDIQTPQVLWIGCSDSRVPETTILNLLPGEVFVHRNIANVVPRSDINALAVMEYSVTVLKVKHIIVCGHYGCGGVAAALGPNLNNLLDHWLRHIRDVIEDNREELDAIEDPQLRRLKLAELNTRAQAISVTRVGFVREAMEKRGLQVHGWIYDLSNGQIKKLDITDAIKKAKYGTYDS O94256 SET6_SCHPO BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 52; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 62; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 65; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 71; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 75; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 83; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 87; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" SPBP8B7.07c; CHAIN 1..483; /note="SET domain and MYND-type zinc finger protein 6"; /id="PRO_0000316541" MDAPLIASVILPEFGKGTVATDNIPIGKIIIRKRVDILSLDSANLTRTCSTCTEEKVKTQRCAACKIIHYCSKGCQKADWPFHKLECKALQASKQNGILPSVCRLLIRLYLLWQKNPAIIEPMEGHQNEFQAVSSSWSDAELIASAASHYTQIYQAELFQKLFCRLAVNAMNLVTSSFDSLGMCLDTILCRLNHSCDPNCQIIFDGAIVQLVSKRDIKKDEQLFISYIDIRLPKSIRQKQLLKKYFFSCYCPRCENDHTTKETDGSKWMGRLRNSKSLMKNLAMARDLWSCGWKQTAFPWSNLLHHIKLGMLDESNFNGAFAALYLKSSADEFLDALHVVDEYQLLLLGKQVAMEVKHLMFPNDKPLEMEFPSSSQPQQTVPTNNSLFLLKNIPSFGGLHHCILGRYSISLDDFVLWLLDRAQRLQQAVRISHPSTTFCSNVENDIKEIFEVCKDYCMLHVQNNLKAFEEKLWAACKDFLVTY O94259 UTP16_SCHPO MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP8B7.10c; CHAIN 1..327; /note="U3 small nucleolar RNA-associated protein 16"; /id="PRO_0000343135" MQSSRKIMILKRNIKGLKSSAIIATYLTLNKLFIDKFCKTQESTYPIHFVHCHFGGIKKFHSHCQLSSSYTNSGQKSFKSFNSLRFIVLKSKTCLLRYKLLIKTFCCITYSKIENLSNTRMARLTAPSKGPSFSNLNKPNDLLKAEIEDNEASHYSQNQSSDSDSDEAPEEVSLKSSSDEVKKRLQRLKGNELQLRKAEREKRRLQNERNRERNAQRVSASKLDLAILEAAEVEEINSTTEIEEKVDEASLDLYTPKGHKIVFPNNEIPKKRTRSFRKGDFKVSVLKETNDPLLAPNYEKKLSQRKRDWINRQSVPRASKRRRPLTY O94260 G3BP_SCHPO MOD_RES 145; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP8B7.11; CHAIN 1..434; /note="Putative G3BP-like protein"; /id="PRO_0000194802" MTAENATLLEPVLGKDEIGWMFVQEYYTYLNKEPNRLHCFYTKKSTLIHGDEGESISLCHGQQEIHNKILDLDFQNCKVLISNVDSLASSNGGIVIQVLGEMSNKGKLSRKFAQTFFLAEQPNGYFVLNDIFRFLREDVEEEEESPDAVEKEKKDVASEPYVNGVQSQEHLPSAKEEGHYQDPAATENNFATAALISNETDSLNQATLAVPEEPVIQVTEASVPSFVSQQENQLQDEALTSNSKNADAIGASDANVATAPKSWADLIARNHPDVKSQASVSSTASTTGQTVKGVNADQTQQPTAPYTQSNELLETSVFVKNIPPETSDVSLKSAMSIFGPVKAIEFARRKGTAYVDFVNHECVQLALNKKTLQINNATLNIEERRRLFSGKFNKSGDKKSNDNYNGMKRNFRKGNRGAFDGRSKEVTTSKKQNN O94262 VAC7_SCHPO SPBP8B7.13; CHAIN 1..251; /note="Vacuolar segregation protein 7"; /id="PRO_0000351433" CARBOHYD 18; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSEPKPMQMSVETETVLNVSQVQIPSSCDRKASLETLKTKKNAQKKKKISLPNVMTSKAAMFAARVASAVDQDPNDEESENFVYENLIPTNDDELHSPSASIHSFQTYNLPLEMLPTINHVPYYGSAGTNALNGGPLSNSRKLIPKRSAKFSSMVGSSDTRCNSPTTARGLATSPLQINPTTSKSPLLNKKLSSTSQEPFRTSRRSGQESGDVTTKMLRNLLHKRLWISFFFACFVVLSLVYFHYAVQPLL O94266 THI22_SCHPO BINDING 76; /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"; /ligand_id="ChEBI:CHEBI:16892"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+); Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:Q08975}; CATALYTIC ACTIVITY: Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP; Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7; Evidence={ECO:0000250|UniProtKB:Q08975}; SPBP8B7.18c; CHAIN 1..551; /note="Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2"; /id="PRO_0000315973" MPYNPLYESLSNQFDPSRIETVLDPMGYTIKRRALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQGLDISNINSVSDMERCAAVIHKLGPKHVLLKGGHMPVNNLGLKSSDDEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAITHSPPINNCSTNILNHMTRLRIVPFAPGHFIEYILSHPQVVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIEEKELHVSMCSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYFCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPYYEYVTKQNLEDKEFS O94270 ERD2_SCHPO SPBP8B7.22; CHAIN 1..212; /note="ER lumen protein-retaining receptor"; /id="PRO_0000194170" MTFFSALGDMAHLAAIFLLLHRMKKSKTCSGLSLKSHLLFLLVYVTRYLNLFWRYKSLYYFLMRIVFIASESYICYLMLMTLRPTYDKRLDTFRTEYILGGCAVLALIYPTSYTISNILWTFSIWLESVAILPQLFMLQRSGETESLTAHYLFAMCLYRGLYIPHWIYRIAVHKKVIGVAILAGIIQTVLYGDFAVVYRRTVLQGKKFRLPA O94278 THI5_SCHPO SPBP8B7.30c; CHAIN 1..857; /note="Thiamine repressible genes regulatory protein thi5"; /id="PRO_0000351074" MCPSDFSSRSLFLEAKEEEYKQRRRVPLDSRRRVRRACLSCRAKKIRCSGSEPCQACIATPSQCKYADSLKERTPSKQFIAELSQRQKCFEYLMELLCPSLPHDTRSLVKLCKHVESSLASGSDVRSLLIPGSIDQSVLKVAATNNKDDSSAVKSANVSFPSSSTPPSSDSNFSSIQNTDLNTSIKFTENISANAIHVNQDKVIRSANNLIINSQPILPVRSFLDALGEPIYLSPTSSTYFLNSVLASLQLNSSNTPESLLIDYQSKIPEDLSSSLLPLELNTLQSTPTSVSVGSASSQGTHEYSIINLTSNHSSFSLKALKKIAHNLLPPVSVAERYANEFFLRYQSFFYFYPPSVFSNRYQILADGLVNSDTLDTGFLAVALLIVVLGHFSNNNINVLPKEVQLSHIDSMIQISEQLISSLLNRCTLSSIQAVFLLSLYHFLTGNFKCAYSYLGFAIHSAHTLGLEHGSTDNSTLNEVSTEETSIRICWSLRVLASFLYIQSGITPIINLFPNGLNSLKLPTVVPELEARHLPSSVFHFVAIIKYAEISVRSLNSLYESSSDYLMDVSNFPKLLLKVERIYSQARNWKLNLTHQQLNGTNDTSDLLFHSNVSLHLFYHYLIVKVSCPIMFFYLNNWYSVKPSSFTKGLNNKPSLEDVFSNLETCYESAKAIVQLSSKLLSAGQMDKCFYLEFEILYCSAIVLFLFSVMHLGAENPLLESIYLLEDMGSRTIDSKVRLEKLKSAIEIFDINSATEMPINEPLSASFESVNKENSQSGYMAWQNWVTELSSSNIPLGHALGNPESNNSSNSFKPSHPSQSFLVNESLDFSSNPKEPPFLPWSEALLNMDMQLNRLGP O94279 MGDP1_SCHPO ACT_SITE 14; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q96GD0"; ACT_SITE 16; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q96GD0" BINDING 14; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q96GD0"; BINDING 16; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q96GD0"; BINDING 137; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q96GD0" SPBP8B7.31; CHAIN 1..172; /note="HAD-like hydrolase superfamily protein P8B7.31"; /id="PRO_0000352835" MVKNIEFPKCVVFDLDYTLWPLWIDTHVTAPFKPSKNDPGVLIDKYGTEICFYSDITGILQELRNQKVTLCVASRTCAPKYAKQALNLMKVPIDGSLKPAIEFFTYVKAWPGSKMDHFKEIHNESGIDYREMVFFDDESRNREVERLGVTFLEKIKKNSLNILSFLKNHMHG O94281 CSK2C_SCHPO PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}. SPBC2G5.02c; CHAIN 1..254; /note="Casein kinase II subunit beta-2"; /id="PRO_0000068256" MSRKNLIKLNHDPTVTYSTKDDADELFDDLSSSPLHENVSWISWFCSRPGREYFVEVKEDFIEDLFNLTGLNLAVPFYNEALDLILDRTAPDTLENFDMDVIETSAQILYGLIHQRYIITRTGLHQMAEKYSMGIFGCCPRVNCCYTHVLPAGLSDIVGKMPVMLFCPNCLDLYAPSSSRYKNIDGSFFGATFPHLFFESYPELNPKRSIPCGKIYQPRIYGFKVSELSKTGPRMQWLRMYLEDSGSDSESESD O94288 NOC3_SCHPO MOD_RES 120; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC887.03c; CHAIN 1..747; /note="Nucleolar complex-associated protein 3"; /id="PRO_0000173482" MAARKNQKSPKPKVASSKLKNIKKSSKRNNSQSSTEPRKNATSLDSKKTTKKGVALPEIAERELTQEDIEFFNENPSSLKYLSSINPEDLGKKVEKGPRPDIYDLKKSQQFELDTSRLSSDEESVLDYSKDSEDEQDYELRPRVSSSWNNESYNRLPIKTKDGLLQNVVADVNNGEEFLSESESEASLEIDSDIKDEKQKSLEEQKIAPEIPVKQQIKNDKEALGIQAQQLLEEPVENLHLIRNIFEKFDSPYITIKKLSLLTLLAVFRDIIPGYKIRPLSEEEQGTKLSKEVAQRWEYEQTLLKHYAKFLQTLETILKSFSSTLDETQLSLYQVAVRCCTKLIEQASHFNLSEKLFALAVRQISHKTKRPGFDGIINSLKNIFEEDNLGKTSLKCVTILSRMFKQRNYDVLPDVYDLFLSVNILNDMKIKDEAWQDDTTNFKKRKKDLPYLTKKARKNYKETKKITQEMKEADAVITAQDKEKYQSEILKIIFITYFKTLQLKGKLIGNALEGVARLSHLLNIEFLGDLLQVLRELVMDDTVFLPKDKSGVQATREALLTVSTAFEIASAQGVGKLNLDLDLGLFVQRLYKIIFPFSLNPDADLNLKIKRLKDPDAPSKPFVVNATTEMEMLLKCFQVFFFKSKNISSSRLSSFSKRLAIASMQLPEHSASADLALLKKLLSRYSKLSRLLTSEEQIGDGIYNPFIEDPDLSNSSTAVLYEPFLLKNHYSPAVSQSAKELLKSTSL O94291 SNX3_SCHPO BINDING 66; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 68; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 92; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 97; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250"; BINDING 106; /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)"; /ligand_id="ChEBI:CHEBI:58088"; /evidence="ECO:0000250" SPBC887.06c; CHAIN 1..143; /note="Sorting nexin-3"; /id="PRO_0000238590" MDKLSRPEIRQQTTQQMYDVPENILEIDVINPQTHGIGRNMFTTYEIVCRTNMPYFRLHNSSVRRRYSEFEKFHDMLERESGRVSIPPLPGKIFTQRFRDDVIEERRQGLENFLRLVAGHPLIQTHSRVLSSFLQSPEFKPTP O94295 PUS2_SCHPO ACT_SITE 97; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 157; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a uridine in tRNA = a pseudouridine in tRNA; Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC887.11; CHAIN 1..451; /note="tRNA pseudouridine synthase 2"; /id="PRO_0000057531" MTSISKRKNQQEHIPAEDLETPKLPKREKIEGTKESNKVRIIILLGYSGYGYHGIQINNPLKTIEGDVVAVLKKLGYLKTNNIDAEHLCIARAARTDKGVHTLRNLISLNLFVDKPLDISLLKTELNEALCSQIRVWSVFPAPKYFNPRISCESRTYEYLIPSFALLPPKPSCPLFKKMQKNLSRKLDNELERNLVYSMNDLISFWNTVKLKQKEIQEMFDTNKDAFTNPFKGMFYEKPIPAGIVIPPQAKLKKALKQAEYYCYMNYRIKEDRLKVLQQLLKKYEGRHNFHNFTVTDDSTSPSNYRFIESVTCGTPFVYENWEWIPVTIKGNSFMLNQIRKMMAHVLMIIRSCAPTGLIDKAFDPNITMNISKSPGHVLLLKDIKFSSYNDSVTDGLEKIQFDCFEEDILSLKIKTIYPDIIKLEQKEKLFFSFLSYIDQHTGHQFDYLFG O94300 YOOH_SCHPO SPBC887.17; CHAIN 1..625; /note="Putative xanthine/uracil permease C887.17"; /id="PRO_0000316575" MSITQKVRNWVEEFDVIVARSAFGRWFRLEGCGHPRERKGSRFSLEISAGLTTFFAMAYILAVNATILVDTGGTCECTEANRDDCDKLDDYVLCKEDFHRDLVTATAAISALASFCMGLFANMPVGMAPGMGLNAYFAYQVVGYNGTGRVSYREALLAVFVEGFIFTGLTVIGLRQWLARVIPASLKFATGAGIGLYLTIIGLSPSAGLGVIGHSSSDIVALGGCPPEYLNADYSCNGHQLQSGRMWVGIFCGGVLTAILMMYKFKGAVLAGIALVTITSWPRRSLVTMFPHTLTGDYNFDFFKKVVSFRKINRILVAQQWNVTGGQFAIALITFLYVDIMDMTGTLYSMANYAGLVDPRTQDFEGSAVAYIVDALSISIGSLFGCSPVTAFIESGSGISAGGRTGILGMVVGICFFISLFFAPIFSSIPVWATGSTLVLVGSMMMKSTTLINWSYLGDSIPAFITIALMPFTYSIAYGLIAGIICYALLNSIIYAIDKMSRGRLVPADYNQKEAWTWRVEGGLLPQWVRRLFKGNRRFWEDPDDRKAMDNATLEMATSRSYSEDGKNEKTTHEDVTMKETSLKKMDDERISVDEAVGESESFSNRQQDFRTPYAGIDMDTDDRI O94309 GBG_SCHPO MOD_RES 69; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPBC215.04; PROPEP 70..72; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000396773" CHAIN 1..69; /note="Guanine nucleotide-binding protein subunit gamma"; /id="PRO_0000194810" LIPID 68; /note="S-palmitoyl cysteine"; /evidence="ECO:0000250"; LIPID 69; /note="S-farnesyl cysteine"; /evidence="ECO:0000250" METEALLNEKISVQQARQEFANYANNIPEPMMVSVAPPKANPSVSSKTKQQQHFKPGKATKDKATTKCCTIS O94311 YH56_SCHPO BINDING 6; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 9; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 21; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 32; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 35; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 47; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"; BINDING 50; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01145" MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC215.06c; CHAIN 1..180; /note="UPF0743 protein C215.06c"; /id="PRO_0000373990" MVSFCCEVCQDIIKKPKLDQHRSRCHGAYFTCIDCNTTFERTDYRNHTSCMTEAQRYQKGLYRPTKKELKKAKMNGNAVNSKELSPNTDNQNTPAGPTKHSLDENEKDKENKKSKKETVSSPAEQLLALTQNQEISLYKLLKKYNKQASKEDSLDSKEVLKHLAITADAKGNYLVKPITK O94328 MU118_SCHPO SPBC725.12; CHAIN 1..141; /note="Meiotically up-regulated gene 118 protein"; /id="PRO_0000278506" MMNKRKRVEELGETKHRQVRQRILQEHKNDILENLAFELSDKVRRLRSNASLLASTIRMRGEMRIAAIPRAQRNMHLRDLKNHLSCNVSATPWRTKIKEFYNLDELSSQKSARQPTKTVASSSSSSSKSTTVSKSSSKSQV O94330 NAGS_SCHPO CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1; TRANSIT 1..19; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC725.14; CHAIN 20..500; /note="Amino-acid acetyltransferase, mitochondrial"; /id="PRO_0000372579" MQKPSLSQDLIWILKSVQSRRSTKGFLQKHSSLKDGSPNKKSFAQPISSSFLNRISITKIDDVDSLSDNTLYGIGRSINSLARLGIQSVIVPTSNPIGMTSPFKYLENGTVVAKKRKLSIFEELQQQQNRVIRVSEIFSKAGVLTRPSYSSVCQLGPEGPSVENVQGIFQALSSLYTVIVPSSILMPNVIEVPIDGNEVLAGLTYSLHKPNFGFWVDRIVILDKNGGMPCSKRQTGSSHVLINLAQEFDELAKTLPPYHRKNLILVRRCLKMLPDDASALITTPEDAMLTNPVLDKNPLIHNVLTDRSIISCSLPRDRSPITKTTVLRSGVPVYTFLGPKCLTDGSVSWERLWVLINDSFKRTLDMDAYLDRLKNSLAAVIIAGDYLGTAIVTYEQPDGTTNEKVPYLDKLAVSQGAQGSAAISDVMFNVMTDLFPKELIWRSRLTNPVNKWYFERSVGSLKSSKTPWKLFWTGDSHVRNLDRVNQYMSVIDKIQPTWLN O94331 PYRE_SCHPO BINDING 25; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 33..34; /ligand="orotate"; /ligand_id="ChEBI:CHEBI:30839"; /evidence="ECO:0000250"; BINDING 71..72; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 98; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 99; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 102; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 104; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 124..132; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250"; BINDING 128; /ligand="orotate"; /ligand_id="ChEBI:CHEBI:30839"; /evidence="ECO:0000250"; BINDING 156; /ligand="orotate"; /ligand_id="ChEBI:CHEBI:30839"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; SPBC725.15; CHAIN 1..215; /note="Orotate phosphoribosyltransferase"; /id="PRO_0000110800" MSYKLELLRRALEHNVLKFGTFTLKSGRKSPYFFNSGNFTHGADLCALAEAYAETIIAMNVDFDVIFGPAYKGISLAAITAVKLYEKTGKSYGFAYNRKEAKSHGEGGNLVGAEMEGKKVLLLDDVITAGTAIREAISFLEPKHVKLAGIVLLLDRQERLDPEVNESTIGRLKKELNLPVSSILTLDDIVDFTKSDLTAAESKAMDAYRQQYQAK O94332 RRN11_SCHPO SPBC725.17c; CHAIN 1..200; /note="RNA polymerase I-specific transcription initiation factor rrn11"; /id="PRO_0000097446" MFSPCTVKEKRSTLRSVAPNPESSVIPPIPLPSRRYKTRHIDALCSLMHLCLLRKDYPRASRAFSLLLRSKSVDISKLWNIGLEILNKVNPEASSEYMERLIARYPARPSINNSYPNRNAEHFFPAYIMLLIQRQEYNKAMKLLDEYLLLPPYNQNPALHEYSGMLCFELAKEEASESERTKWIEKAKYNFSNAGIDVEL O94334 POF13_SCHPO SPBC1271.01c; CHAIN 1..396; /note="F-box protein pof13"; /id="PRO_0000119978" MRPTHWSSNQCEVDFTAEALTTLSLSNRNHEEDPIQPVLKNSNLFLLNRDIWSLIINYLDAFDILRLMHSSRQFYYWLRKSAVDECCFNNNFLNLQPYQRTVPVASDLEWATEVDLYGNPPILKLQLRDSFVWSMLAKFQGLQTIALDGTGVTISSVTNILLNIPTVKTLSIRWCVGVCSLSLIEFLQNSKSRTFSLENLYVLGVKGLELLKPVLLDGSEDDTLTSNWHSRVILFQNALDALPTTHGNPVECDISRCPLNACKIAGQETELADLFSLQKVPACIYCLREWKKPICRYCIDLRSCLVCDSFVCPSCISLDFDLQIQAFARQHRVISTLGVVYPEREDSCFHKIKAAQWHQISPRSLLFQFQEQNHIHHKKIRRKLLAAGWKWPQSQI O94337 DHYS_SCHPO ACT_SITE 322; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 96..100; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 122..124; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 127..128; /ligand="spermidine"; /ligand_id="ChEBI:CHEBI:57834"; /evidence="ECO:0000250"; BINDING 128; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 229; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 234; /ligand="spermidine"; /ligand_id="ChEBI:CHEBI:57834"; /evidence="ECO:0000250"; BINDING 276; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 281; /ligand="spermidine"; /ligand_id="ChEBI:CHEBI:57834"; /evidence="ECO:0000250"; BINDING 301..302; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 307..309; /ligand="spermidine"; /ligand_id="ChEBI:CHEBI:57834"; /evidence="ECO:0000250"; BINDING 316..322; /ligand="spermidine"; /ligand_id="ChEBI:CHEBI:57834"; /evidence="ECO:0000250"; BINDING 335..336; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine; Xref=Rhea:RHEA:33299, Rhea:RHEA-COMP:10143, Rhea:RHEA-COMP:10144, ChEBI:CHEBI:29969, ChEBI:CHEBI:57484, ChEBI:CHEBI:57834, ChEBI:CHEBI:82657; EC=2.5.1.46; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; SPBC1271.04c; CHAIN 1..350; /note="Probable deoxyhypusine synthase"; /id="PRO_0000134486" MDESLAKDAVFVASSKPSDLTTEVVGPDFNKYDERKKAGGPGITVEELVESYGKIGFQATNLHDAVTIINEMRNWRDPNPPEEKSDRATIFLGYTSNLISSGVREVLRYLVQHKCVDVIVTTAGGVEEDIIKCLGPTYVGDFHLDGKNLRAKGLNRIGNLIVPNDNYCRFEEWIFPILNKMVEEQETLGTHWTPSSFIRRLGKEINDESSVLYWAYKNNIPIYSPALTDGSIGDMLYFHTYKATPRPLVLDIVADIRNMNTHAVRANKSGIIILGGGVVKHHICNANLMRNGAEWSVYINSANEFDGSDAGARPDEAVSWGKIRGDAKKVKVYGEVSLLFPLIVAATFAK O94347 NNRD_SCHPO BINDING 121; /ligand="(6S)-NADPHX"; /ligand_id="ChEBI:CHEBI:64076"; /evidence="ECO:0000255|HAMAP-Rule:MF_03157"; BINDING 174..180; /ligand="(6S)-NADPHX"; /ligand_id="ChEBI:CHEBI:64076"; /evidence="ECO:0000255|HAMAP-Rule:MF_03157"; BINDING 209..213; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03157"; BINDING 228..237; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03157"; BINDING 238; /ligand="(6S)-NADPHX"; /ligand_id="ChEBI:CHEBI:64076"; /evidence="ECO:0000255|HAMAP-Rule:MF_03157" CATALYTIC ACTIVITY: Reaction=(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate; Xref=Rhea:RHEA:19017, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074, ChEBI:CHEBI:456216; EC=4.2.1.93; Evidence={ECO:0000255|HAMAP-Rule:MF_03157}; CATALYTIC ACTIVITY: Reaction=(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate; Xref=Rhea:RHEA:32231, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076, ChEBI:CHEBI:456216; EC=4.2.1.93; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03157}; SPCC61.03; CHAIN 1..327; /note="ATP-dependent (S)-NAD(P)H-hydrate dehydratase"; /id="PRO_0000315959" MTSGSPKITNLLTRVKRIIPPLLDTFHKGQAGRVGVFGGCQHYTGAPYYSSMSSMLFGSDQSHIFCEKEAANVIKSYSPDLIVHPFLREKDKAGPEDSVDKCFELIKPMMGRLHAIVIGPGLGRDEWMQEIMAKVIEYARKNDMPMVIDADGLWLIQQRPELVSGYHNVILTPNVIEFKRLCDKLDIKSDGPDACNQLAGKLNLLIIQKGQSDIISDGATAYACSVPGGLKRCGGQGDILTGILATFLAWRHAYLSKEWDTEGNMDAKECLFLAAFGASACTRWCSRLAFKECGRATQSTDLVRHVGKAYNALMEDEIPSVEEKIKD O94348 YIP1_SCHPO SPCC61.04c; CHAIN 1..227; /note="Protein transport protein yip1"; /id="PRO_0000232732" MAYYNNPANLQYYDYSYTADNSFNTQSRAAGFYDEPLHEPLSQGWLAAFSTSGYPGEPSLLEELEINFGHIKQKTTHVLNPFKHVDVHIMDDTDMAGPILFCLLFSTFLSLHGRSHFGYIYGIALLGSLSLHFVLRLMSAKNLFFTRTVSVLGYSLLPLVVIAFFKNIFTFNGIAGYALAALACIWCTYAASAMFVGILQVNNMRFLVAYPIALFYGVFAVITVFSK O94350 CBL_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate; Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; CATALYTIC ACTIVITY: Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) + pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 202; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPCC11E10.01; CHAIN 1..390; /note="Cystathionine beta-lyase"; /id="PRO_0000352810" MPSDCKYSVDTELVHVEGNEDQYHASSVPIYQSATFKQPCLEHMGKFDYTRSGNPTRSVLQVHLAKLMKAKHAFVTSNGMSALDMILRCCKSNSHVVAGHDLYGGSDRLLSFNQRQYGFKVDNVDTSDLAAFEAALRPDTNLVLIESPTNPRISICDIRAIVKITRSKAKDALLVMDNTMLSPVLCNPLDFGYDIVYESATKYLSGHHDLMGGVIATKSDEIAKSVFFNINAMGAAMAPFECFLLLRGIKTMGLRVERAQQNAIEIAKFLKSKGLQVNFPGLDPDAKSTAIFYSFARGPGAVMSVFTGDVEVSKTIVNTTKLFEISVSFGAVNSLISMPAYMSHASIKKEVRDARGLSEDLIRICVGIENVDDLKADLENALAQANFKQN O94355 RTX2_SCHPO SPBC428.06c; CHAIN 1..240; /note="Transcriptional regulatory protein rxt2"; /id="PRO_0000374023" MKQFEEQIERFKQALFEDSDASDSDSSIGEALTNRGLKRKKGSKNVYYGCVGNSSGSSIDIDYYNIGNTKRGVVSHFRRRIDPEWLDHDNPYNDINIAEIMSPLTKPQDLLTHPAISSIFEQNYLSILASSALEIISAEHKYTAHLEQLMVALLGDDPSLPGPPHEVFGISPEQCRELTITVQEALEKSKEFIRCWTNVRMDLLRAIRFKNKVIAYCQGEDYNGNTQVLSKNESDGKPNS O94365 UTP15_SCHPO SPBC428.19c; CHAIN 1..494; /note="U3 small nucleolar RNA-associated protein 15"; /id="PRO_0000307922" MSAPAGRLQPQRFAALPNPVTAENKFWRSFKVPVVAKEYSAITSIHFSAESPYDFAVTSGARVQIYGASSRSVKKTIARFKDTAYSGNIRKDGKLLLAGDATGLVQIFDLSTRSILRALDAHQFPVHVTQFCPYANTTFLSGSDDKTVKVWDLSTGAVQYDLSGHEDYVRTASWMSATRLVSGGYDGTIRLWDTRIADPEVMSFSHGEAIDVVLPMQSGSTVISAGGPSIKVWDLVAGRQTPTKKLSNHQKSITCLAMNSENTRLLSGGLDGHVKIYNISDWKVVHGMKYSGPILSMGLSPDSCNLVVGMSNGTLSQRTRRITKQTSSKTPFLGGVGSAFGVVGKKKQIYKGENDEFYVEEARRKRLRPFDKALKSFCYSDALDMVLENGSPVLIITMLIELLHVGGLRIALSNRDDLSLTPLINFLRKYIRDPRFSETLCIVTSTILDIYGAALGGSVMVENAISKLREKVEQEVAVTQRANELVGMLQMLSA O94368 PPR1_SCHPO TRANSIT 1..36; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1604.02c; CHAIN 37..697; /note="Pentatricopeptide repeat-containing protein 1, mitochondrial"; /id="PRO_0000352820" MLKRAHYVALHVTLNHNGLSYQRVFSCLTQFPMLRHSSTAAKNNVSMISKFQAPEDKFFPSFSLKSMPKQSSHMSASLLNSLNTSMKKSFSRKKYREAVSLFRKNLWKYEESWIRNQDFIDCCIIACSAYEKLCQPLRIKKTFIILSQLCPKLPAELCRVFLSYATGCVNYGHNVALTCFENSPKELIDYNYWLSWLSFSKSSPVVLWLTFTRISSAGLSPNAETFEILLVAFASQKNFWFFEKTYDLFMQSKLTWRPFTYRVLIESFMKFGNFEEAEKLAYSYVKNKIDSLSSDVFFSAILKFYAVGGDFQGFKKLLSFMTDYNVNFSVSTLNQLLRLNLYHAMDEKISTFSSEHITKLIEQQIKPDLESMLIISEYLNEYKPSPKMRELINWLYSNFHLPKTVSLHFLREVQSLVFRYPLLHSKIHLAISTLKDSGCDWNVGLSYLNWLFVNKRITEAINFFYTITINAGTRPPNELFDVFISNLLKFTSAETTSSAIRKVQSKYPSMCGSSPAIKLILFSKSFSVLQSTSEKIEQLLVSFQRNPSAYSKSFTLALAEWLFSRRLFQSALLYSFKVSDVDDSHFSFRSQILICWCYYRLNDFKSLIQHTNNLLQSNNASLLRRLAATLYRIQIRENNGYKRVLLDRLRKKAILRAFPSRTLNRTEKVKLYNEDAKFRSIFSRVLLHQSHLGNVIS O94375 REXO4_SCHPO SPBC1604.09c; CHAIN 1..260; /note="RNA exonuclease 4"; /id="PRO_0000131699" MSSSNWEKLKKKLDSAKSGRVEKKHSNEKKYLKSVKGKNNENENSYIVDKKRMNELKKFAKENDIPESQVLDAYGVDASKLTRKTNLETLGKYIAMDCEMVGVADDMSVLARVSIVNYHGHVVYDTYVRPKEKVTDWRTWVSGVKSFHMRDAPSFEKVQAEVAKILDNRVLVGHAVHNDLKVLLLSHPRRMIRDTSRFSGYRKLAKGRTPGLKKLAEVILGRDIQSGQHSSVQDAQATMELYKKVKKEMDEVAFKGLSKS O94377 ATPK_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1604.11; CHAIN ?..96; /note="ATP synthase subunit f, mitochondrial"; /id="PRO_0000002636" MAPFPLKSFIPPQVANPTALNAFPSSARMGRIVDFYSRLPHGPAPKKSSNSFFSWYYKKYLGKNASGAPLLHLVGAVLVFSYASEYYYHIRHHEEH O94379 RM32_SCHPO BINDING 77; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P25348"; BINDING 80; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P25348"; BINDING 90; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P25348"; BINDING 93; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P25348" TRANSIT 1..47; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:P25348" PTM: MRPL32 precursor is processed by the m-AAA protease, which cleaves the N-terminal transit peptide (By similarity). Cleavage by the m-AAA protease takes place prior to assembly into the large subunit, an essential step for mitochondrial ribosome (mitoribosome) assembly (By similarity). Proper processing by the m-AAA protease is dependent on the zinc-binding region within the tightly folded C-terminal domain of MRPL32: zinc-dependent folding halts degradation initiated from the N-terminus and triggers the release of mature mrpl32 (By similarity). {ECO:0000250|UniProtKB:P25348}. SPBC1604.13c; CHAIN 48..103; /note="Large ribosomal subunit protein bL32m"; /id="PRO_0000030517" MALLRGNSLAISQKMLSVFQASALPHISLRIFISPPSIANIWNSILLAVPKKKTSYTKKRSRLLSGKALKDKTVNRCPICGSFKLAHHLCSHCFRNIRREFNE O94380 GPI16_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity. {ECO:0000250}. SPBC1604.15; CHAIN 23..545; /note="GPI transamidase component PIG-T homolog"; /id="PRO_0000024109" CARBOHYD 168; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 227; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 336; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 391; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 467; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 182; /note="Interchain (with C-73 in PIGK/GPI8)"; /evidence="ECO:0000250" MKKNGCLLLFAYSLLSFSLTAATIDETYDESLFIKSFSSRYSYVSFAFEIGASTDSTHSSVFSESSFSLFPLSIARVMDECQVSELHIRATRGRWDYENWKESPDNGFYSGGLGFEVWAFMANDPSMKYWLKLTNQLSGLLCASLNYIDSSNTYQPQLSYPGSFSFSNNTQYFASLPQEDVCTENLSPLFKLLPCKRKAGIASLLDSHLFFDTDWHSFSIDVYPSENQSLASVKMGIIIQAVVDVERNGRRKGKTTFQPPSEYCHDEDMDSLHCLMSGYSTEHHTVDDLFHKVPKERCLLSSTFSDVFVSNGDKIDTFSLDEAANIQIPIQSTSDNHTVTVDRSLSNDGNHWGSLSSTIYNPSSSPRTIVYFEKFPWFVRVYLHTLTITLNGTRINTKDFIEKLYYQPLRDRKAGTMMEIQFSIPPHTNLIVHFNVEKTPLRLDEYPPDANRGYNLPPAIISVFDENNTKLCSLRTAALLMFIPTPDFSMPYNVIIFTSTVIALTFGGIFNLLTRRFVPQQSKFQNRQPSMLQRLKEKIFHKKRG O94385 PO152_SCHPO SPBC29A10.07; CHAIN 1..1250; /note="Nucleoporin pom152"; /id="PRO_0000224645" MVTRVASSERPRPLVPESIVDAPTQRLYAIGVFVALQAYKIYDLLKLETSSISDVPKSGFLVKWIIIDAIYLRLLPKFRIPWLSFQPAATLLQIAIFAAINLLLSSLSSLKWISIGSILLPYFKKKELSISEHKINPNNVIHNSSRILGQYTLQVLPEGTAKINPLHENYCLNSLRKDQYVDLAIQFNSTIPKYIQYSHVDLETKEETLVEVSGRSLRKLLSSSSKNPKEPRLQTIYLKTNKRGLYTLKHVVDKSKLDVRIFRSEAVVVSCPTATFASRQSGGRLRERCVGDTDNAELKVTGVAPLQVTYRNWDGKHFNTHIIDSTIPDDFHPPAVVLSSNPKDIVFYKGIDIQWARSSEIFVPINTLLKAPGQWIYAVTQVTDALGNSQQFPSNDQFLLRFAHGYTEADGESHSLPENVYSVFVHQRPDIQFRGCSIESPANLFPNKETSLSLYSSFSEYNSLEVGVDRYELGLDPQNITVPPLSHKTYQISPRSSANINVKKPGIYVLSSVSSQYCSGEVLEPNTCLVVTPPEAKVSVSFEEISDQCAGSIGARADLELEGTPPFTIAYRMTKDNEASRIQYVTTDRTRYQLNFTPKKAGKYRYIILGIQDANYGYRELSGSSFYKDQTVFPLADASFEERRNGDLSTVVKTSCIGDTMSLPVLLTGSAPWTLEYEIFRNNKREESHVVESKDPRYILEVPMLVHGSQYTITLVSVKDSNGCKRSLNTADTVIKVRRQRPTATFYSSDNTYTLKSVEGALMKIPLRLAGEKPWYVEYSHTSGLNKVSHHKEVLNDPNSYLTVRKSGTYTLLSVSDSSCPGTIQNVEQKYQVEWLPRPFLSIPSLESSVKGKTRYYEQNAVCAGDSSAFEVQLSGSGPFLLKHDKILVDEKSKTYPKQKSELSTVQNTVLVKADTAVPGVYHYEFTKLSDSLYSDSDAVTIVNNQSYQAVVLQRVNSLPKASFMNVEKLYTFCINTDVTQSNAQLIAIQLQGASPFSLVIGIKNELTGSVSKYTLNDIHESVYKFAFPQEQLTLGKHVVRLLQVRDANGCAASITKTQPAAKVSVVEMASLAPLGSRQYYCVGDRLSFALQGLPPFDVEYEFNGVTQHATSDSHILTRLIELPGVVAMKSISDHGSHCKSYINPPIEQIVHDIPTVRISNGKDVIENIHEGDQAEISFHFTGTPPFSFSYARRALGKKRPGKVLETHTVTGINEYEYKVLSSVEGVYTVLSVQDKYCRYPQDSTSSSNI O94386 YGS9_SCHPO SPBC29A10.09c; CHAIN 1..427; /note="Uncharacterized protein C29A10.09c"; /id="PRO_0000310341" MEIHGKNFLETLKELEKHVDSAHYVSIDCEFSGLLRDFNLNNKNTLQDRYELLRKSSIRYTILQIGITFIYLQNNGKSSCIPVNINVSPLVKDELHLKRDFCSEASSIKFLIQQGFDFNKQLTEGVPYLSRIEERNLIDKVNERSTDDLTSSILDACDEEILVDARNQIKNWLSSELSHSTSKYLNITTSNRFIRKAIQSLVKIEFPTLKSYPKRTFLQVRKAIENSTTQCSATSKSELKEDIASDQLILNNLNLIKQNVGLRHLWDYILKKKKSVVCHNGMADLVYLFSLFEGKVPETILEFSELCLSSFKSIYDTKLLYLKSDDLQHVSDGIPTDLLSLVSKISLPPVPSNSSSQRSNVSLNSLIECPYKSMMSRKRPHEAGKDSYDTALLFVYYVMRTKHSDIQRWQNVLPIHGSFLDLNKYCS O94388 VPS92_SCHPO MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC29A10.11c; CHAIN 1..402; /note="Vacuolar protein sorting-associated protein 9b"; /id="PRO_0000316572" MSFLNSWRAVKYTNKPKEEDIKLPNSASNLPTTVQACVIQFISSLVSPVHPQLLSPEELAKAFQNFYKHTDEFIASTLIPQPSSKDQNVPLLFPEEIDAQKKARQHLLNQKDEWMDQIEDIVCEYLYDRIFCLSTSTDAAKDDLLKKFIASEEKKELINCIPIPDDEKLTNRLHEVSEAFFALDEQHTPRSKINTFMTVNSSILNASQLPQEELNADSLLNLTIYCILCYPGFHLISHLNFVLRFRNADFLSGEQRYCLTTFEAALTFILRACPNLLTQSSIQPSDDPLSLEVANSETVSTSNSLHDPSAEPYPVNRSSLSNLRNLGLALEKSYASLLSKVANHTAKSSEDSSNSVEFVGDPPLERFLTVSDASDLKIGEIELLLSDYKRLARLLFEKNGNQ O94391 CYB51_SCHPO BINDING 38; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"; BINDING 62; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" SPBC29A10.16c; CHAIN 1..124; /note="Probable cytochrome b5 1"; /id="PRO_0000166033" MSVKYFEPEEIVEHNNSKDMYMVINGKVYDVSNFADDHPGGLDIMLDYAGQDATKAYQDIGHSIAADELLEEMYIGDLKPGTEERLKELKKPRSFDNDTPPLPLLIALIVLPAIAVIVFVKLNK O94401 YQF8_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPCC126.08c; CHAIN 23..312; /note="L-type lectin-like domain-containing protein C126.08c"; /evidence="ECO:0000255"; /id="PRO_0000316862" MFFSVKNVFLLGIFGFVLGALAETSHLERLSLEAPYINHGMRNLWWEYGGSTVIDRKNGIFLTQDVQNQQGWISTRLPTPSSSFEVLFQFRINSESTSLFGDGLAFFLAAERAKPGPVFGFTDKFNGYGIFIDTYNNHRPGTLFPRVIVMKGDGHTPYDYENDGKANEIASCSALNVRGNDYNLGKLKYDKNAKKLRFEIAYQGSSSFIKCFDLNEVELPLTTFMSFSAHTGDLSESHEIASILSRTITDIDDEGTPEIPAEELKGTTYGQKKGSFKKRLIILLLSLIVIFSIFALRSYQVQQEKNRRTTVL O94402 ZIP2_SCHPO SPCC126.09; CHAIN 1..389; /note="Probable zinc transporter zip2"; /id="PRO_0000317132" MNNSKGWILSLSINAFCVFGASGIYLDKLVNKWFGYEVLDLANSDNALVTGLATSSGILLYSSWASVMQESFHFLEKISMFDTFLVRVFQFCAFFFGGIVFYIFNHFLHKWLHESSQTGFLHDHFSVSDPSPSTAQNHRSPPASCKRLSSCESSGSPSSRVVGSLQGSYCPSGTHLHEGSLLLEDSSARHSSDSVHEYLVKKPSNCDCECHAHFSSFPTHSGTPDDIEHIHSVYTMGIQTALLICLHKVPEGFITFLASTVDTGFMVLVAMSIHNIVEGFTIAYPLYLAWKSRPKAFLTAATLSSCSLPLGSLIAFLVMEAGGIGSSDFLNFLYGIIFAGTAGMMLILSLRVILPEALRHDHSENKRHSFICFTIGILFTLFLEIFDSH O94407 SEC65_SCHPO SPCC126.15c; CHAIN 1..213; /note="Signal recognition particle sec65 subunit"; /id="PRO_0000135210" MISHLLPTTSLTIHMPSIILYPIYFDKSRPRRFRCVPKDKAILNPLAKNIADVVRDLGYKCKLEPLKTHPADWVNPGRVEMVLPEKIQKKYVINEIAKVLLLRPTVKTDPLSLPIQNVPARLPENPPAYPKGVLGNTILPLHSPALSGGGISENMFQEMMQEMQKQPGLAGGMNPMAALAGMGGPAPPMPTPQASSSQRKQKSIEPEYDLDLE O94409 WTF23_SCHPO SPCC1620.02; CHAIN 1..368; /note="Meiotic driver wtf23"; /id="PRO_0000193234" MKNKYYPLRSSMDELSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSENINLKDPKQMGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFGVWCAICLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILGGIGNAMMGLANAFRGGNDNNNNIPLGEMDVEGEV O94411 MFR2_SCHPO SPCC1620.04c; CHAIN 1..509; /note="Meiotic fizzy-related protein 2"; /id="PRO_0000300505" MIIKKKESFKSPGRLWRVTKIRKLTAAKKNELQNRKCNQASNEEKKILYKSNFLDRFIPSKANSDAFRIMENAFTEKLNTQESLLPDILNLNVKGVLHYKDNKKQKTTRLIESTNYQRQTIHGASSSLVIEVEENGHLSNMQGSLYETPLRILDAPGLLDDFYISPLAWSTNGELAVALAQNVYLWSEISGPSIMELSPTTYEVSSLAYSSDGGFLAIARVNGFVEIWNRKTKNNRCDYKFHHDGDISCMAWSPINWTLLVGGSTGNIYVYRRTKSMMRRVHTIKKVHQEQVCGLEWNYDGTQFASGGNDNLVCIFDIDSLENKKFYWIHLAAVKALAFCPWQKSLLAVGTGSNDQQIYFYDTFRGHRIHSLFCGAQVTSVIWSRRYKEFCYSLGYSPEGTNSSLIVYRWPQLTKVFDIPSAAIDGWGQDLRTIMAIHTHRKYSNNTWEEGEYVVVANSDETVKFYKIWGNEMQEIHNDRVLYREGIFGSHILEMLENIPEQVLTNGVR O94415 SUCB_SCHPO BINDING 68; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; BINDING 75..77; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; BINDING 136; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; BINDING 228; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; BINDING 242; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; BINDING 293; /ligand="substrate"; /ligand_note="ligand shared with subunit alpha"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; BINDING 350..352; /ligand="substrate"; /ligand_note="ligand shared with subunit alpha"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219" CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_03219}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03219}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03219}; TRANSIT 1..23; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219" SPCC1620.08; CHAIN 24..433; /note="Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial"; /evidence="ECO:0000255|HAMAP-Rule:MF_03219"; /id="PRO_0000033364" MLTRSVLRKAPRAFSPFLQKRNLALHEYISHDILRKFGVDVPRGAPARSGEEAEKVARDLKVTDLVVKAQVLAGGRGKGQFDSGLRGGVRPVYDATEARMFAEQMIGHKLITRQTGPAGKICNVVYVCERKFIRKEYYFAILMDRENQCPMIVASDQGGVDIETVAAENPSAIIKRSLPNSPNLDPHIAEELVDKLGFSSSSKPKAVDAIVKLYKVFNDCDATQVEINPLAETTDHKVLCMDAKLNFDDNAEFRHSNIFVLRDISQEDPDEARAAKVGLNFIKLDGNIGCLVNGAGLAMATMDIIKLHGGEPANFLDVGGNANAEAIREAFSLITNDPKTTAIFVNIFGGIVRCDVIAKGLISVVSALNLNIPIICRLQGTNQGAAKEVINNSGLRIFSFDDLDEAAKKACRFSRVVEMAREADVNVSFELPL O94417 CWC26_SCHPO SPCC1620.10; CHAIN 1..306; /note="Pre-mRNA-splicing factor cwf26"; /id="PRO_0000079607" MHSAHMSNADYIAKKYLRKDQGKKKKKKEKDFVEIQDEDVAGWDDDNSFSLVNRELTSLHDAPTIVANESLKDRDIDAIYQNIEKTTNKPAQLWKAVGNDEVVESEQQDSHDAESIPQFGLLTGKQVTFKAEERRKREEKSSNLDEEELRKSRETVYRDATGRRIDLVLARKEAKRKLKEKEEEARRQKEQQQGVVQVRQQKEYLKELERQKTVPLARYEDDPEYNKELKERSRWNDPAASFLTNKPVSSKATYQGYAPPNRFNIRPGHRWDGIIRGNGFENKWFQRQNERKAQEHEAHMWAIEDM O94418 MUG87_SCHPO SPCC1620.11; CHAIN 1..851; /note="Meiotically up-regulated gene 87 protein"; /id="PRO_0000278569" MTVASDDSPKEARGIPFLDQKSRKLANELLEPCLPFIQFNLGEIEQRAKHYLNTVPTSKDGNTKAHYLLAGSGINAEQTWKKIESLSLQVRPPTTLELSFTDVDMFLKYHREKNVLNSLEALVQNTQIAFDQYLEEEWRSKAAKSRPSFDNILLENKKRVSFYPFSVQRSQKFASTLKMCLEEEALHGFQSKLVSSFCEVAREFAHDTKSLLLYESWKLLSSVILDKDSVTVFGNKGIISKAFDIETEDGSVNSRFYQRISDCSRKFLEAQFFEVLNKEIAKTPQAALVGGVPSIRNKIRAYLNIRLLRNGVWINPDLEIIQDVPIWAFIFYLLRCGFLKEAVDFTEENRDLFEKVAEKFPFYINAYAKAPNGILPRQLRSQLFSEFNQTIRLQESSDPYKYAVYKIIGRCDLSKTSCPSICSVTEDYIWFQLILSREFTEKSVSAHEFFSLEDVQHILLSYGSDYFTNNGSNPVMYFFLLMLCGLYERAINFLYPYFPTDAVHFAITCAYYGLLRTAPSSSVVSNEPGKIQSMLVETKSGKPSLEFDRLLIDYTQTCQELSPVMSACYLIPMCKIDKYISMCHKSLCSLVLSTRDYVNLLGDIRGDGERTPSFLENHRSLIGLSSVKEYLSKITLTAAKQADDQGLLSDAILLYHLAEDYDAAVTVINRRLGSALLRFLDQFVFPDKLISLTKSMMDVYNRNPSLYAKVDYKNRETTNLLLLTVEAFNAYTNKDYEQALSSLQQLEILPLDPLDSDCETFVVRKLAKEFRFLNENLLQNVPGIVLIAMNSLKELYAKQKSSSFGNDAISVDKLRLYRQKARRIVMYSFLIEYRMPSQILEQLNRCEIEMT O94419 YQG2_SCHPO SPCC1620.12c; CHAIN 1..640; /note="Putative GTPase-activating protein C1620.12c"; /id="PRO_0000374036" MSKSVNASLSSAINSVTLVKQENLKENLQNGSAVSVGSSESSNHSMKEISLDYSSPSLQQTEEQDRELNFIDSSMLRPTPPQESDNRLAVEKPNIQPLQGHSPVPSFMSTASTNISSSKINNNQTEFEQLRDSYKSHGDLNSAINDSRIQSIIFELNQQCEKESIPVSNIDWLQWASVPLFAYDLPPDPSNPNATSSSPPPLTPILELIKQNNFCIPSPCRKLVWQSLVSAERNELLTLYATLSTTNNSLDSSIRKIIRMQSFRGPLEPFKYSSTTRHKVSTESIFHVLHAFTLFDTTVEYNIEPLLWLTCAFLSYMAQGNAFRSLVCFIQRGGIREFFISQSSSLDESLFALVWGCLGDLAPSVAISLQRIKVSSLCILYPSLACCFADSLQLPEALRLMDLIAIYGLEMFVRLLVAIFLKDRDKIVNMVSHEQWVKYLRSDVLASYRQPLVQKYTFYTRTPVDLNAWVEDSLALNIDTTQFPSYLSYHETSVSHNTYRQNNLEELKNQNDYLTSQITNLEEGMVMLNKENTKLSEALSNHRVTRSEMEEATEILKNNSADLKAQLEKQPQELENRLLQEISILKQRNQKFLKNNATSIQQIQYLDEELGKTLKQLNDLKEKHAQLQTKWKSVSEMFRN O94424 T2FB_SCHPO SPBC1198.13c; CHAIN 1..307; /note="Transcription initiation factor IIF subunit beta"; /id="PRO_0000238605" MSEEKPTVRTEEDDRYEDDAGDLDLGQIGSRVWLVKIPKFLMDKWNSIPEDDAANLGCVRVKNDEIQLLLQNSPENADVPKIYNLRVMNKFVRNSYVFRESETSSSMKSTALVGTVAHECNVSPVINDDYRRVMQKRALAASAPKRKVQMIDDRGGSLLAPGTLGSRSRSTTSFIRNVKPRTGEGLKNSRIPRNELLDILFKCFEDYEYWTLKGLREYVKQPEVYLKEVLDSIAILNKRGPYALKYSLKPEYKGTMDAASVELRNQQASQSESSSIDHTGKNTSPDNPGTNAEEDEDDDGVEMIDVV O94427 MU167_SCHPO SPBC660.08; CHAIN 1..424; /note="Meiotically up-regulated gene 167 protein"; /id="PRO_0000278515" MVRYSLRKAHEYARDGENQEVLGEISQAIMYYGLAKSQFEKICQNTAQPLIKRCANNQIEELMVRIRELRESLPNKQTPISMSMSTRLSPMYTSSLTPRFTSNSMVLPGDHNTTVRLKPSFREALMEDSEDDLYQMYSKFEMQVKKLSTNYGLAVAFSIVPMDDDQPSPSIFSSDESFLIVEGDDFSLGNSVEEDANATSKEDPAYQNTNEQIQPLSNFDISQQEYLNNTRIPYENEDLHLQHITQGTTDDNNVSKFLIPSYNDAKELSEEEMGRSHKREESFKRAFGHASSSESSIGEITDSREDIQSNRLVNGSWENNDFTKEINNNFPDRSETPTLQTIEAPTKLMKYTRRKSLFRFPFFRSISGKKKEEPMESGTDSLESSTAQITVDSQLKIKQLETQIATLQKQLEQFQTSTLDQDLH O94429 RRF2M_SCHPO BINDING 35..42; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03059"; BINDING 99..103; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03059"; BINDING 153..156; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03059" TRANSIT 1..20; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03059" SPBC660.10; CHAIN 21..813; /note="Ribosome-releasing factor 2, mitochondrial"; /id="PRO_0000007452" MLRIVWKPLKIRLPVWRRYQSNISINSIRNVGIIAHIDAGKTTLTEKMLYYGGFTSHFGNVDTGDTVMDYLPAERQRGITINSAAISFTWRNQRINLIDTPGHADFTFEVERSVAVLDGAVAIIDGSAGVEAQTKVVWKQATKRGIPKVIFVNKMDRVGSSLGSTIRSIYTNLDCPYPLVLQLPVYSDGLQERKFLGILDILQQKMILWDTSDNKLGTDGTHVQELPIPESHMERFIEARNALVMSLCDVDETLCDEYLENEDSLAFTNDRLFKIIKQKTISGNVVPVLCGSSLKNIAVQPIMDAIIDYLPSPVEFYEKNASKETSSDKIISLDKRPLLAKIFKVIHHASRGILTYVRVNEGTLSRGMMMFNPRTKKSERAIRLYNVFADQTQEVDCISAGNIGVISGIKQFHTGDIIINKENSKNFHEYLSGNQSVISIPEPVCIASIEPYSLKDEPALLEALANMNREDPSFRYTQDLENGQLLIQGMGIMHLQVSYERLVSEFGARASLGKVQVGYRETLIDVSFNSVTLSTENKENLIINVYLIPISDEGDETLKKYFSEGEIQKVRSKGQEDGVLFYGWKPENSCTLPDHLSFQRIQENIYFGIVAGLSHGPLHGFPLTNLQSFCTISSFLSNDFPLSLLTQASMKATKNAVFSLYKRSPKSFRILEPYMDVTITTPEEYVGIVSKDLVGKRGATIKEITEIGKNAASKDSQIAIGILGERYLPADEPSSVKANNASSLLQSSSVIKCIRAQVPLEQILDYNSVISSLTKGNAKFLMSHPMESQTPKLVNYGSSFHPMSMQRQKRIFP O94438 RS3A2_SCHPO MOD_RES 2; /note="N-acetylalanine; partial"; /evidence="ECO:0000255|HAMAP-Rule:MF_03122"; MOD_RES 251; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22H12.04c; CHAIN 2..252; /note="Small ribosomal subunit protein eS1B"; /id="PRO_0000153540" MAVGKNKRLSKGKKGIKKRVVDPFSRKEWYDIKAPAFFEVKNVGKTLVNRTAGLKNANDSLKGRILEVSLADLQKDEEHAFRKVKLRVEDIQGKSCLTSFNGLSITSDKLRSLVRKWQTTIEADQTIKTTDGYLCRVFVIGFTRRRANQVKKTTYAQSSQIRAIRQKMFQVIQNQTSSCSMRELVQKLIPEVIGREIERATGSIFPLQNVLVRKVKILKAPKHDAQKLLELHGESQDVGTKVVKDVAPLESV O94441 YPP1_SCHPO MOD_RES 632; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 633; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 637; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC637.04; CHAIN 1..862; /note="Putative cargo-transport protein ypp1"; /id="PRO_0000363379" MFSAKAKTYELKLEQTRCNGDWQAIPEVARKLHKHNSSKSFVCELAKIEASLKSALTAELKNIANVLEPKLIDNQYSLIPALPSARTDPLLSQLNSLNIQNATEDEKLQETSIRLLLYIVQRKFPEAVDLDWSPQGIPWTETSTGICILQATVLSSLAQYAQANDEVAYQYVRSAIGLIQNANIGKKPLPELTRWCDLAYSLYAQMSVSACSSQLERANILTTCLSYFTEHKSVNLLYKLVTSRQAIKYLEHILRTNTNGSKIFTKSPVKNLYLNWPQLVLDYGSLLCNFTSFPKAGDQNMFAVEFIELATSIWINTEKSYDITVSLIRMLYQLTGKCFQAQQIFRSLVFFLRHIEEFEEASEAFEIYKFLCVKSHERLARKNSDVAGSFSDIKPVFVDEPKSIIEVCSVMMTVYAQYLRNLKKVSEILDYITKIASDYDLLKRDDIAPLIYHTEGVAYSFMYYQANNPSLRERYHQKSVQSYQKCLEKQPTNTNALFHLAMQYSERRAITDAMQIVRRLLEVNPKYSIVSWHLLVLCVSCSEQYAAGIKLIDSVFETWGINHVNEDGTIEISLTNLTFNDRCALVDLLITKLALFEAEKGVEATLDIQDEIFTLFASIFDLNEYRISKEGSSDELSTLLERSTIQSIKSSKKISKDVENEKGSILGFSRKSSLKRSTVLSKKSHSSYKENFQLRRGKTVSYLNQKLWLTAASLFLKSGNDDQARSALLEAKKIDHECAWVYYLNGLSLLQQGKEVEGYEQLDVAHYLDPEDPLISTALAKCLLQGGYGPMHSRRNRADAILSSCTLQYGWDLPEAWYYTAEIFRQLGDLKQAAFSYDYCIQLADTNPVRRWSNLQPRFMNV O94442 NBP35_SCHPO BINDING 15; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038"; BINDING 29; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038"; BINDING 32; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038"; BINDING 38; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038"; BINDING 68..75; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038"; BINDING 241; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /ligand_note="ligand shared with heterodimeric partner"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038"; BINDING 244; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /ligand_note="ligand shared with heterodimeric partner"; /evidence="ECO:0000255|HAMAP-Rule:MF_03038" COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03038}; Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-cfd1 heterotetramer. {ECO:0000255|HAMAP-Rule:MF_03038}; SPAC637.08; CHAIN 1..317; /note="Cytosolic Fe-S cluster assembly factor nbp35"; /id="PRO_0000278902" MQIQETVPLDAPEHCPGPSSENAGTASACEGCPNQQICASAPRGEDPDLPLVVERLKEIKHKILVLSGKGGVGKSTFSSQLAWGLSLEEDKQIGLMDVDICGPSIPRIMGVEKEEAHQSSKGWSPIYVCPNLAVMSIGFLLPSEDSSVIWRGPKKNGLIKQFIKDVNWENLDYLIVDTPPGTSDEHLSLVQFFKNSGIDGAVVVTTPQEVALQDVRKEIDFCRKASIPILGLVENMSGFVCPSCKGKSNIFTITTGGGEALAKEMGLPFLGKIPLDPLIARSCDFGKSFIDECPESPASEIIIDIINKIDESLQKRQ O94443 YFE9_SCHPO SPAC637.09; CHAIN 1..631; /note="Uncharacterized exonuclease C637.09"; /id="PRO_0000317229" MSKMGSSSMGELQDGITQEDSIEKKSKNVASHGEKRKVKRKKEDLSMDGSNDGVKDSPDSNDDSQSKKKKKKKLKKSQQPLNEENYPRLQTTENNLQKPLKISDLQELVFWCLADGQAPSWVLVRNKQMIHRAVILLVPGLEPSQFGFQPVRGNKHSFLLPNLLNENGPIQLPDFCEVFDRAWPTRSPGDRFRVFSPVNAFLQSPLSNEQKKKRDKETRAMASFSKPSDYLMSYESFIEDEYPLHPTVMKGEEVTQPSGWVASAGDFHSPPINPKILAIDCEMVRTENGLEIARVTIVDMKSEVIYDEFVKPESPVTDYVTQYSGITEEKLRNVTTVLSDVQSYLKKTVDNNTVLLGHSLNSDLNCLKFTHPHIIDTANIYNHTRGPPSKPSLKWLATKWLRREIQKAGALGHDSAEDALACVDLLKLKVKNGPAFGLFNQDFESIFHRLSRQQPTPLIGAIADYGNPESCIGKAAHKSVSCANDDEVVSAVVSLSDMHNFVWGRFRELEHAAMWNANRNTKQENNSDTDTENDSVEEDQVTSYSSALERFNRRIRLLYDSLPKGSLLLLYTGTGNPIEMSKLNAIRQQFRKEYQTKKWDELSVKWTDEENMKYISAVENTRNGLSFMTIK O94445 SUV3_SCHPO BINDING 179..186; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC637.11; CHAIN ?..647; /note="ATP-dependent RNA helicase suv3, mitochondrial"; /id="PRO_0000310786" MFLETLIHGVTFCVPFFSKSARIHTLSKDVFQQRKFPGNTLWAAALNRFTAYLFASKELSSKQAYLAQDFVNVCKDASVFQNVYYYELKKNILTDLGFSDLKNSDKSLALSKSSSTFDLQKIKKIHDCLLSEYRKYVRYQERIEETRPDLQKQLTDLKNPIEWYPGARKLRRHIIMHVGPTNSGKTHRALERLKTCKKGIFAGPLRLLAHEIYNRLQANGIACNLYTGEEIRNDYPFPQVVSCTVEMCNLSTTFDVAVIDEIQMMADPSRGYAWTQCLLGLQAKEIHLCGEESVVKLVRSIAKMTQDDFTVYRYERLNPLHVAEKSLNGKLSELKDGDCVVAFSRKNIFTLKSKIDQALGKKSAVIYGSLPPEVRNQQASLFNSKSSDENILLASDAIGMGLNLGVKRIVFSDLKKFSGVSTIDIPVPQIKQIAGRAGRHNPNGSKQSAGIVTTLYQKDFAKLNRAMNLPTKNLFNACIGAKDDLFFRYLSLFSDDIPQKLIFDRYFKLAKTTTPFVVSEGALSTFIIEYLDHIKGLTIKDKIKLLGCPVLKHSKYAPLFIREIGCVIAQGKRLQIYDLKSVPLEILERGIPTTETELQQLEQLHKLIVAYMWASIRYPAILQNGAAEKTKAIAEAFLIKGISKLQK O94448 RCE1_SCHPO ACT_SITE 126; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q6LZY8"; ACT_SITE 160; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q6LZY8" SPAC1687.02; CHAIN 1..271; /note="Probable CAAX prenyl protease 2"; /id="PRO_0000194833" MRVYLISFFFTAIYVVSLYTFPVARPRPSLNRNDPKVITARCISVLLASSVCCILTRLIIGPSLNVFTFPTDQVLKSLLHAATIFIGPLYEVWIVDKEYRLFFIHLKDCLSNAIAWRNIIIGPLSEELTFRCCIVPICEAAGWSRLKIIFVAPLLFGMAHIHHTYEFLLAYPNAYIAAALQTVVQFSYTTVFGWYTTHLFLSTHSLFPSFLVHAFCNSMGLPTLYGKIGNRNQTRIYYTLLLLGVLIFYMTWGITDFNNHQDFEPRLVPLN O94450 YFF4_SCHPO SPAC1687.04; CHAIN 1..501; /note="UPF0616 protein C1687.04"; /id="PRO_0000343149" MVIALSDSFIENPRSFLQRFQDALFAGSKPDLQGTLGIDEEVSNIFATEERIRKIPNYLDCKWSELKTGQLLRLQGMVQDTNFGHEFFAGAVEVNENIWRGCRYILDFSEDEMHLDESKIVLDERYSLFLTNVPGERTLPVIEALGNWGSESLKERSLKYSNRLQASNDTGVCVKCYGGMETKVQVCQAIDVIGIYEEPSEYSDGLPILHMLCFKDYTQSATQAPSPQQAEIIRPKILKYFEKVLGENIAAESLMLALLSNVVHKTTGLVIGGFTLNLTNCTSELVSQLVSVLRPLIKRMVIQKVNVAELNRKPLYPLSDGETLDTSHLQVAPGTLIVLDETELSSGTLNDVGCRNVQFLSSLISQQDLTFFYPFSSFTVHSNVRIIILSHGRSILPADVGCRCRGDSPDTIEFPTDSDELQEFCNFFHMWNMRANIPENMLDYIQSTYVSSRQYNKEINEKTLSLQINCSRLYAKSFGRQLVSRIDFEAARSLINHWTVN O94452 MCP1_SCHPO SPAC1687.10; CHAIN 1..661; /note="Meiotic coiled-coil protein 1"; /id="PRO_0000096286" MELAKIGDRLNNYYNNIYTLSEKLGYSFTKISFNNIILDALSGHQRKLEIKIINIESKCNELSSEISLLRKRLGIIEEIEIPRTLIDQYECLVTYHNGIRAIYNTKKNEAKNMYKEIERLSVILGESVDEVNFVNGDFEDISDIKLEQLSAKLNELHQIYRLRKEKNIEIKEELKKLQDSLSIKLSMPADDLSKNGIKHLIIYKEKLRFSLESRKSRVDEIVNEMKNMCGKNPTSELPTNYSDKTLTLWENELSSMRKVYFVKYKTEYEFLQKRYLSLARIMFVSKKEMLFTSQFKEIPNVNRELIQSMKQEIGNLEVDLHLQGELNNMIRRYLLLESRVYKESQRMKVLSGSASQPFTLKRLQKDFQLLKAKLICALREWEEDNEKKIYVFGKPLSSRLLMIHSPPILQNQENISSNDNSKSSPESSPPARKTTGKIENKKLRNIDVQSKKSIRFPLRLASHEEPLIDRMVNQSPDTRSVSKSKRLVRETSSGCLFKNHSKSNTLSPRRKGSRHGPREPCLSPDASSSSIPVTDIKEILPSQHDTPHNSVKLTGSSTTPASVSLRQMIEPLLSRTPPKGEFTNSLDDTPTQSNVEKVDRFLENHDWETCSESSSASEDQSLCKQLSSFSLSSSDISKKLKNNLNGLHFSSDEGSKLPTFL O94453 COQ4_SCHPO SPAC1687.12c; CHAIN 1..272; /note="Ubiquinone biosynthesis protein coq4, mitochondrial"; /id="PRO_0000115244" MFYLNAHLEINKVVDVVMSLSKKFLKPSVASNQLRLLFTAAERKVNYPGHVPLSPLQRIFLVAGSAIMGLKAPWRGGDMISVLGDASGQPFFLHRLLNKMLVDKTGREILKDKPRMTSKSLNLPFLRTLPPNTLGKIYVDWIDKEHVGPDTRSPTRFVDDPEEAYVMQRYRESHDFYHAICNMPTNIEGELAIKWLEFVNMGLPVGALSALFGPLRLNCEQASRFRRVYIPWSIRNGLNAKTLINVYWEKELTNDIEDVRRRIRIEAAPPLV O94461 YFFL_SCHPO ACT_SITE 8; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250|UniProtKB:P62707"; ACT_SITE 82; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P62707" SPAC1687.21; CHAIN 1..209; /note="Probable phosphatase C1687.21"; /id="PRO_0000318490" MKVFLIRHGQTDQNKRGILQGSVDTNLNETGRLQAKLLAQRLLPLDIDQIFCSSMKRCRETIAPYLELKPEVPIVYTDLIRERVYGDLEGMNVVEAKKLLNANHPDHYGEGLSHLTSRLLKFWDEYVVPLQGKKKCVIVLCHGGVINVLRTHFMEEKGFTFDKSKLESKIITFNTSITEIEVTEHGTGHIHTFGDASHLESEETGKLIA O94467 OYEC_SCHPO ACT_SITE 213; /note="Proton donor"; /evidence="ECO:0000250" BINDING 208; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 208; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 358; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 386; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; SPBC23G7.10c; CHAIN 1..395; /note="Putative NADPH dehydrogenase C23G7.10c"; /id="PRO_0000314118" MTIVNEGAENVGYFTPAQKIPAGAAIGVPQTKLFTPLKIRGVEFHNRMFVSPMCTYSADQEGHLTDFHLVHLGAMGMRGPGLVMVEATAVSPEGRISPNDSGLWMESQMKPLRRIVEFAHSQNQKIGIQLAHAGRKASTTAPYRGYTVATEAQGGWENDVYGPNEDRWDENHAQPHKLTEKQYDELVDKFVVAAKRAVEIGFDVIEIHGAHGYLISSTVSPATNDRNDKYGGTFEKRILFPMEVVHSVRKAIPDSMPLFYRVTATDWLPKGQGWEIEDTVALAARLRDGGVDLIDVSSGGNHKDQRIEVKDCYQVPFAEKIKDQVNGILLGAVGMIRDGLTANEILESGKADVTFVAREFLRNPSLVLDSANQLGENVAWPVQYDYAVKGHRKLR O94473 YC64_SCHPO MOD_RES 210; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1919.04; CHAIN 1..256; /note="Uncharacterized membrane protein C1919.04"; /id="PRO_0000304001" MDLSFIEGFETIWTVVRAVVLNYLLRSLKILSTILYVSAVISWNVSLKVFGNVLLPGFLTIRTVVIFILRIVSLFLWILADPAILLVQSVYWYFIRAPARFILMVGITLYPLYVLLSWAVFLGIIVGFSLNSVFTFIDSFATPSSNSTVTEAMTKMKNEKVLEYPYKDRNIMLGDLASRIPSKDSEKLDEERQPIALEKTKSLDSISHSSSSSRKSSTELKIPPVETRIVAEIPVPSSVKRRRHRPNKSMGSIKNS O94478 MU137_SCHPO SPCC1919.11; CHAIN 1..420; /note="Meiotically up-regulated gene 137 protein"; /id="PRO_0000278628" MVSRFFSWTNEKPLGDQRAHLPDSFLELEQEIAIREEGLSKLFQATTIWIDSILKKVDGEDKEKCLACENLGKVMINHSKELPQDSSYGITLSQLGKANLKIGEHQTSLAYKARVCYLDFLKRYLVQAKDFHSARKKLESRRQAYESLLQKSFKEKKEDSRLEEDIRLALYKFEESTEQVKNRMIALKDVEADQYQQLTELIVYELNFFKESTGILNTIFNSQNSLTPQKKIQSSERSVENEFLASPMDPSLSKLFTKTTNTEKISPTPFSTPKRKSKKETVFVKAIYSFTGRNEKELDLHTGDVIQVSEQLGPDWYMGEKVNSKAEKLGNSGMFPVNYCTRIYDLHVQKSHETRSLERARSIRRIVSDDPRDYCSPIKQSPIQNLKFLDSDNSLLSSQNVEASSQPIKIRKPLPEIPNK O94479 PFF1_SCHPO ACT_SITE 191; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P80561" BINDING 147; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 159; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 159; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 192; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 217; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 292; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P80561}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561}; SPCC1919.12c; CHAIN 1..843; /note="Vacuolar membrane protease"; /id="PRO_0000174139" CARBOHYD 96; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 109; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 117; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 209; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 275; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 322; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 677; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 703; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 707; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 754; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 788; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MTNSRRHIFERICAKAFQSSLTCSIFGFTVLLILYLLDWKRIAQVPGPNLLKDLEFQRAWNDLEYISSLPHPYNSKQNEHVRSYILKSMRELEATNQSYITVIDDTLTNITFESTDNDTLTYFEGDNILVKFEGKSKDLFPILLSAHFDSVSTGYGATDDGMGVATVMAIARYYAKNQPNRDLIININNAEEDYLFGAKAFASHKLSKNVTAFVNLEGAGSGGKAMLFRSSNGHVSSAYFKGNHYPLASILGNDFFKRGVIRSQTDYIVYEKMHNHTAGLDIAFYENRDIYHTRKDDINHLMPSSLRHMMYTASNAVKNLLNDSKSDLTKFRKPMFFLAFGKYWQLNLPIYQVLNIIFAVICPIVLLLTLIRFPSLYEQLKKPRYTVCFVVSCIFVSIFDTLTVLLLTWINPYVINSHTGLILALFYLTNLIALAFSFRAAATHSKLSSEDLSSIEIVFIWYAQILWYLVFIVSVILSIYFQLGSTYWVTLSYLCTFTCCIMTIIRINYFVDNVVTTQTTHEEDALIGSSINTSSHQHYGSTLNSTPHRRNSIALSNRAHVKLIDNIWTVIYFIFNVPFPVFLCYDILVETILPAGSQTLTDSVFSSKLYKLVIFVVFLSLVNSGPFIFRALSKKSLAVLTMLWITLFVQALSVNPFTESAPLKLSFVQMYDMDRMNNTVYVKNISPFTQDVLSLNPHFLFSNGSCNTSLCYYESTDPDFGGLKTPMSIHIEREKHQLDISINSGSKWCYVDFNTSVFFEAINGNSISGMYSSVRMGQRSFYAPYTLNLTITEVVKAEVTCLYDDIHEGIIPAYNTFVEHLPSWVAGVKASTGLLKVKSSIVI O94480 BMT5_SCHPO CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + uridine in 25S rRNA = H(+) + N(3)-methyluridine in 25S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54588, Rhea:RHEA-COMP:13939, Rhea:RHEA-COMP:13940, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74502; SPCC1919.13c; CHAIN 1..282; /note="25S rRNA (uridine-N(3))-methyltransferase"; /id="PRO_0000343148" MGKKARFKEARRLQKRNLNNAIGSSSINSQNSLTNDKIGKGKNKGPTERYVLPFEKNNRFLLLGEGNFSFAFSLLLHHVSSEGFVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTIFWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYPEYSHRRTIGWIDGISERSPWKGELRDSRHYCFVVNGSNIKPYNQRKEKRKRSELSDDSSDSS O94481 TFC5_SCHPO SPCC1919.14c; CHAIN 1..520; /note="Transcription factor TFIIIB component B''"; /id="PRO_0000361656" MSSQILTSPTKKSMSRFAPKFTARREKVSDQKEVVHEEKNQPLTGNEVETSAQLSRDTANADISSPVVQTVVHKEATENPTASSYRKDDSVKQNEKLLHSNPTFKISKPTVLEQPLNAIEHLSPETDLSSSAEQQFMKELDLFFDENIPLSQLSAVSDGKADSPATKKSRRSYRESSLKRKSQLILENVGTDEKIINISETKMSALCDDPGIGRKSQRFIELEKMLFEEKRAKRIKKQGASTASSSREASLDSTIKQPLSASLLESSEPKEKEEIVGSLEEEGTDESASLEDSLSHPTKSILDQLADKMEVDGLNNNSNYSATPRTRVVNGQIVLDETSLEVDRHERDFVPAEEREYVEENSLSRRVTSATWGNRQKPEKWNAMDTEKFYKALSQWGTDFALIANMFPTRNRRQIKLKFKQEERRNPARVNQALKIKKPIDMEEYSKVSGKVFRPVEEMEKELQKIRENFEEERRRAIEVAEQRQLIVNHELEQEKNAPSPTDDKSYVFEDGVEVVGQVV O94486 CHR2_SCHPO MOD_RES 509; /note="Cysteine methyl ester"; /evidence="ECO:0000250" SPCC417.05c; PROPEP 510..512; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000396745" CHAIN 1..509; /note="Chitin synthase regulatory factor 2"; /id="PRO_0000089573" LIPID 509; /note="S-farnesyl cysteine"; /evidence="ECO:0000250" MLVSNGGTGSAHEWDRTTIDYDIEPSSDTHAIEISSNDDYLHPLAQFKKSEEFDEVPTNTLIHEVPSFSDSASNIQSQRNLSPFKELEIVSKKKSEQTFSSAVDFSAINVKNLNLKSGLFDPEPPSYDPDYAFNQRSLQSDPGSDEMFRNFKKSISLEELKSSYKLASAEMCEPETRLSFLQLALQAEKSSSRRNREYVARKKEEAFDYLTSFVSQGNSFFGYSEALYLLAVCYGTGALRTEINEKEAYRLYKMAADLNHVQAAYRVAICLQMGFGVTQNTEEAIHYFFRAASGQHVGAMHRMALIYFRGLMSVKRDPVKAMYYLNLGALEADHEFPQALYDLAELYEHGSSYLDGLLELSPRKAFVLYHIAAKYGLKDAQLRVARCFELGQLECDINLVRSFVWYRRLARKRNPEAMWKLSQFYLNGVDDVIYPNPELANEWAKAAAYKNHHLASTFVQDVGKEDVFEKTSITISNEERKSRNSESLPKKKKRLSMLSFKRSKNRESCIIS O94491 YC7A_SCHPO SPCC417.10; CHAIN 1..508; /note="Uncharacterized transporter C417.10"; /id="PRO_0000372783" MSSISIDEKLKDPESVQNKEILDVDVGDLSPKGVDAAFNYALDVDYDEIDPETERRLVRKIDCTIFPVMCLVYCIQFLDKTSNSYAVIMGLKEDLKMEGQMYSWSGTAFYLGYLVFEFPASLLLQRFPLSKTLCVFLVIWGFLLCMTSVANYPGFIALRVLLGMMESAASPGFILLTAQWYKRSEQQLRTSVWVAFNGLGQILGSCMAYGLAKRTSLPMRGWKLIFIICGVLAIFLGFVILAVVPDNPFKAWFLTEEDRKLVVKRLRANKQGVGNNHFKLYQFKETMLDIRTWIMFVSSVLLNIPNGGIGTFSSLLIKGTMGYDTLQTLLMGLPAGACEFGGLIAFGFLSLFIHKRMVLATITTCIALIGSCLLSFAGPPRAQLAGYYLLMVSPGAMIVMFAIISSNASGYTKKVTVGVIYLIGYCVGNLIGPQTFKAADAPEYMPAKNTMVGCYAATLVTFPALYYVNWRENKRRDQLAAEGKIEHRPNAEFEDLTDFENLDFRYTL O94495 ELP5_SCHPO SPBC18E5.05c; CHAIN 1..314; /note="Elongator complex protein 5"; /id="PRO_0000343152" MSKFLLNRCIRDLSPLTVLKDNLQQTAKPILNYYAKNAASRGIKVLFISYETLEKEAPEGIDCFLYATSWEKVKSLKELYEHISSWRTQGKQHIVMIDTINPILNTSISSFTMFFGSVLALGSICFLTSFHKDVTLENYPSYLPPCEVFLDFTSTCTVSLIGMQHLSVEHDAKMRSLPNPLLEELQDDKIISLLGSNCETAIVLHVEFRKKSGRIIKESCVLKNGKLEPYTPFEETARGPEPADNQIDFNVSFNLNVSEKERKERDKVFLPYFSAQMVGSQHKSSFVDEGTIIYHADEADDFDEEEDADEDLLI O94501 TCPA_SCHPO SPBC12D12.03; CHAIN 1..556; /note="T-complex protein 1 subunit alpha"; /id="PRO_0000128314" MFQAPRESTLFLSGEKISGEDVRNQNVLATTAIANVVKSSLGPVGLDKMLVDDIGDVTVTNDGATILSLLDVEHPAGKVLVELAQQQDKEVGDGTTSVVIIAAELLRRANELVKNKIHPTTIITGYRLAIREAVKFMTDVLSCSVDSLGKESLINVAKTSMSSKIIGNDSDFFSTMAVDAMLSVKTSNSKGETRYPVKAVNILKAHGKSSRESVLVKGYALNCTIASQAMKTRVQNAKIAVLDMDLQKTKMALGVHVTIDDPDQLEKIREREVMITLERVKKILNAGANVILTTKGIDDLCLKSIIEAGAMAVRRCKKEDLRRIAKASGATLLSSLSNLEGEETFESSYLGSAEEVVQEKFSDDECILVKGTKAYSSASIVLRGPNEYSLDEMERSMHDSLSVVKRTLESGKVVPGGGAVETALSIYLENFATSLGSREQLAIAEFAQALLIIPRTLAVNAAKDSTELTAKLRAYHAASQNAEVTDVKKRGYKNYGLDLLNGVIRDNVKAGVLEPSMSKLKSLKSAVEACIAILRIDTSIKLDPERQPEDPHAGLH O94503 SRB11_SCHPO SPBC12D12.06; STRAND 224..226; /evidence="ECO:0007829|PDB:1ZP2" HELIX 9..11; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 13..15; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 30..45; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 50..66; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 75..89; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 96..104; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 115..128; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 139..147; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 153..166; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 171..173; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 177..189; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 195..202; /evidence="ECO:0007829|PDB:1ZP2"; HELIX 205..222; /evidence="ECO:0007829|PDB:1ZP2" TURN 129..131; /evidence="ECO:0007829|PDB:1ZP2"; TURN 167..170; /evidence="ECO:0007829|PDB:1ZP2" CHAIN 1..228; /note="RNA polymerase II holoenzyme cyclin-like subunit"; /id="PRO_0000080427" MAANYWASSQLTQLFLSTDLESLEPTCLSKDTIYQWKVVQTFGDRLRLRQRVLATAIVLLRRYMLKKNEEKGFSLEALVATCIYLSCKVEECPVHIRTICNEANDLWSLKVKLSRSNISEIEFEIISVLDAFLIVHHPYTSLEQAFHDGIINQKQLEFAWSIVNDSYASSLCLMAHPHQLAYAALLISCCNDENTIPKLLDLIKSTDAFKVILCVQRIISIYYFEDIE O94506 RSM1_SCHPO SPCC1753.05; CHAIN 1..296; /note="mRNA export factor rsm1"; /id="PRO_0000290653" MSFPTDMETNEILDQLDKIDERNEDILLKSLKASKCTYKPWSREEFLRRLLTYRSRWAYVNDPQIGEINCCLNGWLCESNNILVCDVCRNKINLTALQQVDAENDSLNELPEKTKERLEVSLKEEHQDNCLWRLHKFPPDIYHLSVSAELVQVGRRFNSLSTRLVSTHLPEEMTLKRLEKVANKIRVDWEKEDAAVLLGIALTGWSEQVPGRLYVCNYCHRRLGVWNLQSEGQDFDVLEEHKKSCPWVIPQPFTDLLGWQQIFELLCKESIFQSTTKTMDVSQYTDYTFSLLQGLR O94509 GATA_SCHPO ACT_SITE 64; /note="Charge relay system"; /evidence="ECO:0000255|HAMAP-Rule:MF_03150"; ACT_SITE 141; /note="Charge relay system"; /evidence="ECO:0000255|HAMAP-Rule:MF_03150"; ACT_SITE 165; /note="Acyl-ester intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03150" CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate; Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7; Evidence={ECO:0000255|HAMAP-Rule:MF_03150}; SPBC646.03; CHAIN 1..471; /note="Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial"; /id="PRO_0000001204" MSNKYNNLLKEVAAKYASIILNDAKIKSLTSINSAEYLYDSFVEISKLPLEKKLPLKWKLITVKENICTKTNLTTAASNMLKDYNSPFDASIVESLKKAGGIILGKTNMDEFAMGVKSENNLFGRTVNPVVKDSNYDVGGSSGGAAAAIAADICYASVGSDTGGSIRLPAAYVGCVGFKPSFGRISRYGMLAFANSFDTVGIAANNVKGVTKVFNVLDHPDINDSTCLTKEARYFVKEQHKKLSRKPIKIGIPIDWNVSETHPNVLDKWNEFISLLKSNGYLVQEIQLPISLYANSVYSTMAYAEATSNLAKYNTIAFGNCLDEKFEEEIISSTARSFFLGDEVKKRLLLGAYSLARMNSSDLFSKARYVRRAIQLEFNKNFFLPSFSVDDPRGDIDFIVTPSFFNSSQPIETPSSYSHLSDTMLVPANMAGIPSVSIPFGTLNNGLPMGIQIMAQYLNDEDLLSFAGQFA O94511 YN67_SCHPO CATALYTIC ACTIVITY: Reaction=a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA + NADP(+); Xref=Rhea:RHEA:33763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.38; SPBC646.07c; CHAIN 1..295; /note="Putative enoyl reductase C646.07c"; /id="PRO_0000317698" MSITLSSRGRKIRKLPKSLEFPLDGSIDKLRDEVSSVTRLPVERLRFSTADGTTLLPNTTLRKYGVGPGATIWVKDLGPQIGWRTVFMIEYLGPLVIHLFFILNYKWIYRKDYNLCLNQKIAFVLVMLHFMKREYESIFVHRFSLATMPLRNIFKNCAHYHLLSGLFLAYFIYGPWHANDYIKPNHLLFLIVGWAFAVLSNFRTHIILRDLRPAGSKKRVIPTGYGFNLVSFPNYFFESLGWLFFALLTKSWASWIFLFVGSAQMFVWAKKKHARYLKEFPNYPRSRKIMIPFFL O94512 OBP1_SCHPO MOD_RES 182; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC646.08c; CHAIN 1..516; /note="Oxysterol-binding protein-like protein 1"; /id="PRO_0000315946" MPNPNQAIKKENEPIQVENPTELVRDDGEVEGYQKEEGKFKLVLSILKQCIGVKDIASLRFSLPAQLLEPVGNLEYWNYVDRPDYFAVMGDSDDELERMLGVLRWWFTKDLRFVRGRVVKPYNSVLGEFFRCKWVVTDPTVREDHTLDPDSSQLPTYKTEYSETTKFPLGKSYRPKASRTTSSQSVASTMTKSSTKTSKKKSSKKNSKSESNQDSSNDRSSTAPSTAESNNEHLSSSQKSKHSIVFMAEQTSHHPAVSAFYVTCPSKGIEVYGQDQIAVGFTGTSFKVCAGDLNKGVYVRFNKRDNEEYLCTHPSASVGGILRGNLHINLLDSTVILCPKTRIKTIITYIEERWLGKPRSLVEGVCYRYDPSNDTIDSIKAVPKENILATFKGNWRNCIFYSYAGESESRMLVDLNELDLVHKRCPPLDKQFPFESRKIWFPVTHNILAKHYTQATKAKQEIEDQQRQASAAREESHTEWKPRFFVPDEKEGRPTLTEEGKKVLEQSLSDEYIHGS O94514 NOP56_SCHPO SPBC646.10c; CHAIN 1..497; /note="Nucleolar protein 56"; /id="PRO_0000337263" MADYLLYESATGYSLFDVVGADQIAAKTKEVQLSLQDISKFGKVVQLRSFIPFKNAAHALENANDISEGVLNDFLKNFLELNLPKASKKKKVSLGVQDKNLATSIKSEIDAIECDTSELTQDLLRGIRFHGDKLLKQLSPGDFERAQLGLGHSYSRAKVKFNVNRNDNMIIQAIAILDQLDKDINTFAMRMKEWYSWHFPELSKIVGDNYKYAVIVTLVGDKTTINDEMLHDLAAVVDDDKDIAQSIINAGKVSMGQDISEIDLENILSFAERVIKLSNYRKQLHNYLVQKMNVVAPNLAELIGEMVGARLISHAGSLTNLSKCPASTVQILGAEKALFRALKTRGNTPKYGIIYHSSFIGKAGAKNKGRISRFLANKCSIASRIDNFSDAPTTAFGQVLRRQVEERLNFFDTGVAPTRNSIAMAEAYEKALSSVNIDGDEEVDIDVEETVETISEKPSKKEKKDKKEKKKEKSKKKRSADDASEEVKKSKKKKKSH O94515 TCPZ_SCHPO SPBC646.11; CHAIN 1..535; /note="T-complex protein 1 subunit zeta"; /id="PRO_0000128361" MLSLLNPKAESIQRAQALQVNISAAIGLQDVLKSNLGPTGTTKMLVDGAGAIKLTKDGKVLLTEMQIQNPTASCIAKAATAQDDATGDGTTSVCLLVGELLKQAELYIREGLHPSLISDGFNLAKNEALTFLDSFKTDFEVDREVLLNVAKTSLSTKISSKVVESLAPAVVDAILTIRRPDEPIDLHMVEIMKMQNRSASDTQLIRGLLLDHGARHPDMPKQVKNAYILILNVSLEYEKSEINSGFFYSTSEQRERLVESERKFVDNKLRKIVELKKEVCERDPTANFVIINQKGIDPLSLDVLAKNGIMALRRAKRRNMERLQLACGGVAQNSVDDLNPEVLGWAGSVYERTLGEEKYTFVEDVKDPKSATILIHGPNTYTIQQIQDATRDGLRAVKNAVEDNCLIVGAGAFEVACAAHLRNKFAAKEVKGKAKMGVYAYADALLIIPKTLAANSSYDTQDAIVALQEEASEGYKVGLDLKTGMPFDPEVEGIYDNYRVIRHMLHSATVIASNLISVDQILRAGRSSLKEGPPQ O94519 SPF30_SCHPO MOD_RES 173; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1281.02c; CHAIN 1..311; /note="Splicing factor spf30"; /id="PRO_0000290648" MEKELEEYKSQLALVQISLQKTPQNEELQLLENDLKELISLTENLLQESVENDKNTFQNSQNGVAGFNTSKPVHIDFTPGNLVMARWVSGDYLFYPSRITAVSGFGANKKYTVQFLDYPDIETVSLKHIKAMPEEKRQEIEGNKEILKKSTTIRSTPVREPTKAISVASMSTSPSNYASRASSPDMKSSAAVTANVSPIQNVAQHVSTLPKISPIPPSNPPPVPSVSYSQKQQKQLKPKAALEASQNSWKQFAARGVKTGRVGKRKKIGESSIFKSTEDFPGRTNPKNFGNVARSGHREKHIYNYREDEDS O94526 PTEN_SCHPO ACT_SITE 129; /note="Phosphocysteine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00590" CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456; EC=3.1.3.67; Evidence={ECO:0000269|PubMed:15249580}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416, ChEBI:CHEBI:83419; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420, ChEBI:CHEBI:83423; Evidence={ECO:0000250|UniProtKB:P60484}; SPBC609.02; CHAIN 1..348; /note="Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1"; /id="PRO_0000353823" MNILRSVVSRGRKGLKQEKVNRSFAYLDMVYITSKVIAMSTPAAGIHKLYRNDELDVFKYLTTQLKDNWILLNLCAEETVYHLELFKPNVINYGFQDHNPPPLLFLWAIVMNMDALFQTQPLLTLVVHCKAGKGRTGTVICSYLVAFGGLTAKQSLELYTEKRMVRGHGLTISSQIRYVYYIEILKQFPNYLKAVEFNTGTTFFKSFKCLNIKKNSSLILSLHAFSKGRNINPVALWKSSDISSHNVSIKEGKRIWGIQCNLETSEKDLLLRVERKGQFYFPSSVQCWFHTHFQPMLVEYTNGINFQQGINSFLQGQQSISFSWSEMDNSRRSDPFFEQLTIVYENVF O94527 IQW1_SCHPO SPBC609.03; CHAIN 1..809; /note="WD repeat protein iqw1"; /id="PRO_0000316550" MSGISLSLRQLDYRDWFQRKISRDIYGNSTWLTGIDLQKELTGHTGCVNTLDWSADGEFLLSGSDDTRLIVWDVFNEYKPRHLISTGHVQNIFSAKFVPYSNNRQILSASGDKLIKLFDLDSSKEGGMDHGMETQTRCWSCALDSVKNIVPCDNGHTFLVCSEDGTARQYDIREPHVCNQDLDCPSILVNYNPYRINLYTITMSPSNPYYFAIGGTHPYAFLYDRRMVKKSFRDDWTMNTSPEKDCRCVRKFSPDGSCNSQGILDRYITCCQFSAANPNELLVSWNSDYVYLFHVHEDKSYTPTFNKIEDSNKKPSKPSLLQTQPLKRKNYSPWYKNNFGASTPASRVSRNPYTAAQPRKHTFYQMYENIEKFFTTENGGLYESIVSGRLSHFSRSIQYVKDAIYFLENYNYIPDSNGLNHSIRVSALRYWRACVSILALMDDTVSLEPNTIIQAGWGWLYDFMNWVTRYLLGISDHWALQMSPPTNVARQNFVLCDPDEPSRVLFSNPSEMIRAFARIDTNDLSSVRRFFWIHKVLRGCLLLISSDIYWEQFQPWDSSTSDVTSSQRLDDENGFLTLLEPPVNYENEVESSSGENIVSMYTGHSDLNDDDDDYQDEESYSYASDDDDESDEDSDEGPTLLSLRMKKRKAVEPNVPVNTHVKSYYGHCNVESIKNVNFYGQNDEYVMSGSDDGRFFIWDKLNASILAIIHGDSEAVNVIEGHPRCPTLAVSGIDSTVKIFNTENTPPSGCSRNHTSNSYKIIATNEMNRQQGSRDSYITSRMLSHLAYRAHLDDGFGHEVLDTDACSIM O94531 UFE1_SCHPO SPCC895.04c; CHAIN 1..319; /note="Syntaxin ufe1"; /id="PRO_0000210282" MTSRTNEFFGLTKNGDIDAANIPLKRISYTDPFLAEGYRIHETIVNLLVFLKKIRGAYLKDRTFSNVQRLSKPLMECSLEELSKLELDEVQRDEIEHEVSSAISSCIHQIAKLQEIVKEQQSQIPKKSGWLQGLRDPSKLSKKETLVAHHSSVLWYLQSELSDVSSVLYHLQDLRLKRGQEKRNIASDFLTKNPTDENSAVEIPESELQTFFTQQQLQELEQENDVLLQEFEHTMERLRDTGKSLADITRLQSEISAQLSIQSSAAEKLYDDALNVMDSLSGGNQQLIKAKSRSSRTARLLFCIFTVMGLLLLSLDRIV O94533 ELP2_SCHPO SPCC895.06; CHAIN 1..760; /note="Elongator complex protein 2"; /id="PRO_0000316551" MFQYEALHVGCNRIPTAATWSSNLGLIYGAERLIAVADPFKEINYLMAGHSGRINCVCELATNSEYRSPFILSGASDKTLRLWQLEEEYFTCIKTIELEATVNCLCVNENLVVCGCSNSSCIVYSWNAEQRNLTEISRFTCSEIIPLEFAIVKLDHGIILTVCGSSKKIMVYGSDSAISSFKLKAVLRGHLDWVRTLSFKKTSGSTATLASGSQDRYIRLWNISLWGSEDEKVSEEFFESVLSNKPVRFTLGKIDLKIVFDALLMGHEDWVMSVDWHPTKEMILSSSADSSMIVWEPDTNTGIWVVTGRMGEMASSHGSTTATGSAGGFWGGLWNPNGNCVVCWGRTGGWRLWKQDAGQWLQLPSISGHTKSVKGVAWDPEGKFYLSAGTDQTTRLFARFKKDNAWHEMARPQIHGYDLTSISCMPSRIGFLSCADEKVSRVFKFPKTIVRLLYRLCDTNIGEESLPDAANVPLLGLSNKATTASETGTVNAEEVQTPVADVIGSLNHPPFEEHLQRLLLFPEVEKLFGHGYEVYACAISNNGNIAATSCKSQTPEHAVIRLYETQSWNQQQVLKGHSLTVTTIKFSPDDRYILSAGRDRLVCLHEQAENLLDYNNFASIKAHSRIIWDASWAPKEMGYFFATASRDKFVKFWKINDNKKICDVAALQFSDAVTAVDFAPFFHNDELLLAVGTEAGKIFIWRCPRENLTKWYPTRLPDHMAPMESINQILWKPTFETMGLYSLLIAGEDTSVRLLNVTLG O94536 UCP12_SCHPO BINDING 600..607; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPCC895.09c; CHAIN 1..1327; /note="Putative ATP-dependent RNA helicase ucp12"; /id="PRO_0000314097" MGSKGKKGKSSEVNLETSKNKEKNIKGKKKNSLDPIEKNKQETAGLQTTSRPTAKQLVGGSSWTGKIPVVLLNEHCQRSKWEKSDVKVRQTKSKNYIFTSVVLAKKDPKNPSILDHVSLIPPKSYYENGYFPEKETLVEARNVGAVYALHRIMSHKSLQHALPPEHRNIWFDMEKQKKEELKNKHSWLYNEDPFKAAKELQAARASSAAKPPPKASQKNEKVSLTSIKNTSLSHFSKFNFKYALPIHMSLENRRSLENLFRNMNTWDILEDTKNLEPDTSIVNDLISLGFRDIHAKEACQYCVSLEDALEWLIIHVPEDDLPTRFLPSDYTTGISVQNLNSANLAIHYNAKRISETGYSFDLCFSTLQTFENNIQISSEYLQQHLIGESFDGNISLEPNSTEWDDDVSALQSILDNKVSKIENGCRVRIDYPTSEFGELFVDFRRPARSYPAHIPLMSLSSTKRMASYIKLSILKKMVVYAMDLRGECMLSWLYNHLQENIEDFLQNIGSLLNISAATIGVSLSSQNKSAPTAKKNNSFKPKLFRRSRELSEKLCNNWSERVKSPSYQLKVREREKLPAWESRRKIMDAIQHSQVVVISGETGSGKSTQVVQFILDHYLSSGEKDLQTVVCTQPRRISAISLAERVAFERDTTVGKEVGYSVHGEKSISKETLLEFCTTGLLLRRIQQHGLGFLSTLSCVVVDEVHERSIENDILLTLLKLVISRIPNLKVILMSATVNSDTFKYYFGNAGHLHIHGRTFPIKDYYIEDFAPKLNEDDDEEDVPRRKKKEYEIDYHLISRLVSSIDAELGSSSGSILVFLPGVSNIARCIREIKSKDGSKFEVLPLHASLNTSEQRRCFKTYTKRKIICATNIAETSITIDDVVAVIDSGRVKQIDYDVERDLVTFKETWASRAACQQRRGRAGRVKKGICYKLYTRGFEEKGMLGQTPPEVLRTALSQVCLNVVPLVKRFSSAGNSVNQGSIKKFMNSLIDPPNDATVDLALKKLIQVGALTVSEDLTGLGEYLVSLPIDLKLGKLLVFGSIFGYLEPALTITAILSTKSPFLGDDEAREIRSKQSQGWGDVLADARVYHNWLEILETRGVKKTVQWCEEMHLHYTTLQQIRQNRNELSEAAQLLELTTKKLTGNFDWYSTENLTVLSTLIAAALSPNVVKCVYPDKKFVASFSGSLEMEQEARLTKFYDQNNQRLFIHPSSTMFVNSPNASRCTFVAYEQKVETTKPFLRNCTPINTYGMILLGANDILIDPLGKGLILDQAYCIKAWPKVVILLKMLKRCLDASLHERLESSSGLNYESEIHQCIRTLIAGNGV O94542 YCD2_SCHPO SPCC1322.02; CHAIN 1..351; /note="Uncharacterized protein C1322.02"; /id="PRO_0000116543" MIESKGETAPSLNLNDVNVEENDAAQSFAEKVQRFRYQMKVHAAPRQKTLHSFLKKDNANIHDFTKVEKPHIRSSKSKVSYNSITSRVTKYFEEKNNSVDQLHSESLTPLSFGHTIPKKKPLLMTASVSEDSRVRVSKRQFKSKVVHPEIAISIAKRHKPKFPLSDELMNVEPGFHHSNIGCQITPYLWISSFRTNVYYLIGNEGDLLSQQVPSISGELNMLRGVCTRIDDDNRYDIEQAGSCFGMSVFPTSDSGEESFTTLESDPIVNCEHDEKKVADNLLVPQVMCSSNISTFFRSPGGKKLYHYLWKNSNALRISSNDLLEILLKHGVYVSLDTLHSWLQERNVNFEK O94543 YCD3_SCHPO SIGNAL 1..25; /evidence="ECO:0000255" SPCC1322.03; CHAIN 26..862; /note="Uncharacterized membrane protein C1322.03"; /id="PRO_0000372620" MKPRPYSVFLFLHIVFYSLLSAVNGSPSLDYFETCSNFVPRAGIPTFSPYAVIKNFDEVNRMYYIQVVGNLSGVITIVGGNGSHIHAASVYSETYALGKLVTSNTTKLCDVVMDPHSFEVPIKCPWAAGSAAFMVKVPFKSTLSDYSKYELTTLTTRVIVVDGTPEKNVITCMKFGLSTTLYYFYPVISYLVVVSLAYVSFSIIYALFLNPWTGSLDPFKSIFNFNMDPDALRLTSLGFFDFVQYLQFAVSTAQVSVMFPKFYINIMAALSWGTALFRFPIFSEPAEYQFADFADLSVASSSYADYLPKSYGMYSFLDSIGIGTACWLPFLIVMVIYLFAALFVALLVIFLKWLMSRIFNETIAETRWDTWSFIAGSLIRLYFLTYFPTVAYMSFQFVAPPTGYEIIPVLWFIFFGIFIPVYLYMNLAFVEPSSKLLEDQTYLHLFGSIYNSFREERVMFWIFPIAVQFMRGITVGVIGSSGSAQLAIFFILEVANVVAYAYVRPHFPQTSMNTLNTFISTMRLITVILMIPLDPRLKVLGISRDLLAYAILFIHIMVCILFLLLSTQRFMEVSARLLGAKSESKGVPLDRPFGWARVFGINELRRRRLKDPYSNGNTMMFDHSTYNSNEMSVPLTPVSVCSNSLKKDGEAAPPKLFVQTNCIPPVTQASSLVPSKNNTASSSSLMLDSPVTPSSPYSTSQGYSFYRPPKPKSSVRKRDMDQLRALQLDFLNNKPNLLRHDVNYAVREADVYHPHVDTSIDSLSQISSQPFEMRPTAIPPPPKNAFQRAWQIVQSTAKSIWHSDPPKESEKGFVVLRSRPRPNLQKPLPQLHIEPSRDEQYSMERKKTDDSLAESAWSIPHP O94545 KA113_SCHPO SPCC1322.06; CHAIN 1..983; /note="Importin beta-like protein kap113"; /id="PRO_0000290666" MQVDPVVYQLQRAVSQDPIAVKDAEGHLNNWKKEPGFFGKLYSIFLDKQNDMSLRWIAIIQLRNSIDIIWRKNTKMSLLPEERDFIRCNALLGSIKSENLLSIQNALVVSRIARLDYPTEWPSLFHDLLGKLQQSLGTGDYDVALRLLITLHHIIKAMAGNRLLRSRQIFYKLAPELLTILQPILHSSLSSWMMILESSKEIKDSTLLSYMQISRYTLKACRRLVVFGFQNPSESEFSERMLAFCAVHQRKLLSMLGTMLQSSRSPIVVGECLEMAFAHAFLFNKPFFDFSFYSPCLTKFPATIDYISLHYDFLGQISSHLSSYKEKFEESSKNFEKLVIMSLRVFILVIQEFCNTKSSHPETAQVLYNSFLVDNRINNLLDLLITKLLILKEEDFEEWTDSPQQWVLEQSTQDVEFNVRPCAEKLLKCFFDAYGDIIVSPFKDMIYSVFECPKTLTQAVQQDTLISSFGVGYTQLKSIFPFAKWLQEAAVPNMASINDIGISRVYRRRIAIFLSQWIEDSSSEQLLEVIYKLYCSFLNLTDPCNDAVVILTTIDAFKTVLDDWNFSENSFLSIKENLFVHVLSLFKAFESVDARTSILSLLGTLLARAGEHVAPMESTIASLLSQLWDGWKKEPLLRARVLAVMHQFVNAIKAKSFEFSTFLYTVIEYCVNPESPEHVIFEADAMELWSTFLMYIQKLPETFTLLIPHLLYHLSQATSTLPFVLMIVSSYQLLDNTVLMKDYSFTIFEKLNDLLDDVKNETLQALCKTVCLLIETTPMDMIYESLLNSSLLSRLLLSIATNDKHPQVLIEYLLVVSRISLREPELILKVCQTKNINIAMLIGNWILLNDHINHSKDRKLNTLALSSLLRTNHPDVLAVLDSIMNLWFSVLSEVEEDANGDATIYYKNDDYSAVGFYLDETSEEMTRRKQLLLKDPVHSVNSRSFFISVFMFCRDANGGMENFQNQYLSTVNPALLEQFQSML O94553 RPC6_SCHPO SPCC290.02; CHAIN 1..301; /note="Probable DNA-directed RNA polymerase III subunit rpc6"; /id="PRO_0000073976" MADQLRTLPKNAKVIYEHCLKQIPNSLSQQDLVEAIGASISVNDLSSALNILLSRRLLDPLRQGNVLVYRAVRLDEAKTVSTMEGDEQIVYSFIKNSGNEGIWRKTLTLRTNLHVSVVDRCLKSLESKNLVKSIKSVKNPTRKIYMLYDLVPSTELTGGPWFTDQELDVEFIENLKKVIYRYVHSKSFPPKKAAMGPDLVWGPEYNGYPTALQIHNWLRSTNITKVDLSLANVISLVDVLIYDGKVEKRSDGASYRAIRVNNENIDAFTESPCGNCPVSDICDANSRVNPITCEYLDKWLN O94559 LES1_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC23C4.05c; CHAIN 22..431; /note="Nuclear bridge Ish domain protein les1"; /id="PRO_0000373865" MQPRFLLHGALLALGIQLCLSIGKITGHISSIEATAADIHDAPSTTTKYVQRTVYAGREKGKIGGPADSWPQRKLDDFLQNHGVKSLDVPPIETPSQFWRKPLQYVSKVTDKCKSFYEKEKNHASHNAQKLDVWIFNSWTNSELSRWLIKNKYEVPEPGTREQLLETVFQASMGDAISTNDELESWSNNLLLSMLDQKNITVPIGASHDDLIVLARRYYDIEERKSQDKVTNITDSQPAPYMKEIIHLWSDGRLIDFLRERNIPISVLSPRETLLKEAYANRFTPRVMIASNVLDGWSSEDLLDWIWKYNKRGSIFSHVAYNSRHELIHAAKLFYMDVASEWSSSDMASLNDSLYSHPSVSKQSTWTEEELKEELESFGELVPVPFSSTKAFERLLPHLYYYLRGPAFLNRIHYWQTFLGNSLKRAFVLSQ O94560 YGD1_SCHPO SPBC1773.01; CHAIN 1..612; /note="Uncharacterized WD repeat-containing protein C1773.01"; /id="PRO_0000316558" MKSNLSLKRQDEKRADKEPNLYTLQGVIQYLQYEAFKNERDHNLWEIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRKDKNISVKDLDEFHLLDKPAANNTKADAEACLLKSKNYIKKSLQEIVYLTNMQPNVSWNVLQEPTRGIKVPKESNNTQQNNQFVMEPSQNKGNVNDANFFEVEYARNENMNKLSSSELISDDLLEDEIMKPLSSGESLPKKEEEVTKSPSFTLDDSVASNEQTLAQLNIESPVDQKKSKAKKKKEQKWTLKFESDKGTSTQCITHQPLPGSTPSFASGTENGVINVWRLDEDSNDNSMGIIKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTSDSISKILTGSTIFQGHEDCVWELFCHEVKDNNPILLSLSSDGTVRGWKYTGEQLFKIRCDSKQPLSMSVTDSRIAIAYNDGNVRFYDLDTQILVSQMRIAGNSAIGNPAVKDRINKIVWKNGNPDRLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGIAFAVNRPEFAISASDGRVFFLRQDDKLSTLESLPSREAQEEITDLSDILWINSPVDKLEHLIVGCKERISVYDRKYLP O94565 OMH4_SCHPO ACT_SITE 336; /note="Nucleophile"; /evidence="ECO:0000255" SPBC1773.08c; CHAIN 1..440; /note="O-glycoside alpha-1,2-mannosyltransferase homolog 4"; /id="PRO_0000316586" MLGWNKHVFFSESRINFRCLLRKKLKKRCPLSARFVLVLLLIVLIFILKMGYKQLIYKLNHPPLRRIDERNDPLFSNGCKNVHLEAQLHPRMNATFVMLARNSDLPGVVSSINSLEKHFNRHFNYPYTFLNDEPFDEKFKETILKLTSANVEFGTLEKDTFGFPGNVDVDAAREAIASQGDRGIMYGDTESYHHMCRFFSGFFYKHPLLLKYQWYWRVEPDVAFTCDISYDPFYYMEENGKIYGYVVALKELEDTVPNLFRYTSAYRRNNNLTSNMWKFFLDAPKKENYDISRKDPTVGLSFSSHLNAMIDSSYSAETSSMEGESYNMCHFWSNFEIANFKFFRNEQYENFFRTMDATGGFWTERWGDAPFHSLAAGLFLSKEQVHYFRDLGYRHSDIHHCGQSLGCNCECIPELSEIESTSGGCVTQWVNLIGDGFLDE O94566 MU184_SCHPO SPBC1773.09c; CHAIN 1..551; /note="Meiotically up-regulated gene 184 protein"; /id="PRO_0000278520" MLARPETDTSVDYYAILKLQKNATFQQIRKQYLFLALQYHPDRNPGDEERAVKRFQRLQLAHEVLSDATKRLIYDQLFGLSTRTRSQYKPNSTSNPSKHTSAYASYNKGKNSKWSSPFASTTKKPQESSEKYSKKSSTRKKEHFNKKPSFPRDTEYSHIYNMKYDPRSGIGIRVKRQEPESLKKENNNSDYLPKSAMKQKKGGPKDSSKHPSNDGKIPESKPSVYKSRASNLFSSNEQSIHSSFGSKFHFDKSSNPFSFEFSPSSNAAKPSNSEECNIPKFNSSFKTSNDFFTFTKTEESSPYSFSFKLEDSNTPKFKSSSKPVKSSFVFTKPEAESSNPFSFDFGSSGPKSRSDTRNNIRTPLWTSSVFEKPESDLPNKTAFGFMRSNTSTFNQKCDDFSSASFMKEKTEFEEQLQEDNDHSLGDLFSKINISTESPSVAMPSIPVIQPPSFPIFSSIDFNVRNREYWNQLMVFQKLYSKYCTESQHFINSWINIKKELHIVPVNWEIFEKVEKSWDQCEEFVAEFRQTEEKYFLFLKRLRELINKNQML O94567 SYNC_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; SPBC1773.10c; CHAIN 1..568; /note="Probable asparagine--tRNA ligase, cytoplasmic"; /id="PRO_0000176499" MAGLESKVSDMKIKSDVVFYIDEASGNDETGNGSQTSPFKTAIHALETDANCTIFVKKNGSEEFEPITTNALKKAKKGVEQAAKKKAKAAEAEAAAAARAAAAKEAEAKRLEAAKNIVLKEPKDAPAAKKIAIIDSTNFRDSRVRVNGWVHRMRTQKGIIFIILRDGTGFLQCVLSGKVYDRASYDFINLGPESTVCLYGVIKELPEGKSAPGNHELVVDYYQILHAAPTGEEAFTNRLNAEAEPSYLLDQRHLVIRGETASSVLKVRARALRAMRDTFENLKMTEVTPPCMVQTQVEGGATLFKFNYYGQDAYLTQSSQLYLEAALPALGSVYTIQESFRAEKSLTRRHLSEFTHVEFELPFVNFGEFLEIIEEFICQTIDRLLDDPIATPLIKQLNPDFVKPSRPFMRLSYEDAIKYLNEHNILTPEGEQHKFGDDIAEAAERKMTDQINRPIFLTYFPLEIKSFYMKRVVDRPELTESVDCLMPNVGEIVGGSMRISDIQELLAAYKREGIDPAPYYWFTEQRKYGTTEHGGCGLGLERFLAWLCDRYTVRECCLFPRFTERCTP O94569 YGDC_SCHPO SPBC1773.12; CHAIN 1..594; /note="Uncharacterized transcriptional regulatory protein C1773.12"; /id="PRO_0000310381" MVPIKKISTACDLCRQRKLRCNGELPKCQNCVVYSETCKYNKRKRVKKPNVDKDDPHIVVGQPPVKKSTAGITREYTEMIELRNHIITLSKRSVNMESRIDDMLNLLNYDLSEKRETSNEIPSLVQQIQNCGFLIDEKMRRYPGIFQIHPKDYTMNDLFPQSFPTWISVYRNVPEKAWANRCVEWYFRYINSCWPLFDLENFMDLFDNFYSDKEKTKGAWVVSFYAIMALAVSRSKRKDKEKISKSLFSTSWFLVQKPGFFLTARLDKIQALTIMIQFCAHLSLYNLCKVLCGQMCLMVKDLDLHKEATNPNVDIEVDELNRRVFWTCYIFETTTSLIFGTPPELGDLEIDCQLPSMDVLPRFTESSQGGIVFCSEIQLTIIKNEIRKKIYKCLASASEEVYKEAVLSIRGKLIVWERNLPDELKQYYDVIKLNGTIPKNVDFENQHIFTACVEIYLSYCITQLYFYDPLTNYETCLEIARKAADAIRSYFMVIEPIFKKICYLWLFLYCPFTPFQILFSNILKMEKGTSDEKIEDLDRMYSLYRFFVEMKEINGEFADKLSRVALDCIDAAEHYLELKSSVGSNIFELESLLV O94570 AATR2_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P00509}; SPBC1773.13; CHAIN 1..481; /note="Aromatic amino acid aminotransferase C1773.13"; /id="PRO_0000308490" MIRNSEDFSHHLSRESKAREKGPFQMLGRIKSSTGIDAISFSSGLPHPNKFAIRELSIKFPQLGCFKEENGTYAKEVNVTFNIKADPSEGLLNFSQSLQYGQCQGISELVGFIKEHIRRIHAPRYENWDIKMSNGNTSGLEYCLRLLVNYGDHVLTEKYTYPAAITAMRALGVQFVSVDMDSEGMLPESLEEIMRDWDISLGPRPHVLYTVPTGQNPTGSTLSLSRRKKLLALARKYDIIIVEDEPYYFLQMEDYNGSLNPAQQKCDGSTFLKSLVPSLLSLDTEGRVLRLDSFSKLIAPGTRLGYITGNSMFIDHITRIAEVCTESPSGICQSVLYAMLHNWGQEGFCAWLQELQYSYTVRRNAFLNVANKYLPNSVCIYHVPRAGLFLWVELNLNHYRFSDTKKSVSQIEMEIFLALVEKGVKTVCGQFFMANPERSTKIFFRFAYSIADFEDFEEGIKRFTSVINEHFNVESRVRICP O94581 COX12_SCHPO SPCC1442.08c; CHAIN 1..86; /note="Cytochrome c oxidase subunit 12, mitochondrial"; /id="PRO_0000194924" DISULFID 33..65; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 43..54; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MSEQEDQEAPKQFTFGTVGFDARFPNTNQTKHCFQSYIDYFRCIKAKGEDFVPCKQFWHAYQSLCPMEWVERWDEQRENGTFPAPI O94582 TRPE_SCHPO BINDING 54; /ligand="L-tryptophan"; /ligand_id="ChEBI:CHEBI:57912"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 262..264; /ligand="L-tryptophan"; /ligand_id="ChEBI:CHEBI:57912"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 297..298; /ligand="chorismate"; /ligand_id="ChEBI:CHEBI:29748"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 324; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 412; /ligand="chorismate"; /ligand_id="ChEBI:CHEBI:29748"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 433; /ligand="chorismate"; /ligand_id="ChEBI:CHEBI:29748"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 447..449; /ligand="chorismate"; /ligand_id="ChEBI:CHEBI:29748"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 449; /ligand="chorismate"; /ligand_id="ChEBI:CHEBI:29748"; /evidence="ECO:0000250|UniProtKB:P00897"; BINDING 462; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P00897" CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00897}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897}; MOD_RES 390; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 392; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 488; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1442.09; CHAIN 1..489; /note="Probable anthranilate synthase component 1"; /id="PRO_0000154133" MKIYPDLKQVQELAEKHKANKIPIYGVIPADMLTPSVAYLKLNQGKKYSFILESVTQGESVSRYSFIGSPYRILMANGKTDPLARLERELKEVKTAPVEGLPSFSGGAVGYVSYDCIKYFEPTTEMPLEDTLGLPEAMFFMTDDLVAFDHAYQTVKIISHVCIQQGRPIEEAYEAAVFKINMLKKKLESPEIPLPEQKKVHLGYEAKSNVGEDGYKAFVSNLKEHIFNGDIFQAVPSQRIARRTDLHPFNLYRHLRTVNPSPYMFYIHCDDFDIIGASPELLVKSEHGRIINHPIAGTVPRGKTKEEDEAYAKDLLASVKDRAEHVMLVDLARNDVSRVCDLDTTSVDKLMTIEKFSHVQHLVSQVSGVLRPDKTRFDAFRSIFPAGTVSGSPKVRAIQLVYGLEKEKRGIYAGAVGRWGYEDDNMDTCIAIRTMVYKDGTVYLQAGGGIVFDSDEQDEYVETLNKLRSNVTAIEETEKLYAEEENSSA O94585 YQ7D_SCHPO SPCC1442.13c; CHAIN 1..187; /note="Meiotically up-regulated protein C1442.13c"; /id="PRO_0000358937" MAIIVEDGSFITSSQWENVEASPKPPPRKPKIVQPKKKPSKHLSNEDALEKYEMLFGERRKEVELDYMSHIAEEETSLSMIEYDRHFALQTDVKLSKKRKSKLVEMTPKGLKKRKRVQIQEGSVSTNTKKRMDGHVVGSSAPAINNGKGKQLLEMMGWSRGKGLGSENQGMVDPVVAVVKNNKQGLH O94586 HNT1_SCHPO ACT_SITE 94; /note="Tele-AMP-histidine intermediate"; /evidence="ECO:0000250|UniProtKB:P49773" BINDING 29..30; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P49773"; BINDING 81; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P49773"; BINDING 87..89; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P49773"; BINDING 94..96; /ligand="AMP"; /ligand_id="ChEBI:CHEBI:456215"; /evidence="ECO:0000250|UniProtKB:P49773" CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+); Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57890, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P49773}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67917; Evidence={ECO:0000250|UniProtKB:P49773}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q04344}; SPCC1442.14c; CHAIN 1..133; /note="Adenosine 5'-monophosphoramidase hnt1"; /id="PRO_0000314651" MSCIFCKIVKGDIPCVKLAETALSLAFLDIAPTSKGHALVIPKEHAAKMHELSDESCADILPLVKKVTKAIGPENYNVLQNNGRIAHQFVDHVHFHIIPKPNEEYGLGVGWPSYPISPEEIKALGEEISSKIK O94588 CUF2_SCHPO BINDING 11; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"; BINDING 14; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"; BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00055" SPCC584.02; CHAIN 1..177; /note="Copper-binding regulatory protein cuf2"; /id="PRO_0000194931" MIIIDGKNYACVVCLRGHRGSSCQHQERALIEVRTRGRPLLCKKCRAIKQQLKSNLKCVCHLQPFLPFANEYQELLNFTQKNPILASLFLFSTDKDIMNSSLNPASQAYTFDLGRTLPISEDILGYRKPLSLTDASNRIDASQLNEKENDSFTINQEADIFNFAKYLHSKDDISGIP O94590 SEC1_SCHPO SPCC584.05; CHAIN 1..693; /note="Protein transport protein sec1"; /id="PRO_0000316616" MTLLELQKELFLSKINSVECATKWKVLIVDTKTADIINHFITIHSLLEEKIAAVEILENPRTPNSSFEALYILHSEEKLVDCILKDEEYDKRYPGIHIVFLDMVKEPLINKLRTSRIASKIRTVQVAYLDFTSLESRYFQVHDSFSGLRLYHPSNAAIIRQELSKVAHGIFSVCVSLGISPNIRCYYPKNAPHASKTMSFILANQLSEIVEEYCSKHPGYHEAASKSTCLIVDRSLDTAAPFLHEFTYQAMIHDLLPIKNEQYPYEILGPQGTEKRTGKLDDDDLVYTTIRHMHMRDAIEKLMKDFNQFCIDNTLFLDKERATSLNDMRSMLAGLSDFQELRDQYSLHLTMAQECMNIFEKQQLNLIGAIEQDLSTGSNVEGKVPRSVLSELLPLLDEGNAEESTKIRLLLLYIIYRDGIILQDLFRLFRHSNLSTSREQIFQNLEQLGTRVIKNLTDQSSKRKEVANSLPAGEDVYELSRYVPTLKVVLENLIQDKLDPELFPYVRNTTPQTEVSMEQTSLRSSRPSWTRSRSMASKLPREKMLVFVAGGTTFSELRTCYELSDKYNKDIYIGSTVCYSPNEWLDFFSKFQQPREALKFPEDKPRHIPCLEARPSPNRIQEQPNIDVPSTRYENTSSSDAVSIHKDEKKSKGKSHKLGKLMMSSKKDKDKSKEKVPTYGTSDKKKKKRFGVF O94598 SEC5_SCHPO MOD_RES 50; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC622.10c; CHAIN 1..815; /note="Exocyst complex component sec5"; /id="PRO_0000374043" MSADEEILAHYGLTSLSQDYWTEKPDFAIANASVDVQSPTTGVHHERNRSEDILRTGGATSETTKDASAAGPVTPSFAMKRSQTSVQPSMSSQIAIGGMRNPMATRKIAGTYRDAPDNSMQQTSTGVHRSSSWLTTDGTHQLLSLMETNFNKFIAAKETIDNVYAQIISTLSHAGPAKTMDMCEESISGALQQLQLFNTESTNEVDISYGELLVMRECEALFTYPEKFRLYHKQEKYSLLMQEIENAKKLYEKDRERLAKVNPKLVYLVDHAWEIIQATIDGICASIWNQILQSQGDFAFVVRTLCDLLKLKPNPISGRDPVLYATVSQQKYLYNLMKERFSYFEKIIKSRQEDFSKLSCTRASPMLVWRAVARGCNLDYTLRGRPEVFAGMQLIEWANACVLKIVREIKEVELYAKEFISGIQQASYPEAAKHYGRDPKQMGVVVEKLNSQCLEMVYSFVGERGERLEMDGAFVLIQLHYFQRVADLLPKRIRTVFSMAATRCIVDTWMLQHAPQSKSANIEEMFIVDANENQVLEPELMVVDVLRELNKLYIPPHREEIVREIHHAFYKVLYANARFPSMSVSMANWESDVWSLASSTLIDFVQHRNQHDMKKLASKMTTSLPVFSTSITRSDVLHFVTRLLNLRSRLVPYQKFLLQTFPLNEVSPSLDPRISKSLRNLQDLYKLLAIRDTSFSNTTPSSISKLSIQPPTFQLFSTLETIYLELKDSMPPNEAADWMIATTSCMLAQFALHSPYAFFHDIPSISHFLNKCLPPTILDLLQQIQRKAEASSISPTTETATKTRLKFQFIEMIFS O94600 TTI1_SCHPO SPCC622.13c; CHAIN 1..1098; /note="TEL2-interacting protein 1"; /id="PRO_0000353822" MSHIQSIFAQIRDPFRKLSFYSLPLSSETSSVDSNGLKNSLKDAYFGLEKALTNTDADLPLNLCDYIFFPIVPVLKSWYRVPSTGVEYAIQCVNLLYKHGWREAHNEMLTMQLLLMLLNIADGWKSPSETVEQDFRVREITFETLENVITDFKPNFHDKRQYLLFARALSSALDIIPNKNSSRRLQFASLCCVQKLICPKQYRLPTEFLTTFLPGIVSGLTKGLAPNGTCQYFKNVCISLNILGDTVVKAISDDNTKDLPDEKDASSNSHFFGPTKRTKSWKRATCQQLSNAVKAILHLRSSQNLHVQDALFDFCFILFRDCLDSLKDCRIHLLESMLKLINKKENPKLRDYGMNKLVSLIESFNNITMESVLTECLNDWSTTWSSVSTFASEDNKLEELNRLKSLLSISSHLPKTLQLMEPLLDGILSQLVPKSSGIDSNSQKLLTSSTSNEYIHGEFFGGNEMERTTQEIVTSFAKAPNVKYVMQSLLSKATSATNENSVRAFWAFMVLLKSDVETVDSLEMYIDSLEQYSFEVLQQLSQLNVFTKASLEDKQKKEKYNLLCVRSCIAIDSISWISSLQGVKFRSKLMAYFYPLLEHLAFASPYVSSFAEACIQAIATNCNYSTPAELLRENIDYVVNSVALKLNTLDVSPQLPIVMAYVIKNDDGGCIRYIGDVVDAIFGILDAYHGYARLTEGLLGILYAIIKQESINGEEKKLIVGVEEDAMNEDKNKPCKKIREFVQLLLENPNYPLPKDDHELEDMIHDEQQETKSGHEQFREHAMKEKEKKGKENENMGETTVDHENINSNVMDEQGEKQKDDVVDMVRKITEKAQLFLSHEQITIRVEMLKLLSYGSNVLAKEPNTFYPAINTFWPLVVIQLDTDNELLVECALETIYQVCALADDFMTSRIRQDLLPRLETLCQRWHLFNVARTYSSEHRLQRAMLKVTSACVANKLSIVVYLKLMGITAPIIRAITHMSQKYAGDESLVEETWNAFSKQNPDAVYYEREVRGSQMIDTFSTELLIPGKQRVQRTYRRTHEVLEPVGAKTSETVFNDLLGQQGSGKTETQEEPLPSLDNLLHLNQPKKGAKKPLISII O94606 JMJ4_SCHPO SPCC622.19; CHAIN 1..473; /note="JmjC domain-containing protein 4"; /id="PRO_0000300500" MSELSTYKGYSPKHGDKVPVLQNLNDLTPKDFYDKFIATRTPVIIKSSLPESDWKGYLWQQQDYLLSKIGDIVCKVEPIDPVSGTFGQGMSRNEMSIKEFFQKLKNGERLYLTTQYDESNEVLDGDDEVSLLVKSLCPHPTDGLLTDFSITPALMGNLVPQQCNLWIGKSENGTSSGLHHDFHDNIYAVISGYKRFVIISPDHANQLKLSGKISKIHPNGLISYEGEDCPQRSDGLTELDAAIAKTQFLEKKIGSLKELAVPQESIELLEAEYENEMDRVLQMQIGGPEEDWNDLEEGDAASLLDGSVGGDPESDILLNEGNDIEATSLQDTKPELPDHFTKVSVNGLHKFMGFDDAKNVDVDKDELSALAGTVPLVVDLEPGDMLYLPASWFHEVTSSSASSGGSDVHIAFNYWFHPPDNLEDFDHPYLDRNIWQAKRHLVGEAIDQLYATNKKNEKRPAEDDSPSQKKTCQ O94607 STR2_SCHPO MOD_RES 46; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC61.01c; CHAIN 1..597; /note="Siderophore iron transporter 2"; /id="PRO_0000084880" MTENYGSMEHRKKSFRNNENLEQQFHPLREELDNAGPINDRTSELSLEGVSKAEAIASTWSKRSIIVAYLGLYLLSFASSLEQQTTYSLQRYATSNFSAHSNLATINLVGNILLAVVRAPMVKAADVFGRSESLSLALGMTVLGYLSLAFSRNIQMFTVAYILYICGQTGLGLLSQLIIADTSSLLNRGILSAIPELPYLATVWIGPVLAQAFHPEKNYGWRLGYGIWAFILPTVSLPLLASLFLNQRKAKAAGLYREHHNLINHSTPEKLRLFYLFWQELDGLGIVLFVSGFTLLLLPFSHSSQVVSPDSTILTLFTITLSIALLVTLCFYDVKYARYPVFALKSLKDRTILGSCVLIFTYFMSYYIFSNFLTSFLQVSYGLSIDMSSLTLNVFVFSMTTTAILSGFLMKRFGRFKMLLMISVPMYVLGILGIILFGINDNHYTRPLVLVLILAGMGGGLLTLSAQIAVQSVSSHAKLGMNLTLYLTFSSVGGAFGSAIAGGVWSKRLSSRLLHDLKDHLPVPEIESIFRDLRTALSYPQGTQIRNIINVAYTATEKDLFHISLVASLFMFAGLVIIRDVPLSTENHDTAVETPSE O94612 YFO5_SCHPO SPAC1296.05c; CHAIN 1..258; /note="Uncharacterized cyclin-L1-like protein C1296.05c"; /id="PRO_0000310347" MADSLVHSLASSSQLEAFDSFEYAEELCTLGSEWIQEAGVLLNLTQNCVIVCLILFRRYCTLYPPRVPDLDAIVMACVSIGSKTTETPASVQDICNVVVYLKERFKDTNFEARGFIAHDLYSEEMYSSRNRLSNMELEVLRALNFDTHIVIPHKLAIHYLQTLQLIDNKKLLQITWNFLNDASRTRLCVLYPPFSLACGCIAMAARVIGMKLPKDWYRVFDTTKEEIDSLTSILENFYKTSAIAHKTLYLIFTEQVSA O94613 NDOR1_SCHPO BINDING 12..17; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 59..62; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 97..106; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 132; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 343; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 373..376; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 407..410; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 448; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 503..504; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 509..513; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178"; BINDING 584; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255|HAMAP-Rule:MF_03178" CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA-COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; SPAC1296.06; CHAIN 1..584; /note="NADPH-dependent diflavin oxidoreductase 1"; /id="PRO_0000167621" MKNSHIYILYGSETGTAEGLAESLFRSLTRMGYDVLVNSMDDFNLENLLRPLQCVFICSTTGQGEMPLNMRKFWRFLLRKKLPNTFLNDMQYAVFGCGDTSYTRFNWASKKLDSRLRQLGAQSFSSRGEGDEQHPDGVEGVFAYWCNHLYSQLAAIKTPSRPAFGEFDLLPPSFQIIIDESLGCKVKGFEDNNIVRHSRGKIEATLVHNKRISNIKHWQDVRHLAFKIPNFERWKPGDVAVLYPWNDDMSVNSFIECMGWESIKYSPLIISSNVAERKLPWFPNILNVFNLVKYVLSIHSVPSRTFFEMASHFSNNKMHKERLQEFSSYKNIDDYYDYTTRPRRTVLETLQEFKSVQIPIEYALDAFPVIRGRQYSIANRCDNSTGILELAVALVKYQTILKSPRQGICSRWICDLHENTSFNIDILPGFLNLSYQSNKPLIMVGPGTGVAPLRALIQERIYNGLKENLLFFGCRNKSMDFLFEKDWEKYTEEGTLKLFCAFSRDQEKKKYVQHSIQENGELVYNLLNEKDGMFFVSGSSGKMPSSVKDAIAGIVSKYSGCSISDGYSFVTSLEKKNRYYQETW O94615 PPR8_SCHPO TRANSIT 1..55; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1289.06c; CHAIN 56..481; /note="Pentatricopeptide repeat-containing protein 8, mitochondrial"; /id="PRO_0000303930" MQGFGSQIFRKLLRSSNAKVSDALLQNTRTLFTAPPLHSGLQTSFTAETQQHVRQNSQNLLKQLNDEMKARKYTETVATFSSLKPFGILDSQTINRYILFLVDRIKMLNGRGNVDEATLDKLDDILRYAIEHQEIASARFWRIMLQSYIDLNLFDKASLIADMSLSHMEFLPKDERVLGNLYISALQAKILGGASFEQCGKIGSAIHEQLEGKEVVNELVAVYLIYTVFKDQGISSKAHKALVQFNGLTSFHSDVIISVFVNKGLVDQAAAYLKNSNLNERNLPTIYTTVWLLQRLFEAHHSLDPLLTIFDYYLSVSPKDITRLTNAILSLSMKQFERDRDIKKATDFITTFINKMSDVKEFKPSISTANTLFSIASRLKDVKWLSAGFDMIDKYGLKPTHVTYRSLLKAYCLLPSTCEQISQAWVNLEYRLEAISISVADKEINLLKDCILSQPDRDDQQSCLQFLNMVLSKYGKHIRSP O94617 UAP1_SCHPO BINDING 103..106; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 117; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 194; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 220; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 221; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 251; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 378; /ligand="UTP"; /ligand_id="ChEBI:CHEBI:46398"; /evidence="ECO:0000250|UniProtKB:Q9M9P3"; BINDING 410; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; MOD_RES 405; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1289.08; CHAIN 1..475; /note="Probable UDP-N-acetylglucosamine pyrophosphorylase"; /id="PRO_0000185772" MDDKELFDRSIFEETNQLHLYDQLNYLKKNDLQKFRKLLNQVQQLDLRSLWLKYRNAKATSQENRKLSPSEVGPLSIVDTSDSSWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALARAAFPDQEASISIPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEACKATENVDGHKHLLLRAANIAYHYFSFDFLQKASLHSSTLPIHLACKKIPFYDVTSHHYTTPLNPNGYKLESFIFDLFPSVSVENFGCFQVPRRTSFSPLKNSSKSPNDNHETCVNDILSLGKSWILKNGGILSPSDCTYVSPECSLQGESLEWIKGKQVSNCKLY O94618 TIM21_SCHPO TRANSIT 1..23; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1289.09; CHAIN 24..223; /note="Mitochondrial import inner membrane translocase subunit tim21"; /id="PRO_0000043165" MIRTIQRQSATRFSSALVQRRLYSLASDSLNKQRKPQEEGRLARIFKDPSNKAWKDLTAPQKAYRTSANIGNFSIVIFGGGVFGLIIYALVTSIWKGEAHYGDEAFELLKANEECRYVFGDHMKALGEATHPLRRTHGILTSRVWDHHGVEHLVLQFHLIGNERKGHVFGRLVNVQGDYKWEYLFVDVANYGKIIIFDHTNSVRQQHKNFGLWGSLKNITWGN O94619 ADN2_SCHPO MOD_RES 89; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1289.10c; CHAIN 1..743; /note="Adhesion defective protein 2"; /id="PRO_0000303959" MADPGLRSGVGLPSQQGQKHDLQKDQKQPHVNNADRTTQSLLNSYIYDYLIKKDYCEAARAFGREAQVQTLVRSQEETNSLAKRHKRMSPVAVKHEGISNNESSDENMNVNNGNLDSFSSSSAPPPPPILPIDSAGGFLIEWWNVFWDIYNARRGQGSEPAKAYMSHISNLRKKSRLNLQEIQKNSLHTGNTSHPYANASFPHDPANAMGQQIDSSQFHQGAGGLNDRNQHLMRQAMLNNQSRETFPPTAAQLQQLKQLHYRQLQSVQQQQKQHQQKKTPQSGSTPQMQNTTSQPTTHDTHPPKQQGPISDFRSIPSSPKTEGAPSNAQFRPSLPATPNGSVPQSNPLYDTTGLNGGQYPVVQNSAQPLLHEINFASNRNPHLKQGGAVPSSTLPQQQKSLDKPKPAQQPSTGQFSGNQMNQYGFSNSPYSQNMLYNFNGNANPSRLNPALKNYMEELKLLEQQNKKRLLLVSQEKERKGYTSASPDRPLSQTITESSVAKTKSTTPKSTDTPTEATTSPVKVSTKNSNTTENLNGINESNMPMLQNGLPLRTSGDHPSNYSNLIENSSTSDTNNADNGMDVMGNWQLQQTHSSRPTPNASSPLDVRSKQKPSSANSNAPTPAPTVNTTNPESSTNEATSVGPALEPSQGANVHKSDSELDNQNQSGKSNPDTSATPSAPTESTTVATKSSDNQLLDVGNSTDIDAALLNDFDFDKFLKDTSTGDDLWFGLFNLPDNEDSTAA O94621 US109_SCHPO SPBC1289.12; CHAIN 1..365; /note="U1 snRNP-associated protein usp109"; /id="PRO_0000082020" MSTSLWLNNLEEWMNEDYIRAIFENVRKVNYYEDGESGAILKTCCIEFESQDAARNALERQSTQRLISGNPISLDVVPEWQKPSYYMLFISNIDPEVSENDIKYLFQRYNFISARVLRCVDGTSTSIAFIWLANESDIQNAQVEMQGAFCLKRSILVHSVKSDKNTYLSSPGFYGTPQPLNQFTDPNNTAVYVHQLPENITTQELRSYFLHFGEILYTQVNNNSGRIVFAQRYFAEQAINEMNNFPLHGVRIQLSWARPPSMALLPSKQSTYWPALAAPVYPSMKDVPNNPFTPFSPINPYYAKSWNHTASAPLLPPGLKNGSDYPYLSVPPDILNDSYLAMCEAVNSRLDAESTMLLPVHYSQA O94622 YBKD_SCHPO SPBC1289.13c; CHAIN 1..375; /note="Uncharacterized alpha-1,2-galactosyltransferase C1289.13c"; /id="PRO_0000339340" MRWYSYVIPAVILSIIAISGVWWNATLGTRLDQKVQLFLNEHSSILNAVYETTTIVYTEPLHTSVSETITSTSFVTETTTVTPTVTATAQELSTLNPHPENSKIVLLMGSNAQNDPSSPLNPYIRTIIKNRRDYAERHGFKFEFLDLDEYKPSIGDKPAPWAKIPMIKNVIRKYPDAEWVWWLDHDALIMNRDLNLVDHILKHEKLNSLLLRDTEYFSGFGIDSEGFRTPKNQDPDDIHFIIAQDFNGINAGSFLIRNSEVGTWMLDFWNEPLYKEHNGVFVEQQALSHMIYSHPIVHKHVGLVTLRSINAYDSSDPAWGYEDGDLCVHFAGCFVFQTCAQNFEKYGKIITEKQGHDWFDPSEKEYIEQRLFPQP O94625 SPJ1_SCHPO SPBC1347.05c; CHAIN 1..381; /note="DnaJ-related protein spj1"; /id="PRO_0000071092" MFTNNFSQKQILGVSKDASESEIRKAYRQLTKQWHPDKNPGNEEAQEKFIEINKAHEVLSDPEQRKIYDAYGEEGLNGQPGGPGGGPGEGFPGGGFGFDPFGDIFDNIFGGRRRQNAVRRGPSMEQIVQIHLSSFYTGGSFTLEIPVKRTCSVCSGQGFNPKYSADKAIESCPVCGGSGFRVIEHMIAPGFRQQMRMPCNACNGNGRTIKHKCPRCKGERVAEVVESFDIKVPAGAPEGYRIGFRGKADEIPGMEAGDIIVILEAAGGDYGWTRKDNDLYRKETISVREALLGNWKRKIQKLDGSFMEVKRSAGEVVHPGETERVKNQGMPIYNLHKGKTTSAHGSAYIEWEVKFPKKLKGKFLKDLNNLFEKYDNEFDEL O94626 ORN_SCHPO ACT_SITE 202; /evidence="ECO:0000255" SPBC1347.07; CHAIN 1..252; /note="Probable oligoribonuclease"; /id="PRO_0000111093" MQGAFLNNRIILQSYHIKKRLYSKRTSSLHSRFLQPTYRKNICQISKPIFQQDLSTNTNFISKLKSPFSNLKMSNLKQPLVWIDCEMTGLEVGKHVLMEVAAIITDGNLRPVEEKFDAVIKLDEKQLSEMNDWCIEQHGKSGLTERCRQSNLTVKDVENQLLAYIKKYIPKKREALIAGNSVHADVRFLSVEMPKIIEHLHYRIIDVSTIKELAKRWCPDIPAYDKKGDHRALSDILESIGELQHYRSYWLS O94627 RNH2B_SCHPO SPBC1347.08c; CHAIN 1..293; /note="Ribonuclease H2 subunit B"; /id="PRO_0000343167" MQGKIFILPKDSTNQQFVELSHPLTGRPLRYLLTNDHLLQILQVGDSSKQRSWFVGDHVVSDGYLYVCTPIDLLALVLPIIQELTWSRRKEPNRYVSFEDFIEHFDNMGPHYPRVSEVLSPNLLNTLHRICKVNEPVGSLPKTFQLDESSVVKILLRKAKVAQENLPPSIVTELKKQLAPLDLRTPLPQDLLELSCKWHAASLVCEDLQPEWYNKLAYWQEELAPLHAYTKNLEESRKILVEKEALLNSKKRPQNSDITSSLLKKPNRKQATKKSKYFSGEGMTKISSFFTKK O94629 SRO1_SCHPO SPBC1347.11; CHAIN 1..106; /note="Stress-responsive protein 1"; /id="PRO_0000116756" MFSILKQGVISKSLLAATSLKATASRFSFSTSVASRVDGTKNGWSFTASNVADQTTDIGINSESAMSCNDQEQPLSFYVQTVRDDLNSPNWGAEQRKGAFDWEVSA O94630 ARP1_SCHPO SPBC1347.12; CHAIN 1..379; /note="Centractin"; /id="PRO_0000310306" MTVTEIFDNQPICIDNGSGFIKAGFAGDDIPKCLFPTCVGRIKHERVMPSSIQKDMFVGSEAQNLRGLLKIQRPIERGIIQNWSDMEEIWSYIYSDQQLNTLPEEHPLLLTEPPLANIRNKEKIAEYFYETLNVPALSFSLQPVLALYASARTTGIVLECGDGLTHSVPIYDGFSIPSAIQQEEIGGRDVTDYLQLQLRKSGHELVSSAEKEIVREIKEKCCYVASDFRSEIESWTEHKPQIHTYQLPDNQTITLGTECFSAPEVLFNPEMMGSEASGLHIQLFKSILLSDIDLRSTLYSNIVLSGGSTLLRGFGERFISELRAISGKKNQVKIYASPERMHNAWLGGSILASLSTFRRLLITSEEYKNDQNVIFRRRF O94631 MRM1_SCHPO CATALYTIC ACTIVITY: Reaction=a guanosine in 21S rRNA + S-adenosyl-L-methionine = a 2'-O-methylguanosine in 21S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:47772, Rhea:RHEA-COMP:11907, Rhea:RHEA-COMP:11908, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; Evidence={ECO:0000250|UniProtKB:P25270}; TRANSIT 1..11; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1347.13c; CHAIN 12..301; /note="rRNA methyltransferase 1, mitochondrial"; /id="PRO_0000337261" MIRSRVNLAREVPKKAKAHLSKERRLIKEDSEFVFGTHSVKNALATRKRECRALYVQNADIHSEFEEFLNKLQYKIPIKSVNKEHLNQITACRPHNGVVLEASSLNVPTISDLLFPAGEEYNNKNGQDSPHNDLNEGKSSSSDNYPPLYVYVDGITDPQNMGAVIRSAYILGAKGILLSKKHNTFLSPVVSKASAGALEVFNISHVKNPMVFLRNSVLKGWKVIGTKPALPDNKDQIYTPHKIKTELMNEPKILVLGSEKGLRTNILTQCSHYVSIPGGDKYVDSLNVSVAAGILLYSLVN O94633 DPM3_SCHPO SPBC1677.02; CHAIN 1..90; /note="Dolichol-phosphate mannosyltransferase subunit 3"; /id="PRO_0000195003" MQRIHKVILYYVSLTILYRVTYLFDLEEPWSTLRPYTPYLFILAFGSYLGITLLYNVATTNDKPEAYVDLVKDIKEAQDALRSKGMTIED O94636 TRM11_SCHPO CATALYTIC ACTIVITY: Reaction=guanosine(10) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(10) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43128, Rhea:RHEA-COMP:10355, Rhea:RHEA-COMP:10357, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.214; SPBC16D10.02; CHAIN 1..469; /note="tRNA (guanine(10)-N2)-methyltransferase"; /id="PRO_0000316241" MSVYLLHLASTHAHFHLPELETLAKIENVEFWLIPKSEYLNVAFKSDKSRNQALFSHAIKEFQDSISPNDATTQNPFMLAVVNSNEDARRWIRRSIFCKGIYEIYCIGDSFTRLHEKMKELNPAPWDSFKHNSSYKFTFETFGTRRTMKEQLSIISDFEYMQLQGPVSMHNPQHVFTVLENRRNNVEGPKVYFGHWCGSGSRDAIDTFDLKQRSYIGITSFDAELSLVTAQMAMAAPGKLIYDPFVGTGSFLYTCSFFGAHTLGSDIDGRQMRGKNGRSIKSNFRQYKLSPFFLDTFTGDVTNCPLRKNLLLDAIVCDPPYGVRAGAKKIAKCSQRPPKESSSTGNHYPKLEQYQISDMVYDIICFASDRLVDGGRLVLWLPTITEEYGIDDIPSHPYLSLIYNSIQPFTHWSRRLLTFQRLPRAHDSKSLNLLPKINNKTPSHHNFREKYFSSAGRASASTKFSPVLE O94657 XDJ1_SCHPO MOD_RES 410; /note="Cysteine methyl ester"; /evidence="ECO:0000255" SPBC405.06; PROPEP 411..413; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000396659" CHAIN 1..410; /note="DnaJ protein homolog xdj1"; /id="PRO_0000314108" LIPID 410; /note="S-farnesyl cysteine"; /evidence="ECO:0000255" MVVDTKLYDILEVHFEASAEEIKKSYKRLALLHHPDKAPIHEKEEAAERFRGVQEAYDILKDPESREMYDMYGMNSDSNSQFDGGVNLDDVLAQMFGMNFEAGGPGKNVPRDRKRRGSDVIHDYEISLEDMFKGKEVKLRATRNTLCPRCQGRGGKRFAKEKPCLSCDGKGVKQHLKHVGPHHVTNSQVICDTCNGKGVSFRGKDRCKHCKGSGTVPEQRMLSFFVNRSAKENDKIIQRGMADEAYGITPGDVILQLHQKPHPVFERLGDDLKAKLKISLAEALTGFNRVILTTLDGRGLEYVQPIGKILHPGDCLIIPGEGMYKDSKTDLRGDLYLEVDIEFPKDGLIGTTEIEILRDILPSIPKVSVMDDTLIDSVRGVPGDISHFGGDARYANEDYGDETYEGVPECQAQ O94658 RL36B_SCHPO SPBC405.07; STRAND 6..8; /evidence="ECO:0007829|PDB:8ETC" HELIX 24..27; /evidence="ECO:0007829|PDB:8EUY"; HELIX 33..45; /evidence="ECO:0007829|PDB:8EUY"; HELIX 50..60; /evidence="ECO:0007829|PDB:8EUY"; HELIX 64..75; /evidence="ECO:0007829|PDB:8EUY"; HELIX 78..98; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..99; /note="Large ribosomal subunit protein eL36B"; /id="PRO_0000195019" MAPGLVVGLNKGKTLTKRQLPERPSRRKGHLSKRTAFVRSIVREVAGFAPYERRVMELIRNSQDKRARKLAKKRLGTLKRAKGKIEELTSVIQSSRLAH O94660 NIT2_SCHPO ACT_SITE 41; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 114; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 156; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" SPBC651.02; CHAIN 1..276; /note="Probable hydrolase nit2"; /id="PRO_0000314762" MTLAAVAQLNSSGSILKNLAICKELISQAAAKGAKCIFFPEASDFIAHNSDEAIELTNHPDCSKFIRDVRESATKHSIFVNICVHEPSKVKNKLLNSSLFIEPLHGEIISRYSKAHLFDVEIKNGPTLKESNTTLRGEAILPPCKTPLGKVGSAICFDIRFPEQAIKLRNMGAHIITYPSAFTEKTGAAHWEVLLRARALDSQCYVIAPAQGGKHNEKRASYGHSMIVDPWGTVIAQYSDISSPNGLIFADLDLNLVDHVRTYIPLLRRNDLYPTI O94661 GYP10_SCHPO SPBC651.03c; CHAIN 1..373; /note="GTPase-activating protein gyp10"; /id="PRO_0000208019" MKKKEIKQLKNEIKIALLNSDVETLSHIGKEGHGFLMKSLRKSVWVSLCGLSCRHRMECLSRSTSQSSYADQNQVHLDSERSFFQYKLNPFLLRKHRSQLTKLLSVVFKHYPELCYYQGLHDIAQILLLTLPFSHALPLMEHLVFYRLRDFMLPTLDGTVKQLQLILAVIKARDPTLYEYLIKADIQCYFALSWLITWFAHDVSDISVVCRLFDFFISSHPLTVVYTCAQVVLDNRTSIIELLWDNSGADLLHSYLCKLPASINVNQLIKNTCATISAVPFSSLPLDRYQISPYSCLRNTGDPWEYMSRSNGLLLFRLQLAELQEEKHKPGTKVPAVFLQENIFNGCNMLAAITVIGIGIVASQLIPKSTSNS O94664 MU166_SCHPO MOD_RES 184; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC651.06; CHAIN 1..234; /note="Meiotically up-regulated gene 166 protein"; /id="PRO_0000278514" MPRRAVLFRGNSFISFSSISSGNESSAHGDASLGQADKPLTVDVLDAWTTQFTKKQTRVFHEAYVSAYIDLQQKYARLERLQEQILNLERSLLNYKSLKSNSTTTVATVPSEKRYFFRRKPKTSSTTNSLSSSSSSVSHMNQDANPNSTVLTFTAVPYDSCLPAPDRHTPSSASSRASETGTTSPQSMRNQISLLYSKVDQVKTEIASAQAVMHDLLRTYPGSESLQQSTHTQF O94666 RPC1_SCHPO BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 69; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 106; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 109; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 153; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 493; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 495; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 497; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; SPBC651.08c; CHAIN 1..1405; /note="DNA-directed RNA polymerase III subunit rpc1"; /id="PRO_0000073951" MKDPIDDQIPKRIKHLQFGINGPEEFVKDGTVEVSRRDLYTMTDRSPAEHGALDLHMGTSNKQINCATCGESMADCMGHFGYVKLALPVFHIGYFKATLTILQNICKDCSSVLLSDQEKRQFLKDLRRPGIDNLRRSQICKRINDHCKKMRRCSKCDAMQGVVKKAGPLKIIHERFRYVRKSQDDEENFRHSFDEALKTIPELKMHLSKAHDDLNPLKVLNLFKQITPVDCELLGMDPEHGRPENLLWRYVPAPPVCIRPSVAQEGATTEDDLTVKITEIIWTSSLIRAALSKGTPISNLMEQWEFMQLSIAMYINSEMPGLRPSDMPSKPIRGFCQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDQVAVPYRIAKILTFPERVTTQNKKHLQDCIRNGPDVHPGANYVIDRESGFKRFLRFGNRNRIADDLKIGDIVERHLHDNDVVLFNRQPSLHKLSIMAHLVKVRPWRTLRFNECVCGPYNADFDGDEMNLHVPQTEEAKTEALELMGIKNNLVSPRNGEPIIAATQDFITAAYLLSLKDTFLDRKSISNICCYMMDASTHIDLPPPAIIKPRCLWTGKQVFTVLMKPNRFSKVLVNLDAKTRSFSRIKSKTPEMCPKDGYLMIRNSEIIAGVVDKSVVGDGKKDSLFYVILRDYGALEAAEAITRLSKMCARFLGNRGFSIGIEDVQPGKSLSSQKEILVNKAYATSDDFIMQYAKGILECQPGMDQEATLEAKISSTLSKVRDDVGEICMDELGPANSPLIMATCGSKGSKINVSQMVACVGQQIISGKRVPDGFQDRSLPHFHKNSKHPLAKGFVSNSFYSGLTPTEFLFHAISGREGLVDTAVKTAETGYMSRRLMKSLEDLSSAYDGTVRSSNSDVVQFVYGDDGLDPTYMEGDGQAVEFKRTWIHSVNLNYDRHDSAMLPYEIIDYVNRALDDPKFLTNCNRDFIETIRTFVIENIAKYLASVRERRDLAPMLEEPDMDDLDDMEGDEFAPVAKRKSVENIIRVTEKQLRSFVDRCWEKYMRAKVEPGTAVGAIGAQSIGEPGTQMTLKTFHFAGVAAQTTLGVPRIKEIINAAKTISTPIITGQLINDRDERSARVVKGRIEKTYLKDVTSYIEEVYGPVTTYLSIQVNFDTISKLQLDITLADIAAAIWNTPKLKIPSQQVTVNNTLQQIHVHTSSDGKSSETEVYYRLQTYKRVLPDVVVAGIPTINRSVINQESGKIELFMEGTGLQAVMNTEGIVGTKTSTNHVMEMKDVLGIEAARYSIISEIGYTMAKHGLTVDPRHIMLLGDVMTCKGEVLGITRFGVAKMKDSVLALASFEKTTDHLFNAAARFAKDSIEGISECIVLGKLAPIGTNVFQLIRRTEEEEEQKPKELLFDTPSLHQLEITA O94669 AP3M_SCHPO SPBC651.11c; CHAIN 1..425; /note="AP-3 complex subunit mu"; /id="PRO_0000316199" MSTIEAIYLVDTNGALLLQLESRGRTSPITLEHIKNELFRYKLRNEEPPFILHNKNFLIFQELEEDVRLCIPTTCDTEPLYIHDIMRRIVDVVKTFFGGFNASKVEKNVCVIVQLLAEMIDYGYATCMEPNALQDIVPLPSFMNKFMAVTGLQTNTPTLARDTVPWRTAKAKYATNEFFIHVLERVSAVYQPNGKLAFGTVKSDMECKCQISGMPLLLLSLRPGTKLGNVRFHQSVNLKRWKQHPDQIEFIPPDGKFTLASFQTDFATQKSLPVVVEAKNKLDGRFEVRIRNTGKKSVENLKILITIPQALKSVTVTEGNYIFRASKYTHMEEGILEWSVKKLAWTSPALVLTGFLAPLKKDANSTEESSSYSKLEHLDLQYKLQGSTLHNFKVESLKMLNHPDKKSYKGVKHTIIAQNVSFRFR O94670 YBWC_SCHPO MOD_RES 123; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC651.12c; CHAIN 1..273; /note="Uncharacterized protein C651.12c"; /id="PRO_0000303934" MSSKKVKYNPRKSASQNEATSASAGSKAFGFNSAKKEKLHRMALSMEAIEDVEDQSFNGKSSNLVRKRRGLDEDIDEFSSSSEDERKPARHPQSSSQKPFASSTYNVELPTSPTKITNIGQSSPRALRYLSPESQRIKNAKMKSPISTHLAKYSIHHMGTPPSKPSFLSSSVSSPASSKQKSLFQCTKDLEKRYINRVHRSSETELVQLSSIKVLDRFLSDIYLVEAEKNEEKCTVLLLKRSNTDVDNSSSLSLTLPLCKFTKNGHQVHIHPC O94676 UTP22_SCHPO SPBC776.08c; CHAIN 1..1097; /note="U3 small nucleolar RNA-associated protein 22"; /id="PRO_0000317218" MNGLKREHESSSSQDGSKTPETEYDSHVDSIEDIHSLASKRKKLNEKKENLEDLTLLKTSAFELKLNELIREISVRGKYFRHANTFVEKIKDLIFKTPVIPETNFWSACKNLEKDKKVIVPLAEPLSAKDTNLRASFVPPKTVTPGIFSCSNKFFLNPDGWSYDLFLEIPESIFTQKDYLNGRYFRKRAFYLTCIAKHLLENLGNEVKLEFVAFNDDIRRPILAILPESKGFAATGKRFTVFLIPTVRQIFPVSKLLPHKNAIRDFMEHEELKPTPFYNNSVLEEQNLLFYRDLVKKYSVNPQFLDACGLGSTWLNMRGFSSSIHSNGFGLLEWYVLMALLMSSTGLPAGNVLNTYLTAAQFFKSMLQFLSSKNLTSTLFKLNADSSNLKIGNGHLPTLIDCNTGFNLLGKMKQSFFEYFQASCRHTLNLLDENANYNFSKIFITHVNVPALEFDVSGCIPLEPKELEDPNFCRKTDLDSPYSLYLEYTWDLLQHALGDRVCQIILYSSICTSCSINESLKTKLPKLISFGLLLNPDALLRLVDIGPSPDDTVGSQKFREFWGEVSELRKFKNGSIAESVYWECSSPDERIRIPQRIIRHILNRHLGNNVGDRVSFRNEKFRVYVHSKISPNTDTYNEYVPVMEAYNEAVKSLINLSDIPLSIAEILPADESLRYSSSSVPFYESSTCAPIDVVFQFESSSKWPDELEGIQRTKIAFLLKIAELLEALDNVERASVGLENTDNPTHNCCFLQVLFSNNFTFRYRLRNDREIFFWKSLERNPSTKLSAQKGLYAYEHMFQFIPRHTLAIQAICQAHRSYSMAVRLAKHWFYSHLLTDHVTDEVIELLVASVYINSSSWRTTSSGETSFCRMLHFLAHWDWRFDPLIINSNGKLPHDVRHQATEKLESIRKQDVAIAHNAYYIITDYDFDGNHIGYYKPSKIIANRITSLARASLSELLKDTPNYKSIFKSSLDIYHVVIDVNINKLPMYRESNLTKYKNLQNMSSERPGFEPITEFVKELHRCFEDTISFFYNKKNPKVVTGVFNPRILANRPYRTNIDYPFKVVDKDTVVLDADVVCEEIRQVGGDLIRSIQLQLKA O94677 COG6_SCHPO SPBC776.10c; CHAIN 1..675; /note="Conserved oligomeric Golgi complex subunit 6"; /id="PRO_0000339330" MDVKSKHGHIKSNPEESLLFRNSVSKNIAQLSSINYADRNVQAALEQLSERKFKNEREARKQLPFEVFSDLIWTNGSIIKELSELSSQTLSVQSQLLKVKNSIDSYKNEWSKKTNDAQILLNSYETFCEEEALIEEKLKNIEIFEKNFVIMDDDLIHLTSSTDVDDRFYLILDKAQEIHDSSDSLFASLSGFVEYSSFEEIVKKMSRYIEAAFEKLFRCVQTELSDPQTAQTLEANSHLKKAFTKLFSEPTMVNKSINLIVQARQQILSTAYLTALTRGDFLSSSRPIELSAPDTVRFIGDLLAWIHQTIVNEKELVEALFAARKRQIQLNPFPPWDVPNVLEDQMNSLLDGSLYGICRPLSSRAQTSVLDLSDIVRLYNVIEILGFYREAFSKIVHDECIILRIIKTLEDFTYQRMKTVLDDELYTISNTNLSITDDLLPPDFVTTFLRNANSIFKIRGASLSVQGVDELPFKMLFMQLFDRILEICAAMTEDVRPPYKGIILMLNVLDSCTNYVGRYTFLNELFEYLQEKTTYYKNNLTTLLNNDYIAQAGLSDLLQKIADTTDDKQALKNYLHSWKWDQQIDKFSTFIRKTLSETIDNLQLLTSPIVTNQVLKETAISFVGAIETVDKALELSNLERRWPLSTEELLIAMNVDSMDTLSDIGQSDIDNLSVN O94685 UCP8_SCHPO MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 113; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC83.01; CHAIN 1..829; /note="UBA domain-containing protein 8"; /id="PRO_0000065716" MQPLQLSPIEQQEFDRLLESLHPEQKDLIPGSVIGPFLLKFGLPQKILAKIWDYCDQEDKGSLDRNQVYACFRLISQAQRGATLQELDYNKAGDPPILPKQAKDDHHIKRSSSETADFTPFRIPINPDERSEYEKEFRENLRGHEDSARPGCMPSSIAKPILLKSSLHYAVLAQIWNLADSAHVGYLEMYQYVIARHLVAICKQYNLIHLPRSLPADVIESAKSETPAMNTNIEQGVTQPSLVNTEQLSHQQSISSTKSSKLDEISADNNAQSAVDNKYSSPPQTIDPQANIKALITPEDRSNFYQLFSKIDNENKGYIVGGEAVPFFMASHLDSEELARIWDTVDTQDRGYIDKDEFAVAMEIIKLRLSGKSLASILAYDDNPTEPTMQQNLVSDDTNASTAVPVAFTNDNVSNVPLSVADNEPNSTLNLLASSDTAAFEPTAVSLHENPSSSLEDLQSAFQNTSFQDQVSTQNQANTADISQNTESGSSTQGQMFGIPPTTQSIPLKMAGFPGGVNSSLTDIKEEEAVSENAPQQEERSFEQIKTSIHIAPENISAIEESKSVPLPTSFATTIPGSTSAALDDQQTTEAPFEEPDEPAHEPTEEEQEEMRKLEEKIESTKYGLETIQTSGKTIKQRIEQKKTRLMILREELQELDAIKEEAQKQISQSLIADQQLSTQIGSVGMGKKQAVKELRKLQAKIDSIIADSMSPMGTGAVNSPAIKPQVTPAPPTPAPTPAVKHHPPPPPVRSSISPSMPPAPLTHANSSTPMNYVSQPESPPQSYESIQNDNELLQELLSMGFPREKAVIALEATNYDVNEAANILLSSV O94686 RL43B_SCHPO SPBC83.02c; CHAIN 1..94; /note="Large ribosomal subunit protein eL43B"; /id="PRO_0000139837" MTKRTKKVGVTGKYGVRYGASLRRDVRKIEVQQHSRYQCPFCGRLTVKRTAAGIWKCSGKGCSKTLAGGAWTVTTAAATSARSTIRRLREMVEV O94691 JMJ3_SCHPO SPBC83.07; CHAIN 1..752; /note="Lid2 complex component jmj3"; /id="PRO_0000084288" MQQNVKEKHAGKSDTSVSSLECEIDYHIEGSDGIPVVEPKISEFVDMESFIRRVERLGKKYGAIKVVRPSSVLNPWNEDTMKPSDVKMDLWLERMVRRKGEYFEIQSDIDHGSAGPKKPTDMNVDDRFPSNAGSSNDFENNVAKAIAYYWRSLTHDSLWYGYTNRPSIPFYFIPSISAAQKDRVHLRSNTLINTWPNVGHLFAGKWKTTLPWRVESPELHAVQVHLGGSSLQWYVIPSAHSESFKKLAGKLAQDEHWRCSDFLLHQNILFPPSTLVQNGIVTYSTVLKQDELLITFPGTHHSAFCLGDAVLRRFVFRSPRSASNYEFSNLRRLMVSESLYSSKSLWPHSHKPQRACSQKFLDEFYLHDLPESNIHDSGNFHPIHSSVDNNSFSQRDFDSPNSINPPSPLMSNHESASTEHFNSTTTTEKELSSLHVGEERKNRSLPLSLIWNSKAREEYIKKQKEENGDNIEFSHFDPLYTRPSSHPLHPPPILGLPVPAQFARGELFLGRILEDRVSEHMLLLECEKSDVVEVPYECILTSSSAAGRRESSYYNPALKAPNIVYDDGVPINWNEYSELPSLDRFVLPKLLPGKPIEFTPPISVEPTSIKTIAAEESSEPTSSVDVAPTPVEDVNVNLESISNTNESVVDLSDPLVSKNGFEDVERSSVADLEEDVLETRSSIFETSDIDDRLTVIDRSQSVVPSESEFSIAGANLTRRNAVDFSVSLDTYELYVSDEVENVDDFSLFPSLE O94695 YG1B_SCHPO MOD_RES 348; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 352; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 355; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPBC83.11; CHAIN 1..449; /note="Putative transporter C83.11"; /id="PRO_0000315881" MVLRERLSHILFHEKVGFLLLCLLWYISSAVTNTTSKSIFNELRCPVTLTFLQFGFVAFFSAVCLLFRKQFLGGTGIQKPSKYVLYTTLPLSIFQIGGHVFGSLATTKIPVSTVHTVKALSPLFTVLAYRFMFRHVYSAMTYFSLVPLTFGVTLACSFELSADIVGLLYALISTCIFVSQNIFGSKIFMEAKSHSTHTKKHYNKLNLLLYSSGVAFIVMIPVWLYQEGFAYLPEVGSPVFLNLIYNGLSHFFQNILAFTLLSIISPVAYSIASLIKRIFVIVVSIIWFQQATNFTQGSGIFLTAIGLWLYDRSKKGNLYESCKVKEFEKDALELEEQTMEDEKSYPSSGTQSPFYGKNFLPQITPRLDSVVPLISDSPMTPNSVYSNEGVTSSVSGNATPASVRQSTQNDFSNSNIHDRRSSYTFQLNNFKAPQPSRLWATETVPTLKI O94698 NSA1_SCHPO SPBC83.15; STRAND 2..7; /evidence="ECO:0007829|PDB:8EUY"; STRAND 10..15; /evidence="ECO:0007829|PDB:8EUY"; STRAND 33..37; /evidence="ECO:0007829|PDB:8EUY"; STRAND 45..47; /evidence="ECO:0007829|PDB:8EUY"; STRAND 54..59; /evidence="ECO:0007829|PDB:8EUY"; STRAND 65..68; /evidence="ECO:0007829|PDB:8EUY"; STRAND 71..73; /evidence="ECO:0007829|PDB:8EUY"; STRAND 75..79; /evidence="ECO:0007829|PDB:8EUY"; STRAND 96..98; /evidence="ECO:0007829|PDB:8EUY"; STRAND 101..103; /evidence="ECO:0007829|PDB:8EUY"; STRAND 111..115; /evidence="ECO:0007829|PDB:8EUY"; STRAND 121..124; /evidence="ECO:0007829|PDB:8EUY"; STRAND 131..135; /evidence="ECO:0007829|PDB:8EUY"; STRAND 137..148; /evidence="ECO:0007829|PDB:8EUY"; STRAND 150..159; /evidence="ECO:0007829|PDB:8EUY"; STRAND 177..181; /evidence="ECO:0007829|PDB:8EUY"; STRAND 197..203; /evidence="ECO:0007829|PDB:8EUY"; STRAND 224..229; /evidence="ECO:0007829|PDB:8EUY"; STRAND 234..238; /evidence="ECO:0007829|PDB:8EUY"; STRAND 242..244; /evidence="ECO:0007829|PDB:8EUP"; STRAND 246..249; /evidence="ECO:0007829|PDB:8EUY"; STRAND 256..262; /evidence="ECO:0007829|PDB:8EUY"; STRAND 267..272; /evidence="ECO:0007829|PDB:8EUY"; STRAND 277..281; /evidence="ECO:0007829|PDB:8EUY"; STRAND 286..290; /evidence="ECO:0007829|PDB:8EUY"; STRAND 298..304; /evidence="ECO:0007829|PDB:8EUY"; STRAND 307..312; /evidence="ECO:0007829|PDB:8EUY"; STRAND 315..321; /evidence="ECO:0007829|PDB:8EUY"; STRAND 326..331; /evidence="ECO:0007829|PDB:8EUY"; STRAND 336..343; /evidence="ECO:0007829|PDB:8EUY" HELIX 41..43; /evidence="ECO:0007829|PDB:8EUY"; HELIX 84..86; /evidence="ECO:0007829|PDB:8EUY"; HELIX 205..207; /evidence="ECO:0007829|PDB:8EUY" TURN 116..118; /evidence="ECO:0007829|PDB:8EUY"; TURN 168..171; /evidence="ECO:0007829|PDB:8EUY"; TURN 173..175; /evidence="ECO:0007829|PDB:8EUY"; TURN 239..241; /evidence="ECO:0007829|PDB:8EUY"; TURN 263..266; /evidence="ECO:0007829|PDB:8EUY"; TURN 273..275; /evidence="ECO:0007829|PDB:8EV3"; TURN 282..285; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..387; /note="Ribosome biogenesis protein nsa1"; /id="PRO_0000320403" MKLLLGDEIGQLKFIEIKKGTDTSNPESEAPVIQKFGELDREKGVLFMLKHEMNVFVARKNGTIECWNVNQEPPILSSLWQLDSSLLETASIVSMKYSNGWLMLALSDGNLLFRHIESSKLRKLQLHGPLSAVELHPRIPGIIAAGGKENDVCLYSCNPTCKSNIDELELWRTENVVKVFQGKNVKNDSLNLRVRVWITGIVFTEDIINVIDGKSEDDESLCFHFATITHYGQLRFYDTKHGRRPVSTFDVSTSPLSHVGLLPSIKLLYFADKRAQISIFDHSKKKVIGRFQGVKGAPSSIHCLGNVVAITGLDRNVRIFDADRKPLANAYIKALPTSIIVINERDAEIIKKEEELEAAKEEEEEIWRNMEQLEDTEDKKPSKRIKL O94700 MBF1_SCHPO SPBC83.17; CHAIN 1..148; /note="Multiprotein-bridging factor 1"; /id="PRO_0000149812" MSDWDTVTKIGSRAGPGARTHVAKTQSQINSARRAGAIVGTEKKYATGNKSQDPAGQHLTKIDRENEVKPPSTTGRSVAQAIQKGRQAKGWAQKDLSQRINEKPQVVNDYESGRAIPNQQVLSKMERALGIKLRGQNIGAPLGGPKKK O94702 ERMP1_SCHPO ACT_SITE 207; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P80561" BINDING 161; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 173; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 208; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 234; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561"; BINDING 307; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:P80561" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P80561}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561}; SPCC1259.02c; CHAIN 1..822; /note="Putative endoplasmic reticulum metallopeptidase 1"; /id="PRO_0000372386" CARBOHYD 146; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 291; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 617; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 682; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 706; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 758; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MVLVCASSSKCKRNTFLQLAMVLFAVVMARIALYFHNHLDEPLVDPYDANGNPQFSEANALKHVIHLSDDIGYRILGTIEQERAREYIMNEVLALQKQLQDGPNADIHQMEVSLESGDGAHRFDFMNKYVIKKYQNLKNIVVRLSNGTEACKEEAVLINAHVDSTLPSPGATDDALAVAILLEAIRIFISRPVPLTHSIVFLFNDAEESLQDASHMFITQSPLRDTIKCVVNLEACGTTGSEILFQATSNEMIKAYSHVPHPFGTVLADDVFRTGLILSDTDFRQFVQYGNLTGLDMAVVKNSYLYHTKKDLAPYISPGTPQNFGENILAILTYLVSPEADLNNMKSSGTVYFSVFNSLFFMYSKLTSKILNTLVGGLGILLTLRGSEGSFTVALIAQVISIAGIFVIPNIWAYILGNVLDCGMSWFRNEYWPLFIYLPAIFASLFFTESLFKRSEHLALRATIFIFSLLTFIPLPSAYLFTIIDFFMVFALFLNDKILAKPGTVHPLTYFIGSIGAMTVGFESAINLLEIFVPLTGRIGTDKVADNVVATVCVCGFNIYFPLMSPWIQRFRSRCCFRLGLLFSIFVVGFSSFILAKQDTYYDSLHPRRIFVQRMENITSNEVSLHIASADSAPGFDKLSSDLSSLLTDEPVVKTEMDDWNSDWDTVYPFSQFLGSYRIPLNDTVDVTTLPSIKFSNKVVKDNVVNVTVTVEHPGLIWTVVSFDADVLSWSLPEVPSTVRRHHVREVSAYGLDSYSFNMSYLEAPIYFDFVGVDGVGHYPSKASEGRDRASIQLCEKLTNDYLPDWTDTLCIGVVSGNFKLE O94705 COX9_SCHPO SPCC1259.05c; PROPEP 56..58; /note="Removed in mature form"; /evidence="ECO:0000250|UniProtKB:P07255"; /id="PRO_0000041772" CHAIN 1..55; /note="Cytochrome c oxidase subunit 9, mitochondrial"; /id="PRO_0000041771" MAVGPVTGMFKRRIVTDFSVTMILGTLGACYWWFGYHKPAARQREEFYVKLAAEKNAE O94707 RXT3_SCHPO SPCC1259.07; CHAIN 1..351; /note="Transcriptional regulatory protein rxt3"; /id="PRO_0000374009" MEEKTPENEQSKKTFDPKDSMKIEETSTNGSSQPSQPSNIKLSIGSILESSNDNGDPEYSENGMGNMNMNTLPMATSTPMSYTKQPSEAKYPNSVWERKGVSDQEENTSSVKRQKTLPTQSSGEEEAKYSHPGAPTATSADSISMESRPSNLSTSLSKTTSYPQFQVRQFVSPIISIDNSALEPFLNRYPASESLFPVTEYEYTPWLEFPLLYSSIGKFVRVTIDIKWLNAAINPRLCRREIWGTDVYTDDSDIATILAHCGCFSLLKPVRKIAVVDLYILPPLVHYKGTRKNQIESRSWSSRQDGISLKIKEVTWKPACASIFENSIHTLTLEERLQARLELSRSSTFKI O94709 ODPX_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 76; /note="N6-lipoyllysine"; /evidence="ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU01066" SPCC1259.09c; CHAIN ?..456; /note="Probable pyruvate dehydrogenase protein X component, mitochondrial"; /id="PRO_0000020486" MLKHYIHQCVKASSCKHSLSVKQRYFHCSALNGVASMFRMPALSPTMEEGNITKWHFKEGDSFKSGDILLEVETDKATMDVEVQDNGILAKVLIEKGSNIPVGKNIAIVADAEDNLKDLELPKDEASSEEQSFSSSKEEVKPIVQDRETKSNVEHKSTSQANDAVNKSFLPSVSYLIHQYKIENPWSIPATGPHGRLLKGDVLAHVGKIDKGVPSSLQKFVRNLEVLDFSGVEPKKPSYTEDSVPVRKSTMIETLKTVPMKDEYITFERSISLEKLKSLLAKRKEKDAFGIDEVVSAMIGDALSISELSKVEPNSIESAYDLLLGAPIVKLKSSVSNFQPKLFPKNNNTKDLHKYIRDSMIGLPSNLSDYVKLNFSSVTKSSSNNVEFLDDVYDMLLGSNSDSIDSRINRHEEPSTTEDLTLTLSIKDNISKSRAIKFVDCLKSNFENPEFVLSRW O94710 QRI7_SCHPO BINDING 157; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 161; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 179..183; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 212; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 228; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 232; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 328..329; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 363; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179"; BINDING 364; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179" CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence={ECO:0000255|HAMAP-Rule:MF_03179}; COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03179}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03179}; TRANSIT 1..78; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03179" SPCC1259.10; CHAIN 79..412; /note="tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial"; /id="PRO_0000255599" MLCLVYNSILCKQRRISLKVLQQFRCWNISKTFLSYRTLTALAIETSCDDTSVSVVRTSDSSSHCQNEIICLNTHRTISKYEAYGGIHPTIVIHEHQKNLAKVIQRTISDAARSGITDFDLIAVTRGPGMIGPLAVGLNTAKGLAVGLQKPLLAVHHMQAHALAVQLEKSIDFPYLNILVSGGHTMLVYSNSLLNHEIIVTTSDIAVGDYLDKCAKYLGIPWDNEMPAAALEQFASPEINSTSYSLKPPIPLNTREKVHSASFSFSGLESYACRIIRKTPLNLSEKKFFAYQLQYAAFQHICQKTLLALKRLDLSKVKYLVCSGGVARNELLKKMLNDTLMVLQFEHQPTDIKLVYPSPDICSDNAAMIGYTAIQMFKAGYTSSFDVEPIRKWPINQILTVEGWLTKKNKKV O94714 SPT2_SCHPO SPCC1393.02c; CHAIN 1..406; /note="Protein spt2"; /id="PRO_0000339143" MAGTPSFQKLMALADSQSAQAAVQIEQLRKAQIREKAREITEERNRQRKLQRERELRQKYEEEQRRQQAMEAKRIAASTRQTSERPPLSAEEAKRIREVKEKDRLESKKNERQGKPRSYNELLRQASSAPAVNETSSSGLLQSKDKRSQSPHSPKKPVKNSSSRDQPVRNSGATSTASLPPAGLRAGRGSQISASLAWLKTGGASAAPSNPRQPPPTSNFSNRKARYASNGLVQLQTGPKRDKRSAGEVQDEIMKRRQNSSISQAATPRTVSNSETSYVGSPALKQSKPNSLKSNNTSRKTSASSAITKPKARPHTSRHDEFVVSDDDELNDRVPDVSSEIWKIFGKRKQDYVSRDVFSDEDDMEATGHDVWREEQAAARAARLEDELEEQRERERELAKKRRKNK O94715 RS15A_SCHPO SPCC1393.03; CHAIN 1..153; /note="Small ribosomal subunit protein uS19A"; /id="PRO_0000130049" MAEEHDEAVRVAELRKKRSFRTFAYRGVELEQLLDLSAEQLVDLFHARARRRMLRGLGPNASRFIRKLRKAKTEAPLNEKPATVKTHLRNMIILPEMVGSVVGIYNGKLFNQVEIRPEMIGHYLGEFSITYKPTKHGRPGIGATHSSRFIPLK O94726 MNL1_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAC23A1.04c; CHAIN 23..787; /note="ER degradation-enhancing alpha-mannosidase-like protein 1"; /id="PRO_0000373874" CARBOHYD 479; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 609; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 670; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 693; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 756; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGSLHSIFCVCLILLCIFKENSIVGAINSARMVELRETSRRLFYHGYNNYMQFAFPNDELAPLSCEGLGPDYENPNNIGVNDVRGDYLLTLVDVLDTLVVLGDREGFQDAVDKVIHHINFERDTKVQVFEATIRILGGLLSSHIFASEEKYGFQIPLYKGELLTLATELAERLLPAFRTPTGIPFARINLMKGVAYREVTENCAAAASSLVLEFSMLTALTGNNKFKASAENAFFSVWKRRSGIGLLGNSIDVLSGRWIYPVSGVGAGIDSFYEYAFKSYIFLGDPRYLEVWQKSLESLRHYTASLNEYYYQNVYSANGMVMSRWVDSLSAYFPGLLVLAGELELAKKMHLYYFSIYLKFGQLPERYNLYTKSIELNGYPLRPEFAESTYYLYRATKDVFYLHVGELLLSNIENHLWTPCGFAAVENLEKYTLSNRMESFFLSETLKYLFLLFDDDNPIHRSHHDFIFTTEGHLFPVTNQTRLSTSQRIYDGGEVCVAEDYDRSKWPMLYSLIASRDDYDYVSHLVGIDNKAIPSYLIDPSGVCKRPEYSDGFELLYGSALVSPIKSVERVTNNVYISDIIGNKLKFVQKEGSNSLFLYTAGAESINENDTVFLTDPDYETFTRPDALYFDRTIAQLENPNSGQKTFGKFLQFDNDNSLPSKVFKTVLLNNSMCQKPSDTLDKDTAYIAPLGNCSWVQQAKNTNKAGLLILITDGEFINPLENIHSQNSLFNWVKPYIPPTILLKNENNFVSKWANVSVRQSDFDAPSYFQGTPVSNLYLCLKCINS O94729 TTI2_SCHPO SPBC1604.17c; CHAIN 1..467; /note="Tel2-interacting protein 2"; /id="PRO_0000116753" MQYYKELARRLHTLQSKNEKEALEKQIDFLDKLVVEVDSLVHEQDLRPLLEFISPTESWFLLGTATIFYIKLLTHPDPESIDVVIKEAYVVRAHRILSIFQEQFIENVVKEINWEILAILISLSGIENGLVRNLSEFLSTSILSAVPRQKFLLYLLEKYQINLFHREERLTDQGRPVAFELPPDKFHSDQSKALLEPKWKTKNYLISHLIFWIIDQQSSSSIEVCWHRIIPSVLRILNDLSPNIKLQGIELVNRLLKITEREFLLYTGILKILKDDLLVFYTFIPPRFTIQTSVTLINASFATLVSLYPEENENLNSIMLNGINSVFQFAFDYPLILQAAFSQIMVLTDKMNVSYLPYLTLTLDELCRIIQNPQIIQIPSTLSFFLEILTKLLEIYSYRISAHHVELLMALVVCSRNYMRCNLQEHHNAIVQALQNLFTLIKLNITVEQLGDYNVILPLLEPLQIPL O94731 TR851_SCHPO SPBC1604.19c; CHAIN 1..658; /note="Transport protein particle subunit trs85-1"; /id="PRO_0000343161" MDIATNFITRSLSEIAPNASQSSLHVTPSSVSNNAFGLKLRQLISDTYCPHIFIMASDDTENFMKRKGFDDFASFIRPFGDRIFQSSTNNSAISKETLDSRIFDNDHDSIRFVPMEAVQVPRQWKRNKAWNTENGLENCANSRFAPGGDIDSFRVLSQKLIEEWVQSGSNNYPENGFLNPILDYLKLLLSGNPVAEHETFSHPVGCLIVITSHNTNPMATVMRLFKEINNAPFPNFISKEILHYYLFIHDEDNNDLSNSKQIFQQMRRSLGANSHFIRLRSNYISAKPLDTDRYDTSSIQSLKNAPRDSMESESFCSSSDDAKPITFVTKNLRKFPIPEWRSSLEVQAESEQSCLPLYPLLPVEEVEGMKKFVQTMLYDSIYPFMQRCVRAWEEDLTPQYGNLTTRLLFASKKYWSRNHSSHSQGNYDPLSLIYSSEKQESIKRKMADFSFMLRDYKRAYEIYDEIRNTFSQDKAWNYLASCEEIQIICLLMQNRNISLKSQISYLNKWFDEMVYIYAVRLHSFYYTFRSVLVTSLLLSLKPAFSIDFAASWLAKILEPGPISLNPFETSFLNTTIAGMYSNKEHVGVTDGNRRRKAAFWFAYSAGFWRDCGHCKMAEICWNLANRVYSKSGWESLSEHMLDLKPTLSENFRVKNTFH O94744 GIT3_SCHPO SPCC1753.02c; CHAIN 1..466; /note="Glucose receptor protein git3"; /id="PRO_0000195085" MLHLDYTFNVSDATSTSSIIIVSRRELANLRIMVIIASAISIVFSLIAIFWRWSRRRTIREQFHIALFSVLFIRSIVQMIHPCLALSDPFFWAPKHRCFTIGFFLLVLVRMTDYWIFINILHNALLVLFPHVDTERRGLYRFRHTVFTLSFVIPLTIGGLAFTNKRNTFVNLQTRCYLPYTPVRFMFGLNWSFDYALSIAIIALQTCMFISIRRKIKRFKKYSHQQTNVFDTLNVIDSYPTAPDQVALPPFPDTNSTLTYTPSNSQSIYSSQSQPSPYSRPLLSSVHPNLPPGSQSTPANLNQSGIHFEQDFRDSPNRTNGLEDHTSFKLSSPLTSDEDGASSVLAAYGNDMQDDPLLKQRKRILSQSKFLFAYPAIFIFMWILPQIQIIVILAQPLHCSGSCKRFAFVAVFADNFVAIFIALSDFIWICYRGYTYLKERDSSKSYWDQIKELTLKWWRGKFGEEK O94745 MPPA_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC18E5.12c; CHAIN ?..502; /note="Probable mitochondrial-processing peptidase subunit alpha"; /id="PRO_0000026772" MSFLTTPKMLSEYQCLKNIGFSHKTVLKRRLFRKECTPALKSFYSTQDPALNEVRTEKLKNGVTYVCDPRPGHFSGLGVYVKAGSRYETKKFSGVSHFMDRLAFQATERTPVGEMKAKLENLGGNYMCSTSRESMIYQAAVFNDDVKSMSKLLAETVLAPKIQEDDLVHYRDSIIYENSELWTKPDALLGEFAHVTAFQNNTLGNCLLCTPDKVNGITATSIREYLKYFYRPEHLTLAYAGIPQEIAKEITKELYGHLPSSSLPPLEAIPSHYTGGFMGIKKSEAPPVPYQQEFTHVVIAMEGLPVTDPDIYALACLQFLLGGGGSFSAGGPGKGMYSRLYLNVLNQYPWVETCMAFNHSYTDSGLFGMFVTILDDAAHLAAPLIIRELCNTVLSVTSEETERAKNQLKSSLLMNLESRMISLEDLGRQIQTQNGLYITPKEMIEKIDALTPSDLSRVARRVLTGNVSNPGNGTGKPTVLIHGNVDEVGDVFALCKKAGIGH P05501 CYB_SCHPO BINDING 82; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_label="b562"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"; BINDING 96; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_label="b566"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"; BINDING 183; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_label="b562"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"; BINDING 197; /ligand="heme b"; /ligand_id="ChEBI:CHEBI:60344"; /ligand_label="b566"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"; BINDING 202; /ligand="a ubiquinone"; /ligand_id="ChEBI:CHEBI:16389"; /evidence="ECO:0000250|UniProtKB:P00157" COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P00163}; Note=Binds 2 heme b groups non-covalently. {ECO:0000250|UniProtKB:P00163}; SPMIT.05; CHAIN 1..387; /note="Cytochrome b"; /id="PRO_0000061762" MKILKSNPFLALANNYMIDAPEPSNISYFWNFGSLLACVLVIQIVIGILLACFYIPNMDLAFLSVERIVRDVNYGFLLRAFHANGASFFFIFLYLHIGRGLYYGSYKYPRTMTWNIGVIIFLLTIITAFLGYCLPANQMSFWGATVITNLLSAVPFIGDDLVHLLWGGFSVSNPTLNRFFSLHYLMPFVIAALSVMHLIALHTNGSSNPLGVTANMDRIPMNPYYLIKDLITIFIFLIGINYMAFYNPYGFMEPDCALPADPLKTPMSIVPEWYLLPFYAILRAIPNFQLGVIAMLLSILVLLLLPLLDFSAIRGNSFNPFGKFFFWTFVADFVILAWIGGSHPENVFITIGAIATIFYFSYFFILIPVYTILGNTLIDLNLSSIKR P05752 RS6A_SCHPO PTM: Phosphorylated. MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000255"; MOD_RES 236; /note="Phosphoserine"; /evidence="ECO:0000255" SPAC13G6.07c; CHAIN 1..239; /note="Small ribosomal subunit protein eS6A"; /id="PRO_0000137339" MKLNISYPANGTQKLIEIDDDRRLRVFMEKRMGQEVPGDSVGPEFAGYVFKITGGNDKQGFPMFQGVLLPHRVRLLLRAGHPCYRPRRDGERKRKSVRGCIVGQDLAVLALAIIKQGEQDIPGLTDVTVPKRLGPKRASKIRRFFNLSKEDDVRQFVIRREVVPKKEGKKPYTKAPKIQRLVTPRTLQHKRHRFALKRRQAEKNREEAAEFAQLMAKRVAEAKQKREVVKARRASSLKK P05767 RL39_SCHPO SPCC663.04; STRAND 44..47; /evidence="ECO:0007829|PDB:8ETC" HELIX 7..19; /evidence="ECO:0007829|PDB:8ETC"; HELIX 25..29; /evidence="ECO:0007829|PDB:8ETC" CHAIN 2..51; /note="Large ribosomal subunit protein eL39"; /id="PRO_0000127043" MPSHKSFRTKQKLAKAARQNRPIPQWIRLRTGNTVHYNMKRRHWRRTKLNI P08090 MEI3_SCHPO SPBC119.04; CHAIN 1..148; /note="21 kDa protein inducing meiosis and sporulation"; /id="PRO_0000096401" MSSQNTSNSRHPASSASALPNRTNTARRSTSPRTSTGSSSTNTNTKTVDHAGTTFISSTSKRGRSTKAGSVHSVPMKRTKRVRRTPAQRIEHENKENIQTEKVYRIKPVQRVLSPSDLTNELTILDLFHVPRPNETFDITDRVNNTSR P0C5Y7 TEN1_SCHPO SPCC1393.14; STRAND 20..31; /evidence="ECO:0007829|PDB:3KF6"; STRAND 34..39; /evidence="ECO:0007829|PDB:3KF6"; STRAND 42..47; /evidence="ECO:0007829|PDB:3KF6"; STRAND 62..71; /evidence="ECO:0007829|PDB:3KF6"; STRAND 74..82; /evidence="ECO:0007829|PDB:3KF6" HELIX 9..14; /evidence="ECO:0007829|PDB:3KF6"; HELIX 88..100; /evidence="ECO:0007829|PDB:3KF6" CHAIN 1..102; /note="Protein ten1"; /id="PRO_0000312638" MDSAKLIFINQINDCKDGQKLRFLGCVQSYKNGILRLIDGSSSVTCDVTVVLPDVSIQKHEWLNIVGRKRQDGIVDVLLIRSAVGINLPRYRQMVSERQKCD P0CAN8 NXT1_SCHPO SPAPB1A10.03; CHAIN 1..115; /note="NTF2-related export protein 1"; /id="PRO_0000373860" MESSVKYAQEFVQRYYSSLDTNRNGIAEFYRENSLILWNGKPMQVTEFTSMIVNLPYSKTKVEDFDSQQVMGNDMNIIIVVSGTIRFDGKKPHVFSYVSFYCIYLLVLRSSTNFL P0CT34 TF21_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAC9.04; CHAIN 1..1333; /note="Transposon Tf2-1 polyprotein"; /id="PRO_0000097504" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQLQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT35 TF22_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAC167.08; CHAIN 1..1333; /note="Transposon Tf2-2 polyprotein"; /id="PRO_0000424424" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQLQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT36 TF23_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further. {ECO:0000269|PubMed:9774697}. SPAC2E1P3.03c; CHAIN 1..1333; /note="Transposon Tf2-3 polyprotein"; /id="PRO_0000424425" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT37 TF24_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAC26A3.13c; CHAIN 1..1333; /note="Transposon Tf2-4 polyprotein"; /id="PRO_0000424426" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQLQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT38 TF25_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAPB15E9.03c; CHAIN 1..1333; /note="Transposon Tf2-5 polyprotein"; /id="PRO_0000424427" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT39 TF26_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAC27E2.08; CHAIN 1..1333; /note="Transposon Tf2-6 polyprotein"; /id="PRO_0000424428" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT40 TF29_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPBC9B6.02c; CHAIN 1..1333; /note="Transposon Tf2-9 polyprotein"; /id="PRO_0000424429" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQLQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT41 TF212_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPCC1020.14; CHAIN 1..1333; /note="Transposon Tf2-12 polyprotein"; /id="PRO_0000424430" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT42 TF27_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAC13D1.01c; CHAIN 1..1333; /note="Transposon Tf2-7 polyprotein"; /id="PRO_0000097505" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISIAPAHFQYFINTILGEVKESHVVCYMDNILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT43 TF28_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPAC19D5.09c; CHAIN 1..1333; /note="Transposon Tf2-8 polyprotein"; /id="PRO_0000424431" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISIAPAHFQYFINTILGEVKESHVVCYMDNILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI P0CT56 RS14A_SCHPO SPAC3H5.05c; CHAIN 1..139; /note="Small ribosomal subunit protein uS11A"; /id="PRO_0000123358" MATNVGPQIRSGELVFGVAHIFASFNDTFVHITDLTGKETIVRVTGGMKVKTDRDESSPYAAMLAAQDAAAKCKEVGITALHIKIRATGGTATKTPGPGAQAALRALARAGMRIGRIEDVTPIPTDSTRRKGGRRGRRL P0CT57 RS14B_SCHPO SPBC18H10.13; CHAIN 1..139; /note="Small ribosomal subunit protein uS11B"; /id="PRO_0000433423" MATNVGPQIRSGELVFGVAHIFASFNDTFVHITDLTGKETIVRVTGGMKVKTDRDESSPYAAMLAAQDAAAKCKEVGITALHIKIRATGGTATKTPGPGAQAALRALARAGMRIGRIEDVTPIPTDSTRRKGGRRGRRL P0CT58 RS22A_SCHPO SPAC22A12.04c; CHAIN 1..130; /note="Small ribosomal subunit protein uS8A"; /id="PRO_0000126622" MVRQSVLADCLNNIVNAERRGRRQVLIRPSSKVIVKFLTVMQKHGYIDEFTEIDDHRSGKIVIQLNGRINKCGVISPRFNVKLKDIEKWVNQLLPSRQVGVIVLTTSRGIMSHNEARAKDAGGKILGFFY P0CT60 RL23A_SCHPO SPAC3G9.03; STRAND 19..22; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 24..27; /evidence="ECO:0007829|PDB:8ETC"; STRAND 29..32; /evidence="ECO:0007829|PDB:8EUY"; STRAND 34..40; /evidence="ECO:0007829|PDB:8EUY"; STRAND 61..66; /evidence="ECO:0007829|PDB:8EUY"; STRAND 78..82; /evidence="ECO:0007829|PDB:8EUY"; STRAND 84..88; /evidence="ECO:0007829|PDB:8EUP"; STRAND 90..92; /evidence="ECO:0007829|PDB:8EUY"; STRAND 94..96; /evidence="ECO:0007829|PDB:8EUY"; STRAND 101..104; /evidence="ECO:0007829|PDB:8EUY"; STRAND 107..109; /evidence="ECO:0007829|PDB:8ETC"; STRAND 112..114; /evidence="ECO:0007829|PDB:8EUY"; STRAND 118..121; /evidence="ECO:0007829|PDB:8ETC"; STRAND 136..139; /evidence="ECO:0007829|PDB:8EV3" HELIX 69..71; /evidence="ECO:0007829|PDB:8ETC"; HELIX 122..127; /evidence="ECO:0007829|PDB:8EUY"; HELIX 129..134; /evidence="ECO:0007829|PDB:8EUY" TURN 4..7; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..139; /note="Large ribosomal subunit protein uL14A"; /id="PRO_0000128629" MSRGRGAASGTKYRMTLGLPVQAIMNCADNSGAKNLYIVSVFGTGARLNRLPAASCGDMVLATVKKGKPDLRKKIMPAIVVRQRKAWRRKDGVYLYFEDNAGVIVNPKGEMKGSAITGPVAKECADLWPRIASNAGTVV P0CT62 RS30A_SCHPO SPAC19B12.04; CHAIN 1..61; /note="Small ribosomal subunit protein eS30A"; /id="PRO_0000174008" MGKVHGSLARAGKVKSQTPKVEKQEKPKQPKGRAYKRLLYVRRFVNVTNMVGGKRRMNPSS P0CT63 RS30B_SCHPO SPBC19G7.03c; CHAIN 1..61; /note="Small ribosomal subunit protein eS30B"; /id="PRO_0000433420" MGKVHGSLARAGKVKSQTPKVEKQEKPKQPKGRAYKRLLYVRRFVNVTNMVGGKRRMNPSS P0CT65 RS16B_SCHPO SPAC664.04c; CHAIN 1..140; /note="Small ribosomal subunit protein uS9B"; /id="PRO_0000433419" MQSVQCFGKKGNATAVAHCKVGKGLIKVNGAPLSLVQPEILRMKVYEPILVAGADKFAGVDIRVRVSGGGHVSQIYAIRQAISKAIVAYYQKFVDEHSKAELKKALITYDRTLLVADPRRMEPKKFGGHGARARQQKSYR P0CT66 RS18A_SCHPO SPBC16D10.11c; CHAIN 1..152; /note="Small ribosomal subunit protein uS13A"; /id="PRO_0000132226" MSLVVPDNFQHILRLLNTNVDGKVKVMFAMTQIKGVGRRYANIVCKKADIDMSKRAGELTTEELERIVTIIQNPSQFKIPSWFLNRQKDINDGKSFQLLANNVDSKLREDLERLKKIQTHRGLRHALDLRVRGQHTKTTGRRGKTVGVSKKK P0CT67 RS18B_SCHPO SPCC1259.01c; CHAIN 1..152; /note="Small ribosomal subunit protein uS13B"; /id="PRO_0000433418" MSLVVPDNFQHILRLLNTNVDGKVKVMFAMTQIKGVGRRYANIVCKKADIDMSKRAGELTTEELERIVTIIQNPSQFKIPSWFLNRQKDINDGKSFQLLANNVDSKLREDLERLKKIQTHRGLRHALDLRVRGQHTKTTGRRGKTVGVSKKK P0CT68 RL20A_SCHPO SPAC3A12.10; STRAND 4..12; /evidence="ECO:0007829|PDB:8EUY"; STRAND 24..32; /evidence="ECO:0007829|PDB:8EUY"; STRAND 55..62; /evidence="ECO:0007829|PDB:8EUY"; STRAND 72..80; /evidence="ECO:0007829|PDB:8EUY"; STRAND 83..85; /evidence="ECO:0007829|PDB:8ETC"; STRAND 87..97; /evidence="ECO:0007829|PDB:8EUY"; STRAND 121..127; /evidence="ECO:0007829|PDB:8EUY"; STRAND 162..164; /evidence="ECO:0007829|PDB:8ETG"; STRAND 167..170; /evidence="ECO:0007829|PDB:8EUY" HELIX 33..47; /evidence="ECO:0007829|PDB:8EUY"; HELIX 98..112; /evidence="ECO:0007829|PDB:8EUY"; HELIX 137..142; /evidence="ECO:0007829|PDB:8EUY" TURN 52..54; /evidence="ECO:0007829|PDB:8EUP"; TURN 117..119; /evidence="ECO:0007829|PDB:8EUY"; TURN 131..133; /evidence="ECO:0007829|PDB:8EUP"; TURN 154..158; /evidence="ECO:0007829|PDB:8ETG" CHAIN 2..176; /note="Large ribosomal subunit protein eL20A"; /id="PRO_0000213938" MALKEYQVVGRKVPTEHEPVPKLFRMRLFAPNESVAKSRYWYFLKMINKVKKATGEIVAINEISEPKPLKAKVFGIWIRYDSRSGTHNMYKEFRDTTRVGAVEAMYADMAARHRARFRSIRILKVVEVEKKEDVRRNYVKQLLNPHLKFPLPHRRTGVVGLAGKKVFAPHRPSTFY P0CT69 RL20B_SCHPO SPAC26A3.04; CHAIN 2..176; /note="Large ribosomal subunit protein eL20B"; /id="PRO_0000433417" MALKEYQVVGRKVPTEHEPVPKLFRMRLFAPNESVAKSRYWYFLKMINKVKKATGEIVAINEISEPKPLKAKVFGIWIRYDSRSGTHNMYKEFRDTTRVGAVEAMYADMAARHRARFRSIRILKVVEVEKKEDVRRNYVKQLLNPHLKFPLPHRRTGVVGLAGKKVFAPHRPSTFY P0CT70 RL2A_SCHPO SPAC1F7.13c; CHAIN 1..253; /note="Large ribosomal subunit protein uL2A"; /id="PRO_0000129760" MGRVIRAQRKSGGIFQAHTRLRKGAAQLRTLDFAERHGYIRGVVQKIIHDPGRGAPLAKVAFRNPYHYRTDVETFVATEGMYTGQFVYCGKNAALTVGNVLPVGEMPEGTIISNVEEKAGDRGALGRSSGNYVIIVGHDVDTGKTRVKLPSGAKKVVPSSARGVVGIVAGGGRIDKPLLKAGRAFHKYRVKRNCWPRTRGVAMNPVDHPHGGGNHQHVGHSTTVPRQSAPGQKVGLIAARRTGLLRGAAAVEN P0CT71 RL2B_SCHPO SPBC2F12.07c; CHAIN 1..253; /note="Large ribosomal subunit protein uL2B"; /id="PRO_0000433415" MGRVIRAQRKSGGIFQAHTRLRKGAAQLRTLDFAERHGYIRGVVQKIIHDPGRGAPLAKVAFRNPYHYRTDVETFVATEGMYTGQFVYCGKNAALTVGNVLPVGEMPEGTIISNVEEKAGDRGALGRSSGNYVIIVGHDVDTGKTRVKLPSGAKKVVPSSARGVVGIVAGGGRIDKPLLKAGRAFHKYRVKRNCWPRTRGVAMNPVDHPHGGGNHQHVGHSTTVPRQSAPGQKVGLIAARRTGLLRGAAAVEN P0CT72 RL2C_SCHPO SPBC839.04; CHAIN 1..253; /note="Large ribosomal subunit protein uL2C"; /id="PRO_0000433416" MGRVIRAQRKSGGIFQAHTRLRKGAAQLRTLDFAERHGYIRGVVQKIIHDPGRGAPLAKVAFRNPYHYRTDVETFVATEGMYTGQFVYCGKNAALTVGNVLPVGEMPEGTIISNVEEKAGDRGALGRSSGNYVIIVGHDVDTGKTRVKLPSGAKKVVPSSARGVVGIVAGGGRIDKPLLKAGRAFHKYRVKRNCWPRTRGVAMNPVDHPHGGGNHQHVGHSTTVPRQSAPGQKVGLIAARRTGLLRGAAAVEN P0CT73 RS11A_SCHPO SPAC31G5.03; CHAIN 1..152; /note="Small ribosomal subunit protein uS17A"; /id="PRO_0000128522" MATELVVQSERAFQKQPHIFQNAKKGAGRRWYKDVGLGFKTPAEAIYGEYVDKKCPFVGQVSIRGRILTGTVVSTKMHRTIIIRREYLHFIPKYNRYEKRHKNLAAHVSPAFRINEGDVVTVGQCRPLSKTVRFNVLRVVKHTEGPKQFGKF P0CT77 RL11A_SCHPO SPAC26A3.07c; CHAIN 1..174; /note="Large ribosomal subunit protein uL5A"; /id="PRO_0000125103" MAEKAQNPMKELRISKLVLNISLGESGDRLTRAAKVLEQLSGQTPVFSKARYTIRRFGIRRNEKIACHVTVRGPKAEEILERGLKVKEYELKKRNFSATGNFGFGIQEHIDLGIKYDPSIGIYGMDFYVVMDRPGMRVARRKAQRGRVGYTHKINAEDTINWFKQKYDAVVLGK P0CT78 RL11B_SCHPO SPBC17G9.10; CHAIN 1..174; /note="Large ribosomal subunit protein uL5B"; /id="PRO_0000433412" MAEKAQNPMKELRISKLVLNISLGESGDRLTRAAKVLEQLSGQTPVFSKARYTIRRFGIRRNEKIACHVTVRGPKAEEILERGLKVKEYELKKRNFSATGNFGFGIQEHIDLGIKYDPSIGIYGMDFYVVMDRPGMRVARRKAQRGRVGYTHKINAEDTINWFKQKYDAVVLGK P0CT79 RS28A_SCHPO SPAC25G10.06; CHAIN 1..68; /note="Small ribosomal subunit protein eS28A"; /id="PRO_0000136841" MDSSKVPVKLAKVIKVLGRTGSRGGVTQVRVEFMDDTSRSIIRNVKGPVREDDILVLLESEREARRLR P0CT80 RS28B_SCHPO SPCC285.15c; CHAIN 1..68; /note="Small ribosomal subunit protein eS28B"; /id="PRO_0000433411" MDSSKVPVKLAKVIKVLGRTGSRGGVTQVRVEFMDDTSRSIIRNVKGPVREDDILVLLESEREARRLR P0CT81 RS32A_SCHPO SPAC3G6.13c; CHAIN 1..25; /note="Small ribosomal subunit protein eS32A"; /id="PRO_0000198073" MRDKWRKKRVRRLKRKRRKMRARSK P0CT82 RS32B_SCHPO SPAC3F10.18c; CHAIN 1..25; /note="Small ribosomal subunit protein eS32B"; /id="PRO_0000433410" MRDKWRKKRVRRLKRKRRKMRARSK P0CT83 RL12A_SCHPO MOD_RES 67; /note="N5-methylarginine"; /evidence="ECO:0000250" SPCC16C4.13c; CHAIN 1..165; /note="Large ribosomal subunit protein uL11A"; /id="PRO_0000104466" MPPKFDPNEVKTIFMRAVGGEVAGGSTLAPKIGPLGLSPKKVGEDIAKATKDWKGLRVTVKLTIQNRQAAVSVVPSASALVIKALKEPARDRKKDKNVAHSGNVSLDEIIEVARTMRFKSLAKELSGTVKEILGTAFSVGCTVDGKNPHDVQKEIDNGEIEIPQE P0CT84 RL12B_SCHPO MOD_RES 67; /note="N5-methylarginine"; /evidence="ECO:0000250" SPCC31H12.04c; CHAIN 1..165; /note="Large ribosomal subunit protein uL11B"; /id="PRO_0000433408" MPPKFDPNEVKTIFMRAVGGEVAGGSTLAPKIGPLGLSPKKVGEDIAKATKDWKGLRVTVKLTIQNRQAAVSVVPSASALVIKALKEPARDRKKDKNVAHSGNVSLDEIIEVARTMRFKSLAKELSGTVKEILGTAFSVGCTVDGKNPHDVQKEIDNGEIEIPQE P0CU02 PLB4_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SIGNAL 1..19; /evidence="ECO:0000255" SPAC977.09c; CHAIN 20..673; /note="Putative lysophospholipase SPAC977.09c"; /id="PRO_0000024642" CARBOHYD 72; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 125; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 191; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 194; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 272; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 301; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 374; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 404; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 481; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 516; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 545; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 574; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MYVNYIGLFAFVQISLTLAYPPGRVEISEIYDFEESSSYKGQDIDTSVLYTLSKRKPALVKRSTDASYAPFNVTCSNDNLLRPASEGLNEGEQSYINKRISKVNSELRSFISKTGLNVDLDKVVNSSDGPRLGIAFSGGGLRAMVNGGGAFNAFDSRFESDSPLSGLLQSAMYISGLSGGSWLVGSVAINNFTNITYLRDNVWNLEHSVFAPHGDNVIENLNYYNDLRKEIDQKKHAGFDCSLTDLWGRALSRKLVDAERGGPGITYSSMRNQSWFQNADYPYPIIVADSRLEEETAIPANTSIFEFTAYEFGTWDNGIKAFIPMEYVGTHLLDGVPPDKSCIHNYDNAGFVMGTSATLFNSFLLDWNENVKKNDTYYDILHAILEDLSKHQDDIAPYPNPYQNYTTSNTSVVNAFEPYDTIDLVDGGEDRENIPLWPLLHPQRFVDVVFAIDSTYNDPYGWPLGSSIVATYERVVTFNANKSVDVRGFPYIPDENTIISLGLNTRPTFFGCDGKNTTAGNHDVDNNTPPLLVYFPNYPWTYYSNISTFTMSMDDKMANGILENAFMSTTQNNNESFAVCLACAIIQRSLERKKLSTPTQCSSCFQEYCWDGTLATSTASVYDPTVMSAATTSRAPSGTTSGTASSTTSSSVASATPTHKHWWDSIFEAKENP P0CU03 PLB7_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SIGNAL 1..19; /evidence="ECO:0000255" SPBC1348.10c; CHAIN 20..673; /note="Putative lysophospholipase SPBC1348.10c"; /id="PRO_0000437228" CARBOHYD 72; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 125; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 191; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 194; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 272; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 301; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 374; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 404; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 481; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 516; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 545; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 574; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MYVNYIGLFAFVQISLTLAYPPGRVEISEIYDFEESSSYKGQDIDTSVLYTLSKRKPALVKRSTDASYAPFNVTCSNDNLLRPASEGLNEGEQSYINKRISKVNSELRSFISKTGLNVDLDKVVNSSDGPRLGIAFSGGGLRAMVNGGGAFNAFDSRFESDSPLSGLLQSAMYISGLSGGSWLVGSVAINNFTNITYLRDNVWNLEHSVFAPHGDNVIENLNYYNDLRKEIDQKKHAGFDCSLTDLWGRALSRKLVDAERGGPGITYSSMRNQSWFQNADYPYPIIVADSRLEEETAIPANTSIFEFTAYEFGTWDNGIKAFIPMEYVGTHLLDGVPPDKSCIHNYDNAGFVMGTSATLFNSFLLDWNENVKKNDTYYDILHAILEDLSKHQDDIAPYPNPYQNYTTSNTSVVNAFEPYDTIDLVDGGEDRENIPLWPLLHPQRFVDVVFAIDSTYNDPYGWPLGSSIVATYERVVTFNANKSVDVRGFPYIPDENTIISLGLNTRPTFFGCDGKNTTAGNHDVDNNTPPLLVYFPNYPWTYYSNISTFTMSMDDKMANGILENAFMSTTQNNNESFAVCLACAIIQRSLERKKLSTPTQCSSCFQEYCWDGTLATSTASVYDPTVMSAATTSRAPSGTTSGTASSTTSSSVASATPTHKHWWDSIFEAKENP P0CU05 PFL6_SCHPO SIGNAL 1..27; /evidence="ECO:0000255" SPAC977.07c; CHAIN 28..416; /note="Putative cell agglutination protein pfl6"; /id="PRO_0000437229" CARBOHYD 19; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 344; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MNFFLYFRTIFLIQLYFFNYSTFGCSASSTSVQSDTTNQVSVSCPKYTTIYTSGTSPDTKTIYPESTSTKSITTSTQSHSSPVIVVSTVGTVTETTISGSTEYTTTIPAEGITSGTVEIVEPTAGTVTETITSGTLPFTTTLAQASGTVSGTVEIVSPKNNPTTVYSGTVATTETFSSSTVVVIPTAICDGVRGLEYAVYDYTISSSMNEFCYPKNGQTDVFAFNEPAYFGSSDLDQSSPLFTGVFSSTDDIPEWASSWYLPPYPPQASDMASTYCACKVIVYQFFLRIPETDTYTLVVNNVDDVFFGWFGDKAISGWSNNNFDAYSYWHESPNMGLGTVGMGNFTVGNYPEGYFLPVRFVVANGAYIGGFDFYFTSDSTGPLATTSYSYTKTCTQQFLPFGQGNGGVNGPTEKLS P0CU09 YIP12_SCHPO MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 118; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB17E12.02; CHAIN 1..235; /note="Survival of motor neuron protein-interacting protein yip12"; /id="PRO_0000437231" MPSKRKRNPLQYQTSGSLDEETNQRSAFPQIDNNSASESLEYDIPLDGLDYLATVREEARKLVPFVAARREPETRETIPLRKLEIEAGKKSFDPFLRYLLNIIDKEGERLEQYMESSSLDASILPKNLQQWRVYIEHKAPCWAILAVVDLATVLEILESLSSWLEKDAIDLQSQWIFCFCYKLPELLNGEDISTLRSVLKSLRSTHTSFPALQMSASALQAVLVYRYGQKDLFQT P0CU19 FEX1_SCHPO CATALYTIC ACTIVITY: Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, ChEBI:CHEBI:17051; Evidence={ECO:0000250|UniProtKB:Q08913}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160; Evidence={ECO:0000250|UniProtKB:Q08913}; SPAC977.11; CHAIN 1..311; /note="Fluoride export protein 1"; /id="PRO_0000317096" CARBOHYD 181; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MLLTQSYFCIMSMLGTLARLGLTALNTYPGAPFSGLLWVQFVGCVIMGFCQTESVFFPRPKHNATFLLAITTGFCGSLTTFSSWMLQMFTGMANLDPFERRGRGYSFLSVVSDFMVTMCIAMSSLIWGKQIGKTTGQWRIGKVAFAWPIPAHTHIVVRVLLLLLSICFFVGAAFYTAYTTNVTHRGIGFSLIFSPFAALTRLYLARFLNSPQYFIPYGTLCANVFATLLLSIMYMIPQITHCTPVSRSVMYGIQNGFCAVLSTLSTFSNELHTMPIKRAYIYCIISVAISFSICVIVDGATAWGHGYTEKY P0CU20 FEX2_SCHPO CATALYTIC ACTIVITY: Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, ChEBI:CHEBI:17051; Evidence={ECO:0000250|UniProtKB:Q08913}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160; Evidence={ECO:0000250|UniProtKB:Q08913}; SPBPB8B6.06c; CHAIN 1..311; /note="Fluoride export protein 2"; /id="PRO_0000437237" CARBOHYD 181; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MLLTQSYFCIMSMLGTLARLGLTALNTYPGAPFSGLLWVQFVGCVIMGFCQTESVFFPRPKHNATFLLAITTGFCGSLTTFSSWMLQMFTGMANLDPFERRGRGYSFLSVVSDFMVTMCIAMSSLIWGKQIGKTTGQWRIGKVAFAWPIPAHTHIVVRVLLLLLSICFFVGAAFYTAYTTNVTHRGIGFSLIFSPFAALTRLYLARFLNSPQYFIPYGTLCANVFATLLLSIMYMIPQITHCTPVSRSVMYGIQNGFCAVLSTLSTFSNELHTMPIKRAYIYCIISVAISFSICVIVDGATAWGHGYTEKY P14575 COX3_SCHPO CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00420}; SPMIT.04; CHAIN 1..269; /note="Cytochrome c oxidase subunit 3"; /id="PRO_0000183851" MNLSTKFQGHPYHIVSASPWPFFLSVVLFFNCLAATLYLHGYKHSSVFFGISFLGLLATMYLWFRDMSTEANIHGAHTKAVTKGLKIGFMLFLISETFLFASIFWAFFHSSLSPTFELGAVWPPVGIADKTIDPLEVPLLNTVILLTSGASLTYAHYSLIARNRENALKGLYMTIALSFLFLGGQAYEYWNAPFTISDSVYGASFYFATGLHGIHIIVGTILLLAATYNIYTYHLTNTHHNGFECGIYYWHFCDVVWLFLYLTIYIWGS P14965 PYRF_SCHPO ACT_SITE 95; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10110" BINDING 40; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 62..64; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 93..102; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 214; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 233; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU10110}; SPCC330.05c; CHAIN 1..264; /note="Orotidine 5'-phosphate decarboxylase"; /id="PRO_0000134683" MDARVFQSYSARAEGMKNPIAKELLALMEEKQSNLSVAVDLTKKSEILELVDKIGPYVCVIKTHIDVVEDFDQDMVEKLVALGKKHRFLIFEDRKFADIGNTVKLQYASGVYKIASWAHITNCHTVPGEGIIQGLKEVGLPLGRGLLLLAEMSSKGSLATGSYTEKTLEWFEKHTDFCFGFIAGRRFPNLQSDYITMSPGIGLDVKGDGLGQQYRTPEEVIVNCGSDIIIVGRGVYGAGRNPVVEAKRYREAGWKAYQQRLSQH P15258 RAL2_SCHPO MOD_RES 604; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC21.05c; CHAIN 1..611; /note="Protein ral2"; /id="PRO_0000119142" MSEVKRNISLRNSTNIFTSTFSLSSNNVPKPLIGESVIKYGDEAFVYGGRDALNAQLVNDMYVVDLNTCSWKQVEYQGNQKPIPRYFHSGDLWNNKLIFFGGMGFNDDTKCLYVLNDIDIYDIETKQWSHIPGMITENQTNDDAKEVNGSDVDEKSKHLYPSARYGHLHCVLDHYLIIFCGQDLSNSYIEEINIFDLDSGKWVFKSLFNHHCGIYRSNCVVINKDSEFLQMCRPINTTQDSNEHSIGSLFFYLNYNFVNVKRQVIYLELFELDTAESEKKSAALAKDNNQSFRFLELDVTEKFLSSAMPPGLRFPAVNILGDNLILSGIYLTSSRQAFVLWVYSLDKELWLQLDMLGVLNHGSWFKCLVLDCTNRFVVFGNKTRKLTQDYNLRQSNYDHIVFIELEGYGVYRKPQMGRVTERSEQLGKLLLNGISDMEILTIERMHIPCLSRMLYKRWPAFQKIMDRAVEKNQEAFQAEVSQLGPQLTDLPFSSIHSTGSRALYMPYSFETCSAFLHYIYCGTLNGSYCTAKNLCNLLILCKGFEGLETFFAYIVHLLHGVLNRNNVKLIYETAALTGAKGLQLRALRRIARIEQGGTAISPTSPLPNLDD P15567 PUR6_SCHPO BINDING 134..189; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" CATALYTIC ACTIVITY: Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+) = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2; Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21; SPCC1322.13; CHAIN 1..552; /note="Phosphoribosylaminoimidazole carboxylase"; /id="PRO_0000075027" MSEKQVVGILGGGQLGRMMVEAAHRLNIKCIILDAANSPAKQIDGGREHIDASFTDPDAIVELSKKCTLLTTEIEHINTDALAAVTKSVAVEPSPATLRCIQDKYLQKQHLQVFKIALPEFCDAPDQESVEKAGQEFGYPFVLKSKTLAYDGRGNYVVHQPSEIPTAIKALGDRPLYVEKFVPFSMEIAVMVVRSLDGKVYAYPTTETIQKDNVCHLVYAPARLPFSIQQRAQTLAMDAVRTFEGAGIYGVEMFVLQDGETILLNEIAPRPHNSGHYTIEACPTSQFEAHLRAICGLPFSEINTQLSTSTTHALMVNILGTDDPDYVSKIAKRSLSIPGATLHLYGKAESRKGRKMGHVTIISDSPQECERRYQMLLDVKDPVESPVVGIIMGSDSDLSKMKDAAVILDEFKVPYELTIVSAHRTPDRMVTYARTAASRGLRVIIAGAGGAAHLPGMVAAMTPLPVIGVPVKGSTLDGVDSLHSIVQMPRGVPVATVAINNSQNAGILACRILATFQPSLLAAMESFMDNMKEIVLEKADKLEKVGWKNYSA P17476 RLA1_SCHPO SPAC644.15; CHAIN 1..109; /note="Large ribosomal subunit protein P1A"; /id="PRO_0000157707" MSASELATSYSALILADEGIEITSDKLLSLTKAANVDVEPIWATIFAKALEGKDLKELLLNIGSGAGAAPVAGGAAAPAAADGEAPAEEKEEAKEEEESDEDMGFGLFD P17477 RLA3_SCHPO SPBC3B9.13c; CHAIN 1..110; /note="Large ribosomal subunit protein P1B"; /id="PRO_0000157708" MSASELATSYSALILADEGIEITSDKLLSLTKAANVDVEPIWATIFAKALEGKDLKELLLNIGSAAAAPAAGGAGAPAAAAGGEAAAEEQKEEAKEEEESDEDMGFGLFD P17478 RLA4_SCHPO MOD_RES 100; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23G7.15c; CHAIN 1..110; /note="Large ribosomal subunit protein P2B"; /id="PRO_0000157684" MKYLAAYLLLTVGGKQSPSASDIESVLSTVGIEAEAERVESLISELNGKNIEELIAAGNEKLSTVPSAGAVATPAAGGAAGAEATSAAEEAKEEEAAEESDEDMGFGLFD P17937 RL7A_SCHPO SPAC664.06; STRAND 16..19; /evidence="ECO:0007829|PDB:8ETG"; STRAND 88..94; /evidence="ECO:0007829|PDB:8EV3"; STRAND 119..124; /evidence="ECO:0007829|PDB:8EV3"; STRAND 140..143; /evidence="ECO:0007829|PDB:8EV3"; STRAND 159..162; /evidence="ECO:0007829|PDB:8EV3"; STRAND 165..168; /evidence="ECO:0007829|PDB:8EV3"; STRAND 234..238; /evidence="ECO:0007829|PDB:8EV3" HELIX 26..46; /evidence="ECO:0007829|PDB:8ETG"; HELIX 54..72; /evidence="ECO:0007829|PDB:8EUY"; HELIX 103..111; /evidence="ECO:0007829|PDB:8EV3"; HELIX 127..135; /evidence="ECO:0007829|PDB:8EV3"; HELIX 147..157; /evidence="ECO:0007829|PDB:8EV3"; HELIX 172..178; /evidence="ECO:0007829|PDB:8EV3"; HELIX 187..196; /evidence="ECO:0007829|PDB:8EV3"; HELIX 201..207; /evidence="ECO:0007829|PDB:8EV3"; HELIX 240..248; /evidence="ECO:0007829|PDB:8EV3" TURN 136..139; /evidence="ECO:0007829|PDB:8EV3"; TURN 179..183; /evidence="ECO:0007829|PDB:8EV3"; TURN 220..224; /evidence="ECO:0007829|PDB:8ETG" CHAIN 1..249; /note="Large ribosomal subunit protein uL30A"; /id="PRO_0000104647" MAEDAPVVQQTMLEPEVLLKKRKVNERTRKERVEQAIAKKEAQKKNRKETFKRAETFINNYRQRERERIRLNRSAKNKGDIFVPDETKLLFVIRIAGVKNMPPKIRKVLRLLRLSRINNAVFVRNNKAVAQMLRIVEPYVMYGIPNLHSVRELIYKRGFGKINGQRIALSDNALIEEALGKYDVISIEDIIHEIYNVGSHFKEVTKFLWPFTLTPVKHSLMEKKVKHFNEGRKAGYCGEEINELIKKQV P19117 IPYR_SCHPO BINDING 80; /ligand="diphosphate"; /ligand_id="ChEBI:CHEBI:33019"; /evidence="ECO:0000250"; BINDING 117; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 122; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 122; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 154; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC23C11.05; CHAIN 2..289; /note="Inorganic pyrophosphatase"; /id="PRO_0000137586" MSEYTTREVGALNTLDYQVYVEKNGTPISSWHDIPLYANAEKTILNMVVEIPRWTQAKLEITKEATLNPIKQDTKKGKLRFVRNCFPHHGYIWNYGAFPQTYEDPNVVHPETKAKGDSDPLDVCEIGEARGYTGQVKQVKVLGVMALLDEGETDWKVIVIDVNDPLAPKLNDIEDVERHMPGLIRATNEWFRIYKIPDGKPENSFAFSGECKNRKYAEEVVRECNEAWERLITGKTDAKSDFSLVNVSVTGSVANDPSVSSTIPPAQELAPAPVDPSVHKWFYISGSPL P21535 ATP6_SCHPO SPMIT.07; PROPEP 1..4; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000002620" CHAIN 5..257; /note="ATP synthase subunit a"; /id="PRO_0000002621" MFITSPLEQFELNNYFGFYLFNYHFDFSNFGFYLGLSALIAISLAIINLTPYGSGAKIVPQKFGIAMEAIYFTMLNLVENQIHSSKTVSGQSYFPFIWSLFVLILFSNLLRLIPYGYATTAQLIFTLGLSISILIGATILGLQQHKAKVFGLFLPSGTPTPLIPLLVLIEFVSYIARGLSLGIRLGANIIAGHLTMSILGGLIFTFMGLNLITFIIGFLPITVLVAISLLEFGIAFIQAYVFAILTCGFINDSLNLH P21537 ATP9_SCHPO SPMIT.10; CHAIN 1..74; /note="ATP synthase subunit 9, mitochondrial"; /id="PRO_0000112235" MIQAAKYIGAGLATIGVSGAGVGIGLIFSNLISGTSRNPSVRPHLFSMAILGFALTEATGLFCLMLAFLIIYAA P24487 ATPA_SCHPO BINDING 197..204; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" TRANSIT 1..27; /note="Mitochondrion" SPAC14C4.14; CHAIN 28..536; /note="ATP synthase subunit alpha, mitochondrial"; /id="PRO_0000002432" MLRQAGTRLLKVPVCGLRPSITLKRGYAEKAAPTEVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDTILNHKRWNNSSDESKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIRKEGVLSKTTEDSLKAVIKEFLSSF P25457 RL7B_SCHPO SPAC3H5.07; STRAND 82..84; /evidence="ECO:0007829|PDB:8EUY"; STRAND 90..95; /evidence="ECO:0007829|PDB:8EUY"; STRAND 99..101; /evidence="ECO:0007829|PDB:8EUY"; STRAND 120..125; /evidence="ECO:0007829|PDB:8EUY"; STRAND 141..144; /evidence="ECO:0007829|PDB:8EUY"; STRAND 160..163; /evidence="ECO:0007829|PDB:8EUY"; STRAND 166..169; /evidence="ECO:0007829|PDB:8EUY"; STRAND 223..228; /evidence="ECO:0007829|PDB:8EUY"; STRAND 233..237; /evidence="ECO:0007829|PDB:8EUY" HELIX 17..79; /evidence="ECO:0007829|PDB:8EUY"; HELIX 104..112; /evidence="ECO:0007829|PDB:8EUY"; HELIX 128..136; /evidence="ECO:0007829|PDB:8EUY"; HELIX 138..140; /evidence="ECO:0007829|PDB:8EUY"; HELIX 148..157; /evidence="ECO:0007829|PDB:8EUY"; HELIX 173..180; /evidence="ECO:0007829|PDB:8EUY"; HELIX 188..197; /evidence="ECO:0007829|PDB:8EUY"; HELIX 202..208; /evidence="ECO:0007829|PDB:8EUY"; HELIX 241..249; /evidence="ECO:0007829|PDB:8EUY" TURN 181..184; /evidence="ECO:0007829|PDB:8EUY"; TURN 229..232; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..250; /note="Large ribosomal subunit protein uL30B"; /id="PRO_0000104648" MVASSTVPSVASIFAPESLLKKTKAQKQSREQIVAAAAEKKSARQKKRELIAKRAEAYEAEYRAAEREQIELARKARAEGNYFVPHEPKLIFVVRIRGINNIPPKARKIMQLLRLLQINNGIFVKFNKAIKEMLQVVEPYVTYGIPNHKTVRELIYKRGFGKVNKQRIPLSDNAIIEAALGKYSILSVEDLIHEIYTVGPNFKQAANFLWPFKLSSPLGGWRERKFKHFIEGGDAGKRDEHINGLVQKML P26674 STE6_SCHPO SPCC1442.01; CHAIN 1..911; /note="Protein ste6"; /id="PRO_0000068899" MRFQTTAISDYENSSNPSFLKFSAGDTIIVIEVLEDGWCDGICSEKRGWFPTSCIDSSKIQNFFSSFHSSNEKDPNAQCCAPFHVEAHLQDSAWFEKHGVQAINSIPSSEEFLRKNLQNDIHHLVKGILTTAAAVSQSIKKEGTQVIVFGIETVRSMVLSFPLIILSTLDENFLSEVAQVFSSLNLLPELSRMGCTYGELCIRFTKLLKQLANKFLFFFRPDVSFPSYFLGSLIAHEIHFLPWDFNMLCSNSVQSAHTNLQPDITSFVAILSLSHEAYHCTENEFWNLEAQKLTENTTQKVLQLVAEDALEAWKLDILEDIDRCIQCCRRFLSANQRINYSSSENNPFSFTSQDVEALKDELSSNLCDLYLWSIDLEQISPSDCLLDNYSLFVDLLVTLKVSLLRIKSIIVQFSERIVFLSLEYKFLTNIQPELNDAEKSQLDGFDLNKTNWFDSKGLVCYLMKQTSPEPLLIRNLLFSFWSCNGKIEQDGKIKTATLVFIINYLLRTDIDSTFFTTIFLNTYASMISSSDLFSILGAHFRFICSLNFGKISFISHEFYRVSKRFLDILLIWFESYLVEELDNSKSIFFLFKIYKVFEVFVVPHFASAEELLHSLSHLLHHPSTKRSHKMLEGKELSQELEDLSLHNSPDPIIYKDELVLLLPPREIAKQLCILEFQSFSHISRIQFLTKIWDNLNRFSPKEKTSTFYLSNHLVNFVTETIVQEEEPRRRTNVLAYFIQVCDYLRELNNFASLFSIISALNSSPIHRLRKTWANLNSKTLASFELLNNLTEARKNFSNYRDCLENCVLPCVPFLGVYFTDLTFLKTGNKDNFQNMINFDKRTKVTRILNEIKKFQSVGYMFNPINEVQELLNEVISRERNTNNIYQRSLTVEPRESEDQALQRLLIDSGIF P28189 RS13_SCHPO MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 32; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC6F6.07c; CHAIN 2..151; /note="Small ribosomal subunit protein uS15"; /id="PRO_0000115688" MGRMHSKGKGIASSALPYVRSPPAWCKADADSVVEQILKFSKKGMSPSQIGVTLRDSHGIPQVRFITGQKIMRILKANGLAPELPEDLYNLIKKAVSVRKHLERNRKDKDSKFRLILIESRIHRLARYYRKVGALPPTWKYESATASALVA P30597 CHS1_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; SPAC13G6.12c; CHAIN 1..859; /note="Chitin synthase 1"; /id="PRO_0000193716" MRRWFKKTLPRPPDEEESAGLTNKDIVETNHLYPTITNLSLNSDTSSILFDKNKKPLKPKIIIPDKEFDLDYYLKDETESIQSPFEGFTAQPNFSNFNKQGNTMNREANFQRTNEKIQRNKSIKRVKLFHGNLILDCPIPKKLLVTLPQQTEREFAYMRYSAATCDPQDFSKSLFTLRQPLFFQPRKTEICIAITMYNEDEVLFARTMHSVMKNISHLCTRKNSQVWGKDAWKKVVVCIISDGRTKIHPRTLAYLAAIGVYQDGIAKNQVNDKEVKAHIYEYTTQLSIDPNLKFKGSDRGIVPVQMIFCLKEKNQKKLNSHLWFFQAFCPILKPEVCILLDAGTRPGDQSIYHLWKSFDLNPQVAGACGEIVVMKGKLGSGLINPLVATQNFEYKMSNILDKPVESVFGFISVLPGAFSAYRFEALQNDSQGNGPLASYFKGELQNTGKSGIFEANMYLAEDRILCFELVSKKNEAWILHYVKSAYADTDVPDRIPEFVLQRRRWLNGSFFAAAYAICHYYRFFRTSHTISRKFMLSIEFIYQLATIVFGWFNIGNFFIIFYILTSSLASTSANFLPGEILFRIAIWIYASLLVTCFVLALGNRPHGSPNFYLSMVIMYSILMGYLLFCSGWIAYRAISDAIHNASSTSSSYTSALLNSNVFINIVISLSSTYGMYLVVSIISFDPWHMFTSFVQYIFLSIMYTNVLNVYAFCNTHDVSWGTKGDHFTNNDLGVARLLQKGADVEIAIPTNQSDIDAKYEDAVKLLASPSLEFNSPIINHGEQEDFYKNFRTYVVLTWILSNLFLVGIVLSIPKINGISISNNETSAYLSFLLWSVVAFSVFRFIGCIFYLFIRLCTGE P31397 MAP3_SCHPO SPAC3F10.10c; CHAIN 1..365; /note="Pheromone M-factor receptor"; /id="PRO_0000195075" MLPIGIFYQFYAYFALVLSIPILYMQLRARNIPCLLLLFWLTLTTLIYVVESAIWSNPYAETIRWMGYGLCDITSRIVTCSSIGIPASAFTLVLYLDTVIRRDHPLKRYENWIWHVCLSILLPLIIMAMMVPLESNRYVVICMNGCYSSFYQTWYTLLFFYIPPCLLSFGGLFFVSRIVVLYWRRQRELQQFFQRDSQLTSKRFLRLLCLAAVFFLGYFPLTIFMVVANGKLQQFLPFNHELVEAWHQESITYYPTTKVGLNDWVPPTVLYLMSLFFSTSGGWTEKVALILWSLLVWLPFTKNTALGRHAQFKLDCCKSIESTMAGKTLDSTDFKEKCLVLERQWSKSSIPSDNSSELQDAAKYV P32834 SXA1_SCHPO ACT_SITE 94; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"; ACT_SITE 325; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" SIGNAL 1..23; /evidence="ECO:0000255" SPAC26A3.01; CHAIN 24..533; /note="Aspartic proteinase sxa1"; /id="PRO_0000025932" CARBOHYD 79; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 106; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 138; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 153; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 166; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 271; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 278; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 299; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 319; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 439; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKASFFVFAISALQALQASVASAYSEVPGKRSVVLNLQHSQYDHVARKLERTKVLNKRDSSGYPVLDLEYTDAGGYFANLTLGSNERVYSLTLDTGSPYTWVTAKNITALSASEIWSDTDGVDAGRSTSDIRTNACTNYTCFDYSSTTARRTNSSTIGFLASYGDNTTVLGYNMVDNAYFAGLTLPGFEFGLATREYDSSQISVTPGIIGLSVAMTITGISSDDKVVAFTPPTIVDQLVSANVIDTPAFGIYLNEDVGELIFGGYDKAKINGSVHWVNISSSDDSTFYSVNLESITVTNSTSSNNVQSSKRSSKDIEVNTTVTLDTGTVYIYLPEDTVESIADQYQGIVSEYGYVVIYCDSFSDSDYISFNFGSDADFHVSVNDLVIYRQESTSGDICYLALFEGDTSSYLLGQYFLQYVYSIYDWDAQKIGLAALNSNATSTANHQILNINSALRSVTSGQSVSATPTVSMSIAATSFGSSLVLTASASPSSTSVDGSSSSDSSEASGAASVGVSISAIVLCASTLISLLFA P35679 RL4A_SCHPO MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP8B7.03c; CHAIN 1..363; /note="Large ribosomal subunit protein uL4A"; /id="PRO_0000129365" MAAARPTVSIYSKDGSVSSETIALPFVFKAPIRPDLVRSVHTAVAKNKRQPYAVSEKAGHQTSAESWGTGRALARIPRVGGGGTHRSGQAAFGNMCRSGRMFAPTKTWRKWHVKVNQNEKRYAISSAVAASGVPSLLLARGHRIEEIPEVPLVVDDAVQSFQKTKEAVALLKEIKAYRDVVKVANSRKLRAGKGKLRNRRHVQRRGPLVVFNEDAGIVKAFRNIPGVEIVNVRRLNLLQLAPGGHLGRFVIWTKSAFGLLDSVFGSTTEAAQLKKNYFLPENIISNADVTRLINSDEIQSIVKAAGPSRVKRAHVQKKNPLKNKAVLARLNPYAKAYKANVKLNTGKTPKAAGEKFLTVLHEN P36579 ARF1_SCHPO BINDING 24..31; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 67..71; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 126..129; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P84077}; SPBC4F6.18c; CHAIN 2..180; /note="ADP-ribosylation factor 1"; /id="PRO_0000207416" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000250" MGLSISKLFQSLFGKREMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYRNISFTVWDVGGQDKIRPLWRHYFQNTQGIIFVVDSNDRERISEAHEELQRMLNEDELRDALLLVFANKQDLPNAMNAAEITDKLGLHSLRHRQWYIQATCATSGDGLYEGLEWLSTNLKNQ P36584 RL3B_SCHPO SPAPB8E5.06c; CHAIN 2..388; /note="Large ribosomal subunit protein uL3B"; /id="PRO_0000077250" MSHCKFEQPRHGSLGFLPRKRASRQRGKVKAFPKDDASKPVHLTAFLGYKAGMTHIVRDLDRPGSKMHKREILEAVTIIETPPMVVVGVVGYVETPRGLRSLTTVWAEHLSEEVKRRFYKNWFKSKKKAFTKYAKKYAESTQSINRELERIKKYCSVVRVLAHTQIRKTPLAQKKAHLMEIQVNGGSVADKVEWAREHFEKTVDIKSTFEQNEMIDVIGVTRGKGNEGTTARWGTKRLPRKTHRGLRKVACIGAWHPANVQWTVARAGNAGYMHRTQLNSKIYRIGAGDDAKNASTDFDATEKRITPMGGFVRYGVVENDFVMLNGATPGPVKRVLTLRKSLLTHTSRKALEPVSLKWIDTASKFGHGRFQTPAEAKQFLGTLKKDVA P36585 RL28A_SCHPO SPCC5E4.07; STRAND 4..6; /evidence="ECO:0007829|PDB:8ETG"; STRAND 72..74; /evidence="ECO:0007829|PDB:8ETC"; STRAND 96..98; /evidence="ECO:0007829|PDB:8ETC"; STRAND 100..102; /evidence="ECO:0007829|PDB:8ETC"; STRAND 109..112; /evidence="ECO:0007829|PDB:8ETC"; STRAND 123..129; /evidence="ECO:0007829|PDB:8ETC"; STRAND 143..146; /evidence="ECO:0007829|PDB:8ETC" HELIX 8..11; /evidence="ECO:0007829|PDB:8ETC"; HELIX 75..77; /evidence="ECO:0007829|PDB:8ETC"; HELIX 78..81; /evidence="ECO:0007829|PDB:8ETC"; HELIX 84..90; /evidence="ECO:0007829|PDB:8ETC"; HELIX 103..106; /evidence="ECO:0007829|PDB:8ETC"; HELIX 133..140; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..148; /note="Large ribosomal subunit protein uL15A"; /id="PRO_0000104902" MPTHVSKTRKLRGHVSAGHGRIGKHRKHPGGRGKAGGLQHLRSHFDKYHPGYFGKVGMRRFHLMKNPLWRPTVNLDRLWTLLPNEARDKYLGKNTEVAPVINVLQSGYGKVLGKGRLPETPVIVQTRYVSRRAEEKIKQAGGVVELIA P36589 CDC14_SCHPO SPBC24C6.07; CHAIN 1..240; /note="Cell division control protein 14"; /id="PRO_0000089442" MEDLLNNAKQHLCMRNPKLIRIGLRQVESIVYHVAKPSHDDKIPREIFLKLQDSPLYNSTTPCIYALDSLLEYQQNEEAYEKNFQFIQKLIDDLLHVIEGLVLIHPKSQTLFEDKATLRLFIHLLQPSQPSMLQVAAMKTLVCIMADRPLAIRLFEQINGLQQICVVFKHKQTSQDTRFQILEFFYFYLSPEPYSIDVIAYRKTRTEKQAYLSKYLSNVQGLRDDLDKFQPFGKLDETFD P36599 PDE1_SCHPO CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; SPCC285.09c; CHAIN 1..346; /note="3',5'-cyclic-nucleotide phosphodiesterase"; /id="PRO_0000206790" MHAALEIKEAEFQTDQVVGLVENSFTLYSLGQNGGPLESCCSSHLISDGAFQEIISLDGGSHLSALVELIQSKHLSVDSWSSITKYDNYTVENESYAKAWHLSEQRIKTFLITHCHLDHIYGAVINSAMFGPQNPRTIVGLNYVIDTLKKHVFNNLLWPSLDKAGFINFQVVEPSMYTSLTTTLSILPFPVNHGSSFGQELKSSAFLFRNNLSDRYFLAFGDVEPDMVASEPLNIHIWRACSSLIAQRKLSHILIECSTPDIPDTLLFGHFCPRHLVNELCILQSLVQSYGVIMPTLTCLLTHLKSHPLQSANPADVILEQLESLSSKSSLSVTFKILQRGQFYKF P36605 HIS8_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766, ChEBI:CHEBI:57980; EC=2.6.1.9; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; MOD_RES 223; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000305" SPBC11B10.02c; CHAIN 1..384; /note="Histidinol-phosphate aminotransferase"; /id="PRO_0000153508" MFDLNTCLRKNILELQPYRCARDDFSEGVLLDANECAYGSVISVDGVEFNRYPDPRQIEVKQRLCDLRNKELSITKPLTPDNICMGVGSDEIIDSLIRISCIPGKDKILMCPPSYGMYTVSAKINDVEVVKVLLEPDFNLNVDAICETLSKDSAIKVFFACSPGNPTAKALKLEDIKKILEHPTWNGIVVVDEAYIDFSAPDMSALTLVNEYPNLAVCQTLSKSFGLAGIRIGFCLTSKPIATIMNSLKAPYNISEPTSRLALDALSPQSIDKMHTYRDAIIQQRVRLCKELTTIKGMGKIIGGYDANFILIQVLDRPEGGKPSNDAAKYLYLQMATMHKVVVRFRGTEPLCEGALRITVGTEEENTILLKTIKLVLQEYYTKK P36611 HAP3_SCHPO SPAC23C11.08; CHAIN 1..116; /note="Transcriptional activator hap3"; /id="PRO_0000204632" MSADGLDYTNLLPIANVARIMKSALPENAKISKEAKDCVQDCVSEFISFVTGEASEQCTQEKRKTITGEDVLLALNTLGFENYAEVLKISLTKYREQQARSASMKETKQSRSEEPQ P36622 STE4_SCHPO SPAC1565.04c; CHAIN 1..264; /note="Sexual differentiation protein ste4"; /id="PRO_0000072264" MGDSDDFYWNWNNEAVCNWIEQLGFPHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSMKKQQKDKLQQENKDQELKNIEESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKLVKTLNSLNSEFLQLLRKIAINVKEGRQLTTENSSDTSSMTHPVQPSPSVLGSFDLEVNDSLTNAEKNRKLNVNLTYNEVLCSMLQRYRIDPNTWMSYDLLINYDDKEHAIPMDVKPLQLFRNLQKRGKSPSFVLSRRSC P36624 DHSO_SCHPO BINDING 42; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 48; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P07846"; BINDING 67; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 153; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P07846"; BINDING 201; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 206; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 277..279; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 301..303; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q00796"; BINDING 303; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P07846"; BINDING 304; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P07846" CATALYTIC ACTIVITY: Reaction=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+); Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924, ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P35497}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q00796}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q00796}; SPBC1773.05c; CHAIN 1..360; /note="Sorbitol dehydrogenase"; /id="PRO_0000160823" MAPAEKAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAAKENESLPDYAQRYKQAIIEKYGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVIIGGPDA P36627 BYR3_SCHPO PTM: Phosphorylated. SPAC13D6.02c; CHAIN 1..179; /note="Cellular nucleic acid-binding protein homolog"; /id="PRO_0000065031" MESESVPTVPQTTRPGPRCYNCGENGHQARECTKGSICYNCNQTGHKASECTEPQQEKTCYACGTAGHLVRDCPSSPNPRQGAECYKCGRVGHIARDCRTNGQQSGGRFGGHRSNMNCYACGSYGHQARDCTMGVKCYSCGKIGHRSFECQQASDGQLCYKCNQPGHIAVNCTSPVIEA P40369 ARLY_SCHPO ACT_SITE 161; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P24058"; ACT_SITE 282; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P24058" BINDING 28; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 115; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 160; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain C"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 290; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain B"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 322; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 327; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 330; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058" CATALYTIC ACTIVITY: Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine; Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682, ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000305|PubMed:1868575}; SPBC1773.14; CHAIN 1..461; /note="Argininosuccinate lyase"; /id="PRO_0000137725" MAEKSSKKLWGGRFSGATDPLMAEFNKSIYSGKEMCEEDVIGSMAYAKALCQKNVISEEELNSILKGLEQIQREWNSGQFVLEPSDEDVHTANERRLTEIIGDVAGKLHTGRSRNDQVTTDLRLWLCRKIKEVEVYVINLLKVFTNRAEMEIDVIMSGYTHLQRAQPVRWSHFLMSHALPLLGDLGRLRQLYTRVSQLPLGAGALAGNPFNVDREFLRKELGFEGIIMNSMNAVGDRDFVIEFMFWAGMVMLHISRFAEDLIIYSSSEFGFVTLSDAYSTGSSIMPQKKNPDSLELLRGKSGRVLGDMIGLMITVKGTPTTYNKDLQEDKEPLFDAFKTVSDSLQILTGVVSTLTINPTKIAESLTPDLLATDLAEYLVRKGLPFRQTHHISGSAVRMAEERNTTLDKLSVSDLQSLHPLFDEDVSKVFNYEESVEKRCSIGGTAKHCVQEQIEHIRSAIL P40374 HIS7_SCHPO CATALYTIC ACTIVITY: Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040, ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19; MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC21H7.07c; CHAIN 1..216; /note="Imidazoleglycerol-phosphate dehydratase"; /id="PRO_0000158247" MRRAFVERNTNETKISVAIALDKAPLPEESNFIDELITSKHANQKGEQVIQVDTGIGFLDHMYHALAKHAGWSLRLYSRGDLIIDDHHTAEDTAIALGIAFKQAMGNFAGVKRFGHAYCPLDEALSRSVVDLSGRPYAVIDLGLKREKVGELSCEMIPHLLYSFSVAAGITLHVTCLYGSNDHHRAESAFKSLAVAMRAATSLTGSSEVPSTKGVL P40379 REC16_SCHPO SPBC2D10.06; CHAIN 1..472; /note="Transcriptional activator protein rec16"; /id="PRO_0000046816" MDSDRCLTDEISLNTLSSTFASDNNLRRKENFLKSRYPSKFDLNVSMLTKSDDVGKTPFSIFDSPSNPGFSRSHQMCSDKNKSPFLFDKIRDEPVSVDPVKLIINNRNKRKINRQKSRLQGLYRSDANGLQPLNSENVKMKKSTALSLTSSPLNSWKTDFKTPPKANVVCISLVIEGDGCASLLYEDLNQISNSCPEVAPNRQNALFSDETLTTMFYSGVTEDEGSCNNLLQSSFGDDLDLGMQRSATWAPGYNYPSKFDSIPFASASPKIKAAFPFDPNVYALNTNDGPVTSTDNNCDQLNTRMQAWNNGFNYSNLNGDIQYPAVTPKFFQQEGRALNVSDCNFGNEEIAYGGIPMRVCHSDSTLCDARIAAKQALKGKRQYDTSTSKAELSTPPSKRRHIDDADLVFHSSPLLSRSRFICCYCTKPFLSISKLQEHESSCSHVERLFGFAPNRLYDDGDGFLGSSFCSDW P40385 TO6BL_SCHPO SPBC21B10.12; CHAIN 1..260; /note="Meiotic recombination protein rec6"; /id="PRO_0000097225" MHRVRSARDGIVLKYHFKEDWDETQNSPIDCIASSRLKFWKRLNFNIYLDPEVSNQNLKLLKTLTLHCDFQSPKKNLTMSKFKAMAVELIHEAFLKHIVSILSKECPLSFQPSYYSKMFNAMSNANIIAGSISRILTRESLDKSFEQSHFQLLMYKKCKLIYTRTLRKNEFDGIHKFPDLEDSKQKLQVADDEENKQYSESSLLDDSQLLCSSPPVDSTEEARTCNVEEDQDEILSVALVTTDTILSSDNFVNDMLSAAD P40388 UVI15_SCHPO PTM: Palmitoylated. {ECO:0000250|UniProtKB:P38216}. SPBC649.04; CHAIN 1..87; /note="Lipid-anchored plasma membrane protein uvi15"; /id="PRO_0000065748" MSAQQFYGDKGYAPAPPQQAYGGPNYYPPQQNYPQQGYAPPQGYPQGGYPAQQPMYVQQPQASDPGGDLCCGLLTGLACCCCLDAMF P40389 RRG1_SCHPO BINDING 117; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 143..145; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 165; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 198; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 221; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867" SPCC338.11c; CHAIN 1..303; /note="Protein-lysine N-methyltransferase rrg1"; /id="PRO_0000097443" MILEDTDLPLSHEQPSYSQIKDVLDKIPTGEHLWDLPKYEEKIILNWLIKLLATNLEWITVEEERDYLVSTICERIAERSGRLAAPTRKREFSLSNGVSVVLREPTMTYNTLGFKTWGSAPLLSANLPKWEDLSNSINALELGAGTGLVGISAAIQLGWQVVCTDLPDIVENMQYNVDYNSELIQQYAGSVSCHVLDWMNPPDDDNRPSWLIKPFQRIIASDCIYETHFGELAIALFRKYLAKDGIVITEYPLRETHLEEIGVFEKGMDAAGFERQMGEEIGEEDFGSLYPVTCRWSRWKYHG P40900 ISP4_SCHPO SPBC29B5.02c; CHAIN 1..785; /note="Sexual differentiation process protein isp4"; /id="PRO_0000213787" MIGSINESPIEEHMNDSPSTKEKADSVDISDYIVSHSDDSLSKDIKKDTKSFLDVEHGEISTVDEFEEDSPYPEVRAAVPPTDDPSMPCNTIRMWTIGLIYSTVGAAVNMFFSLRNPTVTLSVLISELLAYPALQIWDLIFPDREFRIGRLKFNFKPGPFNVKEHALIVVMSSVSFGNAYSTDIILAQRVHYKQRFGFGYEICLTLATQLIGYGLAGLSRRLLVRPASMLWPVNLVQCTLIKTLHRKDLRNAVANGWRISPFRFFLYVFIASFIWNWFPSYIFQALSLFAWVTWIRPNSPTVNQIFGESTGISILPMTFDWNQISAYILSPLMAPADALMNILLGVILFFWIVTPALNFTNTWYGDYLPISSSGIIDHFGNSYNVTRILTKDATFDLDAYQNYSPIFMSTTYALAFGLSFASITSVIFHVILYHGKEIYDRLRDPPAPDIHEKLMKAYDEVPFYWYLSVFLAFFGMMMGTIYGWKTETPWWVIIVGVIFSAVWFIPIGIVQAITNIQLGLNVFTEFIVGYMYPGRPLAMMIFKTVGYITMTQGLAFAADLKFGHYMKLPPRIMFYTQMIATIWSCFVQIGVLDWALGNIDNVCQADQPDNYTCPNATVFFNSSVIWGVIGPKRMFSGKNTYTGLQYFWLAGVLGTILFWALWKKWPQKWWGQLNGPLIFGGTGYIPPATPVNYLAWSGIGLFFNYYLKKIFADWWQKYNFTLSAALDTGTQLSVIILFFCLQLPMVNFPDWWGNDGAFNTLDATGAAVRKLVNESAGEFFGPAEW P40921 EF1G_SCHPO SPAC29A4.02c; CHAIN 1..409; /note="Elongation factor 1-gamma"; /id="PRO_0000208830" MSVGTVYGKIGSPRVLFCVSVAAVAGVEVEHVDVQPHNFPADLAAKFPLQKMPVFVGKDGFPLSETLAIAFYLASLNKTRALNGTTAEEKAKVLQYCSFTNSELPGAFRPIIAPRVFGAPYDEQAAKEAETAIALIFARFDEELASKTYLVGSRLTLADIFFTCFLKFGATYVLTKSYLAKYTHIYRYYQTIYHQAKLDAITEPLKFIDQPLPIIKAENKEAAPAKKAEKKKDEKKKNAPKPQAERPAKPPKHPLASAPNGSFDIEEYKRVYSNQDTRSGALPWFFEHFDPENYSVWKVDYSYPEDLKQPVFMTNNLIGGFFQRLEASRKYIFGCCVVIGENGDNTITGAFVIKGHDYVPAFDVAPDWGSYTFTKLDINKPEDKAFIEDAWAWDKPIEGREVADGKVCK P41000 CPS3_SCHPO SPAC3A11.02; CHAIN 1..583; /note="Protein cps3"; /id="PRO_0000213911" MTKKNAFKNSEDMKKYHLSEFNSEATSLTRPSPKSLQHVPCKFFRQGTCTSGKNCIFSHDLELATEKTICKYFQKGNCKFGSKCALEHVLPDGRKVKTRAFAPSTTAMGSSSQNISAAPMANIISNNDKILPMTTMASATASEEKNRIKDEALVIKKEESNVAIPSEVTVAANAFSASTEDVYSIVGDSLSKKASVKDFSDVTGIETIPAYVEATNGSSTVRSPHAKRSLSSISVKSSTSPFSGSKFLSSSSYPHTPEAHLNSNHISPASFGSGIRTRNIFNPESMSLGLKPPILNRSYSASMAPGFSMNTFTATGNLGRPTKSPSVPTSVGSNKSRKFPGINGSTLTATPSSLENLYPLSSRRSVPNLISSLGTSPSTFSSQFLKSTDRTHSFTSKLQSFNPVGTSLLASSLGTSQEDSVNYDIPDEFANEEDFIPNSLQELLTPEELERKMSHGDEAVSSSSASRFMSKVSSNLNSGNPTPYNSYNGTPTSSRFVAFFDRHRQESEKATPPSLNKVSQEPLTATTPKNLGNLTAISETLENGQTLKSNMASSIEKSKTSTEVVASYDTTLDEETQFQMDEA P41836 PRS8_SCHPO BINDING 186..193; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC23G7.12c; CHAIN 1..403; /note="26S proteasome regulatory subunit 8 homolog"; /id="PRO_0000084731" MTEVLKTNVLQSNENIVQYYTQKIQDAELAILQKTQNLRRLEAQRNGLNARVRLLREEIQLLQEPGSYVGEVIKTMGKNKVLVKVHPEGKYVVDISPDIDIKEIKPNIRVALRNDSYQLIKILPNKVDPLVSLMMVEKIPDSTYEMVGGLEKQIKEIKEVIELPVKHPELFESLGIPQPKGILLYGPPGTGKTLLARAVAHHTDCKFIRVSGSELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSSRSDSSGGSGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPPPSAEARAEILRIHSRSMNLTRGIDLKSIAEKMNGASGAELKGVCTEAGMFALRERRVHVTQEDFELAVAKVLNKGDSGEMSLQKLFK P50514 ARLZ_SCHPO ACT_SITE 160; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P24058"; ACT_SITE 281; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P24058" BINDING 26; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 114; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 159; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain C"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 289; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain B"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 321; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 326; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058"; BINDING 329; /ligand="2-(N(omega)-L-arginino)succinate"; /ligand_id="ChEBI:CHEBI:57472"; /ligand_note="ligand shared between tetrameric partners"; /note="in chain A"; /evidence="ECO:0000250|UniProtKB:P24058" CATALYTIC ACTIVITY: Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine; Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682, ChEBI:CHEBI:57472; EC=4.3.2.1; SPBC1539.03c; CHAIN 1..460; /note="Probable argininosuccinate lyase"; /id="PRO_0000137726" MASSQKLWGGRFTGATDPLMTAYNESIHYDKRMFNADIDGSKAYAKALEQRGIISADELDKMLDGLEAVRDEWKTNKFTLQPSDEDIHTANERRLGEIIGTGIAGKLHTGRSRNDQVTTDMRLWLRDELDIIQKSLVGLLQVFVARAESDLDIIMPGYTHLQRAQPIRWSHFLLSHAFSILNDLDRLKQIYSRVNRLPLGAGALAGNPFAVDRKFLQKELGFEGVIMNSMNAVADRDYVIEFMFWASMVMTHISRLAEDLIIYSTSEFNFVTLSDAYSTGSSIMPQKKNPDSLELLRGKSGRVFGNMMGFMVSVKGIPSTYNKDLQEDKEPLFDSSKTVLDSIQILTGVLSTLTVNPENIAKSLTADMLATDLAEYLVRKGVPFRETHHISGSAVRMAEERNTTIDKLSVEDFKSLHPLYEEDVADVFNYESSVEKRCAIGGTAKSCVLEQIQTIKKALE P50515 VATL1_SCHPO SPAC1B3.14; CHAIN 1..161; /note="V-type proton ATPase subunit c"; /id="PRO_0000071761" MSTDLCPVYAPFFGVMGCTAAIVFASFGAAYGTAKAGVGISAMGVLRPDLIVKNTIPVVMAGIIAIYGLVVSVLISGNLKQILSLYSGFIQLGAGLSVGLAGLAAGFAIGIVGDAGVRGTAQQPRLFVAMILILIFAEVLGLYGLIVALLLNTRATDNVTC P50519 HSP9_SCHPO SPAP8A3.04c; CHAIN 1..68; /note="Heat shock protein hsp9"; /id="PRO_0000084082" MSDPARKSFTEQGKEKMTPDSSKSTLDKAKESITGAYDKVASAFTSDEDKSTSQEAHDKAQRFVDDKL P50523 QCR8_SCHPO SPAC1782.07; CHAIN 1..92; /note="Cytochrome b-c1 complex subunit 8"; /id="PRO_0000193550" MGGAAGGKTYLGWWGHLGGPKQKGIITYSLSPFQQRPMAGFFKTSTQNMFRRVMTEGLYVAIPFGIAYYIYCWGKERNEFLNSKHGRHLVEE P50524 RPN12_SCHPO SPBC16G5.01; STRAND 184..187; /evidence="ECO:0007829|PDB:4B0Z"; STRAND 213..215; /evidence="ECO:0007829|PDB:4B0Z"; STRAND 218..220; /evidence="ECO:0007829|PDB:4B0Z" HELIX 7..14; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 18..34; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 44..63; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 67..81; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 91..104; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 108..117; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 123..126; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 128..141; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 145..153; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 158..160; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 161..182; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 188..194; /evidence="ECO:0007829|PDB:4B0Z"; HELIX 200..210; /evidence="ECO:0007829|PDB:4B0Z" CHAIN 1..270; /note="26S proteasome regulatory subunit rpn12"; /id="PRO_0000173850" MSTLDLNHLADLYDRKDWNACKKELLKLKVELAKQNLFVPTSDKEKASFARNVFEYGVLVSIQTCDIESFARYASQVIPFYHDSLVPSSRMGLVTGLNLLYLLSENRIAEFHTALESVPDKSLFERDPYVEWVISLEQNVMEGAFDKVASMIRSCNFPEFSYFMKIVMSMVRNEIATCAEKVYSEIPLSNATSLLYLENTKETEKLAEERGWDIRDGVIYFPKEANALETEDGMLIDEEDELELPPTASKHTISSIRQLLSYTSELEQIV P50999 TCPD_SCHPO SPBC106.06; CHAIN 1..527; /note="T-complex protein 1 subunit delta"; /id="PRO_0000128343" MSKAATVPVAFQDREKPQEVRLSNIMAARSVADAIRTSLGPKGMDKMIQTGKGEVILTNDGATILKHLSVLHPAAKMLVDLSAAQDVEAGDGTTSVVILAGSMLACAEKLLKKGIHPTVIAESFQRAAGFTVDCMKENALAIELSDRESLLRAATTSLNSKIVSQYSNLLAPIAVDAVLKVIDPRVATNVDLKDIRIVKKLGGIIDDTELIPGLALTQTAVKSAGGPTRIEKANIALIQFQLSPPKPDMENQVVVNDYRQMDKILKEERQYLLNMCKKIKKAGANVILIQKSILRDAVNDLALHFLAKLKIMVIKDIERDEVEFICKSTGCKPIADIESFAEDKLGHADLVEETSSSGEKIVKFSGVKNAGKTVSILCRGANLLTLEEAERSLHDALCVIRCLVKQRALIAGGGSPEIEAAQRLLEHARQLEGREAICIRAFSEALEIIPVTLAENAGLNAIQVVTELRSRHANGEKTAGINVRKGIVTNILEENVLQPLLVNISAIQLAAETTKMIMKIDDITLAR P52808 RL30A_SCHPO SPAC9G1.03c; CHAIN 1..109; /note="Large ribosomal subunit protein eL30A"; /id="PRO_0000146140" MASVVTKKSKKSGDTINAKLALTMKSGKYVLGYKSTLKTLRSGKAKLILIAGNCPPLRKSELEYYAMLSKANVHHYAGTNIDLGTACGKLFRVGVLAITDAGDSDILDA P52822 RL5A_SCHPO MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 12; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H5.12c; CHAIN 1..294; /note="Large ribosomal subunit protein uL18A"; /id="PRO_0000131452" MPFIKAVKSSPYFSRYQTKYRRRREGKTDYYARKRLIAQAKNKYNAPKYRLVVRFSNRFVTCQIVSSRVNGDYVLAHAHSSELPRYGIKWGLANWTAAYATGLLVARRALAKVGLADKYEGVTEPEGEFELTEAIEDGPRPFKVFLDVGLKRTSTGSRVFGAMKGASDGGLFIPHSPNRFPGFDIETEELDDETLRKYIYGGHVAEYMEMLIDDDEERYQKQFSGLIADGIESDQLEDIYAEAYAKIREDPSFQKSGKDAAAFKAESLKHTQRKLTAEERKERFNAKVIEAGRA P54280 PMS1_SCHPO SPAC19G12.02c; CHAIN 1..794; /note="DNA mismatch repair protein pms1"; /id="PRO_0000178010" MSTVKPIDANTVHKICSGQVITDVASAVKELVENSLDSGATTIEIRFKNYGINSIEVVDNGSGIDAGDYESIGKKHFTSKITDFEDLEALQTFGFRGEALSSLCAVGQVIISTATQNEAPKGVQLNLDHEGSLKDKLTIPFQRGTSVMVNDLFCTLPVRRKLLEKNYKREFSKAISLLQAYATISTNKRFMVYHQTKNSGKLLQLSTNSNKDMKLNIMNVFGTKVSSSLIPWNDGIIEGYISRPHVGSTRASNERQMLFINRRLVNLPKIARVIQEVFKPYSMAQSPFFAINLRITNGTIDINVSPDKKSVFLSEEDSIIEFIKNSLQNLCESCGHAISCSRSQSIFSYSSQIPDSSGDSTDQELPQSIPATESETSDDSSFSYKRSPCKRKLVEATAQPAISTSVAEGASLAQVSKPLPERLQKDSMRRSSPLNEKVTASSERMKKKLALFASSTDTSMQKTIDSSFPLKQPINKPSSNPNNLLLNDPSPASTPVAKTINLNEIESVHNAESVSTLSSIPRTEQTSVANRIPSKTAALQKLKFFQSRPLDGLNKFSKKINISLSGVQKDIVRSDALLKFSNKIGVVHDISDENQEDHLNLTVHKADFLRMRVVGQFNRGFIVVVHGNNLFIIDQHASDEKFNYEHLKSNLVINSQDLVLPKRLDLAATEETVLIDHIDLIRRKGFGVAIDLNQRVGNRCTLLSVPTSKNVIFDTSDLLEIISVLSEHPQIDPFSSRLERMLASKACRSSVMIGRALTISEMNTIVRHLAELSKPWNCPHGRPTMRHLLRLKDI P55877 IF1A_SCHPO SPBC25H2.07; CHAIN 1..138; /note="Eukaryotic translation initiation factor 1A"; /id="PRO_0000145112" MPKNKGKGGKNRRRGKNENENEKRELTYAEEGQMYAQVTKMLGNGRIEAACFDGVKRLGHIRGKLRKKVWINQGDIILLSLREFQDEKGDVILKYTADEARTLKNQGELPETAKINETDTFGAEGEDDLDFEFDVDAI P56289 IF5A1_SCHPO PTM: Lys-52 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function. {ECO:0000250|UniProtKB:P23301}. MOD_RES 52; /note="Hypusine"; /evidence="ECO:0000250|UniProtKB:P23301"; MOD_RES 75; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 77; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 78; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26H5.10c; CHAIN 1..157; /note="Eukaryotic translation initiation factor 5A-1"; /id="PRO_0000142485" MAEEEHVDFEGGEAGASLTFPMQCSALRKNGHVVIKGRPCKIVDMSTSKTGKHGHAKVHIVALDIFNGRKYEDMSPSTHNMDVPVVKRDEYQLVNIDDGYLNLMTTDGTTKDDVRLPEGELGNEIEEGFDEGRDLIITVVSAMGEETALACRDAPSS P56329 IF2B_SCHPO MOD_RES 45; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 137; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 138; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 139; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC32A11.04c; CHAIN 1..321; /note="Probable eukaryotic translation initiation factor 2 subunit beta"; /id="PRO_0000137414" MTETEAVVDQIDLNGALPEKKKKPKKSVAFDDEVDAVSKDGPEASSAGATDEDDSERKSSAKDLTTPVTEGEVDELKDMFSSMKKKKKSKKSSASAEEQTEDITTESGELDFSSMKKKKKKKKSADLSAFEKELEASSTGDATSDLSKQTFDSENMGEHAWLKSDRDYYYPELLNRFFTLLRTNNPELAGEKRKYTIVPPSVHREGKKTIFANISDISKRMHRSLDHVIQFLFAELGTSGSVDGSSRLIIKGRFQQKQIENVLRRYIVEYVTCKTCKSPDTILTKENRIFFMTCEACGSVRSVQAIKTGYQAQIGKRKHVS P58234 RS19A_SCHPO SPBC21C3.13; CHAIN 1..144; /note="Small ribosomal subunit protein eS19A"; /id="PRO_0000153833" MAGVSVKDVDAQKFITAYAAFLKRSGKMTTPQWIDIVKTGTHKELAPYDPDWYYVRAAAIARHIYLRKQVGVGRLCKVYGGSVNRGMRPSHHRDGSGSVQRKVVQSLEKIGVLEKSDNGGRRISQQGQRDLDRIAYSLLEEESE P78761 QCR2_SCHPO TRANSIT 1..30; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC613.10; CHAIN 31..426; /note="Cytochrome b-c1 complex subunit 2, mitochondrial"; /id="PRO_0000026799" MKSFTRNLRRFQTPRRNLHGISYTPKKVEGVSFAGRETPTATGSLSVVINAGSRYQPDAGVSHLLEKFAFKTTEERSALRITRESELLGGQLSTQITREHIILTARFLNEYLEYYARLLAEVVDATKFLPFQLTEEVLPTARIESELFREDILRVAMAKLHEKAFHRGIGNEVYLPASASPSISEIKDFASKAYVKSNFSVISSGPDVQKASDLCAKYFAVIPDGSPLKSAPTKISSGESRVYSKGTNYFCLGFPAPAASPELFVLSSILGGDAAVKWSHGNTLLAKAAGTASEYKATAVADLTPYSDASLLSVVISGSCPKAIKATASESFKALKSLSSNIPNDVVKSGIAMAKTKYLSAFEPVTLNAISASSLVSASKGSDAFISGFDKVTPASISKVVSSLLAKPASTVAVGNLDVLPYYDEL P78773 ACSA_SCHPO BINDING 201..204; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250"; BINDING 320; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250"; BINDING 395..397; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 419..424; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 510; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 525; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 533; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250"; BINDING 536; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 594; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; MOD_RES 596; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC191.02c; CHAIN 1..662; /note="Probable acetyl-coenzyme A synthetase"; /id="PRO_0000208419" MTKNPVDHTLIIEPPVRLHGDPTVPKPNIASLDEYKRMYEESINDPSTFWGNMARDMMTWDKQFSTVVQGSIDKADSAWFADGAISPCYNLVDRHAIARPDAVALIYEADEPNQGRYITYRELLASVSQCAGALQSMGVGMGDRVAIYMPMIPETIIAMLAIVRLGAIHSVIFAGFSAESVADRVNDSECKVIITADESHRGGKRIPLKGVVNKALTECPTIKKVLVFQRSAEPTASMVEGRDVWWHDIIPKFPRYCPPAVVNPEHPLFLLYTSGSTGKPKGVVHCTGGYLLGAAATCKYVFDLHPTDRMGCAGDVGWITGHTYIVYGPLMLGAATLVFESTPAYPDYSRYWSVVERHRLTQWYIAPTAIRLLQRAGNEFVKHDRSSLRVLGSVGEPIAPESFMWYYEVVGEKRCAVADTYWQTETGSHIVTSLGPVTPMKPGSATLPFFGIDAVIIDPLTGKIIEGNDVEGVLAIRSPWPSAARTVWRGHDRYIDTYLKPYPGFYFTGDGATRDKDGYIWIRGRVDDVVNISGHRLSTAEIEAALLSHDAVAESAVVGVHDELTGQAVNAFILLKPGYEATVELEKELIMAVRSTIGPFASPRKLIFSDLPKTRSGKIMRRILRKILAGEVDQIGDLSTLADPKVVEHIIHAVHYAHQKKP P78790 ETFA_SCHPO BINDING 285..313; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per dimer. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC27D7.06; CHAIN ?..341; /note="Probable electron transfer flavoprotein subunit alpha, mitochondrial"; /id="PRO_0000008659" MLRTTSRTFSRALSSSNFKINCGRRHWFSVLTLLEHQGGNLSPASLSAVEAAKRTGGDVFGFVIGKDSSQISQKVAKSVNDLKKVIYVENPSYEHNIPDQIANVLFENVKKNEISHVFSAHSTVGKGVMPRLAAMFDVMQISDIIGVVSADTFVRPTYAGNVNVTVSTKDPIKIVTVRASAFDAAPSSGEGAATVVEGIDPKPAALQEWVSENIIKNARPDLSSAERVVAGGRPLKDKETFERILTPLADKLGAAIGATRVAVDSGYADNSLQIGQTGKIIAPKLYIAVGIDGAIQHLAGIKDSKVIAAINRDENAPIFQTADVGIVGDLFEIVPELTEKL P78798 PEX7_SCHPO SPAC17D4.01; CHAIN 1..308; /note="Peroxisomal targeting signal 2 receptor"; /id="PRO_0000051119" MLSLRTPGFQGESVQFSPLVENKIAVAAVTHYGLGGSGRLYIHDVTPKGIQVCQHYDVEDSLFGVRWSQNCENQVYACCGDGSLRLFDLTMPSKPIHKWKEHKAEIVAIDTNTVDRRIVVTGSWDGTIKLWLGNLPNSVQTLNNGSNSRILTVATHYSSPNLLGYTSSDGLCKFWDFRSSDKFMSIEIPNQITCMNWSKSNHRMVYTADNNNLVYCYDIANLKTPLSVLSGHQLAVRSIKSSNSAHDLLATASYDMTSRIFDPEQHSCIRKVDLHSEFVRDVDWSDFGDGSWIASVGWDESLYIWNAF P78804 DHE4_SCHPO ACT_SITE 113; /evidence="ECO:0000255|PROSITE-ProRule:PRU10011" CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4; MOD_RES 252; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC622.12c; CHAIN 1..451; /note="NADP-specific glutamate dehydrogenase"; /id="PRO_0000182794" MSTPYEPEFQQAYKEIVGSIESSKLFEVHPELKRVLPIISIPERVLEFRVTWEDDKGNCRVNTGYRVQFNSALGPYKGGLRFHPSVNLSILKFLGFEQIFKNALTGLPMGGGKGGSDFDPKGKSDNEIRRFSQAFMRQLFRYIGPQTDVPAGDIGVTGFVVMHMFGEYKRLRNEYSGVVTGKHMLTGGSNIRPEATGYGVVYYVKHMIEHRTKGAETLKGKRVAISGSGNVAQYAALKCIQEGAIVKSISDSKGVLIAKTAEGLVPEEIHEIMALKEKRASIADSASLCKKHHYIAGARPWTNVGEIDIALPCATQNEVSGEEAAALIKQGCRYVAEGSNMGSSAEAVEVFEKSRASGEGCWLAPGKAANAGGVAVSGLEMAQNAQFSTWTHAEVDAKLAGIMQNIFEQSTDVASKYCDSGSNNIPSLVDGANIAGFLKVATAMQAVGDWW P78814 SRP2_SCHPO PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}. MOD_RES 186; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 188; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 276; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 294; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 308; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16.02c; CHAIN 1..365; /note="Pre-mRNA-splicing factor srp2"; /id="PRO_0000081963" MSETRLFVGRIPPQATREDMMDFFKGYGQILDCKLMNGFGFVEVEDARDARDIVNDFQGKEFMGSRIVVEPARGERRRRENFRESAASKYPRPRRTGFRLIVENLSEDVSWQDLKDVMRKAGEPTFTDAHRENPGAGVVEFSTEEDMRNALTSLNGEVIKGQAVTLREDPDAANEPLPEVPSRFRSRSPPARRRYRDDYRRGGDYRRDAYRPGRDDERRYAPRGEYRRNNRDEYRRGGRDEYRRNSRSDYRRPHDDEYRRPRGDEYRPGRDEYRRSRDDGRPSHDDEYRRDAYSRSPSPRRDREENRSPAYEGSKSYSAAPEASMESSAPTESYDKPAASEEQQPLQNHSDVGNGSAEGQVAAEW P78825 ADK_SCHPO ACT_SITE 292; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPCC338.14; CHAIN 1..340; /note="Adenosine kinase"; /id="PRO_0000080061" MSSYILFGLENPLLDYYVGGETATLEKYGLKSNDAVLASESQMGIYKEPCVSYSAGGAAQNSCRAAQYVLPPNSTVFAGCVGQDKFADMLLESNEKAGLRSEFSVDPTTPTGVCAVVLSNNNKNRSLCTNLGAANNYKLKDLQQPNVWKFVEEAKVIYVGGFHLTVSPESMLCLAQHANENNKPYIMNLSAPFLSQFFKEQMDSVIPYCDYVIGNEAEILSYGENHGIKSTDVQEIALALSSVEKVNKKRTRVVVITQGADATIVAKDGKVTTYKPNRVPSEEIVDTNGAGDAFAGGFIAALSQGQGIDYAVTLGHWLGQECIKVSGTTLPLPKKQFPLP P78847 NU186_SCHPO SPCC290.03c; CHAIN 1..1647; /note="Nucleoporin nup186"; /id="PRO_0000290670" MDVWESQHFSALLYLLQCIESNPSNPNVSSRLLIQCLESYSKDFLKFLALDPANANSRKKLESGEVELGGVINKVNEQFIQLSLTLSTQLNLDEIQCASLLQRGIEASQNLDRTPVQAALYFFFLAREQLLECLESLTRVVGLKDLESDISTALKSYLQSLCENGNNLVKTCIDTIPILDNKVSEILKSEAGGQILGVSEVVDFQEFIRLSHEAHVAELETISVILYQLAKVDLFQNSHFESLLVMLRKYDSPNKNAVLILPTLYAFIDKVLEVEYLPDQKVQLRSNSVEILQKIHQAIIQSPSQDWRSSQFKNILGIWWVTRLNATCKQIEKVPSFIDYETTIKNAANEIIQNGVFSDMITLLVYPFRQSETEGMEWAFAFKSRSRITVNWSLIRPFIASIIFSELRSFAQAFVSYMPDILKTLRLLEEDRYLTNTTYPTSIPGEQIEEYFPFEEFYYLLSSIYTYNVSWISDFWDDIESDMYGFLTWSMGSQIPGIITAFTLLLASLCKNTTSASKIYELFSEPIPEVGHLESLMITSPSWSYIFNVFRYYISHLKPVQTVVTSSGLARVHTDPSEIDTDSALILQAYILLFSSVVRQDAQIASTFCENQDLNPIATLFELLECRLPDSVRICIVRALESLAHLSTGSFNNALWTALDNWFVSSVLFDVDGGLAPMSIPAISKRSLTKPVTSCGPLLNNIRRLTVNLEMKISFVNLLTSLTRNKSELNVNLTFPENLGASYRTPGVQPYVDYVVETFVASSTQWRLMRDVGSIRLQYACLQYMLAVLDGLNIDLLLYSRILSSKVRDNLQNNNLHVYLTRHPAISLLEALYTESVYSGLFDLVEYGFDQLEDVSVPKTIVITVSASLCILRNVLSLQRVLFKNVVPYIAELGISKYILDLTISRRAYKEVFMTRISSIVHLALLVGSRHKCFLRSAIEILSYLVDAEGFMNKRNPDENKLLCSIIRTANESKRIIFGFIRTFESQFLTLLSTNDESSLILKLLLNNLKQSGGVYSLALLILGFDISSTNVITLRDQPGYVGSRVSLMNSLLDFIEGRTIVNGIWETPVIMVQALEIVAFLCSCPLTSEVTLSVIRARPGLLVKMVDGEPILTQQVIQNLGGFSSEEVSMVSRCIRSRTQIMNMLATEIHYAASVGQNKYLNEYVASLIRTNEKTHSTELSQKESGFKILEFMDILRIDPQSITFELPNIPGFNLNMFITRFDRGHSDFQFDTERVLKIYRLFFEAEMTSLGGSAEEKYSWLEQQNSKLKELAQRLNTFNAHVVLLQDIHGCLTAWARLTGLLVDDCNEVISDVHFDDFIWEVLRLVLPGVTVHNLGTQGTVSVTSSVIETILPHALRRIGALKPEELGKSTYFMEGIHDVIVGLLKGIQCQQSDESIRENLYGSLLSILTVFQKHTSANGGDKVDPVFKDAFQKLITPNLLTSQFFDVLTKDALYTNGSCWELSVIILNFLHHVSPDISTHLYKYYLRRNFVSSFIDAFSRAFSELLSSNKDVLEVLSGLEAGQCLLITFAQNKLTVHSVLTFDYIKLMVQMLLQLCKQGGIQYLKPPVQRLMIQLLQIFILVLMRVTLKEISNKDKLLLQSIFLLSRKLQDSVQTGADQALSPEMNTVKKYVETISRLLDLYRD P78860 MRM2_SCHPO ACT_SITE 173; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P0C0R7" BINDING 59..62; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9UI43"; BINDING 80; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9UI43"; BINDING 96..97; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9UI43"; BINDING 133; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9UI43" CATALYTIC ACTIVITY: Reaction=a uridine in 21S rRNA + S-adenosyl-L-methionine = a 2'-O-methyluridine in 21S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:47760, Rhea:RHEA-COMP:11901, Rhea:RHEA-COMP:11902, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; Evidence={ECO:0000250|UniProtKB:P53123}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC2G2.15c; CHAIN ?..218; /note="rRNA methyltransferase 2, mitochondrial"; /id="PRO_0000155590" MFGSKTLFSWAAKRSKDFYRKKSKIDNFRSRAAYKLIELNSKYRFINKEDVVIDVGFAPGSWSQVAKKLVGNKGKVIGIDIQHIAPPEGVLPIYGDIRDPNTLTKLFEALRLLHEPNTNDSIDCRVVDAVISDMLHKATGIRIRDHALSMELCASALHVALTFLKSNGSFICKFYMGDEDADLQNLLKSHFRFVQVMKPKASLKESREAYFVCLERKP P78898 TGCE2_SCHPO ACT_SITE 210; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 378; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P80035"; ACT_SITE 404; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P80035" SPBC16A3.12c; CHAIN 1..443; /note="Probable lipase C16A3.12c"; /id="PRO_0000312660" CARBOHYD 134; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 177; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 304; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 335; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSGFNKNQIYWGDYVGVIAAFVGVYTELVARIFIYMIPERVREWFRVRIIVLYHYYISSKTTDGMTDAVQKCRNIYEICEAFGYRVEEHLVRTQDNFILCLHRITHPKQSQHKREVVYCHHGLMTNSELWVAVNESERSLPFVLIESGYDVWLGNNRGNKYSRKHITYKPKDEEFWNFSLDDMAMFDIPDTVDYILRETGREKLNYIGFSQGTAQAMAALSINPDLNDKVNIFIGLAPAYAPKGFSNYFVDYIVKVNPKIMYHLFGRRCLLPSVTFWQNICYPPIFVKIVDVSLKILFNWDLSNISLNQKLCGYAHLYSFSSVKSVVHWLQIIKNCTFQLYDDDMALLAGYGSRHYQVPLFPTNNIKCPMLILWGGKDTLINMEVMRTALPPHAKEVSIAHYEHLDFLWGQDVKEEVFPVVIDALKHHSLGKAKHFVKQNGFH P78921 TCPQ_SCHPO SPBC337.05c; CHAIN 1..546; /note="Probable T-complex protein 1 subunit theta"; /id="PRO_0000128377" MALRVPKASGPQLFREGYRIMQGVEDAVIRNCNAIRELSEITRTSLGPNGKNKIVVNHLQQTFLTNDAATIIRELEVIHPAAKLVVDATQQQENELGDAANFVVVFTGELLAKAENMIRMGLTPLEIAKGYEMALSHTMEVLEEICADKIETVESEKELIKAIRTCISSKQYGNEDFLSDLVAKAILTVLPKDPSKFNVDNIRVVKIMGSSLYNSQVVKGMVFPREPEGTVTRSKEAKVAVFSCPLDISQTETKGTVLLHNAQEMLDFSKGEENLIESHIKEIYDAGVRVVVTSGNVNDLVLHYLNRFEILVIRVPSKFELRRLCRVVGATPLARMGVPMPEEMGSVDVVETIEIGGDRVTVFRQVEDITRTATIVLRGATKTYLDDLERAIDDGVNIVKALVKDNRLIFGAGASDMQLCIRLISVGEKTPGIYQHAIKQYGEAFEVVPRTISENAGLDPTDVISKLYAAHHKENGESIGVDVECENDGTLDAKEAGIFDVLLAKKSAIRLATETVLTVLNVDQVVMSKPAGGPKPPGPNPHWDDD P78946 RL26_SCHPO SPBC29B5.03c; STRAND 5..7; /evidence="ECO:0007829|PDB:8ETC"; STRAND 30..34; /evidence="ECO:0007829|PDB:8EUY"; STRAND 45..48; /evidence="ECO:0007829|PDB:8EUY"; STRAND 54..57; /evidence="ECO:0007829|PDB:8EUY"; STRAND 66..73; /evidence="ECO:0007829|PDB:8EUY"; STRAND 78..87; /evidence="ECO:0007829|PDB:8EUY"; STRAND 89..91; /evidence="ECO:0007829|PDB:8ETC"; STRAND 93..98; /evidence="ECO:0007829|PDB:8EUY"; STRAND 103..107; /evidence="ECO:0007829|PDB:8EUY" HELIX 11..19; /evidence="ECO:0007829|PDB:8EUY"; HELIX 23..29; /evidence="ECO:0007829|PDB:8EUY"; HELIX 36..42; /evidence="ECO:0007829|PDB:8EUY"; HELIX 74..76; /evidence="ECO:0007829|PDB:8EUY"; HELIX 100..102; /evidence="ECO:0007829|PDB:8EUY"; HELIX 112..120; /evidence="ECO:0007829|PDB:8EUY" TURN 61..64; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..126; /note="Large ribosomal subunit protein uL24"; /id="PRO_0000130800" MKFSRDVTSSRRKQRKAHFGAPSSVRRVLMSAPLSKELREQYKIRSLPVRRDDQITVIRGSNKGREGKITSVYRKKFLLLIERVTREKANGASAPVGIDASKVVITKLHLDKDRKDLIVRKGGKVE P78974 HEM2_SCHPO ACT_SITE 199; /note="Schiff-base intermediate with substrate"; /evidence="ECO:0000250"; ACT_SITE 252; /note="Schiff-base intermediate with substrate"; /evidence="ECO:0000250" BINDING 122; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 124; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 132; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 209; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 221; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 279; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 318; /ligand="5-aminolevulinate"; /ligand_id="ChEBI:CHEBI:356416"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per monomer. {ECO:0000250}; SPAC1805.06c; CHAIN 1..329; /note="Delta-aminolevulinic acid dehydratase"; /id="PRO_0000140533" MPVDISSLLHAGYSNPLLREWQGVRPITKSSLMYPIFISEIDDAKEAIDSMPNQFRWGVNRLEEFLGPLVKKGLRSVILFGVIESKKDYCGSMADSENGPVIKAVKEIRHLFPELVVACDVCLCEYTDHGHCGLLYEDGTINNAKSVERIAEVSGNYALAGAQIISPSDCMDGRVKAIKQKLVELELSHKVCVISYSAKFASGFFGPFRAAANGAPKFGDRSCYQLPCNARGLAKRAILRDVREGADGIMVKPGTPYLDILAMASKLADDLPIATYQVSGEFAIIHAAAAAGVFELKRHVMETMDGFMRAGANIVLTYFTPELLEWLEY P79009 RS25A_SCHPO SPAC694.05c; CHAIN 1..89; /note="Small ribosomal subunit protein eS25A"; /id="PRO_0000192889" MAPKKKWSKGKVKDKAQHATVFDKSIIDRINKEVPAFKFISVSVLVDRMKINGSLARIAIRDLAERGVIQKVDQHSKQAIYTRVPAATA P79010 COX4_SCHPO BINDING 120; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"; BINDING 128; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P04037"; BINDING 143; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"; BINDING 146; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00692" TRANSIT 1..33; /note="Mitochondrion"; /evidence="ECO:0000250" SPAC1296.02; CHAIN 34..164; /note="Cytochrome c oxidase subunit 4, mitochondrial"; /id="PRO_0000006113" MFMNSMLRVSRQRAAVRSTVSLYRGFVSASIRRNEQNVVKAAAQELANAKEPSDLIGPGGRDGEVPTDLEQATGLERYELLSELSGRDAFDMKPLDASRKGTLTDPIMVTSLDPYRHIGCTGSPSGSHNLIWMTVYKDKLRRCPECGSVYKLKFMGDPNAEHSH P79011 T2EB_SCHPO SPCC1672.08c; CHAIN 1..285; /note="Transcription initiation factor IIE subunit beta"; /id="PRO_0000211229" MSSLSDQLSSFKKKVANQPIYAKPQPRQPASPTPTAYLNSNDGHSSAASSPGSYSLKKKRSKTSLVYSQPADSGVGTHYLSQLHYAVEYLKERNEPKTAEEIASYLSTPLTPMLLNLLKKNNRIYYDERNETFTFKPLHNIRSGAGLLAYLDSQKTHVGMSIKELRDGWPNVTVELEELEKQGEVLLLRTRKDGVPKMVWRNDKSCDCHVDKEFQQVWHEIPIPPTLDLASELGKYGLKPTSVDPSTVKRAGHNQTPKQKKPKTRRGKITNTHLNILRDYSSMKP P79016 RS19B_SCHPO SPBC649.02; CHAIN 1..143; /note="Small ribosomal subunit protein eS19B"; /id="PRO_0000153834" MAGVSVKDVDAQQFINAYAAFLKRSGKMTTPQWIDIVKTGTHKELAPYDPDWYYVRAAAIARHIYLRKQVGVGRLCKVYGGSVNRGMRPSHHRDGSGSVQRKVVQSLEKIGVLEKSDNGGRRISQQGQRDLDRIAYSLLEDEE P79064 RAD31_SCHPO SPAC4C5.04; CHAIN 1..307; /note="DNA damage tolerance protein rad31"; /id="PRO_0000194974" MGNHNINAEEIALYDRQIRLWGFNAQQALKQSRVLLITASPLANEIAKNLVLSGIGKLCVLDSMTVYEKDVEEQFFIEASDIGQLRANVFKKKLHELNPLVEIDTDTSLISEIDEGKISKFSMVIATQLDYEEFCRINELTRICNASFYATSCFGLYGFAFCDLINHNFAIDRVVDNTKVEEDMFIVQKPMKEAFQSILGETLKPRLAKKIPTLYPAMLSLLKSKKSDPDSIRQVCIEQKLNEKTVLNGEFLSKFSSNISFQWTPVMSVVGGVVSQDALNSISKKQFPIDNFWIFDAESGLAPIYRL P79081 ATS1_SCHPO SPAC1002.07c; CHAIN 1..168; /note="N-acetyltransferase ats1"; /id="PRO_0000074538" MGSVRIRSVIKEDLPTVYQFIKELAEFEKCEDQVEATIPNLEVAFGFIDEVTPVAYGVFIEENDQPAGMAIYFLNFSTWTSRVGIYLEDLYVRPQFRGKGYGSYLLSYLARESLRIGGRRLDWVVLDWNQRAIEVYEKAGAQKVGGWSMMRVTGENLKALADKLPGNF P79088 SC61A_SCHPO SPBC354.02c; CHAIN 1..479; /note="Protein transport protein sec61 subunit alpha"; /id="PRO_0000131787" MSDLRFLDLVKPFAPFLPEIAAPERKVPFKQKMLWTGVTLLIFLVMSQVPLYGIVSSDSSDPLLWLRMILAANRGTLMELGISPIVTSSMLVQLLVGSQLIEVNMELKSDREMYQLVQKFLAIIIAFGQATAYVLTGMYGRPQDLGAGICLLLILQLAAASLIVLLLDELLQKGYGLGSGISLFIATINCENIFWKAFSPTTYHIANGVQFEGAVINFVYVMFTWDNKAAALYQAFFRSGLTSSQIQLPNLWNFFATLLVFGVVIYLQDFRVEIPIRSQKFRGYRSTFPVKLLYTSNTPIMLQSALTSNLFFASRLLFNRFSSNFLVRFLGVWEQTATSGLSYYLSPPASFQDALIDPIHTLVYVFFTMFACALFSKLWIEVSGASPRDVAKQLKSQQLVMAGHREGSMYKELKRIIPTAAWLSGAVVGALAVASDLLGALGSGTAVLLCTTTIYGYYEQLQKEIKGDQYGLPVTPMMQ P87015 ASPG1_SCHPO ACT_SITE 49; /note="O-isoaspartyl threonine intermediate"; /evidence="ECO:0000250" BINDING 96; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 129..130; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; SIGNAL 1..16; /evidence="ECO:0000255" SPAC186.03; CHAIN 17..360; /note="Probable L-asparaginase 1"; /id="PRO_0000002363" CARBOHYD 27; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 35; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 40; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 82; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 106; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 144; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 179; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 246; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 302; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 351; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MWRSIISFLFFSVALCQPFLFQKRSSNISDFISFNASLPNVTIFAMGGTIAGYASSSTETVDYAAGSVGIATLVDAVPAIKNFSNIRGVQVTNVGSEELTPANVLNLTQLILAEVAKPDVHGIVVTHGTDSLEETAMFLDMTVNTTKPIVVVGAMRPSTAISADGPMNLLNAVVVAASNRSIGRGTMILLNDRIGSAFYTTKTNGNMLDTFKSYEAGFLGMILDQRPHFFYSPATPTGKVHFDVSNTTELPAVEILYGYQGLNPNLAKAAVDLGAKGLVLAGMGAASWTDPGNEVIDGLISNQSIPVVYSHRTMDGFSDYYYNGIPSYFQNPQKARYMLMLSINAGYSIQNITDIFSLEY P87041 GMS1_SCHPO SPCC1795.03; CHAIN 1..353; /note="UDP-galactose transporter"; /id="PRO_0000213362" MAVKGDDVKWKGIPMKYIALVLLTVQNSALILTLNYSRIMPGYDDKRYFTSTAVLLNELIKLVVCFSVGYHQFRKNVGKEAKLRAFLPQIFGGDSWKLAIPAFLYTCQNNLQYVAAGNLTAASFQVTYQLKILTTAIFSILLLHRRLGPMKWFSLFLLTGGIAIVQLQNLNSDDQMSAGPMNPVTGFSAVLVACLISGLAGVYFEKVLKDTNPSLWVRNVQLSFFSLFPCLFTILMKDYHNIAENGFFFGYNSIVWLAILLQAGGGIIVALCVAFADNIMKNFSTSISIIISSLASVYLMDFKISLTFLIGVMLVIAATFLYTKPESKPSPSRGTYIPMTTQDAAAKDVDHKH P87052 MUG10_SCHPO SPAC57A10.04; CHAIN 1..344; /note="Meiotically up-regulated gene 10 protein"; /id="PRO_0000080990" MALLKTMPIIRSLTRGKSIRLLQKQSTKRTNPCVYLEAKAVEQTPATEFNSILQEIISTEYNYSVDLKKTLNEIIMPIEGQSMEREAIGICTCFKTLNQLHTKLYQQMISSGSPVYSLSQSLPAFRDVYHMYTINLSGISAIEKIISDPSSCNSQLLIPLQHLLRYPIHLARVCKMLRKYPFLNGDFRMAVKTLDDFRELCSYIDQEKAREESYQVLSALCGNQGVAVDIPRHIKFKGSVIPATSFIYDFNACVFCDDGLVVWTRYVKKIEMKAVSIEQCLRVDELSNSILVCTLNMKGKLLNRHLAPQTMAASVFLKWYHERAGISNGKENKLNRLKVVNAKT P87056 YDJ8_SCHPO ACT_SITE 183; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 336; /note="Charge relay system"; /evidence="ECO:0000250" SPAC57A10.08c; CHAIN 1..364; /note="Abhydrolase domain-containing protein C57A10.08c"; /id="PRO_0000312658" CARBOHYD 326; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MYFFTISRLTSFISYGILGALGILTFLYLYDAYLAKSFQRLVIERRSKRESLSKNLSPNDNSHNSKIDISSDYQLLNEYKVAYYLRPGIIPLNHNLAKQEVFVFLHGLGGQMSQFQKVMSYFPPTACLFSFDYWGCGLSRQAFPNQRIGSVDQLTTKGLSKLTYKVLEKLFPENTQFILIGHSMGATIASRVSKMLQTRCTALLLLNPKIRFTSKEISMIVRLRKTPNAFISLYRLLDRFHGLRSSSVTRSLSKNIKGDGDAVRAQLWLWNRQSNTKIWKTMLMGLEELLEPGFHFPKCPILILFGEFDPVSSLKDKVFFQDYPGNYTFKEIDTGHCSMLEQPSEVYNCIDSFLDKFSTTDHNI P87057 NHP6_SCHPO SPAC57A10.09c; CHAIN 1..108; /note="Non-histone chromosomal protein 6"; /id="PRO_0000245222" MPRAAKSSRKKDPNTPKRNMSAFMFFSIENREKMKTDNPDATFGQLGSLLGKRWKELTSTEREPYEEKARQDKERYERERKEYDTKLANGEKTGKASAPAAAAAAKEE P87109 YDK2_SCHPO ACT_SITE 524; /evidence="ECO:0000250" TRANSIT 1..13; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC20G8.02; CHAIN 14..757; /note="Probable phospholipase C20G8.02, mitochondrial"; /id="PRO_0000316026" MILYIVLPFYVRTKPYSILPSYSSLQWITNAWCSLPSIYILCHCSKHQEEITILALKPLIAMNNSEEWPLKHVQPPKLSFRHLLSRSVTDAPSLRVRWFYAVDRPLRKSRTGPTEIKKAKNFLPFSAEDSEHIEKSYLKAVENDGQSEPVNVNEDYLYSVNVVSRELSPIYWDGPVYRILRGTWFFSRGDKLYPCEENLATQVEEGYLNSCPYREFSNEKDSAAAQSKTWALLGRYTGGFVQYTGSRNARLVYDDFYRNVSVKIMNRFSPASFHRSDKLVRGYELDMLESNSKPSTPVPTEELTSTTLLNDSSDPSDNFTPSNTESTIDLPSATDASHLMSRPDREVNHLILCCHGIGQKMGERVETVSFVKDISNFRKTLKKTFNSSPDLQAVYPKLKGGGNGVQCLPLLWRQDIRFGMARDLDSSFADDDDDDDESLNMSRDLALDDLEDDSIPTLDNINIPTVTGLRNIISDVLLDVLLYCQPNYRDKILAAVVKRLNRLYNLYKKNVPSFNGHVSLLGHSLGALILFDIIRYQGNIKYSKLQLDFPVANFFALGSPLGLFQMLNGKKIAGPIPKTNLTRSLSYSEQSFDSGVSILSCQNFYNIFHPTDPISYRVEPLVVKQMARLKPQKISHFRPHQDLSSSGVGHKIAGGALNVLSGLRSGIANTLILKSLSYASVFNEATADSHDESQGAENIRDWHIDERMYRLNKTGRIDFMLQEGALDTSYSYVSAMNAHSEYWKNVDLAHFILTQLL P87110 ITR2_SCHPO CATALYTIC ACTIVITY: Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in); Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268; Evidence={ECO:0000305|PubMed:9560432}; SPAC20G8.03; CHAIN 1..557; /note="Myo-inositol transporter 2"; /id="PRO_0000050454" MDFNNIPLATIKSSDDKGKDFIVEMTTRPSETKKKVPFSEDMREIPSLPNEEEANATDPQANEVADENGEGFEAEKISSWIWVLSAVAGISGLLFGYDTGVISGALAVLGSDLGHVLSSGQKELITSATSFAALISATTSGWLADWVGRKRLLLCADAIFVIGSVIMAASRNVAMMVVGRFIVGYGIGLTSLIVPMYITELAPARLRGRLVIIYVVFITGGQLIAYSLNAAFEHVHQGWRIMFGIGAAPALGQLISLFWTPESPRYLLRHNHVEKVYKILSRIHPEAKPAEIAYKVSLIQEGVKVDFPEGNKFQHFFHSLKVLFTVPSNRRSLFIGCFLQWFQQFSGTNAIQYFSAIIFQSVGFKNSISVSIVVGATNFVFTIVAFMFIDRIGRRRILLCTSAVMIAGLALCAIAYHFLPADTTQNTNSGWQYVVLASIIIFLASYASGIGNIPWQQAELFPMEVRALGAGFSTAINWVGNLIISASFLTMMESITPTGTFALFAGFCFVGLVTSYFTYPELAGMSIENIHKLLEKGFWQAVKESTKRVRKGRIDEA P87111 ETFD_SCHPO BINDING 93..107; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000255"; BINDING 575; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255"; BINDING 601; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255"; BINDING 604; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255"; BINDING 607; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]; Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.5.5.1; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC20G8.04c; CHAIN ?..632; /note="Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial"; /id="PRO_0000008666" MSYLSRSALARSVGAKHLTGVLRKIGRRGGRSMHVLPLASPSTLLKISSQTLRQDFTVLGARNFHSSSVRLNELTDNLRKLDTIEREVEDVDVCIVGAGPAGLSAAIRIKQQAAKANRDIRVVVLEKAAEPGNHSVSGAVIQPTALDELLPNWRDDPPENCTAVTHDKMKFLIPKLHFPIPVPPAMKNHGNYVMSLAEFTRWLAAKAEEYGVEIYPSFAASEVLYNKDGSVIGVATNDFGVDSKGLPKDNFERGMAFHAPVTLFAEGAHGSLSKSIIKRFNLRGNCEPQTYGLGVKEVWRVPDENFRKGEVAHTLGWPMRNDTYGGGFMYQFGDNYVTVGLVVGLDYPNPYVSPALEFQRMKQNPFFAKVLKGGKCLEYAARALNEGGYQAIPKLVFPGGALIGCSAGFVNVAKIKGTHTAMKSGIVAADAIVDAFGRDAASKPLLLNDYEENLKNTYVFKELYSVRNIRPSFHSFLGNYGGMAYSAVEAYVLKGRVPWTLKHKGGDAKATKSASKYKPINYPKPDNVLSFDIPTSVSRSATMHAENQPCHLFDHRPKDRKSCFETYKGVENKFCPAGVYEYVNDEASSYGKRFVINSQNCVHCKTCDIKDPLQGIQWKTPQGGDGPKYTLT P87112 NOT1_SCHPO MOD_RES 1341; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1568; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC20G8.06; CHAIN 1..2100; /note="General negative regulator of transcription subunit 1"; /id="PRO_0000318140" MKSQEQQTPETREKSSSTSESGHPISLDSKTPPPNDSKIESIVKAQILFLLSTLREDQYDTKLEQIRQLINKNAPRVYHHFLRRLIQGNSYRIFGTGKSSDGLATYKLLLDELKSLTKSWVMAKRFSDAISGSDSEVFEDFDIEAFLDHFQFSPLERTNLLIGLTTSVKPTLAKKASALLKNTFQSLLNQLSDPTQQQSIDKNDLDLLREGLFTTDYDRIPLIKVPKFDAIIEKKLANSRPLTALFGPMKASKATLKSMKEAILKKYPPGTATETDVAYLINSLVAIHDYGAWDTVLMGKAIVSSFENLNWEAMLSMFDNPKFMITGTPSLVLFFTIFTNAYKLRQTNFTLDFLWVLWRNPLPQLSIISHIILSPTSMFDIREFNVNPVVSVDSLKDYSEELVNYAKIYEKSNLNCIELVQILLRLLSEVVTYETSLFLNFLDEKVSAELLLLGTLQLPLAWNPVQESLAFQWCSDFFSNFKEHKFVFVRIERTNPQFLFAFLRSLWLKDSSSVNQVVEFIIENDFTSHIGNIQPNRFALEIAALAAARKALSFQDWLDKKMLEFEDADGLNVFLVEVLDFLMSRAALQKNESEQKEESVVLSIDTVNVLLTTLMDNVSISEEVSEHIKDVQILCLQVYPRLFSLGHDRDSIVIATNTTNSFSPDVESEVESYFQALYERRISIGKIVLTLQNFKKSENPRDLDLFACLQHSLFDEYRFFPDYPLEALALTAVLFGSLIQFELLSFVPLGVALRYVYQALLMPTDSKMFRFGMQALVQFQEKLPKYINYCNLILGIPSLQLVRPDIYDSIREMIASNENTEVEKDKLDSFSALANPASPKAPEYTFVSIHVPPLNVPNAEGEIEESVCDNILFAINNLSQLNFNEKLKDVKDNLTPAYLPWFSHYIVTQRVSREANFLSLYGKFLEELKSSDLYKIVFRDTLQAILDIMNNNAETLSPSEKTNLKNLGSWLGSITLLRNKPITTLQVSFKDLLLEGIDSGRIDRVLPFVCKVLEKASSSVIFKPPNPWLMGILKLLVELYQFADFRLNLKFEIELLLNNLNVKMDNIEPSEMYRNHLVQKADLEKELPEDVLNAEFPDGTDVITQYIVAASSQITVTDAVAQVFGKPKPAIKNITQLIIQQSVLEIISAVVRRSVGIAAITTKSLLQKDFAAESNPSRLLLAARQMAKTLAGNLAMVTCREPLQMLMINNFRTIALQDVENVHAAVAQAIDELVSQNLFVASSVIESVASETAIAEIDAEIEHMIVERVRHRKTTPNLPFVDPAGAANLHLNLPSVLKLSSELTPQQFQLYENFDRLSLSTIMSNNSFTSLNGLRTDSADSTDALNSNLNNTVENEANQTALNYARNLLIIIGQLFQLAAQMPYTSMQEVPADHELHELVNQFLTGVASINHPIADHVFLLCAQECCRILLTDSKSPFILEVFSAILEYICQASTKTAINVSLYWNFSNDLEKLNLPIILSLIRFGILTSGEVDYHVARGVRSEQGSGPVTDFAIELLRTAVGGENPMALPGNFVNSITSLYEISESFSGETKQAYEQLVETMNKSVSPASEILSDLDNKQQLNDQIIIVFVSWVHLLRNSATNDETKAAFVYQLHKQGILSEPELCIQFFRCNLEAVLVAFLEAASVNAPDYFNVDAYASLLVNVVKYTEGSTEGTVSSKSVLFRKIIALIIGVFAELHNSMAEFVHQKTFFRLFSSILSELDDAKDVLESCFVDIYSVILECFLAIQPRSFPAFTFAWLSLISHSYLLPKVLLVNNDKINDLFSEILMSFLKFLDLKDDIDKAQFKLLYNGFLRIILVLLHDFPGFLATHCYQLIPYIPLECVQLRNMVLSAFPSDLHLPDPFAQGLKVGRLPEVTRAPLISNSVSASLEKFASALDLEACFSSSKPAEVAKLLLEVYSSQDTPTKLNEWANYFMLCLIRHATRDSPAKQAPQFQSKSPECVIISTMNRSCDSKCRYFLLTAIANQLRYPSSHTYYASCCFLYLFKSSSNNPQELLIKEQMTTVLLERIICNRPHPWGLLITFTELLKNEDYNFWKHPYIKRNDEICRLFDSLHEHVMAPSSANNVSTEEATELMGQV P87119 MU145_SCHPO SPAC3A12.03c; CHAIN 1..309; /note="RING finger protein mug145"; /id="PRO_0000280180" MPIPKNRPMHVEEEVSSQTNTEILLFALVIILSVIFINFFFFYLCRCCVYFYHTLENQEGDDERPLIQHHMVNRSTGSLSPSVDRLGNVLGYDIPSRRRRSVVSKEALSCISLEIPYIKWLKKRKGHAKGESTFLDNRSENQSVIVQGQGETPSVIITYDVRRPNLGSTSFVEMSSALSNIYNTDASDGDSSDDSCLLEDEEDFCIICYADYAFDDILRVLPCEHVFHTQCIDTWMTTMKASCPLCNEDYYKYFLQMDAASSVTHENAAWSIPLSPGDSRTHSAETDRSLLSAMSVRNSRMPYIVSSTL P87120 RNP3_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; SPAC3A12.04c; CHAIN 1..235; /note="Probable ribonuclease P protein subunit 3"; /id="PRO_0000140033" MFIDLNVVWPTLGVKDLNLVKTVKTLERLGYTAIALNYQYDGKLQNVIKNPIVKELYPEQKIKIYSRITLTIESMPQNKVLSNVTKEFDILAIRPIGDRLLQQTCSDLEFDILSIDFTQRLPFYLKHTFMGLAVSRDIGIEISYSSGLRDVSNRRNLITNATSLVRATRGRGIIVTSETRTPLECRAGFDVINLATFWDLKQDQARKSVGESCRSVLLHAETRRDTYRSILNGCH P87121 TAF2_SCHPO SPAC3A12.05c; CHAIN 1..1172; /note="Transcription initiation factor TFIID subunit 2"; /id="PRO_0000356181" MSQLVDVPARGHQKVAIDIDFASQTIIGRTDITVNPIDSNLQKIVLDCYQAEIHSVYVNGDLTKFSYSDALKKLRIDEPNSTVNQHHQLNLQYEALMNDLGGINIFLSKPPGDELRPLIVSIDFSVHQPIFGITFVGIDPVDHRYPHVFTNNSIIPYSTCSWLPCVDGIWERSTWEFEITLPKTLSSLMHREKTQPSDLNNGANGVDGHDDNYENNRFDHQFNLSNEPDLLEDHDIEVICCGDLLDQVTHPKDMRKKTVYFSVTTPVAPNYIAFAAGPFKHINLTDFREPEDDDAMGSSAIDITGYYLPKYAEEVENTCVFLYKAMDFFVREYGSYPFNSFKLCFVDETNFPIISTPSLVISSNSILYPKDSLDQIYDSTKTLTWALASQWIGVYLIPKAWSDLWLIYGLSYYICGLFLKKLMGNNDYRFRLKKQVYRLLELDIGKPPISQRNINIPIDPNTLDFIALKSPLVIHILERRLTKTGGSLGMSRVIPKLLLQVMSGDMLNGCLSTSHFLKTCEKASHMRLDVFAQQWIYGYGYPIFRVVQRFNRKKMIIEMGIDQVQTKEAPRAPMSDKNFLSDAIRHLNNESIPTGLPVFSGPMTIRIHEADGTPYEHVVELKDSFTKLDIQYNTKYKRISRNRSTKNVKRDGDHNGDDSDYVIRSLGDVLQSDEDIERWHLYDYTKEEEDTMATEAFEWIRVDADFEWICDLRVRQPEHMYVSQLQQDRDVVAQLETIRHFTSESFTVSQQVSTVLLRTLLDNRYYYGIRQEAARALARCAIPELDWVGYYHLRMAYLEKFCFKDSTIPKSNDFSNITEYYVKCAMLESFPNIRDRKGVTPSSVKKLLLDLLCYNDNANNEFSDAYFICLLIDSLVEGLIPRGETVQYAFSDPEHMEFVNQVINEIDRYMRIDACMPSFKNIITCKSLKAKLRLAQTFHLEFGPKELLPYTQEGNYVLVRCIAFNLMLQAGALKYTPLIKYIFYILTNDLSPVVRRSLLYSVQDGLGALARGGTKSDVASEDLIVEEDITKAVEKRIDITSRASISGAIEALRNDLGQNHDFATEIWNAINNPKSDLLTKRNLLMICRVLYKAKSSLLVTLKIPSLIPRLRAIHLGKGKIVIKKAPLKQITSKTKEKSTSPTPPSITINPIKPKGPTLKIKLTNLRSTPPSH P87123 RPB11_SCHPO SPAC3A12.07; CHAIN 1..123; /note="DNA-directed RNA polymerase II subunit RPB11"; /id="PRO_0000149314" MNQPERYELIELMGLPKVTYELDSKSPNAAVVTLEKEDHTLANMLANQLLSDERVLFAGYKVPHPLNHNFILRVQTVEDCSPKQVIVDAAKSLITHLEEIKVNFMREWELKMISVEGVEMEFS P87128 EIF3J_SCHPO SPAC3A12.13c; CHAIN 1..274; /note="Probable eukaryotic translation initiation factor 3 subunit J"; /id="PRO_0000116638" MDSWEDFLVEDPAKPAEFDFPLGKDSQSSSKPKKRFDDEEDEDEEENKESLQNDSHSVSQKSSSSSQNDQGSNKMTRIQQKIQERNFEKAIKASEAAAKEESLESSKEAMRQAEIDSDLANAMDLFDIVDKNSASANRSKQADQRQLKTKADYAAFQADILKKVKNCQTTAEYNNFVQDLIPLLLTGLNATNLKAVQKSVNKLVVNKEQQEKTQSKRGAAAPAAKPVSTAAPSKKGGKPTVNVNSKKTVADKSAYEDYIEDEYDDYADDFDDFM P87129 VPS53_SCHPO MOD_RES 728; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3A12.15; CHAIN 1..756; /note="Vacuolar protein sorting-associated protein 53"; /id="PRO_0000116639" MSNGNDNSLIIKNIGNNEFKFVETLHELLPEDITYDDLGSLRLSLSERLQESVKKLDANKKTYEDAKLSMGEKMDDLNSSIVSLLQELSTLQSVAENTQSSIVQMTSEIKNLDFAKQNLATSMTMLKRLQMLVTAYEKLRTLRQNQKFGEAISLMQATLQLLNFFKKYRSVERIASLSRSISEFQKSFYEQVFDTFQSQFKKESGMRGGFSPSSVQYLNELCRFIDIFAGDPPESVIRWYCRHQLEDFMKVFRENEEAGSLENLPRRYTWFKKLLQTYDQLHKPIFPPHWKVDFRLYEVFCEETKNDLSKLLKDDRLSLQVFVASLEQTLEFESFIDHRFYNTKSRFNSNFEPKERQAYNALSSVFEPHYTLYFNQQSQEFSILFENFALEKQTSTDESSQVLSSSIKLFQAYRKTLTQFVRLTRSSPLVGLKNLFIKWLRRYTQVELLDYQESSTFKDIAIRLNTAEYIYRTTIELEKRFQEISNKEFKDKMSFSEVLEVISSSRGTLLKFATGKFENVLNSDLEPLSKMDLKNIETVGDQSSYVGGAVQNMTAKASEFLSVVDLNMFARNFCDRSCESFTRQFLNAIYLAKPISEVGAEQLLLDLYSFKNALLKLPDLKQDYSITDSYINHLTIFMGYIETVLKTLLTPASPKAGFIQSYIFLVKDRSVTNFTVLLELKGVGKSDISSFLQQFSDFVKKTPQLEESSPIFKYLTINTAVEQAATRSRLSLDLAPESSRTLQNLGRLFTSKKKHV P87130 TIM17_SCHPO SPAC3A12.16c; CHAIN 1..164; /note="Mitochondrial import inner membrane translocase subunit tim17"; /id="PRO_0000210295" DISULFID 11..78; /evidence="ECO:0000250|UniProtKB:P39515" MASADHTRDPCPYVILNDFGAAFSMGTIGGAIWHSIKGWRNSPPGEKRISAIAAAKTRAPVLGGNFGVWGGLFSTFDCAVKGVRRKEDPWNAIIAGFFTGGALAVRGGWRATRNGAIGCACILAVFEGLGIALGRMNAEYNRPVAPVIPDAPASGSTSAAPAAV P87139 YDM9_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" MOD_RES 280; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A7.09; CHAIN 25..372; /note="Uncharacterized RING finger protein C57A7.09"; /id="PRO_0000310482" MSYYQIIVCILASISYIILLEVIALDLGVLDNIFIPKRFAASTDVAIQLPDRNVTLWSRQAVFGKHFTNASATTVINLYLPSNFQEDMSGCPNRNDTDASYFYENDIIDYDIEYIEQKSYSSKPSARVQKDDGGESKDEAILDFLLVQRGKCTYFDKALEAQRLGFKGVIVGDNRSPSSFRLHYMVAPDKVDESKVHIPSLFVSTSSYNLLWSDLLHSYRQPLKLYAKPEELGDMFWPFLLCFSPSIIMLITVQALAIRKFIRTYRTKSKTRRFIEDLPSRTISREGFYSEEEEIENSTQNGELVPLMDESTRRATFGVECVICLESFTKGDKVVALPCKHEFHRPCIAKWIVDYRHACPTCNTEVPPPKPF P87142 YDMC_SCHPO BINDING 39..46; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 500; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A7.12; CHAIN 1..566; /note="Heat shock protein 70 homolog C57A7.12"; /id="PRO_0000078399" MQLKLTKTLPFSENFIMADSEEYKTVIGISFGNQNSSIAFNRDGKTDVLANEEGNRQIPSILSYHGDQEYHGVQARGQLVRNADNSVTNFRDLLGKSHDELTLHHCHYSANPVNVEGQIGFKITVQEDEESDPKEKILTAHEASVRHLRRLTESAEDFLGTKVNGCVMSVPVYFTDAQRKALESAANEAGLPVLQLIHDPAAVILALMYSEEVLIDKTVVVANFGATRSEVSVVSVKGGLMTILASVHDENLGGEQLTDVLVNFFAKEFEKKNGIDPRKNARSLAKLRAQCEITKRVLSNGTTASAAVDSLADGIDFHSSINRLRYDLAASATLNRMADLVTEAVEKANMEPFDISEVILAGGASNTPKLTSLMESIFPEQTIIRSSSSVTPLQLDPSELTAIGSGVQASLIGHFDAADIAASTDAQVVDVPHLTAPIGINEGENFVTIFDIETALPARKTVEVIAPKEGAAFIPIYEAERSVKVTKVEPEPIDEEEAFSDDEEEEPEEIKERIAIPKTLIATITLPDVSPNAKIELVLQIDAEGKLTASARPKDGKGTNVRGSTA P87146 TIM22_SCHPO SPBC25H2.04c; CHAIN 1..175; /note="Mitochondrial import inner membrane translocase subunit tim22"; /id="PRO_0000210300" DISULFID 46..119; /evidence="ECO:0000250|UniProtKB:A0A1D8PI78" MSLSGLLPPNLGGNSPNADGNLTPEEKAALQQAKIIGYMNRISESCVFKSSMAGVLGFGLGGIFGMFISSLDLQHIDPKIYEKPFREQIRIQARDMGSRSFSTAKNFGLLGLIYSGSECCIEAFRAKTDIYNAIAAGVFTGGALAVRSGPKAIVLGGAGFGLFSYGIEKYMHWGE P87147 NACA_SCHPO MOD_RES 122; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25H2.05; CHAIN 1..173; /note="Nascent polypeptide-associated complex subunit alpha"; /id="PRO_0000135593" MSVESQPVEKISELPAGSTTVVHAEKAQKLIQKLGLKRVEGITRVAMRRPKNILLIINEPIVYKSSNNAYIVLGKVTVEDMAAQARAFNESQKQATETKEEAAITEESGDAQPADTAKIEESFEQEKAVDETGVDAKDIELVMAQANVSRAKAVTALKENNSDVVNAIMSLTM P87148 YIF1_SCHPO SPBC25H2.06c; CHAIN 1..293; /note="Protein transport protein yif1"; /id="PRO_0000253961" MPPKLYHPQPTHAIPVSNMRVNTRYEPTAGFSGTSVPSVQAANPSAYLPNSATAQMGFQLGKNAVNAGQEYVEQNFGKWLSTTRLHHYFTVTNSYVVAKLLLIIFPWRRRSWARKLRRSEINGSAEGYCPPAEDLNSPDMYIPLMAFTTHILLLCALAGLQDDFQPELFGLRASKACAVVLVEFLATRLGCYLLNISSQSQVLDLLAFSGYKFVGLILTSLSKLFEMPWVTRFVFLYMYLATAFFLLRSLKYAVLPESTMAINATITSHQRSRRIYFLFFIAASQILFMYVLS P87153 TCPH_SCHPO MOD_RES 176; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC25H2.12c; CHAIN 1..558; /note="Probable T-complex protein 1 subunit eta"; /id="PRO_0000128371" MSLGGPQIPVIVLKEGTDDSQGRGQLLSNINACVAVQDTIRTTLGPLGADKLMVDDRGEVVISNDGATIMKLLDIVHPAAKTLVDIARAQDAEVGDGTTSVVVFAGELLREARTFVEDGVSSHLIIRGYRKAAQLAVNKIKEIAIHLDLSDEGKLRDLLTKCASTAMNSKLIRSNSTFFTKMVVDAVLTLDQEDLNENMIGIKKVPGGAMEDSLLVKGVAFKKTFSYAGFEQQPKFFKNPKILCLDVELELKAEKDNAEVRVDKVQEYQNIVDAEWRIIFSKLEAIVATGAKVVLSKLPIGDLATQYFADRDIFCAGRVAADDLNRVVQAVGGSIQSTCSNIEEKHLGTCDTFEERQIGGDRFNLFEGCPKAKTCTLILRGGADQFIAEVERSLHDAIMIVKHALKNNLVVAGGGACEMELSKYLRDYSLTISGKQQNFIAAFARSLEVIPRQLCDNAGFDSTNILNKLRMQHAKGEMWAGVDMDSEGVANNFEKFVWEPSTVKSNAILSATEAATLILSVDETIKNEPSQQPQAPQGALPPGAANRIMRGRGRGMPR P87155 MUG16_SCHPO SPBC25H2.14; CHAIN 1..235; /note="Protein GMH1 homolog"; /id="PRO_0000278494" MSRSFRNGFRLLKLSQMDFERAWWDMANLFRAPRRVYRSITLRKQNINRYGREDFSFIVLFSCMIVISALLWALFYMNTPKGYVTTITFMLFVDFGAVGVIMATMYYFIAKRFLMKSNDTILSSTDYQLEWNYCFDVHCNSFFPSFVLLYVIQLFLLPVITRDNFISLFMGNTLYLVALCYYSYLTFIGYQILPFLKNTHALLLPIPMFFIMWALSLLGFNVPKHVVDVYFGKSA P87158 RS4A_SCHPO SPBC19F8.08; CHAIN 1..262; /note="Small ribosomal subunit protein eS4A"; /id="PRO_0000130839" MVRGPKKHLKRVAAPHHWLLDKLSGTYAPKPSPGPHKARECLPLIVFLRNRLKYALNGREVKAILMQRLIKVDGKVRTDSTFPTGFMDVISVEKTGEHFRLVYDIKGRFTVHRITAEEAKYKLCKVKRVQLGAKGVPFLVTHDGRTIRYPDPLIKVNDTIKLNLETNKIESFIKFDTSAQVMVTGGRNMGRVGTIVHREHHLGSFEIIHVKDALDREFATRLSNVFVIGETGKSWISLPKGKGVKLSITEERDRRRALKGLA P87171 KPR5_SCHPO BINDING 152; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P38063, ECO:0000255"; BINDING 154; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P38063, ECO:0000255"; BINDING 167; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P38063, ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000250|UniProtKB:P38063}; SPBC3D6.06c; CHAIN 1..341; /note="Ribose-phosphate pyrophosphokinase 5"; /id="PRO_0000309464" MKNLVVFGTESHPKLTESICEHLCLDIGRVELSKFSNGETSVRIKQSVRGCDVYIVSPASGQVNDHLMELLIMISACKTASAKKVTAVLPVFPYSRQPDQKFSFSGAPLSDLQDAVVPCKKQTGYHPWIAQSGTLVADLLMCSGADHIITMDLHDPQFQGFFDIPVDNLFGRPLLKHYISLNIPNYHNAVIVSPDAGGAKRATAIADALGLDFALIHKNRRHEYGTSLMLVGDVQNKVAILIDDLIDTAYTLVRAAEFVKEHGASKIYALVTHCVLSGDAIERVKLSCIDKLIVTNTAPQTITPSGCFDIIDVAPTFAEAIRRIHNGESISILYDHNQVWV P87177 YB1C_SCHPO MOD_RES 769; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3D6.12; CHAIN 1..922; /note="Uncharacterized WD repeat-containing protein C3D6.12"; /id="PRO_0000051492" MVKSYTRYEPTEFFGVIASSGCNILGQPSSSAKSVGRAIVGGLESVLEWDLKTGQLLSKWKDSDCSAKVTCIANFDEMYAVGYADGSIRLWKDGELLITLNGHKSAVTTMDFDKMGTRLASGSMDTDIIVWDIVAETGLFRLRGHKDQITKLLFITPPSKNTAEETVVDTDIDSGDMDVDSKSSDSFLLSVGKDSFMKLWDLSIQHCVETHVDHQGEIWAMCVSPDAKRCLTAGTGSDVKVWEISFPDDNNFTPTTKAFQQLGTFTRQSRDRPITLAYDVSNRYVVFQAHDRLLEVFRLRSSAELEKILNRRRRRKKSEDVSITLKDEYEPFALIRTTARASSVAWIPGNRTPTLVTSLQNNSIEVYALDVKSEGSAAPLTERASRISAIEIPGHRADVRTLALSANHDVILSGANGSLKLWNKKTTSCIRTIECGYVLAASFINNDKCIVSAYKSGELEVYDIASSSLIERIQAHDGAIWDLAVGHDGTYFATASADHTVKLWSLKSSFDFVPGTTRKVTTLKLEQTRQIDFTDDVLAVKISPDGRFVAASLLDNTVKVYYLDSLKFFLNLYGHKLPVLSMDISYDSKLLVTCSADKNVKIWGLDFGDCHKSIFAHQDSIMEVTFQPDTYNFFTCSKDREVRYWDGKSFDLILKLRGHHSEVWALAVGPTFVVSGSHDHSIRLWEQGDDLVFLEEERERELEEQYESTLVSSYENAEADGEVKDGDVAAVTKQTIESLKDGEKILEAITIGIEDLDQEIQYRLDLLKSPGKARGPRNPILAHLGVSAEEYVLNTFKKIRSSHLDDALLVLPFEHVLSLFRFIDIWASRKWSIPLVSRIIFFLLRTYHRQLTTTVKMRPLLNNIRSSLRGSLQEERSLIGYNAAGLSYLRHEWELTHNTSLEDIDSTSLEVDGKKRAFSNIV P87178 YB1D_SCHPO MOD_RES 708; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3D6.13c; CHAIN 1..726; /note="Uncharacterized protein C3D6.13c"; /id="PRO_0000116494" MRSNTFGSVMRISWVVAFITMVQTLVSGVPLTDNDLESEVSKGTWFIKYYLPSCGACKRLGPMWDNMVEKAKEQVEGSNFHFGEVDCSKELSSCANIRAVPTLYLYQNGEIVEEVPFGASTSEASLLDFVETHLNPDTDPDIPSDEDVLTDEDTEEVASIQPALSTSVSSLSLASTAMSKSASASEFSGSSVTKASKKLTSSPTSVASKKATLSSVSKVASTSSLPVTSVSASVDPKSAASKVQDAEFSIQTAPSFPKEKEEKENTEETEESKKSINPTGTSKALALDADIDAALTDKEGWFIQFYSSECDDCDDVSTAWYAMANRMRGKLNVAHINCAVSKRACKQYSIQYFPTFLFFKEEAFVEYVGLPNEGDLVSFAEEAANFEIREVELLDTVNAEKNGDVFFLYFYDDDSAEYLNIIRKTGIQLLGHANLYLTTSQQIAKKYRVVSFPKLIVVRDGIASYYPAKMAQDNKDYRRILGWMKNNWLPVLPELRTSNSKEIFNDESVVLFLLNPELDDFDETKRTAQKIATEFLDEEGRTYQSNWQKETDKKNSLVNEAEEKNDLEAIEAAKNFHVNGKPSPTRFAWVNGKFWAQWLRKFDIDIEATGPRVIVYNAAQDIYWDETAKGTPISIEKDTVFDIIKQVETDPDHLKFKILKKNLGVEYLESYGLNIRVLYMVLGIVTVGILVWYFSGRRARTLQRRRHSTPILPVSMRSTGNSGKFD P87214 HEM4_SCHPO CATALYTIC ACTIVITY: Reaction=hydroxymethylbilane = H2O + uroporphyrinogen III; Xref=Rhea:RHEA:18965, ChEBI:CHEBI:15377, ChEBI:CHEBI:57308, ChEBI:CHEBI:57845; EC=4.2.1.75; SPAC31G5.08; CHAIN 1..251; /note="Uroporphyrinogen-III synthase"; /id="PRO_0000135253" MKTALLLKTKSQPFDPYVEAFEKYGRDTAFIPVLRHKRVHEEQLRDKLKNVRKTYCGLIVTSQRVSETLDEALKQEDETERQKILMETPIFTVGPATDDSIRRLGFQQTHGKDCGRGEVLADLIEEWYTTTKQHKPLLFLVGEKHRDIIQRKLGDDRVDSLIVYATQELENTETQIKDTIRKHPTIDWIVAFSPTSICSLLNTFELKIATIGPTTGDYLKKLGTQPNVVSPAPNPESLASSIVAFDEENSS P87215 DIMI_SCHPO SPCC16A11.05c; CHAIN 1..142; /note="Mitosis protein dim1"; /id="PRO_0000218285" MSYFLPHLHSGWHVDQAILSEQERLVVIRFGRDHDEECIKQDEVLYRIAEKVVNMAVIYLVDIDEVPDFNKMYELYDRTTIMFFYRNKHMMIDLGTGNNNKINWPLEDKQEMIDIIETIFRGARKGKGLVISPKDYSTRHRY P87230 COQ5_SCHPO BINDING 117; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03191"; BINDING 143; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03191"; BINDING 173..174; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03191" CATALYTIC ACTIVITY: Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201; Evidence={ECO:0000255|HAMAP-Rule:MF_03191}; TRANSIT 1..34; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03191" SPCC4G3.04c; CHAIN 35..305; /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial"; /id="PRO_0000193360" MSRLRAPVAKFLADGLKGIRSTALAGSRLSNCRYTSTSSKDTDTSSHMTHFGFKDVPEDEKEHLVKNVFSSVAKKYDEMNDAMSLGIHRLWKNIFVSRLNPGNSTVPMKILDVAGGTGDIAFRILNHATNHNGDRNTRVIVADINPDMLSVGLRRSKKTPYYDSGRVEFIEQNAEILDKIPDNSIDMYTIAFGIRNCTHIPKVLEQAYRVLKPGGVFSCLEFSKVYPAPLAELYRQYSFKILPLLGTIIAGDSQSYEYLVESIERFPDAKTFAKMIEDAGFTLAGETGYETLSFGIAAIHTGIKL P87234 GYP3_SCHPO MOD_RES 191; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 193; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4G3.09c; CHAIN 1..635; /note="GTPase-activating protein gyp3"; /id="PRO_0000312837" MAGITEHSTIMNDANFKEENAHLSDASIHFGSSEQDKTPSDYELDDVLDLYNDTTEDDADDADDVNNYIMSPSSSLSSESEHALDALVYPIYSHHNILEHENNSDYASITPSNHPAFTSCAYLQNPVVDSNNEYESKFRLSLEIPPTDFLSTSTELSKRESCLSTETSSSKFSAVTAATITNETQSEKRSSQTDPSLPFKTNSLNCDVTYEEGPLTKKLRGPKKYKPSHSSWDIYGFKKANQFYTVDQYNTWYGPYSRYLERREQRWKLFLQENGIDYIHQSPSIFPSRSAKTQRFIRKGIPPEYRGNAWFYYSGGYELLQRNPKLYETLWRCACIKKPSDSDLIERDLYRTFPDNVHFRHKSKHSRNSSDASEHSSEEPDVPMISKLRRVLMTFATYLPENGYCQSLNFLAGFFLLFMSEEKAFWMLVITCRKYLPKMHDANLEGANIDQSVLMASVRESLPAVWSRISLNFDGIPVNDIVAKLPPITLVTAAWFMSAFVGILPTETALRVWDCFFYEGSKVLFMTALCILRLGEDDIKSKSEQTEVFQVIQDLPKSLLDANAFLSLCFRRNFRRTPSQKDIERRREKVAKKRNSSASKLEMSDSSKHHLSRSSSRFSKSHIISQLHNHLKKST P87235 RHP42_SCHPO SPCC4G3.10c; CHAIN 1..686; /note="DNA repair protein rhp42"; /id="PRO_0000218297" MPPKRKASKNSVRGRKRRTRTNNLPLNPEVKEETVVSSTHRQTRSQSKKPSLSSSAEPPSESLDDNISALNSLQRSASSSEKGSDEDNEKLGSSEDDEFDDDFDTWEQVDLSPNKQEDKKDLHIVTQHITPQLTKESKKGSSSAMDKSIRLSIHIMHFTCLLYHGSVRNRWLMNSLLLDGLRDLLVEKQPSVVEAWVCSSQTHEDLLKLLNGLRMWWNKSFKIESHGLRKLGYRTLKQGFDIGFSPEIFHNFHEYQASLLSLKGSRDLAAQGFTALCRSLNLKARLIFSLQPLTFSTASYDDWSPHILPEETSTSIDDDLRYPIFWTEIYDQSEKKWIAVDAVVLNGVYTNDMTWFEPKGAYAESKHLRMGIVAAYDNDLYAKDVTLRYTDYQSSRLKKIRHVSFADKYFDFYKAIFGQLAKRNKDAEDIYEEKELESKVPIREPKSFADFKNHPEFVLIRHLRREEALLPNAKPVKTATFGNGKKATSEEVYLRKDVVICKTPENYHKEGRVIKEGEQPRKMVKARAVTISRKREHEFRVAETNEPVLQGLYSSDQTELYVPPPIKDGIIPKNGYGNMDCFVESMIPKGAAHLPYRGIAKIAKKLNIDYADAVTGFEFRKHRAIPVTTGIIVPEESAQMVYEEFLECEKIRIEKQQMKERKIIYGQWKHLLNALRIRKRIEEQYA P87236 MU154_SCHPO SPCC4G3.11; CHAIN 1..316; /note="Meiotically up-regulated gene 154 protein"; /id="PRO_0000278509" MGKLIRRTSLTSKIINLPIDYFIYVCEQFDSVEWDKVSDRYSIPFSLAVNFIFLLMRIYIKSTHVPVQRNQLFVDKQSINTSRSWFRAFLSFLSICFLFISFLNFIFSTRFQNKLYRTLPQDKRTTTSTPNVKPVFQHSNNDDGDEQVFELKVWSPNQFLLNFACLFSPAHALILWFYSTSLRVTLLTFLLSFTTLHFVNKFSLLLKDQQYLHRQVFFEYDKKFVEPRLSVVKRDVAINTTRGPTTASIEYFTPRKPIDTFLEHRSSSHDHLTSTPRTPIALQRRSVHHLHDSGISRDSSSPFKRFPHLSDGSSRF P87239 MDJ1_SCHPO TRANSIT 1..66; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC4G3.14; CHAIN 67..528; /note="DnaJ homolog 1, mitochondrial"; /id="PRO_0000314109" MFSKYLQSRVCGLHSFTNSSAQQLFSKSIAHSSRRNFVISSSCTKFRNVAIQRNAKREFSRCAALKNFSYHARCFHATRAVWEMTDPYKTLGVSKSASASEIKSAYYKLAKQYHPDANPDKAAQDKFVEIKQAYEVLQDPKKKKAFDTYGAGAFKNGEFTGGDFEGFQNGFAGASSFSSGFPGFNFEDLFGFSSRGPQARRNTSFDVFVGEDIEASITIDFMEAVRGAKKDLSYSVSSTCSSCHGSGLQPGSHKSTCFACKGTGQRLHFIPPSFHMQTTCDSCGGTGTTIPPNSACRSCMGSGTVRERKTVSIDIPPGIDDNTVLRVMGAGNDASTAKGGPNAKSRPGDLFATIHVRKHPFFVREGTNVTYNAKIPMTTAALGGTLRVPTLTGNVDLRVSPGTSTGDRITMAGKGIRKVNTSRYGNFYVNFEVTIPKILSPHERSLLEQLADALNDSTARRTQSSPSGTNSSTSTSSTSSKHSTGISTEPTTGEENKQDGSVGGFFKRAFRRLHPDEDQNPKKDESSS P87240 NOT2_SCHPO SPCC4G3.15c; CHAIN 1..306; /note="General negative regulator of transcription subunit 2"; /id="PRO_0000356247" MSLANRLSHLNITGGNDFKASIGPSVGRQNEATNPWSSTSHSLENSAATVVNELQTTKEQKTPEQSTTANPLFPGNDFSDFNNHKSKLLGVITGKSTPSSQAEKSDTTNSKTGSTEELTETPADENAKQYMLESLLPIIRMEDSEMSTLQLGCDLAALGFDLAPVEEDRLISTNLFSPWAELNTKKPVSQPMFKLPACYKNVNPPPAISKIFQFSDETLFYIFYTMPRDVMQEAAAQELTNRNWRFHKELRVWLTPVPGMKPLQRTPQFERGYYMFFDPIHWKRIKKDFLLMYAALEDRAQSAVHS P87242 HDD1_SCHPO BINDING 41; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P53144"; BINDING 69; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P53144"; BINDING 70; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P53144"; BINDING 73; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q7Z4H3"; BINDING 78; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q7Z4H3"; BINDING 79; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q7Z4H3"; BINDING 139; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P53144" CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167, ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474, ChEBI:CHEBI:65317; EC=3.1.3.89; Evidence={ECO:0000250|UniProtKB:P53144}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P53144}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:P53144}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P53144}; Note=Binds 2 divalent metal cations (By similarity). Shows activity with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (By similarity). {ECO:0000250|UniProtKB:P53144, ECO:0000250|UniProtKB:Q7Z4H3}; SPCC4G3.17; CHAIN 1..198; /note="5'-deoxynucleotidase hdd1"; /id="PRO_0000311393" MNAAKSLSIVPFLDCLSRLKTTPRTGWLYHGIEKPESIADHMYRMGILTMLCNDPSINKERCLKIAVVHDMAESIVGDITPHENVSKEEKHRMESEAMVSITQQLIPLNLSLQAEEIKELFLEYESASTPEAKFVKDIDKFEMIAQMFEYERKFNGEKDLSQFTWAGKLIQHPLVKGWLNDVLQEREQFWASVRQKKL P87243 RIX1_SCHPO SPCC4G3.18; CHAIN 1..828; /note="Pre-rRNA-processing protein rix1"; /id="PRO_0000343216" MSDLLERGSLPLVKSWLAITFANEEDLPFQVPQIADILVHQKCIERLGTSENALSVRKNWCTSLTKMLQSKDFRIRWSAIILIHCTISQSWDCLVEHGATWAKLLIALLNRPETPKTLEIAMITVSKMFSSTVGRPAVTRELVTPNLPTFVNNCLRIAESGKCLCTVCSCLYQGIISHSPTFRPFVSSIRNICIKILDGEEVVPSSLQKKAAVLYASLYRCVGKGNFEDYWKQSIISILKEYHLTLDFLFQFVIEPQTYPTREENLMFPKLKGHYEETYQKALHRCRTLNLILISFLSTKTDKIVLLPINALKDLIQRVYTVQLSLPVKSVESSVQALLFMVLPHLHTLVNELTLKLFVVIPPAIILSFDSYLDSLNDCLLSESTHTGVLCSSLKLLSKFLDVTHMNVPLSKYENIVTLVLEYLANSSKGLASKSIEFSKNRGHSQKKRKTLSESQAGDTLMSSEESHQLYDSDVMDCCFSFLASILTHSIALPRLLRTKIDLCTLQISLSNPTSTVLISMHNLLLASILSPGDSQAVIVPHAIRIISGPLGLVHPDPLVASHARSSMQTIESLIHPRFPPLQKHLSPSEFENTFESRFEPVSLENQSHISPPQVDSQSEYKESSILAPSNPPFETESITDSTEIEGIKESFASTDTGLQNNSTATSENKRSESELTMSNVLSNEGDRNEEGSEINSSQPSTINHGTDHINIVSENKETTVSLLHGDVEVEETTNVALNNSQDTETKFTAIDVDFVDRPTSVVSSQIENINGDENGNTTSSVVETFEKTTDVVDEKTTSINVEGNGEDDEEEDNISLPSINLESDSDS P87294 TCP4_SCHPO MOD_RES 96; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 98; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16A10.02; CHAIN 1..136; /note="Putative RNA polymerase II transcriptional coactivator"; /id="PRO_0000215950" MAGKRVIASGDKASSKKPKTEKQSDHELHWALNETEKKRITLSEFRGTRYVHIREYYEKDGDMLPGKKGIALNINEWKKLKQLIHEVDDSLGLVDSGSDSEDEIKEKAENNASLKNDEDDLNTKTENKTDDSSVEN P87295 PEP5L_SCHPO SPAC16A10.03c; CHAIN 1..847; /note="Pep5-like zinc finger protein C16A10.03c"; /id="PRO_0000055994" MNINEWEKFSLFQWQECPSIKILHDSVGNKISCIGKSTKRIAIGTLDGRIVILNSRLQLIRDFYACEQGIVQQIYITADQSALCCVVLDKQNFVYLQFWSLNPSKKTNSNSPLCLYEHRLYGIPNPPFPATSLYVSIDIKTVVCGFANGLVIRVEGDFVRDLGSRQDIILREKDSITNLILYSPKKLFVSTTTQVMVYKIKNNTKKVISNHGIPLFCSIQYQGKYIMCAGGSFLSVYTTPDMQLQNTYCVDGTFELLFSSFGLVFVVYTRKNGENGLENNSSIREIKALDVEKRYVLYESLLEQSYDNIFFNSFDCIFFSSTKVPCQLIRLPSDFVLCKMKGKKEHKDAFKIANYLGSPEDTIRECALAAAGECRQQLNFQDATYYYIEAIPFSDSAEIIKFYLEKKLIKELTSYLEALSAKGFAFSHEISTLIYLYIKLRKLDKLTEYVSGCPTEISLPILRKYKCLDQMELLGTIRKLPNVCMEVYQEKGDVEKAFNHLQVCNLPELLRTSNSFGIWLFNSDPMRFMKEAIRNIEILNSQGKDKELSNILKIVYLGIFSQNVQIQLIFLDELLKSKKSENVLKFIYTRKLYALMQKELQHSNPQNELDALQIIHDSQGLLDYESSILCLQAVSWKQVTDLLYSHLSLKEGQDDSLIQQIISDPETVKTLSETYSSEDALHVLKFFVRERSITNKYEDILYKILEACFMQFRIPIQHVLNILVKDGTLNFCFLKPLLLKWMNDYETRIHQNDDEIQVIKNDIEKKRQLLGTIQDSEKVCDNCEGLLDVPFVSYSCLHLVHRDCATETVCPKCKAGYLDKKNSHDQKKTSTFSELFHDFESIDSVML P87303 TFB2_SCHPO SPBC13G1.13; CHAIN 1..447; /note="General transcription and DNA repair factor IIH subunit tfb2"; /id="PRO_0000119266" MQAEFKSSINDFLEQLPNHARLYQKPAACLAVFRLLPILARQYVMSMLFNPMPVALSDFDLWIKLSSKVYQSESFNKLVRMHIFQFDGQYITLNSEFRKQFITALTGGGNHNSFGVPCTDEDKHLVTVDFLDAYAKETWETILHFMVGTPEAKFPGEGVLSLLKRGGLMSGPKNQLRITRAGFQFLLQDINAQIWTLLLDYLKLSEDTHMDPVQVLHFLFMLGSLDLGRAYSVDFLTDTQQIMLEDLREYGLVYQRKITSKRFYPTRLATGLTTDYRSLHGKQSENDDDKGFIIVETNYRLYAYTSSPLQIAIIGLFANLRARFSNLVVGVITRDSIRRALMNGIAAEQIITYLTTHAHPQMRSNVPLLPPTLVDQIYLWELEKNRLRATPGILFRDFLTDSGFDQAVEYAKELGVLVWDSSLKRMFFITTTGAQPMIAYLKRRAVK P87305 CHAC_SCHPO ACT_SITE 105; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:O75223" BINDING 12..17; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:O75223" CATALYTIC ACTIVITY: Reaction=glutathione = 5-oxo-L-proline + L-cysteinylglycine; Xref=Rhea:RHEA:47724, ChEBI:CHEBI:57925, ChEBI:CHEBI:58402, ChEBI:CHEBI:61694; EC=4.3.2.7; Evidence={ECO:0000250|UniProtKB:P32656}; SPBC31F10.03; CHAIN 1..203; /note="Glutathione-specific gamma-glutamylcyclotransferase"; /id="PRO_0000339309" MKTLSPEGSLWVFGYGSLIWHPPPHYDYSIPCFIKGYVRRFWMRSEDHRGTVNSPGLVLTLIPYEEWKQFSDWSFTPFDEGCWGMAFRIPAKYATQVREYLDDREVNGYTAHSVPVYAHTGDEIPVLENCLVYVGTSKSPQFQPSDDLTQMAKIISTRRGKSGDNFVYLFELAKCLRHLSPESKDIHVFELEAEVRKQMQKTR P87308 LSB5_SCHPO SPBC31F10.07; CHAIN 1..304; /note="Protein lsb5"; /id="PRO_0000315965" MGIFSETVPITAVTTYIDRLTSRDTDDEDLSGIVQLSEAVNLTVTGPREASRTLRKKLKYSTPHEQVRALVILQALIENAGSHFLQNFSDEKLEDRMLQCATNSEYSKPVRKRAIHMIKLWHNDYSNVRGMESMSSLVSRLPQRQSSASHSEQPTINLKKVGPILERLIASSSMAATNLSNSLVRINPNTENPAKNKQIMVYYVDCKRAHRSLLRYIQAIQDEMWLANLLKANDEIVTAIDAFKEKCSENSDYSSDSGSYSSSYSRHLDDRASYISRSSSGGSNAQRSEDLDVNNPFGDHNRLE P87309 MDE2_SCHPO SPBC31F10.08; CHAIN 1..278; /note="Mei4-dependent protein 2"; /id="PRO_0000096322" MENYTKSTTMCGKRKPTFEIYRESDFSKITNQGTVTAFDIISNKETFSESKQLKKAKSRNVTLVDKNTKADKRYKSEKLSDYLLNQEHHKNSPKIINDVLVIGKSDGLINSFPLSQNYISSSESQTSSGNVDIIGNDNSHASPYLPKFELKSQSQSNHSNVVKNQPIKLCKKTEGGTNLDHNKSINGAVKSGTSKSANKDRIYVFYEDEEVMEYRYIFGSRMQTKNHDINANNKRKIFYQNSFSNFHLLHKIIQPNYEPASAEERKLCIEILDEVLQY P87311 MUB1_SCHPO BINDING 498; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 501; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 519; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"; BINDING 523; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" SPBC31F10.10c; CHAIN 1..574; /note="MYND-type zinc finger protein C31F10.10c"; /id="PRO_0000218324" MRESNVSIVWNNKASVTINTVLYDRRALDCDSEMSLMNSLSHLVYLTSTSPKIREILTMDGGLMRLMNILRAGRGQTFARMTIWQLALQCVVNVGIRGSEAIRIRVVEAGIVPIVVTLLDDFLFALESVVSHHSRFQFSLTPSTTPPPSSASAPFPINSNISNSLDSVSQHNSSADSLFVNGDVPSPFGASTASSSSRRVYSVDLRDSGDVQLPNQSTFRHSVNRDLLGSSSTTSHDRSSGSIYSNDSFQDPRVQANSPLTIQRISSAAPSTPTSTENVNYNMTTPSSPSYSRQTGPASETINDEIDSPNFFFPTPLNIMTTTQDSSRDVQLSLNNVQSQALNNRQRRNQLLPGVPSTSALLDGRRPENVVDYHGIASFFDNFDKKINKLPREEDILFGLQILAYTSKNYFHMRPYFESSKDVPSLRMSPLRSGSKTWNIFQLVEQFTLKFYPPQVQYWARAIMNNYCRKDESHGGIRRCANLLCNKWEEHSRQFAKCRRCRRTKYCSKECQHQAWPGHSRWCRVIHKDGRNSKRESSKINSVTESESTASPAASVIPVGTESVTSSTQSDSRL P87317 YB2G_SCHPO SPBC31F10.16; CHAIN 1..649; /note="Uncharacterized protein C31F10.16"; /id="PRO_0000116495" MSDSFFKDIPEFLETRVNESLDARSKSIAQFKELGPPDQVNTIKVNAKNPSKEVGTYHFVSGVDASSSASLAAYLNTLSYSLDKSQQWFGKGNAWRVSHGVYCCYNVFSQVDVRVEAKIPGGVDTYAIDENGQKHIVDARMWTEAYMSEVLRSLLYSDDTNSRFAGHRRFNPIPNPDAELRFFEAAEQLFTLGYTLGSSSEVRVPTHVNNHLVRGIFAYLKQTCRYSAALNLFEKLRVSIPEVSVLLAELYLLMDHEVHAVRILHDSLLKQRMSASLLIVQVKFLISKERYDLALICAKRAVHASPSEFATWACLADVYLHLEDFKSALLALNSCPMYTYYERDAYPLPPSARAHLPFPVNFPKEELEVENNAQNGYTVSTEITDPYLARLPSPSLRGTFAKAYEMLTLICAKIGWDELLRVRSAVFVMEEEYRSLNDITEGNASPDQNEVAEESVAEEVVGLDKPETSVGSLPKNATVQSKRLCERWLDNLFMVLYEDLRVFTIWRAEYTHFKSQGLAYRKAPAEWEILGEVAFRLHHRVEAVEAFCACLESMFSFKAWKTLLIIYSEDNNIELVLTAIAKLTLYNYRWYQEYSPFLLEQMKNRIMQDGALKMKSILASTRLDPYILNLIHKLYFEWAIAFQIPGHEL P87319 VP13A_SCHPO SPBC21C3.01c; CHAIN 1..3071; /note="Intermembrane lipid transfer protein vps1301"; /id="PRO_0000116877" MLEGLVAGLLNKILGSYVDNLDTKQLNIGVWGGHVSLHNLRIKPEALDKLGIPIEITSGLIGTFTLEIPWSNLRNKSLTINIEDIYLSIHPQAKNSLTRDELEQSQQALKQEQLDSFEILRKNFRETLEESSSNPNISRKQSFIEYLIAKLTDNIQIYIERIHLRFEDNLSDLEKPYSLGLTLYSLRVTSTDASFTEYLLSTDPIPSSCIHKIITVDYFSIYWISKCEISKCTTTEDIFSYLKNLIPSAEKSPAYNYILKPLRATAHVVLFRHPTDQIMQLRGKLSVEEISITLSDHMYYSLLGVIDYFRVVMKQQYYLQYRPKSTPKEKPLEWFKYAILVVKDSVHESRYHWTWKYFKRRRDDRIAYMHIIRKRYLNEQISKEEIDLQKKIEKRNSTYDLIKYRSRVHTSLIEERNSIYLKPKTSAAHGLYDWFSGYIRKPQSQDEDTLASTDKTAADLTDQEQKEFFSAIEWSGQLYPDTVNLDPDMCMANVEVSIAKGSFVIQSHINGRVIPLIKQRFESFATECFIRPQSLKLKVSLKDLDMFDGITNPELEPARVIFAKPSVEESESLQKIPEAYRTHLFFLLLDTKPVYKASSTLIVHLRTLVIIYNRVCIESLLAFFVPPRTKIEHVSEWGYSAAAKVMTLARQTRASLDYALEMHKTSDMTIDLQAPLIVVREECTDLKSPTLFLDVGRALVHTQLVDDAIIDKFRKLQSKKINNEQLKQLENLMYDKFTISLFNVRCLIGPDYETGWRCLPKGCDYHILKECSLDINFEISILQKATNLTKFKVSSHMKHAEIMFSDVQYKVFINMMSNILPTLPVAEIPFTYQQFLDAVKPPPFFDAPDNFQITHTSLGSHANENTAAQFMAQQIFAFYFKVDYAICSLYRRSENYLIPVVRAFTEFYIDLVVRKFDYLVTSKLNDLVIKEFTYPSSLCDNVLVRSSPSPKNNFDDTVFISYTSIDYDSPELDSVYEGVRTTIAVVLSDLILNVEPTGFSFVYDFIRATFTSLNDEYMIGEDPELTRKISPVEGIIPEDANVRFDNVDIFLYDCDQHFSTVCLYSANMHMEFREKFFLQARFYDLEVKNHMKSNNPPKTIVKIDDNDLFIFKYESYDIPKDISKPTCDCVYDISFGSLTFYFQKSYFNAIYDFLLKLKRFQELFSSIRYAIYYKLYGNKVSLTYPKFELRIKHPKVYFDDVLDEERNCRMQLIVKPQSFYAFSKCPIVEKNSKKSIFSCEITKVEFHTAVPSSSHHDVLMEENNVHLDLTYDANYTTGAYVFKATGDLDPVILNMCQSHHVIFWDLIDVATTFARVDSSFYTSENLRRELDKAFDRSGTAAKLKHPKKTVVETLDILTTFNLPEIRLNVHTDDFWIHGGDLTQLHSILSFFGFSLDYNFYSSGRCYAEFSIDSIQLKDCNPQDNVVFLDVLEYSENHNRLVNGCLEYDSQNPRYNLVLDIDSPKIFVNLNYLYSIWSIFVHWHRAYYSHLDYLTEVEYFIMGNPNQNACGEESYWYYRITFVDMTLLFFRNVSDANLYSLPMFFGELLITQQSIFAVTANNMKINACPLSETANISNQLADPFGFRYTYSQHTVNKIQIITNITLDFDSFVLRTTVNDFLFLQTILRKIYNFYYALYDVPTTDVELLKRTKDDQLATNPDFLQLSVDTGQPSSVFGIRICKEEFLLTVDGIRLLVISQLHDLPLLNINIKPFQVDLNDWSSELNSNAHLELFMNFYNFSNSHWEPFLEPWKVGVHISRNPNTSKTAVHVFSREKLDLVITPQLIETLHFGFTKVISTPFPIEFKCDAPYRIHNYTGHAVSVWADFENAADSCVRHLENNEETDWKFEEWRQMQDVVKQDQDRSYIGFHFENSKWESLRHVRVNRVGEHIYPLISYDQDELKHYMVVDVNLGEDYIKHITLRSPLLLINETQMEIDVVFCDSDGIQRSQIYHMSPEESCSLPIETAYYYSIHIRPVSEFKFNWTSEAISWKDLVDNKQSLVTCQHSDNTFSTPACRFAANAELKSQTISNHYPFMHITISALLEVKNLLPIDLNIRIIDKDQEGVWMSNVGIGECAYVHSINISHVLLLQAESSESHYLPSSLATIITNDSAQERDEYMTITLQGGRKTRLGLSYTEKYPGIYHIEIFSPYIIINKSGSFLFVGPKNDYNRISFSSASLSSGEDGKVVPCMFSYSHNYGSRRCRLRADNSNWSEPVSFDAIGSVFEVELPSKEDHNKVYRLGIFVETGPDGYSKTNIVTITSRFIVRNKTRWSLVIAEPYNDFIAEIAPEGEEFLTYLRKHSHPMLKLSSSDCYLWSSSFYIEEIGSTHVRLMTSEGEKLLRLEIVIKNATIFISIFEETGDWPYYIKNESGVLLKFWQVNPIDASEGKNNTALLKYHDIPPHSEVKYSWDYPCCANKEIALCYGDQKCLTTLAEIGPLSPFKFTDASNNTKFISRDIVANGLSKILILKDYDPSKAVRKPKIYSKVSTEERDFNLEQFDSGIDLSVKFLLEGIGISLVERNTQELAYLTFHGINLFFTDSHLIRTFKLDVRWIQIDNQLYGGIYPIILYPSILSQEDTMNDNSLLPTFHSMVAVVKNDTYGVTYVKYATILLQELTIEIDEDFAFAALEYIKDSVPRSKRNTGKMFDDSLELVPENLGNDLKVYFEVLNLQPTEMHLSFVRTERINNTDGTVVSSHNPFVFFVNVLSMAIGNINDAPVRLNALLMDNAHVSLRRLFELVKNHYSQELLSQVHKIVGSADFLGNPVGLFTTITSGFADIFYEPFHGFILNEGSYELGIGFAKGTASFIKKAVFGITDSISKVTGTISRSLSVITLDPKFQSRRRAARIRNRPVHILYGVTAGAASLYTGVRSGVRGLALQPIIGARRNGLPGLVKGLGKGLVGFTTKPLVGLFDFASSISEGARNTTTVFDERHIEKLRLSRLMSDDGVVYPFQLREALGQYWLKHLDNGRYFKDFYKAHIIIENKVLVILTNNRILFVQPQQLNCKKEIHLSKVKTVKLQSKEHIFLQLLKGVNFEFSVPENSVRTFFYRKIRDELAAYKHKVNYELEVAL Q03319 PRH1_SCHPO BINDING 119..126; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC2G11.11c; CHAIN 1..719; /note="Probable ATP-dependent RNA helicase prh1"; /id="PRO_0000055155" MVKVSGKLRNGGSITKQNLTDGLVGGQRIKAPNKKKNRKASKNTTKKSTVSVVNFLEQDTDFGANEVVGSDNSSPEKRSENSPSKRKDILEQRKNLPIWEAHDTLCQQIQDNRVIVVVGETGSGKSTQIPQFLNECPYAQEGCVAITQPRRVAAVNLAKRVAAEQGCRLGEQVGYSIRFDDTTSKKTRIKYLTDGMLLRELINDPILSQYHTLILDEAHERTLMTDMLLGFVKKIIKKRPALRVIIMSATLNAERFSEFFDGAEICYISGRQYPVQIHYTYTPEPDYLDACLRTIFQLHTKLPPGDILVFLTGQDEIEALEALIKSYSKQLPSNLPQIQACPLFASLPQEQQLQVFLPALANHRKVVLSTNIAETSVTISGIRYVIDTGLAKIKQFNSKLGLESLTVQPISQSAAMQRSGRAGREAAGQCYRIYTEADFDKLPKETIPEIKRIDLSQAVLTLKARGQNDVINFHYMDPPSKEGLLRALEHLYSIGALDDNGHINDLGYQMSLIPLLPSLARAVLAAREHNCLSEVIDVVSCLSTDSMFLFPQEKRDEAIEARLKFLHSEGDLLTCLNALRQYLESSHDSRKQWCSQNFINRRALKTILDIRKQLREHCLKDGWELNSSPEVNSENLLLSFLSGYITNTALLHPDGSYRTIIGNQTISIHPSSSLFGKKVEAIMYHELVFTTKSYVRGVSSIRSNWLNAVAPHYLARRST Q06975 GAR1_SCHPO SPBC20F10.01; CHAIN 1..194; /note="H/ACA ribonucleoprotein complex subunit gar1"; /id="PRO_0000208565" MSFRGGRGGGFRGGRGGSRPFTPSGPPDQVIELGLFMHDCEGEMVCQSTNVKIPYFNAPIYLENKSQIGKIDEVFGPMNQVYFTVKPSEGIVSSSFKVGDKVYLSGDKLIPLDRFLPKPKTVGPKKPKGARNGPAGRGGRGGFRGGRGGSRGGFGGNSRGGFGGGSRGGFGGGSRGGSRGGFRGGSRGGFRGRF Q09094 REC15_SCHPO SPBC1711.14; CHAIN 1..180; /note="Meiotic recombination protein rec15"; /id="PRO_0000097222" MSYSVSAAQLWSRKLAMQAEDMQQHQKSQSNQIASCLAEMNTKQEVVNQTIGQLGRSISEVQQQNSQLVLQSLNQINMSMQQVALGIQDYASRINKLEQTMSDMNLKFEALQKEQNSNTKTLADCTSQMTIITKKLDAELKKRYMTTKQTRTVQNQTMPRSNTTTKKRVLAIDFLADDDY Q09100 RNP24_SCHPO SPAC3G6.04; CHAIN 1..369; /note="RNA-binding protein rnp24"; /id="PRO_0000081808" MEPIQKMDSLNNKEGQPDKKRKKHESEKEGENEVLEIDVTKPVPPSKKLMRKLRKAGKIDKDGNWTPEALEEAKKKEEKRLKRLDAKYGRKEEGESQEESKRSPWGIWVGNLSFHTTKEILTDFFVRETSEMIKEVSEENIKPITTEQITRIHMPMSKEKRFQNKGFAYVDFATEDALKLALQCSEKALNGRNILIKSNTDFSGRPSKPANTLSKTASIQSSKKEPSSILFVGNLDFETTDADLKEHFGQVGQIRRVRLMTFEDTGKCKGFGFVDFPDIDTCMKAMELGHNSWRLEYGEDRSKRMRNKSPMARSGRFNDAESLGQEDKPNFKRARKIDPRSVRPGAALAKAQRSSAAIVEPAGQKIKFD Q09127 RL10A_SCHPO SPBC18E5.04; CHAIN 1..221; /note="Large ribosomal subunit protein uL16A"; /id="PRO_0000147127" MARRPARCYRYCKNKPYPKSRYNRAVPDSKIRIFDLGRKRAGVDEFPLCIHLVSNEYEQITSEALEAARICANKYLVKIGGKDSFHLRVRAHPFHVVRINKMLSCAGADRLQTGMRHAFGKPNGLVARVNIGQILMSVRTKDSSRATAIEALRRCQYKFPGQQRIIVSKKWGFSQYARDEYIEKRSRGEIIPDGCYAKFLNKRGSLQEKLDLFPEASFNLA Q09146 HBA1_SCHPO PTM: Phosphorylated. {ECO:0000269|PubMed:8621569}. SPBC365.13c; CHAIN 1..399; /note="Brefeldin A resistance protein"; /id="PRO_0000213673" MTSKMENNKDESISTKNALEEKSNETKDETSKRKHDPAEEESAVSTKVSKSEPLEDKGNAEVKEFKETTKSNGVKPEVEITESTKIQKESNTEPCISTGGKVEEKELKVNKDVDENEGHVAVETGKKESAAKPAASVSPFSQFASFSNASSPFSNVSTASSEPKEEKSAFGAFASSKSAFTMKSVKDSPFKKFAAGTAVETESGSGKEKENDKKSSENFDELLANTSAKAFENQKGSAGETKSEPKEADKGSGDSTKSTMHQLSDSEIITGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLQIASASSGGSANYLKIFVIENGKSVLYAVRVKDNSLAEQLRNHVLEAIPKGGREDA Q09150 REC14_SCHPO SPBC32F12.02; CHAIN 1..302; /note="Meiotic recombination protein rec14"; /id="PRO_0000051198" MRKEYLVSHIEENAHQADIYSLNVVAGNLWSASGDSKIKKWSIGDAEHSLVEEIDTPHKLGVHHLATSLDENVVVSCGFGQDVYVWNPETNEFRDLGNNAQHPSECWSSCISPDGQTIAFTSVDGRIAVWDNPSDCKISELDTKGKFGLCIDYSPNGRFIVSGHQTGQLFLISTETGRLFHVLSGHTSPVRSVAFSPGSTLLAAAGDSKMITIYDVLSGDQVGQLRGHAAWIFAVAFNPVGDLLLSADVEGKIKIWDIDTMECISTQSETDGAIWAVAWYKNGFIVAGADKSIRWYRAAATE Q09184 CDB4_SCHPO MOD_RES 8; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 362; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23H4.09; CHAIN 1..381; /note="Curved DNA-binding protein"; /id="PRO_0000148991" MSTKEATSETAVDYSLSNPETVNKYKIAGEVSQNVIKKVVELCQPGAKIYDICVRGDELLNEAIKKVYRTKDAYKGIAFPTAVSPNDMAAHLSPLKSDPEANLALKSGDVVKILLGAHIDGFASLVATTTVVSEEPVTGPAADVIAAASAALKAAQRTIKPGNTNWQVTDIVDKIATSYGCKPVAGMLSHQQEREVIDGKKQVILNPSDSQRSEMDTFTFEEGEVYGVDILVSTSPSGKVKRSDIATRIYKKTDTTYMLKLQASRKVYSEIQTKFGPFPFSTRNISFDSRTNMGLNECTSHKLLFPYEVLLDKDGGIVAEFYSTIALTKKGTIILSDSEPKEDFIKSDKKVEDPEIVALLETPIKVTKNKKKSKKPSKANE Q09190 CDD_SCHPO ACT_SITE 59; /note="Proton donor"; /evidence="ECO:0000250" BINDING 46..48; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 57; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 89; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 92; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+); Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; SPAC1556.04c; CHAIN 1..133; /note="Putative cytidine deaminase"; /id="PRO_0000171684" MEKEDIEKLFQEVKKSLQYSYCPYSNFAVGACVVSDDKNTYIYGANVENASYGNCICAERVAITKAVSMGYTKFMAIGVMSAKGRVTPCGICRQVIREFSKDINVYMFHDDGGYDMKTIEELLPDSFGPDDLK Q09668 RL22_SCHPO MOD_RES 49; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 50; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC11E3.15; STRAND 10..15; /evidence="ECO:0007829|PDB:8ETC"; STRAND 51..53; /evidence="ECO:0007829|PDB:8ETC"; STRAND 60..67; /evidence="ECO:0007829|PDB:8ETC"; STRAND 91..97; /evidence="ECO:0007829|PDB:8ETC"; STRAND 100..105; /evidence="ECO:0007829|PDB:8ETC" HELIX 17..22; /evidence="ECO:0007829|PDB:8ETC"; HELIX 27..37; /evidence="ECO:0007829|PDB:8ETC"; HELIX 71..85; /evidence="ECO:0007829|PDB:8ETC" TURN 45..50; /evidence="ECO:0007829|PDB:8ETC"; TURN 88..90; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..117; /note="Large ribosomal subunit protein eL22"; /id="PRO_0000215513" MVKKNTKVSNKYIIDATAAVNDKIFDVAAFEKYLIDRIKVDGKTGNLGSSVVVSREGSSKIAVIAHIDFSGRYLKYLTKKFLKKHSLRDWLRVVSTKKGVYELRYYNVVVGNDEEEQ Q09670 OYEA_SCHPO BINDING 28; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 189; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 189; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 192; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 242; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 334; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 361; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; SPAC5H10.04; CHAIN 1..382; /note="Putative NADPH dehydrogenase C5H10.04"; /id="PRO_0000194477" MNDRGELFKPIKVGNMLLQHRIVHAPMTRLRATDYGKITGLMVEYYSQRSMIPGTLLIADATFVGEKSGGFPNNPRCFTKEQAESWIPLVEAVHKNKSFLFIQFWPLPGDLKDEYRNDLEKMQKITYSDCPQDPGGLPAGIHSFDAVQGVEVYKKKYMSKRDIQEHIQDFVNAADLAVNIAKADGVEIHQVNGFLLDRFVLGGFGDQCDPEYRGSIENRCRFPLEVLEAVTRKIGQERVGYRISPFSGWMQKIDFMEVNIYLMSEIAKRFPKLAYIHAIEPRKYWSGHKLVSSEQNTSFLQKYWKGPFITAGGYDPETAVQAANERGVLVAFGRNFIANPDLVFRIKHHIPLNKWDRSSFYLPKTEKGYTDYPFSKEFLQSK Q09671 OYEB_SCHPO BINDING 34; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 196; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 196; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 199; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 249; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 341; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 368; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; SPAC5H10.10; CHAIN 1..392; /note="Putative NADPH dehydrogenase C5H10.10"; /id="PRO_0000194478" MAVQKLYESQSKLFQPIKVGNMQLQHRMVHAPATRLRCLDNGLVMTDLVKEYYKQRSSIPGTLLITESLFSGAKSGGFSNIPCLYNDEHVEAWKPIVQAIHDNDCFVFIQFWNLPGELKVDYLEDQERLEKVTQGECPMDPTGLPAALGSAYSICGEELYVDKFMTKQDIQEHITTYTEAAKRAVFGCGADGVEVHQVNGFLLDKFVLNGYGDKCDPEYCGSLENRARFCLELLESVVNAIGQERVGYRISPFSDIWKDKDSFEAHVFMIKKIKERFPNLAYLHAIEPRQYWNGHVHITQEKNTLIYKNLWGDPFITAGGHDRDSAIQMAEQENTLVAFGRYFLSNPDLPFRLKYNLPLNKWDRATFYTKMSPKGYIDYPFSKEFLDTKKVE Q09673 PANC_SCHPO CATALYTIC ACTIVITY: Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; SPAC5H10.08c; CHAIN 1..283; /note="Pantoate--beta-alanine ligase"; /id="PRO_0000128297" MQVLKEKLLIHQQVDNWRKDGNRIAFVPTMGNLHEGHFSLVREAKRHAEKVVVSIFVNPMQFNNPQDLLLYPRTMDQDCSQLQNLGVDLVYAPTVEELYPEGSQDITFVDVPKLSTMLEGASRPGHFRGVTTVVSKLFHIVNPDVACFGEKDFQQVAIIKKMVRDLNFFIEIIQVPIVRADDGLALSSRNGYLTSEERKIAPNLYKILKKLAQELSNGNGDLEKLIAETNTELSRCRFIPDQLEICDSTTLEPFTAGTKNVVILAAAWLGKARLIDNIQTTIN Q09679 GMH1_SCHPO SPAC5H10.11; CHAIN 1..329; /note="Probable alpha-1,2-galactosyltransferase gmh1"; /id="PRO_0000215166" CARBOHYD 127; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 169; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLSFFTKNTLTKRKLIMLALAIVFTFFAFGLYFIPHDEISVFDFKLPALQYETTVTSLDNFLIGGSTTLYTATVNHEDLNEPKSHEIVMLLASDGNVGSFESNLLDDCFKNRIEYAKLQNYNFEFVNVSSLVVPPVWGKMPAILQTMRKYPSAKWIWWLDQDALIMNKNLSLQELFLSPAMLQKSLLREQPIINSFGEDNFRITPAAYSKEMIEQIQFLISQDHNGLNAGSFLVRNSRSIALLMDLLTDPSLADAGVVRHEQDLIGYFIQKHSQVASMVGILPQRFINAFHEGPPTMQWQEGDLALHFAGCWVENKCAELWTKYKDKII Q09689 IF5_SCHPO BINDING 28..35; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" SPAC2F7.05c; CHAIN 1..395; /note="Probable eukaryotic translation initiation factor 5"; /id="PRO_0000212526" MATINIRRDVKDSFYRYRMPKLQSKIEGKGNGIKTVIPNMSDIAKALGRPPLYVTKFFGFELGAQTTIIADMDRYIVNGAHDAGKLQDLLDVFIRRFVLCASCQNPETELSINKKDQTISYDCKACGYRGVIDGRHKLTGVIVKNPPAKKKSHKHKRDSPVAEEEDGAEDELTRRIRQEAAELPTAEVVNDEDWAVDTSEEAVRARVQELEGNMKDSLTLSDLRGDEEEAESSRYDQFGEWLEDNYPGVSDVEIYKKMKEENIHHKSKAIVVLVQCIITSPYVGEFEKHGALFKKLCTTDKHERALLGGFERLMENTELVHIDVVPKVLLEIYQNDLVSDDMFEKWGAKASKKYVSRETSKKIHEAAEPFLTWLAEASDESESEDEEEEEEDDDE Q09691 RF1M_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: Methylation of glutamine in the GGQ triplet is conserved from bacteria to mammals. {ECO:0000250}. MOD_RES 270; /note="N5-methylglutamine"; /evidence="ECO:0000250" SPAC2F7.17; CHAIN ?..396; /note="Putative peptide chain release factor 1, mitochondrial"; /id="PRO_0000030338" MLLTKKVLWYFRHGIEYQIRSIACKKGYSEHNVSRVLIEKARSLSSEYLQFHQVNNKDQSAMTNDTDLAKRIARLRRVHNAYSKFKSLSEQISDLKQMEAQESDAEVKMMAVTEINEISNKIPKSIEDLENTLLPQADSYALPALIEIRPGVGGTEAAIFANELVEMYFQYANFKGWNCKFISKSAVQGLEAITEAIFSIEGEGAYGHLMLEGGVHRVQRTPATETKGRVHTSTASVIVLPQVSNDESSSLYDSSEVKIEVMRSRGAGGQHVNRTESAVRLTHIPTGITVSMQDSRSQHQNKEKAFLVLNSRLAALNAAKENEAERLKRKNQVTSSDRSEKLRTYNFNQNRVTDHRIGLSMHDLSTFMQGEEKFDEFLEKIRIWNREQLLLHSEIV Q09692 SYWC_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; MOD_RES 288; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 290; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F7.13c; CHAIN 1..395; /note="Tryptophan--tRNA ligase, cytoplasmic"; /id="PRO_0000136743" MSVEEQIVTPWDVKGSIVDGEEKGIDYERLIVQFGTRKITPEQLERFEKLTGKKPHLLLRRGAFFSHRDFDMILDRYEQKKPFYLYTGRGPSSDSMHLGHMIPFMFCKWLQDVFQVPLVIQLTDDEKFLFKQGVSLEDCQRFARENAKDIIAVGFDPKKTFIFMNSTYVGGAFYQNVVRIAKCITANQSKACFGFTDSDSIGKIHFASIQAAPSFSSSFPHIFNGAKDIPCLIPCAIDQDPYFRLTRDVSGRLKFKKPALLHSRFFPALQGPQSKMSASKDSSAIFMTDTPNKIKNKINRHAFSGGGATIEIHREKGGNPDVDVAYQYLSFFLDDDEKLKQLYNTYKAGTLSTGEMKGECIKLLQQFVSDFQAARSKVDEATLDMFMDGSRKLEW Q09696 MED1_SCHPO SPAC2F7.04; CHAIN 1..454; /note="Mediator of RNA polymerase II transcription subunit 1"; /id="PRO_0000096371" MDRPHLFSEVHFRRNASNPNQINWTRYWIDCLSSVPWNDISVTGFEYLAKKYGLEVFQDSSKPNEVVLSLAGKIILIDITVPINASPKDINVVLAFANASGEQYNNPVAEKLLKDAIYNCNTPLFEKNVKWLATFDHSSPSVQQSCFQYLDSLSSSLNAIYEAELSLLAQEENVIMHGNGKPLSNYEGQLGLRIVYWKLLDKTYSTQIFMDNLSHESLPHLLFGYNLLNSPPILQSSKINWALENTLTPIPTTMELVFDDINLIIPEQGVKPLLDLLHVHDITIPWPVQNYSHMLGLPSKSTVNYKFINKNQAIQLTGFDVSARSLRHVPFHHPKQIRGILAIVRQYLLLQLILENIKSADLAETAASSSLHLSLYFKEHPIVHAQYQEINKLNNSEQIIIVLSVLSDGRLNVDYMSSGGKELSKQQSHVFQKLIQQTCNIGLAIEVFIKKVVN Q09698 YA27_SCHPO SPAC2F7.07c; CHAIN 1..607; /note="Uncharacterized protein C2F7.07c"; /id="PRO_0000116383" MDAKPWNHTSEAFQASILEDLKIIQKAGAERNAKSSHGSINSRSASPNKATSRRNRAQNGNSNGRASVDNSDDGSKDDLDYSPSVKRKHVNGEGAEKGDHDTSNNGPSITKLRRKVRRTYDTKDGFVAWNTLDDDFRPIVPDQERSRKINPQKGNNNNLLKENKSLKTTAKDLSDISSSSMKKANNSSKPLFSGKLTFKANIPVPTSEVVTENNVTRNVTVYSNQKHLGNESENFNDMEGRAEDISSNELLPTPEEYPYRYNNDYCSACHGPGNFLCCETCPNSFHFTCIDPPIEEKNLPDDAWYCNECKHHSLYNELDEQEELESNVKEEGTMVDVWMQLCTYIDSHNPIQFHLPHSISSFFRGVGSGVMGEYIETDVLKHLKSSRRSNGEERDPLLLKSKSGTPILCFRCHKSALVSQSILACDYCNSYWHPDCLNPPLATLPSNLRKWKCPNHSDHVTPRYRLPEKAKVIRVGLPRGFKNKGNIVIDENEDEPSVQTIQLQGKIRVVPSKPFKLNFLEQIRDNVINLRKMVEQDEQLCIETFSKFDFYATRDCELPLRILCDVANDNLENDDYVLALRDLLRISKWDPNQPVPAPFDLANLLSY Q09699 SNF5_SCHPO SPAC2F7.08c; CHAIN 1..632; /note="SWI/SNF chromatin-remodeling complex subunit snf5"; /id="PRO_0000205963" MDKDIGSAVAELQVCSTHYAMTIVSCGFHSPQSLMNADLQHCLLADQNYLLNNSNKNKGSIIEENTRKPFQSARNLQTSLKTHPESAITRYGLGYAGFGNGWTALKPKILFPSQKRRVKGRFTFPFSRRSNLAQSKLPVDLVPIRLEIDADRYKLRDSFTWNLYDKCISLDQFAEQICIDYDIPLHNVHIVQNISKSIQAQINDYEPRKAQSNLSFVSDVSSSTSETVYAHEPSDSLAKASKQQIPTVQNDLRILIKLDITIGRLNLIDQFEWNLFAPESSAEEFATVMCLDLGLSGEFCTAVAHSIREQCQMYIKYLSLIGYLFDGSEIEDEEVRSYILPPLKNTLRFSDMESSSFAPMIYELNDAEMERQDRGYDREARRMRRRQGRAKHGIMLPDLRDIPKIHRSLFPSSSVPSDDDFMHALSLSTNSDGETLNEINTNNPEREHLIVRLKVDSQKLKIIVEQSQTLTLNNFQQRKLTPLPNSMSFDSLNEFESERNTPSTYGQNISPLPQFSSPSLSSDAFLTNSNSSESALVHMQKLNLPDFTPSWVKRCVIETFAKFPNDRFNVIVKPALNPAERMTVRICCHDCINEYFTAGPGFTFGNFHIHLLSSSHQQKKEVRMNTVLDRNT Q09712 GPI18_SCHPO SPAC18B11.05; CHAIN 1..464; /note="GPI mannosyltransferase 2"; /id="PRO_0000116387" CARBOHYD 108; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 139; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 326; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MYYIGHPSYYRKHIEHVCFQHSGILKKRNYQKNQKKYIMKLNESAMKNAEKKSNSYLAIRMTRSGYNYFKGICVCTFLLSTILYLGIAVIMSHLCVFDDTAMLYLRQNRSRLAESNIFRTLFISWIRWDAIYFVDMAVNGSLFEQEWAFSSLWPKIISFLAFRSKDVVLLGIVSCFASIFFHAIACYALYLLTKSIFSNQKMTAYTVIFYCFSPSGIYMSVGYTESLFAAFSFLGLLLFIKKQQYPAAFLWSLATLIRSNGIFWCIFFGMPAIGTLKISLERLQLTFMQVSQLVGYGTKCLIILVPFFYNQYLGFKLFCPGVAWCNKSLPLIYPAVQEKYWNVGFLRYWTLNNIPNFLFALLSIIPILFALFYSISGSTLHSFRSIKSHLVLSALYLYIGCFHMHTQVLNRMSSALPLLYWSMAHATLYAKSRNLKAFGHCILFVWIVYTVIQAGLYGSFLPPA Q09720 PSB4_SCHPO SPAC31A2.04c; CHAIN 1..194; /note="Probable proteasome subunit beta type-4"; /id="PRO_0000148054" MESLLAVQGQDFVLTASSSSAVRGITVLKPDDDKSQILNSHNLMLYCGEAGDTTNFAEYIAANISLYTLRHNLNLSPEATASFTRKQLATSLRSRKPYQVNILLAGYETNLGKPELFWLDYLATCVRVPYACQGYSSFYCLSIFDRYYKPDLTIDEAVRIMKLCFDELKKRMPIDFKGFICKVVDKDGIREINI Q09723 TR112_SCHPO SPAC31A2.02; CHAIN 1..126; /note="Multifunctional methyltransferase subunit trm112"; /id="PRO_0000215804" MKLLTANFLNCSNKKCTSSPEAFPLDVVDAKLAIQQLELKPEFLIGIMPRIDWNALLKTTRQLGNYSLPDEKPDLVDDSDEVLLKSLHNVLLETEITEGKMVCGNCGHVYPIFEGIPNMLLSESEI Q09724 RM11_SCHPO TRANSIT 1..9; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC31A2.03; CHAIN 10..216; /note="Large ribosomal subunit protein uL10m"; /id="PRO_0000154756" MRCSVAVRASSIYVKNPQLRKSFLHSNYVQLIQESPNFLILQHNNLLPREAKSLRTELKAKVPGSKLQVIRGSIFHHALKVYESIDRLSNGCVDMQKVNLIETHKKAQKIKLDIDNLFVGPLAIFTLGPKLSPEAIRGFMSVLKGYQNKILLLGIRAESKGMDPFEVENLSKIPSLEFLQSSLLSVLSSPASQLRRILDLSKANVAYTLERREPSE Q09726 ATP25_SCHPO TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC31A2.06; CHAIN 29..542; /note="ATPase synthesis protein 25, mitochondrial"; /id="PRO_0000116391" MPTYRFNYLRFNKLCVSFFRSKFDKRPFASQKFPENLVPDNSSNDANSQPEEVSSKKPWYVDEKHNLFPKKAHFDAVALPPIPKGAPNFLADVLNLLKKKYYATDLSFVNSPADSFWCDSDLILLASCNCGSEVVSATNGLLRLLKQKNVGPVNVDGLTSASRRKILERRMRKRSNLSNRQLNTSENNWTCLSIENFGISIHVITKNFREYYKLDNIEHVKDETLYSDLEHGKQSRVSLTSKSTPDNSLPPNFINNHSNVFRRSFHTCNFSLKSAASLYCDTQDILLNVNSQNLTSTLEKYKKMHLQNPNNFSLDFTLSIFERLRKDSSLQLTTKDINTLFSTIALSPTKLSMASKHSKNLVSERMLYLSLMYKSLVDLKTIDSFSLKLLFLKFMICSCMVKGESNFFLDNRIFLLERIMNRYGIPMTIDTFLLMQFILAKSNRWSEVWRRWDNLRKAGVVFNERLYNHVYLLAFESKNERVINYVLTNIFEDMVSQSPPIPASKLMATSLKKCVQSLPEKYAHSFPSVRNYIAKMENSMTH Q09729 YA4C_SCHPO MOD_RES 373; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 374; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 452; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 474; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 493; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 497; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 502; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 507; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 514; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31A2.12; CHAIN 1..596; /note="Arrestin domain-containing protein C31A2.12"; /id="PRO_0000116393" MNILSRKENVASYFDIRVAAEHDLIVIQGLADSAEPTPLSGSVVLCLNEAISVKAISLKLVGKCRISWSEPSPTVRGGQRHNKQEYVVYEKNWIFVPYTGANRTLRAGNYEYPFHVMLPGDIAESVEGLQSCYVVYRLKASIDRTGLASKMVKKKHIRLIRALPADAIEYTQTISVDNTWPNKIEYTISVPTKAYAIGSYIPIHFVLVPLLKRLTIGKISITLKEYITLHVAHGYNGLPASKDEVRTVRSLQTEELEEFSDHYELTKNLELPSSLVECLQDCDLDGIKIRHKLKFSVSLRNPDGHISELRAALPVVLMIPPQLFGDRAEVESLRENFESFNQPLPSYQNSMYDRLYDGLSYSNLDTPLPSGATTPRRRDSMEPTYASNEAHRRQLIAGLTELALQQQPQGRSPNEHSPSNHPEDFPPSFSLGSNPSSGAASAVITRNPSETSLADLSRVPSYKEATRSAVPLESPLQSTLPSYEDVARIEHLSRPPSPGIVTPPQRTSPSFFVSPTESTRQSLDSRRSFEHSTSSSSGISPSHSSASLAHLSQASNPNGSSSAPHRPTSARVGSHRNALDALRRARMLPSGFSRRN Q09730 SFT1_SCHPO SPAC31A2.13c; CHAIN 1..91; /note="Protein transport protein sft1"; /id="PRO_0000097711" MNDQNERRLETLSGQVSSLKNVTYDIYSRANDYTRIDRATESFSGLSNSVKKSTENFFRVVRSAGRRRIMTMVLAIVGSILIIYYASKWFF Q09732 DCC1_SCHPO SPAC31A2.15c; CHAIN 1..357; /note="Sister chromatid cohesion protein dcc1"; /id="PRO_0000116394" MEANEERCILLKYPHPSSDISSEYLLLELDDDLLKTLEENPEEEIVFKSDFDKKASVLCTSDKTYAVRQVVQSNSYLLFDELSPTDWVLNDTCYSFLEVERIYGFIFSDDKISYWDEDSVELKPISLTKDQFIRSVPASRNEVDSFLQKNFFMVKNEFLYRLSPSYICSIIDWIFVIAQQLHIDFASFEFKILKKPAMDDEFDWDSVICVLESISSPIKDNVLPKKFNIDLELTTFWYGRFLLEGINSISSDEFIQLWDNRLPYPCKGLPSLNLLKGYYFHDTPNTIQYLSGDQLPREPSRRFQSLFQLKSKWLYEELWSFVKDLALSKSRVEALILKYGRKQTSRDGVYINSRGTW Q09735 YA55_SCHPO ACT_SITE 292; /evidence="ECO:0000255"; ACT_SITE 366; /evidence="ECO:0000255" BINDING 280; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 285; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 285; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 303; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 362; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 364; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 364; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; SPAC13A11.05; CHAIN 1..513; /note="Putative aminopeptidase C13A11.05"; /id="PRO_0000165853" MKGLGLSTRTFNWSSLSSILLPRIPLATTKADSLILAVRHDKQVFSEDYRQVVDQYFETSPKKNDIRLFWNTQGFVRLAIVQLEENVSEKSVRSAAAEAAKILKSNGAKSIAVDGMGFPKDAALGAALATYDFSLRRDHLSVYQDEKVVEKENLFTSPAPERLTFQLLSNTSEKKTATAEENAFKVGLIEAAAQNLARSLMECPANYMTSLQFCHFAQELFQNSSKVKVFVHDEKWIDEQKMNGLLTVNAGSDIPPRFLEVQYIGKEKSKDDGWLGLVGKGVTFDSGGISIKPSQNMKEMRADMGGAAVMLSSIYALEQLSIPVNAVFVTPLTENLPSGSAAKPGDVIFMRNGLSVEIDNTDAEGRLILADAVHYVSSQYKTKAVIEASTLTGAMLVALGNVFTGAFVQGEELWKNLETASHDAGDLFWRMPFHEAYLKQLTSSSNADLCNVSRAGGGCCTAAAFIKCFLAQKDLSFAHLDIAGVMDKQLNSWDCDGMSGRPVRTIIEVARKY Q09737 PDC1_SCHPO BINDING 29; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 118; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 395; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 418..420; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 450; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 451..452; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 477..482; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 477; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 479; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P06169"; BINDING 483; /ligand="pyruvate"; /ligand_id="ChEBI:CHEBI:15361"; /ligand_note="ligand shared between two neighboring subunits"; /evidence="ECO:0000250|UniProtKB:P06169" CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2; Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1; CATALYTIC ACTIVITY: Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06169}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P06169}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|UniProtKB:P06169}; SPAC13A11.06; CHAIN 1..571; /note="Putative pyruvate decarboxylase C13A11.06"; /id="PRO_0000090767" MSGDILVGEYLFKRLEQLGVKSILGVPGDFNLALLDLIEKVGDEKFRWVGNTNELNGAYAADGYARVNGLSAIVTTFGVGELSAINGVAGSYAEHVPVVHIVGMPSTKVQDTGALLHHTLGDGDFRTFMDMFKKVSAYSIMIDNGNDAAEKIDEALSICYKKARPVYIGIPSDAGYFKASSSNLGKRLKLEEDTNDPAVEQEVINHISEMVVNAKKPVILIDACAVRHRVVPEVHELIKLTHFPTYVTPMGKSAIDETSQFFDGVYVGSISDPEVKDRIESTDLLLSIGALKSDFNTGSFSYHLSQKNAVEFHSDHMRIRYALYPNVAMKYILRKLLKVLDASMCHSKAAPTIGYNIKPKHAEGYSSNEITHCWFWPKFSEFLKPRDVLITETGTANFGVLDCRFPKDVTAISQVLWGSIGYSVGAMFGAVLAVHDSKEPDRRTILVVGDGSLQLTITEISTCIRHNLKPIIFIINNDGYTIERLIHGLHASYNEINTKWGYQQIPKFFGAAENHFRTYCVKTPTDVEKLFSDKEFANADVIQVVELVMPMLDAPRVLVEQAKLTSKINKQ Q09740 GFA1_SCHPO ACT_SITE 2; /note="For GATase activity"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; SPBC12C2.11; CHAIN 2..696; /note="Probable glutamine--fructose-6-phosphate aminotransferase [isomerizing]"; /id="PRO_0000135288" MCGIFGYINYLVERDRGYILKTLVKGLKRLEYRGYDSSGCAVDGDEGEDFIMFKEVGNVSKLEASIKGSNVNKSTKFINHCAISHTRWATHGIPSPINCHPQRSDPHSEFIVVHNGILTNYRELRTVLESRGMVFESETDTECVAKLAKFIYDTTPGVDFTSLAKLVFRELEGAYALLIKSSHYPGEVVATRRGSPLIVGVKSEQKLKVDFVDVEFPEPAEGLPGTPKPTSLHPVFSNPATNGMLRGDKPDLLHRAQSRAFVSGEGVPGPIEYFFASDATPIIEYTKRVMFLEDDDIAHVRDGELHVHRLRREGGGSTTRTIETLEMEIASVMKGNYDHYMIKEICEQPDSLLNTMRGRVNFVNRLVTLGGLESYYDIIRKSRRLIFVACGTSYHSCVAVRPLFEELTNIPVVVELASDFVDRCPSVFRDDTFIFVSQSGETADSLLALQYTLENGALAIGVVNCVGSSISRKTHCGVHINAGPEICVASTKAYTSQYVALVLMALYLSRDSVSRLERRNEIIDGLAEIGEKVQETLHLNAAIKQTAIEQLINKDKMLIIGRGYHYATALEGALKVKEISYTHAEGVLAGELKHGVLALVDNDMPIVMLLPDDYNFPKAWNAFEQVRARGGKPIIITDKKLDNLEGFTIIKVPKTVDCLQGILNVIPFQLLSYWLAVKRGHNVDQPRNLAKSVTVE Q09741 SPEE_SCHPO ACT_SITE 168; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 44; /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"; /ligand_id="ChEBI:CHEBI:57443"; /evidence="ECO:0000250"; BINDING 74; /ligand="putrescine"; /ligand_id="ChEBI:CHEBI:326268"; /evidence="ECO:0000250"; BINDING 75; /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"; /ligand_id="ChEBI:CHEBI:57443"; /evidence="ECO:0000250"; BINDING 99; /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"; /ligand_id="ChEBI:CHEBI:57443"; /evidence="ECO:0000250"; BINDING 119; /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"; /ligand_id="ChEBI:CHEBI:57443"; /evidence="ECO:0000250"; BINDING 150..151; /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"; /ligand_id="ChEBI:CHEBI:57443"; /evidence="ECO:0000250"; BINDING 168..171; /ligand="putrescine"; /ligand_id="ChEBI:CHEBI:326268"; /evidence="ECO:0000250"; BINDING 168; /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"; /ligand_id="ChEBI:CHEBI:57443"; /evidence="ECO:0000250"; BINDING 236; /ligand="putrescine"; /ligand_id="ChEBI:CHEBI:326268"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16; SPBC12C2.07c; CHAIN 1..298; /note="Spermidine synthase"; /id="PRO_0000156461" MSVQELSHPLIKDGWFREINNMWPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAYTTIPTYPSGSIGFVVASKDASIDLSKPLRKWSPEEENKLCKYYNSEIHAASFVLPTFARDVVDKATSS Q09755 AROF_SCHPO CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; SPAC24H6.10c; CHAIN 1..368; /note="Putative phospho-2-dehydro-3-deoxyheptonate aldolase"; /id="PRO_0000140852" MDKHTPLLPGDSVFSRCKTEDSRIKGYDPVISPALIQSELAASDETLAFVSDQRRQAADIIAGRDDRLLLIVGPCSLHDPVAAKEYAIRLQKEAIKHKKDLHIIMRAYLEKPRTTVGWKGLINDPDLDGSYNINKGIRVARRIFLELLETGVGIASEMLDTISPQYLADLICWGAIGARTTESQLHRELASGLSFPIGFKNATDGNIGIAIDAMNSSANPHHFLSVTKQGVVAIVTTTGNPDTHIILRGGKSGTNFDADSVAGAKAKLEECNKLPSIMIDCSHGNSSKNHKNQPKVAACIAEQVANGQKAITGVMIESHLNEGKQAIPEDDLSSMKYGVSVTDACIGWDDTTAVFEQLAAAVRSRRSH Q09758 GUP1_SCHPO ACT_SITE 468; /evidence="ECO:0000250|UniProtKB:P53154" SPAC24H6.01c; CHAIN 1..583; /note="Membrane-bound O-acyltransferase gup1"; /id="PRO_0000213141" MLRLFRFDVLETSTKDTERPNSKSSRLSSTSGSSHPSSSSRLTVRSAVPEKSAFGSIEFIFYFSVILSILTIACFKIHYVSSPKHPNYKNIEKYLKPGWLFGQKVDSADFQYSAFRENMPILLLVIIVYNFLWRLVKLVFTKNTNDELAIKNNYRLCFSLLFALLVYGTGVIYVLTIALINYLISKSLKNSIFNPLLTWTLDISVVFFKEYFAYCKFSSLHPGLGFLDQYTGILERWYVLFNITMLRLVSFNMDYYWSLKHNSEKLNTLIFDKDREPTTLTFRERVDYSCLDEDYNLKNFLTYIFYAPLYLAGPIISFNNFMSQMKYPTVSTLKYRNLLYAIRFLVCVLTMEFLLHYAYVTAISKDGNWNQYSAVESAMISFIVLFMTWLKLLIPWRLFRLWSLIDDIEPPENIVRCMCNNYSAVGFWRAWHRSFNRWLIRYIYVPLGGSNHSILNLFIIFTFVALWHDISWELFAWGWLIVLFILPERLCCFMSRRTGLTKHPYYRYISGFGAALNIYFMIICNLIGFAVGIDGIKNVLVSFFLTLKGAMSAIAAFIMFFSAVQIMFQIRVNEEEEGINLRC Q09766 YA7D_SCHPO MOD_RES 725; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 726; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 727; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 729; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 737; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 761; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24H6.13; CHAIN 1..871; /note="Uncharacterized membrane protein C24H6.13"; /id="PRO_0000116398" MSDSSSSSTSAFVSSLVFNFAIFCAFIGLFLCLRPREKHVYQPRCIIDTQPKEEKPEPSPSSPFGLFAYVVKRSETYLIQYAGVDGYFFIRYLFTFGALCILGCLVLFPILLPVNATNGVGEKGFDILSFSNVKNHNRFYAHVFLSWLFFGFTIFIIYRELRYYVIFRHAMQSSGLYNNLPSSSTMLLTELPNSVLNDEETLHELFPNASEFTCVRDLKKLEKKVKKRSDLGNKYESTLNSLINKSVKKHNKLVKKHKPLPSTLDYTAYVKKRPTHRLKFLIGKKVDTIDYCRDTIAELDEVVDKLQTSLEERKKVGSVFIRFRSQTDLQTAYQAFLYSKKFRKYRFGRALVGIAPEDIVWSNLDLSMYTRRGKKTISNTILTLMIIFWAFPVAVVGCISNVNYLIEKVHFLKFIDHMPPKLLGIITGILPSVALSILMSLVPPFIKFLGKFGGALTVQEIENYCQNWYYAFQVVQVFLVTTMTSAATSAVVQVIKEPASSMTLLASNLPKASNFYISYFLLQGLSIPGGALLQIVTLLLSKVLGRIFDNTPRKKWNRWNQLSAPSWGTVYPVYSLLVTIMICYSIIAPIIIGFAAVAFVLIYFAYSYNLIYVLGHNADAKGRNYPRALFQVFVGLYLAEVCLIGLFVLAKNWGATVLEAVFLGFTVACHLYFKYKFLPLMDAVPISAIESVSERPEIKYPMDLGTSEMKNVGRAYPEILEKLSSSSGSDEFLETSSRTSENTKEKIDKDDEGFAITNISSVHKMPSFVLSYFSDLAASNRILTGFDRVLQLLPSFYDIPVRVRNVQYVSPALKATPPSVWIPKDPLGLSTYAIEDARGKVDIFDDNTTFNEKGNLQYTGPPPDYDEAIRS Q09767 ARL_SCHPO BINDING 23..30; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 66..70; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 125..128; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" SPAC22F3.05c; CHAIN 2..186; /note="ADP-ribosylation factor-like protein alp41"; /id="PRO_0000207423" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000255" MGLLTILRQQKLKEREVRVLLLGLDNAGKTTILKCLLNEDVNEVSPTFGFQIRTLEVEGLRFTIWDIGGQKTLRNFWKNYFESTEAIIWVVDSLDDLRLEECRNTLQELLVEEKLLFTSILVLANKSDVSGALSSEEISKILNISKYKSSHWRIFSVSALTGLNIKDAISWLANDLKEIKLGTIDY Q09773 MUG62_SCHPO SPAC22F3.04; CHAIN 1..1487; /note="Meiotically up-regulated gene 62 protein"; /id="PRO_0000116399" MSLKSFFNFNKKTKLHDIEEDVISEIGSAGSALRTDAHMLKANDVYYKSETDSHTVLRFMKPSENEKIHPVRHSKYEDKSKLPFETIPDPVLKYVKRARDAELQPQLAKVSQKLFADISTATAAEKLQFTVPRRARFEINDPRNPTFSMMALQDIISVLEYRRNKNPTSTAHICIDKKGKEAVSYSWDKILNRAKQFASVAQNHVGLKPGTRVILYYRKSEASEYIISIFGCLLLGIVVIPLSPSSSSESLKLVVNEEKVRVAFTTEATYRIFIKDTEVNNAKSLAWWKSNDFTNYKFEQIKQYRMRANDTVLIDYTFSSSTYNDIKAVYTTKTFLSQMRNLTSSMITNPARQAGWKLHNFEDSKDVLITNFHPSMPLGLIMGVFNSVFAGYCTIFCDEEVLKTPGLLAYLITKYRCTYSLFDYAGLKQTVYNYQEDPKSTLSFKKNYTPNLSSLKLCMVECEVVDPEFNIIVSDRWLQPLGTNNSKEVITPILCLRKFGGIPISFKDWMISYTNRQKHERQMADTCYQEILVLKSSIEKEKVEIVPFLDIRKYSPNEVLCMSPFWYPIPEASVAVVNEDSKNICKVGEVGEIWVYSDCLPKLKAASVINNPQGEQLTDYENNQENKFEKNNSFMDSGLKGFLHNEKIFVLGNKDEQIRQYRKTMVADKLMEEKYVHYSHYLIKKIMKYVPEIFDGVAFEIEIDKAVYSVLVLESPIIKRSLIRNNRLKGRDLFSELVKITESSFQVTQDIFKLDVLSILIAPYKSLPRSRYMGIQAINTNKCKLAFLSGNLPVSYVRFFMDSALPKSKINLNNSKGIWSKDASKHHREIISLNVKQKMDPYKHQNKVSKARENLLNHFTILDFLKTKSAKTPTSPAILTFNAIEKTKVELTWAHFELKVASHVEYMQLSVKAKARSHILLLYYDPLEFLISIHSCFHLGVIPIPFQIREISQLIGEIEEFTKIAKAFNVEAILVDHKVLISLKSRDISNHFQQTCIDLNMKAPKIFETTGIPISKRAKKALNLITPGELNNKGKVALISINKLEDGSIIPTQFSHSSLLAFCHEQKEFVIGNEEKPIIGGIEFSSGMGLLHTALLGVYAGVPTLLIKQENLCNNGSLLFEAIEQNSLSKVMIPLNICQKSFSTAQGCNSIVINSTLSSIIVPCYDRPISSRVNSIIEDIARIGLAPNKVKLAYSHPINPFVCWNADSSMEKMKDYFDANQLRSGLVNVREDVLRNRQPLLYGSGTSTLYNEICIVHPEEKYICQEGEIGEIWINGKHGSYCENNELNSGCELLVQETLDKKSYSRTGQLGFIHHLKKKDQNMEKVPVLYTLDFIWNTLELNGLNHSVKDIEETIELVHPNICTDGCILFQASGSVVILLEVHSQQKFASLIPIIVATALAAHEIILDCVAFVPKGTFLRRPTGEKRRADILKQWTGGDLKHMTSYLIRQDFLLNEDFVGTELIGTTDSYDYSDENLIINSSQLNLL Q09776 SNU23_SCHPO SPAC22F3.11c; CHAIN 1..173; /note="U4/U6.U5 small nuclear ribonucleoprotein component snu23"; /id="PRO_0000116401" MDRYNPPRRNGNSKKNEVVITGGRTQRIDFEKDVNKTTILPAGASVGRRGRGAGWYCEACNETYKDSLSWLDHLNSTQHLRKTRTVIIEKRATLEEVKERMEYWRRQLLEPEKGSEEYSLKERVERYHQELEAKKLRRKQKKVNKEKNSPRLVGENTELAAIMGISSFGSTNL Q09779 THO2_SCHPO MOD_RES 1406; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1408; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1577; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1D4.14; CHAIN 1..1628; /note="THO complex subunit 2"; /id="PRO_0000116472" MTSLPEKDQQGEVSVSENQKKLSEEWEPYIDKLVASNRTRDERVESIQELFQKCVIEEKLPVDIFFSIFSLAFERLEEKNTLASYVIDTLWLFDTEWIKNFHEGSHDKAEKRLVSIGKGLKEFLPEEWLLSRLDCKFLENINVVPNGDFLNRKIVRTNTSLLYRQKKFNLLREESEGFSHLMINFFDALTCLRNKSLNEDYLIVQVNKSIISTIGAFDLDPNKVLDLILLLFSENLLDSWRFFLSILRNSPWGPNKERKFWNQLPDREKETFLNNLSNANGIFNFDERFTNTKSIMSQVLGHNLQYMYKEDDENLESYFMMVALLIKYNFISIDNIWAHLSPSDEELGKELGKYKDKLDEQTFKAKGNALTMAAPLPDDEIEDGETMDGQKAEAVPEIKKAKPSQKLGLLKSLLSIGDLSSSLLILGRYPFLLRAYPELSNLYHKLLHISISSIYANYSPLKLLPNDVRERLKQPKFIPEDSRLREITLRPPKEKNLVFSLDPFADRFNKTESEVFYYFENYDEDIPILRNLTEFYNIAIPWLRLSGLALCHDPVIVTKLCRIGQKCVDNSSESRTLWLDIIRSLLLPLITLIDVNTGLSYELFELLSKFDSSTRYALYGEWSSTSMKKFPELKLQNSITEKETKGILRRLTKTNVKQFGRLLAKVCHSNPCTVFSIALNQIETYDNLVEVVVDSARFITALDFDALTFIILSSFSNEFKKRLKSDGTSIAHWLQGLASFCGRVFRRYSSLDCTSIVEYVIKQFKVNQMFDLVILKELLSQMTGLQPWTNLSDNQIQGAAGGPVLRQLSLSLIYENPDVVRKSSMRLFNTLQKNGLATQLLVLLSQKYSTCIYDVTDENSHLKLISSLQDECSDVLYLLMEFLNMVCSPKSYYKLIPSFEQLIQDFHIQPQVAFYLSRYKNLDHSLTGSNTEDAMDIDYENTSSPNTASNPVWSIDNSVITELLPKQIWDYFSPNFYLTFWKLSLYDVFVPLERYEFERSRAFDQIRQTDAANTFYSRHRHDRQKIMQLSNSLQNELKEHINSLESVRKVLQGDCVKWFIPNGVFPNGTRLEHARFNCARYLWTLCIAPRLKMSPHDALYCAKFVKLLHSLGTPNFSTMSFLEILFNSQLPSFIFSMTQREADNFGRFLYEVLYDITSWYRDKILYERECLANGALPGFRLYWSDEQNDPDLSAVLPYNKFVLLFSKWHKYLTSYFESCLLSTEYMHIYNSVIILEKILPCFPLIIESGSALKRAAERLKDEEKREDLKVLALGYFAKLSKKQPEWVSFNSFSGTVRPSNSEKLQRPQQLSVAATSAVDSKTASISEEQAKIDKQKVALNPSAPEFVPDSTPSDAVASETDNKNLVENKAVEKRVEARSSANERKQEERRRKTTPEGNRRALRTRTPTNEDIQRSDSKLREDQSRDRTPQSRSFTNENNDNLRSVSRHTRREPQQAQNLNARREHESQKSDRWRQNGNVNRNPRVSNNNSTNVSRERSSEANHRTSNDNKRDEVTEGKDKNKRQDISGESNSRQNNAISRAGRSNGSNRGNDSRDADGRRSTHYASNKRPRSSDSQSPSNLREEDERENSRRRARQDDRRDRDSRQQRDRPRDRTSRSAREEKRRKIQ Q09781 RS3A1_SCHPO MOD_RES 2; /note="N-acetylalanine; partial"; /evidence="ECO:0000255|HAMAP-Rule:MF_03122" SPAC13G6.02c; CHAIN 2..252; /note="Small ribosomal subunit protein eS1A"; /id="PRO_0000153539" MAVGKNKRLSKGKKGIKKRVVDPFSRKDWYDIKAPAFFEVKNVGKTLVNRTAGLKNANDSLKGRILEVSLADLQKDEEHSFRKVKLRVEDIQGKSCLTSFNGFDMTSDKLRSLVRKWQSTIEANQTIKTTDGYLCRIFVIGFTSRRVNQVKKTTYAQSSQIRAIHQKMFQVIQNQANGCSMKELVQKLIPEVIGRAIEKATNNIYPLQNVFVRKVKILKAPKHDAQKLLELHGESQDVGSKVISDVAPLESV Q09782 GPI7_SCHPO SPAC13G6.03; CHAIN 1..758; /note="GPI ethanolamine phosphate transferase 2"; /id="PRO_0000116402" CARBOHYD 28; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 77; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 178; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 493; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRFAFFGIFWLQIFGSILFLLGFFPHKNDSTGKAMSNQFSPPAVIDQVVFVMVDALRADFVFSKSHNMPFTQSLLYNSTHGIGFSAFARSPTVTMPRLKALTTGTIPGFLDVLLNIAESDTGSSIEAQDSWVYQLNSFNKKIEFYGDDTWLKLFPSAFSKFEGTTSFFVSDYTEVDNNVTRNFDHALPSSLSHSWDALILHYLGVDHIGHLYGPSSPLLNIKLLEIDTIISRIYKYLQEYDEKTNTHSLIVLCGDHGMNEVGNHGGSSSGETTAALSLLFPSNELSHINKPILNMDDNPYSILERVEQVDVVPTICLLLGIPIPKGNMGKVLSPVTELWKDTKTAKMAALSNLFQLSLLKNPSLTTSELSTQFQDSDLNDIRLALENLQSQMVAQSSSYSLDRMLVAISILGACSILSLILFRNLYNYKELLAFAPFVVQNIIIVFSSSFIEEEHVIWYFAAVSLSLLQLLNPKTRLAGSLQLFCLSIIKRWNQTGQKYSDLRDIVDDFIAPSTFMKTILCVTSAFMPAIRSPSPINFLSSMFIAFYKLMPIISKHLNELPIIASFDYTFFVRIIWSLLLISFLSKPTFKQLRCQLSLFILLLTRLENMGLYLLYDIWQRTMPEEGTLASVMYYVAEQVAFFSLGNSNSLATVDLSQAYTGLDSYNIFAVGILLFTSVFAGALWWCLHQPKRMMDRSVKTFWIMSSISLTFLCISCFIMRHHLFVWSVFSPKLLYNASWASMYFLAKCLISTIMVRLR Q09783 TIM8_SCHPO SPAC13G6.04; CHAIN 1..98; /note="Mitochondrial import inner membrane translocase subunit tim8"; /id="PRO_0000193593" DISULFID 44..67; /evidence="ECO:0000250"; DISULFID 48..63; /evidence="ECO:0000250" MADATKNPIADLSESEQLELSKFIESEQQKVKLQQAIHQFTSTCWPKCIGNIGNKLDKSEEQCLQNCVERFLDCNFHIIKRYALEKFGFLFCWLGFSC Q09784 YA95_SCHPO MOD_RES 180; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC13G6.05c; CHAIN 1..253; /note="Uncharacterized protein C13G6.05c"; /id="PRO_0000211590" MIVHQQLPMSVNVASLDFLLIELVHTAKRLAEDRKKKSSSEKSIESDFQMLESIGFQVGRKITERLLLNRNRITETTDVMRFLCRELWPIVFRKPLDNLKTNRRGIFVLTDTYFYWFTKMTAMTGTEMAQITTPYFYFPSGFIRGVVYTFGYSAQVIAQCPNLPTCIFHVKFSPNPTQTSPGKPSTSESSQTDTSTRPANSQTPTTTRASSYTTLVSTSNQVSNEAEASAVETSANQAQNTEDATENEDRLPS Q09788 ASL1_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPAC13G6.10c; CHAIN 19..530; /note="Alkali-sensitive linkage protein 1"; /id="PRO_0000014190" CARBOHYD 55; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 120; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 128; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRTTFATVALAFLSTVGALPYAPNHRHHRRDDDGVLTVYETILETVYVTAVPGANSSSSYTSYSTGLASVTESSDDGASTALPTTSTESVVVTTSAPAASSSATSYPATFVSTPLYTMDNVTAPVWSNTSVPVSTPETSATSSSEFFTSYPATSSESSSSYPASSTEVASSYSASSTEVTSSYPASSEVATSTSSYVAPVSSSVASSSEISAGSATSYVPTSSSSIALSSVVASASVSAANKGVSTPAVSSAAASSSAVVSSVVSSATSVAASSTISSATSSSASASPTSSSVSGKRGLAWIPGTDLGYSDNFVNKGINWYYNWGSYSSGLSSSFEYVLNQHDANSLSSASSVFTGGATVIGFNEPDLSAAGNPIDAATAASYYLQYLTPLRESGAIGYLGSPAISNVGEDWLSEFMSACSDCKIDFIACHWYGIDFSNLQDYINSLANYGLPIWLTEFACTNWDDSNLPSLDEVKTLMTSALGFLDGHGSVERYSWFAPATELGAGVGNNNALISSSGGLSEVGEIYIS Q09792 PPK8_SCHPO ACT_SITE 364; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 247..255; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 270; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; SPAC22G7.08; CHAIN 1..513; /note="Serine/threonine-protein kinase ppk8"; /id="PRO_0000086040" MAVITEENSNNLFCTDSLELTSNKQDDQVISNYLKPVRSYPYIKYSRSSLLLTASTTLPENFVISFTNSIESEESDKSDYLLDHAHSLQELSTTHSSLSSTLTSMSEESSSTESKFATLNDGINGGNPYSRLYRKNPSSDPNDIPPQFHFKKKSKSFYSSMYDKMKIRINILPNGNDNFIKKRNSGFALAPIACYNHTSDLRKLLKHKVTGSNASIFKRINPRSRKRVVNPECSVTDTPYGKLNNVIGEGASSFIRVINDRNKLPIYVAKVFRPPLDTSLLRRYVRYFIAEYTFASTLRHPNIIKVLDIIYKRHTILQIIEYVPYDLFTFITKGHCSALKADQMFFQLLDGVAYMHSLGIAHRDIKLDNIMLDENLNVKIIDFGTAFVFHYPFESTTLMSDGVVGSKPYVAPEVLTQKPYDPSAVDVWSCAIVYCCIALKRFPWKVPHTSDKRFNLYVTQRNDPNTKSQLIESLPMNSRDTIYHMLDIDFNTRCSISGARSTTWMQQVRKTLI Q09796 KA111_SCHPO SPAC22G7.02; CHAIN 1..990; /note="Importin beta-like protein kap111"; /id="PRO_0000116404" MDGNEIAHAKKLVYDLYSGSLSPSAIAATEKELQKAQRSQQGWNIGLFMLQSKDVYEQFFGALTLQMKINTQLETLSDKDLVQLFVQLLQKLLWDDGLPALVERKVICTLASLTIKYELEKKEEASLKVIYCLFCNKLEFFNADMNAASVLNNLFPPASSRNAQLTASYINELLLELSFSIYTKENEDALFNNVFRPCSNIIVSVLVFIFTNYSLDLSKEKNVAALEEALNCMIAISSYLAKASVSVQSVLPAFTECMDLTVNCIALDEVSEKAMNCLADLLANYSNFITQPTIERLWTILTGPWGETHLQQELEDPDSGEENDYSFLNIVIGFAEAMLPQIIDHIQEEKSIRLLYILASLLSFPGYAIVEEKVSWRTLEFWTTLIEDFSMSKAATDPSKDEIFKQIAFSVVEKAWWKMLLPSPEQWNSWPSSSRDSFNSYRRDLGDLLESSYSIFGERLYAMYITTIENFFSDGTGSPQSLEVSFYCLCCILEYDTNDSDTLDAWLTRLFETSFAIKASAFQNPQLLKTCSQLLSSCSCFLQNHPQYLNISLPVLFDALHISETSIQMTVSRSIHTLCTTCASHLLTEIDGFMAVVEELTPKLVYVPSVLEKIYSSVGYVTQRIEDIELRISYLMRLLNCILAQLQPSLYPNLEIFENVLKSCLQSVAGVALSQSPIGESPIIDVEQSTQETTFWQQSCIAEFQAKLISFLTHSESMALQYSDVVGLICKIMIAGLNEVEPSPFSLPIVTTIQYFCDRFTEFPAAVLLTLGSAILTCPYGQTDIIDKVLIDMCSSIQNSVVIINEESFMNNIDITVELYHFFSIILQKHPSFLETMYPDFTQLILNRAINLLGKPERLLESAAGQFIISFITSEKSDLLNTHTDFVNAIRSPLIAKILLGFGGNASRSSLPLLSDILGKLKAQNFSATRACLTQSLEEEGFPSRNVSNEIKRRFLTDLLKARIKDKVKQFWILCKGLESTPYGNSSWTF Q09799 KRI1_SCHPO MOD_RES 222; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 225; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 476; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22G7.05; CHAIN 1..598; /note="Protein kri1"; /id="PRO_0000116407" MPRKKSAAKKAREALVQKKVINSNVPTDKKSIDQLQENVTSKSHLLEESSSEDEEINSFQINEEYAKRFEHNKKREELQKLEAKYGEQMANGVDGEGSDESSSEEEEDSDGELVTPEVDAAILRMIVKIRNKDPDLYDSQQKYFDEVEKDVQGSLKSKDGFRSVTLKDYHRQKLLSGEILDAEEDEPMPNDANPTHVEEQERLRKETIAAFHDVNGNKDAVSNESDEDGDFLVKKEKTKKQLEEEEHGYERFLLESAQSKEARKVLEDLSSSYVKQRPSVLVNTEDDENGIKPSDEDFLLKYMMNRGWRTSNTKQPSYEEIIDEVDAENRFDEDAEEFENKFNFRFEEEAGSQIVSHPRNVADSLRRKDDSRKRARDRKKERLEEASQKRLEEVNRLKNLKRKELEEKLNQVIEIAGSKNIDVSKLDLDEDFDPEKWESKMSEIFNENYYEEDSAKKPEFGDDIDIDDIAQVDNGSEDLGSIENKTVEDTGNREKSKKSLRKDIREKKRKIDEYVEEKYGVPEAVIVKNSKFRYQQVAPETFGLDILDILNASDADLNNYVGLKKMTPYRTPEEIARDKKKYGKKKRLREWKKQVFGK Q09801 FIP1X_SCHPO SPAC22G7.10; CHAIN 1..344; /note="Pre-mRNA polyadenylation factor fip1"; /id="PRO_0000215043" MSNADQHMDVDEDEYLYGETIEERNDGVTVSNAKSPEQASEESDDSDIEFIIETKPGERAEPLGGSIATLGSTRPSAKPQVEKTAVEVKTTEPQDLSTAETAPKVDIDAVPTIDGKNIFEIDLESFDDKPWRKPGADISDYFNYGFDEFTWAAYCAKQTTLRDDFSPQKFMASLAQIPGPLPSGNVPSPAEFQAMMASGFPPFMPIPPPIGGPQEDMGYSRNFPVHASSNYNTTHTSGGGVHSGAATPNAYVNNNPSSSRRESESPANSPNITSSAGMTHAQPTHNPTSSYGNGASTNYNASRPPSNHPHSSNYPSSSRRKPSPDRYSNYSSRGSGGRYRRNRY Q09812 ATG22_SCHPO SPAC2G11.13; CHAIN 1..529; /note="Autophagy-related protein 22"; /id="PRO_0000207627" CARBOHYD 198; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 218; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 299; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 359; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 489; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNSPIQLHKKFSTTVWHVLSWILYAVGAGPTAIISMGVYVPLIVMKNAHDHGFLRTDHTIPCSLYPEEPCSLNIVGPLWIDVSSIVFAASAISTFLQMAMMVSLGVICDYGNNRRYILFSCVIIGSISGIILSWSPSSFLLGKIVFLILVDLNFIISQSCYDSFLPIFLRFYPITRGPITLESALQDETDDLDSYITNTTIDSSEEEPYLLEHSLILNESAPPADVEDEHKAKIAARLSSVGFGSFFGAAILFQIIFTPILYKTNNNPIILPITVTVCSCWWLILSTPLCTIVTLPVENHSSDAILTLLYNSVKESYHSFKHAMSISSIRLFLFSRLFINCGIQTSLSSAVIFGKARLNLSNFQLTLLGMGISSFALLGTVIIPYLTEYFQLNSLQVVMIISILLPMAPLYGLLGYIPGFENAGIRTSADVFRATLFFGFFLGGAHSYCRSVYAQLVPSGKETRFFALYALISQTGVLFSHISLTLISNYTSDLRAVYIFVIVVMTLPLSSLWIMYQHSKTPNLHRSSS Q09813 T111_SCHPO MOD_RES 244; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2G11.14; CHAIN 1..979; /note="Putative transcription initiation factor TFIID 111 kDa subunit"; /id="PRO_0000072397" MSFDGLIVENENTKSGYNDGNDLTDLFKQNGTDMSVINSLLGDTNNPGMNESPKILDSSFENSNPQDGPNYEDFDFMGSIHKEFGNNINEMDDMEDVSDDNLPEEEQAVNYTGDKDDEDFGKLLAKEMGEEAAGQVLSGVGFSIPSGLVPPSEPSKTVSSTTEELQNEAQIRESIVKTFFPTFERGVLLNFSELFKPKPVKLAPPKKKTPKVCVPGRLTLEVDTDYAIIFNSKKSLPLKRNVVSPISTHTKKRRRTANTSQRNDGLDLNTVFTTNDWEKNIIYDESDVNKTNQSSFFIDKSLVDIDFAFDENIFDGDTGTSKVVLNLNDPKLLLQPQLPKKEDSQRSFADTHQRNSLAWKFNISNDPAYEMLKQNHQSKVRNTLSQLAIEHAAFAEKLTFPYYKTRLSKRAVRSYHRPTMSFKPNAAIVFSPLIVRKRSKDKHKSERELIPTTKEITMGDTTHAILVEFSEEHPAVLSNAGMASRIVNYYRKKNEQDESRPKLEVGESHVLDVQDRSPFWNFGSVEPGEITPTLYNKMIRAPLFKHEVPPTDFILIRNSSSYGSKYYLKNINHMFVSGQTFPVTDVPGPHSRKVTTASKNRLKMLVFRLIRRSPNGGLFIRQLSKHFSDQNEMQIRQRLKEFMEYKKKGDGPGYWKLKSNEVVPDEAGTRSMVSPETVCLLESMQVGVRQLEDAGYGKTMDEINDDEDEEQPAEQLLAPWITTRNFINATQGKAMLTLFGEGDPTGIGEGYSFIRTSMKGGFKPAGETADDKPEPQTKNAHAYNVAKQQRAYEEEINRIWNAQKRGLSINNLEELAKKYGINSIHDDYVESNEETTREETPSSDKVLRIVRLYRDKNGNLERKQETIHDPIVIHAYLKKRREIDEQSTALDAVVPTGDEAIDRRNRRRLEQELAKSQKNWERRRARHAAKEGINLNGEGRKPTTRKCSNCGQVGHMKTNKICPLFGRPEGGLATMLDKN Q09816 MTAP_SCHPO BINDING 16; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000255|HAMAP-Rule:MF_03155"; BINDING 59..60; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000255|HAMAP-Rule:MF_03155"; BINDING 92..93; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000255|HAMAP-Rule:MF_03155"; BINDING 198; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03155"; BINDING 199; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000255|HAMAP-Rule:MF_03155"; BINDING 222..224; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03155" CATALYTIC ACTIVITY: Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000255|HAMAP-Rule:MF_03155}; SPAC16C9.02c; CHAIN 1..307; /note="S-methyl-5'-thioadenosine phosphorylase"; /id="PRO_0000184557" MNKQAEPILLGVIGGSGFYDLPGFDIVESVNPITPWGYPASPISIARTTSGFLIAFLARHGVGHIYTPTEVPSRANIAALKSLGVLAIVSFSAVGSLREDIPPEDFVLPTQIIDRTLCARPNTFFESGCVAHVSFGDPFDQDLYEILSSCGSNLKNGSKLHTKRKGDDLTVVCMEGPAFSTRAESNLYRSWGASIINMSVIPEAKLAREAEIAYQMVCMATDYDCWRMNEEPVTVETVMEHISNNKDNAKIFLLEAVKKLEAPLLQGFLGRNLRESVQNGIQTNHKHRNPDAIRRLQFLFPNLTIPH Q09819 YAC5_SCHPO MOD_RES 47; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16C9.05; CHAIN 1..404; /note="Uncharacterized protein C16C9.05"; /id="PRO_0000116415" MASSINNSSQPTVPSISNNSHGDSFVNEGPPSNFKNNSLTSSTHSSTDHVNVLPISQDKEMDISSPVKKQKASYSNKSPNKAPIQKSRGSSLKSHLETESQQTPVKRRRRKATIRNVDYCSACGGRGLFICCEGCPCSFHLSCLEPPLTPENIPEGSWFCVTCSIKSHHPPKHPLSIWSQLYDWIDSQNPSQYRLPDDLVHYFHGISRGDTGAYKETEGEMDTDEFSALPTGSSITNLAYCGYCSKPSMGACWVYGCQLCDTFYHKNCKEHAKKCSHDSIGKKGMRVPKNAVVIRTPLVLDTTSNTLNPKVMISGWQFLMGEFPSDELLYFPRLPVSCLYKVSEDGLIKDFLYAIGIEAKKFNNERKKRELEVIPPDVKSALLPARTHPNLPIALRTLFNKART Q09824 REP2_SCHPO SPBC2F12.11c; CHAIN 1..219; /note="Transcriptional activator protein rep2"; /id="PRO_0000097249" MHFADIPLSKPCLNNPPTYPWSSPILSSIANPSLCDIVSSPSSVSSFASSDDFAFMNAYCLPIQQNHQFGSPVAASPNQQPLVESQNRRNVTYASLVIGKLGIAQLIRQQTDPPQIIHRKQDKGLMARVLSRSKKQEERENHSSDARDAIKSALRRRMRRREGRVQKALRPTPNLICSKCNTTFNHSTALMMHEATCLNQVPFKLSDFFVEDVIDDWLF Q09827 SC61G_SCHPO SPAC4G8.02c; CHAIN 1..70; /note="Probable protein transport protein Sec61 subunit gamma"; /id="PRO_0000104210" MADNADDLFQIPKNFYKEGSHFIKRCVKPDRKEFLSISKAVATGFVLMGLIGYIIKLIHIPINKVLVGGA Q09828 SYLM_SCHPO BINDING 631; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000250" SPAC4G8.09; CHAIN 22..874; /note="Putative leucine--tRNA ligase, mitochondrial"; /id="PRO_0000035811" MLKSVGTNGRKVPKIASLCNFLKFNKNIHSNPDFLAIAENWKSYWKSHYPFVKNDKGKKKYILSMFPYPSGLLHIGHVRVYTISDILSRYYRMKGYKVIHPMGWDAFGLPAENAAIENGISASSWTYENIKKMKEQTYHMNIYFDWDREISTCNPDYYKWSQYLFLQMFHKGLAYQAEATVNWDPVDCTVLANEQVDSHGRSWRSGAIVEKKNLRQWFLKISDYSDQLLDDLETLPKWPDKVKKMQRNWIGRTTGFEISFPLLNDKETLTVFTTKPETIIDVSFIALSKNHKLVLLESQKDPSLAEHLRNESLLDKGYQLPCFAKNPVTGKALPIFYAPYVLDCYGTGAVMGAPIHDRRDFEFAKRNNIIFSKESCIGSYFTNEGKELLNHHDSSNLMDIKQKMLQQKIVSYLEEKKLAKRVKNYRLKDWLISRQRFWGTPIPMVHCETCGAVPVPESELPVKLPDLDKIYEKGTSPLSNLETWMKTTCPKCHGPATRETDTMDTFVDSSWYYFRFLDSKNSELPVGLASASSLMPVDIYIGGVEHSILHLLYSRFFSKFMKDIGLWNGDKYLNEPFTQLITQGMVHGLTYTTMSDERILNPKEVQKIGDEYFLISNPKEKVQLSYQKMSKSKHNGVDPIRTIQKYGSDIIRAYIIFSAPVEGVLLWNENAIMGTKRWLTKIWNCVHQLLEREKKMSDAMRQTKLTIVDDHNSRKLESQYNEFISQCSAHYENVFSLNLVISDAMKLTNNIADALKNNKVNIGTIKASLEVLVKCIAPIIPCFSSECWLLLGHNSSVYSNWPISKNKKENMEEPVTIPVQINGKVRFKIEMPKLNDENEILNFVLETNDGKRWLSNKKVLKSFVKQKIISLVTD Q09832 TYW2_SCHPO BINDING 228; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"; BINDING 235; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"; BINDING 275..276; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"; BINDING 302..303; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01021" CATALYTIC ACTIVITY: Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315, ChEBI:CHEBI:73550; EC=2.5.1.114; SPAC4G8.06c; CHAIN 1..418; /note="tRNA wybutosine-synthesizing protein 2"; /id="PRO_0000116416" MISFLVQKSEAKYWKDVVQNKNKFLKNIGIISGPKLVDTYSNQFEADFLKKCVLIPTSYNKEDLPKDILDCPRIYLIEEEVKSVQTDEKLQIKVLRYVSQILHTTVSEEQYPVPSRFVIYPPLALLSLNSFGTKEWHLFFQSYANVDVKAGLFDIFAREWNVSHIAINEPIPVGDVMRRPLSLKPLYGDFGVLIDGNPSEQDFQKAFWVSCRQNGIYQTWAPLYTMFSRGNSIEKARVLNFSYIKDEIIADLYAGIGYFTFSYVKAGASTVFCWEINPWSVEALRRAALKNGWSIYVVRNGENYEFKVGTHRIVVFLESNVYAAERFSKMNISARHINLGMLPSSEKSWSTATSILKRESHSFIHVHENVKDEDIETYSSEVNSCFSKMLAKNTVCVTNCVKSFSPRVSHIVYDIETV Q09833 YAD7_SCHPO ACT_SITE 478; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"; ACT_SITE 517; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10015" BINDING 182; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 188; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 191; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 276; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250"; BINDING 347; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"; BINDING 383; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"; BINDING 404; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"; BINDING 451; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35; SPAC4G8.07c; CHAIN 1..527; /note="tRNA (uracil(54)-C(5))-methyltransferase"; /id="PRO_0000162060" MYPYCLKYLTNGLRSKQMINFLCIQNILSARTLKICRFRFLPTPSHPTHKMAQETRAISSISEAANKRARKLSKRRAKKPVEEGSSGHVLLLEIENLIEKPVLANVPFERFQEIEVKISYLSSSGDGIGLVCNDQYAVVVPFTLPGDIVKAKLHFLADTYALADFLEVISPSEDRDDTLIKCPYFAKCGGCQYQMLSYDKQLLQKKRVVEKAFQYYSKLDSSLLPAIKDTVGSPLQYNYRTKITPHFDVPKGGTKGPLIIGFQEKGRRRVMDIEECPIATKTINEEYPKIIEDVQSRANTFKRGATILMRDSATEDGKHCVITDHKMIVREQFGDLSFTFPAGAFFQNNNSILEKFTSYVREQLLNPFGRKEHQRPKYFVDAYCGSGLFSVACSKGFLSVIGVEISADSVRYAEENAKRNNVSNATFIVGQAEKIFSSIETPPNETAMVIDPPRKGCDQSFLNQLLEYSPYRIVYISCNVHTQARDVGFLLSQEKGRSYKIDEIRGFDLFPQSHHVESILTLTKVVS Q09835 GOS1_SCHPO SPAC4G8.10; CHAIN 1..182; /note="Protein transport protein gos1"; /id="PRO_0000212556" MKSMLLRDSVKKASQFQRSLHSDPNQAKILLEERRKLLEEANSSADENDSHSMATIKSHFERLKRDEQLLNGVLKKYDAKQEVLSPEELRDAQNFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIRRRRDSIILALLISVLMLLFLFFH Q09837 SMP3_SCHPO SPAC4G8.12c; CHAIN 1..533; /note="GPI mannosyltransferase 4"; /id="PRO_0000215790" CARBOHYD 261; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 378; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 419; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 425; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 452; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 477; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 518; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFKNRKYAIIYTFLLILRFWFSQGSSYIHPDEHLQSFQIFANKLFGWKVELPWEFTTKKPIRSVVPLNVMLLPIFLLCRCICKSNCSPYPILLFTRLYMCLISLLIDLSIWNIVPLNARWSALLLYSSSFMATTFQTHTFTNSIETIFFFLTILFLSKLNSVPLNKKISYLYTFLLAIVSVLGFFTRITFLAFVIAPYIYFSVRCFKKNVNNPKDIFLHLCIFVSVSFATVLACILEDYKFYGVFVITFWNNLKYNSQIENLSQHGLHSRLTHFFTNMPLLCGPLIFVPKLWDVRKPATWLWLLPVFILSLFPHQEPRFLLPAASIFIVNSGCLVRSYWIKFLFVMYAVVLAVFFGIMHQNGVIPAVLEVKNIIEQRNVTTMENCNLYFNPEMPTTIYFWKIYSAPTWMLARPKFSQINTSHLYNYSTKQMISKFWETYYEEVKVVNLPEENTTEFQASTLLVCPVAMLQTSSYLQNLTMLHYIPYHVDLDDTDELPLAELIMNHGIGIFTAKEICENNTITNELPTVLRSVG Q09840 AMY2_SCHPO ACT_SITE 233; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P56271"; ACT_SITE 257; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P56271" BINDING 109; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 147; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 202; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P56271"; BINDING 231; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 233; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 236..237; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 237; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 257; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 261; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 325; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3"; BINDING 372; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P0C1B3" CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P0C1B3}; Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. {ECO:0000250|UniProtKB:P0C1B3}; SIGNAL 1..24; /evidence="ECO:0000255" SPAC23D3.14c; PROPEP 552..581; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000255452" CHAIN 25..551; /note="Alpha-amylase 2"; /id="PRO_0000001355" CARBOHYD 291; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 332; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 56..64; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 176..191; /evidence="ECO:0000250|UniProtKB:P56271"; DISULFID 267..311; /evidence="ECO:0000250|UniProtKB:P56271" LIPID 551; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MNYRRNICLRIGWMLLFAFIPAYAGHSAEEWKRRSIYQIITDRFSLEEGATERIPCDPVRFMYCGGTWNGIRNHLDYIQGMGFDAIWISPIFENVEGNDIDGSSYHGYWTTNLYELNHHFGTKEEFMELIQELHKRDIWILLDVAINSMAINGPLEQMSFEKVIPFNDASFFHPHCWVDYESNDIESVQNCWLGDENLLLADVDTENEVVLSVLEKWIKNVVQEYDIDGIRFDAIKHAPIEFWLRMSKAADIFTIGEYFTGSPAEACDYQNSGLDSFLNFPLYWPITWAFNNTGLQCEALAIAINQINEECNDINVLGTFIGNHDLPRISHNNTDQARIMNAITFVMMWDGIPIIYYGTEQNFNSYHDPFNREALWLSNFDMENVYYKLIGILNRFRKSVQRQEENYVNTRSTILSVKIHHIVVQKLNVITVLNNYGIHNEERLSIVFKPLGASPKDTFFDIINNQKYVVNTDGTLKVVITNGFPIVLYPTSKIETSLPQFTATLLPEITFVPSITVTTHYVLPTLLAPLGYDIREHPGGQQFWNTLTAKSEAKTIRSFTKLKLFILLIAVPFALPMIILI Q09841 PSB2_SCHPO ACT_SITE 36; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; SPAC23D3.07; PROPEP 1..35; /note="Removed in mature form"; /evidence="ECO:0000250"; /id="PRO_0000026655" CHAIN 36..267; /note="Probable proteasome subunit beta type-2"; /id="PRO_0000026656" MMGINERKGFDFEYYQRNLLLQEKGFPTPKATSTGTTIVGVIAKDCIVLGADTRATAGPIIADKNCKKLHLISPNIWCAGAGTAADTEFVTSMISSNIELHSLYTNRKPRVVTALTMLKQHLFRYQGHIGAYLVLGGYDCKGPHLFTIAAHGSSDKLPYVALGSGSLAAISVLETKYQPDLERHEAMELVKEAIEAGIFNDLGSGSNCDLVVIDEEKATPYRGYSKPNERATKQSKYTYDRGTTAVLKEDIYKFVTVQDLDEMQVDV Q09842 PDP3_SCHPO MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 236; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 238; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23D3.01; CHAIN 1..407; /note="PWWP domain-containing protein 3"; /id="PRO_0000116417" MMVARTRSQKRKLEEINNQKKIKTKKKATGQQTSNTKNLRDVKKKGKQLAYVPRTSPRKSYKNGEYVLAKMSSFPWWPARVASQKSIPTEVRERLKRNFRMDNGIFVQFLPSRDYAIISSSNVLPLTVDESRFILDHDLSTKYIQKTVGLIIASVKRKVSFSDVEEDEFEPENTRKKLQKPIEKPKKEKIEATPKIDGGKRLKNEKSSAEISQTSKQRPSRRSARVRMATDNAQKSPSPIPSPKKTAKKRVRFAGSLEELPKFSLEYQLAQPISTVDMYAQVHYIRFNTLLYYRYQLQEILLSYNHYPQESDMSHVHQILEMIENFSAINSELLESTKLYSLFTLLVKLSDIPLDEKYDFSSRFSTLLLQFQAFVQPKTMTSNVSTAPIGKNAQVNTEAARPSVITT Q09848 US108_SCHPO SPAC23D3.08; CHAIN 1..337; /note="U1 snRNP-associated protein usp108"; /id="PRO_0000050160" MDSGTSVVSISADILRPPVLTAAQTFGDNENECRVRLVLTAQQVQEWNLLPQDIQQEILKNGQVRVETYSSSNTARKIFICTSSVSNLASSIPALIKVVTPTKEEDASLNINLAVSSLILGSKVLIHQNLIPSLFSVSNSTKLLYSASLLPRSSERLVTLETNEIDASVVIETLLKYILSRISFIPRVSVVPYIPDAAYGIYGSPSTFTQFNHMSSMVTPENPYGIPPIALTSAGGNPDPLRTTQVFPHSGPSIPLNIAATQVVSQKMSVPSSLLDQLYHAMPHKLMEISQNTNANITVEESDSNSNEKFISVVGTSEANQSALMQLYAALISLGRK Q09852 YAEC_SCHPO MOD_RES 297; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 299; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23D3.12; CHAIN 1..559; /note="Putative inorganic phosphate transporter C23D3.12"; /id="PRO_0000050478" MNRLNPFSKSHSKNSNENNEVSLADVAESDTRRHWLGLTKREFKLMGFAGAGFFLDSYDLFIINLVSPIYEYLYWGGLEGKKPHYPSGIHGLVNAAANIGNVFGQILFGFMGDFFGRKFVYGKEMIVVIIATVLVIALPKSIPTPLGKMMWIFAWRWLLGLGIGGDYPMSATITSERSLLSRRGTLLSIVFSFQGFGTLAGAIVTIILLACFEKPLNQRGEYTKLEGVWRLQMGLALVPALLVLIPRLTMKESKSYEQSKALNKYTDNDTYIADDDEPKKDNQNVVEEKQINLTTSSDSHPTSTEDFGDKRASTVPTSENTSGFIEYFSQWHHFKHLLATAVSWFLLDIAFYGVNLNQSVILKAIGFSSGKNEYHTLMRGAIGNLIIAIAGYVPGYWFTVFLVEKLGRKWIQLQGLFITGLMFAILAGSWDTISTGGRFACFVIAQFFSNFGPNATTFLYPAEVFPARVRGTAHGLSAALGKCGAILASLLFNFLTSVIGYGNVMWIFCGCMWGAIFFTLLLPETKMRDADEIDREEVLRGGNGKTHQGRWSWYFNGIF Q09853 MON2_SCHPO MOD_RES 43; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 660; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23D3.13c; CHAIN 1..1616; /note="Protein MON2 homolog"; /id="PRO_0000116419" MSLYDSLLSNLQSINVDTRKKNADLKKLADGSLKFLYTNKNLSQDSLVSKLKGNEAFYKPFLFCCAKKIERHIYISLNSIQLLAINDALSPDILESLFNSLNAVIQLGQDSQLRVLQIIPIICTHYAASMKLPILISLFRICFNLHNSKNSVVSNAAAATLRQIVILVFDYLDYDTLAHKQEADLFLDSLSLFKGLCSLLSAGKSESLNVDHISTTFGLELLESILVNHHRLFQIPEFQDSVRKDLLPIITASLASMSDFPVALRISRILNIIFQHYVTSLTLDIEVIFSFIISSLDNSEAAWKKALFLEVLRSIFSNTNLLYLMYTLFDGNEGRKPIIKKLVTSLSRIVNEKPSVIGVGSRVVLADTFEDYSSTSSGNPPSSMEKVSGSFTGTKPEQIIGICRATILKTPCIEQFDKQEPPIIPFAYLVYLAMCSLASISNGIADFVFQFYEDVGKKEFTLLIEGIKCENFDSKEDSTARPQNIIKCQYGLISENWTSFLVAYSTFVSSALAVELLKFCLNSYVNFVSVCTLFGLETPRDALLTTLSNKAVPSNLLSGNMTHSASSSISHNGRLSTSTMFSVEGLKEAATTIAAIASYDSNHDEKQKCFSLREILFLRCLSSIAKVVGEKMGKGWKILFETFDKADIILNRSPTSKHLSTSSLNRVNSSNSNFQDSKSFSTLMDYELVSYKNELSELMYVTSSYSQPAYMEFLESLLAVITSSSVHPIQTLTAPRQSFNEDLLSANTKNSVYKTSANRSISGGIRLLRKSSEVFYSFSILETVCSCNLDRFLDSKLDHSGWSLISKSLSEVFKIINVAPELRTRAANCLANILVDVASRLSNENSPDSYAFQEIFFESLGMLLPVTEVSDNTSRGVEYDISTIGLEALVSILETVGHHVLHGWQYVFEMLRFNCLNGATCFGSEKGAKIVRLAFSCLQLICTDFLASLDTSNYLDLMDTLLVFCRQLEDANVSLTAVGLFWNVSDTLKNMFSTSDFSCAYNSVEDLYAFTSMKSKEILPEVLWIMLLVHLADLCENSWASVRNGAAQILFRIFNSQCSKLGTNAWASCCQLVIMKLLHSQPIQNVSDVNNKKDEDDHEQTSCLIISGIADVFSENMSLLLNVNGILDVLEEAFQLMLRLHSDIYPKICISNFKALRELSFSISEFGKENATFTLLIKLVFINWGRFCEVSFSERRLANISQEGLTLLIESVVFLLKAYNFGIEEIKDSLLQVRKAVFYEESTSFALDVDFLSSLQLAVESLTDLLISKFKLNHLVLELWSDVLTYAFNEEKTIRASLPTLICLSKKIFENAENVVENHSLDFLNRGTMQHMFESLLVPMRLKYRCPKASRVNQSTLPIWVLASKCFVRLMINCFKDLKGSDAIEDAEKMQCLFLLTVEATNSIISPNADYEYVWSLEDVFENEDVSSLKQLHNLWKPHLQLNCLSDEVAQYYITLCKGSFYYQMRNTEDMVISRSNLDIQKEAARNFFPSTESPVSNRRQRIAVDCFSILLDDYNSSYEHVSLTIRPILQSRLCWSLKRYVADKSVSGYLPLSKSQEMDMSTVAECLNNHPSLYSNPIHYLLRKAYHTTNASPVATSLNAILGQLTLKNEVLNAI Q09855 POF11_SCHPO SPAC29E6.01; CHAIN 1..506; /note="F-box/WD repeat-containing protein pof11"; /id="PRO_0000051138" MNQDDNGKNVVSKVSDLTSCSDFSTSSPVPCLNPLSHENNRIDLIRDLLASLSKEGVVAVYNHVRSLLFTDFTEVFPEEVSLRVFSYLDQLDLCKCKLMSKRWKRLLEDPGIWKALYMQKGWFVNENVLNEFEAWRRTHKFPQPRFENFLKQQNIIGPYGTMFLPQQFIFDSNGRPLLNWSYLYKEHAHLDSNWRHGRFLVSTFNNPSIRFPADQDFRATLDSVYCVQYDDEIMVSGSKDRTVSVWDVNSRFILYKLYGHSGSVLCLDFCRRRNLLVSGSSDSTIIIWDWQNRRPLKVYFGHTDNVLGVVVSENYIISSSRDHTARVWRLDATSPAEACMHVLRGHLASVNSVQYSSKTGLIVTASSDRTLRTWDITTGHCIRIIHAHQRGIACAQYNGKFIVSGSSDLTIRIFEASSGKLLRMLQGHEDLIRTVRFNDEKIVSGGYDGTVRIWNFNTGEQHCVLHNSRNSRVFGLQFDHRRIIACTHSSEILVWNFDDGLDCTFF Q09860 SYC_SCHPO BINDING 46; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 350; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 375; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 379; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 411; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661, Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517, ChEBI:CHEBI:456215; EC=6.1.1.16; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPAC29E6.06c; CHAIN 1..754; /note="Probable cysteine--tRNA ligase"; /id="PRO_0000159552" MSTRNPAQSHWGVPKGQRTELYVYNTLTHSKVPFVSNGSNLTWYCCGPTVYDASHMGHARNYVTTDILRRILQSYFGYNITFVQNVTDIDDKIILRARQQYLFEEYKKQQGTNKSHSEAREKVTEAWFAYAKKNLPEPPSSMSEWPQWLASHDIPTLAINNPKLPMHVDALKSALDALQVSEASEIISLDGFWPKVQDVLVPLLDAELGSTVTDPAIFRKLAAYWEDDFNKDMANLNVLPPTAVTRVSEYVPEIVDFVQRIIDRGYAYPVTDGSVYFDTEAFEKGGHFYAKLEPWNKGNRELIAEGEGSLAALTGKKRPGDFALWKASKPGEPSWDSPWSKGRPGWHIECSVMASALLGSNIDIHSGGIDLAFPHHDNELAQSEAYFDCPQWVNYFFHAGHLHIEGQKMSKSLKNFITIKEILKKFTPRQLRLAFLLQQWNTQLDFKETLLAYVLNIEQALENFFRTVRALMNETEGVSANGGHVPEKFDKLEIELLEKFQQTQQNTHLALCDSFNTPLVMQHIDNLVTQANIYIREVGQQPCSRLLGQIASWITSMLQIFGLDENGHPNAVGWSSSKGSSSENTDAMPYIRAVSSFRDRVRELCIAKASSQEILKACDIFRDYDMAALGVSFNDRPQGSALVKLVDAEELIAAREQKLEEERAKQAKKAQAKAEQEKKQVERVMKGKTSPSEMFKMFKEYLSFDEAGLPTKMRGEDGSEIDVPKSRKKKLQKEYAQQEKLHKEYLSYIESNKS Q09863 NST1_SCHPO MOD_RES 883; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC29E6.10c; CHAIN 1..1085; /note="Stress response protein nst1"; /id="PRO_0000116425" MNDKALRTEALSVGLEPPSFKDLLIPIPNSGTKKKNKKKKKPKAKKNVETQANVDLLGSAGTDSAVTDVGANNGVIDHQASLELSNLNSRISHPQLVSANGDDSSLINVEGISSTDWQFTLESDDTIEHSPQCILSTSSFVDEAEFPVHIPGLEDATSSNMSPNSVQNNMNLNTVALGSSTSSKRKKKKKKKSKANSASLNVDDQRDFEQVYSTDVAITYRNGQALSYYNGSVRQASMNNNVNNNKSKDIWSSSNTEEREQIREFWLSLSESERRSLVKVEKEAVLQKMKEQQKYSCSCSVCGRKRLAIEEELEVLYDAYYEELEQYANIQRNLANTESVNASDEGSDKSQKGIISDSPKLLSIPLNNVPSKSLNDDITQDELNSSNADVDEEVIETTSLEEKNVDNQEFVTSISNGNQTLEDTSHSPQTQPPFQPPYPSKADEKNSYHSDLYNFGSSLTVKGGILTVADDLLKNDGKKFIEMMEQLAERRMQREDNSNFHEPELYESGLEYDEDEEEDEEDVDEDELDLMTDEQRMEEGRRMFQIFAARLFEQRVLQAYREKVAQQRQAKLLEEIEEENKRKQERELKKIREKEKKRDKKKQLKLAKEEERQRREAERLAEQAAQKALEAKRQEEARKKREEQRLKREQEKKQQELERQKREEKQKQKEREKKLKKQQQEADREKMAREQRLREEEEKRILEERKRREKLDKEEEERRRRELLEKESEEKERRLREAKIAAFFAPNQTKEGSDGCTTSSQLGLFEKKGDLVNDEDKLSSHLLDSVPNALRQAPIGLKNTNNLSERNASSNLLNSSLFSSFNSVNPLISLEPNPLNRTLNNSVNLTDFGRKPNGLHSPSSLLSNSNNFGLNPNARHSLSRANSPVHHYPFATPPSQRANKYPLNNGANVPALLNSFSSPQLSPLVNRVLNEPSSSPLSSSSLKSPLSKEGVLNQQGHEQYNFSLSPSIRNKLSPICRPSQGSSPKLKNNLSNTEERMGSRALLDDKTDSVITASNSTTSGLSRDESSNPNNYELLNAFNQNTWKISRSTSNKSLIPESPWGVALGAFTPNASTQSIPWGNRTWTD Q09866 YAG1_SCHPO MOD_RES 394; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 397; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12G12.01c; CHAIN 1..905; /note="Uncharacterized WD repeat-containing protein C12G12.01c"; /id="PRO_0000051489" MLNRSKKRNGCYFWVNGSSDEIRYVAVKASPKVNWKTHIIWRSLKNVKCIDSFHGNNEILGAGSSTGNISLLSVKHPEFQAVVTPGYARPCNSLAFSETEHLVAGFAKSRNESSLKLWDLNSLLSDPKSSPLMQSSTLDGVSSVCYKKDTPLLLTGSTSRSVHIIDTRQQLDSVSSVNTQYYSNIVVDPFSPNYFAANSYDGDIAIFDTRYFKSDNYLQIILRNENKKPKNPQLFALKYSEWKPGQLAVLSNNSITLRQLLPCVNGNEGSANNSVFVNYEKKYPVKPNSQCSGIDFFTPSTAFPTHVQILGVINEQPKLFSVHDEVIPFSFNPYNDLIFSFKEKLYPLNSSPFNTLSDVPQFDVSEFVDENSFDSSSSCSSKVFLTTRNNSINSEDSAHEVLLSYNRVLGSDIQGTILDRVKKGYQFDSQKNSELVSDLYLKDLWSWIHLSHRQSEESLFGDTGDTDFSYQGALGIWFMDTELTSMSDVFEAKESKFLEKKILRLARDVIERLDLDIFTSIQTKRPLRQLALLACGLGMSNDDLLLEIRRLIRKNEHVKAAGLALFHGKIENVVRILSSGNELEKTISTAVAGYITSQGLSNFGSDSLWKEMSRNLSTELEDPYLRAIFAYVSNSDWRDVLDEVSLSLKDRLGIALRFLPDDDLSNYLCDLCHTTVQSGDPEGLLLTGLTPLGMELLQNYIDHTSDVQTAALIAAFVVPKKFLDKRAEDWTESYRELLNRWKLYRERAKFDIFRTELSKNHTGEITRKATEPSIRIICNFCRKPIFPFSNRNECNNLPTPIQRGVSKAGPAKHLGKSCPHCGQPLPKCSVCGFSLGDEDVPQKDDFSQKPQNYVKEVNLQKSRFGLWFSFCLNCGHGAHASHASEWFSTHTICPVPNCDCECKLK Q09868 CIP2_SCHPO PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:16407405}. SPAC12G12.03; CHAIN 1..576; /note="RNA-binding post-transcriptional regulator cip2"; /id="PRO_0000082018" MAEGTSQRPLTPLSQAFLSTNTLSPASSPLTFHSEAASLRRKRSNFFPKLDELNGAQDEEMRGLNIPGGSGYLENRYGRDKFTFSDAAVNSAGMGGSGIFSHNNADDGLGDGSSTVLPSSLKQMLDPEISTANNPSAKPRRTRLQTAWKEATNSAGLSLRSASALDVLKNSGPATTSLLSSTTYPFDSLNAFNEPSHSHVPNSASSTALSRGMSNSVTLTAPPEPDEETIPTAIVIKNIPFSLKKEVLFKVFTALDIPRPYAFNYHFDNGVFRGLAFANFHSPEEAKTVVQVLNGYEITGRRLRVEWKRQLPPAERERVERGKQEKRAVEERKNQLKSPFSVANIGAGIDFDLNDPAILNVYSHILLFYYRSDNTNDLVFDSSTTQEERRVAALLASRLNLNHSVTGDGEAKQVVITMPSTHFTPANNSSANHSPLMAPNASTLNPSSLGASNLSQPSLANHLSSSGLFDNGLFSSGGLSSNFSSLRRPAPSMHLADSIRSLRGLNDSKAFSDIRSMPATPLELATPFANLNVSSPLDRNATNSSNTLNGSAMNDYFASLTPSNTGAIGSRTFTKN Q09873 WDR21_SCHPO SPAC12G12.10; CHAIN 1..420; /note="WD repeat-containing protein 21"; /id="PRO_0000116429" MSGLPFHIPGYYYNSEKKRYFRIISSGQSTPSSNIYTKERLKRGKRFNNISKERTKGKGGNPVFNFSTYLFDRQFSQYPYSCNDDRDYLCAKNLKKINLRQLPVGTELQKIGWLREVNTIILTSKNGDILGCCLTPEDKSGVANEKYTSEGSIQDFSLSRIGLSNNPISSLVCNAMQIFWSTSPSLQNEGQFHISTYNQLLGESNNYRWGSLKLLKTPLCAESIGEMGFAVGGTSKIAIINREGKLTQSLQSKGDVFSLKYLGDNLVIAGCRNKSVLVYDLRTKKECVQRFYHGSSICSMQNLDFSQPKLLVSGLESKISLYDCRFLQSKKRPQSIMSYMGHSNLLERNLALMKNENGSIFSSAGDDYVLRFWKTDCSLPFKEMRVDDGKYLCRDGSWVKAMNGTGWVLPYGRGLLIYEP Q09877 SIF3_SCHPO MOD_RES 42; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12G12.15; CHAIN 1..472; /note="Sad1-interacting factor 3"; /id="PRO_0000097759" MSTKDKLNLPPKRTINTRLSTPVHIPPPINSESTRITPQHGSPPRFGDHRISAAQGLFQRRRNARKIDHPLGWFLKNRHAAAHIPQRTTKTSQKLVLLPENHAVNSFNEEESNYEDLLTPSDAYNLIKLENLPRDKREELGFPRATAYCVCEAFQLPKVKHFLKHYHKVRAKKYDEVLYAVYHLPLVYGRSESCRVSSGPAPDDMPSSASNHNQKHLDSDKPDNENFDSHIISQLYRISEIFVFSYGVVVFWNFSLSQEKDILADLTFGGDNSLMVKPLAEEECEIEDLHFHYAPNTKRPRIYNDMIHIPSADNKMKLAMSHALAQSVKLSRFELRTDVTMNSALFYPKKLALYGHLGLSRVEVVRMSGHLFQLRVDVNLISNILDTPDFLWDSEPLLLPLYTAFREYLEIGPRTNVLNRRCKVIFDMLDIFGKSSADRKMNSITWIIIILISLFVIIFTLEVILRLRWAHR Q09878 MET10_SCHPO BINDING 658..669; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 788..798; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.2; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; Note=Binds 1 FMN per subunit. {ECO:0000250}; SPCC584.01c; CHAIN 1..1006; /note="Probable sulfite reductase [NADPH] flavoprotein component"; /id="PRO_0000199948" MVATDSSDQVAKFDVSHKIIEDIVYSLSNRIFSYAEHVPLNRYLTQWNNSGRRNGFSNNVELFNLEARSGASAFLLGSYTAAISSPGVYSMMTPSSCLSLLNPLLSNIIPFYGASKPLVVHVAALAYLEQTYCADNVSVLDFSYANNFTVFASQSNVEAAHLALASTLAAKAAPVIHVYEPDAIVTTTDPSLPLLDSNAVVECFNSYQSEADPVSNASKALKHVNDYFNTSYAPAEYYGSQTASKVIVTFGKSETVAARALLAANPDVGVLSIRIFPFVAENIFNVLPTTCKSLVVLSQVRSTAVGTSSIYYSFLLATLLSTKPSALAISEHRYSLVESVTLSSLFDALHETLQLKAATPKAVHVDKSINVWESDVGDSLVLSLVSAYRTDKSRSVAFRPLFDNLTLAGVRFTVAQVSTANAVLTDVVKDVDADITILTTDRLPLHYRVLAKAAEHSICLLQSSIAPDEATKKLPYEFIADALEKGVKLVLIDPKKFAIDASNLPLLVSFIQLVKPGLGVDEALAVLAKQNNLTDTNLKDAVDSLKQSLSFINLDASALKDREPSEKELPSTAKETSFAPNAVKTLDEDITPQSSNWQTVAKQIIFPEAYKKKDALRPDVSEKVFTVHVRANKRLTPAEYNRNIFHIEFDLGDSGLTYDIGEALGVYGVNNKTHVHDFIEEYGLDANELIHVPSIQHPGHWETRTVFQALCQNIDIFGKPTKKFHEQLLEFETDEKERADLQILISPAGAPDFKRRAEVDMLTYADVLKEFKHAKLTAAQIAQIVPVIKRREYSISSSQKKHNDSVHLLVVVVGWKDGMGRDRYGQCSHYLSNLKVGEPLCVAVKTSVMKLPTSPLKPIVMAGLGTGLAPFRAFLQFKEWQRMQGIESGDILLYLGSRTQREEYLYGEDWEAYHSANLLTHIGQAFSRDQPYKIYIQDVMRSTKDMLKKALMDEGGSFYLCGPTWPLPEITSVLEEVIQSSYDEPVDARKIIEQWKEERRFVIEVY Q09885 SVF1_SCHPO SPCC584.11c; CHAIN 1..380; /note="Ceramide-binding protein svf1"; /id="PRO_0000072334" MKAWLQSSISYYTGTAEPVYGPEAIQPVTASVQGINPFHRLEADDFKWSTPSSSHVETQVFYIKPNEGDYMCFVQLIHSNLGSWTTTAQSTCRIFDLKHPENDLWTSTNMDQFSFENDKTSFVAKNCSVVLEDQKRYRIRASINMDSIIDITVHQDAPPFKIGEDGNSTYGTDPSKPWASMKHTFWPRTRVEGSIVARGRVVDVTGPGMFVHALQNGKPHHLASSWEFALLQHKKFTAIMMQFKTPPSYGSTIVNIGGIAMKDKIISATVDNTIEHVETTLDPDTEWHEPTRISYEWDGKDAETYTEDIHLSVDAPLGRRLQRIDVLAEIPSWLKGFVHGVSGTKPFIYQYFSPVKFTLKMGDEVIEDEATLFNETTFIS Q09889 YC9F_SCHPO MOD_RES 584; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC584.15c; CHAIN 1..594; /note="Arrestin domain-containing protein C584.15c"; /id="PRO_0000116541" MNKIKGGRHKSPVKLFEVRLYNAEANVIVLYGNSMDTSARLSGIVVLSVSSPIRVKNIKLRLSGRSFVCWADESRHASPGNRIRRQVVQILDKSWSFLAPNESAKVIDQGNYEYPFYYELPPDIPDSIEGIPGCHIIYTLTASLERATQPPTNLETALQFRVIRTIPPNSLDLMHSVSVSDIWPLKVNYETSIPSKVYAIGSEIPVNITLYPLLKGLDVGKVTLVLKEYCTLFITSKAYSSTCRKEFKRALVKKTIPGLPMVDDYWQDQIMVKIPDSLGECTQDCDLNCIRVHHKLRLSISLLNPDGHVSELRNSLPLSLVISPVMFGARPTEGVFTGDHNSYVNENILPSYDKHVFDVLWDGIPSENPQLQSGFTTPNLSRRNSSDFGPNSPVNIHSNPVPISGQQPSSPASNSNANFFFGSSPQSMSSEQTDMMSPITSPLAPFSGVTRRAARTRANSASSVFNSQLQPLQTDLLSPLPSPTSSNSRLPRVRSACTLNVQELSKIPPYYEAHSAFTNVLPLDGLPRYEEATRPSSPTESVEIPSNTTTIAPSPVPTIIAPALPSTPAPPLPSHPMATRKSLSSTNLVRRGVR Q09897 CHR3_SCHPO MOD_RES 393; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24B11.10c; CHAIN 1..932; /note="Chitin synthase regulatory factor 3"; /id="PRO_0000076206" MKDSHSSRRKYEKEKLVFATNNGKRTEGTPAFLKSGNTASSSSPTLQFRPTSRYPTLSHEPVYTNVLDLSSRIDANRASIMSATMGTPPSALKFSKKKISRPVVSEDTFKDKLPRATIPVKPEPQPQYKIPAAPAPTSKRVVNRGLKLNTNLRQASPILPSPSLKLDRQDAPIQINHEQKEDFLVSIPRPTPMTNLDDGKDEIGQPDPHRKYMAPPRVNSISRVQRRMSYIPYGGFDDFLDNYYKDDDTVLEDNQLKSNSRIETLEEEDGAESDSITNTVSNASSDAEPAHRHLGPVYENSGHLPSKSHFSSTDSNTDSFGLESDERSLPSVSNDLKSSETLKNPRNDDLLTLQQPPRYPHSQMVMLPARSPVEVPAPTFDRRNVSRNSNNNSPEGYDNNRTNPTVNNLPSYPTNLARPKAIKPMPTSIHGQTSPLSPIPPVHTTHGLVSDIRPLPSVSSPIMRADSTPISHNLAVTPSFSPIPQQSNKSIGNHKNTSVANVSSKVANSKFERNISMMSNSNASSPAIFEVGAEAKEKTKDAIPCHPDDKLMIPSPKIVTHGDAMQEEQRLRQKSQITPDDEVELAKVYLNALETLENKPSLAPDQASYNTRINVYRTRAVELLKKNAYPSKTQNTVPEALFLIGQFHSQGVLGFRRDLGKAFELYSLAAKKGHPLSNYRVAVCLQTGTGVKPDTSKCVAIYKKAAEMDVVEAMFRIALIYLNGLLGQKRNISLGVQWLERACKSKGPESVRAMYELAKIYEQPDRYGVSATPERKFELYKQSAVYGYAAAQCKLGECYEHGLLGCLAEPRRSIFWYTRAAEQDYGEAELGLSGWYLTGSEGILPKNGEEALLWAHKAACKGLAKAQYAVGFMMEQGIGVAADPSSAHNWYIRAAKQGFPKAKKRLEEQALSSKQTHSKAPKKKQQEQCVVM Q09899 HEM3_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61; COFACTOR: Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; Evidence={ECO:0000250}; Note=Binds 1 dipyrromethane group covalently. {ECO:0000250}; MOD_RES 251; /note="S-(dipyrrolylmethanemethyl)cysteine"; /evidence="ECO:0000250"; MOD_RES 327; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 329; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24B11.13; CHAIN 1..336; /note="Porphobilinogen deaminase"; /id="PRO_0000143043" MPSCTSFPIGTRKSKLAVIQSEIIREELEKHYPHLEFPIISRDTIGDEILSKALFEFKRQLAKSLWTRELEALLVTNQCRILVHSLKDLPSEMPDGMVIACIPKRSCPLDAIVFKAGSHYKTVADLPPGSVVGTSSIRRRALLARNFPHLRFVDIRGNVGTRLAKLDAPDSQFDCLVLAAAGLFRLGLKDRIAQMLTAPFVYYAVGQGALAVEVRADDKEMIEMLKPLQHQETLYACLAERALMKRLQGGCAIPIGVQTDVLAISNSSYRISLLGTVLSADGLRAAFGNAEAVVSSEEEAEELGITVALALLKNGAGPILEEHQRSSDSEESLKNY Q09900 RL38B_SCHPO SPAC30D11.12; CHAIN 1..74; /note="Large ribosomal subunit protein eL38B"; /id="PRO_0000215444" MPRQVTDIKLFLQLAHRGDATSARVKKNQNKAVKFKLRCSRYLYTLVVADAKKAEKLRQSLPPALTVTEVGKKA Q09903 DRS1_SCHPO BINDING 303..310; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC30D11.03; CHAIN 1..754; /note="ATP-dependent RNA helicase drs1"; /id="PRO_0000055086" MLWNTQYFRIEGMISLGWPRLAKTSILKFVPIAQNHRIRKMKVQDDFILTIDDSEDDIHYDDYDADAVDEEMPSNVELKKKSKKATPAKDSDFNGEFLFEADVNKDLSSATDMNWDFDMGSKTESNRASNTVDLDAIISRNRKPDDDEFPSSFPSEEELQEPEQENIDSDDEDLAIDGFGAGAIAENEDESSQDESESEEEDDITEPVPSFANISTQDFNSDSAAGSSDSEEDEEEIAKKNAFFAEGDKEKSMMTTTHSSFQSMNLSRPILKGLSNLGFEVPTQIQDKTIPLALLGKDIVGAAVTGSGKTAAFIVPILERLLYRPKKVPTTRVLILCPTRELAMQCHSVATKIASFTDIMVCLCIGGLSLKLQEQELRKRPDIVIATPGRFIDHMRNSQGFTVENIEIMVMDEADRMLEDGFADELNEIIQACPKSRQTMLFSATMTDKVDDLIRLSLNRPVRVFVDNKKTTAKLLTQEFVRVRPQRELLRPAMLIYLCKELFHRRTIIFFRSKAFAHKMRVIFGLLSLNATEIHGSLSQEQRVRALEDFRDGKCNYLLATDVASRGIDIKGIEVVINYEAPATHEVYLHRVGRTARAGRSGRAITLAGEGDRKVLKGVFKNSSAQNTKLVNRNLDFNKVEKFGKEIEELEPVVQKVLDEEKQERELKIAERDLKKGENIMKYGDEIRSRPARTWFQSEKDKQASKASEAKDKKSLAKRKKQMEKEEVPRAYKKTKNDRLSNKKSTKKSKSKRK Q09905 AP3S_SCHPO SPAC30D11.05; CHAIN 1..165; /note="AP-3 complex subunit sigma"; /id="PRO_0000193823" MIYAVFIFNNKGKPRLTKFYTPIDESIQQKLIGDIYAAVSTRPPTACNFLESNLIAGKNRIIYRQYATLYFVFVVDEGESELGILDLIQVFVEALDRCFNNVCELDLVFKFQEIHAILAEVVSGGLVLETNLNEIVLAAQNQMPKTKRSNAMPFSNTLSSFATRF Q09912 PSI1_SCHPO SPCC830.07c; CHAIN 1..379; /note="Protein psi1"; /id="PRO_0000071130" MVADTKLYDCLEVRPEASEAELKKAYRKLALKYHPDKNPNGEKKFKEISLAYEVLSDPQRRKLYDQYGITEGNAAPPPPGAEGGPGAGFGGFPGAGPGGARTFHFNMGGPGGAQFFSASDPNDIFERVFGHAFAGGGGMGGGMGGMGGMDDDMDMDGGFGTRTRGGGMPGGFANMFGGGGAGPHARRSHPSFGGSRPSQPPAQNEVITRPLNVSLEDLFTGCTKKMKISRHIIDASGQSVKADRILEIKVKPGWKAGTKIKFAGEGDEKPDGTVQDIQFVLAEKPHPVFTRSGDDLRMQVELSLKEALLGFSKQISTIDGKKLKVSSSLPTQPGYEITYPGFGMPLPKNPSQRGNMIIECKVKFPTELTPAQKTAAEAF Q09913 ALLC_SCHPO CATALYTIC ACTIVITY: Reaction=allantoate + H2O = (S)-ureidoglycolate + urea; Xref=Rhea:RHEA:11016, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:17536, ChEBI:CHEBI:57296; EC=3.5.3.4; SPAC1F7.09c; CHAIN 1..342; /note="Probable allantoicase"; /id="PRO_0000205913" MSVENVERLSPEQADAFFGQSSVDLISRALGGQVLGCSDDFFASCENLINPADPIRKAGVFVETGAWYDGWETRRHNTAPCDWVIVKLGPSSGRVTGCEIDTTFFNGNHAPEVSVEAAFLPEGNPDAKTNWTPILPKLPCGPTQRHIYRFKEIPQQNFTHVRLCMYPDGGIARFRLYGNVVPVFPADLDARLDLAHMYLGGLVVQCSDQHFGKKDNLLLPGRGVNMGDGWETARSREKGHVDWVIVKLGARGYIDDALIDTNHFKGNYPKEVILEAIDSPDHIPGPDAQWVTILPARKLGPHMEHVFTNLQNNSTPMTHVRMIIIPDGGVKRLRIYGRRAAN Q09918 HSP35_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000250|UniProtKB:O74914}; SPAC1F7.06; CHAIN 1..251; /note="Putative glutathione-independent glyoxalase hsp3105"; /id="PRO_0000157855" MDERHEAAGETSEKPKVLFLLNSYYGPFYDDGDNTGVNVVDLYEAFKVFEENGFDIVIASDTGDYGFDDKSFRDPAIVDETQSIFSNPDCSLMKKLKNIARLDRLNPSDYVIVYIPGGYGCSFDFPHAKVVQDFLYRFYETKGIICAVAQANIALAYTTNSDGQALCTNRRVTGCTWKDEVQNGVLNVMNRLNFYSFGHIAENIGAIFESPPVYVEDPFIVEDGQLFTGSNTNSAKGVAMEAVRAVLNYDG Q09923 YAKC_SCHPO ACT_SITE 56; /note="Proton donor"; /evidence="ECO:0000250" BINDING 126; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 208..218; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250" SPAC1F7.12; CHAIN 1..340; /note="Aldo-keto reductase yakc [NADP(+)]"; /id="PRO_0000070398" MSIPTRKIGNDTVPAIGFGCMGLHAMYGPSSEEANQAVLTHAADLGCTFWDSSDMYGFGANEECIGRWFKQTGRRKEIFLATKFGYEKNPETGELSLNNEPDYIEKALDLSLKRLGIDCIDLYYVHRFSGETPIEKIMGALKKCVEAGKIRYIGLSECSANTIRRAAAVYPVSAVQVEYSPFSLEIERPEIGVMKACRENNITIVCYAPLGRGFLTGAYKSPDDFPEGDFRRKAPRYQKENFYKNLELVTKIEKIATANNITPGQLSLAWLLAQGDDILPIPGTKRVKYLEENFGALKVKLSDATVKEIREACDNAEVIGARYPPGAGSKIFMDTPPMPK Q09925 LCB2_SCHPO CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 398; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC21E11.08; CHAIN 1..603; /note="Serine palmitoyltransferase 2"; /id="PRO_0000163861" MAQADFVSPTSIDVSEKKEVEFHKKVDHVENPPLSTESAKLEAEEVAAEKLNSEHLLENEFAPITDPTHRRVSKNPDGAELFQFEDEPSYYYVVATYLTYLVLIIIGHVRDFFGKRFHKDDYKYLKDNDGYAPLYNHFDNFYVRRLQHRINDCFSRPTMGVPGRVIRLMNRYSTDSNSTFKLTGDTSLALNVSSYNYLGFAQSHGPCATKVEEAMQKYGLSTCSSNAICGTYGLHKEVEELTANFVGKPAALVFSQGFSTNATVFSTLMCPGSLIISDELNHTSIRFGARLSGANIRVYKHNDMTDLERVLREVISQGQPRTHRPYSKILVVIEGLYSMEGNFCDLPKVVELKNRYKFYLFIDEAHSIGAIGPRGGGICDYFGISTDHVDILMGTFTKSFGAAGGYISATPNIINKLRVTNPGYVYAESMSPAVLAQIKSSFLEIMDNSPTSAGLERIERLAFNSRYIRLGLKRLGFIIFGNDDSPVVPLLLYNPGKINAFSHEMLKRGIAVVVVGYPACPLLTSRVRFCFSASHNKADMDYFLRACDEVGEKLQLKFSTGAAGEDVGKTNVEKMKKNQGWFKPPRWKIEDVLKHGVHDALTQ Q0E7J8 REV7_SCHPO SPBC12D12.09; CHAIN 1..213; /note="DNA polymerase zeta processivity subunit"; /id="PRO_0000361056" MENDTGWSVKKCIDIFGEFLLVSIHCILYARRLYPQDLFIKARKYNTIVWQSRHPILCEYIEEVVQSCIEELQTGSVHQVALSIINKEQREEERYVFSTDSIPIIPDFLLEKQISTNEPFTDAYVEYMRASLIQLLNITNGLPLIEQECTWTLRVTLKDGFPRPKQWEEWFLPPQARETDATRQFKGITIPVRNVDIGPMMTEIWVEKYTNSD Q10061 LHS1_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; SIGNAL 1..21; /evidence="ECO:0000255" SPAC1F5.06; CHAIN 22..848; /note="Heat shock protein 70 homolog lhs1"; /id="PRO_0000013557" CARBOHYD 134; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 247; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 359; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 457; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 462; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 488; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 555; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 632; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 678; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 733; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 817; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKRSVLTIILFFSCQFWHAFASSVLAIDYGTEWTKAALIKPGIPLEIVLTKDTRRKEQSAVAFKGNERIFGVDASNLATRFPAHSIRNVKELLDTAGLESVLVQKYQSSYPAIQLVENEETTSGISFVISDEENYSLEEIIAMTMEHYISLAEEMAHEKITDLVLTVPPHFNELQRSILLEAARILNKHVLALIDDNVAVAIEYSLSRSFSTDPTYNIIYDSGSGSTSATVISFDTVEGSSLGKKQNITRIRALASGFTLKLSGNEINRKLIGFMKNSFYQKHGIDLSHNHRALARLEKEALRVKHILSANSEAIASIEELADGIDFRLKITRSVLESLCKDMEDAAVEPINKALKKANLTFSEINSIILFGGASRIPFIQSTLADYVSSDKISKNVNADEASVKGAAFYGASLTKSFRVKPLIVQDIINYPYLLSLGTSEYIVALPDSTPYGMQHNVTIHNVSTIGKHPSFPLSNNGELIGEFTLSNITDVEKVCACSNKNIQISFSSDRTKGILVPLSAIMTCEHGELSSKHKLGDRVKSLFGSHDESGLRNNESYPIGFTYKKYGEMSDNALRLASAKLERRLQIDKSKAAHDNALNELETLLYRAQAMVDDDEFLEFANPEETKILKNDSVESYDWLIEYGSQSPTSEVTDRYKKLDDTLKSISFRFDQAKQFNTSLENFKNALERAESLLTNFDVPDYPLNVYDEKDVKRVNSLRGTSYKKLGNQYYNDTQWLKDNLDSHLSHTLSEDPLIKVEELEEKAKRLQELTYEYLRRSLQQPKLKAKKGASSSSTAESKVEDETFTNDIEPTTALNSTSTQETEKSRASVTQRPSSLQQEIDDSDEL Q10062 PPOX_SCHPO BINDING 7..12; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 32..33; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 40; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 61..64; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250"; BINDING 466..468; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX; Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; SPAC1F5.07c; CHAIN 1..490; /note="Protoporphyrinogen oxidase"; /id="PRO_0000116445" MSIAICGGGIAGLSTAFYLARLIPKCTIDLYEKGPRLGGWLQSVKIPCADSPTGTVLFEQGPRTLRPAGVAGLANLDLISKLGIEDKLLRISSNSPSAKNRYIYYPDRLNEIPSSILGSIKSIMQPALRPMPLAMMLEPFRKSKRDSTDESVGSFMRRRFGKNVTDRVMSAMINGIYAGDLNDLSMHSSMFGFLAKIEKKYGNITLGLIRALLAREILSPAEKALKAALLAEPKTAELSNSMKSTSMFAFKEGIETITLSIADELKKMPNVKIHLNKPAKTLVPHKTQSLVDVNGQAYEYVVFANSSRNLENLISCPKMETPTSSVYVVNVYYKDPNVLPIRGFGLLIPSCTPNNPNHVLGIVFDSEQNNPENGSKVTVMMGGSAYTKNTSLIPTNPEEAVNNALKALQHTLKISSKPTLTNATLQQNCIPQYRVGHQDNLNSLKSWIEKNMGGRILLTGSWYNGVSIGDCIMNGHSTARKLASLMNSSS Q10063 EHS1_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPAC1F5.08c; CHAIN 25..486; /note="Calcium influx-promoting protein ehs1"; /id="PRO_0000021160" CARBOHYD 33; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 49; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 59; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 82; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 93; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFFFSTHLILKILFFWSITRNIFGATYTSLLLNNTINGNINDQSTAYYNLTWEGNTAYNVSLTLSTCTAFDGANDLMLYISNNTFDEALPLDNFTITASENGLATIFVTGYSPLYIAVSSAFSQFAPNFFVESGESTLEGNNVINYELAAGIDTPFSQYNATKFLFAQDTDFQAALLITGNLTTNETSIIPSYEIYVNPSNSTYDNTFNKFSSSFCAFQNNPSTVNTNNADRSMTLRGLGPFAKEQFYLKGLDPNVTYTAYLVEPNIGQPGGTVYPGVTFTTKTSPACQLIYDLQFCSEVAYAVPGNSSLFSASALAEWYDQQAYGYYQNFTYTLDLIPCNATSWSAYSLLKNCSDCANSYKNWLCASVIPRCADINDNSSYLIYKNYDSRYPLIDEVIQPGPYKEVLPCSYLCYSLASSCPLDLGFACPKAGYGLEFSYGEVSNVTGLITCNAPGVEFYESGSALLNISWRTFFISLIFWILFVE Q10064 YAMB_SCHPO SPAC1F5.11c; CHAIN 1..3655; /note="Uncharacterized PI3/PI4-kinase family protein C1F5.11c"; /id="PRO_0000088855" MEDGFEKSLSSSIELLKAESTEIEEKIKLTKILITKVSSISSDASQLYAELIPLLLDFLRNTEVNLYRNSSVNELKIEALTLIQSCAHRDEFKQYAQSCVLSFISLIKADNEEVAVFCLKVIMDIFKTFKFCIESTAQPFFDLVLELSTNLPYLIPSIFVENPKSNEEENTTLAFGSYLSTETSIIQQRVNSLAISTQPLELASQSFRVYVECPVIIVLILQAYRQAAFPGVQAIIPCFLKMVQIDVPIDIASYAMIEKDSSIDFIEFIRNKYQYRNFFMAQVKTLSFLAYILRTHPNTLSEKDIIPDIVIKLLRRCPFDMCFARKELLVATRHILSTNLKSLFVKKLDFLLDLNILLGNGVGTQKLLRPLAFSTLADLLHHVRDELNETQIRKSIMIYSTNMHDLTLSIGLQTMGARLILNMVDRMISLPSIPDAIFLLLSIFDSFVNKFSELNDSLDQFFKKKYEEEIKETKSPTRSSPRDLSSFSTSVNDGSFLFKNLMFGLRALMYGLRTCKSRCIEIGGEQFSGFLTNIKPFEAVTFQKLFFEVGKGFSYFRPEQVYLETFFCCEEESLDRPAISTLPRNKDEKDCLEVFATIFIHLEPSIFLKVFETNLPTFFDQLKKNLTLFHIPQFLLSNESTSSKFLNILLRFLLSRIEELGSSDIRHGSVLLRLFRLSFVTVSMFATENEPVLRPYVSEIIVKCMKLAPNSANSLNYYYLLRALFRGIGGGRFESLYKEVMPLLHALLEAFNSLLISARTPKEKDLFTELCLTIPVRLSLLLPYMSYLMRPLVMSLKSSQELVSQGLRTFELCLDNLTPDFLDPIMAPYIEDLMNALWSHLQPLPYNYNHSHTALKILGKLGGRNRKLLDRVQSLKNSPEPNNDFTLLLSIKGVKQPQLLHYTQYVDEAVNLLSSPSSDLEVKQQAFTYVCNISKLYVYKSDATNSLASSIRCTADKISKSNFDFRRPYSVIPSRMTGRSSFTQLSDDSDETIILASATYGLFFATTVDELREEAYFWLEKLAVNVIVHDIFYAFDVIQGNHSKFTTNLQKEVIISPHYFAHCLSEVVCNDNSKMGDAVKHVLKFMFSFLESIFENPERAFILPIFEVLLSDFRHKCYDPHWYKKYGGCFGLECLIEQDHSSKWLFDRQVDILTALFFTLKDTTSEVPTVCKDHVMDVLKQLFRKIYASKDTEIAPGILGHLVLELSNHNSVVRSSTQKLLSLLSELSNTPIVKLVSPFKERLLSPIFAKPLRALPFHIQIGHIDAVNYCISLGSELITFSDELIRLIHETTALAEADDDALIGIGKTSHFKNAALLIRLRVVCVELLSTCILKIDFNNPQHAHLREGIIVVFFKSLYAKSKELIEAASLGLKNALQEDQKLSKELLQTTLRPILYNISDYRRLSVAGLEGLGRLLRLLTNYFKVEIGRKLLDHLKALLENVDFQKVSSLPLFCQTEMKIVRALIDLFHLLPNNANRFMDELLICVVEFSLRLQRTFPNYFSEPLLKYVNRYPEDAWKFFMVRYDEAAFTSVFVELLRLKDSDPLLSVVKDNWLFFQTILTNEINTVTANRYSFALDSAIVILQRDPSFFKDKNDFFRGSMDAVLAISHLVENESILESMVFWNDLLVRTSTFLLEVYDLCIYNYDDGLKLLSCFHMYKNSLAKNLVSDLTAHLVKKIEEPDLENNVKLILNLILSKDYGFLLKENLAGILLTYLNQNVSSLEKCNQIFSIFYEVFFQHPSTNVYANDEGIKIGALQIISFFLKNVPEITVQHQTEMLKMCSLFGNSEDVMIKQLSIYVMSLFILRSQFPYELVNVVYMALLKSSPIEVRHLVKSSFDNIFSYIFSEEPESKKSPIWFELPLQVISSQSQNISQLLNVYDFISSHSDIFIEHRGRYVPILIDSLYKFGAIPNPNPEIRALSLGLIKVLLEWNDLQLKVDQKEIFSNNQKRAILSYLFRFVCLFSEPFTEGLCSEAISLLERLLSSGTWASLGMKLSFFTKSITHFDATDANSVMFANSLRTLSIVVGHSDSAWIEENLSDLKFLLEKSLENESVGVQSAIGNFVSTILTLSNTHPSIAGNPIFNDIWTSIASWTERRLQSCSQIEVTLPCVECFFKYKKDALHTLLPGFMRCFHKVAKEFLSLGSQPSGNSLNLQIVNAVDERVSILKSMIELGCSYISYLGDQRRWFLSALVQIIEKSSSYEICNYLLEIVRGWIMNSPVPVPTVKEKAALLLKMVTFEGRFSQNEQNDLFNKYLSFIADIYEMEPYKNSELTFRLEAVYLLGTRVANKKLKERFIKGLNSSFPSDLFSRFQFLLGSQHWESLSNTYWIVQLNIFLSRCFDLNQRCQFYKKPKLFSCFSIYCREFDEDLTSQAQDTEMLHNNLLKYGIIDFNQNSMLVSDFVLPVLSLQFSNSKIAEYLWRDFFNASVCSFTKDEIPLCIGSIISFLSREYHIRLLGKTPNVLETILTSIVSSDMPIPLPPHLLVYLSKTYGLHHYCILLLENSLQNNPGLSEDELTVYHKSCLDALSDIYYSLDEHDLYHGLWRRRANFLETEVATSHEQCHEWEKAQLVYEHAQLKVCTGSLPYSPTEHGFWLDHWILCAQKLNQWDVLFDFSKQEGCAELYLECAWRLSDWSTEQDTLEKATKSLSPFTSLRRHTADALLYLNKTQRKMGSVTEFSRIIDECMQFSLRRWQQLPKRVYQSHVSLLHHFQEIVELQEAFGIYSQLNDTNIHNIDNKLRDIKVVLQGWRERLPNVWDDIDIWSDLIAWRQSVFKSINKVFLPLVSIAQQSTNKSNTNSVSYLYRGYHELAWIINRFAHVARVHHLPEVCINQLTKIYTLPNIEIQEAFLKLREQAECHYESPSEMQLGLEVINNTNLMYFRNRQKAEFFTLKGMFQNRLGEKDEANQAFATAVQIDIGSGKAWSEWGLYHDELFQANPQEIHHACNAVSCFLQASSLLSSSNSKPLLTRVLWLLSVDDSHGSVSEVVSSFKSEIPTWNWIPFIPQLLSALSHRESIHARAILIQIAKTYPQSLHFQLRTAYEDFLMLKKQQAANVLRGNSRLRENDSSSDNKSKDLSPSGSFSSVSQFNSKNGSPSSIDSSEKHQISTVKPAWELIADVTSILKTAYPLLALTMETMVDQIHTRLKSFPEEDAYRLIVALLNDGLQYISRLGVVSKNTFQLPMSQANIQRFAENVLPVSVREAFLRDFVETKLDLLTYVDKLRMWRKKFENILDQRPKFLHLEQCSLYLSEFQHQKFDEVEIPGQYLLDKNNNNDFVRLERFVPNVDLVRGHTMCYKRLTLRGYDGKLYPFALQYPATRHSRREERMLQLLGTFNTVLRSKIEIQNRNFSFQIPSSIPLSSHMRIIADKPSYVTMQTISDEYCKNRGMPLDYGIRFYFDRLQTGLIQLKRASASMLSNSTVEEKKQIFRQRALQLRMQLLETLNSSVFPESIYYDYFYKTFERYCDFWFFRRTFTTQYAYMIIMTYVFNIGGRSPQKLFIVKDSGQVMSQDLLPSMTSNQPVFHNTEAVPFRLTPPIQYLISDLGVEGLLSGLVMSIAQSLSSPTTDIKQYLSLYVRDEVFWWSKQQRKPIPQGIQLFETVKVNVELLFRRISVISHNVPEDLPLNQTLVDLVSQATNPQQLAQMDQLWQAWL Q10065 TRK2_SCHPO SPAC1639.02c; CHAIN 1..880; /note="Potassium transport protein 2"; /id="PRO_0000070463" CARBOHYD 9; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 239; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 283; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 293; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 294; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 321; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 443; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 460; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MQLSGFSTNGSGSLNTIVCEKLLFKPNFVQDSFIIGMTILCSVILYGSGNLRYIDALLLASGSCTQTGLQPVDLTQISIYQQLTILLFGVLSTPITVNLGLTLFKLYFYNKRYDMVITNNKLRMTYTYHTVRRRDTPEPSKVGNRKIRVLLDQGNQMHRPVAPETKAEEAEHQENEKHHRHHFRLRKFANAIDRPSFFRGNTMPALPSYAGVRNSQENEDRTEALSPALGKRRMASIDNGSLSVVQNNARNNPVDFYIPSSFEESSFQTIPEDFEPQVHDHENQTQLNHHLDNNSSISSHNPSLETANDGNQETVSSSNSNYSTTRVDNDPHVASYSPQNSNFDHQAAATTNDAHQNVVRGSAITIAPTPVPRHNRRPIYFADDTNGAEQEKGAHRLDGRGRKRGKSFAVTPTLHRNERSMSVLPFQLAKSFTSALPRRLTFNRTHTKASTMSLPYLSYNATVGRNSAFYALTPVEREELAGIEYESLRILTVILVVYFLFWHILGLVAFLIFIYTAKTSGRVVTDGGINRGWWAAFTSSSLFDNLGYSLNSDSLNSFQKAIFPQVLGTILIFLGNTFFPIMLRFIIWIMIRTTRFSPNFQQALYFLFEHPRRSFTLLFPSKTTWVLFLNLTLLNFASFFFFMVLDLGNSYVDKIPVGYRIMNAIFQNAATRSAGFTVVDLSQIAPAVMVTYMFMMYISAYPIAMSIRQTNVYEERSLGIYAADTENDDDNNINNNNNDNNTPKRKNFLMDHIQRQLSHDLWYLFLGYFIITIVEGRRLESEAEPQFTLFAILFEVISGYGTVGLSLGYKNDPSLTAQFRKISKLVMVALQIRGRHRGLPSALDRAVLMPSDKNFDREEEDYMRRHGKKNTNRADPVPSS Q10066 ARGI2_SCHPO BINDING 119; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 142; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 142; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 144..148; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 144; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 146; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 155..157; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 198; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 247; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 247; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 249; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 261; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608"; BINDING 292; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:P53608" CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742}; SPAC3H1.07; CHAIN 1..323; /note="Arginase"; /id="PRO_0000173710" MSPHKISDNHRHLMLSRFMMGNGVSIINMPFSGGQPKDGAELAPEMVEKAGLVDDLEHLGYDVKLIQNPEFKSRPSKEGPNQALMKNPLYVSNVTRQVRDAVQRELEQQRVVVNIGGDHSLAIGTVEGVQAVYDDACVLWIDAHADINTPESSPSKNLHGCPLSFSLGYAEPLPEEFAWTKRVIEERRLAFIGLRDLDPMERAFLRERNIAAYTMHHVDKYGIGRVVEMAMEHINPGKRRPVHLSFDVDACDPIVAPATGTRVPGGLTFREAMYICEAVAESGTLVAVDVMEVNPLLGNEEEAKTTVDLARSIVRTSLGQTLL Q10071 STE24_SCHPO ACT_SITE 333; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 415; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 332; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 336; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 411; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" CATALYTIC ACTIVITY: Reaction=Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.; EC=3.4.24.84; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPAC3H1.05; CHAIN 1..474; /note="Probable CAAX prenyl protease 1"; /id="PRO_0000138847" MSPGLCFLKEISVIQATPKPTTRSFANCCKMGILQHLMHILDIPGFPWKIVIAGFSIGKYAWDLYLRRRQVPYLLREKPPAILAEHVDEKKYQKALSYARDKSWFSTIVSTFTLAVDLLIIKYDGLSYLWNITKFPWMDKLAASSSRFSLSTSITHSCVFMFGLTLFSRLIQIPFNLYSTFVIEEKYGFNKSTLKIFVIDLLKELSLGGLLMSVVVGVFVKILTKFGDNFIMYAWGAYIVFGLILQTIAPSLIMPLFYKFTPLENGSLRTQIEELAASINFPLKKLYVIDASRRSTHSNAFFYGLPWNKGIVLFDTLVKNHTEPELIAILGHELGHWYMSHNLINTIIDYGMSLFHLFLFAAFIRNNSLYTSFNFITEKPVIVGLLLFSDALGPLSSILTFASNKVSRLCEYQADAFAKQLGYAKDLGDGLIRIHDDNLSPLEFDSLYTSYYHSHPILVDRLNAIDYTTLKKNN Q10076 HSR1_SCHPO SPAC3H1.11; CHAIN 1..582; /note="Hydrogen peroxide stress regulator 1"; /id="PRO_0000046865" MVFFPEAMPLVTLSERMVPQVNTSPFAPAQSSSPLPSNSCREYSLPSHPSTHNSSVAYVDSQDNKPPLVSTLHFSLAPSLSPSSAQSHNTALITEPLTSFIGGTSQYPSASFSTSQHPSQVYNDGSTLNSNNTTQQLNNNNGFQPPPQNPGISKSRIAQYHQPSQTYDDTVDSSFYDWYKAGAQHNLAPPQSSHTEASQGYMYSTNTAHDATDIPSSFNFYNTQASTAPNPQEINYQWSHEYRPHTQYQNNLLRAQPNVNCENFPTTVPNYPFQQPSYNPNALVPSYTTLVSQLPPSPCLTVSSGPLSTASSIPSNCSCPSVKSSGPSYHAEQEVNVNSYNGGIPSTSYNDTPQQSVTGSYNSGETMSTYLNQTNTSGRSPNSMEATEQIGTIGTDGSMKRRKRRQPSNRKTSVPRSPGGKSFVCPECSKKFKRSEHLRRHIRSLHTSEKPFVCICGKRFSRRDNLRQHERLHVNASPRLACFFQPSGYYSSGAPGAPVQPQKPIEDLNKIPINQGMDSSQIENTNLMLSSQRPLSQQIVPEIAAYPNSIRPELLSKLPVQTPNQKMPLMNPMHQYQPYPSS Q10077 SNT2_SCHPO SPAC3H1.12c; CHAIN 1..1131; /note="Lid2 complex component snt2"; /id="PRO_0000072032" MLVIEADSNLLFTAMFDLDKNTNIESNHVKIGNKNTTRRLIIKSSKNSVRIAYAPPEKHFVDVTDRFLLPETETQNLKTRLGIFELEPLPPNGLVCCVLPNGELIQPNDFVLVNSPFPGEPFQIARIISFEKSRPCVSTNLYDSVRLNWYFRPRDIQRHLTDTRLLFASMHSDIYNIGSVQEKCTVKHRSQIENLDEYKSQAKSYYFDRLFDQNINKVFDVVPVTQVKNAPDDVLEDLFKNYDFIVTEYGKGRALLNEPSNCKVCKKWCAFDFSVQCADCKKYYHMDCVVPPLLKKPPHGFGWTCATCSFATQRKKSTFQKENANVDANHATENNLEGQATQKSVSILKGHNKALSNVSLQEDHGKRRNLKSLRSSRNLHQQSRKSLDENKPNSFSNVSKLKRLPWNMRYLDLKSDLTVEKKSDIYPSRARISISPMLPTSSEDNLHPLQPLTTADEEMDLDLKSDERFKVDIPTFFERWPFLKDLPLKGYLFPLCEPNLQSAMLLVPITYSDALLDDYLCSCWNLWKKLRLPVSAFVFLELTITALYETKLSPAAAFEKLKSWMPGFGDPKNCTGKRVDEHKINSLVKEFGVSLQCFVEKLKFEYSLKEIFFSFLSWASSPKGLNTFKKLSDSSLSTTTTDSHGLPTCCYDIGMYDLQKILKLKKTPICRWCHSKRSSEWFVAPPIEESSPKDKSKIVALCQRCGYVWRYYGYPLQQATPSDLRNCDFEPVKKRKADWDHLSNHDNEVKKENNRIRNASSLMENPRVSTKTFDNFTLTHDSTINVKADTVKRARQNNIKNKDDVNFSEDRKKCCALCGIVGTEGLLVCFKCGTCVHERCYVCDDYAENEQMLVSASHLSGRTTRNSASPGIVSGKKSYAKKDQVLSWACLSCRSNDNLGQNNDNHCVLCLQSASHSLMKKTVEGNWVHLICASWTPDVYVPAEESEPVCGIAQLPPNRWEKKCEVCGNSFGVCVSSPNSGLTSHVTCAEKANWYLGFEFVKQDQSPFSMLSNLKSLSFFGNVTEINTNKCMINSWTSLRPVLFGPSEQLPRNFLLRNDIVPNTNNSAWSEYIRNLYPKAYIYLLQYTIAVCKPTIAPTNVACCCSKCNSTMSPFWWPGNICQACHCLRVE Q10092 HSP34_SCHPO ACT_SITE 124; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 125; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 155; /evidence="ECO:0000250|UniProtKB:Q04432" CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000250|UniProtKB:O74914}; SPAC11D3.13; CHAIN 1..222; /note="Probable glutathione-independent glyoxalase hsp3104"; /id="PRO_0000157856" MVLFMKTVQRPEHISLKSCIPFKSLQRQGIVFRLSVRMVMLADDHSISDSALSDSDKNAFKDKNNDFWKAIKNAKNASDINFSDYSIFFAAGGHGTLFDFPSATNLHKGAAKIYSMGGVIAAVCHGPVILPCIKDSTGFSIVKGKTVTAFNEIAEQQMNLMPTFEKYHFKTLNKLFQEAGSNFVDPQEPFDDFVKTDGKLVTGANPASAASTAKAALNSLNS Q10104 GLYM_SCHPO CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; TRANSIT 1..20; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 265; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC18G6.04c; CHAIN 21..488; /note="Serine hydroxymethyltransferase, mitochondrial"; /id="PRO_0000113514" MAVLRQFVKNSYSSIPKRFYALSANQKKLLKAPLAECDPTVYKILESEKSRQKESIALIASENFTSRAVMDALGSIMQNKYSEGYPGARYYGGNEFIDQAERLCQTRALEAFHLDGEKWGVNVQPHSGSPANLQAYQAVMKPHDRLMGLDLPHGGHLSHGFSTPQKAISAVSTYFSTMPYNVNKETGIIDYDSLEKAAIQFRPKVIVAGASAYARLVDYKRMRKITEMCNAYLLCDMAHISGLVAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFYRKGTRSHDKRGNPILYELEDKINFSVFPGHQGGPHNHTITALAVALGQAKTPEFYQYQKDVLSNAKAMANAFITRGYKLVSGGTDTHLVLVDLTDKGVDGARVERILELVNISANKNTVPGDKSALIPRGLRLGTPACTTRGFDEKDFERVVELIDEVVSLTKKINEAALKEGKSKFRDFKAYVGDGSKFSEIAKLKKEVITWAGKFDFPV Q10105 GCN1_SCHPO SPAC18G6.05c; CHAIN 1..2670; /note="eIF-2-alpha kinase activator gcn1"; /id="PRO_0000116458" MSVEEPGIEAHGHKDRMLYAMLLSKDTSLAFLGSKKIMIDILQHICRTQDIDEESAIAALEDIFETLPRNLSRDARKQIEITINHLVSRLPSIVLPFLVRRLTTIAGRLDRFRSTVSVSFDCLNWVNSMIPNLPEKELQYWILELLPLQSSFLSYALRDGKPSVADSAIKSTRRCYRSLFCKKMDSLKKLVSFLLTETENAILPPKSLPLYGVIISTCYYFHQSPNPRNEISQQAELFSKIMAQNVLMAKPALEKYLYHEFCYSLGLLLSVDQLKLYLLPSIEKALLRSPEIIFSGILSSLAHGFADSKVDASSLILSSVLTSFVNGLKSSNAEVRRNCFQTFKDLSANASDNESLSRVASELITSLRTGKVTASDQRVLFVDALSSLSLKHIDASMLLNELLPLFTKAKESDFNSLASLIVKTLKFLLMNGRNPGDKIYDFLSKSLQRPVAHESMFWLTSLATMAWDLPASDDVQIEFINFFLNNLSILTEKALMSVSGATQNGTYLAPIIYLSFGVNKLSVWNSERISHTLELQDILVKLSTPKNNDVFIFSSKITNKLNDDQSKLWYFQGLCDFAKVSDNLLFSNFVERWFQSVIGVFSFASRENSNRALKILKSAILYRPHLRMSICSQLWNYHADFEKSKSVGKFDSAKYDEISSLFQSLILSSMSADTSNFSNQELVDFDKYLVELLFLSFAFKDKFDWIRFCQVSKRDPATLVSERIHSIIEEIELLLSSAIKDSKETAAIASISMIVFVAPEESIPLFVNVFRNQLLHLNISSVSSTDLEIWKTPEGVLWDNVLEKKSSKKLDKNTKDYETKRWEAEVRAKQSAKKPAKLSKDQQALVDAQLDAEAKIRSRVNLIALSLERGLGIIRSLGEAVQLAPALWVEDAIDVLLFHNVLKYSEPFLKNLAYDTFLLTLKASGFSERLGDRSYSSSLASILAHTFSVNSSENIKELTKSILYKLRFAIEQNYFEPQMFACIFPLLYDLTFNITNSDEEDEAELQLLVTEILEFQALYSASLRRMRSKLIKSLLHLLEIAPTQYQENKNSLLSLCEGLHSTYTDEELNLLLSNLFHPESSIRSAVLQALQAFDLSRFEFIKEIFLELYDDNETNASIAHQISTQNGLDATETSFFELQIFFTQDSDYLQQIIGKSLIDLLDEFEELGQFIPKELMRTYRENALPSAPEYDEYGIIKKETIGRDLGRIARESVAVSFFHISKYLSSNLLLPFLEFLLTASEAEAQIPVTDASQKVSSKMLEAGKLAIFQSGAHQVEALMELFEQKLNVDSLPTDANDRLREATVVLFGTVAQHLPSNDPRLAVVMDSLLSVLSTPSESVQLAVAVCLPPLVKKSLGKSKEYYELLSNKLMNSTSLADQKGAAYGLAGLVKGYGIKAFQDFNILDSLSELISNRQNATHRQVALFAVEAFSRILGIYFEPYLPDLLPLLLTSFGDNANEVREATMDAVKQIMSQLSAFGVKLLLPTLLDGLNEYNWRSKKASVEILGLMSYMAPKQLSVFLPTIIPKLSEVLTDSHSQVRNTANKSLLRFGDVISNPEIQTLVPTLLKALSDCTRYTDDALEALLKTSFVHYLDPPSLALVIPILKYGLRERNAGTKRQSAKIFGLMASLTEPENLAVYLESLMPRLREVLIDPVPDTRATAAKALGSLIEKLGEKKFPTLIPELFNVLRSECSEVDRQGAAQGLSEILAGLGLARLEDVLPEILKNTSSPVPHIRESFISLLIYLPATFGSRFQPYLARAIPPILSGLADDSELVQTASLRAAKMIVNNYATKSVDLLLPELEKGLFDNAWRIRLSSVQLVGDLVFKLAGINRKALQEDEEEEGTHSDVSRKALLDIIGQERHDRILSTLYIVRQDIAAVVRTPAIQIWKAIVVNTPRTVREILPTLTSIIVSNLNSSSNDRRTMCVKSLGDLLKKAGFDVLPQLLPVLKQGLESANSGDRIGVCIALEELINSATPEQLEIYSDDFVYAVRRALMDGDLEVRETAAEAFDSLQSILGDRAVDDVLPQLLKLLESENQSEQALSALREIISRRSSTIFPVLIPTLIKKPVSAFNARALSSLAQVAGVTLNKRLPSILNALMESSLASTGDDLVALNGAIDKVNLSVKDQEGLQILMAHFYSFSESEDFRKRLFAAEHMLVFFQNCKLDYYRYVGDWVRHFITLFEDKSQDVVVAAVAAQNTLVSALRKDQLDSLVSIAYHSLRDVGSQGVNLPAFEVAQGVNSILPIFLYGLMHGTMDQREQSALGIADIVLKTEPSKLRPFVTQITGPLIRIIGERFPVEVKCAILYTLNIILSKISTFLRPFLPQLQRTFAKCLGDPSSEVIRSRAATALGTLITLQTRLAPIITELVSGARTPDAGVRKAMLNALFAVVSKSGQNMNEASAEAIEQLLDEISAESSEHMVICAKLYGALFSHLPDAQAKQLLESKVLSLEIQSEFSVLILNAAVKFGSQKIIELKLSDIVCSIISTASLQKEVTIAENGILALGKALLADIPQSFGNAKNLVEALKVNIEAPPSTSQDSRRLALLIIRVVSKENYSLIKPHISILAPAIFGCVRAIVIPVKLAAEAAFLALFQLVEDDSVLNKYIETLEGPRARSFVDYSRRVAVKLAAAERDRINSGSERVKLEEVEDLAEINAVGRDNEVSTNDP Q10106 UTP11_SCHPO SPAC18G6.06; CHAIN 1..249; /note="Probable U3 small nucleolar RNA-associated protein 11"; /id="PRO_0000211051" MSSSFKNAGQRKNHRERAQPFERRKWGLLEKRKDYAQRAQDYKTKQKKLKRLREKALERNPDEFYHEMTHKKTKNGVPLEQREDSTIDMDTIKILKTQDIGWIRHHRNVERAKIDHLEQQMHTVGAHRNKNESRKHTIFVDNVKEAKSFNPAEFFQTTDDLVGRTENRVKKDQIENNELTNQPFSGKLHSKLKEKAATELLLRQKRDKKLAAAEERVELDRLLQGKGGRQKKKVVNGKPVYKWRNERKR Q10110 RRN3_SCHPO SPAC18G6.11c; CHAIN 1..599; /note="RNA polymerase I-specific transcription initiation factor rrn3"; /id="PRO_0000211429" MPSIISSTNPQYINKCVNNGTMASSTNVPDRTVGSKSFASSVSKNDGRLMQQMLRAFVNKALDDKAEGNFAGYEDLRRQFAAKSDTKDAPSSLQLQNLLSALTCNVSRLDSSNSSLVMSVLDSVWVSRDESFVRCYTRFLGNLISAQSNYLPLVMTMLIQHMLYRPDSLAIHYEHAHMALKYVLELVPRAHSFLYSSILEEFPYKDESLLAQMTYISNVLSICEYVPSIKGPVLHAIIDKIIQIDVEIQVEVDDDDEEEDEVVTDDDGTSNADSEVITASTLYERHTAISSEMTSSTILTPPSLTDTRQLMQQLDQLLYTLFSYLDSNLKSTSRDRYLVYNSLIKSFVNTVLKTFRCRYTQFLIFWASQLDPEFTDIFLGVLTEVCLDPSQPYTLRLSGAMYIGSYVARAKALEKNTIQIIVNMMTRWVEAYLDQCENELSDDLLSKHSVFYAINQSIFYIFCFRWRELCVSDESESMEPRPNEWIPGLEILHRSVLSRLNPLRYCSPNIVLQFAKVANHLNFMYVYSIIEQNRKGIFREGFDTMDAYFPFDPYRLTKSSIIVQPFYNEWQQIPGLDDDEEEEDTDYESSTVMLGESPF Q10136 STE7_SCHPO SPAC23E2.03c; CHAIN 1..569; /note="Protein ste7"; /id="PRO_0000072267" MFLEIILDSATYSFDRVITGKICFETNAATSPRSFQIQLRIKGYAVYHHGFLSSPSHKHPTTASASDSDEATEIFTHSQPLPIPAGPSSKSHAIDFKFKFPSKSASSLPCSKSNDSMVNICYMLKATISKRYAFLGSSQSAKAELIMVPPNLAGKPLSANSSFGSSAKTFQLPEFDSVTPSASLYKQPSFNSNPAPITTSSATHTSQFSTSSSSSVNSVHTPVMVPNPYFQYNSSMTAPSSSSSSVAPFVPRRQFSVSSASDPPQTPISMSPPIPPTPSQFSAFMYQNQQSYLSPQSHYENPLSISSRPSPCCPSTPSSAVTLSNGFDSQSNAYNNSGTGPPMLYKFPQRSYTAPNTSFNSQRRMSSITSLPTASFCPVKHGVSPPSLAGNQPSPLSSPLTNSNVSPSTICSPDNNVTFVNLAPGEKLTFKIEPNDLMDEEEVVENSNMYSIPGKTVATTVCHSSSSSGDFSALSCHRNLSFSESLPTAEDQVHNNHCAVSPSRRSSSNALYLATLPMGYERSNSVSYCSDSSLSSPLPDDNMLQDPHALNMAYAKEFDVLINEVLQSL Q10147 TCPB_SCHPO SPAC1D4.04; CHAIN 1..527; /note="Probable T-complex protein 1 subunit beta"; /id="PRO_0000128319" MSLNPHQIFNESGIQERGENARLSSFVGAIAVGDLVKSTLGPKGMDKILQSNSSGDIVVTNDGATILKSIALDNAAAKVLVNISKVQDDEVGDGTTSVCVFAAELLRQAEIMVNAKIHPQVIIDGYRIATKTAIDALRASSIDNSSDPAKFRSDLENIARTTLSSKILSQNKNHFAQLAVDAVLRLKGSTNLDNIQIIKILGGKLDDSFLDEGFILNKTIGVNCPKVMENANILIANTAMDTDKVKVFGARVRVDTTGKLAELERAEREKMKAKVEKIKSHNINCFINRQLIYNWPEQLFADAGIMSIEHADFDGIERLSLVTGGEIASTFDHPELVKLGHCKKIEEIIIGEDKMIKFSGVEAGEACTIVLRGATHQLLDESERAIHDALAVLSQTVAESRVTLGGGCAEMLMAKAVEEAATHEPGKKAVAVSAFAKALSQLPTILADNAGFDSSELVAQLKAAHYDGNDTMGLDMDEGEIADMRAKGILEALKLKQAVVSSGSEGAQLLLRVDTILKAAPRPRERM Q10150 MON1_SCHPO SPAC1D4.03c; CHAIN 1..513; /note="Vacuolar fusion protein mon1"; /id="PRO_0000116468" MEPTSEHSSIKEEVENDNVHRSHESECGSLLLNPGNVLMAAPSVSEDDQEVSRSTPELRSHVENVEQLLSDILHDNSSPLNVSTSVSSSSNNTAVDEIIKLLSLISFDLAKQKRTYLIFSSSGKPVFSNIVDDSIEPSTVGALQAIISSFEVSKEELTSFSTFSNVIVVLSKNPLYLVGVSPSTTLSAAYLLSELNLLYCQILTGVTAKAMQLTLNSRPNFDLRRLIGSNEQFLKELCDQLNDYELVPTLNAISPLPLRSSFRDQLSQLLLRETPKSLLFTFIAIRGRLVCMVKAKKLLLHANDLYLLFLSLFRTQSFNDSMEHWVPVCFPTLNPDAYIYIYSYFLCKDTVLIMGSSESGVFFEMQSVKCKVAQEIQDHGWLKKLIYCEEMDRTTPRNPGSPCISHYLFYSKKYSQFYTPGYSFSTPNFNTRTLYAIYASLHDQAFHKKNSFSINMTVHESLLLFTWSTASFDFHCIANATTSSQLLIANVNKILRWIRREENRLFIQTNLSF Q10153 PIS_SCHPO ACT_SITE 77; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P9WPG7" BINDING 52; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 52; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 55; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 56; /ligand="a CDP-1,2-diacyl-sn-glycerol"; /ligand_id="ChEBI:CHEBI:58332"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 60; /ligand="a CDP-1,2-diacyl-sn-glycerol"; /ligand_id="ChEBI:CHEBI:58332"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 66; /ligand="a CDP-1,2-diacyl-sn-glycerol"; /ligand_id="ChEBI:CHEBI:58332"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 73; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 73; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P9WPG7"; BINDING 77; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P9WPG7" CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+); Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11; Evidence={ECO:0000250|UniProtKB:Q59RA2}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q59RA2}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q59RA2}; Note=Divalent metal cations; Mn(2+) or Mg(2+). {ECO:0000250|UniProtKB:Q59RA2}; SPAC1D4.08; CHAIN 1..237; /note="CDP-diacylglycerol--inositol 3-phosphatidyltransferase"; /id="PRO_0000056823" MGKNEQKDPNVYFFVPNLIGFTRVFLVLISLYFMSWHPNYCTIVYLYSSLLDAFDGWAARKLHQATNFGAILDMVTDRCATSCLLCFLCAAYPKYAIIFQLLVSLDLASHYMHMYSTLHQGASSHKTVTKKHNWMLRLYYGNNKVLFIFCAANEMFFVALYLLSFTPRTPPKLGYLPVPSFIYSTGELPLSYPTLLAVLCGPICLAKQIINVVQLVNAANALVKMDVEQRRAAKKLQ Q10154 RTF2_SCHPO SPAC1D4.09c; CHAIN 1..240; /note="Replication termination factor 2"; /id="PRO_0000116471" MGNDGGSLPTRNELVKEPGKVPPLDIDFKRSVKSSQFSQCAITDEPLYPPIVSCGLGKLYNKASILQMLLDRSSVPKSPSHIKSLKDVVQLQVELDDSGKVLWLCPITRHVMSDTYQFAYIVPCGHVFEYSALKQFGEKMCFQCNQVYEEKDVIPINPNAEQLKTLSKRLLDLALSEKTHSLNKASKKSNKNGDKKRKHVSKSNSKHAKHELRTNRMLDGENVKSETSVTDMERVKRVKI Q10160 RMI1_SCHPO SPAC26A3.03c; CHAIN 1..235; /note="RecQ-mediated genome instability protein 1"; /id="PRO_0000116473" MNQTTTLSTELTELGVRVQNRWLQSLLDYLAKKHSTGANTTPQLVMQYLVASDIRESTTSEGAAPYIVSEQHNVRIENTMLLQIVRVREIGISIVNQLEYLNDLEELKKLKGQKVIRLVHDESGDEEQNDDDGLTEAQDAVQKGSELKKMCRLILEDSNGQRFWGLERKPIKGIQLSTKLGTKLLVKNVLVRRGVLMLDPNNTTILGGSIEEWDKDYFPKRLIEELKGELSKTKA Q10162 BUD23_SCHPO CATALYTIC ACTIVITY: Reaction=a guanosine in 18S rRNA + S-adenosyl-L-methionine = an N(7)-methylguanosine in 18S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54584, Rhea:RHEA-COMP:13937, Rhea:RHEA-COMP:13938, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; SPAC26A3.06; CHAIN 1..268; /note="18S rRNA (guanine-N(7))-methyltransferase bud23"; /id="PRO_0000116474" MSRPEHIAPPEIFYNDVEAGKYSTNTRIQSIQTEMSERALELLDAEGPSFILDIGCGSGISTQIGESQGHVVVGMDISPSMLSVALESQEIEGDLLLCDMGTGVPFRPGTFDGVISISAIQWLLNADKTCNVPQRRLNRFFQTLYISMKRGGRAVMQYYPETEKSQQMIMDTARKAGFAGGIVVDHPESKRQKKYYLVLQAGGTRTLDISSMTLDQEGTNAKQRKLKKKQDMSTREYIIHKKELNRKRGRLHVPKDSKYSGRRRKAAF Q10165 CNT6_SCHPO MOD_RES 207; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26A3.10; CHAIN 1..923; /note="Probable ribosylation factor GTPase-activating protein cnt6"; /id="PRO_0000074230" MDGSDSLLKSVDVSKLDNGSTISFRAREDGFLESISSSSGKLVDMVLDSTSKECLPKFSFQNKLDFYFLFSDRVLQLQKERKVLVLIHCESLQSFDSFFAQKLKYADLISSDNVHEIFLPDSNAANIRYHWEWSPPSGKLLEYECKNYSCIAVYSTEDCTLERISKFSYYTVSRCGDSMDDTFFSESQRVTSPLTTSQTVQTQPPQSPEAKTELSLINTKTVIFPENYEDGPSFRSMLHELEQKSSLMKYYCKKIMKRIVQLSDAYDASQVAVMKLSETLSEASNSTSMNMDILLDSYLTKAMDIHATFIQKLNYDLINLLYEPFHNIYSSFIKPIDDRRLEFDEQSKSFYGSLSRYLSAKKDKKGGDSKFFQKEKTFALQRYDYYCFMQDLHDGSIINDINGIFLQYFHRQYDHIALFSNLMNSVLPNLQQLNLKLEKTKWSTTRRDKGREMHRSQVIQTSGRPKSMAPPSPSPISPSFPLHEIQSPMPNRRMAASADDISQTSNFTTEIKGKCISNGGSASPDKIFKEGLLLVFGATELGTDLAMVSKAAWHKHWIVVENGSLWEYANWKDSVKSNVSSISLKHASADKVRKQGRRFCFEVVTPKLKRLYQATSAEEMDSWIEAICEAAKISSFQLSRVATPLSASVRRPSKVFPLFSTSFETTPISRKLSGSGIKKAFSRKGSWNLQQFFRSDNSGTMHMEQLERYHASANIFIQMLRKTDVSNSVCADCGSVKDVTWCSINIPVVLCIECSGIHRSLGTHISKTRSLLLDSLSQQSKVLLCKIGNAAVNRVYEKGLSNPSLKPKPEHNAQVKLAFAQKKYVEHAFIDFAGVDADATLLEGLEQNKISKILLGLAAKPNFEENGVVFLKAVTRDTSKLHLLELLFMNGLLLPDSEQLSEHVSPDMQSYLSQKQFTKYLKE Q10169 DSK2_SCHPO SPAC26A3.16; CHAIN 1..354; /note="Deubiquitination-protection protein dph1"; /id="PRO_0000114901" MTNISLTIKAANDQKYAVTVDSESSVLALKEAIAPVADIEKERQRLIYAGRVLKDEESLKTYKIQDGHSIHLVKTLGQNPAAAATNVSDRTQQVPTNIQAGQGANNPLANLTSARYAGFNIPMPSASMFGPNPENPVPPSTEELANMLSNPMVQSSINEMFSNPQMLDMIINSSPHLRNAPPYVRQMMQSPEFRRAMTDPDTMRQMAQLHQQMGAAGIDPMSLMGGGLGGAGLGGLGGAGLGGFGGANNATAGIAGAAPVDQTAAANTIQNLLNNLGGAGFGAGLGDAGLGAGLGGAASPPAPAQDTRPPEERYAEQLSQLNEMGFVDFERNVQALRRSGGNVQGAIESLLSDL Q10170 RMT2_SCHPO BINDING 140; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"; BINDING 174; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"; BINDING 194..199; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"; BINDING 215..217; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"; BINDING 242..243; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"; BINDING 261; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00892" SPAC26A3.17c; CHAIN 1..357; /note="Protein arginine N-methyltransferase 2"; /id="PRO_0000116476" MDAPLVNESVEFQESQESLSLLEASKQLDLKKIQNLVDQGAVTSAIDIESGKNALHFIASYAEKETEVQAIEVTKWILSNGGVWNGIDRANETPGCIARRRNLLRLYETIVDAGVRSELLLSLLERKELTNEQLDTNEKYLQSALSYTQPTEDSSSLLDSDANAVMMSWERKIMHRSAEIIAPTKGRRVLNVGFGLGIIDTFLQEKEPSLHVIIEPHPDVLKHMRKNGWMDRENVIVYETTWENAINDIASKYVFDGIYYDAFAESYEDLRNFFDSVVGLLDPETDSKFSFFNGLGADNQTFYDVYKKLVPIDLVSFGLQCTYESMPVSSKDEEWKGAKRRYWDVSKYFLPIVTFDF Q10171 UBLH1_SCHPO ACT_SITE 83; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"; ACT_SITE 158; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10091" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPAC27F1.03c; CHAIN 1..222; /note="Probable ubiquitin carboxyl-terminal hydrolase 1"; /id="PRO_0000211074" MWRPLENTPEVLEPYLQKIGVQDASVFDLFSLEEIPEYIPRPVHALLFVFPSSGTKTIYKGSRILPKDSDKVLWYPQTIPNACGTIGLLHAVSNGELRRKVNENDFIKSLIRTAEGSSIEERAKLIEDSKELEALHAAFAGPPLEVEGSEEDVETDLHFICFVKGKSKDDNHFYELDGRQEGPVQHSEIESDLLNAEVLSVIKNYIQSIDSPFFSLVAITTP Q10176 OST1_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPAC27F1.07; CHAIN 19..450; /note="Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1"; /id="PRO_0000021959" CARBOHYD 290; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 383; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 405; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 422; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLVLKLLLWSIISGLSLAEQVWRNSNAIRTIDLRSTYTKTLTSLIIVNEGDEPQNTYRYFQQTSPGESVLSLSVSIKEEEKKGTNPIKVNNNVYDIPLQPPVKPGESRTLLIQAGLDGGVRPLPAAVDQDEEQYLVYLTTLYLDSPYTTDLQRTRLILPSAKIDTYTTYNIDGAELPNRVGNTLVYESRETITGEDNDLGEIYVRYEHTVPIPRGADLYVQIDMHEYRKMLEVSERVVFENHAAKLKSNFDRAKWYMGNFYNPVSTAINRVVYSLPRNSKDVYYTDEVGNITTSHMRVEPHQTWIELNPRYPVFGGWNYLFQLDWKMPYEEFRSSKNRREYLDIPLAWSPGDMIYEKAVWSYVFPEGATNIEIEMPVEISNSNVTKIHKFLDTLGRQVFTYEALNVTDGVPSDIVHISYEYNSSAFFLRIAIITTLLILLAAAAYMIWAP Q10187 UCP6_SCHPO MOD_RES 595; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3F10.13; CHAIN 1..612; /note="UBA domain-containing protein 6"; /id="PRO_0000065715" MEDLDTKIKTLKNMGVSESDAKDSLERCGYDVESAAEFIFSGQLEKSRLVPIMSSTSIASSLPSYQDTFFLPSPRKRRRLPGRIGTVLKPSALFPAIAPFLFVVFEIPVALNTFVHATCKGLLFAEDNASFHRPFTDVSAHLSSSSLSKYNHHSNHRLASPGWWYGEDSCISQSLDPRSVMQVQTIRAFEFLFSSHRLYLDTVHITAALSQVLAGLGNTNTSMSDGDCIAAFLSSYFSPPNAEFDSTFCSTLSSLTNSEKPTYIFNFKPNSTPDLRLSIESCLDLLLHPPSSAQKNWSWIKHVGKVFCCSLPGNNASGTPRFLLTPKIDLSKCIIENRDEMLRRYQLETVYRKTLLEWEDLYKRLTGVTLTDKDIGELLTDGQQFLEKRNPALSSHLQLLKETLQTKISTLISNTNATQHKLSTLYRGMQNKCTRRLLAVIIEPSIIYICLKNSAVQSNRNVSPSANHNEQWYLVRFTTSATISQDSPPCIVEPVTFEEVDLEFEKHISYHNRLLIYVDDDCEASTRTVIPTSVKNFIAEDNEYFDDELAGIIHSPTVSTRSSRSSDVSEYDLEDQGGLQLTVPHINTDVQCHRSRNSACEFPESMHVEHSG Q10190 LSG1_SCHPO BINDING 209..212; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 308..315; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 352..355; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" SPAC3F10.16c; CHAIN 1..616; /note="Large subunit GTPase 1"; /id="PRO_0000122453" MVLPKSKNQIGLGRAIQSDFTKNRRNRKGGLKHIVDSDPKAHRAALRSVTHETDLDEFLNTAELGEVEFIAEKQNVTVIQNPEQNPFLLSKEEAARSKQKQEKNKDRLTIPRRPHWDQTTTAVELDRMERESFLNWRRNLAQLQDVEGFIVTPFERNLEIWRQLWRVIERSDVVVQIVDARNPLFFRSAHLEQYVKEVGPSKKNFLLVNKADMLTEEQRNYWSSYFNENNIPFLFFSARMAAEANERGEDLETYESTSSNEIPESLQADENDVHSSRIATLKVLEGIFEKFASTLPDGKTKMTFGLVGYPNVGKSSTINALVGSKKVSVSSTPGKTKHFQTINLSEKVSLLDCPGLVFPSFATTQADLVLDGVLPIDQLREYTGPSALMAERIPKEVLETLYTIRIRIKPIEEGGTGVPSAQEVLFPFARSRGFMRAHHGTPDDSRAARILLKDYVNGKLLYVHPPPNYPNSGSEFNKEHHQKIVSATSDSITEKLQRTAISDNTLSAESQLVDDEYFQENPHVRPMVKGTAVAMQGPVYKGRNTMQPFQRRLNDDASPKYPMNAQGKPLSRRKARQLTALELGVSPEALSSATSKKHNKKNKRSKQRSGVVIDDY Q10191 LTV1_SCHPO MOD_RES 171; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 179; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 244; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 245; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3F10.17; CHAIN 1..386; /note="Protein LTV1"; /id="PRO_0000116480" MGKKKFVNKNKAQTFHLVHRSQRDPQYHDENATERVLVSAETLNKTARRLNRQTLDEEYGSTIRPNEGEAANYGIYFDDTEYDYMQHLRNIGNEDATWVEAPATRKTQDKQKKQQIQLRDQPSILPQEVLPSEVELERTYQDQQSVPDAISGFQPDMDPRLREVLEQLEHSDINDEETSDFDEEFEKLVASGKADESEFYAQPFVEEGEKDYDEAAAAKAGKSEWEIEFEKFKLEQKKQPDVASSDGDFSDEPESEERDEVPELVSSSKSKSKTKRKARTALSSVSMSSSALFRNEGLTLLDDRFDKVEEEYTPIKDERELIDPDQKDVFDLVNDNQFNDIMDEFLVSYGPTLGRKKAPSRMSNSKKKSSLEELDNVRKMLGRARI Q10192 RL18A_SCHPO MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 87; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 89; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 134; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 136; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 138; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC11C11.07; STRAND 15..17; /evidence="ECO:0007829|PDB:8EV3"; STRAND 81..89; /evidence="ECO:0007829|PDB:8EUY"; STRAND 101..107; /evidence="ECO:0007829|PDB:8EUY"; STRAND 121..123; /evidence="ECO:0007829|PDB:8EUY"; STRAND 138..140; /evidence="ECO:0007829|PDB:8EUY" HELIX 23..38; /evidence="ECO:0007829|PDB:8EUY"; HELIX 42..51; /evidence="ECO:0007829|PDB:8EUY"; HELIX 55..57; /evidence="ECO:0007829|PDB:8ETC"; HELIX 63..70; /evidence="ECO:0007829|PDB:8EUY"; HELIX 109..117; /evidence="ECO:0007829|PDB:8EUY"; HELIX 125..131; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..187; /note="Large ribosomal subunit protein eL18A"; /id="PRO_0000132782" MGIDIERHHVKKSQRSKPASENVYLKLLVKLYRFLARRTDSRFNKAILKRLFQSKTNRPPISISKIAALTSRKSASSQNKTTVVVGTVTDDERMLTVPKLSIAALRFTKSARARILKAGGEVLTLDQLALRAPTGSNTVLVRGKKHAREAYRHFGFGPHKHKAPYVRSEGRKFERARGRRKSRAFKV Q10201 YBX7_SCHPO SPBC17D1.07c; CHAIN 1..949; /note="Uncharacterized protein C17D1.07c"; /id="PRO_0000116531" MKMLQNKGPLQELTLNAMAPNGIFQDEPMIQKFENHYVFKKDMKSKRNKEVKNQMNDWLAYGYLCSVHEAKKWLEEETNNEYQNLDDFVDALVNGKVLCQLAFKYYPKLASNWKPRYQISERNTVYLNAFFHFLDFIGMFTPFRFETKDLVRRFNIPKVIYCLHALSYLLDFLEVTRHVPSLYGKLRIKKSQLNTATKEISLLKKAKKFPNFPKLKNFFCSYSHRHETATSNKQVSCFREVPAWIKQCQSQCRGFLTRKCVSIEKLRRDDMSERLGWLPKLETKLSSISDEERLILLKESHQIYRKMVSLHLELLHLPQLEMSLDFCGFSSDDSSIAISSQLVPPILNNLIFKLEESPQIWILIISRFSSDGIDKIDVQNFILLILKFFGFAISASDRRSFLNLIMSCVMVSIQQSSAEVGHSTSDSLISWASRLFTKGFCLQLQSFFEKHLGNVVDKFFLEHLCETTIESDAMRVVTEMLVSCYENRERIPNELPMVLKQIYYSRSESFKPSAIKEFIEYFLCDQLMNCLSVYYSKYFEGKDSKKFTLVKHFMNSLFGRVKLNEQTEIIWHTRNYRIVEALVRKLIHLSTPKIIPVYGGRTLSCTHKDIFDLQNILRYCDERGDFSSFPSFKKLISLLGSPKLFKKHENQILLLESKNEVIHSSLPCSKSSLYQLSLSLCIPLIEGHLRNSLEEILFGVPTELENQKFMSVLRNDKLIKSIHPGSLSGISNSFVNSKHPIEQWQSRLRKILHLFSGRNEDIASLQCVLQFGSSERIHLEDIQNSHRYLCSLKKNNSQKDIHRNPLLSHVFDTNTKSFDTLKTLNYKHAILKKSMGELYKMEMIHECPRQLFGQILVVYLNRERTLLNFYLIENSKTIDEATLQLTDLIQAIKTGIYYLRMFNLPFHVKQLYTWLAPISKYDSEISFNQKKERRKTFLSFERRGKNRKF Q10202 DBP3_SCHPO BINDING 209..216; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC17D1.06; CHAIN 1..578; /note="ATP-dependent RNA helicase dbp3"; /id="PRO_0000055088" MQFCFRILILYISLSIDNNYLVTTLISLKENVFLHIFTLTFLFKAFLLKMAKRSVEELKRSADEEASVKRKEKKSKHEHKKHKKDKPSADKDRISKKDKKKSKKGKSKTKEESIEINAEEGAKIAQPAIGSANASNHNDEEAYDRYIKKHNISFADPKSSENLLPILQFDELDVSAKLREGLKNYKEPTPIQAATWPYLLAGRDVVGIAETGSGKTVAFGIPALQYLNGLSDNKSVPRVLVVSPTRELAIQTYENLNSLIQGTNLKAVVVYGGAPKSEQARAAKNASVIIGTPGRLLDLINDGSIDCSQVGYLVLDEADRMLDTGFEQDIRNIISHTPDPTRNGSRQTVFFSATWPESVRALAATFLKDPVKITIGSDELAASQNITQIVEILDDPRSKERMLDNLLRKHLSSGGKDDKILIFVLYKKEAARVEGTLARKYNVVGIHGDMSQGARLQALNDFKSGKCPVLVATDVAARGLDIPKVQLVINVTFPLTIEDYVHRIGRTGRANTKGTAITFFTPQDKSHAGELVNVLRQAKQDIPEGLFKFGTAVKPKLNAYGSRVVDVPVKAATKIVFD Q10206 DPH2_SCHPO BINDING 93; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P32461"; BINDING 114; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P32461"; BINDING 334; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000250|UniProtKB:P32461" COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P32461}; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit. {ECO:0000250|UniProtKB:P32461}; SPBC17D1.02; CHAIN 1..503; /note="2-(3-amino-3-carboxypropyl)histidine synthase subunit 2"; /id="PRO_0000083392" MSFELSAPVPLSDNSEAILEKEIGETVKIEGDLVEVYEINRTVDFIKSGNYNSVALQFPDEHLADSGKVASILTNLVEANVQILADTNYGSCCVDEVAAEHMSADAIVHYGRACLSPTSRLPVLYVFGRLPINLHKLEKCLTIPLDQNILLVSDTRWYYAQDSILKSLKTLGYQNVYESHLKERIEPNLEEASTSYTIPGRTYSLPKSLSLQDMTLLYIGPDSPTLSSILMSHYSLVNQFLSFDPLSNKIVEESSFTGAKLRRRYALVQRCRDAGVIGIVIGTLGVHRYLHVLNQLRKMILNAGKKPYMLAVGKLNPAKLANFQEIECFVLIACGENSLIDSKEFYRPIVTPFELVKALSSDMSWNNDFILSFDEVLKLSEGKQSKEPSEVLTEESAEPHFSLITGKFVNSTPMRHLDVTLETADAKNNDSSSASIEKRGMRSLAVNGVYSPAAAFLQSKSWSGLDSVDEGEGPSKLYEGQSGIAKGYVGEGSKEKIQRDFGK Q10217 ACPM_SCHPO TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000255" PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group (By similarity). {ECO:0000250}. MOD_RES 69; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" SPAC4H3.09; CHAIN 29..112; /note="Putative acyl carrier protein, mitochondrial"; /id="PRO_0000000565" MLSRFSSQLRFISAVRPVIPKFQPLRFYSVARPDAEKRILKVVSSFDKIQDPKKVTPTSTFANDLGLDSLDAVEVVMAIEEEFSIQIPDKDADEITSVGDAISYITKNPEAK Q10220 PCC1_SCHPO SPAC4H3.13; CHAIN 1..88; /note="EKC/KEOPS complex subunit SPAC4H3.13"; /id="PRO_0000218926" MSEMIVLPHKVTVKVPLASRVDAERCLQVLAPDRELKEELVQRNLFVDDNYLVVNYSCSSARMTRVTVNSLFENLYLIIDTMHELSSL Q10221 YAYE_SCHPO SPAC4H3.14c; CHAIN 1..345; /note="Uncharacterized protein C4H3.14c"; /id="PRO_0000116487" MGLEGSEKLEHEIEQVHDNIENRKEEVSTLQDMANDLEKLTDHIEATYIGRGVPHDHAKTGSRKPSSGQLIATMQNEIDRLKKEGDKVSILLMQERKKRKELESAKNNLLNVYDSLKMQKASVSSMVNRKQRAAKEEQKIQEEFERQITDLLEEQQQLKLEIERLEAETERANSETEQYEKQKEALEEEYEELRNECLKHDPQLDAEIRTLQDTFEEVERTLTKQVSDAKIADKPLKDSMFNSNSEKEKIMHALEKAEKDADIYSEFIQQYMEQLESSLEKSSTAIENAQNRLAEMTAHLAESSDYDNDDDTDGIINETDYELDTSQSEFATLTTSSNKSILNES Q10222 PTA1_SCHPO SPAC1071.01c; CHAIN 1..670; /note="mRNA cleavage and polyadenylation specificity factor complex subunit pta1"; /id="PRO_0000116838" MEVSETDEHLTRLNQARDIVKTDQSLFPEIVRNILSVANYSDIRYKKWMANFLWFGFSSKNVKFEQKLDLAVTCLDTIVSLYAVDNEEVKKDVISCSCTIYPLVFLHCCTSPNDSSTWDTLTKLKNEIINDFDKGNKPLLISCIKFISCVILTQVPGIRDPRLVTKSDVSLSKVPTHHPFINSNILRIEANDLIEKIFSILFSDSLNVLYITSVLNILPVLVKRRKELAPKIIGSLLEFHLPNPKDEIELSNESKLAIRCIEKNLKLILLHLAKSTGASSSSVEKIHAYLSGQIYHTKVDESLKKRQYEGNISAASKRVKSSAVQSLVERMQPQLSSHDGLQNNPLISIFASQTAINPLANFDVTSIPVEVATEIVLTSLLKIDKNYFHQQINMLRERVRSLSEPESLGLDQQVDEDEDEDYEPPEVDVQTINASVEREAARLEGSAPSNVVTDAFELPTPDSLSPMAILEYFHGALSRLFDYAPQFERSIVSSSNLQNLTLENVDNTVWDKRHWAILLPRLCTRGLLNYQPVTSGEESGDASFTLSSFVRGQLFTYVASNWRSSTNLILNWLSEEWYNDRLMLENPDCHEYEDVKWEGPQYEKWALKVIDSILPYLEAKDKVFMIFMSELPELTDAIVDKIKFVCLDPDKTKLGFMTFQYLIMFRLTCT Q10224 TRM9_SCHPO CATALYTIC ACTIVITY: Reaction=5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43208, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:10408, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74851, ChEBI:CHEBI:74882; EC=2.1.1.229; SPAC13D6.03c; CHAIN 1..228; /note="tRNA (carboxymethyluridine(34)-5-O)-methyltransferase"; /id="PRO_0000116489" MEIEYENEYVHQVYDKIATHFSDTRYKPWPVVEKFLKSLPLGSVGVDIGCGNGKYQKVNPNVYMIGSDRCVKLVKIASNLGPMVISDGLHVPHPSNRFDFALSIAVIHHFSNENRRLQAVQEVLRPLVKGGKALFFVWALEQKNSRRGFSEDGPQDVYVPWILKRQYEYPNAKPEELKGHDPAENIAYQRYYHLFRKGELNELVETAGGSILEHGYDRDNWWVIAEKN Q10232 RL9A_SCHPO SPAC4G9.16c; STRAND 9..11; /evidence="ECO:0007829|PDB:8EUY"; STRAND 17..20; /evidence="ECO:0007829|PDB:8EV3"; STRAND 26..28; /evidence="ECO:0007829|PDB:8EUY"; STRAND 35..37; /evidence="ECO:0007829|PDB:8EUY"; STRAND 45..48; /evidence="ECO:0007829|PDB:8EUY"; STRAND 53..56; /evidence="ECO:0007829|PDB:8EUY"; STRAND 87..92; /evidence="ECO:0007829|PDB:8EUY"; STRAND 95..97; /evidence="ECO:0007829|PDB:8EV3"; STRAND 100..104; /evidence="ECO:0007829|PDB:8EV3"; STRAND 109..113; /evidence="ECO:0007829|PDB:8EV3"; STRAND 122..125; /evidence="ECO:0007829|PDB:8EV3"; STRAND 130..138; /evidence="ECO:0007829|PDB:8EV3"; STRAND 141..147; /evidence="ECO:0007829|PDB:8EV3"; STRAND 166..168; /evidence="ECO:0007829|PDB:8EUP"; STRAND 177..183; /evidence="ECO:0007829|PDB:8EUY" HELIX 22..24; /evidence="ECO:0007829|PDB:8EUY"; HELIX 62..84; /evidence="ECO:0007829|PDB:8EUY"; HELIX 115..117; /evidence="ECO:0007829|PDB:8EV3"; HELIX 149..162; /evidence="ECO:0007829|PDB:8EUY" TURN 105..108; /evidence="ECO:0007829|PDB:8EV3"; TURN 170..173; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..190; /note="Large ribosomal subunit protein uL6A"; /id="PRO_0000131109" MGRDIYKDETLTIPKGVTVDIKARNVTVTGPRGTLKQNLRHVDIEMKKQGNTIKFIVWHGSRKHNACIRSVYSIINNMIIGVTQGFRYKMRLVYAHFPININLTENGTVVEIRNFLGERITRVIKCLPGVTVSISSAVKDEIILEGNSLENVSQSAANIKQICNVRNKDIRKFLDGIYVSERGNIEELEE Q10234 RT05_SCHPO TRANSIT 1..22; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4G9.17c; CHAIN 23..387; /note="Small ribosomal subunit protein uS5m"; /id="PRO_0000131687" MLRSFSHFLQIGSRRQPTYFRCFHKTTVHLNSFKNDPKKELNSNLNEKSVEESSKNETKEQFNSSSIPRESESEGKTASNTSPLSPKKVENLSKLFNDINEDVSIEELKSRFKDHLPFYENYIRNHPLAIEALQKSTAPRQTGLKLNYVSKLDKYVTPLDGYSHLGSEESNGEIPDKWEDFKDDLTFEISSKFSPFDFGDAGKSTSDAEFLSDISGIPKSDLRALMFVPLVRRRVVNQTRKGKIASMYVLTVVGNRNGVAGFGEGKAESYSLAYKQSCGRAVKNMVYIPRYDKRTVYGVIHKKFHAVRLTLRSRPAGFGLRCNPILHEICRCAGIKDISGEILGSKNGMNTVKAMFEALQSQRLPEDIAMERGQKFVDVQREYYKQT Q10237 YD14_SCHPO SPAC4G9.04c; CHAIN 1..638; /note="Uncharacterized protein C4G9.04c"; /id="PRO_0000116564" MDLVELDYLSALEDLTFNSKPIIHTLTYIAQENEPYAISIVNAIEKHIQKCPPNCKLPALYLLDSISKNLGAPYTYFFGLHLFSTFMSAYTVVEPRLRLKLDQLLATWKQRPPNSSSLEPVFSPIVTAKIENALLKYKSTILRHQSPLLANTSISSFSAPIDANINSYSSFSDPASSYKPSLPSVPFGFQHISGTSPSPGFITLDSLLSDVNRMIVTEQARFIKNPYDNMAKKRFEILLQLKNVLSSSALPYDQLLAIKNQLAQLEKPASPSTSSVATSAPSVPSALSSISSTPFMKPSIPSTIPTIPSAYSASVSSQPPLTHSYVHPGPQSHKYSLSSGPPASLYNANALTPEESSSIDSLFANLQAAGLVPPSAGGKSQGPQASCTEAVSLTADIDLSKSSLATPRPKLSSLLYENYSNQCANCGRRYGNDPESRKELDKHSDWHFRINKRIRESSLHGINRCWFVMEEEWVNSKEEEDLITETAQEIEEQRQKQMESVRSQYVLTPLDPIAASEPCPICQEKFQSVWHEEAEVWVFMNAVEEEGRIFHATCLQEVRPSENKHSNTNTSTQNLAEAAVSSNIKNATGDASKDSQPDVQNLLQGIDIQSILQALGKRKERDDSMDSMSSKVIKQESK Q10239 CHZ1_SCHPO SPAC4G9.06c; CHAIN 1..113; /note="Histone H2A.Z-specific chaperone chz1"; /id="PRO_0000116565" MSEEPKKIDIKGKGRAIEDLIPDIDDEEDDVDFQDLSSSGESDDSDDSMQEDYDDIHDEEPEDYSAIDPTNIMCSTRTRRKKIDFTKVLEEGQNEDDFEEEDEDYIPPQDKTM Q10242 GNTK_SCHPO BINDING 21..28; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391, ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216; EC=2.7.1.12; SPAC4G9.12; CHAIN 1..193; /note="Probable gluconokinase"; /id="PRO_0000087538" MTVTPINPTNQPYKYVFVVIGPAGSGKTTMAKAVSEKLGFEYIEGDDLHPKANIEKMSQGHPLNDNDRWGWLHNCGGACAMELDKESIKGVVLTCSALKRSYRDILRSSLEHRPAILRFIYLAASRETLIKRTTSRKNHYMKADMVESQLAILEAPTADEKDVITISVENGKEQSEEECLDIVHKMVNENKQP Q10243 VPS26_SCHPO SPAC4G9.13c; CHAIN 1..298; /note="Vacuolar protein sorting-associated protein 26"; /id="PRO_0000073014" MDYFFKSPIDVDLHLDNEEERTFVDYEFEQGRKDKAPIYESDETVKGTVMIRLKDGRKLDHDGVKIEFIGQIENTYDKGNIHEFTRSVQELASPGEMRHAQMFEFEFKHVDKPYESYIGKNVKLRYICRVTVSRKMKDVIREKDLWVYRFENEPETNSLIRMDVGIDECLHIEFEYSKNKYHLKDVIIGKIYFILVRIKVQRMEVSIIRRETIGTSPNQYSNSETITRFQIMDGNPNRGETIPLRMFLNGYALTPTFRDVNKKFSVRYYLSLILVDEDQRRYFKQSEITLWRRRDEHE Q10245 MKAR_SCHPO ACT_SITE 216; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 220; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 61; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 115; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 142; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 177; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 216; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 220; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 249; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 251; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330; Evidence={ECO:0000255|HAMAP-Rule:MF_03107}; SPAC4G9.15; CHAIN 1..341; /note="Very-long-chain 3-oxoacyl-CoA reductase"; /id="PRO_0000054869" MDGEVLANKSCCGAVVTAFSVIGIVFTILKFTSFASFVYKTFFAKGVKLSVYGAKKGYWAVVTGATDGIGKEYATQLAMSGFNVVLISRTQEKLDALAKELETVAKVKTRTIAIDYTKTTAETFEKLHQDLVGTPITVLINNVGQSHYMPTSFAETTVKEMDDIMHINCFGTLHTTKAVLSIMLRERQKNEKGPRCLILTMGSFAGLLPSPYLSTYAGSKAFLSNWSASLGEEVKKQGIDVWCFNSYLVVSAMSKVRRPTLTIPTPKKFVRAALSSIGLQRGGTNPYISQPYPSHAVMSWSLEQLLGSAKGFVVSQVAAMHLSIRKRALRKEARLQAQNQA Q10254 ALG10_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + an alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + a di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502, Rhea:RHEA-COMP:19512, Rhea:RHEA-COMP:19522, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256; Evidence={ECO:0000250|UniProtKB:P50076}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29544; Evidence={ECO:0000250|UniProtKB:P50076}; SPAC56F8.06c; CHAIN 1..445; /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase"; /id="PRO_0000215460" CARBOHYD 76; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 239; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFLGKAIILILWIFLAFTGLLAIQYYVPNPYLDEIFHIAQAQRFCRKDWDWDPAITTPPGLYLVSVALSPFIGCSNVSLRLINWLVGVIGLPWLINDIVSLLNNRKGDVVTYFAYTLSSLPPLWFFSFLYYTDIGSTFFVLLAYDFALRKSAFSSSVSCFFSLWFRQTNIVWMVFIAVTYFASNMSFFNPHLAEATFADVLLTIISFLGVFLKNLRRFSCPILSYGAVFCSFLAFLLWNGSIVLGDKSHHQASIHLSQINYFLWFFFFFSFPSYIIKYLMSHSRRSKLLSAVFSKKSFLIVSVLLLIAHFNTIFHPFILADNRHYLFYVFNRLFRIWWLKYLGPFSYLILYYFFLDISKLQMTSLTFFLLISTTILTLVPAPLVEFRYFLLPFLFWRFHLPLPSGRECLMEYALHMVINSVTLYIFLFRTFIWPSEPNALQRFMW Q10257 RRP8_SCHPO BINDING 132; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43159"; BINDING 175; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43159"; BINDING 197; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43159"; BINDING 209; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43159"; BINDING 226; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:O43159" CATALYTIC ACTIVITY: Reaction=adenosine(645) in 25S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(645) in 25S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43792, Rhea:RHEA-COMP:10695, Rhea:RHEA-COMP:10696, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.287; SPAC56F8.09; CHAIN 1..318; /note="25S rRNA (adenine(645)-N(1))-methyltransferase"; /id="PRO_0000116569" MFKVDWDLGPVSKSASDQTKESRKEKKRKKGERKNVGDKGEKLNEKVLKKAKSVTTNNSLKSEIKKEKSVPSIKEKNKGDAKHTKLTSLQQKMKDKLDGANFRWINEQLYTTESDKAVQMFKENPDLFDIYHAGFRYQVEGWPENPVDIFIQHLKIRFEHSNAKKKNNIVIADLGCGEAKIASTFRKSRSLQVHSFDLVAPNEHVVACDIANVPMADETVDIAVFCLSLMGTNWQSFLKEAYRILKVGGLLWVAEIKSRFSDKSGEVFAKELPKLGFETKSIQLQNKMFTLFEFKKVPVHGKCEELPPILSACIYKRR Q10259 SPC3_SCHPO SPAC56F8.11; CHAIN 1..185; /note="Signal peptidase complex subunit 3"; /id="PRO_0000218949" CARBOHYD 148; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIVDTFTNRGSTFFSKLSTVLFFLCAVITFQGVIQRREVELDTPVYVHYAKYRSARFYHAFRNVRQQYAQVKFNMDADLSELWDWNTKHVVVYLVASYSTEKHEKNQVVVWDKILSSPEESKMFMKDTLSNIQAHPFNEYSNQFEGKNATYTLHWTVSPKMGFLSWGAGPGSYEIPFHKIITQPK Q10264 PSO2_SCHPO BINDING 109; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 112; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 126; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"; BINDING 130; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01256" SPAC22A12.01c; CHAIN 1..560; /note="DNA cross-link repair protein pso2/snm1"; /id="PRO_0000209129" MSKRKSSSILDFFKKSNNGKNMWGNEAVSVEKTDSTTKPSTVKNAISSSQIKNEKFSQEVLLQFNDPSFTSEVGESPQWQSFGDANILEPLKNELVKNEESTMSELLLCPICGITLESLTVDANIHVNDCLDGRTTEAVSKKLKKDSVVKADPSNSSTFPISDSCKQALLPLPGKQINVRSVVPFYKLMPYNIPFAVDAFAYGAIDGVEAYFLSHFHSDHYGGLTPKWKHGPIYCSEVTGNLLINVMHVDEQYVKRLKLNQPYNIMGITVYVLDANHCPGSAMFVFETLQSNQTRRVLHCGDFRASKDHVMHPVLREKTIHKVYLDTTYLNPKYTFPPQADVVQACADKAISIKKSTDSRLLVVVSTYSIGKEKVAVAIAKSLSSRIYVVPRKMHIIKQLENQDLIDLLTDDPTQASVHMVTMMGIHPNSLLDYLEQYNSSFDKIIGYKVTGWTFQPLENRAQLSSSLDSIISRPPKFVEYDLRAIRGSTDKVAAFVAPYSEHSSFYDLTMFCLSMNIGHIIPTVNVGSQRSREKMNVWLDRWAWRRKKQGLLSLENVDW Q10265 HSP71_SCHPO MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250" SPAC13G7.02c; CHAIN 2..644; /note="Probable heat shock protein ssa1"; /id="PRO_0000078379" MSKSIGIDLGTTYSCVGHFSNNRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTIFDAKRLIGRRFNDPEVQSDMKHWPFKVIEKDGKPLIQVEFKGETKTFTPEEISSMVLLKMRESAEAFLGGKVTDAVVTVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDRSNQHETNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDSRLVNHFAQEFKRKNKKDITGNARAVRRLRTACERAKRTLSSSAQASIEIDSLYEGIDFYTSITRARFEELCADLFRNTMEPVEKVLRDSKIDKSSVNEIVLVGGSTRIPRIQKLVSDFFNGKEPCKSINPDEAVAYGAAVQAAILVGDTSEKTQDLLLLDVAPLSLGIETAGGVMTPLIKRNTTIPTKKSEVFSTYADNQPGVLIQVFEGERARTKDCNLLGKFELSGIPPAPRGVPQIEVTFDVDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDRMVSEAEKYKAEDEAETSRIQAKNHLESYAYSLRNSLDDPNLKDKVDASDKEAIDKAVKETIEWLDHNTTAAKDEYEDKQKELEGVANPIMAKIYQAGGAPGGAPGGMPGGAPGGAPGGADNGPEVEEVD Q10271 ARB2_SCHPO SPAC13G7.07; CHAIN 1..321; /note="Argonaute-binding protein 2"; /id="PRO_0000116575" MFRKKKSRVLQRDVNFGNCLEDMNLQITNDFYLRKLNAPNELYEFQVTKDKEYNEKFYFAVLDHVYSWTLQNSLLTRISIPLESSPSEPHSWIYATRNWQTNENGIVIIIQSMSHPLIWSNRNLREGDVRRATVLDVIAKCTEKKLSVVIFSPSALLWDQSINFPRTTRYFTSQGLQITKKSIIKDVETPESYVSIGLNYVMSNSVSTKIHFVGSEYGSYLLNSYLDLNWKKFSGKAGAILLIMNMSINEELHDPDYVSYLIEHARNYLPSHEPCRHLMNSIMTESGIPNFSAGKYIDEFYDYIGDVLLEMIALDTNTSKS Q10276 KICH_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + choline = ADP + H(+) + phosphocholine; Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216; EC=2.7.1.32; Evidence={ECO:0000250|UniProtKB:P20485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838; Evidence={ECO:0000250|UniProtKB:P20485}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P20485}; SPAC13G7.12c; CHAIN 1..456; /note="Choline kinase"; /id="PRO_0000206225" MVNFASEVDKNNAFDSAHPSRKCKGSLDCNDPDPIFRHKVLVIIHKLAISSWNRIPLTLCNKLHIKRISGALTNAVYYVAPPEGYHAPKLLLRIYGPHVELFINRQVELENLKRLARHNIGPYLIGEFSNGRFEQYMESTTLTCKTIRDPKLSIYVGRRLCELHNFILLHPHEVLEMPAAWKNCLVWLPKAKAKILGRKHSLAITSEFMKTLEEDFNAYYNWFVEWSRDKKDWFGLKMVFSHNDTQYGNLLKIKAKKRSIPLSQKHRTLVPVDFEYAGPNLCAFDLANYFAEWMADYHHPTHNYLMDRSRYPDFNARKLVYHAYVEQSAVINDLLEIEDASLLKTDISDELKNTFEKQIMNLEESVRAISPAANIGWALWGILQCLEEDDEWEDLSVSSQVADRPEKQLVEGSTVPPIGTSSFDYIGYSSEKFDLFYEGCAALGLNGRNRSTFSYA Q10277 MSA1_SCHPO SPAC13G7.13c; CHAIN 1..533; /note="Multicopy suppressor of sporulation protein msa1"; /id="PRO_0000081648" MVVSSPSVSLLHSPVEKLSAQLEKTTLLQDIPPGSLSENDNSTTFIKPPLETASSSTPIPSSSSSGVLNPSSVRGKPVACLFVASLNSSRSEEELTATVKDYFQQWGPLLHVKVLKDWLQRPYSFVQFQNTDDASKALSEAQNTILDGRHIRIERAKVNRTIRISSAPHQPYITKKDIDNLLEPYGEVEDVTEIPDQSAFLVRFVYRDEAIAAYTALKHSAWPVLWAENVTYQNGHYKKKGSSPFSPPNAHSRRRKSQGKDQSNTPVIKAPAPIPFSVSSDPPSTMGRSNSAVQSPSYFAHSLVNSTEFSTPNESLSSLPSILPSIPSLESGKAELPTDGSFEQPGYPMNPSMMFAAMPPPIDPYSIFVGQLDPVNCTHYLLVDLFSKYGKVIDCKIIHQSKKPAFAFLRFDSQQAAYAAVCGKTRSPHQKKPLRVEFRQLRPMQQFSPQYQYPSYPYPMFPAPFSPPRNAMMPIPAPMDQFSTFHQSMATLPPGAVPTSIPQSYYPIYSPEMAMPQSYSPMYYTHNPPMDGN Q10286 ITR1_SCHPO CATALYTIC ACTIVITY: Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in); Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268; Evidence={ECO:0000305|PubMed:9560432}; SPAC4F8.15; CHAIN 1..575; /note="Myo-inositol transporter 1"; /id="PRO_0000050453" CARBOHYD 432; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSISSKDFQNVTSAGFADDTFAADTFAADKKSPFESSVFENKTQVLPVDSVSRLSNGARSRSNSNISLSEPHALNDTVEDQPVSKWVWVLAFAAGIGGLLFGYDTGVISGALVVIGTSLGGHELTNGGKEFITSATSLGALLGGIIAGALADFFGRKPVIAIASIIIIVGSIVQVTAHHLWHMIVGRFVIGWGVGIASLIIPLYLSEIAPSKIRGRLVIIYVLLITAGQVIAYGIDTAFEHVHNGWRWMVGLAMVPAAFQLFILIWLPESPRLLVKKERSQEAYNTLARIYPTAHPYEIKTKLYLIQEGVRDPFSGSRWQKIVKTFKELYFNPSNFRALILACGLQAMQQLSGFNSLMYFSSTIFEVVGFNNPTATGLIIAATNFVFTIVAFGVIDFFGRRILLLLTVWGMIAALIVCAVAFHFLPKDENGNYTSGQSNAWAIVVLISMIVYVASYASGLGNLPWQQSELFPMSVRGLGTGMSTAVNWAGNLGIGASFLTLMSEITPTGTFALYGGLCFLGWLGALFCYPDLTDYTIEEIGELLKHGFGVRESMRHLKRVRQERAWSREDKEQNN Q10294 PAC2_SCHPO SPAC31G5.11; CHAIN 1..235; /note="cAMP-independent regulatory protein pac2"; /id="PRO_0000058166" MQTYTGIIKTPLDAIILFEACRIGLLPRVQRRLSDHERSLIRAGSVFVWDEREAGMRRWTDGKSWSASRVSGSFLTYREMEGKRKPYHHGLSTDGSLKRSPSADTTGNSSLNAYSNEDSGAASLSDEESVDDENLRGLHYKPNGLIKQSFSITTSLNHKLHLISYSSPIPDPSLVTPSSDVNLSRITIPYGLYPDAGPPLVQAPKFLAPYDILVEKVACSEDARVLDKLRQALWL Q10297 IMB5_SCHPO SPAC22H10.03c; CHAIN 1..993; /note="Importin subunit beta-5"; /id="PRO_0000120777" MVESKIIKLLEQVQSADPNSRIQAELGLRDLEKYHDFAAKLTDIASSGASVPLRQGSLIYLQRYIVHHWSPLFEQFQDGPIPDENVKKHVRETLLHLLVSLDNFTLIKAVAYAVSLIANVDYPDEWPEVVPAVLHLLQSTNENSINASLDVLDELVDESLVEEQFFIIAPQLASILYQFIFSAPPNDSMRMLQARGIKLFRSCLELIEIYKETKAEHVRVFLEQILPPWMDMFSHKFEVSLVDDRQVILPDSCGYFCIMGEIAMTLTKLRELFPSKLTPYVVTFVELVWNIIEKLLDPYIREVVFSDGLDDSAFGDKYPIRYLVELLLFVSVALQSKFVQNLFVSNTVPVPPLPPCIPLLVQYTQLPKHQIEVYESDVSEYIANEFSMDFASDTVRGAAISVLSAFEEHTTLPIQQSLREMSATYILNNEINWIYQEALLYACCSVDAASDDTYDDYLDPIYEAIKVRIDYSDAPILLLSRFFLFIGYFSESTVVASQFFQIIMNNLVNALQVDTVQYAAMKAIERFCSVGKVKPILSLQPMILEVLSQYASKSSDEALVLLVEAISSAVKLDCAKAAELGNSVIPLLFNLVATNASDPYICGIIEDTFEDIIHAANNYESMCEITLPELLQVLNQEDPIMVNIGATLLSCLIRAGPSPLPNGFVGYVLPPVYKITQIHSGDTELLQLSQEILKGLLEKDTPQLLETEISGSSGFQYILFILHQLLDKESDDSACFLVGPILLELADHASQMVDLQSILLSCIKRLAIAEQPRFIQSIIYVFAKLIVKDSLGMMHFLTSSLLNEQGLTAFEVLMTVWCDNFVYFSNFKNISIICIAMTKIYSFDSPLLDSVQVKGELISHSNRIITRSQSKLHPEEYSYVSVGEKILRLLSEEFVSLSKDAIVEEVSDDGADDWDDGPISAETFGLSANDVNELSKDEFSGVDNSEDEDNTDLQFYLLEFFKEAMKSNLHNINEVVFRLPQEEQDALVQIKEK Q10298 YD44_SCHPO ACT_SITE 112; /note="Proton donor"; /evidence="ECO:0000250" BINDING 51; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 53; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 79; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 79; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 111; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 161; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 236; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; SPAC22H10.04; CHAIN 1..307; /note="Putative serine/threonine-protein phosphatase C22H10.04"; /id="PRO_0000058918" MIDLDNIIERLYEKQLIAESVIAYLCSLAKEVLMQESNVVRLSTPITVVGDIHGQFDDLLEIFRIGGPCPYTNYLFLGDYVDRGYYSIETITLLICLKLRYPKRITLLRGNHESRGITQTYGFYSECLRKYGNANVWKYFTDIFDFLTLSATIDDTIFCVHGGLSPSIQHIDQILVLDRFREFPHEGPMADLVWSDPDPSVQEFSLSPRGAGFSFGEVIVTKFLEYNNMKHILRAHQLCSEGYQILFEKKLSTVWSAPNYCYRCANLASILQIDTDQSRFFNVFDAAPNQETPFVEPAAKVTAEYFL Q10299 CLP1_SCHPO BINDING 11; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03035"; BINDING 49; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03035"; BINDING 116..121; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|HAMAP-Rule:MF_03035" SPAC22H10.05c; CHAIN 1..456; /note="mRNA cleavage and polyadenylation factor clp1"; /id="PRO_0000116579" MKEIFIPKECEWRFEVDEPAIQIRLVSGNAEYFGTELALGPPYHFTRVKGAIYTWQGCTLEVEGEPSVEYVAEETPMSTYLNLHFALEGLRLQAENAAANDESSYGPCVCLIGPRSCGKTSVLKILESYALKQSRHPICVNLDPTQPMLALPGSISAFHNATILDIQDADGFGASTSTGPTHVLAKVPLVYNFGLDSPLDNPKLYKLSLSRLALAVHSRMSQSKDARVSGCLVDTSSIQENAEKYQDILHSIITDFRINIIIVLGSERLYSSMKRKYADATWLSVVKVSSSGGCIDREEEWIQQFQARCIKQYFYGDDRMPLSPLSMIVDSTQLVVYRVLEASESGPKSSVLPLGFEEENTQSEKQDGNTSLRLHGKGEFLERISTEAMTILQNSILAVSSVGEDEDEATVVDSCIIGYVFVSDVDDVKNRMTLLSPVPEQLPSNALIMGTCKWQE Q10304 YD4B_SCHPO MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22H10.11c; CHAIN 1..629; /note="Uncharacterized protein C22H10.11c"; /id="PRO_0000116583" MALTNGRIEEYDIQNGYQNTEEIKKLPAELNFPVDFDKMPTFIFQEERQKLDLPLSDSEENQFHDFSDSKLSLGFEIGRSKEKFVDEKPFYSNKEPLKINSWKKSSSHPKSKEVSNGLLKVSTPPTEFVKRENAGIRRRSSNQGSFALEAPKILKRDAMFKESWKNKCFISPQKDNQGFSKSKHLSTYEGETENGFSTSTEEEEEEEEDIVSASWVDNLDMDMASFNSHRERFLTEHVNMDERSDDDFLLGLISSDSSVDDHDNEQDDVDLIGWECFFDDSSDELNTLSHQADDEGDTTDEETPELQNNKLLNLSTPKKSFGQTPRIKTELSESPNSQRTLLSAVPTPLELSAELAYKEDLTSLASRANISDNSTGLTPTLAKATLAQPVSTVVSVASFELDPRLNITQPKPPVMGTWAKEPNHLIGIIDGKHSHSLHHDKFDACTKGENTANNGYGPQTLNETSEEPSLDDILDTSLLQPSTQTDLQEENSVSFAQEDNSLSRWEKIPIGTFRKNQYIKSMARRDELIRDEWFTLAIKTREKRRHKINATGMTTTNSVPLRPKSRKARRALKKKARKMTFRQMHSDFQSALEDEHNDGSYLDNDYETVGLGLGPELSPLFEILESSGY Q10306 CISY_SCHPO ACT_SITE 320; /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"; ACT_SITE 366; /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"; ACT_SITE 421; /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU10117}; TRANSIT 1..16; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC6C3.04; CHAIN 17..483; /note="Probable citrate synthase, mitochondrial"; /id="PRO_0000005478" MMIILNAPRFMTNTRLASTRRLASSLLSQASLRSRQLNPLFTSSYSTRSSSLKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGKQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKHDYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFANNEEFVELMRLYLTIHADHEGGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGVASQLIWDRALGLPIERPKSFSTEALKKMVETK Q10313 TRNL_SCHPO ACT_SITE 117; /note="N6-AMP-lysine intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.3; Evidence={ECO:0000305}; SPAC17G8.01c; CHAIN 1..787; /note="tRNA ligase 1"; /id="PRO_0000116589" MTRDQRVCIFGEKKSTVRSVTFKAPKSNYDLTSWRIWEQAFRLNVSNSKKCFDTISGHRITLPTNARGLFTGYDYESKRHRIVIRGYDKFFNIDEVPITTWDALSQHTKGPYELTVKENGCIIFIAALPDGQIIVSSKHSLGIVEGQSVSHANVGERWLEKHLQSVGRTKQELAHELLRRDMTAVAELCDDEFEEHILPYTGNSRGLYLHGLNRNCPQFITASSCEVAEFAEQWGFMKVSSFFMDSIHELKAFLENASKDGKWNNRAIEGFVIRCHSDHSSLEQQSSNDFFFKYKFPEPYGMFRQWREVTKMLISGKKPSYTKYKKVTAEYITFCDKKFKEDEDAKRLYMSNKGIISLRDEFLVLSKLDLMHLSVSNDNDCGKEFTLLVPIATIGCGKTTVAKILEKLFGWPVVQNDNLPSGKGGPKRFAKAIIEEFRNGHSVVFADRNNHISNMRSTLQTDILALIDGVRFVALPFKHTPEVPEFVQNRVLQRGDRHQSIKVSEGVDKVKAIMNTFYKQYKPFDPAGNKHDANYDDIIELDPLIGSLENARRIVNYFKKNIPELIPNDPSDDDYAAALNYAVNEYVPTYRKTFGNDSKKIKNKITAEGITGSSTCFKKAPRYFGVLLDRKTVESSLVQVLTIANLQWQEAFSRYTLQDSFHITMIHESQKPVNSRIWEQYLQHMHDKNTTKMGNISFRITHLVWDDRVICFRVTMNENSVWYGKTCNPQLHITLGTSSSDVKAFESNFLLKKLRWQGDEVDSTDGNVRYLTVLPKIIIEGMLEPVY Q10317 MED20_SCHPO SPAC17G8.05; STRAND 3..8; /evidence="ECO:0007829|PDB:5N9J"; STRAND 32..45; /evidence="ECO:0007829|PDB:5N9J"; STRAND 51..58; /evidence="ECO:0007829|PDB:5N9J"; STRAND 63..68; /evidence="ECO:0007829|PDB:5N9J"; STRAND 72..76; /evidence="ECO:0007829|PDB:5N9J"; STRAND 95..105; /evidence="ECO:0007829|PDB:5N9J"; STRAND 108..117; /evidence="ECO:0007829|PDB:5N9J"; STRAND 124..130; /evidence="ECO:0007829|PDB:5N9J"; STRAND 169..172; /evidence="ECO:0007829|PDB:5N9J" HELIX 12..15; /evidence="ECO:0007829|PDB:5N9J"; HELIX 18..29; /evidence="ECO:0007829|PDB:5N9J"; HELIX 78..87; /evidence="ECO:0007829|PDB:5N9J"; HELIX 136..150; /evidence="ECO:0007829|PDB:5N9J"; HELIX 175..185; /evidence="ECO:0007829|PDB:5N9J" TURN 59..62; /evidence="ECO:0007829|PDB:5N9J"; TURN 69..71; /evidence="ECO:0007829|PDB:5N9J"; TURN 153..157; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..193; /note="Mediator of RNA polymerase II transcription subunit 20"; /id="PRO_0000116590" MPVHGVIYYSSPSMATFLSPAQDNLVRTYFAQHLKKWVVQYKLYRNAVTPKTLEFLKQNINPSMLACVDEATMIDAEPELEDIIVRTKLWNFRQSFTIEGSIYEVGSFKVAIANVLQKSVWKGILFHVTYDGTESVDLARPIIQEFFLKCFLQNNKSVTPVYESFFNQPRHSLDSKLLLQLFKQRIDTVSQRT Q10320 YD68_SCHPO SPAC17G8.08c; CHAIN 1..287; /note="GDT1-like protein C17G8.08c"; /id="PRO_0000212468" MKNPIKWAIIAVLLSTVVAKKIVGEGMADVSAIKHPEEVHPTNRDFLRSLIFSISMIFGCEIGDKTFIVAALLAFENSRLTVFAGSYSALFIMTLLGVLLGHAAPLLFPRKLTDILGGVLFVIFGIKMLMEAKEVMDSKESMSDEFQNVRNEIAANGPIDQLLEEGAAPSHYTGHRSRSGHTLMSQLKSKGRNVMATLFSPLFIKAFALTFVSEWGDRSQIATIAMAASDNVYGVFMGANVGHACCTALAVISGKYISTKIKVHKVMFIGGILFIAFGLVYFYQGFF Q10328 PHX1_SCHPO SPAC32A11.03c; CHAIN 1..942; /note="Homeobox transcription factor phx1"; /id="PRO_0000049410" MRSYSNPENGGQINDNINYSEKRPTMLPENLSLSNYDMDSFLGQFPSDNNMQLPHSTYEQHLQGEQQNPTNPNYFPPEFDENKVDWKQEKPKPDAPSFADNNSFDNVNSSKLTNPSPVQPNIVKSESEPANSKQNEVVEATSVEKAKENVAHESGTPESGGSTSAPKSKKQRLTADQLAYLLREFSKDTNPPPAIREKIGRELNIPERSVTIWFQNRRAKSKLISRRQEEERQRILREQRELDSLNQKVSQAFAHEVLSTSPTSPYVGGIAANRQYANTLLPKPTRKTGNFYMKSGPMQSSMEPCIAESDIPIRQSLSSTYYNSLSPNAVPVSSQRKYSASSYSAIPNAMSVSNQAFDVESPPSSYATPLTGIRMPQPESDLYSYPREVSPSSGGYRMFGHSKPSSYKASGPVRPPNMATGHMRTSSEPTSYDSEFYYFSCTLLVIGLWKRLRASPQDLMCFYSPPKKLFAYLIQFQGIQYRIEYSFFVIESIHVFRVEEPLLNELSATASSRDKPAPNEYWLQMDIQLSVPPVFHMITSEGQGNCTDFTEGNQASEVLLHSLMGRATSMFQMLDRVRRASPELGSVIRLQKGLNPHQFLDPQWANQLPRQPDSSVFDHQGRNPPIQGLSHDTSSEYGNKSQFKRLRSTSTPARQDLAQHLLPPKTNTEGLMHAQSVSPITQAMKSANVLEGSSTRLNSYEPSVSSAYPHHNLALNLDNTQFGELGTSNISYPLSAPSDVGSLPRASNSPSRPVMHPNTQGINTEIKDMAAQFPNSQTGGLTPNSWSMNTNVSVPFTTQNREFGGIGSSSISTTMNAPSQQLSQVPFGDVSLATENSVPSYGFEVPSEESVYAQARTNSSVSAGVAPRLFIQTPSIPLASSAGQDSNLIEKSSSGGVYASQPGASGYLSHDQSGSPFEDVYSPSAGIDFQKLRGQQFSPDMQ Q10329 PSA4_SCHPO SPBC106.16; CHAIN 1..259; /note="Probable proteasome subunit alpha type-4"; /id="PRO_0000124164" MSGYDRALSVFSPDGRLLQVEYGQEAVRRGTTAIALRGNECIVIGVERKNVPKLQNVSNFQKIAMVDNHVCLAFAGLNADARILIDKARVEAQNHKLNLADPVSIEYLTRYVAGVQQKYTQSGGVRPFGVSTLIAGFDVGDNTPRVYQTEPAGIYNAWKATAIGRASKAAREYLEKNWKEGLSRDETIHLAVSSLLEVVQTASGNIELAIMDPGKDVEFLHSDKIDTIVKEIQDEKEAEAARKKSGRSAPGVSTTSTIQ Q10334 ALAT_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate; Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; MOD_RES 326; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPBC582.08; CHAIN 1..505; /note="Putative alanine aminotransferase"; /id="PRO_0000123938" MFTDYPNDINCESPRMSDLDGFCQNAFSDLNSLNQQVFKANYAVRGALAILADEIQDDLLENPSSYPFSEIVYANIGNPQQMGQSPITFVRQVLSLCQYPTLLDHAEEKWFQNLFPTDVVQRSKMLLKESGSLGAYSASQGIPLVRRHVADFIRARDGFDCEPSDIYLTSGASHAARLIMTLIIARPTDGVMVPAPQYPLYGAQIDLMSGSMVSYSLSEENNWDIDFDQFKKSFDEASKKGINVRLCVVINPGNPTGACISENSMEKVLRFAKAKGIVLLADEVYQNNIYQNKFHSFRRKLGELREKEPDNHWDQVSLISVNSVSKGQFGECGQRGGYLDVVNIPEPAKDQILKLATIDICPPVAGQLLVDMLVNPPKPGDPSYDLFIKEVDEIHEALRLQCRQLYEGTKRMKRVSCLEPHGAMYLHPSVSLPEKLITTAKAQKIQPDEFYAIELLKRSGICVVPGSGFGQPEGDYHIRITFLAKGTEYIERFVKAHNEIMDLYE Q10344 TCTP_SCHPO MOD_RES 78; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F12.02c; STRAND 3..5; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 20..22; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 24..31; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 34..38; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 62..66; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 143..147; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 149..152; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 154..160; /evidence="ECO:0007829|PDB:1H6Q"; STRAND 164..166; /evidence="ECO:0007829|PDB:1H6Q" HELIX 67..71; /evidence="ECO:0007829|PDB:1H6Q"; HELIX 81..101; /evidence="ECO:0007829|PDB:1H6Q"; HELIX 106..122; /evidence="ECO:0007829|PDB:1H6Q" TURN 7..10; /evidence="ECO:0007829|PDB:1H6Q"; TURN 16..18; /evidence="ECO:0007829|PDB:1H6Q"; TURN 123..128; /evidence="ECO:0007829|PDB:1H6Q" CHAIN 1..168; /note="Translationally-controlled tumor protein homolog"; /id="PRO_0000211310" MLLYKDVISGDELVSDAYDLKEVDDIVYEADCQMVTVKQGGDVDIGANPSAEDAEENAEEGTETVNNLVYSFRLSPTSFDKKSYMSYIKGYMKAIKARLQESNPERVPVFEKNAIGFVKKILANFKDYDFYIGESMDPDAMVVLMNYREDGITPYMIFFKDGLVSEKF Q10348 YDA6_SCHPO BINDING 43; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 114; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" SPAC1F12.06c; CHAIN 1..252; /note="Putative endonuclease C1F12.06c"; /id="PRO_0000159701" MNNDNLHDKLTIWRQQQIELKGMLQLIPKFQSLNEIRYVVGLDISFDKSSPKAVSALVIYDLEQRMIIYKDYLCIEKLEEDYVPGFLSFREIKWYLPLLNHIPHQFRIDIILVDGNGVLHPVGFGLACHLGVLLNLPVVGVAKNYLHCVGLTESLDAHRETLKKHVLKKTTDHPILIHSIDQSSEILGAAVWTSSNSKRPVYVSIGNQMNLEQSIQLVQKCSSSHSRVPEPIRQADIYAKFVLSQSKRNKKN Q10349 SERC_SCHPO BINDING 45; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 79..80; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250"; BINDING 114; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250"; BINDING 169; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250"; BINDING 191; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250"; BINDING 214; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250"; BINDING 265..266; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810, ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452, ChEBI:CHEBI:58538; EC=2.6.1.52; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250}; MOD_RES 215; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC1F12.07; CHAIN 1..389; /note="Putative phosphoserine aminotransferase"; /id="PRO_0000150140" MSSREEVVNFAAGPAAMITSVVEEFGKDFVNFQGLGMGVAEISHRSKQGSGIVTSAESNFRKLYNIPENFHILFMQGGGTEQFAACLYNVYAHHALKNGNAKSLVANYIITGAWSKKAYAEAERLGFPCHVAVDMKELAGKYGSLPEDKDLKFTPDGETSLVYYCDNETVHGVEFNEPPTNIPKGAIRVCDVSSNFISRKIDFTKHDIIFAGAQKNAGPAGITVVFVRDSVLARPTPAELHKLNIPVSPTVSDYKIMADNHSLYNTLPVATLHAINLGLEYMLEHGGLVALEASSIEKSKLLYDTLDKHDLYISVVEPAARSRMNVTFRIEPQELESEFLAEAEKHHLVQLKGYRSVGGIRASLYNAISVEQTRRLIDLLESFAKAHSN Q10351 PIGS_SCHPO SPAC1F12.09; CHAIN 1..554; /note="GPI transamidase component PIG-S homolog"; /id="PRO_0000218607" CARBOHYD 132; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 375; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSPCKWLTMFLKGCWGKIANMNHLDSCFPLRYIIGRKKASKLLCTMDSGLKSDSHEVERSNFQLNKPEKSLKRYALLSFYVIILLAIPVWWKTTHYERSSLPFEDMENAPSTVQTHLRFSPTFRILDDKGNNLTKEVQKVLEAEPQIYSYNLKVLEDDPVDYRIVLRESTDLQWFWDENNFIIDTPSKGPSELAILIVNCLWEAFSPQVMEVWSKFTRFSSTVEPSRAETKRTVQFSPQYRVLLSLLVGEGNHEPINWDIENAIQKYFNPLIEQLASLAKLNIETQIQYFVEDAEAYIKDDKFCTKHADLPNLVNNFEKYLSFSPHIREPTIHFVLYVPSPQIQPLWLENEDSNIIPTNSMLLPQWGSITTINFNVTEKKLLHDVDLKDYFRVISRDLLLLLGINDVPVSSLSATLADRLLRQRIAESCIEASDTLQNLAKLVHSMQSMAVPKEIQMYVKDTLLSLDMAYKALSQNNLNEALSYSNNAFSKSQEALFHPSMVTTIYFPDESKYGIYAPLFAPILIPLLISFIKEVKDMLRERKLHRVANVPKPN Q10353 RLP24_SCHPO SPAC22E12.13c; STRAND 7..9; /evidence="ECO:0007829|PDB:8EUY"; STRAND 11..13; /evidence="ECO:0007829|PDB:8EV3"; STRAND 17..22; /evidence="ECO:0007829|PDB:8EUY"; STRAND 28..33; /evidence="ECO:0007829|PDB:8EUY"; STRAND 50..52; /evidence="ECO:0007829|PDB:8EUY" HELIX 34..41; /evidence="ECO:0007829|PDB:8EUY"; HELIX 46..48; /evidence="ECO:0007829|PDB:8EUY"; HELIX 53..57; /evidence="ECO:0007829|PDB:8EUY"; HELIX 68..70; /evidence="ECO:0007829|PDB:8ETC"; HELIX 84..113; /evidence="ECO:0007829|PDB:8EUY" TURN 58..60; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..192; /note="Ribosome biogenesis protein rlp24"; /id="PRO_0000136908" MRVHTCYFCSGPVYPGHGIMFVRNDSKVFRFCRSKCHKNFKMKRNPRKVAWTKAYRKAHGKEMVYDTALAVTAARRNVPVRYDRNVIATTLNAMKRVSQVHAKRERLFYKKRLAGKRAQELQEAQKLIAQNVPQFTEPEGEVETAEVQEPQIVSDEEYTMEEEVAEPVKIPVLAKKRKNKKSRNSSSAMQMD Q10358 RER1_SCHPO SPAC22E12.05c; CHAIN 1..184; /note="Protein rer1"; /id="PRO_0000207591" MEFIQRHIENVKEKKNFAVRLYRHWVDRTIPYTTYRWLTVSGLIALFFIRILLVRGWYIVCYTLAIYLLNLFLAFLTPKFDPSVEQAMKDEEIEEGVLPTSKDDEFRPFIRRLPEFKFWYSSMRATLFALVASFFRIFDVPVFWPILVVYYLVLSFFCFRRQIQHMLKYRYVPFDIGKKKFGSH Q10359 GMH3_SCHPO SPAC22E12.06c; CHAIN 1..332; /note="Alpha-1,2-galactosyltransferase gmh3"; /id="PRO_0000215168" CARBOHYD 130; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAVLQWKLSRVIFVLLIIGISSFLIYFQFGNSFSASPALERLQDVFSKPSVQEYDYLVPLDEDMQGLSTTYHQATINEDDPQEPKSHEIVILLASDGRSSGNMAPETFNQCIENRINYAKHHNYGFEYVNVSQMNIPPVWAKMPAIIQTMNKHPHAKWIWWLDQDALILNTELSIQEHILSPDVLVEKLMKNEPMISPFSADLERLTPSSYTVDSARSLGLLISQDLNGLNAGSFFVRRSPMMALFLDLWGDKSFRENKVADHEQALLGYFVRYHPEIAAIIGILPQTLINSYPVGQPEMGWKEGHLVIHFAGCWVENRCQVLWDEYRERVH Q10360 RRN10_SCHPO SPAC22E12.08; CHAIN 1..97; /note="RNA polymerase I-specific transcription initiation factor rrn10"; /id="PRO_0000116604" MSNPPTRPTLYNLVNADGELSYRARDLVQDFSVPIPHELPDPDLVHSIQDFATEYMLATGKKSFECLDESALLGLGYLVTEWMDAMVTDCLEEFEER Q10367 GLO3_SCHPO SPAC22E12.17c; CHAIN 1..483; /note="ADP-ribosylation factor GTPase-activating protein glo3"; /id="PRO_0000074229" MTATKEESQKLLTSLRSQRDNKVCFDCGAKNPTWSSTTFGIYLCLDCSAAHRNMGVHISFVRSTVLDSWTYAQLRVMRVGGNENARNYFKRHGGVSLLNSKDCRLKYSSKTAKQYLEKLKSLAVEDEANYPDILDMDFLSNTHEGSSAADTTNEDDDFFSAWDKASVKKSDDNLDDKTDLASTSSSVVVESGEKDEPVVVTEEKTMVSPPSRPDSTSTTKSKTSSISSARARPIRASSRPTASKLGASRPQKLGIKKANADIDFDEFEKAVLSSESAPTKKPAAVASKESTVDTLVDNGVEEVKESTSTTVQGKPVKPVLKSAASAKSTKSDDSNLNANFARLGFGQFAAASNARAKAAAKARELKKNEVNAPTYARDHFASQKSISSDQYFGRGSFDPEAAAEAQERLSSFRDATAISSKSYFGEEEDENEEGESSHRPDSAYLRDIAETATEDIEAIKVAIHQGAEKLSDFIQKVGARYNF Q10369 YDBJ_SCHPO SPAC22E12.19; CHAIN 1..661; /note="Uncharacterized protein C22E12.19"; /id="PRO_0000116608" MDLTTPEVAEHPDVLRNMSRYTLGLLPSEPPVGDMNNEDSDTNTSITQSPTNSEKLTDILQESQDTKALQEKYLQNIYALTQNQLFKNVEDYSFYNLNREKFQRDKQTIVGVMRKRRHVLNKKIKRLQSHWKQVLGRWEENIARVDRLTEIDKTKNAKKSEPFIKRSTRKVMSNFTAGDIVRSEEEFLEILAKLEQQEKEASNVSEASRIATIPPMILSEEEVKSQYFNDQSRLVTDCPKFYHFQSMPDIWNEEQHSIFVQQFILHGKKFGKIAEAVPGKNSKECVLHYYLTKRTTDYRALVASATKTKGRRRKKLLPSQRGGKKKSKGSALMVDIEAADINKTEENINNQFQEASVTADNMNTWDNTPSVENVESANENVNNHNADEQMDEKIKSLVEGNSAYEIEKGAQEPDPMSIDMTDKSETVSGFKHDVDVYDTAENEGNNTLLQIKESVHEKTPTQDEPMDISQDTIKQEDYYEPKLEQHSSSKRNSISTRKEEDAASALANLSAVGRSISAVDESAHQGHLPGWDEKEEALIFSLAQGMNPMKMPLTPRRASTGPRPRPTFQLTEIDSPNRRRASDCITPSISKILKMVSEDAKSQRIDELSVEDQEHTTHSSHTTSDINAFPNSQSFPRASIHTLAALGEDIVERQSKNDKIV Q10408 YD83_SCHPO SPAC1F3.03; CHAIN 1..1004; /note="Uncharacterized protein C1F3.03"; /id="PRO_0000116596" CARBOHYD 27; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 392; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 418; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 421; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 627; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 859; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSFFKKKLSKGKEILSKSNLKTHTSSNASLSIDDLNRFGFSLNPVLWCLDHQQGLLAIVSSTNRIYIYGKQHVQSVIVPDCSTIVHIALCAAYLIVIDSRNTVLSYPLMKHRDLSKPAATYFLKQKVTCTVTDPTIDWVFFGMSDGSVVPWDVTRHCLGKFKVPNLYVPRHEEWRMMGYSYAPVPGKLSPVVSVQIHPKDLGVILIAYPDGVVLYSIRTDEVIRFYELEYAPGSTAAVLSPHNYRRPIVKGIEWSPWGDHFVSYYTDSTFAFWDVDQEYPVQVRNFVDSNIHTYTPMQRNPPKTELEPIRSMRWCCCEDPTVSFILMLGGLPKEAPVKGISLFSYRNLPAKKDVETFAEFFANPNSQRFFPFIDIPPVRDMLVIPSSSPHYNGSHNPKNLLLLSEDNSLSLLDISTGNISNMSLSIPPSLCFLASDFRVIAFQTVTKKVWNQIEDTISVNSHYSCLFGGSPSPGYLKKLDERNLLITSTGLSLSIWDISQGFMNPSLCVNLDFSSVMRKHLTPSAFITTASFSTYNPEFSCADSFGRVIVCKRKNHKENLPAQLANGIYRLDDTLVLEGTLHAQYYIDLKRGRVTLNQMSNIGFVCIGYQDGGITIIDMRGPHILCNTSISELGLERRGKPDPDFLTSAEFVVMNPKGSPSSIYVVTGTYRGMTLLFRIDPSSSGRFSAYFESSRQLDIKNIYKICSLTQDGQIATATGSSLQSVGYPLPQEVFLVYIGDSGISVFNKINNQVGNLDWRKPVCCRAALVLSTVSKHMGSVVCVNSDLSVNWYSLPNLREERKMQLPLDIDKNRLKEGDILGNGDYIFPTLGAHELAFGCVLGSGRTLANLAPMMLITHNASHVPPRPSKSLWNWLLGEQSTSAEELDILLGGENRAESKVHTLETPKVISARPAESVKQPLTPVPSMTSQSAQSYIPPRRQQQQKGFFAQINDHLAQRGNMLGGIENTMDDLEEMSAEWANEIKDSLAGTKKDLILSGLKSYIP Q10409 TSR3_SCHPO BINDING 43; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:E1QU22"; BINDING 91; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:E1QU22"; BINDING 114; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:E1QU22"; BINDING 129; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:E1QU22" CATALYTIC ACTIVITY: Reaction=an N(1)-methylpseudouridine in rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-carboxypropyl]pseudouridine in rRNA + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:63296, Rhea:RHEA-COMP:11634, Rhea:RHEA-COMP:16310, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; EC=2.5.1.157; Evidence={ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-Rule:MF_03146}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63297; Evidence={ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-Rule:MF_03146}; CATALYTIC ACTIVITY: Reaction=N(1)-methylpseudouridine(1191) in yeast 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-carboxypropyl]pseudouridine(1191) in yeast 18S rRNA + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:63300, Rhea:RHEA-COMP:13852, Rhea:RHEA-COMP:16309, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence={ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-Rule:MF_03146}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63301; Evidence={ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-Rule:MF_03146}; SPAC1F3.04c; CHAIN 1..288; /note="18S rRNA aminocarboxypropyltransferase"; /id="PRO_0000094427" MGPRSSNRRSNAKDGFKGSNKASKFPLPLAMWDFGHCNPNACSGKRLERLGCVRNLRIGQKFRGVVITPNGKVPVSPADKEYFDNGGASVVECSWARIEEIPFSRIGGRCERLLPYLVASNPVNYGRPWRLNCAEALAACMYIVGYPNEARLLMDNFKWGHSFFEVNEELLDIYAQCHDAQDIQEKEKKYLEEMEASYQEQRNQTTDDIWSAGNLNHKPTLNTSSTHSNSEESRSPLHEPSEASLAHDEHSIPTDDNEETLTNLQANDVDEDEVWRKIVRMKVHSTDT Q10410 YD85_SCHPO SPAC1F3.05; CHAIN 1..510; /note="Probable ADP-ribosylation factor-binding protein C1F3.05"; /id="PRO_0000212688" MRSSQTLSKYIDKATDQFNLEPNLALNIEIADLINEKKGNTPREAALLILKRVNSANPTVSYLALHLLDICVKNCGYPFHFQIASEEFLNGFVSRFPNHPISRMNKIQSKMLEMLEEWNYMLCKNNRHREDFSRIHDIRELMAFRGYKFPAVDEDSIAVMKPNNSLRSAQELAREDLEAHKAKLQELLRRGTPMDLAEANALMKVIAGYDEENTEDYSALAAADLESIRSKALRVKQFLVNQTVSLEEGTLADAVESLKVYQTKIARILREENEDEYYVQKLLSLNDLLINVIEECSNSDLIHSGTNVVSSQPNVVESHVPPSSNDTKQESSLIDLMKLTEEPAVPSPSLPTNVPANQSLSMLSSLSNSMSSTSNGALNSPSYSQAAIPNTNSSLTSILQSDSLMISTQLTSVQKSSGFASYSVQFSNCSLTWPVSEVVFQVAVVKSLKLQLLPHTGDAIIAPGKQNAAHEIMNITNIPADASDLRIRWRVQWIIGTDHRVEQGESHLPL Q10414 MU161_SCHPO MOD_RES 296; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 298; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 317; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 319; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 331; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1F3.09; CHAIN 1..561; /note="CWF19-like protein mug161"; /id="PRO_0000116599" MIFYDKLKPADVLVIGSADGRVIEAIEYIADLHKQHGFKFAICLGNLFSHKRTTSADVVKLKNEKVKVPIPVYFGVGTAGLPESIISHMAMYGPEVAPNLFCMGICGFMKTFYKFTIAQLGGSYNEEKYYQPPEKFEQSLNEKCFHRSDVQKLSKRCDILFSSEWPEDVQENSTLPERKLPKGCMPLAALAANCMPQYFFVPGPVYYEREPYKNSAAINVNTGTVTHFVALAPFKNSKNEKFSYAFTLYPLTTEYMQPAPPNCTASPFEHRPIPLKRASEDQIIPQQTNKFHKSKSSTALFKSKKDSSSSLNKMHKSESHSALNNLHKSESGTSLNNRRSKVGPGSCFFCLSNPNVALHLIVAIGNEAYMALPKGPLTTTASNTPALASSGHVLIIPIAHASALSTLSDTSYEKTLNEMNRFRKAVTDMYNACDSDALVYEISRANGVHLHWQMIPIPKISSHRIESVFLEMAKEAGYDFEERDVEPHELNYFRVFLPSGKILIHRLQLRERFDLQFGRRAAAKILGLEDRVDWRKCVQTEDEEKAESEAFKMCFKPYDFT Q10415 PMIP_SCHPO ACT_SITE 545; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 544; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 548; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 551; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" CATALYTIC ACTIVITY: Reaction=Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.; EC=3.4.24.59; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion. {ECO:0000250}; TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1F3.10c; CHAIN 29..762; /note="Mitochondrial intermediate peptidase"; /id="PRO_0000028582" MQVRTLLTLGKKKVIGNRQCILSLYRKYSNVQSRKAEDQLLRQIFDDQNIAVNQITKRNGIQGVGLFRNHFLSDKDTGFLRLAETASEKCKAVIEDLLLEDTEDGSIVVSKFDRISNLLCSVIDLFEFVRCAHPDKMVVMKAEEAYSYLFELMNTLNTHQGLYEKLKCSLQQTPTLKDTDPEAYTVGRVFLQDFEKSGVNLESSKRNSFVKKSSESATLGRAFFNNSMNRPQRYLTISKQRLAGSDPYFVRSLSKNDKNFIMIPTVGYEGTQALISVANPDVRKEIYMEGHKGTVEEVELLNSYLRSKAEVAKLVGKSSFADLQLIDKMANAPKHVVEFLENLSLKNSSVLKKILNNLALMKKKELNLNFLPSFDVWDREYYTARYKQSLINQKPSLNPSITNYRRFFSVGTVIQGLSRLFSSLYGLRFVPADISPGEVWHPDVNKVNVYNENDHVMGVIYFDLFARTGKTDGAAHFTIRSSRELDLTSFDDSISLGFDDATNIRVKDNKRYQIPVISLLCNFVRSSGMDPTFLDLWDVKTLFHEMGHAMHSILGHTKYQNLAGTRCATDFVELPSIIMEFFMSNPAVLPLYARYEGTEIPLPVQVLNHHNMVENSSAPLDLQSQICMAMVDQLFHSKVVLDPSFNSIDEVTNVTRKFSGFESAPPAAWYLQFSHLYGYSATYYSYIFDTVLASLIFSKLFAGNPLSREAGEKFRKAILRWGGSRSPWECVAEALEQPILATGGEEAMRRIGSEGIKATSTF Q10427 YQ29_SCHPO ACT_SITE 216; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 240; /note="Proton donor"; /evidence="ECO:0000250" BINDING 94; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 132; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 133; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 185; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 214; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 216; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 219..220; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 220; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 240; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 244; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 307; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 355; /ligand="substrate"; /evidence="ECO:0000250" COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 2 calcium ions per subunit. {ECO:0000250}; SPCC11E10.09c; CHAIN 1..478; /note="Uncharacterized glycosyl hydrolase C11E10.09c"; /id="PRO_0000054345" MNLICSILPKKEPSYLKLWRKQVIYQVLTDRFALDEDNFYAKASGNLYLGGTWKGITRNLDYIKSLGCTAIWISPIVKNISETTDCGQAYHGYWAQDMTQLNENFGTEEDLKELVNAIHEKNMLCMVDIVVNHMGHAGSKPVNFLLYQPFNSGKYYHNWQFVQNYDDPHETITGWLGDSHVNLPDIRTEKNEVRKFFQNWVSDLIKRYQFDGIRLDTAKHVEKSFFPTFIEAANVFTTGEVFHGDPKVVGDYQKYLPSTLNFPLFFQLRETFLDPKHSMFSFYDKAVLDVRHYFKDVTVLCNFLENHDFPRFFHETKDIALALNALTALIFMDGIPIIYYGQEQMFDGGSDPDNREGLWKSKYNTSNPMFRHLSSMIRTRQNLVETYPEFTYVLSFQLYIDDSVYVFTRPGVIIAISNEGSTSSFKVEIDLKEHWKEVPSSFTDILTQKTIPCKDHKLKIKSKSGLPKILISSDPSFL Q10435 YDE1_SCHPO ACT_SITE 1614; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; SPAC12B10.01c; CHAIN 1..1647; /note="Probable ubiquitin fusion degradation protein C12B10.01c"; /id="PRO_0000194999" MSVQAYTNTPNLPNLIHSESITNSPVFIPNLRSKSDNKHRLNTSEELPFTKKRRATKHFLKMEVSAKISEPPSSKSVEFGRHLNMRHDFSELLEQPLTTSKTRVFKSFNEKLKGKPQLVKSDKGVLPLNKQSDILNSYERVLSNASVDSALDKKAEVDIIPFDKSVMEPKNITFNDKSGLTKFGNSNSYETTYSDSSNYHTSTDSSQYNDQDDHVYDDTNDGTDDDINNNEYKDDESSSGSESYERDEDVDEEEEEDDDENNDEGDDEDENENDELRSENGSPNPSAAVINEQENMNMSGIEEYDETNLLNELGRIRRGNQFQSLASSILSSGNLENSDDEDVSLGPQTYRFNSSFHPFRSAFSAPGVQFGRLLEGIKDFSDPTVQMLSLQELSEAFAMSTEDMLVGLFSTDSYIAAFSEILSGRNYDFGEVSIQLMLSCTTCVSNMMEALPLCMAKIAYSPIVRILCERMFDMQYIDIAEQALGVLERLSKDFGICILEHRGMLAALQYFDFFYTTVQRTAISLAANCCKFLDESNASAAEEIIPLLSNILQSSDTIVVSKAYSCLETIIESLKTSPNIIETIISEDLITTIVNALTNSTSQNKSMHLQVQLLHIISSLCQSSSALILPFLNHNLPDVMYEMLCGIPPSDTSHQADMITMQSLYYCPIELIENLLRAITSLLPKNTSNLSDEFNTKLYRLNSILLTVVMDIYFIVPLHDIRSLAVTTALKMLCSIRENNLDGLVCSLPLSSFIASILNSRKSDNFLKRDALEMCLFLLEALPNVYSSLFIREGVVQEVGFLVRSTNADMKKIKLSISFSQNKSAARHEELKNLSTLKSLAKEFLSNYKEENLENSTLVQLKQLSKHLLSETKQDESFSELAKIFQEGSNITSHELLHSGLIHNLLLSLKKFGSSSLRTFLLAMNTCDEREVLEFGNGPLVSLIFCLQNLLSTVENFQLSTLPPDTENAVDHVFSRQFKLRLMALPGSRIRPPFRSLVVSINGLATIRTLDNYLHSRISVRNETGRRFSILREAGSLRESMSGSSRNSSGDYTDSMSQDAPNHTTEPSERRDSSTSSHFEEHFVFSLMGKKVPRNKTIFRILYEYIQLSDDHTLDDFWKTPVPIFYGEPDCIHNDMKGELNYENETEGFSINIREILDLLSILYYGIRDVHTLFPDKHFRGNIENILTDFSNWKLSAKLNRQLEEQQLVVHGCLPSWCISLTSAYPFLVPFETRYLLLQSTAFGLSRSVSFLLSRNPELSKNESSSILQFVSLHRQKIRISRKKIFNYALHLLATYAASENILEIEYEDEVGSGLGPTLEFYTSVSKEFTLNSLDIWRNDQPNSKFVYQASGLFPSPIPLLGSSPENERKISLFFALGQFVARSIYDSRIISIQFNPLFFARNIPLTISSVAKVDKGLANSLRYLEKLIPGKNPTNAETDIKLEDLHLDFTLPGFPSIELIPDGASTPVTTFNVSDYLNYVIDYTVGKGVQQQLEAFQNGFSSVFPYTSLQVLTEHELVTLFGTVDEDWSYATLMKSIVADHGYTMESPTIQRLLTLMSQMNFQEQRDFLQFITGSRKLPIGGFAGLNPPLTVVRRLNEPPYVPDDYLPSVMTCVNYLKLPEYSSSEVLGSRLSKAILEGQGSFHLS Q10438 TTL_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-tyrosine = ADP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H(+) + phosphate; Xref=Rhea:RHEA:17605, Rhea:RHEA-COMP:16434, Rhea:RHEA-COMP:16435, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58315, ChEBI:CHEBI:149554, ChEBI:CHEBI:149555, ChEBI:CHEBI:456216; EC=6.3.2.25; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; SPAC12B10.04; CHAIN 1..403; /note="Probable tubulin--tyrosine ligase C12B10.04"; /id="PRO_0000212447" MSSTKKDIKVYVNYRDEYAEPKIISALKNSGKELTFTNSAKEANFQWAQYEDIDFDEVYKNPKTKLCCSYVIRKALIRKEYLWRTVITYLAKHPDSILSKSVPEAYSLELDYAEFLDDSLMEAYELRQELEENATKNISEKQWYILKPSMCDRAQGIRLFSTIEELQAIFDSFDDEESESEEAGLEEKGDITVAFNNKIVISQIRNFLVQKYISKPLLLDHRKFHIRAYVLATGALSVYLFNEMLCLLARDKYKKPTPDPDLLFSHLSNTCLQGDNVEQSSIRDFWNTSIENKDDIFKSILNIIGDVFEAAATTQGIHFQPLENCFEIFGVDFLVDCESQVYLLEVNSYPDFKQTGKNLSNIIENLFSAVVETAIIPFFESSTKRNVDSKLTLAKKLQLFGFR Q10439 ICP55_SCHPO BINDING 317; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 328; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 328; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 407; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 434; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 457; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 457; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.; EC=3.4.11.26; Evidence={ECO:0000250|UniProtKB:P40051}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; Note=Binds 2 manganese ions per subunit. {ECO:0000305}; TRANSIT 1..19; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC12B10.05; CHAIN 20..486; /note="Intermediate cleaving peptidase 55"; /id="PRO_0000185096" MSGYIRTLFIRNRFSNYRLRSQIIKYKYSNVSYLNKSALRCGQATDSTHPHILQPGELTPRISAQEYKTRRDRVASLLEDNDFMIVTSAPVRHMCGAAFYEYHQDPNFYYLTGCLEPNAVLLMFKNGASGSYDCSLYLPSKNPYIEKWEGLRTGSTLGKKLFQIENVYDSSLASSVINALGKKSNRIFYNYQTGYLSKMPAASAPEFIQDTLTKLFRTSTQRSVDELLHPLRSIKSTAELECMKEAANISSNVYREIMRKRFEKEAEMSAEFNYRFCIGGCDRSAYVPVVAGGKNGLTIHYTINNDIFRPDEMVLVDAGGEFGGYVTDISRTWPINGKFSTVQRDLYQAVLNVQKKCIKYCCTSNGWSLADIHFESVKLMHEELKQVGIHGTKREITDILYPHSIGHEIGLEIHDCSTNNGYQPLRKNQVITIEPGLYVPEEDGWPQWAQGIAIRIEDSVIVGDDKPFVLTSAAPKEIEEIEALKK Q10441 TILS_SCHPO BINDING 30..35; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2); Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665, ChEBI:CHEBI:456215; EC=6.3.4.19; SPAC12B10.08c; CHAIN 1..456; /note="Probable tRNA(Ile)-lysidine synthase"; /id="PRO_0000181822" MDTIKLKEFYNSLVSIRRRVGHRRLGIAVSGGVDSMLLSWFMKESQIMFGWPNQFIAFVVDHRIRKNSTEEALQTIWNLNRMLIPNVYLNINWGNDDVHSLTNLETIAREHRYQVLTRACITHNIRHICTAHHANDQAETIFMRLLRRKPGTWGGLCAMKPVSQIPESDSICGASNIELLRPLLPYYKNQILNTAKQHGIAWEEDPTNADINLTPRNAIRRFLNQHAALTVEATKLATAFQSLQVNIDNKVDEILKDNIVSYHQPSGTLSLCFSKNELKKHSNLTKEELLLRCLTLTTSCRQIKRSSVVSLCNSVFDGKKLTIAKCLLTSSSIKDDTKLQLQISRQPFSKAELKKKTITINPDRYVLWDHRFWIKYSCKNTQTTLILRPLLSKDLNSLKGFLSKEEFLKFCIQVPGHIRFTIPVLSEENDKLVGIPTFGFNFRSDIISNCLHKFKL Q10445 RHP41_SCHPO SPAC12B10.12c; CHAIN 1..638; /note="DNA repair protein rhp41"; /id="PRO_0000218296" MMSDEDNTYSDDEEWLDLDLGLPNNDIKTAPILNSSLLSSAVHGERLIQERPTHDFGDVEATVDRTVEKRSRLKITSVDRKIRLQIHQLHLLCLTYHLCTRNTWCDDNRLNYLVKYIPPGIRVSLHPSSQKSQMIRNKTFLHGLAGLVEVWKRKYKITTNGLRKPNYGLLQNNSLISESLSLEEFCKNSKLLSGSRDYGTQLFASILRNLNVPTRLVFSLQVLSFRFKGAINEASSHEIVPAWSQQMENDSSSDISESAHITSRFRKRRKIIQPSFSNLSHLDASDIVTEDTKLKVIDSPKPVFWVEAFNKAMQKWVCVDPFGDASVIGKYRRFEPASSDHLNQMTYVFAIEANGYVKDVTRKYCLHYYKILKNRVEIFPFGKAWMNRIFSKIGKPRDFYNDMDAIEDAELLRLEQSEGIPRNIQDLKDHPLFVLERHLKKNQAIKTGKSCGRINTKNGVELVYPRKYVSNGFSAEHWYRKGRIIKPGAQPLKHVKNGDKVLPLYDEEATQLYTPKPVVANIVPKNAYGNIDLYVPSMLPYGAYHCRKRCALAAAKFLEIDYAKAVVGFDFQRKYSKPKLEGVVVSKRYEEAIDLIAEEIDQEEKEAEARNVRKTCLLLWKRLITGLRIRQRVFEEYG Q10447 PPK2_SCHPO BINDING 394..402; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 417; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" MOD_RES 358; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12B10.14c; CHAIN 1..665; /note="Protein kinase domain-containing protein ppk2"; /id="PRO_0000086829" MLSNSTFHEHHAKSHFHNNACQSNASSSACRASEDHLVSSFPNDSIIDLQPSRPAPEPPKKKFGYYARRLSGHFLSLIHGSGNSTRSPPFHLQNQKSNGQSEVWHSSDDSGSPKRLNRSRSSKEDMYRRRSLHGLPSLSRRNSKKSSTLSRSISLHLRSESAPISLPIHLYKSYSYNHSPSSLPTVLNSQALSSPPVPTTPDEVSTNRLSSSTSSMNCRNLVPDNFNISIRPNTTNYRSSIQENSNGNRDSISPSAYDAPLLHNVDTQSIDGFVSVASHFSSASTAESLDDGHSATTIQQGDVSSYPLSRSVSTPVPMSPISISPAKPSPQSPKLSQSAVGHPSSSIPAAAMHKVSYSDDLMRFVAREKYYLQIVDCLCTQKDPLFFYTDFTKICQQDTVGTYVARQTLDKEVVVIKRFDISAVTHRRLLLEELQRLSGLSHKNLIRYNESFWYLNNIWSVFEYKDPSTKLSALIPKYFFSELNIASICYEISSGLAFLHNSGIAHHNLTTECIYLTKSSCLKIGNYAFSSPYIERQTNRGAVSHVPDWLIEKNYKEGFMKDVKSLGLVALEIFQGQPNFFRKSIQSIQLTPNANVLVNRVRGLISQEFKEFLLQTLQAETLQGPNINMLLETSSFLEKRQTLNFEICLNNLNLRERKASRYSYL Q10451 PPR5_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1093.01; CHAIN ?..1261; /note="Pentatricopeptide repeat-containing protein 5, mitochondrial"; /id="PRO_0000116844" MVYTKAWFLQNIARQTLGKNVAVHRPPLKLGNMTNWIQQQQAQTNLSLSNTKAPGSLDERLFLTEDDIIFHDRSIQLGYFDPSLSERKQSPPGKSLHRFVDNLNPNSSHFSASLLPASLSSLCDSTCGDVDDEQQFNSLATSPLSTETQSEVSDPLLDTLTPNSLESSFASISLNSFTSANEFIQFLKRLASSKLSIHTFDLYKLVRNSPELLTLEAYNIVLQCMSTDDYFLSSSKNIQKIIKVYVDMLNSFISPNVTTFETVIFALCRRAKFVHQKIESLSKRTIYAHPSIAKEIQPELLDLQSEMPLQTAVFMFTSSLINHDLIYSPQFYAILIESVSLYGTQSQLDSLLECVPLGTIEANGHPDLLPALIRALGRAKRLNSCFQLLERYNLSDPTSDTSMTNVRSWEGLMEAYFDTDHHVEASALMKSFFRKADSNQVIPSSILDCFLRRLAQLGHYKESAEWLGMAIEKISTYKASPSTLSSILEAACLNNNDKFAIAFVRKYTLSRFSDCHAVLLRYLDLLARSGNVDLLHLHAYPVICSVSSHTNFTFSNVYKAFIENGKIDVALRLLRKHIDPKVSLGNNTAPSSNSVALQLSILNGFWEVLTEELQKDVHVLLSLVSTLENQVNFPQVDFTTPLLRHITGYLVSRRLEPELISPRVFGFLLEYAAFNVVQTEGTFTSKVILTDLLKCYSNGTYKASFKNVHVVLRSFTYLKEDEMLVASVRDDIVSEAVVGFSTDNNGQKILADISQVCYCLDDLECIDQSINSLVSKMLTSASPEQVDVNILFFQFGKLIETNKFLHPEVYPTLISVLSKNKRFDAVQRVFEHSKHLYRKISTKSLEKANWFMALILDAMILSSSFARQFKSSNLFCDNMKMLGYIPRASTFAHLINNSTRRGDTDDATTALNIFEETKRHNVKPSVFLYNAVLSKLGRARRTTECWKLFQEMKESGLLPTSVTYGTVINAACRIGDESLAEKLFAEMENQPNYQPRVAPYNTMIQFEVQTMFNREKALFYYNRLCATDIEPSSHTYKLLMDAYGTLKPVNVGSVKAVLELMERTDVPILSMHYAAYIHILGNVVSDVQAATSCYMNALAKHDAGEIQLDANLFQSQIESLIANDRIVEGIQIVSDMKRYNVSLNAYIVNALIKGFTKVGMISKARYYFDLLECEGMSGKEPSTYENMVRAYLSVNDGRKAMEIVEQLKRKRYPLPVVNRISSLVNSHMGQKPKRRSLNTSHSSLASLGNASTQHSINSSIN Q10477 MED27_SCHPO SPAC17C9.05c; CHAIN 1..273; /note="Mediator of RNA polymerase II transcription subunit 27"; /id="PRO_0000096380" MSLEEQRTRDELKHKLLDLNQLHEQLAELRTICPSLLKLLHPETGTSRKFEKSAQEAIEKVNSFYTHLKSSQNVFDYAEKSLQADSSNLLPTYLYNSEDLSNDTENNETKSINGKSALDLKEPHHSELHDNDNFQNSDINIESFKGDIEASGSILTTHENKSFTLKLANELEFIFFHDTRGKFSVYCSSSKDDAITFSINRNNNFLGNLWSLMPKILDYQHLYSKPCDFCKSLISPVYLELPSVRRNANSTVKPTSKDILALHAECVPAQSDL Q10479 ALG8_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + an alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a di-trans,poly-cis-dolichyl phosphate + an alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + H(+); Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502, Rhea:RHEA-COMP:19521, Rhea:RHEA-COMP:19522, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521, ChEBI:CHEBI:132522; EC=2.4.1.265; Evidence={ECO:0000250|UniProtKB:P40351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31308; Evidence={ECO:0000250|UniProtKB:P40351}; SPAC17C9.07; CHAIN 1..501; /note="Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase"; /id="PRO_0000174167" MGKLSMLYNAAIASTFVKVFLFPSYRSTDFEVHRNWLAITHSLPISEWYKSSISEWTLDYPPFFAYMECVLSWIAYFFGFDKAMLDPYNLNYVSPSTVVFQRGSVIVLELVLLFALREYVLSSNVKDQRNALLTAIDIFLSPGLLIIDHIHFQYNGFLFGLLLWSIVLAKPEKNMLLSAAIFSALICFKHIFLYVAPAYFVYLLRVYCFTPNFRPQFLNILKLGSTVISIFLLAFGPWIYMKQIPQLLSRLFPFSRGLCHAYWAPNFWALYSFVDRVAFAVLPRFGYALNQGTSINAPTRGLVGESSFAVLPNIPPALTFYICLGLQITVLIKLFIKPTWRVFVGAVTLCGWISFLFGWHVHEKAILMVILPFSILSLIDRRYLEAFRPLAVSGYLSLLPLLFTLNEAPIKYLFTGAWIAMLLTFDKCAPVPVKRVFLLNRVNIAYISGFVPLFIYNCFIHKLVMGDKFEFLPLMLLSTYAAWGIFWSFVSLLWLYFTDLK Q10488 ETR1_SCHPO ACT_SITE 72; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:Q8WZM3" BINDING 157; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q8WZM3"; BINDING 183..186; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q8WZM3"; BINDING 206..208; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q8WZM3"; BINDING 279..282; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q8WZM3"; BINDING 304..306; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q8WZM3"; BINDING 365; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:Q8WZM3" CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104; Evidence={ECO:0000250|UniProtKB:P38071}; TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC26F1.04c; CHAIN 19..372; /note="Enoyl-[acyl-carrier-protein] reductase, mitochondrial"; /evidence="ECO:0000255"; /id="PRO_0000000903" MSFFKTAVRRFSSTSITRGMAKAIAYSEYGNPKEVLRAVSYNVPKCSKNQVNVRFLASPINPSDINQIQGVYPSKPPFTNDVCSSKPSAVAGNEGLVEVVDVGDQFKGTFSPGQWAILGSVNLGSWRTEMNIDGRSLVPVDKSAFPSIAEAATLSVNPCTAYCLLQHVVQLNKGDWFIQDGANSMVGIATIQLAKHFGYKSINVVRNRPDIEKLKEQLKSLGATIVITDEELMDRKTMKQKVPEWIQGGEVKLGIDCVSGRVAAEMAKYMSKGATMATFGGMSRQPLPVPVSLLIFKNLKFHGFWVTKWKSEHPEEFLKIIHKVEDFYRNGTLKTVNTELVSLKEDADEKTFLDTFLNAIEGHGKKIIKFEH Q10490 SYLC_SCHPO BINDING 740; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; MOD_RES 460; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26F1.13c; CHAIN 1..1111; /note="Putative leucine--tRNA ligase, cytoplasmic"; /id="PRO_0000152154" MATTEPSVEQLETKTAKLKLENTTKRDTLIELEKKYQQKWQEEKAFEVDAPLEDVPIDELRKKYPKFFGNMPYPYMNGALHLGHAFTLSKVEFTTAFERLNGKRVLFPMGFHCTGMPICASADRLSREIEMFGPSFDVPEEKEEEVEVEVKTPNAREDVTKHSGKKSKAAAKTAAVKYQFQIMESLGVPRTEIHKFADAKYWLSYFPPLCQRDCTEFGLGIDWRRSFITTDVNPYYDSFVRWQVNHLHDSGKIKFGERYTVYSIKDGQPCMDHDRKSGEGVGPQEYTGIKMEVLEFPEAARKALQSIDLSNKKVCMIAATLRPETMYGQTNCYVGPNITYGIYESNVPNELFICTRRAANNMAYQKLSKERGVVSELGTIKGQDLIGALVNAPLSVHKQVYVLPMETVLATKGTGVVTSVPSDSPDDFATLTELRKKAEFYHLNPEWMKYEAVPIIRTPSYGDMCAEFLCKKLKIQSPKDVKQLAQAKELAYKECFYQGTMIIGKYSGEKVETAKPKVRKELIDQGLAFVYNEPEGQVISRSGDDCIVALCDQWFLDYGEASWKAVTEKALDRLNTFSPEVRNGFLKTLDWLSQWACARSYGLGTRLPWDPQFLVESLTDSTIYMAYYTICHLLHSDVYGKVPGALNIKPEQMTPEVWDHVFRQAPKPKNTSISDEALARLCREFQYFYPFDIRASGKDLVPNHLTFCLYTHTAIFDEKYWPKGIRANGHLLMNGEKMSKSTGNFMTLHEATKKFGADATRLALADAGDTVDDANFEEALANSAILRLYTQEAWCKEMMENLDNLRTGPYNFHDKVFENEINQLIESSREAFSATLFKAALKSCFYDLQNARDWYREVTADRKMHRDLVCRWIETQVLLLATFAPHWSEHIWLTTLKKPQSIHVSGRFPQVSSPVNTALSNSLLYIRTLSRVIREAEAAQLKRQKKGKGMLFDPSKPKRLTVFVAEKFPEWQAQYVALLQKYYNESENKFDDKAIISSVDKKEMKRAMPFIQQFKQSVINRGEHVSANSIFSRELGFNELEVLREVKPYLVRNVGIQELRIVLLQKPADKSSAAIGLVESGSDAGATVEIAPNFANTVPGQPTFLFENVSA Q10491 SEC74_SCHPO MOD_RES 67; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC26F1.01; CHAIN 1..928; /note="Arf guanine nucleotide exchange factor sec74"; /id="PRO_0000120221" MDESSRIASSSALHGLDEMVSAHKPSPPLPSRRKGKSALRSALEKKNRKSKSKPKVTITSDTPKVSSQHSPVSSAYTGDSTTDLDSKSGHSSSQKLSNKVSSALKLTIPKRWRSSKSSSSQCSSPFLPTSSSNGHGDDASLNLPDKKSRPSSQSSIFLSNWSTIFSSNASPTDSQLSPTHTSTIAELAASTLSIFPSGSYAGSTFGSPSRSSIDSSTYLPRSKSVNSLSSNFSARTPASNQSSVSEDFGAAPNCDHKHNSVTLSDFALPDIDQHDTVETILEKVEFTIPKQFTPAILSQGTSSLLKLCLRKYLSVVNFKCISLDMALRKFLAVYVLPNETQQIDRVLSTFSDQYFHCNPDLYDSSDECYILTFSLMILHTDFFNIHNRQKMTRAEFISNTNLPTILPEILECFYDNITYTPFVHVEHIGCVVTSPSNEKPSLSQRLGDSQFRLTKRNTFATESDHQALQEQLTGFRINLDSILDLKKIDSVRTSIESPTRTADDLYKEFARAPFLQIVSHRSQPQAFSYHFEPSAESESTNPAIINVKVFKLGILIQNEKVRKDRLLSNREVGVILTSSQLMFFKNVYWISGLLDQLEDFKRSHSFSPCYFSPHLTSLSADYIIPLSDLVAYGDGSRIENELYSFSVKQKNQRTHVFSVTNVDELNDWLVKINFVSTFATAGLAPRERLPCVESSDKSIKASVSVLPDIYEDSDAMSKASKETRSEVLECSKVRVYIVQNRIYKLEEALRQGESKMTVQRRNAANILHLEPIQSRTRIRLARCSNTLKKNMLAQMIEIQKFKISIKFLKEDLEMDSHLQDYLRSVFPSSVMGKENASEDTILESNFRNHSNPSVRRSNLRVGKTVESVQNTKLKSVENDSGKAETETVGKNPEVVRKSPAKLPNIANIMTVNGHRYSVVELPDDFLRE Q10494 YDG7_SCHPO ACT_SITE 60; /note="Proton donor"; /evidence="ECO:0000250" BINDING 118; /ligand="substrate"; /evidence="ECO:0000250" SPAC26F1.07; CHAIN 1..321; /note="Uncharacterized oxidoreductase C26F1.07"; /id="PRO_0000124680" MSAEQKYFENAQNVHFTLADGSKIPGLGLGTWRSEPNQTKNAVKTALQYGYRHIDAAAIYGNEDEVGDGIKESGVPRKDIWVTSKLWCNAHAPEAVPKALEKTLKDLKLDYLDEYLIHWPVSFKTGEDKFPKDKDGNLIYEKNPIEETWKAMEKLLETGKVRHIGLSNFNDTNLERILKVAKVKPAVHQMELHPFLPQTEFVEKHKKLGIHVTAYSPFGNQNTIYESKIPKLIEHETIQKIAKSKGEGVTGATIAVSWAITRGTSVIPKSVNEQRIKSNFKYIPLTKEDMDEINSIGIRARFNQATFSNEPVFAGLEDGRT Q10496 GYP51_SCHPO SPAC26F1.09; CHAIN 1..1031; /note="GTPase activating protein Gyp51"; /id="PRO_0000208061" MAFTEANEREVQSSYEKENVKIIREEEAKDQESTDDIAVEDGTGTSPDLNFFSTQNVMQMNFEDEYSEFSNEDDEAEIDNSFADSIPNEPEIPDMQDEYSRDSHSQQSVEEQNNTTNTDEDASVNEFSVAADISDVNTLGKDNSESTEEPVNEVNETATLGNEDVGERSGFPSEGLDNEPESQRDLDETGNLAPEDLKDEVKSVHEFNEPNDLRQQEESYSDDDDTNVNEFEDVNEIENEHQLSVADEDQTSRLVKGKMIFVGKEDFGEEADISNSVFIEQNGPNSDTVSGFKETSSIVNSSSTTEKPGVALDSQNDTSIFNEEQTNSLTETFNDLTLDHLPENVESEPVAGKENETAKNESGASDNDHKANVHVFVLKSSEDAITLNEEKIATQDDPLEAPTPIVASSSTIFLNSNQRNDELSASGSQEPHPKDGTNSTSSLPLDTNNLSNSEPPSHVLDASSETIEVIQTIKKLQNQVPETIKDEVGKKNTAFSPGTSLSTNHVKTKSRSAHNNSTSPFSTAVSSWLNPLRYPSDKSPRVISSYLESVFISKPRSIGDAQKLEILEYLQSQSSTVSNQVFTLLSNFIQNPLFVLDECFDEFRNLILMHNSHTVHTVVWKTISSWTSYDYEMQYSSLSIKNCDSDKAIRKDLDRTFAPEILSHFFSNRQQLEPTDNIAESTANLHRVLRSLAIVLPQVGYTQGMSWIAGALLMHLPAPQAFALLVFLFKNYHLQNIFSSEMRGLSRVLHQFTRLVEDYMPSLAIHFKRQDIKTCSYASEWFLTLFAYKFPLEVVAHLYDILFLYGPGILFNFGLALLSHSQESLLKLNMDRLISYLKEDIFLAFKETQEGENYDTSLFVKTAFSFEIQPDVLDRYGNEYDILLKSEHELDSSLEEMRNRHKSLNEHFIMLSDSMANLQVEHENMSALLLKEKMYLKNQTVEQASLKSEIASLNSQLAKQKSEIEQAFQGDMEAIIAENLEIMVESQSLEDEIFRKEKQLAETKVNLAVLDEDHMMALQKWSQLMNRIKTK Q10499 AIF1_SCHPO BINDING 97; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"; BINDING 99; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"; BINDING 117; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"; BINDING 120; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00628" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; SPAC26F1.14c; CHAIN 1..611; /note="Apoptosis-inducing factor 1"; /id="PRO_0000116625" MLLRFFINQPRFIQFTFLRNKKDRILGLQLGKQPFRMSSSSGLKQQGLAQKKKFQLEFDPSSVSKNGTKTEAKVVGTEFGVLLVRARNTYFATAGKCSHYGAPLAKGVVTSDGHIVCPWHGACFNAATGDVEDTPAIAALRTFPVTEEGDGSLWIEVEDKNDNGASVLQPEGCWRNKATEVYNKGSVETEVTAPHVCIIGGGKGASVAAEYLREKNFKGKITIFTREDEVPYDRPKLSKSLLHDISKLALRSKEYYDDLDISFHFNTDVTKIDLAEKKIYCGSDEKPTESYTKLILATGGEPNKLPIPGLDSKNVYLLRSIADASKLAAVTTEAGDKKNIVIIGSSFIGLELAVVLKDHNVSVIGMESIPFEKVMGKEVGTALKALHEQNGIAFYLENSIKEVKTSSNDSSKAEHIVLKDGQSIPADVVILAAGVKPNLRYLGNAVSLEKDGGVKVDEHCRVLGAEDVYAVGDIAHAPFAGLPSSGEKSHTRIEHWDVAGNLGRVAADHILFGNKAGYTTKSFTPYFWSAQGKQLRYCGNNAAEGFDDVVIQGSLSDYKFACFFTKGEKVVGVCSIMKDPVVSQCARLFIKDAMPSKSQLKENFDVLSIPL Q11118 WOS2_SCHPO SPAC9E9.13; CHAIN 1..186; /note="Protein wos2"; /id="PRO_0000218958" MSLNTQIPEVLWAQRSNKDDAEKNVIYLTVLIPDAVDPKINLTPEKLVIDSKSGANAHYAVQIDFFKDIDVEKSKYSVTGRYIFFVLYKKELQEEFWPRLTKEKLRLHWLRTDFDRWVDEDEQEAQPEVSPFGAGGMPDLSALGGMGGMDFSQFGNLGGAGAGEDASDSEPELEEEEEVGSNEKKE Q12238 UVI31_SCHPO SPBC16E9.06c; CHAIN 1..102; /note="UV-induced protein uvi31"; /id="PRO_0000201231" MIRRFFHTMGRQDRIYKTLSEALKTDKITLYNDSYKHSHHIAMKGVPDTNETHFRLEIVSPEFSGMSRVARHRLVYGLLKDEFDGGLHALQITSSKTPDEVS Q12519 YJ87_SCHPO MOD_RES 9; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC330.07c; CHAIN 1..500; /note="Uncharacterized MFS-type transporter C330.07c"; /id="PRO_0000372716" MEPSQRSGSFSSISRRRSRVDSRPTYFKVTSKDLGFVDQVSEEYEFYTYPKKASEVESVTETFQSNRSSLVPTYPVDENANKLPPKVSIAFILINSLMSDMSLAVALPTSASYTQSLGGTNAFSGLVIGIPTLISLIFLYPMLCFANPKSANGYTLYFRPMVVSSFAHIFGHLLYCMAYRANWIYLILIGRMLNGIGFTTFLYHKKYTTDKLLVGQNRRTFLATMNILAQTLGFMAGPFLGGILAKATIHSKNAVWNQYTVASWVMLFMWFFYMLTIIFFFKEVTADKSEKVSQQKENDDEDRPKLSWKHKFLLFFLAEVAFIAYFTVNGYQASISIYTGKLYNYDAFQSGNFIALSALIVAPFILASSFLSRWLEDRHIMLGGLFLGILAVAIHLVLDAVHKLPMQVYFFLYSLMIYGYSIGSAPLISLSSKQLHPRHHNTASIVVQVGVSLSNTFGSICGGAIYNITTVGFISLCLGLAAVVYMQLIFMWGSLKCKTH Q12704 DPOG_SCHPO CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; SPCC24B10.22; CHAIN 1..1018; /note="DNA polymerase gamma"; /id="PRO_0000101277" MFYKACPSTLTCSKWIHSIIKTKKFLYCRHYSSKSFIDNAPLRINPVGVQYLSPALQNQVFPQQNTQISQLHLDLAKFHLAKHQLLNKETIKLPSFNFRLPPLQGKTISEHFYNIGLEFAEPHLSKAIKFSKIDTPVQPKTWKRQPGWTKYAKDGSISCVPYPDSDCMVFDVEVLYKVSPFAVVATAVSEDAWYCWLSPWLLGKSENDRQLIPSNPKGALFVGHNVSFDRQRIREEYNIKSSRNVFLDTMSLHVATHGMCSRQKPTWFKARKAYIRSQSTETSEDDDSSSFDDDYQNYLKQEPWLAHSSVNSLKDVAKFHCNITLDKSKRDDFASLEKEPILQKLNELITYCAHDTYSTHQVFKKVFPQFLEVCPHPATFSAMLSLGSVFLPVNHSWTRYINGVEEQYQQMIQLVDQKLSQYAEKAKDLINTKDTVLKDPWLRQLDWTPCNLYRKLKKATQEVPVVPKWYKKAYCKTEKRAVITAKSRLAPILLRLKWKKHPLAWSDTYGWVFSVERTSKDEIEMLLDQGLVPCSREEDTKLDYNNYIFFKVPHKDGPEARCGSPLSKSYQRYFEEGILQSDYEVAKKALEMSASCSYWSSARDRIRSQMVVWDKDAELGVPSSVDGFGIILPCIIPMGTVTRRAVENTWLTASNSKKNRLGSELKAMIRAPDGYTFVGADVDSEELWIVALMGDSQFRLHGATALGMMTLEGKKSEGTDLHSKTAAILGVSRDSAKVFNYGRLYGAGLKHTTLLLMQMNPTLKTAEAKELAKKLYASTKGVKSKMSKRLQEMGLPKLTFWSQGTESFVFNKLEAMAQLPSPRTPVLDAGITQALSSKNLSKNSFMTSRVNWAIQSSAVDYLHLLLVSMNHLIKKYYLEARLSLTVHDEVRYLSSDKDKYRVAFALQVANLWTRAFFCQRLGINELPQSVAFFSSVDIDHVLRKDVKMDCVTPSNKVPIPPGEELTIESVLEKLEQSGQSLEPLEQIQCFVDVKATTSAEITEEDKKNIAYLKAQAFY Q1K9C4 YFK7_SCHPO ACT_SITE 997; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; SPAC167.07c; CHAIN 1..1029; /note="Probable E3 ubiquitin protein ligase C167.07c"; /id="PRO_0000351435" MPLSFEGTFKAKRNVNLGGKRVSNDRAQLLRKAAMERKNREEERKAENNSVAVQSLSRGFLARRKFKQDFRERWIYKYTKSGRTSIRFNTLEDIKCSISLLVLFAEPDIDLPFVSQVAHNILVWLENLIPLSNGMDDTPKSHLKVKILKVQETLSNSNDSWLWQRFSSLLLNCLVSSINSHRIEGTDTSAETSLLHCLAYVAPYLKSSELSTYYDSVMTFYAQIYPKQNMTNLEDIMSLSLLTPVSSKTDENANSSSAFLFHVLASDCFSSIENCIPPDLIIDKVFSSSLQLSEEACISSLLNLGMIKVFSLAGNCLHLLHTEYKNSSLWKFCSYILDALYVFSGESVNSRIQVVSDVDDDEDDENAFSQNYYSHLQMVAKHFSKNYANQSGIVQRSFAECISSTFITKAFKLVSSNTLQAMSHFYATMIKLFPSNRTSILMYISLVETNEGSLTRSFSRFSWDMFSESPVYQLFHKKFDVQNVLKNDSGYWFQLQLLIDVYSRMLFTMIDDEFHNDKQNPLYPVMAEFCTVLKNLVLGLYWDVQAAKDVDCKSVVDISQLRVSSTSLLQQLYRINSRKQFLPEDFFLMSEYFNLNEFEANALQESELASHAEAEINITYKFDNFSESRPRLNILNNCSFFLPFHFRIHLLQQLLLLDKQANGYAQPFGHLKHAVIRRNRIFDDGFDAFYNFGKLLKGPIRITFVDEHGVVEEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAHLLYPNTHAYAQDVERLRCYEFLGMLIGKCIYEGIQIDAAFASFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVENDMALNFTVVHEEFGVRNVIDLIPNGSNISVTNENRLQYIHLVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVPIDIDDLRRHTVYAGGYEPNSPTIVLFWEVLREFEEEDKRSFVKFVTSVARPPILGFKALMPSFCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRSGVGFGFS Q1MTM9 YFN1_SCHPO MOD_RES 220; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1327.01c; CHAIN 1..977; /note="Uncharacterized transcriptional regulatory protein C1327.01c"; /id="PRO_0000351072" MMQQRSGSLSLLSNAVQAGQSSDPMQDDPAKTEPGTPKGYDGSKNSSPASVPSWIHEKTKAGKDRKRLPLACQSCRKKKVKCSGERPSCDQCLKHNIPCIYKSNSTKRSHSRHEEIHHQQQLHLNHQYQHQHKNVAANSIDNLSRQYSQPNHINTHDSVNSPPSYGIMASATNQPLSHPTIVPSSNSSSLLNSTNNISHNPQVSLMSASLSKNLVLDPASPKSVSPDLVYVSSDNPPVSTAASAYSSSLPISDVTRALPLAPASNSQHPSLSSQPVSVPSNTINIPTDSLSIVSNPSQTPAKFDSNRISQVPNSDYSIYSNFNNFPIANHAPSFPQSSVKKLDSSFSPTSLPTFTTNSASSGLSTSYTNNNDTTSDNNSLQAVPRLDPVPSLTLSSTPVAELPPLELRIHLAEVFFHCCHGQSYNLFHRPTFFESLNNNTVPLVVVYAVCAVSARFSSRMHDRFSPPYMAGEQYAREARRLALDNFDRPDLSLVAALLLLSLHDSGTCETGKSWMYGGMALRMAAALQLNCEQGSNPLDLDNIDSGPRISFLERELRRRTFWSCFLMDRYASSHEHLQFLDENDIGIQLPVHELLFTKQIAGVTQTLDGRILEGVPSIVIPADTTENMGVAAYTVKIIALWGRAVKYLKQDGKRRDPYPYWHRNSDFSHISEALYAWADGLPQRLKYSAVGLENHLSIQQGAQYAFLHLAYHHTLMWLFRSIGETENNQLSKISSSVSLAGNTVSFSPVSHTPINVTNGESQNNSNNDPSANGAARRLHKAAREICLRCANAISMIVDDCRKHNVILTSPFIASGVYTAFCVQAEAAFGSNVLAASTARHNLEIDLRLMLEMKNYWGSISALCDKMSEIWADWVQRTSSGIQEEDTIPNEMIDEERMLDLEKHFMYITESPIVPNQAAQKSYSPDLMSYFGFAKNSDLQQWNGLWPSDDLRNYQESTIDSLVAYATGNPGWNISFAG Q1MTN7 RPM1_SCHPO CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.13.1; TRANSIT 1..54; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC1322.01; CHAIN 55..957; /note="Exoribonuclease II, mitochondrial"; /id="PRO_0000353825" MNYRQLFLLQNVNLESNYLLKRVCLSLKLSPCKLTRKFHHACPSSSKVLKYFRITGCLINFGKQPANDHHLWGHCGARLKHTQSDLIDRFKNANLKSVNEENLKKFFSELENHGNIRQWLKDKFEKDKRAAVCPTTTKSEEEKLENDFEYSFDLEDFSSENFRQYDRGDLLVFYRGSEGIELAACTGTNVWNYSNVLTSINENGTIKEFRTSRVLLRCPNVFKKLKEVQQPLSDVSVPSDVLPFTIKLLKKISQRAQDLSRSHRNEFLRILTEFNIPNKLDNSASFSDLLKFVYKTSKPSPYAKISLLHFLLTESKHFLISDHIFSEIQKVYFLPSSQNDSFDDVVACLRQKSTPYLSFIKKARHLIQVSRDKYKLPISTEEIKPVVYSQVTWTEFEKKLLRYLVQEMIAKSIQSLPNTHLCQVYKEVGLQTHERGLTSDQFAKFLTDIGVWASWQPPRLFQQEYSIAGLGTNPQLDAVYERECNHFKKFVKNELKDSLESQRVDLRHLKAFAFDSSSTKEIDDAISVEELGMSNSWLHIHVANPTSTVDIRSPLGTFAERNFQTIYHPNKIVYMLPLNITQKYWSLDSSSTAQRALTFSAKISKNGDILDYKVRPSFISSVIKYTPQQLDKALHSNRSIAKDIVSGPVDEETKGVSNDHMKDILRIYELSKQACFSRLQKFAFVIAQPTPTVELLPNNVPYNLGDLNHPVYWSSFPTISLNVSEGYSLAESVISECMILAGRVSSLFFQEHKLPGIFRGQPYPIMDGVRRKAFETLLSNRSSWGLVETKYSLSVMPLFESSHLASTPVSHFSLGLKDGYIQSTSPLRRFTDFFTHHQIQSVLLKTPKNTIPDGILRGKLNLYNQKEKSIKTIGRYINRFWALKYIERLPKVQKNIYHGYLMVSELSTPQVMLEELGVKAHIDILPDEAFRLANTRQAFTIKDVFPESNILLVALAT Q1MTQ5 MUG89_SCHPO SPBC1773.11c; CHAIN 1..396; /note="Phospholipid-transporting ATPase accessory subunit mug89"; /id="PRO_0000278570" DISULFID 81..134; /evidence="ECO:0000250|UniProtKB:P25656"; DISULFID 188..203; /evidence="ECO:0000250|UniProtKB:P25656" MPEALNENVSDTASNGPVAKTRAPPNTSFRQQRIKSWQPLLTPKIVLPLFFVLGIIFGPLGGGLLYASSIVQELVVDYTDCETLASYDEFSAVPSKKYTASFDQSGTIGFDKESTYWKLEKILDKDLDMDVNYCIIRFTVPSVLKAPIFIYYRLTNFFQNHRRYAKSVDEKQLQGVALTADEVKGGNCFPLEVNEDDKPYYPCGLIANSLFNDTFSSLRLLDDNSVYTFSTKNIAWASDKRRFLKTNYSPDDVAPPPNWVLRYPDGYTESNMPDLSTMENLQVWMRTAGLPTFSKLAMRNDNDDIFPGTYEIKIGLFFPVKSFDGTKSLVLTTRSVLGGKNPFLGIAYIVVSAVCVVLGTVFTLRHFIRPRKLADHRYLNWDSEENNLAPHLSDRP Q1MTQ9 NIP7_SCHPO SPCC320.11c; CHAIN 1..180; /note="60S ribosome subunit biogenesis protein nip7"; /id="PRO_0000343163" MRPLTHEETKTFFEKLAQYIGKNITHLIDRPDDPHCFRLQKDRVYYVSERAMKMATSVARQNLMSLGICFGKFTKTNKFRLHITALDYIAQYARYKIWVKSNGEMPFLYGNHVLKAHVGRITDDTPQHQGVVIYSMNDTPLGFGVTARSTLELRRLEPTAIVAFHQADVGEYLRDEDTLF Q1MTR2 RNPS1_SCHPO SPBC13G1.14c; CHAIN 1..243; /note="RNA-binding protein with serine-rich domain 1 homolog"; /id="PRO_0000372694" MLISTFVFLLYEVTALSTAIHVTKSYTHTRTGTSFFMYQKEAFYRGRSSTRQFNNTRSPSGRSASRSSNFSHRSSSRDSFSSNRSYSSSLSRSPEEPLRTILVENLTRNVTKEHIAEIFGIYGLIDHIFMPIYKKSELNKGYCYIEYVYHDQAANAVDKMNNAELDGEELFVSIKRFPFESLHKNHKHYENSYRPSRSQNNSHYNDKSFHRSRYSRARSRSPGSNISEYSDQSPPYHSYRHRP Q1MTR3 VID27_SCHPO MOD_RES 405; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 415; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 478; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1685.14c; CHAIN 1..801; /note="Vacuolar import and degradation protein 27"; /id="PRO_0000339146" MFMLKSLGKYIWGNTNSTEIVQIPYGQLYSVHENYRECMFKDASASIRRTTAEFQYQLVIQRAYEEGEEELEDDGDEAEDEQSFLLDEKLHLRFDVNKDSITIMWDNPDFQDGTLYEFTCENCLQEGVAYTFEMVALQCMYERKYRQSHEKATLADLEQFSNPITRPSKEVDSLENIVTKLDLESEDLMRLKKQEQLDDEIAKKYLLGQQEAEEPLVQQQTSIVNPEKEEVTKTENIKSLEGELMGTISAELHLFDAVEEVFILQDPNVEASVFDLGDWNYWFTISTEEKTWLSQSVDADMNPVFSFEHLSFIWNYFDANSNAFSWLLRFDSQVRMEQFQELLMRALWESLNQQRWLKIDDEQRDYVMETFHEDEELEDSEDEEFARQQLLSRKEEEEEEDEEASDFEDSFADFSDGEADDLDESRWRKEAAKEHNSLLAVGYKNDRSYVVRNNKIGVFKHVDEKGLKFQTALNNLSTPKGKSLRPSKLMLHNQDSSILFQTENAPHSLYHMDIEYGKIVDEWKVHDDVPLVTFTPDNKFAQMTAEQTLIGLSNNSIFRIDPRVEGNKLVAEQFKQYATKNDFSSAATTENGYIAVASNKGDIRLFDRIGVNAKTALPALGEAIIGVDVTASGDFVLATCKTYILLIDTRIKEGRYAGRLGFERNFAKDKKPKPKRLQLSPQHIAMMQRELKGGASFTPAKFNTGIDAKETTIVSSIGPFLISWNLDRVKRGFTDSYKIRRYDANVQAEDFRFGTDRSLIVALPDDVAMVDKSSLRRPTRESICTPVKKLRSKHDIVNAPY Q1MTR5 YG66_SCHPO SPBC15C4.06c; CHAIN 1..556; /note="Uncharacterized RING finger membrane protein C15C4.06c"; /id="PRO_0000352823" MHLCNNQLLDHLDCNAVYRGYVSQENKVKRRKRLFNAIRKLWNERRRYRMPKDESISPTPISYSFRSLRRGHTSGHASEHTSSSRSSHDESDSMSSSSESDSDSVSSESNPKSYSDSSTSSARSSSTSGSISLYDDYYPAYSSNAPNTAISNYVSSGLSYYGNSSIIMNAVEYNQFFPLTITTLIVKNNKNVVSNLPKNVSFYFHSDNTVLLNEYYKSLSKLKNNFRGIIYKTTPYGSCNDTESLQVDTKGSVWFRDVSNMGSSGLIAFAPFDYCAPMHVLQAVQDRAKAILFYNASTASNSLTNFDHFEDAVDMITFETLPMALISYENGIAFEKILNEYSASSLNSVQDGGALVEYFGNIDATARLGVIISKEPKLLGLYIFIGVLLGLIGVIGLFICLHFSGAMNGFYRLLNRHGIPVQERIVNIGPNKPENRVTKEMLDTLPVRMFSGPHLANPNDELVYEKDWKLDKSESFDGQGNVVTTAERGSKYFDQRECTICLCEYSEESPLYRELPCHHIFHPACIDPYLLKNSDLCPLCKQSVTNMLENASEDNV Q1MTS0 YBH9_SCHPO MOD_RES 40; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 327; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 340; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3B8.09; CHAIN 1..597; /note="Uncharacterized protein C3B8.09"; /id="PRO_0000316620" MARKKSRSSSTRKGSSLKVPEIKEKEKINAINTYEDVANSEDEFYNAQDKILFDADNGEQADELELSDEELVALESSSDEEDGNAEENLSENEELSGKKKDAVNEEELYDNKGWGRSAKSYYGGDDYDNEDYSEEDDEFDARMEEQEALRLQRKRLEKVSETDAIDDISQWADNSDLKSIKQDSSAAAIEELVQQISPDLPRTELLKILEAKHPEFQLFLDELNQLKPQLNEIKEKLKTYPSSQLLQAQCTALSTYISFLTFYFALLKDGEEDLKNHPIMVDLVRCKQTWESYCGLDEVLTPTSLEEDGKTIELHEKIASASDIGASEDEEDVDMHESISDNENEGIKDIPVAEDDDITLKFRAAKSKINTNIKNLDDYGEGNRLDDVDAEDKIARKRSLKFYANQIDQKAAKRSRAVLELSGDLDMPYKERRFERQQRLMREAAARGRNQDAGADLDDEDPESMGIPANVDREVEDQDDLDYYESLDKKSKMAKKLRKENHDLERDLIRASRHPELIELGEGDKRGITLDIAKNRGLTPRRPKENRNPRLKKRMRYEKAKKKLASKKAIYKGAPQGGYAGEQTGIKAGLVKSIKLQ Q42598 THRC_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate; Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 117; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250"; MOD_RES 319; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 321; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9E9.06c; CHAIN 1..514; /note="Threonine synthase"; /id="PRO_0000185644" MSSQVSYLSTRGGSSNFSFEEAVLKGLANDGGLFIPSEIPQLPSGWIEAWKDKSFPEIAFEVMSLYIPRSEISADELKKLVDRSYSTFRHPETTPLKSLKNGLNVLELFHGPTFAFKDVALQFLGNLFEFFLTRKNGNKPEDERDHLTVVGATSGDTGSAAIYGLRGKKDVSVFILFPNGRVSPIQEAQMTTVTDPNVHCITVNGVFDDCQDLVKQIFGDVEFNKKHHIGAVNSINWARILSQITYYLYSYLSVYKQGKADDVRFIVPTGNFGDILAGYYAKRMGLPTKQLVIATNENDILNRFFKTGRYEKADSTQVSPSGPISAKETYSPAMDILVSSNFERYLWYLALATEAPNHTPAEASEILSRWMNEFKRDGTVTVRPEVLEAARRDFVSERVSNDETIDAIKKIYESDHYIIDPHTAVGVETGLRCLEKTKDQDITYICLSTAHPAKFDKAVNLALSSYSDYNFNTQVLPIEFDGLLDEERTCIFSGKPNIDILKQIIEVTLSREKA Q50HP3 SPC19_SCHPO SPCC1223.15c; CHAIN 1..152; /note="DASH complex subunit spc19"; /id="PRO_0000142591" MSYLDGLQQCVDSLQISIGTLSSSIDTLESGIHDFPRIKHILKVQRHFNLISEDELSARQAKFEEIVKPILSKAFQRLEDSISSLQRQEDSLKTKYELQEARLDMLKNRPATSAFSVTTESSEQLKAIIAKRQKLVYTLERYTLQLQQKRGH Q5FC18 SGF11_SCHPO SPAC57A10.14; CHAIN 1..117; /note="SAGA-associated factor 11"; /id="PRO_0000337264" MQPASLAGISCTIFENLLKDYTHELTQTVHKNAKLSLQKCPACNKHCRQYCTKPGYDIYGNSVQTPSNVPYYSCLMCKREIAASRYAAHLEKCKGRSLSNATSYSTLFEDDNADEED Q65ZA6 CTF8_SCHPO SPAC19D5.11c; CHAIN 1..109; /note="Chromosome transmission fidelity protein 8"; /id="PRO_0000239056" MSEIRLIRAINDELYLVEVQATLERKADSLHIGDLKIIKEKNSEKKKATLTVGNQYMEGVVESLKKPLAVLQKTNADPVDVYSSPSHELKCCSIIRERIRFSSRPLPTK Q69Z14 VA0E_SCHPO SPBC1685.16; CHAIN 1..67; /note="V-type proton ATPase subunit e"; /id="PRO_0000071736" MGGLVVLLVGLLTALMSVVSYYVSPKGNNTSTWQMSLILTFSCCYLLWAITYLAQLHPLEAPSRVLE Q6LA53 AAR2_SCHPO MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H5.04; CHAIN 1..346; /note="A1 cistron-splicing factor aar2"; /id="PRO_0000339113" MSIEFVGWLNTYYVGIDQSSYEASKLPGIRNVKGGIHLFTWSPTYPAGLISGVFAMVHEDMKYSIDFDSKSETASLQKLDVLYDENFYPFESTKDWDLLTKFITVQDLQRIFATEGEFFYLDTSTYVNADLVSQDPEFSKPSRDDKLLNFAEFNLRRSWSPSATGPERSKQAIDKSFLFQRLVQSVWNDNPISALAELSISFLSYSILSHYGALEHWKNMLSLLLQSYELAETEPEFYASFLELFKLQLSSLSESDLETSAIFEKGVLLSCLDSLSERKVDGSFGSLVNEAIENLLKTISELLNSHEEQAGLMQKGDLYSAADYEAEVHETGDYVIDVSTEEDPIH Q6LA54 YF48_SCHPO MOD_RES 722; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H5.08c; CHAIN 1..933; /note="Uncharacterized WD repeat-containing protein C3H5.08c"; /id="PRO_0000316557" MNGNLPHIQIQSPKNSLDHLNNGRQATHNFEHGKPGDREEANGHADAHSSSGRSRYLSSDTNLLRDGSSSLDPLSKHIMKRTRSEKTLSFLNPSRASSNTHLSREGTNRSSNVTRTVSGRKSNHGSSLTDTGESDQLSLKSFGAIRQPSQHRSSLFSRMLGSTSHIFGIREDMDNESSEEERDGIPRVEGNAADPFSWIPDGKNVWDSPPKYIRVLSHNKKEKSLDHLFLAQELYCKPTLAATHDRYYEPRATDFPNLAHESSEPSSSRHTADAQSITNASVHLHNSSSPLNRTPSVISDTLAVAITSNSSSNSSNNAIWAMKFSRDGRYLAVGGQDRILRIWAVLDSEHARSVASETCSSDPNNPKLNLKAPVFSEAPIREYAGHTADILDLSWSRNNFLLSSSMDKTARLWHPVRKDCLCCFEHSDFVTSIAFHPKDDRFFLSGSLDCKLRLWSIKEKAVSFWNELPELITAVAFSPDGGLAIAGTFVGLCLFYDTRGLRFRTQMSIRSSRGKNAKGSKVTGIQTRTQMIDNIAGDTEMLVTTNDSRIRIYNLRDKSLELKFKGHANAQSQNRAYFDDDGNYVICGSEDHQVFIWDLPPQHMHKTKKKKHEHFKASVRPITAAVFAPTKTKQLLTLSGDPVYLAAISARRSSVISNASIETGPSLRNLKSLSHSYLPIEIMKGHIIVCGDLDGRIRVFRQDSVFAARKLIEKKNIERKNSETLSNSSFFPQALKAHMNSISSPKRHFSLRHKKNASQITNNENNGNDDIKKGDEPEEEHVGLRKNSTQEKNANLDPNEALKRADMMMLQEGASSMVYYSLTNLDNPGATVNEAAKTAATIEQNEHEIQTSVDPISNVKAILPNADDVSSKNSSTEDQLECLRCGNSLFNVFSRSFVFEGAKFSIVCSHCNRKLLKSGSDDGSETHEMSTLP Q6LA55 YF49_SCHPO SPAC3H5.09c; CHAIN 1..2699; /note="UPF0648 protein C3H5.09c"; /id="PRO_0000350759" CARBOHYD 21; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 288; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 293; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 334; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 345; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 433; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 507; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 551; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 655; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 760; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 993; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1000; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1003; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1006; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1009; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1026; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1039; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1046; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1236; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1255; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1344; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1527; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1595; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1791; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1916; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2032; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2048; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2256; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2285; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2388; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2407; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2417; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2508; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 2622; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNPLFPFSLLNPSTMWSSSQNTSFVWVVIATGFLFHLVLFVLSYVLGWPFTNFGFFSVYGLRHTFRNGDSVFISYVALRLHRPSTSKPYLLRIVTKGLIYTPSLSSANDAQSAGKNENQRSRLVFKAKREEEKTEEKFCHAVYMSNLLRNVEQKWIQFLHKSWMKWLHISIQESQLTFPSVGTFELGSLSMEMRPETNNVVGYENPSDPELVSSCVICSIRLANLVYIDRRQSSQQITDYLDLSLQTYYSLDKSNVPDTILRLRSSIKVGVLYIDLDTPLFEHLLNSNSSGGNHSSSSSSSGKVHVMKDNVEAALLKLQEAQIQIGTLKLWKRNVTGCGATYILNGSDFGLNLILLNKKNPSHRMFFPVEACVHQILASALSFNVESITPGHSPHVLLNIPLVTITCLTSALAEYARDASDLHQLQNSILRVNSTLTSPSLDLRLELLHDVLSCFPKKHDSTSRKKPKFPYQYFPYMKFSVSLYEPALRFLIASKSDSDFPGMLVANLSSMFLDIKYSPSSEHIFEIESSLRLSSNKVFYHNPKNKKWLINTSDLITFSLGYICNNDHGSLNMFFRDFQIRIEEEEVINSLKKFIILTKIKSEQVGPRKPRTKLVEPLLFRIPKWLKHIQLEVHSLLLVITAIRPEISPEPRGINCSIDKIHSLYLNDKKSRSQGMRKFDLNLELLMIKSIIFKNGKSLNSHLFLQIPNINFIVSTILRDNTAISRFTTEINFLRCFASLLHNCCIFYAYRACSSLFGENKSHKRIEKTNTSPQEPGVVPEGWNFDFRLKNARVSIFLDDDVSLLLDCGGFTTLKKTEKKYAEMHAKFIQIHTKNSDVPTLWDRFLALGNVRYQLKDLSDLEKLHQVTCSYISIRIPHKFIPFILIESAINTVKAAIRVSAEPLTIDQQHDLAEEIKQPRVVPHIQIKSTKFKFEVDDDPFECRLGMNYRIGLTEQQMRIDRWNIFEERANLLRKAKDPSPKSASESSSFYQNGSDIDDNDSNSSNTSNHTTENANAQQRKLEDLNRSFEDFLGSRPTNNSSFLKNVSVDEDTAREKLMEYDSLSWISNIKRIREFRYHRLRIRRMTAWPESDALDKHILFKENIIPIPIRPPLVDISLLNFDFTLDKPSFPLEELPKFLNTVGRGQPLDYGYSIYFPMYIDWKMDEAKFLIRDYPLPLVYIPKLGRGQDKRISSWHLKSNMVITEQQATLAAIRDVSVKVIPADLTKEGIPYVVNVTRTVSPIKTFSKTEIDVNSSLPTFLLWCNSYQPALSDMTRIMDTFTKMPIDPSEKLGFWDKIRLVAHSQIRLRWLEDGDVFLSLKGSRDPYVILGEGAGFQFCWSGNVSWDIGCDENPANFMIVDSDKFYLTIPDFPRQINGILEGKPLPTKSTKRSYTTFGVLKDLRCRKVIAKLVGKVRWRAGFVPERHCDEDCTVCNRKKACRLWNFKPHWQVITRIPQYCHDTHYGVYDAYRDFRSHYIHCSLALESPRYLDDANAFENVNSYNTIHLTPLVFSHFSSWWNLFSNNMSYPLRSGNLFPTLDSSPNKKFGRHLATFKYALELTPLFISHMYNYKTNKNWQDRTASATGLKARVDNFTIDLHQRSEKHEVKNKANLGRKHQEATSMKVHLAEIDFKTIDLRAISASFDEGALDNSDSIPANVLDEEEKECFSFKNVDGPANWVDIDDYHEADWLLPQQNEKCSIYPLAFSPRFTYYRHTKCHRRNEKNEKEIIPDTCRFGDEFTHRCLMPSRENPKAVQYELLQKRRKELEEFMSSEQERIGFLKSQLESNNDSEEVRQEYEELTKRIVTLSDHYRLLEYLLKDESSCSQASQCSENGQVDLSYASLSESVHAFNNRFVAHNVQVKWNNFIRNAVMSYVHEVERVRGFAYYMSQKAIVFLRDLEKRTESANDDFFGNYTEDDEDRENARHLLKFLLEDSKKRFWVKTSDADREHGSEEGNTNSISNNEYDIIQSYVFRFISPQIQLQCSSNPEKAVIISIQSLQIKILSVVDPIFPDNDINYLIERRFLCKVNESQFFISKKSDFEVVNASSLVLNEYGCEHNTVWPPWVPFETTFDFVLTPAAFSRFLHRVSFSVIYTKHNDLRLQETVHSTRAFFEDLDTHADTLTFDFPRVVFSTDSSQYYDIFTIITDLLLYKEPAQKQRNQRLEEIMLAADFSDLTGTSEVVRALQARVHRLLDLKLQHQLYDVTFGIYAHIAQQLFLQNELHRCGEELYYLIESIAAVQNRGIHQNKVRSNLSWFLMAKEVVWHLLEDNKKPFLDVRLQNATFRRIENSDASNFNTLEIEFMKGSNLAPGCQFENIICPYFNHEFSNEQLLQQKFIRIHWEVLEAVAGIQVIQHFEINLFPLSLQIEQELATKLFAYAFPNRNESDGFPHIYSRNHDKRKENGSQGEADNSNYSGSLMRRRTNDQEEDALATPSSSRRDSRSKRASLIDFTIDKCLDVDDEGRMELQSMLDRAGSNMLITYFKIPSVVLRLSYRGTGGLGLENITGFVFTVPTMEYRNEVCSYLDLAMKLKHDLIRTVVSHTGKLLVEKVKGNYHLKEHEREVSSELLNLQQLSAEHNRHADLESMVMARDDYINVQQPLAEENQEEGSPASAISRNHSTRSSLNSPRQFWAYHGSRSKKIADIVKRHIPPTINGKRSKNKGNEGSNARVDFYNDERYDPVKRELILGASNRRK Q76PC4 YQ72_SCHPO MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 286; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1442.02; CHAIN 1..562; /note="UPF0649 protein C1442.02"; /id="PRO_0000350760" MDWKEAIPGAAKVAIETKDYITYSTLLELILEEARIKDIDEQRELIKCLHEELKQEKNDHITREISWDIIGMVLPYVGKVQNEADEFVDFLAKNGNPREVFLKCCELLINGGFESPQQFISLNSAILSALHRISTKRPVLFVNNFLISLFSGLANILQIDSDELYCVWKISISSIQDAMHRFPVSECYLACLKACSILAQLFLSKETLMLSFRSLLQTKDQYAEFREELSGATTNCDKLDTLSKSIINIFDYLLSHLPESWSIITEHMAQELTKATYVSQSSSISSEDEEIAKNADVPAEVDNNSTKADDKRDEIEFDTKGCLALLTIKSFYQSGNFFLDFLKEKFPSTILETLQQLVSWEIQLDSVGFKDIAVYQGYLLDLPHFQVPDSELEHLSSLLHGYHFMASSTELPWLRVTCNAIVTKCLDSQLPSVRLSYILDTLEECPLLNIKTAILNYYQKQCSLVKDSNEEGLKNFVSPNTLLDVFKVFDAMEDVELDSQSLSYIHQTLVFLYSLEIQNLLSQNQFPTVYFTKISDQINNYEGELPTDGLKYYIELLNSRNK Q76PC7 IF3M_SCHPO TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC18E5.13; CHAIN 40..233; /note="Probable translation initiation factor, mitochondrial"; /id="PRO_0000353835" MNSYLQFPHRKLFIQFSYSLTSVFRKCQSRTFMNSQFASAKLSNSIKKYFDGRIDESIKYQEIFIRGLENKGKLSKTSLVEALARVRAKPETVLYKVADPNENNKYPICSIISYTELSKLRENQSSRLREAEKSKHKNKTRTRYVLFSWRTDVNDIERKLKSVKDFLQDGNIVEIHVQNKKRSQPVSQEVRDSILSKIQLEIEGLGKDMKPPIVNSHSATFLLQPLVSKSSEL Q76PD3 DBP6_SCHPO BINDING 180..187; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPCC285.03; CHAIN 1..604; /note="ATP-dependent RNA helicase dbp6"; /id="PRO_0000232296" MSVEVDKSSHSKPKIEKKSKRNKRKWLNDENKTHVTASEAAIERLKKSASFSQAAQQALKQSRKEDNERDIEMQDVDAEAQPHDLLPIPQPSVEDFVDSKPHVKNITSVLPKWLAEPITVDPNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRHGPMYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEISHPKCLQNKSNILDLDQNISPTFLPDIDTLLPYRLPSPLQKLVFSATLTRDPSKIASLKLHNPRLVLVQNKDMEVDDGGEIEDDAIVFSVPPTLQEYHVSVSSEKPILLYHLIHSKNLTNILCFVKSNEAAARLHRLLELIHESLNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLVQSHEGHHFSKLVKQLRRTLPIKRIKIEFSHISEEFVVAYDKALEALRVEVFNSRYPQQKSFLT Q7LKZ6 YJMD_SCHPO ACT_SITE 400; /evidence="ECO:0000250" SPCC1020.13c; CHAIN 1..669; /note="Probable phospholipase C1020.13c"; /id="PRO_0000316025" MQESSQEEPVHYVQWFYLSNYDLYDETSSMELTGAQSWRRFLNYDNNALEAKYNEIITEEVSQEPNQKNVIVGISGLHVVNLPTLTLKPLYWPSASKNDTLRVVRGLWMYEDTGLPVINELSDMLEEGYQEVKPYAVNWDNVLKEEEEGKDSQDDPSVLSHKRNKSSKELIDAMQWPLKPTSSGKYVFYEDGYRALICQGGLLSYFSKGTQSRRTSIKGMPVVRDFPYFEDDGFNGPKQVTDLFLVVHGIGQKRSETEERFLFTKTCNVFRSLIQIQKNIMKEDPLIRNDYEPQLLPICWRNKLNFNSYIKPVAGDEGRVEDEEFEENRFSIEDIEIDSIPAVRRLLGDVMSDIPYYMSHHKESIIKSVIREANRVYHLWKDCNPYFLENKGRIFIIGHSLGSTVVFDILSLQPTFVKEITIDDDESCFIFDTNGFFCFGGPVGFFLHLNQQSIIPRRGRGSSRYEINKNFINSDVPKSYTYDGYDRYGCLAVDSFYNIYNHLDPVAMRLNPTVDLSFSKGIHPTRILFTRKSSSILRMISHSNTDPVELRSYNQSLQQNKNNEPTAVVPLEPEQTVELETRNFRREERAKWRMQELNENSQLDYVFTSAHGVISNKYLSMLSAHSSYWSSEDLACFLVVETGRNFGIANSIEQFRGKHMPRIFKGDSS Q7LKZ7 BPH1_SCHPO SPBC28E12.06c; CHAIN 1..2609; /note="Beige protein homolog 1"; /id="PRO_0000372305" MDRKANAYSKSVELLSRLEGCPSEKVLLEELRKLRGFIRNDIPSNFFPQLFITDNGFAAIKKAVTKLNFQSLLSLDIFECCLQILGIATSYTILRSWLLSRKHIEAWIELAIRRMFYSFCAIQDDSNISIYAIGTSSKTDSSIQAASPNEDLKSEGAQEIDSQSETVSISSDVDYDEDRKDLKKAKICSAYYLKTRLLLAVLSFAQNDSTFSLLKLVPSLQDNTNASLVELSRVVEAAIQKLSIKPLAFPNVLPQVLLLCPSISIFNLILLHLRALIRSSPENAIKIGYSKTMHFLLTYLFEPPTSFPLSDVSKDLLNEITLHCATFGVSNASTAKVLRTYLKTKSEFLRTWLLKALSHLVAPSFYFNPSTKGYSSIDFTLSSPVMPINGYSVSLWLNIESLMNDDGNYAPTTLFLISDFLKSTLFRLLLDASKKTVVVHIGSSKDTCVVNFSTPITNFFSKIYKDNPSLNPPSWHLITLVHRNEKSSLPNLELYIDGSAVERAACPYPFLSSTLQPLYVSLGPSIGSRNQSTPSTLAPNVAETDALVSENTGAASQKTSKSYKTNDSLKVPPLVPLLIGTTRFFPVPLVSSQIAIISSLGPSYSGCFQGPINDYMTYKASTALTLEIQDSKSNTEDLLHSIQAFSRSPIAFMSCARDYVDIMDLQLSDFCSFSVLETLKKLENQYYSHVYINRAVSSYDKAFSAEQPSFGVSSGSVTPIIMQSISDAIYNIGGSSILLELVGTAETEAELNFGLQVFFSSIEDNWRFSENVEQTHSFEILAQILHSKSHLLVSEETLKIIALMSGVHHTRFKHPLVMNPLLFRYLILDFDLWSKAPNSNLFVQQLGYIVSLIENNDYAGFNVKRLMKMQILKKLLTAMRNCLFHKDLLPILRLLFKVLMTSAFVSENIRSVATYIIYASQATGKSKPIRRSSVSIAVDRSDSNYISIKESGYAICEEFIDLLIKSNGEPSFLRRFSSMITPAWLLFLLRQQDIHYFICGIRLLNQSICSLGSSFLSKFSQKFHGFLILHDNLKDHIHLEELWLNLLFLSLGLGIRSVQFRTDLTYKQKLDFVLKNELDNILPLSEVFPSLFHAIQATLEKVSNVNGKLNSENVAALRYADDTMSFLVTLQTTYSFELTLNYDFSELLTKVVFPFLSPVDTITAEQEMRDLLHNIRQPLPRSSSSKTFGEGIKKSVRKFSMSGSFKRVVTPLGTQLRKDILNDSITDMENTSSFTASFPQSDQALQYFDNFTVQYAEAKDVIKGLLFSILTCIYNRITSGQGFSYSRLLVYLPPSQIEKKSTFFSGILRSTMSKLIEAVKNDKLLLAEPSILANISYIFTKFIRMHLLGYLKGSWLEIVDDLGSLLEEIISRPDFLAKLPKNGRNAAMNMYSCFLDLFLLEVSDLKQTECNAQSDKIIKSITYWQSLLFNSKTYQKDLFSLLWYAVYIMVETTTGVVRLQAVDAWRLLFLHSPGYLSDIAKTCNNDPRFAYEICKTLDNDSDKFVRWLDDNAAEVNQFMLSCFFCRWEDFLKQQHKLADEEASLLQFSRLEHLRKQLAQNTFNENILNESSASYHVWISSLFALECNRFKKMSQDQSDQENFVAAALLSQKNELSHENSILGSKTTSWELDSTEGSERMRKRLMPCLLQSSELDSKLEARSSGARRNRSFDTSVEAPVSLTNEEKQAATLILPSQEETLHDAARSDSNNSMEDEEDDVDEEDKEDKNRTVMRSIESGDSIQDVYNVSRIFGLEATEGILLLGKQYLYLMDNFFLRSDNEIVDVNDNSIIDERDPYLQLLHLQSLSSSGKVRRHISKENNWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLTILSNTKNRDSLYQKLVARAPGADVLSTSHFATSMSRDLGKANGKSNFLSSKLANALSFSTTHPATKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLLLGLNDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSKENMADVRELIPEFFYLSEMFINGNGFDFGSRQKESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFHHLSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQRGPDFTDTPLGPYLFGRFEDSIHLLFQSCSPIIRICKKVAHIQYDPSKDEVGAFAADYTPLGPNTFLAWGRVDNTVQLISDQLDKQPVMFEELHSEKITHVVACDERTFLTASLDLTLRLWTLSTNKPIKASLKRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIQTIAVNARNAEIAFSTGFYCCVVNVNGKILVKDKLSRIYNENSDENILCSCFYTGANSEWLHKNLFITGHPDGIIRIWEKRLQSNAKLEAEKNNADRPKWRFHLLRQLQHTKGLGRNRVATRQNIITITPNGQARGIFAGDDKGQVFSWMLPDTTSNVHLEKDNTSELCSLCDSRFSLMEWRSQCRACGNSNVCSDCVSMLKDTNIKTCYECYRQMPLCYKN Q7LL14 RU2B_SCHPO SPBC8D2.09c; CHAIN 1..111; /note="Probable U2 small nuclear ribonucleoprotein B''"; /id="PRO_0000081894" MNQNTLYVNNLNDKINKNDLRTALYMLFSTYGTVVDIVALKTPKMRGQAHVVFFDPSAAAIAMKALKNFIFFGKEMKIQYAHSKSKIIERIVAENDSRGPLKRLRDEADLE Q7LL15 SUS1_SCHPO SPBC6B1.12c; CHAIN 1..108; /note="Transcription and mRNA export factor sus1"; /id="PRO_0000350748" MYDLIFSTKMTTEKIVEQLYETGDYERLANELEYKLESCGWTTQLRDYTRGIVNSDSKIDFQKLYESALQSATESIPDSVKMDLLKDIKTCVLKLANPPESANGGNKM Q7Z991 YE31_SCHPO BINDING 37..44; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPAC20G4.01; CHAIN 1..280; /note="ABC transporter domain-containing protein C20G4.01"; /id="PRO_0000310287" MEVTVSNLSYTFSPKQPLSLDHVTLDLPKGSRTLLVGANGAGKSTLLKLLSGKSLAKAGHISVGGKDPFRESSSAFVYLGTEWVNNPVIHRDMSVARLIASVGGDKFAERRDFLISILDIDLRWRMHAVSDGERRRVQLCMGLLRPFEVLLLDEVTVDLDVLARADLLNFLQEETEVRNATIVYATHIFDGLAEWPTHLVHLSLGRIVDYGPISKFGALMTRSSTGNSALLETCLEWLKEDKKNRGTREEEKRSTWDDVQESLKVGTDVFTDYFKISRAK Q7Z996 POP8_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; SPBC1709.20; CHAIN 1..108; /note="Probable ribonucleases P protein subunit pop8"; /id="PRO_0000058520" MVLHQRLKSEWSYIILEVVGGTTPIDEIDDISLRHLITLALNQSFGIFGSAIPIDFLHRQSKFLYLRCHKEDKKKVLVALGSYVREPEQIRLMVLHASDFPCQAVPFS Q7Z9H9 FIG4_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:32955, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57923, ChEBI:CHEBI:58088; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC1093.03; CHAIN 1..832; /note="Polyphosphoinositide phosphatase"; /id="PRO_0000317231" MPATNSDEPLVKFELYQLKKCYYIVSENATATIFRILKITQSEDELSISIEEAAKILFRQKLQLYLEKLENESADGKLILVTKAYAILGLFRFTAGYYLYLCTERKVVAVIGGHNVYHVDKTQFIELNPSRRHNTSVERKCMSSIEKVDLARTFYFSYSYDLSQTIQYGFTHPIPQHQVRDMFVWNWNMLRPILDSVGIDSPWCIPLIHGFVDQAKLSVYGKPIIVTLIARRSRHFAGARFLRRGIRDDGYVANEVETEQIVFDGSASSFPISSTTPGIPCYTSYVQHRGSIPLRWSQEFSNITPKPPIGIDFHDPFYASTALHFDRLFGHYGIPCIVLNLVKSSEKVKRESLLLDEFESAIQYLNQFLKDSQKIQYIAWDMSAASKKKVPVTKTLEQMASDIVKKTGFFCTADRFFPGTFQTGVVRTNCVDCLDRTNAAQFVIGKCVLAAQLRALGVLDSPQLDYESDAVRLLAEMYHGHGDAIALQYGGSLLVNTLDTYRKNNQWSSTSRDLIESVKRFYSNSFVDFQRQEAISLFLGNFTVHGKIVVFGEKRLQALTEKFKNGQLVRRDYRYWWTPVYVNQELRCKNAYCDSIQRKGIKFPANYFDNVYTPNSISSFSEVLLPNLISTLNFAPLSLIPLLRKSFLPLSYNGFGIEAPSLNPFIPRRNQPRDMFKTSAEEENEDEDEDDDKFRRVSLYKWLFNNEERPVHKFIRKRLHQIPVSNKVQPRDQKQPDFKIPNTDINVYKIHFQYNNISGLADNYTLLSKHDRAMYNNYADYSPDKIKEIKEKELNTYNDYFNSAISENPTLKSDRSEKVAFYSAWITDYKST Q7Z9I1 PFL4_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPCC188.09c; CHAIN 22..609; /note="Putative cell agglutination protein pfl4"; /id="PRO_0000353812" CARBOHYD 75; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MLFLRFFIFTFFTSIFTVVVSEPPVSAKFAKRVLSATSSSSSTCPEFITIFSEGPSEYITTIYPSSKSSGRGTTNHSTIYTTINSGTVASTYTVTLADGDVVVKDIEPTAGTVTTTITSGSHEFTTTLAEASGTVPGTVEVVEPLAGTVTTTIHSGSVEYNTTLATASGTVPGTVEVVEPAVGTVTTTIYSGSEEFTTTLASASGSISGTVEVIEPTAGTVTTTIYSGDQEYTTILAEASGTVPGTVEVIEPAVGTVTTTTYSGSVEYTTTLVPASGSVSGTVEVVEPAVGTVTTTLQSGSQAFTTTVPASGSVSGTVEVVQPTGGTVTNTVYEGSQTITSTLATASGTVPGTVEVILPGPSTIYSGTVATTITYDVSSTPASTVVVIPTAVCNGERGLQYAVYNYDISSSKNQFCATSGVTDVSSFTQPAYFGSSDLDQSSPLFTGVLSSSDSVPQWTSSYNLPGYPPDATAMGSTSSACKVIVYQFFFRVPVTDTFSLDVTNVDDVFYGWFGDKAISGWSNTNYDTYAYWHATNGQTGIASFSMGSLTADTYVPVRFVVANGAGKGGFDFSFVDSEGNSYNPTSYAYTATCTESFLPFGQGNGGVDN Q7Z9I2 YCP9_SCHPO ACT_SITE 158; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 162; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 17; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 36; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 62; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 89; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 123; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 158; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 162; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 191; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 193; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPCC663.09c; CHAIN 1..253; /note="Uncharacterized oxidoreductase C663.09c"; /id="PRO_0000374029" MATTNKVYFIAGGNRGIGLSLVKELSSREGTTVFASARKPEAATELQEWSKSHPNVKTVELDVTSQQSANEAAQSVAKAVDGIDVLWLNSGICQSYYTVMEAPEEVWNAHYQTNVLGPIHVFKAFYPLLTKKKTRQVIFTSSECGSMGDFRATGFSAYGQSKAAINFTMKELSVELADEHFTFISIHPGVVKTDMNADAIKKFTETSPEMLTYLKKVTIIPEESVSSMLKVVDNLKPENNGSFYRYDGTIIPF Q7Z9I5 WTF7_SCHPO SPCC736.05; CHAIN 1..215; /note="Wtf element wtf7"; /id="PRO_0000193223" MSGSYAPIEDSADELSVHSGNDNEIDLEKGLLPKCNTGNGGTTPCSEPPHYDSDAVVEMDMYENNIYMRTFKLRPFAKSGVTNSSNVVFQMKTYENNRHMQTFRLRPFAKNGVTNGVKLAQSLFLLLPFNFIFFACLFFRKASFTDFSLMGWILFGIWCLTCFLSSFILYAYHESWTKFARERSQEFSLILFGLLFPGIVTMVVFYALYMRSMYG Q874R3 APC2_SCHPO SPBP23A10.04; CHAIN 1..681; /note="Anaphase-promoting complex subunit 2"; /id="PRO_0000237683" MNDTDLSTFTGRSLLIDQLSSVTQGTPVLDFIDKLRIHFYTTIRQNLLKIDLKNICSLHDLTDQLSDFWLVYEQSVLESPILSPELDRILTCFRCLCRRYLPISVIESVLTEYLDQVLKVWLESKTNPCLDMEKFFQLCEKFKQLGLSSVLKERFVYVLQLHVGSLLTTRYAMSWEQSVYHEALEWIRTEFGVLVEHVFSLSNPAVLVQLDHLVSQILAHLRSDNILDIVLHYPNSLGAIEDLRLVARQKQQRQYLTETFVKDCTSSILTASSDSSYILLFYVSTIRCFVALDPPGVLLDKAAKPIRSFLNEREDAYKCLVSLLFVDGEKGLRSELSQIPTENIDSTTDRFDNYHWMPDPIDAAPDFKKPTDRDVVGSLISIFKSKEPLVKELQLLLADRLLQLTDYHYEVEAKNIEFLKYRFGETVLQMCSVMLNDIENSRFIDQSIHMENYVSKGLHVTILSRLFWPTLSVRYFHLPGPLKKELDAYAEEYRERKRKRELVFLPNLGSVELEIELEDRTLTLTVTPEQAAFISLFEETSTLHIEKAAELLDQPKEIVERHLKFWLHHRVLTDIGDDRYRVRETEAETATETVLDEIQGVSAVQSEAESSAAEMRVYWSFVVGMLTNLGALELERIHNMLTMFIPPPNGYTRTQSELREFLALMIKEEKLEFTGGAYKLK Q874R4 PFL3_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPBC947.04; CHAIN 25..973; /note="Putative cell agglutination protein pfl3"; /id="PRO_0000353811" CARBOHYD 75; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 96; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 147; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 171; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 184; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 218; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 253; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 352; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 393; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 848; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MSLFPQILLRLLFLAFTLKSTSNAEKHDKVDYKDFVRRDDGDTCLRYTTIYSQGEYETTITIPPNSYSNGVSLSNGTLLSTSSPLISTSGQFTSNNVSTTSSQRHNTKTITFFSGTSDYTSVYYDTTGTDDVVYEYHPSSERHKSTNDTWSTNLPTNPTTTAIYSTSGSSNITTPYSNRITNSNTSVNDITSKYLSVGTITLTTISGSDLYTSTFPANGTTSGTVEVVIPTAGTVTETAVSGSELYTSTFPANGTTSGTVEVVIPTAGTRTVTKISGSKFFTTTTDASGTVSGTVEVVLPTAGTNTMTVVSGSRFFTSVVSASGTVSGEQVIVYPTAGMVTETIVSGSEIFNTTYPASGTRTGTVEVVIPTAGTVTETEISGSELYTSTFPANGTTSGTVEVVIPTAGTRTVTKISGSKFFTTTTDASGTVSGTVEVVLPTAGTNTMTVVSGSRFFTSVVSASGTVSGEHIIVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTAYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPVQGTVSGTVMIVEPTAGYVTVTTSLGSSSYATTVATASGTSTGTVLQVVPSLFPGCNSKCTSSNAFRILVENDSISPSYLTYRESDGFGIASSNPSPAGSEGIFYYDSTLKRVVTCCDERPYYRTMEGDLAKTYFFIEDEGDGTYKFKLTYGAFSEYLDVKILADSTFFFKAMDSSSSTILNQKVRASNVYFKAVPL Q8NIL3 AES1_SCHPO ACT_SITE 47; /evidence="ECO:0000250" SPBPB21E7.07; CHAIN 1..296; /note="Antisense-enhancing sequence 1"; /id="PRO_0000162386" MTEHSFKQIDVFSNKGFRGNPVAVFFDADNLSQKEMQQIAKWTNLSETTFVQKPTIDKADYRLRIFTPECELSFAGHPTIGSCFAVVESGYCTPKNCKIIQECLAGLVELTIDGEKDEDTWISFKLPYYKILQTSETAISEVENALGIPLNYSSQVSPPVLIDDGPKWLVIQLPNATDVLNLVPKFQSLSQVCKNNDWIGVTVFGELGKDSFESRSFAPLIHVNEDPACGSGAGAVGVYIGSSQKTPTSLSFTISQGTKLSRQAISKVSVDVSSNKSIAVFVGGQAKTCISGKSFI Q8NKC0 ASPG3_SCHPO ACT_SITE 49; /note="O-isoaspartyl threonine intermediate"; /evidence="ECO:0000250" BINDING 96; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 129..130; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; SIGNAL 1..16; /evidence="ECO:0000255" SPBPB21E7.09; CHAIN 17..360; /note="Probable L-asparaginase 3"; /id="PRO_0000002365" CARBOHYD 27; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 35; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 40; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 82; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 106; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 144; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 179; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 246; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 302; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 351; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MWSSIISFLFFSVALCQPLLFQKRSSNVSDFISFNASLPNVTIFAMGGTIAGYASSSTETVDYAAGSVGIATLVDAVPAIKNFSNIRGVQVTNVGSEELTPANVLNLTQLILAEVAKPDVHGIVVTHGTDSLEETAIFLDMTVNTTKPIVVVGAMRPSTAISADGPMNLLNAVVVAASNRSIGRGTMILLNDRIGSAFYTTKTNGNMLDTFKSYEAGFLGMILDQRPHFFYSPATPTGKVHFDVSNTTELPAVEILYGYQGLNPNLAKAAVDLGAKGLVLAGMGAASWTDPGNEVIDGLISNQSIPVVYSHRTMDGFSDYYYNGIPAYFQNPQKARYMLMLSINAGYSIQNITDIFSLEY Q8NKC2 ENO12_SCHPO ACT_SITE 212; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 346; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 160; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 169; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 247; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 296; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 296; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 321; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 321; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 373..376; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 397; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000250|UniProtKB:P00924}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Mg(2+) is required for catalysis and for stabilizing the dimer. {ECO:0000250}; SPBPB21E7.01c; CHAIN 1..440; /note="Enolase 1-2"; /id="PRO_0000134059" MTTIQKIYSRSIYDSRGNPTVEVELTTELGTFRSMVPSGASTGEWEAKELRDNDKNKWGGKGVTIAVHNVNNIIGPALVKSDIKITDQRGIDEFMIKLDGTNDKSKLGANSIVGVSMAVARAAAAFLKIPLYEYIGKLAGSKTTECIPVPSFNVLNGGRHAGGDLAFQEFMIMPIKAPTFSEGLRWGSEVYHTLKALAKKKYGASAGNVGDEGGIAPDLTTAEEALDLVNEAIKEAGYDGKVKIGFDVAASELYNGKLYDLDFKSEHPKPENKLDYKKLYEKYSALIEKYPIVFIEDPFSEEDWGAFSYMSSKTKVEVIADDLTVTNVKRLSKAIELKCANALLVKINQIGSLSETIDAANMAKKAGWGLMVSHRSGETDDSFIAHLAVGLEAGQMKSGAPCRSERLAKYNELLRIEDNLGDSAIYAGTRAADYIKSNTL Q8TFF8 ASPG4_SCHPO ACT_SITE 46; /note="O-isoaspartyl threonine intermediate"; /evidence="ECO:0000250" BINDING 93; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 126..127; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; SIGNAL 1..22; /evidence="ECO:0000255" SPBPB8B6.05c; CHAIN 23..356; /note="Probable L-asparaginase 4"; /id="PRO_0000002366" CARBOHYD 37; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 52; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 176; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MWGFIVTCGIFLVLLCQLRLLSKRKSKSTPYNALLPNVTVFAMGGTIAGCANSSLEIVNYIPGSVGIEKLIEAVPAIKAIANINGVQVTNMGSENLTPADVLKLAKLILAEVAKPNVHGIVITHGTDSLEETAMFLDLTISTAKPIVVVGAMRPSTAIGADGPMNLLNAVAVASSNQSMGRGTLVLLNDRIGSAFYTTKTNGNTLDTFKSYEAGSLGIVLNQKPFYFFSPAVPTGKVFFDIYNIKQLPRVDILYGYQGLNPKLAESAVHLGAKGLVLAAMGATSWTDDGNEVISSLIREHNIPVVYSHRTAEGYSSNSCLGIPSYFLNPQKARYMLMLAISSGYSIRDIEGLFSIK Q8TFG0 DUR32_SCHPO SPBPB8B6.02c; CHAIN 1..673; /note="Probable urea active transporter 2"; /id="PRO_0000314767" MEPILNQGYGYGFALGLGAAFALLMAIITKVLTACMGQTQNSERFSTASRSVKSGLISSSTVSAWTWPATLLSSGAWSYTYGIMGGFMYGVGGTIQITLFLFLAIQIKKKAPAAHTVSECFFIRFGKLGHCVYLFYCISTNVLVSSLLLLGGSQGFSSTTGMNTVAACFLLPLGVMVYTTLGGLKATFISDWIHTVMIYIILIVTCYTVYCSSSLIGSPAKMYDMLKEVQEVYPATGGQSYLSFKNSEMMYLTWSVMIGGLSSVFGDPGYSQRAIASDAKSVFQGYLMGGLCWWIIPMALGSSAGLACRALLLNPASVTYPNVLSSVEISSGLPVIYGMASIFGKSGAAAGLVMLFMSITSATSAELIAFSSVTTYDIFRAYINPAANGKQLVRTAHLSVIGFSLFIGALSVGFNYAGVTAGWLLTFLGIILTPEVSAVTLCLFWNKMTRFSLVVGAPFGTITGVVCWLASTYSFCDGIVNKDTVMTSKACFVGNIVSMASSPLYIVLLSYIWPDKETFDLNQFRNITVGDDIDTTELNAIVSQLKDERILKLQTYWSIGINLFILIGCYVIIPTALLGSNHDLSKSSFSGLIIVCLIWILVAAIYIILFPLWQGRKSLANVISHIIRLKAPENILLDGLTPKQSSEDVGDATSFHMDKLDKEKEKSSELKTA Q8TFG7 TRM5_SCHPO BINDING 231; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03152"; BINDING 269..270; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03152"; BINDING 297..298; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03152"; BINDING 354; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03152" CATALYTIC ACTIVITY: Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228; Evidence={ECO:0000255|HAMAP-Rule:MF_03152}; SPAPB18E9.01; CHAIN 1..450; /note="tRNA (guanine(37)-N1)-methyltransferase"; /id="PRO_0000316612" MHLQIRTVHNMAELLHPNKVEMKPFLKNLDKNLFKKTYNLVAAKVSPKKVGLLNKVCKKDLLDWPRVKHVYQQNNEKLVLLNRDASLDGTRGLSDATVSFIKENNIELVPFQLTLDYDYWRADDILDAILPPGEKEDHPSGFTAVGHIAHMNLREEWLPYKYIIGKVILDKNPSIETVVNKTDTIDTKFRTFQMEVLAGKDDFIVTQSESNCKFRFDFSKVYWNSRLSTEHDRLIQQFQPGDAVCDVMAGVGPFACPAGKKNVIVFANDLNPYSYESLVENIFLNKVANFVKAFNQDGREFIRSSVQKLLGFSKDEKAITVFPPRKRARKLEENKDPVRQDIPIPPVFSHYVMNLPGSAIEFLDAFKGCYYGLEYLFKDRSLPKVHVHCFCRFPDPEEDLINRIYASLGYRFSPEEVDFYYVRKVAPNKDMYCCTFTLPGSIIFAKPVSG Q8TFG9 PFL2_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPAPB15E9.01c; PROPEP 1012..1036; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000415888" CHAIN 24..1011; /note="Putative GPI-anchored protein pfl2"; /id="PRO_0000014212" CARBOHYD 66; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 97; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 165; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 201; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 233; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 259; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 277; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 296; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 312; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 331; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 347; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 363; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 379; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 395; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 410; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 429; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 445; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 461; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 477; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 493; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 509; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 524; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 543; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 559; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 573; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 611; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 626; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 642; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 657; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 673; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 688; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 704; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 719; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 735; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 918; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 924; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 930; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 933; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 939; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 947; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 977; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" LIPID 1011; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MKFFTASTLFLLAAQSLNSGVSASLSDPANTPTILADDIVHGYTPATYLSSVPTLLKRATTSYNYNTSSASSSSLTSSSAASSSLTSSSSLASSSTNSTTSASPTSSSLTSSSATSSSLASSSTTSSSLASSSITSSSLASSSITSSSLASSSTTSSSLASSSTNSTTSATPTSSATSSSLSSTAASNSATSSSLASSSLNSTTSATATSSSLSSTAASNSATSSSLASSSLNSTTSATATSSSISSTVSSSTPLTSSNSTTAATSASATSSSAQYNTSSLLPSSTPSSTPLSSANSTTATSASSTPLTSVNSTTTTSASSTPLSSVSSANSTTATSTSSTPLSSVNSTTATSASSTPLTSVNSTTATSASSTPLTSVNSTSATSASSTPLTSANSTTSTSVSSTAPSYNTSSVLPTSSVSSTPLSSANSTTATSASSTPLSSVNSTTATSASSTPLSSVNSTTATSASSTPLTSVNSTTATSASSTPLTSVNSTSATSASSTPLTSANSTTSTSVSSTAPSYNTSSVLPTSSVSSTPLSSANSTTATSASSTPLTSVNSTTATSASSTPFGNSTITSSASGSTGEFTNTNSGNGDVSGSVTTPTSTPLSNSTVAPTSTFTSSGFNTTSGLPTSSASTPLSNSTVAPTSTFTSSGFNTTSGLPTSSASTPSSNSSIVPTSTFTSSGFNTTSGLPTSSASTPLSNSTVAPTSTFTSSGFNTTSGLPTSSVSTPLSNSSAYPSSGSSTFSRLSSTLTSSIIPTETFGSTSGSATGTRPTGSSSQGSVVPTTSTGSSVTSTGTGTTTGVTEVTETSTFETTEIITSTIEPTTASGTGGGNPTAAPTNEPTVTTGTETTEGTATYTEPTTFTSTFSFTTTIIGGTTTIIPVNPGNPSSSVSAPPTTSFTPGPGGSGYPSYSNTTQGMNTTSIWNSSNSTIVSNVTATITGNVTITTGDLTTIDPTTFTSTYLSSGFQTVSNTTATSGSDDDVKTASTSSSTSYTSSSSSSSSTTSAASSKASVSMGLNGLMIAAVILLVA Q8TFH1 RL18B_SCHPO MOD_RES 134; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 136; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB17E12.13; CHAIN 1..187; /note="Large ribosomal subunit protein eL18B"; /id="PRO_0000132783" MGIDIERHHVRKSQRSKPASENVYLKLLVKLYRFLARRTDSRFNKAILKRLFQSKTNRPPISISKIAALTSRKSASLEGKTTVIVGTVTDDERLLTVPKLSVAALRFTKSARARILKAGGEVLTLDQLALRAPTGSNTVLLRGKKHAREAYRHFGFGPHKHKAPYVRSEGRKFERARGRRKSRAFKV Q8TFH3 OST3_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPAPB17E12.11; CHAIN 20..309; /note="Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3"; /id="PRO_0000372619" DISULFID 65..68; /note="Redox-active"; /evidence="ECO:0000250" MNFFKILSFFSLFVITCFAKLDLNSKTDADGVIQITGRLFHRIVNGKQDFTTVALFSADSSTMNCDVCRLIEPEFKALANSYKLKYGLDSGIRFTYADFGKNKNLFQDFSIESVPNFWIFKPKSIQAIHVDLSHGVTASHLAAIVEKHTGKIADIVYKQDQAKRVGAFLSYIIVGAALFFTRKIIVKIFTSRKVWAALTIITVITLSSGYMFTRIRFSPYSQRGEHGENLWLAGSQQFQFGAEVQVVSLLYTALTMSSIFLAIVAPKVEGAKRQTLFVIIWLAFLWIGYSFLVDIFKRKVSMYPFKLLI Q8TFH7 SEN2_SCHPO ACT_SITE 281; /evidence="ECO:0000250"; ACT_SITE 289; /evidence="ECO:0000250"; ACT_SITE 325; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16; SPAPB17E12.07c; CHAIN 1..380; /note="Probable tRNA-splicing endonuclease subunit sen2"; /id="PRO_0000109461" MSKNHEVYKDALPISLAYPLPPIILTNPLTWIPYIYRYLFRKTPRQVQWQCQLHESDLSCVVTDSEAIKKFWTSGFFGKGNLSRSEPTWHTRTKRSLGLLGFDEDLVAEEVTARRRFQRKQFKAQRAYRENRARERQLLLENGKPIPASLEEDAELPEYLTKSLKDFSRVSENPYHITSVPNVEHLQLTFPEAFFLASLGVLRINYENPNFELLPILKLFANIVANSVALTHDYSLQQSHEDPIIEPDNKFLTELAAYFYFRQQGWVVKNGTKFSVDFLLYKKGPVFSHAEFAILLIPCVGNKQKYNMQWHEVHCLNRVIAQVKKSLILCYVQCPSIEDFNKIWKNQASMNEWDWAESVLRQYLIRCVTLRRWVPSRNRD Q8TFH8 PEX12_SCHPO BINDING 289; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:G2Q5N0"; BINDING 292; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:G2Q5N0"; BINDING 309; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:G2Q5N0"; BINDING 312; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:G2Q5N0" SPAPB17E12.03; CHAIN 1..343; /note="Peroxisome assembly protein 12"; /id="PRO_0000339876" MDSPSLLEVLQVQQVEKLISPSLRFILAYFTHRYPRFLLRAYNSFDGIYLLVKLLLEKSQLKKWNATSVERRFQLKRVIAVRDSSIIAEEFPQESESATSLNGIDVLKKLFLTYCIPYLLEKCESLTTVKENHTAVSILSLQARDKQKGALSVFYSKIKILLVRLKKILHFVFRLIRKSNTYLQWLYYLLYALGKTPYTNLADHILRQRVIYNVENIHSRKLISTREKSSLLTSIADHSMEGFLIIIQLIDWWQSNNYESHLKKGEVAFTELAPPKLPFEINVSTTDICKICGEKIKNPAVLSTGFVFCYPCIQVWLQRHPFKCPVTNLELSRKGESFWRLMI Q8WZJ9 HUT1_SCHPO SPBC839.11c; CHAIN 1..322; /note="UDP-galactose transporter homolog 1"; /id="PRO_0000213411" CARBOHYD 152; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 313; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 314; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAGFMRQLFVCMIGIYGSFLSWAVMQEKIITRPYDGERFSSPALLSLAQSFMTVLCGLLWNWFHGVSARGLLEPKFLGYFSSIAISASLSSYFGYASMFHLSYPTVILGKSCKLLPVIALHVFVYKRKFPPHKYLIVTMITAGVSIFSYFQNTSSKGKHAEHDSPIGLLLLFFNLLMDGITNTTQDKVFGKYKLSSVTMMIAVNLGIACLNGLYLISPFCNQQPLSFINRHPSILKDMLLFACTGSVGQLFIFFTLEKFGSITLVTITLTRKIFTMLLSVFHFHHTVSSIQWLGILLVFLGISLEAGLKILNNNSTAKKKAS Q8X1T0 SDU1_SCHPO ACT_SITE 29; /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"; ACT_SITE 105; /evidence="ECO:0000255|PROSITE-ProRule:PRU01205" SPAPYUG7.06; CHAIN 1..201; /note="DeSI-like protein sdu1"; /id="PRO_0000221634" MKVYINVYDLMPDSPVNKLAWTLGLGIYHTGLVLEGKEYAFGAHEIPGSTGVFATMPRPPLEGCRWRCSIALPNCTLPKPDVDRILIRLSQEFTGLSYSLLERNCNHFTNAAAIELTGSPIPSFLNRISRIGLAFPTITNALLQHGQKNTSDVDDSSDSSSDVDEETLIVSKSKKAHKDIPKFSAPPPSADLNNLITDSLP Q92337 ABC1_SCHPO BINDING 614..621; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 1214..1221; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPAC9E9.12c; CHAIN 1..1427; /note="ATP-binding cassette transporter abc1"; /id="PRO_0000093303" CARBOHYD 49; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 437; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 567; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 581; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 601; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 658; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 703; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 782; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 842; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 994; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1184; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1324; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKMFQSFFSNYIDINFFRNATLDQCLLLFYLSLFSLTNLFLIQKLFHANHTQHPLKKYFGETCLLEYIQIILSIVSAALSFYLDTNAVWWAIRTITHLEIVGLNILSSLKYGSTLFSWISVANAFGLLLLRLISIYDFLTYSSWSFSVKGGSFLLLLPLAYNITLFLLVIIPLFFPRAWSPTVKFSKVARPSPEQTCSIFSLIFTYGWLNGIIWKSWKKPITLTDVPALPDTECTQIWYSRFAKNDRKSLMHTILLSLKSTILLMVFLSVLVSSTLFVTPLAIKKLLQYLQNPKSDEGNSPFLWVFVLLIGPYLASVVKELYVHVSRRFMLRIKAAITQMIYKKVLTSKTLFVAVDGSKINLDYVYNLLAKDVDNIGEMREFIGIIARAPLEMGVSMYFLYQLLGWSAYVGLLLAILSSSFPLLVASKISRLTSIANTSSDERIRLTTELLKSIKITKLFGWERPMLSRIQEKRSFEVNNMYSLTLFDIIFKSGMKIAPFISMFITFAIYTKIMGHQLTPATAFTSISMFGLLRYQFIWLASVSRQFIQFKVSLKRVDNFVYGNMVNDSSIESSDSFVFENTSLSWSPTPSTALFQLKNLNFTIPRNQFTLVVGSTGSGKSTLAMALLGELHVISGKMTTPSISQRIAYVPQAAWLRNGTIRSNILFGEPYDEERYFQIIKACCLDSDLNSMNDGDLTYIHSNGSSLSGGQKQRVSLARALYSNAEVYIFDDIFSALDVSTSRKIYESCFLSTLLQHKTIILFTHNVSLCLPIAENVIVLKNSTAQLVSPDSIQELVPSTFFSSNTKKDNIEEENLEPHSFSFDSTLASSSDNDEQRDFASNSSIVLLGLHYLKYFGSNKYILGSILLVMMSQVSLASIHFWIALWSGNSLFSLKLPSSFSFLWGYAILLFIYFLMDLSRAITFAKGGRTASENIHDILSERVLYSPLHWFEKTAAGRILNRFSKDMYATDNLLWASLEGMLLCVMAILITMLNVTLVMPIFMVPAAFVSLLVYLHGYAYSKAQKQLTSLQSSRTSPVFTMLGETLGGITVIRAFKKEKIFEHENMAFIDDMIQPLYISFAINRWLAIRTDGISGLVGFSTGLIALLRQNIPPGLVGFSLNSAIGFNISVLVFVRANNEILTYINNFRRLYEYMLLPSEKNESSCLTKPMNKEWPTLGHVSIKNLTVSYSIGQAAVLEDINLEILPKEKIAIVGRTGSGKSTMGLTLLRFTMIMSGAVEVDGIDINSLDLEVLRQRISLIPQDPVLISGTVRSNLDPFEEYGDGELNEILKTASCESLVQASNKNSLDAFAIHLDTPVDSGGVNFSSGQRQILALARALVRKSRIVILDESTASVDDTTDRRIQQMLRAAFKHATVLCIAHRIKTIVDYDKVLVLDSGKTVEFGSPKSLYTQRRAFWKMCKESHISL Q92344 PFL8_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC1F8.06; CHAIN 21..385; /note="Putative cell agglutination protein pfl8"; /evidence="ECO:0000255"; /id="PRO_0000116633" CARBOHYD 72; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 270; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 346; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MNSYISLIFTLLFFTSAARSSSVSVETGSCVRYTTIYSSGSSEFTSTITPETPSSSSSTFVPISTHTSSATNTTSGQLSISSSSSTSSEYSSSSIPITTVSSSDSFIPSSSQTISASSSTTDNVIVSSSISSTVSSTPVSTIYSGTSGTTFVSSSTTYQVIPTQICDGVRGLEYAVYNYDLPSESTFCHPSNGYTEVSTFNKPAYFGSKDLKQSAPLFTGIFSSLDDIPTYSASDYLPAYPPNPEGMSSTSSSCKTIVYQFFFRVPATDNWSLFVKNVDDAFFGWFGDKAISGWSNVNYDAYAHWRIGAYGMGTFDLGYLEQDSFVPVRFVLANGAYIGGFDFAFNSSSTGPVRTTSYSYTSTCDKSFLPFGKGNGGLDEGTANV Q92347 NOP9_SCHPO SPAC6G9.02c; CHAIN 1..655; /note="Nucleolar protein 9"; /id="PRO_0000075937" MPKKRKTRGKKHSAKQKEEEVNSVVSPGIAKNDEGAGNDEGAYQVNRYTNEPVQPFFGALDPEEEKYFQQAEQAFANHFTRENEDTRFFVDSIYREVQGKELIVCNNVFGSKVLEKLFPLSTSRQIKSFFSALNGHYVELIQTTFGSYAFEKLLSHMAAILNLETQGVTEDQDDVLEGENENVFMTAETLLMYMYNEIRPEVSMLMSHKLAVHVLGKIFLLLDGYRFVYHDGNRTTMESISVPESFPQFAYSIIDSATDNLDTPELRAYCVDKYASQIMRAFIRIDFERSKKTKKKHDPRLVSKLLLSNEYDLKELPFMETLLKDETGSRILEVIVENMSASHLLRFYAVFEGRFYRLCVHPIANFIMQRYIRRLGRKEIGSVIDELKKNTDNIIRKSFLPVLRTLLEKSNHLHCYQDDIFSMIQTSVTNSGKDANIIPCLLRSKHKRDKANPENKERKLVNNLLGAQLLEEMLHCEKQHIQLLLDSVLDLSKEQILEYCLETVSSHLIEGILDLSDLNPVFLKKFLNILSGSFATLAVSAPGSHIVDKAWKATRALPLYRTRIVRELAEGGDDVKFDFYGKKVCSNWKVELFRRAPDEWYRFMKQDEPSKRVHERARQYGRIVSGSSANTQPLGEKRSTENDEELESGPKRVKV Q92348 MU183_SCHPO SPAC6G9.03c; CHAIN 1..376; /note="Meiotically up-regulated gene 183 protein"; /id="PRO_0000116627" MESNVNDEIEKAFAKDSELAKDIIKQYGKTKSIQPLVHRICKYINTLQKENESGQVKEAGSLKRKDRVQHELGQLVYGVLNLSFQAPMRKKLDVYIYENGIAVTLPGEPNLIEFWLPWNEIRCAIHVPCPRKANVQNNFVIILKSESSAENIVSSDNVKEPVFFTAPYPLKKLNLVEGLRSFTHCTNSWDIFRDYFEFIGTSTLSPSVEEFVCPNPQTGDNGTTYGVEANYKAKDGHLFFLRTGILWGFRKPILFIELASIQHFSYSNVLQRTFTVNFEAGGTIYSFDMVDQSVFRAVNDYATKHGLMDSSLAEEKAAPVPKNPSVSYLNEASSLENVDDMDDIDVKEPLFSDNDEDVENSDSEDGSESIGSEDEE Q92350 YDH5_SCHPO BINDING 169; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 173; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC6G9.05; CHAIN 1..285; /note="Probable nudix hydrolase C6G9.05"; /id="PRO_0000057143" MKLKLRWKGHQRFLTRQNSLVGFIWSPLKNTFSKRNSILNNQVCFEAIKYIQRHYFSSQSHHVTYLHQSPLEKLVSNGVVNENGDLTMDSLSHQIYLLHKNRPTLPLKPTNQPTRFASVLMPLVNTSQGASLLLTQRSPNLRSHAGQMCFPGGRVEPSDGSHYYAALRETYEEIGFLPNFFTYLTTFPPLFTRDEKTEIRAYLAFSVQTSLPSLGTGEVKDLFYVPLTSFLNPKHQKISRFRNTDLLYVEFNIDKIPRIWGITAVILNMYLNSICPDALISIPKF Q92354 RL24A_SCHPO SPAC6G9.09c; CHAIN 1..149; /note="Large ribosomal subunit protein eL24A"; /id="PRO_0000136891" MKVEVCSFSGSKVYPGAGRLFVRGDNKVFRFVNKKSESLFLQRKNPRRLSWTVLYRRMHKKGISEEHAKKRTRRTVKHQRGIVGANLDVIKEKRNQRPEVRAAARAAALKQRKDKKAASESEKKAIKAKSAASSARGQAIKNAKAAARH Q92361 YDHG_SCHPO SPAC6G9.16c; CHAIN 1..264; /note="Uncharacterized protein C6G9.16c"; /id="PRO_0000116631" MKFFLSLKDFKGEKFVLRSELDESSAFLCAISPTCRYVLRDEIPWKRLQRNVTSESLTDELIVDLLCGRSESKHTLQLVVLENLCRIYINYVDPFPLRIAWFELEQQALKDHEHFDVLWECSHSIKDLALASMAQQKNELQKLMAYTEQLQEECKSRERKLIMKFADMIKNARNNEDNEDNHHINYEDESDVGTDEQKQQEGVNSSAVSDTDESAVSDEFMQIKEEFPMKALSASPTADASPESAGEDDSHRRSSHESSETVSE Q92365 RL36A_SCHPO SPCC970.05; CHAIN 1..99; /note="Large ribosomal subunit protein eL36A"; /id="PRO_0000195018" MAPGLVVGLNKGKVLTKRQLPERPSRRKGQLSKRTSFVRSIVREVAGFAPYERRVMELIRNSQDKRARKLAKKRLGTLKRAKGKIEELTSVIQSSRLAH Q92366 RL29_SCHPO SPBC776.01; CHAIN 2..61; /note="Large ribosomal subunit protein eL29"; /id="PRO_0000219140" MAKSKNHTNHNQNKKAHRNGIKRPQKHRYDSLKYRDAKFRRNQKFANRGTVEAIRQAKASA Q92367 AAP1_SCHPO SPBC1652.02; CHAIN 1..594; /note="Amino-acid permease 1"; /id="PRO_0000054166" MTSFTESKKLDEIESPVPEIIVPSTTNGNGTIESYKEKSVGTSFLDFFRSYKLRPDNEFAEVHNSEDFLKPRHLQMIAIGSCIGTGLFVSTGKSLKNAGPGSLMINFIILSAMILALILSLGEMCCFLPNQSSITMYTGRLLNNNIGFAQSWLYFWIWLTVLPSEISAACEVVDFWTTQHLNPAIWVTIFLAYVVLVNAFGARSYGECEFVSSFLKVVIVIIFFFVAIIINCGAAPKGGYIGAHYWHHPGSFRNGFKGFCSVFISSAYSLSGTENIGTAAGNTSNPQRAIPSAVKKVFYRMGFFYIITIFLITLVVPYDNPDLGNVSPFIIAIKNGGIHVLPHITNAVILVSVLSVGNAAVFAASRNAMALVKQGWAPRFLGRVDQKGRPVISYLCSLAMACIAYVNAAPDGSVVFDWLMSVSGGGAFVIWGLSFIDHIRLRYAMKAQKIPDTVLPYKFPGSVYLSYYGVLINFLALCALVYISIFPVTHEKPSAYGFFVSFLGPSVFIAYLLISPIFVKPTFQSLKDVDLTTGRYDLVNSQMYVAESSTSELSEKDLTKPNLQSNDNKNSEDLESNTPPQKKSALQKVADFLC Q92368 RCD1_SCHPO SPAC29B12.06c; CHAIN 1..283; /note="Cell differentiation protein rcd1"; /id="PRO_0000097199" MENLESPNYEPALVYEWIIQLVSGTSREQALVELSRKREQYEDLALILWHSYGVMTALLQEIISVYPLLNPPTLTGPTSNRVCNALALLQCIASHPETRIHFLNAHITLFLYPFLNTLSKSKPFEYLRLTSLGVIGALVKNDSPEVINFLLSTEIIPLCLRIMENGSELSKTVAIFIVQKFLCDDVGLQYICQTYERFYAVASVLNNMVMQLVDSFAFRLLKHVIRCYLRLSDNPRAREALRHCLPEPLRDATFAQVLKDDHNTKKCLAQLLINLSDVAVVNQ Q92371 NACB_SCHPO SPAC4F10.14c; CHAIN 1..151; /note="Nascent polypeptide-associated complex subunit beta"; /id="PRO_0000213553" MDPSKLAKLQAGARIGGKGTPRRKVKKPSKSAMSAADDKKVQGALKKLNMQNLAGIQEVNMFKEDGGVINFRAPTVHSSLPNETTAIYGKAEEKTLSEILPGILNNLGPESLTALRQMAEQLKVSEGEKGADAQADDGEIPDLVEKFDEQD Q92377 MDM12_SCHPO SPBC28F2.06c; CHAIN 1..273; /note="Mitochondrial distribution and morphology protein 12"; /id="PRO_0000096328" MSIDFDWSKLDSELEAKVLHLLEGQVSNLSLPSYIKHLKVVDFHFGKVSPQITIQEIGDPDPQFYENEAFELANQELEGDQCSRNNVSPVLTDLPPYAAEHPFSRLAYFNPAFNSPGILSASGLTSPIPESRPSTPMDNHQERDRSNDFQVTAHVSYDGDANLSLEAVLSMNYPNSEFAVLPFKLSFIRISIDAIAVLAKMGKRTHLCFVDTLLHGTGEHASSVIRDLTVESIIGESNKQLLKNVAKVEKFVSEKVKRIIEDELVWPSYITIE Q92380 REC11_SCHPO SPCC4E9.01c; CHAIN 1..923; /note="Meiotic recombination protein rec11"; /id="PRO_0000097221" MRFEFESDASSHLNEVLTELESVELENVEYEGPSLQNVSICASPSEKKRKWGTQDEFSLTENEENNEIETNEEMHVNSHDYAFPQEFFLKLLDIDMPLEQLSQHYFEDYKSNSADFMLTFINFALVASGCQPFVTNFDVQDVDSIPETLSQVNRSSFQKSSCAYTDYLYTSNSKEAKTVRIRFQLFLVEFISKVYVEDAFLGDSFMETTKAWIFTMTTSPWMLVRHTATTICCDIMRCLCLIVNKLSEKSNQTAEILVLRDLTSRFIDMIHDICDSVLFSRIHDIRASIRIVCVTALYDCCQLLPTYLINRNLIRHSGWGLSDAESQIRKISLKIIDYLSSHEPEKDQDFVVDFLDRFSLRIVEICRYDIDSVRSVALKTCEKLMEKISLNGKCINIVSSCIFDGKPQNRISTMRILVAHTNERYANYCEAKTATISLSKLLRREKIPLLVSSFESLFKMNALLFILEQGFESWFRDSSDHIFSRVKDDDKFVYQSQENNFYDADFIREYDMNNHRQQLIEESMHSIHTNSQLLASWEDVAKLLLYDRFDAKDTNSVLNPCIPSNAVIEFSSIYLHYFATHISKRSKKPGKRLEDEVVNQQQAMLRNLPLLLQKYRESCVSSYFFIKCVEQIPDELLYKREFHKDFSKLYKEILDIFNSTTVNFLMILCSRFFHRLAVNKVVQEDILFAIDNVYNDLAESLHEQLNAYIQRKKINKKNQLNGNDETQNLVLALNKFGCFAKEMVCLRDVNDWNIKLSEKLCEICSLEVGPIVCYSSLKVLFLLLLSDMRDRNCIFTNIFLKAAKVAKQKNGNSFLSKVFITITMLTLFLGSKANNWDINFSDDDLKLMNEEEIMEQIETFKAWSMKFKEKSSGNPSYFFSPEDTEEKELWNNLFEDWYPNRARDPGTLSHLVKGLKETADHLS Q96WS1 WTF11_SCHPO SPCC1281.08; CHAIN 1..264; /note="Wtf element wtf11"; /id="PRO_0000193220" MNSNYVPLTSSVDVEEKMESENGVDLGNDIDLEKGLPLKYNSENESGLPSNSASSYLINPDPTMDLEAQTFNHNESTTSVGHDNSNSPPKCRKTCSSNKVYSNEVPLLFVFVISISIVCIFDLVIFGCLQYNMVSMDDLHVMQRLSWFCASLALLFILMRYYDFWTKACKDGIKHIFKKWKNTPLAFLQVLIFNIIGFFVRKGLKDSFGEQWGLKTSLFAHVSFATMSIFIFIFETLKPGSCSVDWIARILKAVVYFLEDSDEL Q96WV0 UREG_SCHPO BINDING 93..100; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPCPB16A4.05c; CHAIN 1..286; /note="Uncharacterized urease accessory protein ureG-like"; /id="PRO_0000373859" MAIPFLHKGGSDDSTHHHTHDYDHHNHDHHGHDHHSHDSSSNSSSEAARLQFIQEHGHSHDAMETPGSYLKRELPQFNHRDFSRRAFTIGVGGPVGSGKTALLLQLCRLLGEKYSIGVVTNDIFTREDQEFLIRNKALPEERIRAIETGGCPHAAIREDVSGNLVALEELQSEFNTELLLVESGGDNLAANYSRDLADFIIYVIDVSGGDKIPRKGGPGITESDLLIINKTDLAKLVGADLSVMDRDAKKIRENGPIVFAQVKNQVGMDEITELILGAAKSAGALK Q96WV2 YJO2_SCHPO SPCPB16A4.02c; CHAIN 1..339; /note="Uncharacterized PH domain-containing protein PB16A4.02c"; /id="PRO_0000310808" MDPGVSSHLRTASLDEARRLPELERVLKSGWLIKKGHATSTKKQLWAVLRRDQLSFYKDEKEYKTKFIFPTQDISAVAYYKEKSPKTFFLYLNEKIIRLIATSNEDAEEWVHVLRSTTGYRAPFSRHPISYILANSSSRTESEPNVQISDTDFDNISTEPRNQTTSPLDLETGQGDHFCTSLYDLIQFGKLRPPGINEENANYPFNPQEVNTLNKHRHSASLQNLYKLLDENKVLMQGTIHWLHGNLHRWSKCWAVVRGYGMTIYNTNREYKPVKVIPIADIQDVAEINVPESSHKYFFTVITQNKPIEFRVDNEDSLILWVAALKTSIDKANGTFTAC Q96WV6 YHU2_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPBPJ4664.02; PROPEP 3945..3971; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000353806" CHAIN 24..3944; /note="Uncharacterized threonine-rich GPI-anchored glycoprotein PJ4664.02"; /id="PRO_0000353805" LIPID 3944; /note="GPI-anchor amidated alanine"; /evidence="ECO:0000255" MVEKTSPILITLCIFLLIPISSALPFQTFEESLKLKSNISHTGSFFANLSQSYSSTSIIHSVSSPVDCSLDVNNQINTINITSVSAGTNELFLPTLSHAHANDREASLFFPYTDIRYNGFPEPSNTDSTSILSFNTIRLIPSTNVINTSHYKGFNRYPTISSTVKVGKRAATASFSYTNVSSSVIATAYTSASSTILSSPSVEQSTPSIITQTESSTTTEGSSVASSESTIANSDQSSFITYESTQNPTANKTDASQQSTESTSSSASAYSYITTLQTATTAQQTTSENTYSTSGPNLTTSNTSPQISSTISSSSFIVESPSVALSTSSTTTITNASTPAANTIISRSSKPTDTTNSISFANTTPENTSTQITSPTAVNSSTPITSSSVLNSSTPITSSSILNTSTPITSSSVLNSSTPITSSSILNSSTPITSSTVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTSITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITRYSVLNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTAITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSILNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTGLNTSTPITSSSVLNSSTPITSSTVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSVLNTSTPITSSSVLNSSTAITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVVNTSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVLNTSTPITSSSVLNSSTPITSSSILNSSTPITSSSVLNSSTPITSSTVVNSSTPITSSTALNTSIPITSSSVLNSSTPITSSTALNTSTSITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNSSTPITSSTVVNTSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVVNTSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVLNTSTPITSSSVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSSVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVLNSSTPITSSTALNTSPPITSSTVVNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSVLNSSTPITSSTVVNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSVLNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSSVLNSSTPITSSTVVNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNSSTPITSSTVVNTSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTALNTSTSITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTSITSSSVLNSSTPITSSSVLNSSTPITSSTVVNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSLTALNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTSITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTVLNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTSITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTALNTSTSITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTALNTSTPITSSTVLNSSTPITSSSVLNSSTPITSSTALNTSTPITSSSVLNSSTAITSSSIVNSSTPITSSSVLNSSTAITSSSILNSSTPITSSSILNSSTPITSSTVVNSSTPITSSTTLNTSTPITSSSVLNSSTAITSSSIVNSSTPITSSSVLNSSTPITSSTTLNTSTPITSSSVLNSSTAITSSSVLNSSTPITSSSVLNSSTPITSSTVVNTSTPITSSSVLNSSTPITSSTVVNTSTPITSSTVVNSSTPITSSTTLNTSTPITSSSVLNSSTAITSSTALNTSTPITSSSVLNSSTAITSSSILNSSTPVTSSSVLNSSTPITSSTVVNSSTPITSSTALNTSTPITSSSVLNSSTPITSSTVVNSSTPITSSTALNTSTPITSSTVVNSSTPITSSSVLNSSTAIASSSILNSSTPITSSSVLNSSTPISSSTVITSSVVIGSSSVLSYASSIVSSVSLNSSLLSSSGGFSSSAFSTGSSSFSLTSENGSVSSSSLVSSSPVLSGYSESSFDSSVFVPSSVSRSFSYSRFSSGSLDSSSVFNSTTVSTASGISQGSVLSSTRAIESESTASHRSSVLSELSSYDLSTSAFSSSSSEPSTLDYSVSSSSLSSSIGVGSSFSSNSKVTSNKVPSTVSPHSSSISDTKSPATVTISSSSGQFTHSTFSTGSTMHNTVSHATSTSSSFTTSHLPTNTLASTFDNSQSIFSSSSGVPGLSTKSSSLGKIGSSSISLTLSSSSIRDAELPTPSRMTSPSLSETIPQSSSISEASTSNPNILSSTVLSFDSTITNSFTTASTSIMKTTSLNSNSYKWYNSTTQSVYYNATSSTVPWSNSTFRNTSNTMTSRFVSNDFNSTISLQPVVQFNNFTKREITTILITASDGSAVTTSLSTFYSASSLASSVVKPLYILSTFFVAAVFFIIF Q96WW0 YNH9_SCHPO SPBC32H8.09; CHAIN 1..483; /note="Uncharacterized WD repeat-containing protein C32H8.09"; /id="PRO_0000051498" MDFTALFASLNPTFASVSHCGNWIASLSRSGHVLIRNSETLELHHVFLLNAQFIQKVVYLLWKPNLGAEKCHQICVASVDKVFVLDIVQHDYYASIQCDQDPLSSISWSPSGELLLWSSFDSKITVWSLNTQKGYLLPHVKTNVSKVYALHPSMQFCTILSRFNGSDCLQFYQISKKAWILLKECKLPTIDSTGIHWSPDGNWLAVLENVLDAVVYIYHRTGLLFHEYRPNRLIEVGFSDFEWSPFGKYLTLCSYHDSTLHLLETKTFSIVFRLHHCLQYTNTDLEMHIWEEKETIYEQQMTYQKVHKLRTDFPEPSFCSASKIRFNCDETYAATITSKYPNVLWLWNLQNKKLHTVLIQKHHIVYFEWHPGRPDLVVIQTKIRKESKIPSNATFLYFWALSWNTPRVVGVPKKGFNIQKVQWLQPSEFSSRPVIVICGEDAYTVAYIVEDEDESFTEVTQTIISQEVLDNELETTQTISIPS Q96WW1 OMH5_SCHPO ACT_SITE 318; /note="Nucleophile"; /evidence="ECO:0000255" SPBC32H8.08c; CHAIN 1..421; /note="O-glycoside alpha-1,2-mannosyltransferase homolog 5"; /id="PRO_0000357059" MKRYDTLHVWKLIKLLICKFLLFHDFGTALFTSLVKASMLGFHNWRRTYWLYLKKLRPINDTYDAPFAIGCKNVAYEASQYPRMNATFMVLARNSDLDGVLSSMNSIERRFNRHFKYPYVFLNDEPFTTEFKKAVKDATDSSIQFGVLDDELWNFPKDVDKDMIDESIAEQVGVVYANFPSYHKMCRFFSRNFYKHPLMQQYEWYWRLEPEVTFSCDISYDPFYYMDKHNKVYGYVIAIKELAKTVPNLFRYTVAHQKISNLPTTDLWSFFLDKRYETRIKKLKEEQKDQGYYVLPEPPLNRIDGQIYNLCHFWSNFEIARLDFYNSKEYNEYVDALENAGGFWTERWGDAPVHSLAVGLLLNRSQVHYFRDLGYQHSTIQHCGQEYGCNCDCPFNIPDYETKPGSCINEWASVMGGFLDE Q96WW2 MUG93_SCHPO SPBC32H8.06; CHAIN 1..383; /note="Meiotically up-regulated gene 93 protein"; /id="PRO_0000106419" MEEKENVNLVEKSNYVALENTREIDVFDEFLNAIGNENTITPVYADSSLTHLRKKSYTKVVHDCTYALVINPYDKKVIWRRGLAYLRLGHPHLANRDWEHSLELDPNNTYIQKSLHRLKEVYYIYRECAETWQLRHLRVASSQQLPVGLRKQYPNIIRGKIWWKKVHDNCQLCGQQCELKKENLSAMRSMLYMANTYAKDDTENHSPSAQIGIESSEDELENKITKGEHSLLVPEELYRSNYPCPQNIDQFLYMIKVLSAPCLYIETFSFPISTINQLFKAHGMSVEQLNLFLKSIHYIGLCSRFCKQWSDKARSLMQALSGLPWFSFVVQHCLHITAAQILLHIPDIQEEEFRNWHVSKKPINNTDLSSEFEIAEIPINCYT Q9C0U6 XKS1_SCHPO BINDING 88; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 158; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 274; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 275; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 357; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 455..456; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 459; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+); Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140, ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216; EC=2.7.1.17; Evidence={ECO:0000250|UniProtKB:P42826}; SPCPJ732.02c; CHAIN 1..555; /note="Xylulose kinase"; /id="PRO_0000311717" MFLGLDLSTQQLKGVVIDESLNVHQEVAVDFDRDLSDYNTIKGVYRNGYEVFAPVCMWLDAIDLLFERLKASVDVSKIQAISGAGQQHASVFLLKGSKKALNSLDAKSSLKQQLESLIHPTSPNWQDASTTKECEELESCIGGAKALADLTGSKAHLRFTGPQIKRFRRLHPETYENTERIALVSNFLASVLLQTEAPLDISDVCGMNLWDIQNEKFDIRLLEEVAGNSKGPDLANKLGTVEINGAKHLGPIGKYFVKKYGFSPNCQIIPLTGDNPATILSLPLRPGKDVLLSLGTSTTALMATQNYVCSPEYHMFAHPVTQNHYMVMLCYKNGSLAREQVRNTINEKYNVSDNTSWDRFNESILNPNIKGAGEKKQLGLFYPQREILPAVGPGTWRFAIQGTELYQVDKDEESWDYPDEDASAIVESQNLDIRMRITPLLTGIPQPDRVYVVGGASRNEAIVFKISQVLGCDVYRLKHGGSNACAVGGAIKAAYAMNGKGFTFEEYVNKSWDESKKIELIMNKPSAQTYEEYGKLLPFLKKAEDIAIQQSDIRH Q9C0U9 YQD3_SCHPO MOD_RES 14; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCPB1C11.03; CHAIN 1..570; /note="Uncharacterized transporter PB1C11.03"; /id="PRO_0000372786" MTESIISSRTASISSKEGYEIRQGSTDSSSLDLEKKENAVDTTIAKPFDSDEDIADVEKAGGKKINNSLIDETFAFMQDAKKLDPLTPKQESKLKWKLYIYLLLMLGFLDMMLFIGKATLSYSTILGLFDDVHITSNQYNNLNTLFYVGYIVGQFPGHYIMQTFPLGKFVGLVTFSWSVIVFLHCCAYNYGGLIALRFFLGFTESCLLPAMEATMGMFFTHQEQAFLQPVFWISCLSCGIPAGFIAYGLEFVTKSIAPWKLFMIITGGITFFLSIFLFFYYPDNPSKARFLTDEEKLYTIDRVRKSTRGGIENKIFKKHQFIEALKDPITWLFTFAAFTLMLSNNLAYQQNLIFTSLNVSDLNSTLVGVALAGYNTVSAIIATFAMYLIPNQSAYHAMFWMLPSITGGIAFVALPWSNRIGELATMIIASDFGITYIIALGWTTATSTGYTKKLTRGLMFMVGYAIANIISPQLWQSRDAPRYYPAWIVQIVVAWFVTPIIYLVARVILARRNKQRKELKDKKIAEGSLETIEKTYVDTVDEFGNPVKVLIDNSMLDLTDMENLNFVYPL Q9C0V1 AMT1_SCHPO SPCPB1C11.01; CHAIN 1..497; /note="Ammonium transporter 1"; /id="PRO_0000278387" MSSTTDATPTPSGVNGGDSMTVNLNQFYNNGDVAWILTSTALVFIMIPGVGFFYSGLARRRSAISMLFLSMMSVAIVAFQWFFWGYSLTFSHEGGPYIGSLANFGLRQTLGRPSSGASSVPDILFCVFQGMFAAITPALAIGAAADRGRMFPCMVFMFLWTSIVYDPIAFWTWNPNGWLNKLGSYDFAGGSPVHISSGMAALAYSIVIGKRCDHGTTKYRPHNVPHVVLGTVFLWFGWFGFNGGSSAAANMRGVMAVVVTHLAASVGGIVWCVIDFAKNRHWSVVGFCEGAVAGLVAITPGSGFVPPWAAVVIGALGAVFCYAATYLKKIIRVDDALDIFAEHGVGGMVGNILTALFAADYIEALDGSGTAYTGGWITHHYIQLGYQLADTVSCAAYSFAVSCALLFVMNYIPGLSLRVSREDEVLGLDKIELGESAYYYKDSTDEPPPITTSGVQYTSPTVSDSASNEKEQEHRAQNEAQKEEEYRAESEAQAPAI Q9C0W8 TIP20_SCHPO SPBC691.02c; CHAIN 1..678; /note="Protein transport protein tip20"; /id="PRO_0000116852" MMSQQLIDFIDSRTRHPYKSDEVEKFQQEVNELQLPDPNSLPILSEEEKRQAREDAAFRRSSEGLEDAWLDSAIPADPTPIFRDTVELLCVYQSFVKKSASLDTVANFLDFSTDFSTLSTKKDETEIAPDCLHYIAELLFQKKEREVKEKWKNELTEKLKTLFNWPAINPNLKESSKFESFFGFVRSIQSFKDSETGLPLFMQVYITPYVNQFRYHFMSQKQTNVLSKPEWFFEFLLKVFRSNRSFYMLMRDIKFFPGVPPFFTFINLLNNVAKEKLTHIIKYDDYLVHLVHETLQYSVRLEQHFHYTQDPLIIFLFEQNGTYDKWLGLETQLSLTKLEDIKIASDAWELESDQSDDFSSAVPTKMTVRFRDMIETTFSVLQNLPSLDYQFNFWRSVQLKPMMQYVNWLEAFYESHESSSSIHLPGSLQTDKSKFDIAEVERMCKLYSNFKLLMDWLDDIEDEDVYIRIGHKMGSENYAAFYQVKPRLSTLTNGSFRMILRAVSQTLRPLLDNYSDLDTWVIKEQLPGAALLSTSVSAEIVGFQSRLKEIIALLQKLLIGSSQCEAIYQIGTLVESWMIKIVMTHQFSVRGGVQFAMDAMQIVLEFSDYPLLKFERLMSTVELLSLESGENKLIKKLIIEINQKNYDFIDEFFKTKEITLSYEDALGVLYRRVDAWKD Q9C0W9 PFA5_SCHPO CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; PTM: Autopalmitoylated. {ECO:0000250}. SPBC691.01; CHAIN 1..312; /note="Palmitoyltransferase PFA5"; /id="PRO_0000212981" MSTNLEEKQRRFSKLQKTLGVVFPAAILLSTGYTVWVFIALICVDSNIKIRNGYRNLGGGIVLIIFFFITSGLAYFSYFRVLFSSPSFCGNTLYTYYGFDNPIFLCGPNGAPRMCGTCKCWLPDRSHHSRVSMRCIRKFDHYCSFVGKDVCFSNQKFFYQFLFYGFSAACMVLISTAIMISRTYHYRSLPGTWIFVLVFSAFGVLFLGVMLVRHTGYLLLNINSHEAKNWKTRIYSFSVFFPEHMDSRVLVQSDPGDLPWDRGYSENWRAVMGDHWYNWILPLRRSPGDGEHFLYSPSFVSKMQSKALSMNS Q9C0X8 RRP12_SCHPO SPAPB8E5.07c; CHAIN 1..1163; /note="Putative ribosomal RNA-processing protein 12"; /id="PRO_0000273518" MAEVNEPLQIELRKIRNSSTAGVINEFDVIVSAVEGTLKEQKTEATPTAYLVALLTLVKEFTDLKKNFKGHTFQLLELVIKYVPSNVLQAKFPQILSVLAPVVNNAETNKTVLLPYLNVLEKLLLLQDYSSWTHGNSCKTSIYILLFFALSNTEKTRVRSLQILANILKNPPAGPVTEHPAIKYTAFEPLRLLESLATAKKPKTPAEVQKLNNSLVLIRVLCSSTHWPMTLVERLCRSCVLIVGQRSTNSILLVYQILDGLSKKSVDYTDAVSLRMTLICLQKLEPSEHDPILMVGWLKAMNTAIRAFNILDKETAKYECLHRFKAFFTLLESESMEIRLQTATTICSVIGCLDTTPNSFAVVEEICSFICDALRDIRFRLAYPECFQIISSLCDKLGPHSDPYLIPALEVIDYLRGSEGFDGKALVDEAIGSFVRAIGPEAMLRVLPLNLELNDKDAVGRAWLLPVLRDNIRFANLAHFTNYFVPLSGQLYQKVIEMNDLDSIPSKLLQTLVDQIWSLLPGYCYLPLDLQSSFTLEFASILVNVLYEQVSLRSVICNSLTALVETNSKVADKLPLDDVISVPVSASDASSNLAFLTNMSSNFLSVLLNVFSSTPSQYRYPILKCIQTWIFISSNDTIHSVYKKVTDLLPDSLNDLAGSFNIAADGISSPMAYSLIDLLIVISPYLNQDYAVTLFEYVHEFLRHVNPAIQKKGYKLLGTLLRVDYGKAYATQHVKEIFEELSSVADRVVSSTRKDRLASLNALYELQSSELVIAIPQLLPEAIISLKEVNEKARHTAFQLLFNIAKSAVNSVEFGNSKPERVEKFVSVISAGLAGSSTHMISATIIAISSIVMEYKVFISEPFLVQLISTLNLFITSSKREIAKAAIDFIKISVSSFPVECIKPLLPELIPNLLAWSHEGKANLRVKVRHLFEKMGRKYGIAEIEPFFPAEDKKLITNIRKTQERNIRKRAMKRDPAKPSSAQPRKTFASAYEAAVYDTDDEAEEEFENDEMNNGNGGDLRMDEAFVQEDNDEEPLDLLDIEAVSKISSTDPRKKLAARKQKLNSAFKSNEEGRLLINDSDEDELIEDSLANAQQHAEVNRTYLEAVAGKESFRRGLNNRVKFSNKRVRDDYDEEMEEVEVPEVTRKPAKQKFDRKQRGQKGY Q9C0Y5 PDR1_SCHPO BINDING 794..801; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPAPB24D3.09c; CHAIN 1..1396; /note="ATP-binding cassette transporter pdr1"; /id="PRO_0000362140" MSEQEKGKGDLDDPNSKNTKCPDKFEQKVEEYLEVLNELHLTGRTSGFCMRNFTVEGAFNPKFQIRSFFAQLLHPINIIFRTGPKRDIIPLVKGFDGYLQPGSSLLVLGHEGSGGSTLLKALCGIVEENERLNGSLHYDGLDYKIAHSQFKADLSYCGEGHSKVATITVRRLLEFVCSCRLPASKYDHPRSHYIRRICEIIRDAFDLGDFYNHRILRVFNSGDQIKVDVAQTMCARPLIQCWDNNMRDFDSISVIDILSRIKVLSHKLGTTLVAIVSQASDRIFHMFDMVTLMYEGEQIFYGPTSRLKPYFLDLGFIPAKHSTTVEFVTSLTYPEMRIINKKHQGFIPSTPAEFRECWLRSEDYAKLIKFMDRYEENHSDIHAFKDAKFDQTRLQKFLRWLNSNPCLIPYRLQVFATAKVTFFQYLHDYSYIATFVFTYVFQALMLGSLFYNLRNESSELYSRGSVLSNAIVFTAIQTMSEVDIIFLKKSLFKEHRVQSLYHPSAALMGSSLVEFPMRIVVVTMYDIIVYFLSDLKRNARSFFIFYLFTIVITFCMSAVFRFIALLSTTAEIAALIGGIGALVLIIFCGAVMPVQYIGWWFRWIAYANPVNYGYESIMLNEFDGREIPCSLMAPAPDTAPIENNFCLATAGRTGTSIVSGYQYLQVVYQYKADFLWRNCGIILGFAIFILASSLILANFIRYDRESVHIPEFQKRKSYSQVASSFLIEPQDKPPSQTEPDNKKVDVSTTLSTNDNLVLCWRDLNFTVVTKTSKKQILTNVSGYLKKNTLTALLGENKSGKSVLLRILSQRGIAGSVEGEITLSGLKNPKNLRKRIGYVRKNPLFISEYTVRETLRLHAALRQSKQRSLSEQYAYVEYVIDFLGLGEVADFIVGDMGKGLSLYHKRLLSIAVELSARPGSILLLDEPANGLDSQSAWMLVCILQKLARSGLSILCSVSQPSSRILELFDMMLILDLNGNTVYYDTMGRDLSKLVNYFKRIHGTNEHSKDTADFVLHCIQFLKQGPEFDYAGAWASTNTHKQIIEHVNFIMDNPELTDDDFPNETRFMTSFFFQIYKISMRNFVAYWRDSSLLRARVAFNIVAGLIIGFSFYKQGVGVEETQNKMFSAYMLTVASTSTMNGLQPKFIYFRSIYEQYEQNTAIYSRTAFIIAFFLVEAVINCCFATLFFFGWYYPSGFYEFNHNIPFYGGFAWLMLMIFTLYYTTLGIGIATISPSIGTASIISGTAFVFIQYFNGMIQLPGVIVGFWKWMDALSPYKYFLEGMIGGVLHDAPITCEKFEIHYVDPPPNYSCGEYFSSFLNSSGHGIVYNPEAYSSCQYCPYKNADELMVGFGYHYNHKWRNFCIMIGYTAFNLGAAIALYYIIHKTPWKRLAARFVPD Q9C0Z1 YKM1_SCHPO SPAPB24D3.01; CHAIN 1..594; /note="Uncharacterized transcriptional regulatory protein PB24D3.01"; /id="PRO_0000115012" MTSVEKASKACELCRRKKIRCNRELPSCQNCIVYQEECHYSKRLKRSYSATKKKNGNPVLESAIPSLSPSPSIENGSAMLNSDITSLSNRIFKVEEKLDLILSLLKNSSEPLDRTERKDFPSLAMQIRDANSLVNTKLKEYSRRFELPSQKTSFDDLFSSTFPNFDAAFKDIPDKEWAFENVQWYFRYINCWWPVFYEKDFMDEYECLYRDRNQVKGAWLVSFYSVLALAASRSKAGKDQKLAESFFSTSWYLIQKPGFFLTPQLEKIQALLIMIQFAAHVSLHTLCKALCGQACLMIRDLNLHRESANADFSNKDAELRRRVFWICYIFEITTSLVFGTPSVLSDMDIDCEHPNYEYGRYFSEMPTGDLIFSSEVSLTILKNEVRTKVYSRTNTSNARNREKAIWQIHEKLLCWERALPIELRQYFIALTENAQIYEELDFEKQRLFSACIEVYLSYCNTLIFLHRLNESVEGANICLDTARRAINVLKFFFIIPIAKNVCYLWVFLYCPFTPFLVLFSNIVNGKEPSTDIAFEDLNRMYSVNRFFVKLRDIGGDLAEKLASVTENFIHAAENYFAVQPAFMADAFDFASFLT Q9C0Z4 DOP1_SCHPO MOD_RES 1671; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB21F2.02; CHAIN 1..1687; /note="Protein dop1"; /id="PRO_0000316224" MNTIIDASNDAKYRKYQDAIRKCIALFQTVEQWPDYISFLTKLHKVLQTHSSFVNIPCSLLVSRALAECLSPGLPSGVHKKTLEVYDYIFTIIGSKTLTNELSTWSYGLTPFFSISSIKTKHDYINIIKKHYVSLGVGIRPCFQAVFISLLSGLEEDVDESSQEVYHLLDDLVKVLNDEKFAWGCIWSTILSFPSQRPGALAYLLRVCNNLAEEDIQTRVIQPDSGLVVRSFAAAISDNDILVQRGYMDALLNYFPIQSTFYKDVKPFDLKLLHMSVASIVLRNDLSLNRRFYAWLMGLSKDTELSISDSSITVDENTLQQNMAIFFEGVKDLLSSKNSLMSFYKAFRILYALSDRRPLFTIVESQILPCVLHSYETLTNVFHRDDSKHLYESAVDHGRRLIMKFSDSELHTFLFHCVNKIVANTTENSDSAEAVKFILDSQNFFFESINTEYSFIIFTNLLMHLEKTSPNSDVDGVSMTILTICKILLNNFDWNFFNYNNSAIDSYAKCTLNLDSDFENGILTYEILYKKCKCSLLSLLKQYIKDSHVHHEVLLISLNLIKEASDTEFENEFLDLSLQGFKDNSWSFQTLGSFVKQLPSRILINSTACVNVILDRIWCELCMFSYFREEELLSVIWTLQEKLQTRIIESYFSTCIVKEQLELRAPTIYYTPFYNLLKKSAQQSLFHFVFDRPLLLLLNSLLEDESGRDYTAMMNWINASSSLQLRVLELMTENLLSLSPNLTSVNSLETAMTRYNINEDQRNSEASRCVYFLKLCTRIISYFQDLHPKEGRLKSAKQVEELCLVTWADALLIQKKSLTYSSFLAFLVKLCLDIVLTPQNIKTSTDVYIIQTWALRLLYQITSIWENPLKFESSLIVGLFALVQEVERSPSSTYRSFILSLLQMLEFLLSRLDGTIDLSSEQHYLLSNFVLVGMLNDDPGLSPKWLHAIKKLLPLLLQNLQLLMVNPIQSLCKFVHSFLDQHESMYLKYPDPVKDYACMDVFIAKLKMLSELVSAALLEFTYSPGPKKSNLEANGIIGNVISGVFAAESSGVSIDVNKRLSMLLTMQDALQTLFLSYSWHIRSSYADKTSKVFMNDSSVLKEASLSGLKEFYFCEPLECVETLVQIYLENNVECCQCIWDIFSFLSDSEPQYIVKQLVSSFFAREGIASYAGPSSLTAKITQLDILCCMSDFVSRVEGENTSKIFTEISKFVREIISSSNSFKNYLLVCLRMLLEVAKNVNTYCESRQQKDFIDLMGKTLSSVLFHAGKSSDPNLTVDFLAYHKAAADTFEVAKTQKKTSSVYLFVKYLDPSLLDFFCSEFVPKITELSKEEDKLVAWATSIVNVFITPLVKARTFPESLTTYHLDLLLVLSKHPFLSKSWRRDFWEIFNDNSLFRFDIDQLRKLSPVIYTALYQEISRLNDLITKSDLGVTTLFTSRDTQLGARQSNICRITILMLSSPRDFFLPSLPPLIDLVKRLITSDPEGVLKKDLFLFIRALALRTSSKHLLPLWPIVVSELLIIFKSYCMPNVAISKETLLDACRLLDFLTALKLEEFALHEWVVMLSPLDAVYWSGKTSRKSLVQKVSERLQEQASEKDDKSSVESEHSILTSTTRTPSLGIYTTDAQLRNFLNRISIDAYEESYSFSTIDIQSFENSIYREVLQRFSNAPLSPFSSIKAPSSLAGSSN Q9C0Z7 RS6B_SCHPO MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000255"; MOD_RES 236; /note="Phosphoserine"; /evidence="ECO:0000255" SPAPB1E7.12; CHAIN 1..239; /note="Small ribosomal subunit protein eS6B"; /id="PRO_0000137340" MKLNISYPANGTQKLIEIDDDRRLRVFMEKRMGQEVPGDSVGPEFAGYVFKITGGNDKQGFPMFQGVLLPHRVRLLLRAGHPCYRPRRDGERKRKSVRGCIVGQDLAVLALAIVKQGEQDIPGLTDVTVPKRLGPKRASKIRRFFNLSKEDDVRQFVIRREVVPKKEGKKPYTKAPKIQRLVTPRTLQHKRHRFALKRRQAEKNREEAAEFAQLMAKRVAEAKQKKEVVKARRASSMKK Q9C104 GDE1_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:16061, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:57597; EC=3.1.4.2; Evidence={ECO:0000250|UniProtKB:Q02979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16062; Evidence={ECO:0000250|UniProtKB:Q02979}; MOD_RES 521; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 523; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 851; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 852; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 853; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB1E7.05; CHAIN 1..1076; /note="Glycerophosphocholine phosphodiesterase gde1"; /id="PRO_0000067250" MLENDLQKVVNLFNTRIVQLDNYVTRLSTEKSPNTEITQALSSSYEAEEKAKQLKELDFRLQQLSSFCEWNKLAFEKLAANMDKHLGTERLVTFYEQKVCKLDFANSSKIYESMIALKALNSSQNDSEVKDKLEKLSIHHPLKKDLLAFIQLDIAAEVVTACINAPDSVLVDILAASIIAGAKACMREVIGRIGLRSECLASALRRAINNLCGPDEGVLYFLEVLKQICSVVYVDSYHSNRLLSRILLVERNSKGQSVMHSVAKLGWAGLCSKFCEIVSSIPDSEPLNWMLPCWRDVMHDTPLTLAIKGNHVEALHALLSAQDKETTSTKPGPVPPLVLTCCVGDYDLIVEELILAGFNPNEVDASSNTALHTAVRYNRPECVKMLLKLGANPSARDFLNSWTPLMLASATGLSEIVSILVASGASVDEVDSSGWTAMEQAVVRGYLHLADKLRTQVALSDKPVNLHTLYIKASSSEMRSRKRAMDLQLSRSVVIIRISDLAGRIRVSLQGDDAVYVSGRSPSFAASRPSSVDFMSQSTDSLSKNDTTASNGSMTPSSSQNNSVIIDIPRSHFDNAGEVCLENLAEPDEIADDSIHLHYDAAQENSPQPVNGSSPPYELVFVTRNTEEATITIDLLANRSHKILGRTVCCLTSLVSDLGNHMQSLKPLAPLPLLSSKTLKPIAHVNADVLISKVTVDDRFSSNDGISTPALSLEAVSNVSRTALEDAERSLHKSATTTSESGKSNGVAVIGHRGLGKNQPDRLSLQLGENTLQSFIKAADLGASYVELDVQMTKDMVPVVYHDFIVNETGTDAQVHSLTLEQFLGASHSPSEEIKDDASDIQQKRRPRAYSSSFTPSGSQVNFGEFAEENARLKPKVYKGNALGHTICAPFTTLKDVLKEVPQSVGLNVEFKYPMLSEAEEEKLLPIAYDYNFYVDTILSIIKKYGGKRKYIFSSFNPDICILLSLKSTNPVLFLTEGGTAYRTDVRAASLRQALKFASQWSFLGIVSACEPLIMCPRLIKAVKQLGLSCYTYGVLNNDVDNVRRQVRFGVDAVIVDNVLAIRRALNQYDESLESD Q9C105 YKT4_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPAPB1E7.04c; CHAIN 20..1236; /note="Chitinase-like protein PB1E7.04c"; /id="PRO_0000314114" CARBOHYD 21; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 24; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 54; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 123; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 225; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 237; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 255; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 267; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 277; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 288; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 309; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 715; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 737; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 768; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 786; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 813; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRLISSLLLLVYSARLALSLNLTNQTAVLGYWGSNLAGKMGDRDQKRLSSYCQNTTYDAIILSSVIDFNVDGWPVYDFSNLCSDSDTFSGSELKKCPQIETDIQVCQENGIKVLLSIGGYNGNFSLNNDDDGTNFAFQVWNIFGSGEDSYRPFGKAVVDGFDLEVNKGTNTAYSAFAKRMLEIYASDPRRKYYISAAPTCMVPDHTLTKAISENSFDFLSIHTFNSSTGEGCSGSRNSTFDAWVEYAEDSAYNTNTSLFYGVVGHQNGSNGFISPKNLTRDLLNYKANSTLFGGVTIWDTSLAAMSYDNSSETFVEAIHKILDTKSKHSSSKSSHDSSQGLESTSSIALNPTSSISSTSSSSSTSSAISTISQDHTKTVTSVSDEPTTITASGATSVTTTTKTDFDTVTTTIVSTSTLISASDSTSIIVSSYVSTVTQPASTRVQTTTVSSISTSVKQPTASVASSSVSVPSSSSVQPQSSTPISSSSSASSPQSTLSTSSEVVSEVSSTLLSGSSAIPSTSSSTPSSSIISSPMTSVLSSSSSIPTSSSSDFSSSITTISSGISSSSIPSTFSSVSSILSSSTSSPSSTSLSISSSSTSSTFSSASTSSPSSISSSISSSSTILSSPTPSTSSLMISSSSIISGSSSILSSSISTIPISSSLSTYSSSVIPSSSTLVSSSSSLIVSSSPVASSSSSPIPSSSSLVSTYSASLSNITHSSLSLTAMSSSSAIPTSVNSSTLITASSSNTLLSSITSSSAIVSSTTVSNISSNLPSATASSQSQLTNSSTLATSLYLSSSSSRTISTSSTNEYNTSFHAPTVSSTTSSSSTTSLAANKGVNSNSITSLNLESTSSVTSTAYTTDSVTSTTALTSQGPSSSVVSSSLSSTTSLSTSIPVTSSVAPAVTSTGSETSSVVGSGTDSATSSSWTAETSSSAITSSVAASVTPTSSSSASSWSSSSEVDPSTAASATGSSTSSIATASVSGSSTSSVATASATDSSTSSIAAASVTGSSTSSVATASVTDSSTSSVATASATDSSTSSIAVASVTGSSTSSVATASATDSSTSSVATASITGSLSSSIATASVTGSPTSSVTAVSSTSSVEGTASSTIAAAASAATLSSDAASGSSTVTSSATASSSSSAATTADSSVTTDTPSNDFNANVDTAGLWYVSALSSYSVPAGFAWTTIDGFSVVMPSANAYKKRSLPIKATANPALNGAGTWKTIHTSATTTAA Q9C106 RPC3_SCHPO SPAPB1E7.03; CHAIN 1..591; /note="DNA-directed RNA polymerase III subunit rpc3"; /id="PRO_0000351041" MSQYAVELCEILVEEFFGDCCSAVASALLRHGRLTIPMLQKRTSLPGPKIRQALVSLMQHHMVLYVTVIENVREVTYYETQWKEIYNILRKGKDVYLISQKLNQEAASVVKYLSTQGRARVLEVFNAFDKKVDGSDEESRMMQKNLTELIYQKFLLVVQPRHLIPVGDQEMQLRIKHLDRRKSENVSEIKKNREVDDSVALEMLELRAADMSELQGLTRKPKESIPHPTKRRKRAVGSAPSVSTDLNNILDDDNSILVPDLSAHVRINSGKLSVLSKNARLTHWVERRIGKSTSLVYSHVLSMLEPRLFSISNQSPVFTLTTMELTRNFPNDIDVESSIVDKQYSVNSASNELRVMEKLNELDELAEEDNYEESVDENANRKSKVLAQHLELLADCSLKFISKIGNRGMGEWAVNFTHLTDMLRAIEYENFIEQKFGERAIRLLRIIKDKGKIEEKQLANIALLRQRDLRTVLQAMAEIGALELQEVPRSSDRAPSKTFFLWFHRPDRAYSLLLDELYHVIARLYMRLRDARAQRAQLIEKAERIDIKGNEEQYLQKFEQAELKKLYSYEEKLLLQASRLDDMVLVFRDNL Q9C1W5 TIM16_SCHPO SPBC713.10; CHAIN 1..128; /note="Mitochondrial import inner membrane translocase subunit tim16"; /id="PRO_0000214096" MSLPRAVGRFIIVGSQVMSKAFVQAYKQMIANAAQQSTGQAAASKSSTAVRRGEMTIQEAGSILNIKPESLEEGELEKRFQKMFEINDPKKGGSFYLQSKVFRAHEKLKSELDQKIQEQSPAKPTSSP Q9C1W7 MIM1_SCHPO SPBC713.08; CHAIN 1..71; /note="Mitochondrial import protein 1"; /id="PRO_0000218766" MEKNTVTVPKTLFSQVIHIFKYAAINLGLPFLNGVMLGFGEIFAHAFIHSLGWAPGHTRIYSIQRHQYIQA Q9C1W9 DNLI3_SCHPO ACT_SITE 433; /note="N6-AMP-lysine intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; SPBC713.06; CHAIN 1..774; /note="DNA ligase 3"; /id="PRO_0000372334" MPPKKRMKNGSSLKSTSKKGEKSRNIITIQDLFSKREAQLTDTPNKLLTDHDQSASDYAYALKLQQLFDSENQATAPEKLPKDVIIPEEEYHTDTFNVVKESNDKPKENLVTSEECKASFFSTDSVNKDSTIDYDALQKDPLTYVKSCRARFVSKDTKSFSYSSLANTFSLISSTKSRIRIVTLLTNFLLTLLYADPDSLIATVWLCTNSIAPNFYGKNLGVGPAMYSKALKEVCGITASALKNLWNKYGDPGDVAFEAKVSVRTLSRPEPLTIKKVYSTLLKIADSNGNGAQNRKLELTKFLLISSNAEEVRYIGRSIMQNLRIGAVQNTMLASLSKAFFIFDNQNEIFNFNSDSLQQQFRQGEEIVKQSFFQVPDYNILVATLLREGIENLKDNMSIRPGIPVKPMLGSITKNLQHMLERLTDHNFSCEFKYDGQRAQIHCDRLGNIKIFSRHLEEITGRFPDVIEVAQLALKHSCDFIIEGELVAIDKSNGQILDFQKLSTRERKKVTVADITIDVCVFVFDIMFCDGKSCLQMPLIERRRMFFEHFNLIPNRFQFVSSLETNEEQSIQEFFSLAITNKCEGLMVKVLNGTNSKFPSTYEPDKRGEGWIKVKQDYDDEFESLDLVPIGAWYGNGRKAGWFSPILLAVYNPDTGAYEAVCKCMSGFSDQFYKELTQKYSLESGNSSLKPIYNFCETGKVTPQIYFAPQEVWEIKGAQITSSPAYKAALGLIQDDRGLSIRFPRFIRVRSDKGPEDASTNSILADMYMKQLNT Q9C1X0 YN55_SCHPO SPBC713.05; CHAIN 1..297; /note="Uncharacterized WD repeat-containing protein C713.05"; /id="PRO_0000316566" MRLEAKTKLSSKAKEPINVVKYNRTGKYVLAAGNERVVRLWNVKSGACIHEYAGHGHEILDLDLVYDSTKFASCGGDKFIQVWDVNTGKVDRRLGGHLAQINTIRYNEDSSILASGSFDSKVRLWDCRSNSFSPIQVLADAKDSVSSIDIAEHLIVTGSTDGTLRTYDIRKGTLSSDYFSHPITSVKTSKSASFSLISSLNSSIHLLDQETGKILKSYIGLKNMEYRVRSSFNQSETIVFSGSEDGKVYLWDLENETQITSTSVVGTPIVTDISCHPTMDDFIIATVHGDLFIYQYN Q9C1X1 PWP2_SCHPO MOD_RES 640; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 645; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC713.04c; CHAIN 1..854; /note="Periodic tryptophan protein 2 homolog"; /id="PRO_0000051178" MKTEFGFSNLVGTIFSKGNLVFTPDGFSILSPVGNRVSVYNLKDNTSYTFPFENHKNISHIALSPTSTLLLSVDEEGRCILCNFLRRSVLHYFNFKSPVGAIEFSPNGKFFAVSLGKLIQVWRTPNSLEEREFAPFVLHREYTGHFDDIVSISWSADSRFFISTSKDLTARLHSVDPIEGFHPCALTGHKNTVVSGFFSKDQQTIYTVSKDGALFVWKYSPLFQAGEVIDEEAEENKTRTHIWLIKERHYFNQNSKLRCAAFHPTSNLLVVGFSSGLFGIYELPSFTMLYQLSITQSNIDTLTVNSTGDWIAIGSSKLGQLLVWEWQSESYVLKQQSHYDALSTLQYSSDGQRIITGADDGKIKVWDMNSGFCIVTFTQHTSAVSGLCFSKRGNVLFSSSLDGSVRAWDLIRYRNFRTFTAPSRVQFSCIAVDPSGEIVCAGSQDSFEIFMWSVQTGQLLETLAGHEGPVSSLSFNSSGSLLASGSWDKTVRIWDIFSRSGIVEPLPIPSDVLSLAFHPDGKEVCVASLDGQLTFWNVQEGKQTSLIDGRKDLSGGRRFDDARTAENSSLNKTFTSICYSADGSCVLSAGTSKYVCLYDIITGVLIKKFQLSKNESLQGVQEMLNSRKMTEAGSIELIDTQGEESDLEDRIDRTLPGARRGDLSARKTRPEIICHGVQFSPSGGAFAAATTEGLMIYSLYNDFLFDPINLDMDITPSTTLTMCAEGEFLISLVMALRLNEYKVVQKVYESIPITDVEHVVQELPVSYLANFMGYLSSFAAETPHIEFHLRWMKSVLTYHGEYLRRKNFEFASQLTSLQKSIVVLSKRLSQLSSNNEFQLSFLLDKMHLRLENTA Q9C1X2 YN53_SCHPO CATALYTIC ACTIVITY: Reaction=(R)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + pyruvate; Xref=Rhea:RHEA:13521, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.4; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC713.03; CHAIN ?..526; /note="Putative D-lactate dehydrogenase C713.03, mitochondrial"; /id="PRO_0000317236" MHSLQCRRVIPFGKLSLSLHAPRNALRFVHKPAFTFESYKSLHRDPKYAKLSEQDVQVFKSIIGKDGSLIDGLDKSTDPADLDAFNIDWMNKYRGKTQLALKPKTTQQVSEILKYCNQKKLAVVPQGGNTGLVGGSVPVFDEIVLNLGLMNQIHTFDEISGVITLDSGVILENADNFLAEKGYMFPLDLGAKGSCQVGGCAATAAGGLRLLRYGSLHGSILGMEAVLPDGTILDNLVTLRKDNTGLDIKQLFIGSEGYLGVITKLSVICPKRPSSTNVAFFGVPSYENVLKAFSETRSHLTEILSAFELMDNTSQTLVDKYSGTQRPLEDEHPFYVLVETQGSNKEHDEQKITALVEDLLEKEIISDGVLAQDESQLRVLWERREGITECLAKAGSGVYKYDVSLPLPVLYDLVNDTKKRLIEFNLLDDTPEHPVIDVVGFGHMGDGNLHLNIAVRQFDKRVEKCLEPWVYEWVSRHRGSISAEHGLGLLKKPFVGYSKSKEMIHLMKTLKNVFDPNGIMLPYKYV Q9C1X5 YKW2_SCHPO ACT_SITE 55; /note="Proton donor"; /evidence="ECO:0000250" SPAP32A8.02; CHAIN 1..283; /note="Uncharacterized oxidoreductase P32A8.02"; /id="PRO_0000310314" MSESQTESTTVTLTNGMVIPRIGFGAFMLKYNECYGLVTQALDSGYRHIDTAAVYGNEDICGKAIVDWCEKNNVKRTDIFLTSKLANCSDYYSTRAAIRSSLHHLGTYIDLFLIQSPAGGKKSRIASWKAMEEFVDSGDIRSVGVSNYGVKHLQELYASNPKFYPCVNQIELHPFLSQDDIVKYCQSHDIAIEAYSPLTHGIRLNDEKLVPIAKKLNISVAQLLIRWSLQKGYIPIIKSTKKEHMLSDLDVFNFTIPDDVVQELSSFDEHWHAGTTYDPTVCD Q9C469 GRT1_SCHPO SPBPB8B6.04c; CHAIN 1..648; /note="Zinc finger protein grt1"; /id="PRO_0000114952" MVLSKRPVRISKACENCRKRKVKCSGGDVCFECQKYNENCVYRQFYRKIKRLKYNNDNSKIDNFSNEQMNIPEFISVRNLNDDSSSIEFFGPASNISFVNQLNHYLRKAERNGYDFLSEGQNDITPEEERKGLEKFGMKLMVLKDNANNFDFSLSNITTEKMNGLLIAYLETWHIPCPIFKAEDLFNLSVRTWKNPSASVHDKALLYLILSIGSAASYFDLQSNSSTLPLARGFFNLALRTVPHIFTELSLDAIRIVFFMSVSAGNLGDTALSYLYSGTAVRMSLAIGLHKCKNFSNDLSDKYQNIRLWVSVWQWEGYWSFCVGRPSCSRQDIPIPAVPNEAFSFSGYGEHGRFLINHEHMRLRVFFSSCCSKIQSEIYSTNRNLLSVLQTVEQISKEVDKEYFSSTNHQLIRSEIGEYCKTLDINSCREWFWIRIYYLYLKLMIFRPFLIFLAYVNISKTSAPDDIIEGLKRGSDQCVQEAIDISKFIVQLNRKVRMLQPIFFICTYLESACTVLLFYIASNSAKIQGQLATEIWAVLRDTCSFLQGSSGPYVGSVSTIAKDALESLNNILVSKKYQDNSVNNTYFDKVMQHVLVHSPAFDDSSDPKFETNRSETPTQYTLDDSANDELMIPDLQGFWEQTLDWINN Q9HDU2 GAL1_SCHPO ACT_SITE 209; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q9HHB6" BINDING 47; /ligand="alpha-D-galactose"; /ligand_id="ChEBI:CHEBI:28061"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 53; /ligand="alpha-D-galactose"; /ligand_id="ChEBI:CHEBI:28061"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 54; /ligand="alpha-D-galactose"; /ligand_id="ChEBI:CHEBI:28061"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 56; /ligand="alpha-D-galactose"; /ligand_id="ChEBI:CHEBI:28061"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 159; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 161; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 163; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 164; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 209; /ligand="alpha-D-galactose"; /ligand_id="ChEBI:CHEBI:28061"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 257; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 258; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P04385"; BINDING 266; /ligand="alpha-D-galactose"; /ligand_id="ChEBI:CHEBI:28061"; /evidence="ECO:0000250|UniProtKB:P04385" CATALYTIC ACTIVITY: Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061, ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6; Evidence={ECO:0000250|UniProtKB:P04385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13554; Evidence={ECO:0000250|UniProtKB:P04385}; SPBPB2B2.13; CHAIN 1..519; /note="Galactokinase"; /id="PRO_0000184656" MATVPTYHDLSFYSNPKENKARYAKLLNSFEQKYHCKPDFFSRSPGRVNIIGEHIDYNYFSVLPMAIDVDVIVSVTTSDDAKVELNNTNPEFKEEILELPSDGAVIEINKTHHTWGNYFRCSMIVAHKYILEKYPELVSGGKKPLKGLKLIFDGNVPTGGGLSSSAAFCVASILAILKANGINTITKEDLVKISVVSEHYVGVNTGGMDQCASIYGEQNKALLVQFKPKLMATPFKMPVLKPHDMVFLISNTLVEANKQETALTNYNLRVVEMAVASEFLAKKFNLELPKESNLHTGTLRGFMDEYYEKHLKQPHWDGSDIDMGVQRMQEMLRLTEIMFSEEQKVGFKTEELAKELGLSVEEFTKVFLTKIPVKYERMKIYQRTVHVYSDAMRVLQVLKLFHQHKDSDDPQKFMLAFGRLLNDSQRSEDIYNNSSSPELREVCKISLANGGYGARTTGAGWGGSAVHLTTHDKLAKLVEALTEQYYKKQFPKITQSELNAAVVVSKPAAGSCIVQLAEY Q9HDU6 PANE_SCHPO ACT_SITE 213; /note="Proton donor"; /evidence="ECO:0000250" BINDING 9..14; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 115; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 115; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 217; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 221; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 295; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 307; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH; Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.169; SPBPB2B2.09c; CHAIN 1..350; /note="Probable 2-dehydropantoate 2-reductase"; /id="PRO_0000157327" MNNTIYILGAGSIGSLLAYELASLKSINNRVILLLRDKSRVNSFKDKNSTLKIDRLFEENVPHLCCQVTASEPSQLNVQSIENMIVTTKAGQTENALSKYLPYLSKNSNILFVQNGMGAVENVCGKLWPEEQNKPSIYQGVISHGCFQTAPFHFSHAGLGDLKISKVPKNPKKILPDEAAETPCEMIKSLGKSELLRLRYMNYPELLVNQCEKLVINACINPTTATLDCVNGELYNDESAKELFRCIIKECVDIFFKCIPLFKNNEEAEKILNVNRLLDRVMFVGTKVNGANSSSTRQDCLLLRETEIDAINGYVVKLAENNGFQATVNKTMMLLTKSRLGLNRCRAHAR Q9HDV9 GCSH_SCHPO COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 101; /note="N6-lipoyllysine"; /evidence="ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU01066"; MOD_RES 131; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP19A11.01; CHAIN ?..169; /note="Putative glycine cleavage system H protein, mitochondrial"; /id="PRO_0000316230" MLARSALRSGFLPSLTSSVKTGFCLKAAAPTLSMKWSAVKYYSTKHFTKEHEWVKVDGDVGTVGITSYAANALGEVVFVELPEPETTVSVGDGIGAVESVKSASDVYSPVSGTVTSINESLGDSPDKVSSSPEEEGWICKIKLSSPDELKSLLNDESYAQFCKEEDASH Q9HDW0 TOC1_SCHPO MOD_RES 204; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 399; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP18G5.03; CHAIN 1..430; /note="Target of rapamycin complex 1 subunit toc1"; /id="PRO_0000304016" MQLQSPFGDGISCECLNIRVLGIPNETKHQWIFVPRDLIKIKIYSLLQICKAENCSAVACRGCNLCILAVQGNIEISEEPQKLFQEENVKVYIYDSAISLSSVRASFPISELGIRMDIIKARAEPREDEIRASFSSLVNKEIKRTVEELLLSKRSTNRLSLLAFMRNQQLNYEAYETKLLEDASTIEKSLEKEVKTIYDSNIASPKESSDAIDADHAMIDESRSTQRRKSKPKKHVAFTDEYQVAFSDKPGKYFNQPMQYSKQFKLDNPDYEASSDSLNDIENLSTLTFRSDEELEFDFDTNNINNNKSGDSLEMSTTIPSDEENEDFTSKVDAMEIHSGSLPLNIDSSPIFTNHSPSSSLSSESSFEASPSSFVDRKNRWIQMLKKADEHSRSIQARSMGYVLSDDLDNSKAFRPYKQSFLAQGWKSLN Q9HDW3 TFB5_SCHPO SPBC32F12.15; CHAIN 1..68; /note="General transcription and DNA repair factor IIH subunit tfb5"; /id="PRO_0000119284" MPRAQKGLLLVECDPTVKQLILNMDEQSPGIVIEEIDEERLLVNESRLEQVKAELERRLEENTYQVEE Q9HDW6 VATC_SCHPO MOD_RES 17; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB2B4.05; CHAIN 1..394; /note="V-type proton ATPase subunit C"; /id="PRO_0000209357" MSKSDFWILSVPSRGGSNADLCDDIERLLVSGSTSLISTVAPFDVPPFKVESLDVLISQSEQLTKQDAQCASAISKISDIIKNTVSSSSGDLKDYFMVQDKSPLEYVSSFAWNSSRFHMNKTISEISDRITSEIISFENDIRTRQTSFQQASSAFQNMQKKQSGNLSQKSLANIVHEEDVVHGSDYLTNVFIAVPLNLEKQFLNSYETLTDLVIPRSAKKLDQDSEFVLYTVVVFKKTADSFITKAREAKYTIREFTFEQGLRETEQSEFDDAAVKEKRMLSSLLRYASIAFSESFQGWIHLKCLCVYVESILRYGLPPDFSSVIFQPMAKSEVKIKNILLSKYAYLAQNPVGNNKVKNVDSSAGLDESMADLNLDEEYLPFVLFTVPSKVFNY Q9HDW9 GPI12_SCHPO CATALYTIC ACTIVITY: Reaction=a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol; Xref=Rhea:RHEA:11660, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57265, ChEBI:CHEBI:57997; EC=3.5.1.89; SPAPB2B4.01c; CHAIN 1..248; /note="Probable N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase"; /id="PRO_0000207169" MIWFWSTLLVTAIAVLSTANESSSGQEKLAVESILFVFAHPDDESMFFGPTIDYLGNQHSTRVHVLCLSNGNADGLGSVREKELVVAASKYQIDKTNVHVVSDPQLQDGMQAKWDPTDVAKHISQIIERYNIKTLITFDNKGISGHPNHIACYEGAMKIVKATPQVQVFVLESVNIFRKYISYLDTIPTLVQSQAGRNDTIIIHADRKSTQRIRDAMVRGHKSQMVWFRYGWIYLSKYMSNNVLKRAT Q9HDX4 MFC1_SCHPO SPAPB1A11.01; CHAIN 1..495; /note="Uncharacterized transporter mfc1"; /id="PRO_0000173447" MSVSDKDFKDIELLPVKSIESKDSIDQCDPLTWPIRIRIINTIIISFMTMLCMYGSSVFMPSIPELCEKFGEPETLVVLGATLYVIGVMLGPLIFSPLSELYGRRPLNIFGYTLFALMQIPTALSVNLAMFVVFRFFSGFFGSVGLGIGAGSLSDMFSKRDRGKYIGIYFLGICLGPAIAPIASGFIAGSSISWRWEFWILLMLSGVSLLAGVVFLKETYAPVLKRKQAKKLLEKQENQKSVEVKISEITESSQQIDPDKSFAEVVHILVTTIRRPLHLLCTQPIMILISLIVGTVYGILYLLFTAFAEVWISQYHFTSGLSGLTYISLSIGQVFAVFVLLPLNQKYWLSAVQKNNGVPEPEFRLPMAFLGCFAIMTGMFIFGWTVQYKVFWFVPLIGTTLVGAGFVMTFNPMNMFIVDNYGRYAASAMAAIAIPRNIFGACFPLFAEKLFERLGYGWGSSLLAFLLVAINFSIAALYMFGKTIREKRPFDHTKY Q9HDX8 ALO_SCHPO CATALYTIC ACTIVITY: Reaction=D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H(+) + H2O2; Xref=Rhea:RHEA:23756, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16292, ChEBI:CHEBI:58277; EC=1.1.3.37; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; MOD_RES 61; /note="Pros-8alpha-FAD histidine"; /evidence="ECO:0000250" SPAPB1A10.12c; CHAIN 1..461; /note="D-arabinono-1,4-lactone oxidase"; /id="PRO_0000128169" MSIPHINKLSQDGRVRFSNWAKTFSAISLGLRCPKTEEQLREILVDANSNGKKIRVVGAGHSPSDIVCTSGYLLSLDKMNKVVSFDPDSLSITVQAGIRFYQVQEILQNLGYSLPIVGSISETSVSGIMSTCTHGSSLQHQVLPHYIKSMRIMLADGSIVTCSRELQKDMFAAAQVSLGALGVIVDITISVVPAFDLVATEDVTTVTDLFQDWKNNLIWESAEFVRVHVFPYANRAVVWRANKVEPNTVPHTPKPSLFRLKLDSFVYQCLLFVGKCVNRVTPYLERFWFKCHYGSKLGTALQVAGPGFDVLQMFCYFSQHVSEWGIPLESAPDALEKLINYTVDDAGKIGAYTHWPIEVRVCAPTPEDECWLSTDCKVPTCYIEAIMYRPFSTSINYKPYFKALEDIANQYNGKPHWAKEYSLTKEQLLERYPNLSKWLSLRKLLDPKGVFWNDYLQRHLG Q9HDX9 SYEM_SCHPO BINDING 37..39; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 47; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 73; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 222..226; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 240; /ligand="L-glutamate"; /ligand_id="ChEBI:CHEBI:29985"; /evidence="ECO:0000250"; BINDING 243; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 278..282; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; EC=6.1.1.17; TRANSIT 1..38; /note="Mitochondrion"; /evidence="ECO:0000255" SPAPB1A10.11c; CHAIN 39..526; /note="Glutamate--tRNA ligase, mitochondrial"; /id="PRO_0000314764" MLSYTSCAKLICSRYIVSKISFYSLKRCNSTAVVRTRFAPSPTGFLHLGSLRTALFNYLWAKKSNGKFILRLEDTDQKRKVTGSDLEIYKVLKQFNLQWDEGPIVGGPYGPYEQSSRLQIYQKYAQHLIETGRAYVSYSVPIATTKIDSSTKYHEISIDDLTDAQRKLYKSKKFPYVVRFRMKEPSPFTDLVYGKIAIKSDSREIEESNNFVILKSDGFPTYHFANVVDDHLMHITHVIRGEEWVPSTIKHIQLYEAFGWKPPKFAHLPLLVNPDGSKLSKRQNDAHVSSLLQEGFLPEAILNFIALMGWSSRQKSDFLPMKELIDLFSIDKLTKSSSIVAFEKLYFLNKNYLRRAISDVNRLDELIELVQPRLIQKFSHSSRSHDKSYTKKLLLLLKNKVHTIKEFEKIVFYFYEASDLQQIRSLVSSLITVEELPKILTTILNKFETIEWNTHEIQISLKEIAMEHQMPLKKIQSLLRYGLCGNLPGGGISDTISLLGKETVKSRLERLLLSLKHELPKRSCIV Q9HDY4 YK16_SCHPO BINDING 421..428; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAPB1A10.06c; CHAIN 1..1183; /note="Putative ATP-dependent RNA helicase PB1A10.06c"; /id="PRO_0000055192" MGRLRKRFNEKGRQSGIQKMLNLKRARLHRSVREQESSSEVHANPEPDNQDSNAEILIDVPKEERQKRKQELKDQLLKENEGSISSKKKKRLDKYIENKLKKEEVASLIAKLAEERIDTSLLSSSKNLGKQATAKEKLKKSLLEEKLGLPLSDADSRLYKVVDVETTTTKSSTAETNAPEKYSTRSGFGFGFSTGTNESEITPNIKVLPPKKKKNASWGKMLNEDPEYDSAEEDYLSTDSEEFSEDSDNSSEENKDTNEPSTKDAEKTVPEDVVNLRSEQKLQPSFGHPEFENEDFDLETSEDDSSDDATERASRFKSWANKQILGADVGEKSHDVAPDNKIDNPDADMVRAQRMPRKLKMREEDVEPTADDIEIKGRKTTYTIINRPPEIQESRLALPIVAEEQRIMEQIFANDVVIICGATGSGKTTQLPQFLFEAGFSSPESENPGMIAITQPRRVAAVSIAKRVSEELTGFSSKVSYQIRFDSTINPDTAIKFMTDGILLRELSSDFLLTAYSAVIVDEAHERSVNTDILLGLLSRIVRLRREMSKSDQKVKPLKLIIMSATLRVTDFSENKLLFSVPPPIIKIDARQYPVSIHFNRTTKPDYLQDAFDKVCLIHKRLPAGSILVFLTGQQEVEQLCQMLRKRFVRSFRPLKSRARIVVSRKTMSVENEDLQSETEDIDQVPTSSSSSVTYDDESEPMYVLPLYSLLTTEDQMKVFDSSPEGHRMCIVATNVAETSITIPNIRYVVDCGKAKERVYNEKTSVQKFEVRWISKANADQRAGRAGRTGPGHCYRLYSSAVFDSSFPLHSLPEILRTPVESIVLQMKNMNIDNIANFPFPTSPGRSRLEKSLKLLSNLGAIDSEGVLTKLGEQMSLFPLSPRFSKMLIIGQQHGCLPYVIALVSALSINQLFVSKQSLLYDAHDKNSRSEETDLIDDDEIKQKEEYKNRMRGYFNAISRFQAIDPDAPALSLLSAVCAYDYASDKRKFCKENYLREKALEEVTNLRKQIIGLLKRYMVRVEKEFFKLQLKPPTSVQIKALRQFIASAYIDQVALYDKEKRGYVTLFPSGSEVVQFVPDRTYNIDSEYVVYLSLHESRSGRVYMSPLTEISPEHLARLAKNTTLLSYSKPLSYPPIRYLDNATKRECWVIPILSANIGTGSPSWNLPAVQIIQKRINGRWVNC Q9HDY7 SCM3_SCHPO SPAPB1A10.02; CHAIN 1..336; /note="CENP-A histone chaperone scm3"; /id="PRO_0000350767" MCNRQPKAVDLPPNYSCPHLLSFQSVEFNTNPTACDDVFCKRIESEKKYNDFLESLFKKYGRDTSDIADEVDLATGEIIVNNGHLEALKTKDDIWDPTFNNLEISASNGYEKKLDSSIGNPGEKAVSPVHIEDFQSPQIYKFKNLSLRDEMVSDCVFADEVPLASLFVENVCNETIPSQSCVRLKINDKTRKVDASALEKKSCLLPNSSGTLTDQRGLDTIKHKSIEQNEILHVISDTLSSPRRRNPLLSSPKTPLRRSFSKSKVRNSNSTKRRNFISLISMISPRPNLSTHHFNLGFQPLSQQTSFSGSSTQNPHSSSTCKKAFCFQCISESKKC Q9HDY9 MAM3_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPAP11E10.02c; CHAIN 19..1082; /note="M cell-type agglutination protein mam3"; /id="PRO_0000014210" CARBOHYD 28; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 56; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 82; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 451; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 475; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 495; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 520; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 548; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 588; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 613; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 638; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSIALAFFILVLLGFSWASPSALDDTFNVSRSVGLISSSNLESCQSSPLEVGNIYNSTSASEILSTLDAKYITIIGVIGSSNSSIQDLIDSVGNSNNAASSNPTSTVTEYVDRVQTVTEYVTLSCGQAFTSTVDISSSTSSSVINSPTGTAVSSQISTLSMSPSSTPVFSPSASVSSKVASSVSYVSSEPSDSSSSTNTVILTTSVNSPAVSSSETLTSVSITSTESAYTSSSVDIAASTTASSTLPVSTSEATVSFSTDIPATPSTLSSPASSSSSYLVETSSTLTDSVFTTVTATSDSSVITYTLINSVTSSSETTNLPSSSSSLVTIGESSFPSSLLSLLTQSFSTVRSTSSSSTDQLTSASPISSSVISPSVSSPTSSILTNSGSIKSGDHQIVTTSFVQTTTHGSQVETLTYVTTLTETILTTTYDSHTFLTTITPSPSNSISYTNNTFIPSSSIKSSIVYSVTPTSAENYTSSEAFSTSSSLVVIPPVNSSLVTSSTSFTKFSSLSSSQLSTENFTSASSSLSLTNAKSSLSTPSTTIPTSNSSVSLQTSSSLIISSPIISSSLTATSTSTPALTHSITPSNTSYTSSLIPSSSTDYSSSLITVCSNVTSEISSTSLASLISTLTSQQISSNKSSEFVGQTTTEYTTSGSVGFTTTLATQSGSVPGTVLVDVPTPSWITETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSIGFTTTIATPIGSTAGTVLVDVPTPSWVTETVTSGSVGFTTTIATPIGSTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVVVDVPTPSWVTETVTSGSVGFTTTIATPIGSTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPQQHATTTTTTTFDGFSGYTSSYTGSITETIVIGTPHHSVVDVS Q9HDZ2 CWH43_SCHPO ACT_SITE 826; /evidence="ECO:0000250" SPAC589.12; CHAIN 1..971; /note="Protein cwh43"; /id="PRO_0000116831" MTEKTSSLVFSAQYVALVHTICSFAAFFIPLALALYTHYYQVVKNEFYGYPEEWFPSVSATIGDWYPERSVFQWLIALTATPRLLVLLLWFTLSGISRPSVIITTALGVLRTALCGGWVYVTSTDDHDWHDIFMIGYLISNAPWFILVSKCSPVNSMASRIRNIGSALFVLTIFPLIYWYIQHKFKHIPGAYTVYAFFEWSLILWDILFDSALYWDFKPLVFNLHTSKTYSNPSSFATRKKEKGEHLSYAEAAAVGTQAKNIKKDSNVKCSKKQILFSLLYFSSEVYLSFVFWSVLTSLGLLVWYFPLWHMGISGYEACILFELSPFLLGIPLLRKFASKVPVIFLFLNVIGIAAYKLEDPVHRLFVTAFSVCCECLAWTSLFSNISPENLAIERKISTFLFGLLASSIAKYSFFSNNPIWPILNETNGGKQIPALIVGIIACLIFAIFHVQQTTANAVEHFKLRKITALSAALSLGTVLFCLHTFLCDSTVLMTWSWDGYPIKGPQPYPHGAVSIVVSICAVLVAPYLYQSGAFMLIGFVLACFGSYFMYINHGWCSYLGGLIFTSYVLIYSFASIRISSFYSPAKVWGGAFLVYILYSLAHVWVVAYEFVPGGPILRERTSYILIFIGWNLAALVPAYSGESKEPNKADSSVVDIKQSDSSYRRRSFKKSLLTGFCLALMALKFAIQNMPPYDYTPYHPNEKLFTAGIWTIHFGLDNFMYASENRIRDAVRDMELDVFGLLESDTQRLIMGFRDLTQVLAHDLGMYADYGPGPDKHTWGAALLSKFPIVNSTHHLLPSPQGELAPAIHATLDVYGELIDVVVSHNGQYESQLDRRLQSTELARIMRESPRPLVFLGYVVSNVGQEPQTILTRDTGMLDIEPADYDRWCQYIFYRGVKRIGYARLHRSTITDTELQTGKFLVTKDLGRNVRIDKEHVPESHRYPSLFEGTGVNGHYYDNNLVVHEPWYYD Q9HDZ3 MUG82_SCHPO SPAC589.11; CHAIN 1..182; /note="Meiotically up-regulated gene 82 protein"; /id="PRO_0000278567" MFANFRNCFKIKNSRLIYDNINKCLLTKEETNQLLKFIHLKWKPAKDQVQISFSRSSGPGGQNVNKLNTKVIVNLPFKQLESCIPMFLINHFKTCEMLRNYRIQNGIKIYSQKTRSQHKNIEDALNKISDLLNKSAETLYVPDTPPEKIARISILKKESNEKRLSEKKYKQKKKTQRRITMD Q9HDZ8 YKP6_SCHPO MOD_RES 185; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 201; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC589.06c; CHAIN 1..202; /note="Uncharacterized protein C589.06c"; /id="PRO_0000372627" MNAQVLNLVAALGVMQYSKKLDFTDPQIVYYARAAYVISNTIIFGVYAIIQARINANNDETPLVYEEPAPPFSGQSNGKLVTTTVKEYDSEQLQKAKRSTMMGVAIMAFMHLYMGYAQPLVIQSILPLISLFTNNLVSIYIFNKAAEGSLSRPFAPPAGLFGGGNKPAAAVTGTSSNSNNASAKSDGPTITELNENETEKSS Q9HDZ9 QNG1_SCHPO ACT_SITE 245; /note="Nucleophile or transition state stabilizer"; /evidence="ECO:0000250|UniProtKB:D1C7A6" BINDING 49; /ligand="queuine"; /ligand_id="ChEBI:CHEBI:17433"; /evidence="ECO:0000250|UniProtKB:Q5T6V5"; BINDING 243; /ligand="queuine"; /ligand_id="ChEBI:CHEBI:17433"; /evidence="ECO:0000250|UniProtKB:Q5T6V5"; BINDING 245; /ligand="queuine"; /ligand_id="ChEBI:CHEBI:17433"; /evidence="ECO:0000250|UniProtKB:Q5T6V5"; BINDING 310; /ligand="queuine"; /ligand_id="ChEBI:CHEBI:17433"; /evidence="ECO:0000250|UniProtKB:Q5T6V5"; BINDING 315; /ligand="queuine"; /ligand_id="ChEBI:CHEBI:17433"; /evidence="ECO:0000250|UniProtKB:Q5T6V5" CATALYTIC ACTIVITY: Reaction=H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + queuine; Xref=Rhea:RHEA:75387, ChEBI:CHEBI:15377, ChEBI:CHEBI:17433, ChEBI:CHEBI:78346, ChEBI:CHEBI:194371; Evidence={ECO:0000250|UniProtKB:Q5T6V5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75388; Evidence={ECO:0000250|UniProtKB:Q5T6V5}; SPAC589.05c; CHAIN 1..346; /note="Queuosine 5'-phosphate N-glycosylase/hydrolase"; /id="PRO_0000327925" MSRVLQDAEFISLNSNDVKVNKGGCAAVATWIKEKLDSLGPQFAEWQNHELHPKTRDVSTLDWIFLVDILNFSFWSDVDVEDSGKHSKRFSIEYKGKLYTGYWSLCAAINKALDAGIPITSPAFYADEKQCPDTLIASVFDSATVEKIPLLEERIRIMRASGRVLVDSYHGSYCGLLKKCHNQAQRLIKLLLADFPDFRDVSVYKGRECYMLKRAQILVAETWACFQGQNYGRFDDIDSITMFADYRVPQILWQLGCLSYSSDFKKRLLKNELIAHNDPMEIEMRGCSIWAVEKILQNINRKDVNAITIDFFLWDLAKEWQAKGYKPSTQVDEVTIPCIRVRSIYY Q9HE02 SSN2_SCHPO SPAC589.02c; CHAIN 1..1225; /note="Mediator of RNA polymerase II transcription subunit 13"; /id="PRO_0000072184" MSYQVCFKKYVKMRQWPHVLSLRVYASYFLLYNNLPLSSAMVHDGVHLISIKTILTDQPCPNTIYYAKYQVQRKDNEDAASLLEDKEAYLRNQDCIVHAKNDLLFVYDFQAIPSIPEESSSFMLLNSGAFSRLALFQKDELALLLDLYINFLQGLKKTVLYWLCKEYNFVPIYGVLLPLKLHPSFDTQLWNIYGYPVVDLQLSVLSKGHIEFYLKPTRQTVYRLSEVDNLVKKLDTVIRLAPTGCLATLTSVHANASAQTVDALKHRYGFSLTTTSKWVGVTLESSALEFSWPLELCFLETSALRMNDDSLSSNLTDLNNLVLPSNVVNNKKELTEFANEEAEASDKRKEGFTEKEETADAVVTLVPSHSSSPVNYSINSAKSTPASIKVNEEILVADHNVSDDILMEEIDDVGITEADFDYFDLPNVEEKVEMIEPNFANTMTTLDNEEINTSISQSNTSPNLNTHENIPKQMEIQSDDRMVTEDLNPYNVEVDIPEISLNISDSKIPTSAYMPSYYSAVIFPSSISSIFQKYNYGGKYWCPSPSLSTEDLFESFSVAESVTSTDEDICSTNFIQQDFTMEYNHDFFSSSKTPTNISEQSNPDSNYDTLSLAHQVLMNESKSANFDFSFLKSLDLQPTITLGKNDLLNAILSQNLWFRSLPFWKSMTTSFMMSQDVLNFSSYMRKPIRDYLEKILLGESSAVFLSKSPENYLSSINNGHHALNDNPPSQVNFSETLVNFSQPPRVLLKYNEKKLSLDSSAPENWISLCLQPYGESKDFEVFLLSSKSPDVSSKAISFFYDVQLAYENCKLGKLNLSETSINERVMGFSTNINETDNYDDNETTQSDTATSYEQLASVCVNELSGKNVLFFYFLEDDSEKLLKACQHFICVKDSIKRLGDNKFEDKSLRICTIPNSIFDSPNSHTTNSNSFFTKVSLDIYNNDPLLMDGSLKRREPAFLLKKPLLSTLNYQLKDINPRSSALGEYALHVTYTTVEEHLLICNWNDSYGEFETERRYFLQDLEIEDALQQILEVTFTFLNSMHMDWIVIVMKIGEMSDAEYLFWDQAIIPENLQGNVSLTVGYCSAEHGPGSTSKVFSRIPYSASSTVIRNNSSHELSLVAFIREMAMPVPNDEFKKISTILARGYLALDEDESYLPLLSIHLLISRNHDPYLMLNLILKHYLSMIYLQFRTYVSFSSLPLHISTVLYQKQLLQFMASDITHPVTS Q9HE05 UFD2_SCHPO SPAC20H4.10; CHAIN 1..1010; /note="Ubiquitin conjugation factor E4"; /id="PRO_0000194996" MSDLEKIRLKRLAKLQQTNSEANSSKEPKESNIAPEPKKPDLKKRFIGSKATTSNSEQKEISPPVTSGAPKHRLFSKDEWMHFITCQALNITLSETDSSKYYLEGFKKDLEEEGSPLLFNENNVDSALLSRLSTTGNNTFSYLLQSWSFLYQYKKRLPKDENQDFKIHYLSLLKSLLVSYAGIVVMLPDTFNSETIDLAEVLIGAEGIPLEFLSEFVQRFEHENLDELFIPVLESLSLKIGLMNVDTVQMNVMQIILQLVSLKPIALLLPKLPSWNPTNNAGEIEYKTFLGRISSLSVFTQDVASRYFSNSTERSAQNISSSISSLKLTMSTYQDVLFQIFNTLIRTSTSLRESVLDFFAMVVNANHKRQSIQVNHFDITSDACMLNFSHVLSRLSEPFLDIGCSKIDRVQVEYFRRNPRVDIKEETKLNADQKASESFYSKPAEGSNNFISDIFFLNLAFHHYGVNATFKALEQLVQSIRDSEKLKERLETEQQNMSGSFQATRLTAQLSRLDQRLDLDRSFVHCYEIMLTQTSDTSRSFSFLNFVAIWLSRLADGQSSTYPKMPLSLPFNENAPEAFKCLPEYFIETITDYMLSLFKTSSSTLTLHSLEPLCEFCVSFLTQANYIKNPYLRAKLAEILYFGVQTHVGRSELLLDVVRTSKVATRWLLPALMAFYIEIESTGQSTQFYDKFNIRFYICEVFRTIWKQPAYFGKLEQEQKTNLPFFVKFVALMLNDATYLLDEALLKLTEIHNLQSLLADAISNSNSNQNVQESQSNLAAAERQASTYCQLGNETIFMLKLFTSSIPKAFCAVEIVDRLAAMLNYNLQALCGPKCSNLKVEDPTKYHFNAKTLLSIIFDVYLNLCNEPAFVEAVAHDGRSYSKEIFERATSIMTKHNLKSSFDIEAIKEFVNRVEAFRLQEATEEEDMGDIPDYFLDPLMFTIMKDPVVLPRSGISIDRSTIKAHLLSDATDPFNRTPLTLDDVTPNDTLREEINTFLKSKRNKHSRNSE Q9HE06 YK99_SCHPO BINDING 48..55; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPAC20H4.09; CHAIN 1..647; /note="Putative pre-mRNA-splicing factor ATP-dependent RNA helicase C20H4.09"; /id="PRO_0000055171" MPNEFISQSLSTLTNTPLNIQKKLLPITKYRNQLLYAVEQNQITIVLGHTGCGKTTQIPQFLYEAGWASQNGIIGCTQPRRLVAKSVSERVSLELNSPPGSLCGYSIQFDHNVSEKTKIKYMTDGILLNEIFFDPLLERYSIVILDEVHERTLSTDLLLGVLKRILEKRNDFRLVLSSASVDANKLSQFFGQDKVCTMSIEGKLFPVETLFLQKPTENYVDSAIETVININSTYPPGDILVFLSGRKEIEYCIKKIEDSLIHASEDCQTLVPLPLHAGLTVDEQMRVFNIYDGDFRKVIFSTNIAETSITIDGIVYVVDSGFNKQRIYNPYTRTSKLINVPISKSSAIQRSGRAGRTMRGKVFRLYTEKAYSLMKEEFEADILNCDMSPLVLFLKGLGLKNILQFPFFVRPPTVHLMAALEDLYLLGVLDESGNLTDPLGIQISNSFLDANISKALLTSNQFGCTHEILSIASILTAGEVFYNPTSSSKNDAFVAHSSFFANEGDIITALNVFESFVGNKKDLQWCRKNYLNYQTLRQALDIRTHLVRFLNKFSIPTAQRLPSSDCSKILKCLLDGFVRNVAHLQNDGSYKTIGGKQVWLDSSSVLHEKKTPWIMYSSAVESETQIFVKNISKIESFWLDKYYKREK Q9HE07 YK96_SCHPO SPAC20H4.06c; CHAIN 1..534; /note="Uncharacterized protein C20H4.06c"; /id="PRO_0000363375" MYANSRKRSNVDVHRHPYVVYGSPFDLEPSRINQGVPVWKQEARDERNRKRFHGAFTGGFSAGYFNTVGSKEGWQPKSWKSSRNENKSVHGMTIDDIMDEEDRADQELSKVYTSKINTIDTSIPIDDPLLREFSNRDDSIGEKMLKNLGWNGHDFVISPFQGYYDDTKLTNQAYHGIGYQADDVFQLERKPVGMAKNLRGGFGSGVLNDDGIEDQDIYDLGAPKMRYDKSINITKKVASPFTPVKHTFLSKKDRSKGKSIIKSQNCSDGLPPLPGFVVVFNLQSPFQNNWFPPPTIPEGWEPKLFTNSQGFSQKKAQTSNERLPLFAEKSETNSNGEASLPSDVNHGVKEDEGSWQLIDIETAKNAMSRKDNPYNDERAGIYEIFLKAHLMNMPRLLRDIDSRHLLEFTQTASLYRPMSKNLSMRFVSSFEASTKKESINSHSETDDSILRRPRTVVTFIPERLLCKRFNVALPYGQEKQKRKNISSIENVPIIAEIENKSIDSIDTRKLNRPQDIEEKPKAPQTLFSAIFGDD Q9HE08 MTNB_SCHPO ACT_SITE 135; /note="Proton donor/acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_03116" BINDING 92; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03116"; BINDING 110; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03116"; BINDING 112; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03116"; BINDING 192; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|HAMAP-Rule:MF_03116" CATALYTIC ACTIVITY: Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377, ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109; Evidence={ECO:0000255|HAMAP-Rule:MF_03116}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03116}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03116}; SPAC20H4.05c; CHAIN 1..228; /note="Methylthioribulose-1-phosphate dehydratase"; /id="PRO_0000315888" MDDFLKKDLGCLRSGDLKKCGELICEICRDLYTSGWVTGTGGGITIRSGDAIVIAPSGVQKERMELHHLFVMSLITREYMRMPALRLKPSQCTPLFLAVYTLRDAYACIHTHSQEAILLSTLFADSDHFSATGFEVLSYIPKGSKNNGFHKPTDKIKIPFINNTAHESDLHDSLQEAINLYPDTCAVIVRDHGIYCWGDTWQDTKMNTEAVEFLFQAYLRRRRLQKPE Q9HE09 MFH2_SCHPO BINDING 131..138; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; SPAC20H4.04; CHAIN 1..783; /note="Putative ATP-dependent DNA helicase fml2"; /id="PRO_0000351000" MIVLRDSSDYSDSEVDLPSIEVNGERGNVPTSVLCNVEGSLLNSNPALRQPNLKCIKHNQDVENTTFQLDLRGCRVPSSQPQVITELENNIDIPKNIDAMQNWIFPQTQQYRNYQKEFCEQALFHNLLLALPTGLGKTFIAAVVMLNYFRWFPESKIIFLAPTKPLLLQQRVACSNVAGMSPGATAELNGEVSPDRRLFEYNTKRVFFMTPQTLQNDLKEHLLDAKSIICLIFDEAHRATGNHSYAQVMRAVLRSNSHFRVLGLTATPGSSTASVQKVVDCLHISKLIVRNEESIDIRSYVFHKKIQLIKVTISSEMNILKSDFANLYRPYFNFLRQKKLIPINCECLNIKAYTLFVSLRKYSFSSKNVQSKEKSKIMSCFTLLISCAHITYLLDCHGIIQFYQKLVETKNKAEGKGSGQSFWLFTSKPFAFYLEHLHNKIQGLSLNHPKMNHLLELLKEHFKDTSEGYQNQRVMIFTEFRNTAEYITTTLLAIRPMVRASLFIGQANSAYSTGMNQMQQKETIDQFRAGVINTLVATSIGEEGLDIGDTDMIICYDASSSPIRTIQRMGRTGRKKSGKVFVLLTEDCEDSKWERSQVSYRRVQKVIESGKKIALKKDVPRLIPSNIQPIFKFQALQNNADATLILNSYNNNSSSLSPVNTLANQAHSRSKRYLPFIVDDVFEDMESNLRVPTEDAKIKRFKSDYRSCIYNARRNVFSKPTYMGDKLTKFAKVPHSLLTLSIYRRGRLLQQCSPSSVTKYLKYEEKFKRKRMKKTSNALFQST Q9HE11 UTP5_SCHPO SPAC20H4.01; CHAIN 1..666; /note="U3 small nucleolar RNA-associated protein 5"; /id="PRO_0000116824" MAVRSRPQLAFQTEKENGIGITAFNETAKLYANVVEALDAQRLRIFDSVAGSLKTEYILEKEKVISCIAWEQKPLYASEQITTDISGSGEILVLGTNSGEILIYSEHLGSLTRTYSFGILQKIIGAHVLANDGFAIDITGKVVCFSVNTGEVRTSFTVPSSSREFSGLYLSTVFKNLALASSHNIHIVDLNHRNPIDSLTTHTSMINSVVFQYLKDENKFYFGVSANQDRFINLYSKELDGTGEFPTNTVKNVGALVCENEVKMLSIAYEIENPETGVLAALTNDGTIEMFENPWLSKLRQNGTNASSLSHRRKLLTSHSTLKICFCRSRGDPPIVLESIAFESTDSLTVVWKESTRTVFETVPWRILSSQATNGLIELVRSKTRLTSKNKTVSNVYDESNATISSGVMQKDLRKTEEIGSAEAMEGEEQEPSLAERLQNLTKLDQQAQALSTQISASTSLSTVLTQALKTNDQSLLESCFNNNNVETIDTTIRRLDPSLAPILLDKLAEKLALRPMRADVLMVWIRCTLITHGGHLVLVDDLKHKLANLHSILEDRASKYSSMLALQGKLDLVLSQIAFRKAGGSKDNAEDEEPISIYYEGYEESMDEASSTGDEGYSSDDSVDNEMYSDEENSSKGAFPDEENENRELSEDYSGDESLENSESE Q9HE15 UPP2_SCHPO BINDING 77..80; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 87; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 113; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 134; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 140..148; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 140; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 204; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250"; BINDING 205; /ligand="uracil"; /ligand_id="ChEBI:CHEBI:17568"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 210..212; /ligand="uracil"; /ligand_id="ChEBI:CHEBI:17568"; /evidence="ECO:0000250|UniProtKB:Q26998"; BINDING 211; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. {ECO:0000250}; SPAC1399.04c; CHAIN 1..220; /note="Uracil phosphoribosyltransferase 2"; /id="PRO_0000120787" MSIPLEQPENVVVLRQTMYLLSLMTILRDQQTGHSEFVRTANLIINMLMQEALSALPYKKCLIKTSSGGTYTGVQPARDICGVSILRAGESMEYGLAAACNYSVPVGKLLVQRDETTFEAKLMFCKLPKDAQDRLVLLLDPLLATGNSVILAIQTLINKGIPEENIVFVNLIACNEGITNVFAKFPKLRMVTASIDPELNANKYVVPGCGDFGDRYFGTC Q9HE16 YI35_SCHPO SPAC1399.05c; CHAIN 1..529; /note="Uncharacterized transcriptional regulatory protein C1399.05c"; /id="PRO_0000310385" MGEVERTRQSSSSLLTFKRKRALEACDSCRKQKTRCLAGSVEDENRACLRCRSLNMDCSLADPNHFIRKVENDNMDAISANINSKLENRLKVLEKAISSITNSPIAGQISLKSEKDVFLQGLLSMDEIELLLEIFIERYGKRWLSVDYSASQYMELLYTKSHLMLATACLIALRHNPSLKARIYTDVLNIVDRLISEELLTTSPSLQFFEAVSMLTLYRPLRLSQKQDLWLLSGFALQHRTLSSTKGWFNGFAGSSATLTYLDIVPARTWNHLCHGHLVMCMGYRRHAMLDENTFDDCRNILTNTKANEFDGNILGMLSVYSMLYRMLRSPTLDLDYAIFQLEEWRKEWCHLWEQPEPQYSRIAYFYSYNVVYEASIQTATDGNDFANIPRYVSMVQSYALKTIDAIFELSAYDMSRCSDHVLFHAGFASASLLRLIYAAKTKEVDTSIVQPKVLNDLVTKIWKWLLVISVDQYHLATKFANYLKEYQKTVNEGTAESTWFKGPLRPVSSTTLQALKPYNLGVATVERG Q9HFE4 FMO1_SCHPO BINDING 13..17; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8, ECO:0007744|PDB:2GVC"; BINDING 38; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8, ECO:0007744|PDB:2GVC"; BINDING 46..47; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8, ECO:0007744|PDB:2GVC"; BINDING 90..91; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:2GV8"; BINDING 91..92; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8, ECO:0007744|PDB:2GVC"; BINDING 137..138; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8, ECO:0007744|PDB:2GVC"; BINDING 223..226; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000269|PubMed:16777962, ECO:0007744|PDB:2GV8" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; SPBP16F5.08c; STRAND 8..12; /evidence="ECO:0007829|PDB:2GV8"; STRAND 32..37; /evidence="ECO:0007829|PDB:2GV8"; STRAND 39..44; /evidence="ECO:0007829|PDB:2GV8"; STRAND 59..61; /evidence="ECO:0007829|PDB:2GV8"; STRAND 71..73; /evidence="ECO:0007829|PDB:2GVC"; STRAND 74..76; /evidence="ECO:0007829|PDB:2GV8"; STRAND 135..144; /evidence="ECO:0007829|PDB:2GV8"; STRAND 147..156; /evidence="ECO:0007829|PDB:2GV8"; STRAND 161..171; /evidence="ECO:0007829|PDB:2GV8"; STRAND 175..179; /evidence="ECO:0007829|PDB:2GV8"; STRAND 197..200; /evidence="ECO:0007829|PDB:2GV8"; STRAND 215..218; /evidence="ECO:0007829|PDB:2GV8"; STRAND 237..242; /evidence="ECO:0007829|PDB:2GV8"; STRAND 252..257; /evidence="ECO:0007829|PDB:2GV8"; STRAND 260..264; /evidence="ECO:0007829|PDB:2GV8"; STRAND 269..272; /evidence="ECO:0007829|PDB:2GV8"; STRAND 276..278; /evidence="ECO:0007829|PDB:2GV8"; STRAND 282..286; /evidence="ECO:0007829|PDB:2GV8"; STRAND 311..315; /evidence="ECO:0007829|PDB:2GV8"; STRAND 318..320; /evidence="ECO:0007829|PDB:2GV8"; STRAND 331..335; /evidence="ECO:0007829|PDB:2GV8"; STRAND 338..340; /evidence="ECO:0007829|PDB:2GV8"; STRAND 387..389; /evidence="ECO:0007829|PDB:1VQW" HELIX 16..26; /evidence="ECO:0007829|PDB:2GV8"; HELIX 45..47; /evidence="ECO:0007829|PDB:2GVC"; HELIX 94..97; /evidence="ECO:0007829|PDB:2GV8"; HELIX 114..125; /evidence="ECO:0007829|PDB:2GV8"; HELIX 126..131; /evidence="ECO:0007829|PDB:2GV8"; HELIX 187..193; /evidence="ECO:0007829|PDB:2GV8"; HELIX 201..203; /evidence="ECO:0007829|PDB:2GV8"; HELIX 207..210; /evidence="ECO:0007829|PDB:2GV8"; HELIX 222..231; /evidence="ECO:0007829|PDB:2GV8"; HELIX 297..300; /evidence="ECO:0007829|PDB:2GV8"; HELIX 342..357; /evidence="ECO:0007829|PDB:2GV8"; HELIX 366..380; /evidence="ECO:0007829|PDB:2GV8"; HELIX 384..386; /evidence="ECO:0007829|PDB:2GV8"; HELIX 394..407; /evidence="ECO:0007829|PDB:2GV8"; HELIX 424..431; /evidence="ECO:0007829|PDB:2GV8"; HELIX 433..440; /evidence="ECO:0007829|PDB:2GV8" TURN 27..29; /evidence="ECO:0007829|PDB:2GV8"; TURN 232..234; /evidence="ECO:0007829|PDB:2GV8"; TURN 265..268; /evidence="ECO:0007829|PDB:2GV8"; TURN 273..275; /evidence="ECO:0007829|PDB:2GV8"; TURN 305..307; /evidence="ECO:0007829|PDB:2GV8"; TURN 321..323; /evidence="ECO:0007829|PDB:2GV8"; TURN 391..393; /evidence="ECO:0007829|PDB:2GV8" CHAIN 1..447; /note="Thiol-specific monooxygenase"; /id="PRO_0000314653" MCLPTIRKIAIIGAGPSGLVTAKALLAEKAFDQVTLFERRGSPGGVWNYTSTLSNKLPVPSTNPILTTEPIVGPAALPVYPSPLYRDLQTNTPIELMGYCDQSFKPQTLQFPHRHTIQEYQRIYAQPLLPFIKLATDVLDIEKKDGSWVVTYKGTKAGSPISKDIFDAVSICNGHYEVPYIPNIKGLDEYAKAVPGSVLHSSLFREPELFVGESVLVVGGASSANDLVRHLTPVAKHPIYQSLLGGGDIQNESLQQVPEITKFDPTTREIYLKGGKVLSNIDRVIYCTGYLYSVPFPSLAKLKSPETKLIDDGSHVHNVYQHIFYIPDPTLAFVGLALHVVPFPTSQAQAAFLARVWSGRLKLPSKEEQLKWQDELMFSLSGANNMYHSLDYPKDATYINKLHDWCKQATPVLEEEFPSPYWGEKERSIRENMWSIRAKFFGIEPPK Q9HFE8 TRA1_SCHPO SPBP16F5.03c; CHAIN 1..3699; /note="Transcription-associated protein 1"; /id="PRO_0000314773" MQLALSHNIPIVIVKYLGKRIRVQLEFKKELAQRSKHLMDVSQCEHWHNRLCDVGLDSKQKANTAIEIRDALDDVLVTEKTNFETFIPLLEDTLSLLEKERPVFSSLAATHRLRIALLELLKKSGSYKGFEAFVNRTFAVLLRIVVNDNEEMAVLALKLVVLLFKDHSSLAKGHVQEFLSIVVENYKSMTTVVSEAFPPRSAPNTPSSHPMSAASSASPAEIGMEHAGPKMIPKASSSFKVTAEFPIIVFLLFQTYKDLIPKMLPLLAPLVLQFISLRPPPQAEARRLAESQKEVFIGVVPSLRRNHLYNDLISAQIKSFSFLAYLLRSFGAALKQFESSIPICTLQLFMDCPSELYQTRRELLVATRHVLSTDYLRGFLPYVDQLLDTKILVGSGITSQHSLRPMAFSMLADMLHYVRMELSPQQIYKVILLYFSILMDDFYTSAIQAMATKLILNLVERIVALEDFSTSRSLLFAILLCLLRKLTSLNFEFMKLRDSLQENADLKQIKIEENKHDLPMFENPTGAAQPSGLDKLKDCIFLFKNTLLGIKPVLFGLKQRNIPLANGSIFTAQEWSEKLHLSSTNEVLLFRRLLVESLKGFSYYQTDEKTGVFKSSKNLAYSQLDSSLTTNPSKLLEEKELLEMLATLFLHLDPSVFVEILESEFPNIFECLVDNLALLHIFQFWMSNEVTSVNCTGIVLSFCCDNLAKIGSGQSTRVSVLLRLFKLAFMTVNVFPEKNAEVLRPHISYIISTSLELTTDAVEPLNYVYLMKALFRNISGGKFDSLYKEILPLLQVMLECFNRLIFTVTSTSQKELYAELCLTLPIRLSVLLPHMNFLMKPLIVALKGPPEIASQGLRIFELCLDNLTQEFLDPLLDSIMPDLLICLWNHSRLNQSNNQLHQSAVRILGKMGGRNRQIYLGTFGFDFLQDENIFPSIQFSFQGSSQNFSLEHSKFLMSSCAVLNNQNSDLEEKKQAFQMVKNSYLLLFASAKPDEDFWESIDTMCRAVVDRMDKNLQQVSNGRLCPDKDESYYLQRSIVSNIFKSLVGSMSCVEFVAEARETINRSLEWLIVLDLVNYADSLQIKDQNIFDNLQSIKMLDLTTCINGIFESLCSENENTRSNALSCIDHYLNAHKMLLNTTLDISKLPSFQNLVTVFCQSCHKELWYQKNAGFLGLKAILSYDSHHKLWIQDRLHDILKALFFILKDTPTDYGVLKLTEVRSFIVDITTQFCILQDVLAPKERANNIINAFSPFFLELLHPNDHVRNTVQQAIENISNNSKLSVVDLLLPIKDRLLSPIFGKPLRALPFTIQIGHIDAITYCLHRSPSFLDLTDELYRLFRETIALADAEDEALVTMLKTSQSKDSSSLRKLRATCLHLLFASLVAHKFDQPQHAQTRTKIIAIFFKDLYSPHKEIYSVAIDALRHVLSQNQKLPKELLQSGLRPILMNLSDHNKLSVNGLEGLSRLLRLLTNYFKVEIGRKLLQHLNVLSDSKVLETASLSLLKTNPRIEIIVSLVNVFRDLPPLSAQFLGDLLSSVVNIEAVLRKYSNSPLRKPLYSFMDLHANDTWMYILNNARNGDLITRFVGALNDPMSEKLRETAGNYWGKLLELISQPVSVENLAPMYAVDIIATVFPYISANVDAGVISAKFIVLSKSLYGMLSSYNEYLFLPIRRCISSITKMLLSSLKKIEKKLEFSLEVFRFKADDDNDFLPEYIDSLCGCLITSTSAAEKKSIFLVCCSIVGDKSVRPFFKAFLLDKVINPLVFKSCGENNFIDKDVVHSVYTHVWRVSIRDFAEVSGATDSFYMGIMCLTTALCKYHSALLNDYRKSVIMSAWNYIKLEDPMVKQAAYATIACFISAYDTPAKIVTPVYVSILKTYQPEVRAFIEFSLASLLSVLTARLSSPSDSTFPLWAKLPRLVISEDVQGISQPLTVYQFICKAPDLFFSCCSHFIVPMVNALPKLVSFSSASTEPRKLALDIVQTFINWQRKQNESENSETTLFSNSHIEAILTFLIKFLSLFPEPVEENPLSKKGLSLFNDLFSFPRWKDCQLNSNFFEKILVDMDFNDNNYRTVANTLFVFGVILKNRGMEYIQREYSHIIALIDKSLRCGKLPVTHSLEQIILLLLQSHPTQAEEEEDTNEADDFKQLLLSVIHDNLAAATNIESAICYLQIVKSSNPEALDGLLLPLNKCFQKVARDHIVACMQSAIQASGKVTLPSASDTVSKLLISFIEIIRVRMASLGDQRRWFLSVVVQLLEKSSSFELCEHILNVTKEWVIVKRDSFLTVKEKTALLLKMRTFEGRFDNKLYIEACDLLSTIYRDPIFAHTELTARLKQAFLLATASKDTKIRMDFMDIFDSSMSRNVYSRLTFILDATSWDTIPSIYWIKQANYILLGAINAKQPVRLTDNSLRFAPVPMTKPILSSLPEVFSKHNGSAIPLGRFTFFKQLDLFLKRNKELTVQKIIFPLAHIQMLSDADANKLWQYIFPLAWKILSSDNRSDLSKSLIYLLTRDYHIKQVNNRPNVISTLVSSFVKCAAKLELPPHLVKYLGKLYGVYHESVSLLEIQLSDKYDMYQNAKVQESRADAVAELYASLNEDDMFYGHWRRNCKYLQTQVALSYEQLGMWGRAQQLYEQAQTKARSEAIPFSESEYNLWEDQWVMCAQKLQQWDVLTELAKHEGSSELLLECAWRISDWSNNRESLEVAIKSLSDVPTPRKLTFQCFMTLQKSVSQPLAIKEFQQVLSEAIQLALIKWHQLPEKVNQSHYSLLHLFQQFVELQEAATIYSHLNAINFQNLPTNVQLIKSALQVWQERLPNVWDDINLWRDLISWRQIVFSMINRVYLPLVPTIQANSSADSSNPPNTSFLFRGYHETAWLINRFAHVARKHKLPSVCLNQLTKIYTLPNIEIQEAFYKLREQVLCYLQNPRDLKTGLEVVTNTNLMYFNSRQKSEFVTLKGKFLEKLNRGEEANQMYAAAVQIDLGLPKAWAEWGRYNDLLFNKSPDNLSAACNAISCYLQAAGTYQSSKARKMLARVLWLLSLNDSAGTIVKAFESYKGDIPVWHWLTFIPQLLNSLSKGDTKCAPVVLKKIAKSYPQALFFTLRTAREDIAQVKRTEMAAWKSNTTDENKRNEDILSIQSNFLSTNQSTNAPATNKEDGLSKKVWEYIDEIMSILKTAYPLLALTMETLVDQIQAKFKCKNDGDAFRLVVALLNDAVQHSIRLGIVTDEMKLPSSTESNLSLFADNILPDYCKQLFKEDFIVNSNGLKSYIFKLRKWRSYFERLLSKVPKKQYLEQYSSFLCEFHHQKFDEIEVPGQYLLHKDNNNSFSCIERFLPEVELIVGHGVCYRRLSIRSNGGTIHPFVIQYPSARNSRREERFMQLTRYLNDALALNCETRRRCLKFYIPAVIPLSSHIRLLEDQPSSITLQKIYEIYSERNNFSRDDPKELFTNELSKHMMELNSQISQESTDAEKLANRKQLFSRRIGMFENIQKLYSPSTILKDYFSSIFTNYSDLWLFRKNFSYQYACFSFITYILSINNRIPAKLVFSRDSGGVWTTEALPSMVSSTPVYHNGEIVPFRFTPNIKEFIGKTCTEGLLGPSIMAIARALSKPDFDLDMYLGIFIRDDLFWWLAQQTKGVPADFSMLNKVNSNTDLIMRRVASLSQVAYGNLPVNQTAIDYLAQASSSKVLAQMDVLWAPWL Q9HFF4 PPK1_SCHPO ACT_SITE 623; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" BINDING 498..506; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 529; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; MOD_RES 492; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517" SPAC110.01; CHAIN 1..1023; /note="Serine/threonine-protein kinase ppk1"; /id="PRO_0000086139" MNAQPFHNNTSDVQSFQDIISNSYQKPLSLVDSTDRALPDSSLSSLSRSTFQFHKHHLSGNENPQPSSESPYFTNNERLNSSSFPQIHDNQLSPSFNTSYQAIPSSSSNRSRGGPYTPSIRDDSLLALLSFSSNHRLHSMPSQLQPFNNASSYTTPMAPFTASFSNKVSHSAYPTRRLPSQAKKTSAIERVPVNLNFLQSDNLVVQSSPQTNFENFEFPKKIPSKEDLETREVLLLPPQTSKLSNKNLDTKSFTDVNKISQQGFVEISSNSSKVTPNTSLHQSFGIASSSSNNYMQTSSELTSSTEKMNGSHPLQLSNKSLLSIHLMQSKNQGHVSMTGSDKLSSHVQSETENAPVSKPSKPNTLTEDEKPLQSTKLPGNSLTVGELYQEPKSIQLPELSVSRTTYSAQSSSVKNCNERIPSAKALKKQKHLVPENKSKLQYVWQKKESLPYANLTSASNTHFFLSENQNDTSERLTRTLRKSTKNYTFGSYILGRTIGTGEFGKVKLGWPLPKANSTIHRSTPQVVIKIVLSTKQNCQTSRLMREVAILKGLGNNHPHIVKYLDFVKTKHHFGIVLDYVNGGELFDYILARRRLEDSVACRLFAQLISGVAYLHSRGVVHRDLKLENILLDTNRNIVIADFGFATTFGHFNTLSEHSLPTEKPDLFSTSCGSPCYAAPELVNCKSGMYAGTQADIWSCGVILYAMLAGYLPFDDDPHNPNGENVPRLYRYICSTPLIFPEFFKSKARDILKKILVPDPAKRVRMSAIMNHAYLRSHVSLFETYNDDEATSLRPSPIRLLSQKSLASVSSVSSISTYSSSIELTPQITKTSLNREKPALHGSINLKHSTRPVVPIADGIYASTTLHPIDNAKNRLVSLLRRPKHKVKHAKVETRESPMKNKPTKKQHKRAFSMFERPTSQKAPLSPVESKINLMVAPKRVLNCASDSLRALLAGKTDKSFWGSRIPFLFNKLKSKQKAVSSSFNTENSFLILQAVSPLTFGGCFKEENAYGQKKQHMRHATVF Q9HGL2 YHLA_SCHPO BINDING 305; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 307; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 309; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 311; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 316; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SPBC800.10c; CHAIN 1..1116; /note="Uncharacterized calcium-binding protein C800.10c"; /id="PRO_0000310332" MSLNLSAEEQTAFDQLFKIADKQDIGVITGEEAVPFLEKSGLAPQVLGQIWQIADAENRGFLTFSGFVIAMRLVALAQEKLPFDYKKSGKIPYFADIHISGVDSSKFVQLNRPNNVSSGDGSDGSFLPPISSDEMTRYQQMFTTVCPTDGLMDGDRASSIFGRAPLSTEILARVWNLVDTHKRGALDIREFNTGMHIINLLLNGSLKSPPVSISPSFIASAASTSSVSAPSQYPGLSRSPPVQAPNIPVSDPWAIPSQDLTSFCQLFSNVDKAHKGYVSGSEAYSFFLASKLPEDVLAQIWDLSDTNSNGKLNIGEFCISLYLIKLKLSGKELPKVLPSSMLSSVAPLMQKSKSVPTSIPSVVPANISSPNPNPTLAPNPTGPSRVTSGTEDLLSLDATPFSPTLAPQHTSSNATKHSAPPVTKSAPFPVVSPLQLNHTPGFPTSPAAKPNSPTSTFFPQSSFGQTIAKNTMDKPSAVRTSVPSQLAAPIPQVASAEQLKLAAEVPKLESQLSQVKKSNDDLQKSSRDVAANLSDVKAKVSEIRKAYDEELAKAKQISLDIETNKAQTEQVNREYSILEATLNALQKQNKQKGEVLEQVVAESEAAKNMVESSNASIQQLKSEVADKEQTLAQLHLQLDEMTQRLVSLDEESKAVSQRKLDLEYKINNSKTQLATATEEYHEHSKQLEAEKQELSKLEDGLKSVNLTEEAPKPEVDSTPRFPSFTSNGITTDKPTLPDTTSSVPTQHNSFDAMHNTLRSPSLNSNNSSAHASTVSRNPFHNLKISGASSPVSNFWESEFASAVFPRSISKTTSLSVNNSSVNPSLDSEPVQLSNMEEPQHQDSSVVDVSTSASQRGSPVLSDLSKLTGSARNTAEPVENTSAEPIENTSAPTPFEIANKQQATEPISAPFATETISTPAPVKPPVPPSRRDRSAQDGVVQQATPHIQDEFPPIQFNEIDDDESSSDEEPPMSNLSPQISIGSVTNYTSAVTELPDPNHQLEMSTTTHVQHPNSETIPSSTENQYFDTTSGAFEANSNTEVTVNSNEVSQPFDFDTANESDNDDDELPVQQVVSGSLANDAFNVDDEFDNQFANLQAAEIKDDDNSSTDEEEHAGHH Q9HGL3 SUM2_SCHPO SPBC800.09; CHAIN 1..426; /note="Protein sum2"; /id="PRO_0000072312" MTEFIGSRISLISKSDIRYVGILQDINSQDSTLALKHVRWCGTEGRKQDPSQEIPPSDNVFDYIVFRGSDVKDLRIEEPATTPSAPPVQPPNDPAIIGSNSGQYNWNQAQTAQPPQPVQPNPYGAPYQQAPPAGAPYYMYPNAPAQFVPPGGLPLGTPLDASTPAVPYYGAPDQQQMGQRPEFAQNVSQGFAGQAPYNVRPGYGMPSNQKPPNFAPGMPAPGPTAVSASPSLQSMPPTNGVIPGAQPSIEASIEKESTSIRNSTVTNDRVVNTTVDVSQSQTVETSGPSKEVPTTQPDASAAKPRTEFDFQTANQKFQSMKDDLLKGKNDEEAEEFYKPKQSFFDNISCESKEKGMEAADRRALRDRERSLNMETFGVAGSGNRGRRGRGRGRGGRGRGRGYARNQYNQYRNSNGSQPRAQPANDQ Q9HGL4 TRM6_SCHPO SPBC800.08; CHAIN 1..462; /note="tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit trm6"; /id="PRO_0000256165" MLRHASTISENSSVFIKLPSDNVRFVTLKPNNTIHLGKFGSFLADDLFGKHFDETFEIYQPKKIRVLKTREVQYIEEEKKTNQELNDCRGNQLMTQEEIDELRANIKAGGLRAEEAIKQLTNSSKTFEQKTLFAQEKYVTRKGEKYLQRFQVLRPCVEVVANYMIEHDPYKILDLTAECISLMLTLGNVKPGGRYLVVDETGCMFLGSLIDRVAGDCKITLVHPNEQPNSSCLEYWGQDFKEDSLVQKGILKTLNWYQVTNPTETLSEYSVEDIPESELNEMKLRHRKRYETKKATFNRLKNTIDDFESGNYDALFILSIHTPMSVLQHLLPKLGISRPFMVYSTYQQVLVETYHQLSKWDNLFVEKTAQSTENDEKVDQGDVAIDTQKEKVIMLDIHEIRTRPYQVLPERTHPFMTVRGDMGFVLSGIKVLTSDSNLAAGRFPKRKGQKETSSVKKAKLEN Q9HGL5 EFTS_SCHPO TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03135" SPBC800.07c; CHAIN 19..299; /note="Elongation factor Ts, mitochondrial"; /id="PRO_0000362143" MLFQRRLHFHQFFGKTRVTGSLSRQWYSKLPSKLADIKKLRSETNASMDLVKQSVEEAGVGNLELAREILKKKIVQRGGKLAEKSKNRTAKEGWIIQCISEDGRKAVMAEINCESDFVAQTTPFQDLARRIASTFLHYLPTNHSSYSVEATLKNEILKHQAYVSKNHEANEKDVSSNVSLEEEIVKMTSFTGEKVQVQRLHCMNARVPSTAIGIFSHGAKQSSPLQQLGRIGSMVQINSDLSTRKGLSNQIAKEIVAQDPSSTSELLSFRSLVDSEKTIKDVLGQSTILEWVRWERGGN Q9HGL6 BRX1_SCHPO SPBC800.06; STRAND 45..50; /evidence="ECO:0007829|PDB:8EUY"; STRAND 71..78; /evidence="ECO:0007829|PDB:8EUY"; STRAND 96..104; /evidence="ECO:0007829|PDB:8EUY"; STRAND 108..118; /evidence="ECO:0007829|PDB:8EUY"; STRAND 122..130; /evidence="ECO:0007829|PDB:8EUY"; STRAND 134..136; /evidence="ECO:0007829|PDB:8EUY"; STRAND 148..151; /evidence="ECO:0007829|PDB:8EUY"; STRAND 182..184; /evidence="ECO:0007829|PDB:8EUY"; STRAND 188..194; /evidence="ECO:0007829|PDB:8EUY"; STRAND 197..204; /evidence="ECO:0007829|PDB:8EUY"; STRAND 219..235; /evidence="ECO:0007829|PDB:8EUY"; STRAND 238..244; /evidence="ECO:0007829|PDB:8EUY" HELIX 55..66; /evidence="ECO:0007829|PDB:8EUY"; HELIX 85..93; /evidence="ECO:0007829|PDB:8EUY"; HELIX 153..156; /evidence="ECO:0007829|PDB:8EUY"; HELIX 159..172; /evidence="ECO:0007829|PDB:8EUY"; HELIX 251..282; /evidence="ECO:0007829|PDB:8EUY" TURN 105..107; /evidence="ECO:0007829|PDB:8EUY"; TURN 289..292; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..295; /note="Ribosome biogenesis protein brx1"; /id="PRO_0000120234" MSTVYKLKTSERAPKNEDEDEEYVPVQNGQGNKHSAGFVPIKQKVLVLSSRGVTYRQRHLLNDLVSMMPHSKKDSKLDSKDRLYQLNELAELYNCNNIFFFESRRREDLYLHIARAPNGPTVKFHVENLHTMDELNMTGNALKGSRPILSFDKTFDTAPHLKVVKELLQQTFGIPKGARRSKPFIDRVCTLTIADGKIWFRNYEIRENEDKSKDPVTLIEIGPRFVMTIINILEGSFGGPVIYKNDTFVSSTMVRAAIRNQAAQRYVNRQESKLERQVRAQQNVIPEDPLDNVFA Q9HGL8 RL43A_SCHPO SPBC800.04c; CHAIN 1..94; /note="Large ribosomal subunit protein eL43A"; /id="PRO_0000139836" MTKRTKKVGVTGKYGVRYGASLRRDVRKIEVQQHSRYQCPFCGRNTVKRTAAGIWCCNGKGCKKVLAGGAWTVTTAAATSARSTIRRLREMVEV Q9HGL9 WHI5_SCHPO SPBC800.02; CHAIN 1..252; /note="Cell cycle transcriptional repressor whi5"; /id="PRO_0000300504" MAGGHKKNEATRQTDEVIQQKYDESLSKHKNRCELSLTFEYKLSNKLRARLKAAFFKVDHGWEDQTLDQVETLVRKENHVHRRSRSINDLDSSKLRRPHHPNSIMGSNTGKLRASSFTRLVSPREGFAQLPYKKPVSPYSSSSAVSSTSSSFDRTSPPWLNYVEPHTELPRLPFELSHASTASAKSPLFGMNYHISRPEETDESLRLGTANLSRIRKSTSLPFPTAYPLSADDCKAAEVMLTLVNSMPSKKP Q9HGM2 GET1_SCHPO MOD_RES 65; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC543.10; CHAIN 1..171; /note="Protein get1"; /id="PRO_0000372625" MMDLIISTILLSLFIHFFDKFAKKRTIDGAYRIYVSVSNNKDLKKNKEILEQLLTVKKELNATSSQDQFAKWARLNRKYEQLSQEWEKQSANVKIFQDTFKRVLSLFLWILTRGFRFYIQFKESKTPVFFLPAFLLPSWALWVLSLPRSIYGSVSLTVWNFAVQKTISGIF Q9HGM5 DBP8_SCHPO BINDING 51..58; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; SPBC543.06c; CHAIN 1..453; /note="ATP-dependent RNA helicase dbp8"; /id="PRO_0000232291" MSEHTRKSFSDLGISPWLIDTLKALAIYEPTDIQEGVIAQILEGRNCIGGAKTGSGKTAAFALPIIEKWSKDPSGIFALILTPTRELAIQIDEQFAALGANLNLKHALIVGGMDMIRQSIDLSKRPHVVVATPGRLADLIRSNGEETIAGLRRIKFLVMDEADRLLSPTFADDLDDCFSVLPASEDRQTLLFTATVTDAIRQLKYQPQKNNKPPLWLYEVETDNISVPSTLQQSYIFVSSQVREAYLVHLLTIPENAKKSAIIFVNRTRTAELIYSILRLLELRVTELHSEMVQRERINSLGRFRAEAAKILVATDVASRGLDIPSVQLVINFDLPRDPDDYIHRVGRTARAGRSGESISIVTERDVDLVHAIEDRVGTKLSEYEHVSENKMLEYIKEVTDAKRQASLEMIDRGFGERRQKRNEKRLMANGISNKLKNSGRKKKAKNTLSTEK Q9HGM6 YHW5_SCHPO SPBC543.05c; CHAIN 1..517; /note="Putative transporter C543.05c"; /id="PRO_0000316208" MNKKDKKFNYIFGSEIVNDVKKRLPYYKSDWIDACHYRVLPACLNIYFSNLLPELAFALDMFAKTNNSFGVNEVLLASVLGSVVFALLSSQPLCIVGVTGPITVFNYTVYDIMHDRGTPYFPFLCWICLWSMIFHFIIAIANGVYFVKHITKFSCEIFGLYVAFIYLEKGVQVLCDQLKYGLTNTFLSITIALLFLMVGWLCDTVGKSSLFSYKVRILLLDYGLVASIIFFSGFQHIGKMREVSLAKLPTTKAFEPTLSRSWFIKFWKIPVGDVFLAIPFSIVLTILFYFDHNVSSVMAQDPSFPLTKPAGFHWDFFLLGITTGVSGILGIPAPNGLIPQAPMHTAALCVKRVDYDEDEIEKTHKEVIDRVVEQRASNFIQGLMTVGTMTGPLLLVLHQIPQCVLAGLFWVMGFSAIFGNGITQNVIWMLSDRKVVSKNHTLNHCSSKRVVWLYTILQLIGFGATFAITQVDKASIGFPIIILLLIPFRTYCMPKWFLEEDLEILDENVGIIAYQKV Q9HGN3 TLG1_SCHPO SPBC36B7.07; CHAIN 1..225; /note="t-SNARE affecting a late Golgi compartment protein 1"; /id="PRO_0000210276" MEDPFYEVKADASNQMEQVRKLYNSFMAARNSGVLSPNTELTYAIDELSETLKDLKAAVEIAMKNSEHFGLDEEELKSRRRFVSELDIELNNIQLKMGAAPSTPVSTEPYTVDNGASAGLSEEDHAVNRQYQEQLYQQQDVMLDGVYDTIGNIRGQAALMGEELGQQADLLDTLDNSIETTNSKLRRGMKRLKDFTIASADSKSGCCITVLIIILIALLVLVIVL Q9HGP4 YK82_SCHPO MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC631.02; CHAIN 1..727; /note="Bromodomain-containing protein C631.02"; /id="PRO_0000211221" MTPVQVPNLDVSVTSSLITTAPVTGNAATISTFTPGSPEPSMNGEEKESSYFPISENDDGTLDLFGDSELEKEQKGDNQETDYSSQYLHPTPPYTNFDDESPSSPTHPSVSNITVDGDSKKHSLQLQEEEKSSESLDSHTHPPKRVRNEDDSLTFSKTSPVSPSSLKDGASNTVTNDASNKIKSEASESASPSALQALDSTAAGSSKEHSSPHDETVKKEENDKDQYPPMTKEQHKYIHAMLRQLRRGRDSIPFRAPVDPVKQNIPDYPTIIKNPIDLGTMQKKFSSGVYSSAQHFIDDMNLMFSNCFLYNGTESPVGVMGKNLQATFERQLKQLPSAYVTSYSRPGRRPRSMTAPKGGARTRRQAAMYSNSSSGIRETMYDLKPHRRKDAAEMKFCQSVLKELLKKQHEAYAYPFYKPVNPTACGCPDYFKVIKHPMDLGTMQNKLNHNEYASMKAFEADMVLMFKNCYKFNSAGTPVHLMGKKLESIFQKLWANKPDFDSETYMGMSSVNTDYYYGDNEVFDSGDEFLEDDGEEFEAVNRQIHKLQSTLQAMKSRARSSSVSRRSRSRSLSVDIYPPITYEMQNELAEQCNYLSADQLSHVAEILRAALPHLRNTDEIEIDVSAMPPDVFYKVYYYVCKGDEIGAEALATASHTHQEKKKGRALSETEQAEKIRQLRAQLDRFSGIAQNKNTVTGNIAAYNTKSLGSDDSSSEDDGESSESSDSA Q9P370 BUD20_SCHPO SPAC19B12.11c; CHAIN 1..124; /note="Zinc finger protein bud20"; /id="PRO_0000351142" MGRVARKRKHHSNGNHALFRTRVYGRDLDQIHNDLTESEKFDKLPIDPDLPGLGQHYCIECARYFDSSQALLVHKKGKVHKRRLKNLREEPYTQEEAEAAVNIGQPKQSVASKLADNSNVVMAD Q9P372 SRP14_SCHPO SPAC19B12.09; STRAND 30..36; /evidence="ECO:0007829|PDB:2W9J"; STRAND 45..51; /evidence="ECO:0007829|PDB:2W9J"; STRAND 57..63; /evidence="ECO:0007829|PDB:2W9J" HELIX 5..17; /evidence="ECO:0007829|PDB:2W9J"; HELIX 64..66; /evidence="ECO:0007829|PDB:2W9J"; HELIX 67..82; /evidence="ECO:0007829|PDB:2W9J" CHAIN 1..106; /note="Signal recognition particle subunit srp14"; /id="PRO_0000135195" MLLSNEEFLKKLTDLLQTHQSKGTGSVYLSQKCNPVDEGEGSSASVLIRAKSGAAEKISTVVELDYFTDFFQSYAEVCKGQIVGLKKRDRKKTKKNKKKTTSSGHT Q9P382 NUP82_SCHPO SPBC13A2.02; CHAIN 1..803; /note="Nucleoporin nup82"; /id="PRO_0000351141" MASTIMSQEVSWTDILEKHPALRWIKPIPEDWEIFPKHLCAFESFLYVAVGQEVRSLDCRLLKHKNEASHKNFYKKLFNPELDFMIEQICLSKNGRFLAVVGKSKIVILGLRSKLSEQNPLAESVSNFGESVNNFSNSEHQENGTNSLKLSEVTICSVAVINPSSQIVSVRFHPLGKSGRSLVVLTETSLLLYEAGNGVLMPDYEIPLKLTHQASNSFDADVDLHIPTAFCFSNVSQGWGVFTIYILTRGGDVFSVCPVMPANAMIPQDVLKQIRLILTKKEDDADAENHRRNVHWITKLLGEAALANDLSTSFVISEGSSELFDSSDYVSVRRPDDFSFIPSMQGPFLLQPAVADDELIEDYCDIYSFGMNPIDVLAIGGSEGRLDLLLLVSEVSGRWSKLNDHGLASMKLIVSQVHSLYLSNNNPYMVLQPDIQSPYSLIAYHANGLHVVDIESWARDLNLNFENSEFLNNEEENDEDELSNVLVSIPSRTSVLERLDTNPLNESTDAVVGCAQLYYPSLGKILISLTRNWQTTVFDDSDLATMGVNKESLSNEMDYSKSLGTSSLEQVDDLDEKLTYTPLYVSLLEKTPFTDPSIPSLVERTIVPAELQNEITVSSASLRFLGKVVARYRETLNLLDHGCSELHHRLKLQREEYERQQNHIYKLSDRISNFREKAWSTEHLEHLTSDMSMCEKRIDQVLQRVMDLRVPDLSDKEKQFIKEIGNYKEKVTGERGIEKRVETLKTLLQRTKPRDAQTTLVASSSDMRLAAIEQLQKLLAQQSLSIKELKTKTVSFQRLLQTS Q9P3B2 RCF2_SCHPO SPAC1565.01; CHAIN 1..242; /note="Respiratory supercomplex factor 2 homolog C1565.01"; /id="PRO_0000351140" MKLSTPEEVKAFNRNTYSALFKGALVGSSLGIAGWLIGNRYSAGFRRLPFSLKSWLVIGSGSGASIIFADKAGLKFEAERYGKFDQIDYSTKGLPWNQRALYYFNEHKWPIILGTWASTMGLSLYAASRNRYDTAPQKLIQARMYAQGVTVVVLLGSVYLSTLANRLEPLEREVLVTDPSNPTKLVAFKQRKERYPGELQWEVLVSQDEERLRKLNLPLREPHGSTGPMSTPTPALNSSRSA Q9P3T6 RS5B_SCHPO SPAC328.10c; CHAIN 1..203; /note="Small ribosomal subunit protein uS7B"; /id="PRO_0000124539" MAASIIPKEVSLDETGHIKLFNKFPFEGVEVKDISLVDYITIGNGQPLPHTAGRFQTKRFRKARCFIVERLTNSLMMNGRNNGKKLLATRIVKHAFEIIALLTDQNPLQVLVDAVAACGPREDSTRIGSAGTVRRQAVDVSPLRRVNQALALITIGAREAAFRNVKSISECLAEEIINAAKGSSNSYAIKKKDELERVAKSNR Q9P3T9 BSD2_SCHPO SPAC328.07c; CHAIN 1..277; /note="Probable metal homeostasis protein bsd1"; /id="PRO_0000364024" MSTNSNQNSIHTPIPEFPENRSTNRSELAAAFEPPDDDVEYSETAPLYSSARASIEGEEAFYQHLSTPDPGNDSGHVRSSNDRIPSTSSNHADGHHVDSVFSNLSAKPTVESNTEELEEEPPSYEQAAADTAPPYWDTTMVIPDYGSNEIYIDGMSVGTGFSFVWSACVAILFPFVGFLVTYVLSTTHLGRYGAQIGLSLTLFQRGYIMISESGMENNDDQYNYDELPHQKLIGSILIIIGWCLVLVDTFGFIRIRRMKNAISRTDSPGETSPEEVV Q9P3U1 GBP2_SCHPO SPAC328.05; CHAIN 1..464; /note="Serine/arginine (SR)-type shuttling mRNA binding protein"; /id="PRO_0000310815" MPKPIEWNEFDSGMGSKLDVSSSLNSSSSNMDRDRSESPKRHVNGSNSLKRGLHFDGEHTERDPHLGNGQKYTQQERRVYVGNLSYQVRWFELKEFMGQVGNVLNCEILNLPNGLSKGCAIIEYSTAEEARTAIKTLSNQKFMGRLVYIREDREQNARFGSSSVSPSASSNGKDSEPDRQLFVGNLPYNVRWQDLKDLFRQAGSVIRADIQMNQEGRSRGIGIVVMSSMKEAMHAIQMLHNTDFMGRTLEVRLDRFAHHKSKPYSTHGNGYTFPAEMQMTTSSTYLPMLGANTQVEDLVYHAYPHGPCSDCIYVGNLPWATSDRNLLDLFTDIGSVIRARIAYEPTGRSKGFGVVQFENENDAASSIEKLNGYRYGGRPLQLSYAHYATPLPAVPTVLSGLPSVAYTPPVMHIPTTNSPLTPQSFTNSFLGYLPISMPVANMPAIAPISVALPENNIEHSLEPS Q9P3U2 YKX4_SCHPO BINDING 499..506; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC328.04; CHAIN 1..741; /note="Uncharacterized AAA domain-containing protein C328.04"; /id="PRO_0000374025" MSLEDCYNVTQSYAAVAIHKEQTADYVEAIALFQKAKRNILMNPEFKYARERLHVMDYEDRHYVETLLCMLEQLTIRIEFLTKEIAQQEAAYKDIQNTQKSLVTQSSTGSANVAYISGNGPGDRSFIDDGNYSASSFERQNRTAPLQSKVTTASLKPNIPRTSMSSSPTASRTSLRKGAGELETHSAVKSAKKASVKSKSVLPPSKSLARTGLPAEVSTQNNANRAALLAWGSLNSSKPKHALPPSYISSEAAQASRSSFQVERHRPTPDNSAVIEAARRTYSSISSSSSPFKKKTQSHLPNRTTEVPSISKQLSKSSTSIATVAPSLASVSSVTKSPSPTPQSAPRAQSASTETAQDLDFLTPPRLSVNNPFLSDLYPASEQGLSSCEEKDSPVDGDEFFNHTNEEEIIEKQFQSTSISAMTSEKQEQILRECPDIDEELGKSILREIVVSGDEVHWDDISGLEFAKHSLKEAVVYPFLRPDLFQGLREPARGMLLFGPPGTGKTMLARAVATESRSVFFSISASSLTSKFLGESEKLVRALFTLAKKLSPSIIFVDEIDSLLSARSSDGNEHETSRRIKTEFLIQWSSLARAAASRQTADHPRVLVLAATNLPWCIDDAARRRFVRRTYIPLPDETTRRLHLNNLLKYQKHSLSLEDIEAIVKATEYYSGSDLTALAKDAAMGPLRSLGESLLFTKMESIRPINLDDFKTSIKVIRPSVNLQGLERYSEWDKEFGSQGH Q9P3U7 GHT8_SCHPO TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000255" MOD_RES 519; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 523; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 526; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 527; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 528; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 529; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 537; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC548.06c; CHAIN 22..547; /note="Probable high-affinity hexose transporter ght8, mitochondrial"; /id="PRO_0000310744" MGKTLTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRFADRYNPVTDTYSYSSARQGLITGMVNVGSMTGCILSSPLMDRIGKRVSIMFWTIVYLIGIILQVTAVPSWVQIMVAKIWTGLAIGALSVLAPGFQSEVAPATLRGTIVTTYQLAVTGGIFIAACINMGTHKLHKTAQWRVSMGINLLWGIIMFIGISFLPESPRYLIAIGKDEEALDIMCKNNVLPREHEIIQTEYHVIKTDCEAEMAGGPATWGDILGADIRYRTFLGLGVMSLQQLTGDNYYFYYGFEVFEGTGMNSPYLSALILDAVNFGCTFGGLFVLEFFGRRMPLIIGGVWQSITFFIYAAVGNRALTRKNGTSNHRAGAVMIVFSCLFIFSFAQTWGPAAYVIVGESYPIRYRSKCAAVATTGNWLWGFLITFFTPFISDSIGFKYGYIFAACNLCAACIIFLFAHETKGLTLEEINELYLSGAKPWMPRPENLGQAAKQQQEVLEKSRGVQGESAAHLENVDNEGMEDTSSNDITSSTSSSEGRAKPESNYVDEQDRYA Q9P3U9 URM1_SCHPO PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4. {ECO:0000255|HAMAP-Rule:MF_03048}. MOD_RES 97; /note="1-thioglycine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03048" SPCC548.04; CHAIN 1..97; /note="Ubiquitin-related modifier 1"; /id="PRO_0000330335" MAIKVELLGGLDLLFNKQKALSLSLSNLGSTKLGSLIDYMAQIIEKPSQKDLFILNGTVRPGIIVLVNDQDWELLEKEEYNLEEGDEVVFVSTLHGG Q9P3W6 YLI2_SCHPO MOD_RES 342; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC458.02c; CHAIN 1..468; /note="Uncharacterized protein C458.02c"; /id="PRO_0000372367" MSSHKPVRPNEALHKEALEELDAKINEAKKRFNEHKEKLGAIRGGGSLQEKNAELRAELDNIRNAQAAIRSSKQTLINKVKAQDELLKKKVKELTAMKKTVPFKSEVELDKHVKQLQAAVDSGTLKIVDEKKYLREISQCNRTRKSFVELNALQTSIDTIRNELNELRDQLNDSESKKLSDKFVEIRSELDEVRKQQDGYYKDQRKLIAERDDEKTALDDLYNQRRALQREYDTQLRAFRTYEREQRAKRQEQFRLERENREKEKRRIAAQRKLEEASIPAFTEEILACENLLKVFHVPVESSTTNAVSTGNTSSKILKPRTLTPRTVDPIPEGTIIKKESSDDAMFSGLKKSKPKKSNKSNNNQADSDRLNLSFGTIKEFDFVGVPAPFTKSQVDSAVEQLKSRIAHFKEQQDSVTKQRIEKAKQEIEKLEAKYNSKEEKTLTEADMVISSEETVTVTNDLEVEATA Q9P4W1 COX8_SCHPO TRANSIT 1..17; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC24C9.16c; CHAIN 18..66; /note="Cytochrome c oxidase polypeptide VIII, mitochondrial"; /id="PRO_0000006172" MLRYSLQARSALRGVRFSSSHSAPKPGSTIPFYINKKPLPTLLYFGTFGVIFSIPFIVVKYHNRNL Q9P4W7 APC5_SCHPO SPAC959.09c; CHAIN 1..744; /note="Anaphase-promoting complex subunit 5"; /id="PRO_0000064624" MQSPAMSMVTPIFPIPLKTNSSKKNFYTTFLTPHKLTLCLLIELYAHRIIQPQHCVPFLDLVLGYFNPNDSQPQTLTRIHDITSHLPSSIEEYSVYSLLHERLWSLHSFEDIHEIFISLGNYIEGVYDSEEEAPHMLFSSSSLLSIFLRKCVVEYEQFSFEQGVQFFKSFLQYRAPSMDFQHEGIEFCKINVRHELMNLASNKTLLQLAFGSIPVSRSSRDIEQLTQVQIEHMQKFGCALPLEMKEKLHDLLEVEENNLNTSYYCKFLNSWFSGDYQQSVENLCRYFDHIMHSDEKVSYQYALLNLAMLQADFGCNEEALHAIEDTINTARESGDTACLNFALAWMFEFKRSQYSNPSPEKNENDDQILEHLARNSQKAQLPILQTTVHLLQVQKFLDDGSSLIGVFSNLTKAFALFCANESFDGFPRYMDLLQSIWYRLGCSILSMTYISIYQKNHVHDSPALDLLQSLITKAWRYAELGRWLDVATILSTAEVQSQRSFQCAHLYGREKTFIYLSKAIDEKNHMDATLYLKNLNGFRHDKMSTFRTQLYALRLDISLGNLSQAIEGIDKLLEEPEKLAIEWVLQLMFLKVDIYMRTEMSNRAVFELLEIIQMASSNYLRLYLLRGLCTLCLIGELDCFTAIDLLDSLIPDIIAADNKPLLALAFHAFASLQIKHLDLLQPSRMFVIQLLDSAIDGYRACYMVEMQKTVVRLKIQYLRQINDPALQPNIEQYCSRFYSDNLLN Q9P4W9 RS4C_SCHPO MOD_RES 194; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC959.07; CHAIN 1..262; /note="Small ribosomal subunit protein eS4C"; /id="PRO_0000130841" MVRGPKKHLKRVAAPHHWLLDKLSGTYAPKPSPGPHKARECLPLIVFLRNRLKYALNGREVKAILMQRLIKVDGKVRTDSTFPTGFMDVISVDKTGEHFRLVYDIKGRFTVHRITAEEAKYKLCKVKRVQLGAKGVPFLVTHDGRTIRYPDPLIKVNDTIKLNLETNKIESFIKFDTSAQVMVTGGRNMGRVGTIVHREHHLGSFEIIHVKDALDREFATRLSNVFVIGETGKSWISLPKGKGVKLSITEERDRRRALKGLA Q9P4X1 YKV5_SCHPO CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; SIGNAL 1..22; /evidence="ECO:0000255" SPAC959.05c; CHAIN 23..632; /note="Thioredoxin domain-containing protein C959.05c"; /id="PRO_0000303923" CARBOHYD 35; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 41; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 140; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 557; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 209..212; /note="Redox-active"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" MKLFLYHFTFIVYYFIISFSYAFSIKQEIIVSSHNASSILNTTAFWFVEFTESKYDKEEFSVIWNEVSMEFPDIRRAKVFCDLDLEFCAQQEIYDHPKVVVLKNGMWMRHVLEKNQITTKSARQFVKSHLGNCDLEQAENETDCFSDDGEYNSDSSSTDPAFELKEDQSWKHSSILRPLETLNFKRFLFGNEIMSKTRAFVMFVSLKHCEDCFHWEAVWSSITRNTDERLKMAQVNCDEEKEMCNHFHIKKFPTFRVFQGFDSIQYNGPLKYQQLLSYSNQVASYQAIKIEEGDIESIENSHPVFFLVLYDFATTSEDFSIIERLKLQLAGVAPLYICNSKALANKYGAQSQPSIIAVRNGMPIVYQAITPREFRDYKRITEWINIVSSPFITELTPTKCHSLLNRKLTVLTLLQPDSEQFFSSQEELLRLGKRWFRFQMQRQRNDIVWSRIKKYSAIAEAKKKGFARKVKRIKYSKISHPTYTESVSFLWLDSSLWLDWIVENLDHTVYVDSITPPVFVIDHSKGVIYVSDRNGNSLTLEEDSLFSTLRIILEHPNSSRLQKLRAPGLCPNGSPNYRNRYKLIVFNLLIALLILSILTIISASRLSRRRRQLLNKQPVFGFYHSLVIAKSD Q9P4X2 OMH6_SCHPO ACT_SITE 220; /note="Nucleophile"; /evidence="ECO:0000255" SPAC959.04c; CHAIN 1..298; /note="O-glycoside alpha-1,2-mannosyltransferase homolog 6"; /id="PRO_0000316588" MYFLILFSSNAELGEVLRTMRSVEDRFNKRFHYPWTFYGMDEFTEYFMSTTSTIASGHCEYGTKGITYTNHLQFILTISYLVHWDLSQVKPLVENNRLYQQRADALAQENLSYVYSPLFHSFQDWVVRSLLYHPQLEYDYVWRIEPGLKLVCEEKKDIFSTFKDSDIVFTNHVCERKHSGIYAMEEAIEEYKILNTQGDFSNIWVYSNNYTYCKYWPFNEILSLKQIRHNQTYTNLINYLLGSGGTYYHRWTESDILSAAFGVLRARANHMESVGFFLNDDVHYCPETIPYTGRCACL Q9P4X4 SEC17_SCHPO MOD_RES 76; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC959.02; CHAIN 1..289; /note="Probable vesicular-fusion protein sec17 homolog"; /id="PRO_0000219075" MIADPDQLMQKAAKKAQGTGGFALFGGGNKYDEASELFLDAANGYRLQKQGSAAGYAFEKAAEMQLKTDDKDDAASTYVEAFKSYRREKPSEAARVLQIAIELFTRRGNFRRAANYKMDLGDIFEQELQDTKAALGAYEDAGEWYSSDQADALANKAYLKAADLAGLCGEYSLAIRKFEQVARASVQNNLLKWSVKDYLLKAGLCYMANGDEIATRRALEHFLEIDPSFASTREYQLLKDLQDTIEASDANMFADKVFTYDQLSKLDSWKTTILLKIKSSIQEAEDDLT Q9P544 VDAC_SCHPO BINDING 11; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q60932"; BINDING 19; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q60932" SPAC1635.01; CHAIN 1..282; /note="Non-selective voltage-gated ion channel"; /id="PRO_0000050523" MAPPAYAAINKLCNDLLQRDFPVGATLLSVRTTAPNGVVFNVSGNQDAKGVISGKLETSFNDKANGLTISQGWTTANVLESKVGLSEQFAPGLHLNVNTTFSPATAAKTAILNLEHQHPLIHTHASVNALERKFLGDFTVGHEGFLAGAEFGYDVQKGNVSNYAATIGYLASPLSVALQASNNLSVFRASYYHRVSSDVEAGGNVTWDAASTANAITLELASKYALDKDTFVKGKINSAGVATLSYFQTVRPGVTVGLGLQLDTQRLGQPAHKAGLSLAFSA Q9P5M9 MUG14_SCHPO SPBC359.06; CHAIN 1..257; /note="Meiotically up-regulated gene 14 protein"; /id="PRO_0000278493" MAKVTGLPEFEDLHTKRKWMLNHMAAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDMDDVISMPEEGRRTAKGLADYKAVLVQNHGIMTVGTTVDEAAYLLSLMERSCQIQLLIDSATKVGERKHVHPTRAKAIRENADNPVGLYTAQQPNFLYEVACSNGELEII Q9P5N1 PFL7_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPBC359.04c; CHAIN 24..358; /note="Putative cell-type specific agglutination protein pfl7"; /id="PRO_0000353814" CARBOHYD 67; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 88; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 112; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 136; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 245; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 305; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MNSLKSLCLKCIVTLCLLVNAFAFDYASLQEQDENLLAACPQYITIYTNGPVPGTTTIYPTSNVASNTSENYPYTGSKSLSSSSILSNSTISTSSSTPITASVPTSSSILSNSTIPTTSPVPTTSSTPTSSSILSNSTIPSSSSISASTITTTIISGSTQFTTTFVDQSIDTVEVVIPTAGYITTTLTSGSSYPVSTTTLQTVSGTQSGLVEVITPSCGCNPENSFHLRLVGDSINPSYVYKNTNVSDPDEGNMYTSTEGNTEAVNVFYYDPTVERILTCDCVRPVYTIYTDDPDSSFDIIKNNNGTFTFVESSSGEIQTLHVSQYGALWITSPEYDGETGGMDDVGFRADDVILVAY Q9P6I0 SYNM_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; SPBC1198.10c; CHAIN 1..441; /note="Asparagine--tRNA ligase, mitochondrial"; /id="PRO_0000315955" MNKFQLPKTLKSLWHHPHNGELISINGWVRSIRKLKNVCFAMVSDGTCQQALQVVTSPEQSKKLSYGASVNIEGQLAVSKNAKLGLQQYELLAEKIKIYGQINDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFTLTPQETHKNKSFERDDQKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEVAFMTSLSQLTSLMEDMIKYTLNSLMEQNYHRDHWDQLLKPWKCMTYSEAIEELSAVKKTWKYPPKWGNDLSSEHEKYLCEILHKTPVFVTDYPQKIKPFYMKSSGPDTVAAVDLLVPQVGELAGGSLRKDHLDEYKTYPPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGENTNVKETIPFPRSVGSIFA Q9P6I1 UBC16_SCHPO ACT_SITE 90; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388}; SPBC1198.09; CHAIN 1..160; /note="Ubiquitin-conjugating enzyme E2 16"; /id="PRO_0000082590" MNSSIKRLHKEYASFQAGDISGLLLLKPVTDVDMFHWKAVIEGPTETPYEGGQWVLDIHVHEGYPISPPSVYFQTKIVHPNISWTNGEVCMDILKTHWSPAWSLQSACLAIISLLSNYDASSPLNVDAAKLLRTGDKTAYNSLVRCTTYLYAKGKIEDLS Q9P6I3 YHG7_SCHPO CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.; EC=3.2.1.101; SIGNAL 1..19; /evidence="ECO:0000255" SPBC1198.07c; CHAIN 20..442; /note="Putative mannan endo-1,6-alpha-mannosidase C1198.07c"; /id="PRO_0000012130" CARBOHYD 75; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 124; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 193; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 229; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 254; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 257; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 356; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRYLSFFFEFFFLFSFAFAFDFDVTSDDSINSALTTVTDGMLNYYQSTSHTFTAYWWMTGAGLNSMTDTYAATGNTTHLDMLISALVANKGDNNDYAPNSEKFDLGNDDQGIWGLSAMSAAEVNMTTGDSSASFTELAQAVFNEIMSRWDTSSCGGGVRWQIYSFNNGYSYKNSISNGILFQLAARLARYTNNDTYVDLAQKVWDWSTTVGFVDLDDYTVYDGASVTSNCSSITNEQWSYNVGVYLAGTAFLYNYTNGSSVWQTHMEGLMNKALDYYFTSDKIIYEPSCEPTESCNSDQTAFKGMLARFLGYTMQLAPYTVETILPYIQSSAEAAALACSGGSDGVTCGYMWYWNNGTWDDHYGLGEQISAVETFQALLAQQSATILTLDTGASSESNPDAGTDDGDTVTITPATKSDKGWAGFLTFAFSFVFLLFSIWLYF Q9P6I5 KGUA_SCHPO BINDING 25..32; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" CATALYTIC ACTIVITY: Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780, ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.8; SPBC1198.05; CHAIN 1..202; /note="Guanylate kinase"; /id="PRO_0000170654" MTPQLSSSVASKLVTLKLKPVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKPGNFDALIVNDDVEKAYKQLEAICLSD Q9P6I8 YHG1_SCHPO BINDING 74; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 97; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 127; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 130; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 133; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 141; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; SPBC1198.01; CHAIN 1..423; /note="Zinc-type alcohol dehydrogenase-like protein C1198.01"; /id="PRO_0000358878" MEYLTNLKTNIMDKQLGHREVSEGSTQPKPDPSGATMKACVWDGPLNVKIAEVPKPTITHPKDVIVKTTACTICSGSDSHIFSGEMPGIEKGAILGHESCGIVAEKGDEVNNLEIGDRVVIAFDLACGQCSFCKRHEYAACDTTNDSKLMDVNYGSHHSAIFGYTKLLGDVPGCQAEYIRVPFAEINCCKLPDDIPDSEGLFMSDVLCTSLHACTLGEVKKGDTVAIWGMGPIGLYAGRWAQILGASKVIGIEVVPERIELARQKFGFTVIDRNEVSDVPKKIMELVSNGVDCAIEASGFRFSTSILHKVERAVGLETDSPDMITECLNAVRKYGHVSIIADYVGTSNQFPIGHVVMKHLTIRSGQCPCQNYFGYVIDNIRSGKIDPRWMVTNKIKFDDLPDAYNKLFYKEDGYVKVYCDMTE Q9P6I9 YHDD_SCHPO MOD_RES 598; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1683.13c; CHAIN 1..618; /note="Uncharacterized transcriptional regulatory protein C1683.13c"; /id="PRO_0000115011" MQMKPRQDKKNQEIFRISCQRCRQRKIKCDRLHPCFQCVKSNSQCFYPEDPIRRRAPKEYVEALERQIAFFEAFVKKLAKVGSDEQSLMIQDMNNKIVNEGNEYDQTPDISARKRRKHFRMLPQNNFRYFQFYGTTNVISASNLTTTSEIPTFKFPIFSKRKYNDTENLYEQPFHLEFDTCQELLSLFFLKQYHNFMFVFRDYFIRDFELGGGPYYSQWLLFAICSIGAMISPDDDLKNLSNTLANIAEKWVLDEGLNSPDITTLQTLLVLGIREIGRGLTFKGWLFSGMAFRLVYDMGLHLDPDHWDHSEESRIDREVRRRCFWGCFTLDKLISLCYGRPPGLYLKQTDVRNTTQLPYISELDEPFEIFNKKSELFAAVSAGEDRRGLVQFWLNQVELCKIIHRMLTEVFEDRTSSVLEASINNIHTELQKWIADIPMELQWNTRSQKETSSTVLLLHMLYHSVIIILNRPSDDNYLKLDNTERYTFEICWKSAKTIVQLLKIYFKKYDADCLPMTFIHIATSAARIILVKLNENIPEDGDVCNIYLEIITNALDVCANVWPLASQASRAILNAYKSCATSPKENNEDSLPLQRSPSLDDVSRFDSLDYIFSPNVKY Q9P6J1 ACEB_SCHPO CATALYTIC ACTIVITY: Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361, ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30; SPBC1683.11c; CHAIN 1..518; /note="Mitochondrial 2-methylisocitrate lyase"; /id="PRO_0000314754" MTTDMDLEQLEYEKEVEEIEKWWATPKQSQIKRPYTASTVAVLSEVTKAYYPSSQQALKLYDLLREHRNKGTATLTYGVVDPVLASQASKAGLETIFVSGCLCGLSSVDEPGMDHADYPWDTVPKAVDRIFRSQNWHARRQKQFHLMKPAEERKQLPKYDYLLPIIADGDMGFGSVTSTMKMTKRFVESGVAMIHLDDLAIGLKRFTVGQGRTVVPTSEYLRRLTAVRLQFDIMKAETMLLCRCDTDHAEFITSVVDPRDHAYVLGATTKIESLIKALKDAESTGVSMKKARENWIERAKLMTFDEAVKSTATPKEYENYISAISKKPFHSISERQELAEKYLSNEVFFDWELPRSSDGQYFFKPTVQTVIERAIAAAPLGEMTWARMDYPKWQDIKAFHEGVRAVYPDRMFAFGFTGNYDFKAAGFSEEQLRNLTSDMAKLGVCWQVQPYFTCQVLNKASVDYSNIWKKDGIFGYVKTVQEPALKEDVDGFENEWCGTYFADKLLSAAGSSDKTIPY Q9P6J4 YHD6_SCHPO ACT_SITE 239; /evidence="ECO:0000250" SPBC1683.06c; CHAIN 1..310; /note="Uncharacterized protein C1683.06c"; /id="PRO_0000316595" MKIIIDTDPGQDDAITALLAIASPEIELLGVTTVAGNVPVSMTTRNALQMLDLAGRPDIPVYAGSNKPLLRAPITATHVHGASGFEGAVLPPPSRKENEGHAVDFIIDTLRNNEPGTITICTIGPLTNIALALNKAPEVIQRAKQIVMMAGAFSEVGNITPAAEFNIYVDPHAAQMVLSSGIPIVMMPLDITHQLHTSAKRIARMEALPNRVGPVVAAWLRMEKAYEAKKYGTDGGPLHDPNTVMWLLRPDIYSGRKVNVQIETQSELTMGMSVVDWWQVGLLPANVTFLRTVDDDEFYEVLIERLGRLP Q9P6J6 BGLS_SCHPO ACT_SITE 225; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; SPBC1683.04; CHAIN 1..832; /note="Putative beta-glucosidase"; /id="PRO_0000363374" MMEHDVEDLINQLDISEKAMLLSGTDLWHTAAIPRLNIPSIRLSDGPNGIRGTSFFNSSPSACFPCGTALGATFDKKLLFEVGEYLAEEAKAKGVSVVLGPTVNIHRGPLNGRGFESFSEDSTLSGLAASYVILGLQSKNVQACIKHFVCNDMEDERNSVSIDVSQRALREVYLMPFQLACKYSNFKSLMTSYNKVNGEHVSQSRILLDNILRKEWEWKGTIISDWFGTYSLKKAIDAGLDLEMPGKPRFRNVNTIQHLVGSKELSESILDERAKNVLKLVKHSWQNTEAENHCELNNDSSCLREALKKFASQSIVLLKNKKKLLPLSRKGTFAVIGPNAKVCNYSGGGSANLKPYYTVSMYDGIAAKIDGVPEYALGCHNYLNLPNIANLLVNPRTGKHGYVAKFYLEPATSENRTLIDDYDLEDGVVRFYDYCNDKMKDGYFYIDIEGYLIPDEDAVYEFGISVFGTALLFIDDVLLIDNKTKQTPTNHTFEFGTIEERNSIYLKKGRKYNVRVEYGSAATYTLSTNLSPSTGGRYSIGCVKVIDPETEIDYAVRVAKSVDCVILCVGLTAEWETEGEDRKTMTLPSLSDKLVYSILQSNPNTVVVTQSGTPIEMPWISEAHTLLHIWYNGNELGNALANIIFGEQNPCGKLPITFPKKLKDNPAYLSFRSSRGHCVYGEDVFVGYKYYEAVEREVLFPFGYGLSYTTFELSNLYLKNCGERLRIDLEISNTGPMSGAEIIQVYISQIVRSVNRPVKELKEFSKVVLCPKETKLIRIELDIKYATSFYDELNEKWCSEEGEYNVLVGTSSKDIALTGKFTLPKTIHWTGL Q9P6J8 YHD2_SCHPO BINDING 17; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255"; BINDING 19; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255"; BINDING 197; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 278; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 279; /ligand="substrate"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000305}; SPBC1683.02; CHAIN 1..339; /note="Uncharacterized deaminase C1683.02"; /id="PRO_0000316220" MTDIERFIEKLPKAELHLHLEGTLEAELKLKLSHRNKIPLKQSSIEEIKESYNFHDLASFLEVYYEGVELLLHEQDFYDLCYQYLRKAASQNVVYAEMFFDPQLHTRRGISFETVIKGLIRARDDAMRDFHIYSQLIMCFIREMSFENAEETLNASLPYKSEIIGIGLDSNEENNPPIKFLKVFQRARQLGYRLTCHCDLHQKNTTTHIRQALEDIGVERIDHGINILDDPELIKLALERNIPFTVCPFSNEIVYPGKAQPEIRIMLDTGLKVTINSDDPAYMHCFYITENFNLAQKGASLTKKELVQICRNSFEAAWISEEKRNHYLEALNSFASAYD Q9P6K4 YLF7_SCHPO MOD_RES 573; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 590; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC30C2.07; CHAIN 1..842; /note="Uncharacterized protein C30C2.07"; /id="PRO_0000304039" MLHFLFHSGSSSNRNSSPKESYELLHGLDKQYQSTKDVTFRLVLVQDIGDRKKTVLFDSNHVDGQKGDSVLRDSANAPLTDLMFGAIPISHKGTTTKLHILHPPNPATRSYMLTQLFQINTHGTVVNSSHETIASATSLFENSSSNFSEDPNKPNSSDAFESNKEDSPLLKSFNDSAIPENAANLSSSSKNMKDSTLSSQKARSNTSSSFLTPLHEQLESRCALHTAAKDPFRSKNSLRCNRGHSPLSSQQILPAISNNTSEKPDSNNCGFLLPSNSTSIKDLKNVKKGNRLNSPPFITIPQSIKNTNSNFLLSSPSLFSDTRTRPASYALALIITVPYEYDEIVHPVSTYYTMLSNFTLSLQKEIDERIRNLLFVSLSSGGDNKNDTGIPLIQSSSSKVGFGPYALSKDLITAKSFHKCILLLKTGFSAPLIKPSVFSGSKWVENMRLLTDLCKSPAQKCLFSNLLTATRKFCLERQKDDVTFKVLLQSSKAPIARRFLYLLAPLMRPSIAQCSDTLLNPIQLYPNSGILSSSSLSTSFGCPSVSGSLRVPSYDMKINDSCKAIDIHSEKPSFADSPRKTSLRNYLSSSWRLKFMRSSYQNNETDPLNPTSGSFLRQPMQYSSPSGVSESAASSFLDIENIDEYLESAENMKYLPRSTVGPGGMLHVDLLETNAKQESEATTSTVPPSPSQVGFLKALHPSFDLQAAPPNSYVSFSDDDFISATLLYMLEDVSRNKSQLLAEKKHLKSQLMVANLDTYSLDCYEIHEFPSEWENDYAPFLLKEHHKVIGETYVSSFDIQQGCFNVIKRRLSSYKWDKSDDSFVSEVLKGDLKEVLRVCSHC Q9P6K6 ERV14_SCHPO SPAC30C2.05; CHAIN 1..137; /note="ER-derived vesicles protein erv14"; /id="PRO_0000315909" MMSFGSFVYIACLLLNGANMLLQIFCVIMFSDLEMDYINPIDLCNKLNDLVMPEIISHTLVTLLLLLGKKWLLFLANLPLLVFHANQVIHKTHILDATEIFRQLGRHKRDNFIKVTFYLIMFFTLLYCMVMSLIQEE Q9P6K7 ARC1_SCHPO SPAC30C2.04; CHAIN 1..450; /note="tRNA-aminoacylation cofactor arc1"; /id="PRO_0000317099" MSFLWAKEFCVLKYPYKLFITHKFSYLLRFETVTLNNIRSPQFYAKLTFSHHQPTVSGTMSTELKFISKYLQISIPETKEGPVSSLFKAVSEQKPELLGNTDFEKAQILEWTTKAFSPIETQSIVEQLDEFLKSSTFIAQDSGISVADLAVYARIHSYICGLSAKEGYKLNNVCRWFDFIQHQESVMEAANSMSMKLANIDLNAPKIQRPSVIKKDKKEKKEGKPSQEASVKSVEKAPKGLEGAKKEKQNKKEKKDKKDKKDKKEKAPKEPPKAATPVPSMIDFRIGFIEKAVKHPNADSLYVSTIHCGDAEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFCASSPDKSVVEFVLPPENAEIGDRLTFEGFDTEEPEAQLNPKRKIWEAIQPGFTSGEDLICGYKDESGLHRLFVKGKKDLGFCKAQTVVNGTLS Q9P6K9 DOHH_SCHPO BINDING 65; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 66; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 98; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 99; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 227; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 228; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 260; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101"; BINDING 261; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03101" CATALYTIC ACTIVITY: Reaction=[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O; Xref=Rhea:RHEA:14101, Rhea:RHEA-COMP:10144, Rhea:RHEA-COMP:12592, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:82657, ChEBI:CHEBI:91175; EC=1.14.99.29; Evidence={ECO:0000255|HAMAP-Rule:MF_03101}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03101}; Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03101}; SPAC30C2.02; CHAIN 1..318; /note="Deoxyhypusine hydroxylase"; /id="PRO_0000283672" MSSEPVPQAVIDELERVLVNLDKSNPLSFRYRALFSLNALAKKGDKRAVDAIYKAFIDDSELLKHEMAYVMGQSGQQYAVQPLINIVNDLDQQVMVRHEAAEALGALGFTESLPVLEKYYKEDPLAPIRETCELAIARIQWKNGLDKNNEKITPSMYDSVVDPAPPMPDHEQDVKSEVAKLRSEIVDQNLPLFYRYRVMFRLRNIGNEEAVLALTDGFKDPSPLFRHEIAFVFGQMIAPASVPALIKVLENTEEVPMVRHEAAEALGGIANDECLPVLKKFSKDDVRVVAESCIVALDMIEYEKSGDMEYAYIPKVSA Q9P6L2 RKM4_SCHPO BINDING 301; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" SPAC688.14; CHAIN 1..468; /note="Ribosomal lysine N-methyltransferase 4"; /id="PRO_0000303948" MLKQAESMLKWAIEKDNYTTSEKIGLNDYRHVHESLGIGFIALEDIKEDEKLVSFKKDSVLCLTNSDLAQLPEVQSLPSWAALLLVMATENASPNSFWRPYLSIFPTKERITSPFYWDENKKDALLRGTVLESNEDCNEITQLWIDRIEPIIKLYPNRFSQVSYEDFLRMSAVMLAYSFDIEKTKSPISNENEKSAAETSIKEDKNGDAAKKNEGSANQDDEKLHSQSLVGNNCEVNSEDEFSDLESEVDPDELEKAMCPISDMFNGDDELCNIRLYDINGTLTMIATRDIKKGEQLWNTYGELDNSELFRKYGFTKKKGTPHDFVLIKKEHWLPEYIEKLGFEEVEARLELLCREELLYNLEGDFTFSKADLTFKEICLAFVLMEKEKELISVPSKSDIKPKHYRKLLKIIEKRINMYPKISDPKNFDEENAKTLIEGEIDILQNLSAKVKEALTKNRPKKKQKVDH Q9P6L8 SRB8_SCHPO SPAC688.08; CHAIN 1..1134; /note="Mediator of RNA polymerase II transcription subunit 12"; /id="PRO_0000072182" MSNRDSANPPGFNDAVPLAICYIDSSTSSHDEYLTLLQSKVSAPDKNFRDETVDGAPFLAGDAISKGHRYSPPVRSDRASAQGLLQQHLEKSSTLENLKRYSSTLLGRQNDAVIDEPFAPFRPPPRVTLSESRRDRWLQGLSDPMVPLSSLIKTIPHGLWGEDILRMLVKFRVPFTRAIWFIRCAGVNEARSFLRKVQTTDITEWVKNWTDVAAGFLISFISSFLNADIYSFADDYTYLLKLFGRLLAEELVSPKHFLLRIVSFSGDSSLKSFSLHFFALQFFSTSLIQYTHICRKCVITILQSYQQLIVDQPANLLKFSLLSKKVSHFLFTLAQKNIESFFFPTEWDKLKPTIILLWKDFPNYSTLLSIMQERNSKAMYMYKPVTSSIRFLQIISCLSFPVGWRTLAKDLFKLLPVYTGVPLLLHWCINCRSIFSGDRNFIVSSIFDNANFDRNLIVDLTLSFVLKLHPLEYNECVAAAQLLDHLAACGYFFFSKYIARLASLGYLRESMLNSSFMDDQRKILVQLPILRMSQQLKNKIYYILSKGNYFVDWSICDEYVKRFKEDHFSFMFKKEENYAIITLSLVKIASTPMSKLYEDYLVMLFAFHYSMFQVMTKLIADNLVHFSFQSCACQTLFFICSVVPKTESQKLLLNEMGKLFQVELNFSYDSPDVNLLIEQFYEITSYESNYDDAFVEYKDATVANRKDFIEFLFHNITVSSKHTAVIFTSDLLMVLKIALNHPPYFDDLATTTFSSLLKRDECTILSFFKILQFYGCKLLSVDQIWAVVSDVYEAQDNNTTLKQFFNYLLDESTWPEGYLEERHWRSILCKEARKHDSGLKLFKLGIKLCTRNEQIMKTIWSFIHVHDCNVISEVIPDQRFLRTLTEHFMIDLRQLDIVTCLKKALVTLDEFSAPLYATWLTTLDDDELSELTDDVVQKKVLESLDNYKSGIWKLVLSGLPNCKTVFEHLLLFSLEERLDLPAAFLQDLIGASAYVMEQVPDSWFLEKLPCPLTQSLQSFSHLSNHIEVLDSTRQSRLTFLCHLILHMHGFVELTDQLATLESLTIRKCIYRNQELLDLLLFSIHLVKPNVETNDEVCNTLKAWENIESRPYTIDFPEALQQYSPRIVLYEPTFW Q9P6N3 SHE9_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC823.13c; CHAIN ?..317; /note="Sensitive to high expression protein 9 homolog, mitochondrial"; /id="PRO_0000351063" MLQRLSQSIKGFAARFPKIYNKGNGSVQQTILQASQRLNELTGYSSIEALKNAVVKQETKLRDFRLSAAEARKRYIEAVEKRSSSQREVNELLQRRSSWSTIDLERFTKLYRDDYSNKEEEIKAQEDVDVAERRVEEAQNGLVRSILSRYHEEQVWSDKIRQASTWGTWGLMGINVVLFVVVQLILEPRKRKRLVREAVDHIDKERELEINDELKKISEKLDKKGEAVGQALELTSPKIDNKNLPKNSASLILPPINYDTFHSFLDSLKYFLSRFLSTDYRIQLTYRQLSILATKFTVGGGVIIYTFIHLFGLAFKR Q9P6N5 DS1PP_SCHPO ACT_SITE 147; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P0A924"; ACT_SITE 198; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P0A924" SPAC823.11; CHAIN 1..411; /note="Dihydrosphingosine 1-phosphate phosphatase C823.11"; /id="PRO_0000359401" MVHKKKNVDIPSSQKYLGIQHVNFYSNAFGKESLRFQLRELILPIVRKETRLLYKIQSFFRNPWLDVYFMYTATLGTHVFFMLALPIFFWSGCIYYTLDITQLFAAGVYFSGCIKDYFCLPRPRSPPMVRLTLSSDAEYEYGFPSTHTTNAMATGFYSLFLLLSMSDSMSSISYYFLLSLVLLYIASISLGRIYCGMHGFMDVSTGTILGVTLAIFQWKYADFFHNVWSSSSTSVPILSVVLALFFIWFHPQPAERCICLEDSISFISVIMGIDLGTWFASPESLSHLHDNLNSYFLLKFFVRVLFGVCMILIWKSFAKQALLAVLPPIFKSLRLSYLEPKSQSEKGIRAATGSNHSPGNIGTELGVITSHQSHPHPVRFDIETIARIIVYSGIGFLCTYFAPKVFLKWKI Q9P6N6 S2538_SCHPO CATALYTIC ACTIVITY: Reaction=glycine(in) = glycine(out); Xref=Rhea:RHEA:70715, ChEBI:CHEBI:57305; Evidence={ECO:0000250|UniProtKB:Q96DW6}; SPAC823.10c; CHAIN 1..296; /note="Mitochondrial glycine transporter"; /id="PRO_0000310801" MSEIKKTEKLGVKSSKHLAAGALGGFISSTTLQPLDLLKTRCQQSQRDSLPKMVRRIILHEGGVFSLWKGTLPSILRSTTGSSCYFYFLNWLRHFAPQSKNIASSHIQNLWMGGFARAAVGFAFMPVTVIKVRYESNLYSYTTIYSSIRDIWKKEGISGFFRGFGVTALRDAPHAGLYVYFYELSKQNLHKLFDRFSPSSSVQGTVPHRNIVNVMSGLISGATATAITNPFDMLKTRVQLEPHIYKNFLHSAKLVYANEGFRGFLDGFFLRVLRKSISSTITWSVYEWALHRKVIK Q9P6N7 TASP1_SCHPO ACT_SITE 176; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 204..207; /ligand="substrate"; /evidence="ECO:0000250" PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity). {ECO:0000250}. SPAC823.09c; CHAIN 1..175; /note="Putative threonine aspartase alpha chain"; /id="PRO_0000420552"; CHAIN 176..345; /note="Putative threonine aspartase beta chain"; /id="PRO_0000420553" MSNGLVILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMDSESGLTASVACCNCCRHPSEACLYILNKRKVMSQHGLVPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKTQIKWKEILYQNPINLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIESFDNKSHSSTCAVATSGTGEHISNTCFACRSSQLLVSEDNVVSSLNKLINDFHEHPSATLYSDLQVGIIFAKVETSNSHNKRIIFGLAHSSPDMVFGFMKGDHSKPTTEISRKGSKRSSVQLYAERL Q9P6N8 RRP3_SCHPO BINDING 90..97; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P38712}; SPAC823.08c; CHAIN 1..465; /note="ATP-dependent rRNA helicase rrp3"; /id="PRO_0000232278" MAPSEKKLTEDKKNSSLNKKIETSNSSSEKSSENNNGDSQNNEAPKTFKELGVIDELCEACEKLGFKTPTPIQQEAIPVVLNKRDVIGLAQTGSGKTAAFALPVIQELWNNPSPFFAVVLAPTRELAYQISEQFEAIGGSIGVRSVVIVGGMDMVTQAVALSKKPHVLVCTPGRLMDHLENTKGFSLKNLKYLIMDEADRLLDMDFGPIIDKILKIIPHERRTLLFSATMTSKVEKLQRASLHQPVRVAVSSKFSTVDTLIQRYLFFPFKHKDTYLVYLVNELAGNSIIIFARTVNDTQRLAILLRTLGFSAIPLHGQLSQSNRLGALNKFKSGARSTLVATDVAARGLDIPLVDVVINYDIPTDSKAYIHRVGRTARAGRAGKSIALVTQYDLEPFLRIEATIGKKMQEYEIDKEGVFLLSERVGEAQREAIIQMKEIHDRRKSKGKLHTKRKRDDLDREEQIY Q9P6N9 PER1_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPAC823.07; CHAIN 25..331; /note="Protein PER1 homolog"; /id="PRO_0000318589" MRVLRNFTIFFLFTALSLFRQISASAGDLHPVYVSCVNRCIENKCHGNPSDTSKLPLDLKLFRWDCGSNCGYECEITAENYFAAHNLPSQQYHGKWYFIRVFGIQELFSVFFSMLNFMIHYNGYHIMRRCIPDEHPAKRLCLSWAIVGMNAWVWSSVFHIRDTPITEKLDYFSAGAFVLFGSYCTLILMLRLDQLPGGKLLCWIIGVIFIAAFIAHVSYLSFYSFDYGYNMKANVAVGLVQNILWYYYSWSNRNSGLYWTRWPAYIVTSLMLATSLELFDFSPIANLIDAHALWHLSTVPITHYLYGFVVRKCSYDLTKGTFKIKAYDSSR Q9P6P0 TAF3_SCHPO SPAC823.06; CHAIN 1..155; /note="Transcription initiation factor TFIID subunit 3"; /id="PRO_0000343435" MEETQIDELYFSLMRIFCSQTLRAAGIDRTKVSLLNSFTDITIRYIRLLSETAMAKAEVGRRSCCDLGDLRLAMEEIGLLNGSEEDVKTLVEWFNGPQVAELRRVSGFVQDSETQVKPKDWLTSLIQKQIRVSGPERFYETVFSASNEEEDVKDS Q9P6P1 TLG2_SCHPO SPAC823.05c; CHAIN 1..301; /note="t-SNARE affecting a late Golgi compartment protein 2"; /id="PRO_0000210278" MAYRDRTGLYITFRQSYSHHGQRLELSGWDPKEERQSLVHKDNKDNTVIEMDMLAPRWVTVEGEIDSLLLNTRRNINLLDKQYAKHVLPSFSDKTEQENEIQRLTIQITQDFQRCQKLLQVTKAQTNSATGSEALMAKNFLSNLASRIQTESAQFRKKQSTYLKKLRGLNANISPVESKLDETVSDVAISQSTIQQVALMEEQGEDEQAIRHERAVAKIAEGIIELAQMFQDLQVLVIEQGALVDRIDFNIEQTQVHAKSAEKELIKAESHQKNTGRLRFICFLILLIVALIVILAIKLLR Q9P6P2 RRP36_SCHPO SPAC823.04; CHAIN 1..265; /note="rRNA biogenesis protein rrp36"; /id="PRO_0000339880" MKSSSLENGTLANAGVYEDDLDSDEELVSEEEFENFNNEDSEDDEDSNNESKTAKSQLAEIPFDTLLNAQRDLLKEQQKTKIDRKNMKHTEKVDKKFLAKERNTPLKNCQVKNQFLVFAKFDSLSGNLSKDKVKKNYGFLNEYRVSEIQQLRDELKICKDQERAESIRQTLKSLLSKMERHLEEERAERVMHEFRAQEKERVKEGKKPFYLKRNEQKKLIQMDKYKSMEGTKALDKYIEKKRRRRAQKEKKHLPRARPSANSQNK Q9P6P5 BET3_SCHPO SPAC644.18c; CHAIN 1..183; /note="Transport protein particle subunit bet3"; /id="PRO_0000317084" LIPID 70; /note="S-palmitoyl cysteine"; /evidence="ECO:0000250" MSKSKIGEDVYKKVDKVNAELFVLTYGSIVAQLCKDMNYEKVNEELDKMGYNIGIRLIEDFLAKTEWPRCADFRETGETVAKVGFKVFLNFSPIISSVSDDGNTFVLTLDDNPLAEFVELPADARQKLWYSNILCGVIRGALEMLQMDVDAVFLRDILRGDEHTEIRVHLKRILKEEIPPGDE Q9P6P6 RM09_SCHPO TRANSIT 1..15; /note="Mitochondrion" SPAC644.17c; CHAIN 16..259; /note="Large ribosomal subunit protein uL3m"; /id="PRO_0000317088" MQSRFLISPTLIRTFAHHANLTPRKILHDLPEAAHARKQIPLRPGVILVKKGMTNAWDEKTGMQVPLTILQFDRVQAIDVRTKEKHGYYAVQVGSGIRKPKSITKAEQGNFFSHNIYPKMHVREFRVRDASGLVSPGTIFTTDYFKPKQYVDVKGITKGKGFAGVMKRWGFSGGNASHGASLSHRTPGSTGQNTTPSRVLPGRKMAGHMGHRSRTVKNLLVWAVDADLECILVKGSIPGPNKSAVYVTDTINRSTSATN Q9P6P8 YIP4_SCHPO MOD_RES 27; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 28; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC644.13c; CHAIN 1..225; /note="Protein YIP4"; /id="PRO_0000259416" MTDIGKHNTEIEQDEMENLLRMDPVRSSLDVESRAIEPDNIAGESIVETRFTGGDSLDEPIRVTLFNEFRAIGEKLVYVLYPKNAQVLRDWDLWGPLIFSLVIALALALSTDKIERESVFTVVVALIWFGEAVCSLNIKLLGANISIFQSMCILGYSSFPLMIASIVCAFVPLIFIRIPVIVAMYAWTLFAAMGVLQNSNLSNKKLLAVYPLFLFYFSLAWIIFL Q9P6P9 PDK_SCHPO BINDING 296..303; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 336; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 355..356; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 379..384; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]; Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2; Evidence={ECO:0000250|UniProtKB:P40530}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:P40530, ECO:0000255" MOD_RES 178; /note="Phosphohistidine; by autocatalysis"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" SPAC644.11c; CHAIN ?..425; /note="[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial"; /id="PRO_0000259609" MSVLGKTLQEKVNLLAQYPQTGLSLKQLVYFGKNPTPGTLFRAGLFLRDELPIRLARRIQDLQNLSPMLRSMKRISSVKAAYGRSMEEIIELKGVELPKCLPKHARYHNAPKWRSSLMDSEILHNPSLANTHLDSSKGRYFETDFSDQDNGVDCNWPESLLKFNSNFAYLLNTIRTRHDNVAVEIALDIQEYRRKTNQIDNSIQIFLDRFYMSRIGIRMLLGQYIALVSEPPRENYVGVISTRANIYQIIEGAAENAKYICRLAYGLFEAPEIQIICDPSLEMMYVESHLNHAVFEILKNSLRATVEFHGVDSDFFPPIKVIVAKGQEDITIKISDEGGGISRRNIPLVWSYMFTTASPTLTDDPHDIVSANSTTPMAGFGFGLPLARLYTRYFGGDLELISMEGYGTDVYIHLNRLCESAEPLQ Q9P6Q0 MED11_SCHPO SPAC644.10; HELIX 17..30; /evidence="ECO:0007829|PDB:4H63"; HELIX 33..46; /evidence="ECO:0007829|PDB:4H63"; HELIX 51..81; /evidence="ECO:0007829|PDB:4H63"; HELIX 98..110; /evidence="ECO:0007829|PDB:4H63" CHAIN 1..112; /note="Mediator of RNA polymerase II transcription subunit 11"; /id="PRO_0000304078" MTNSDDDLFSEKSTSSDTQQVQNILELEAKIPDILSSAGKCIEAIQLNNSLEDFRKYSKEFLETVEFISTGLRRQALELEKAEVPVVSLQPKKRYASTPLSNLIFDQSSKLM Q9P6Q3 BCS1_SCHPO BINDING 249..256; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC644.07; CHAIN 1..449; /note="Probable mitochondrial chaperone bcs1"; /id="PRO_0000084776" MDNIGAADAATSSGISGLLSGNSFLGAGIGLMGFGAGLAILRRGLISGASLVKRRMLVSVEIPSKEKSYNAFLHWMSTVPKRYSNQLAVESNRQLKMPQNAREKPDKQVANRIFSLVPGPGKHYIKYKKCWIQVERERSNRLQDLTTGTPWETITLTTLSRDRGIFSELLLEAQKFMQSAQKNKTTIYTAWATEWKPFGHPRSKRMLSSVVLESNVKKMITDDVHDFLRNSQWYDTRGIPYRRGYLLYGPPGSGKTSFLYALAGELDYDICVLNLAEKGLTDDRLNHLLSNVPPKAVVLLEDVDSAFQGRERSGEVGFHANVTFSGLLNALDGVTSSDERIIFMTTNHPEKLDPALVRPGRVDVKAYLGNATPEQVREMFTRFYGHSPEMADDLSDIVCPKNTSMASLQGLFVMNKSSPADAVDMAKELPDNPPSTPFSFNVHRKSLSV Q9P6Q5 DUT_SCHPO BINDING 62..64; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 76..79; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 130; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 135..136; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC644.05c; CHAIN 1..140; /note="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase"; /id="PRO_0000182935" MSFFVQKLSEKATIPTKGSANSAGYDLYAAAECIVPRRGKVLVDTDLAIAVPEGTYGRVAPRSGLASKHSIDTGAGVIDADYRGHVRVLLFNYSDVDFPIKVGDRIAQLILERIVNPPVILVESLEATVRGANGFGSTGV Q9P6R2 YOH8_SCHPO SPBC13E7.08c; CHAIN 1..429; /note="Uncharacterized protein C13E7.08c"; /id="PRO_0000316238" MSDSKEDIRNGQEEDDLFSENEDNHTSQQDELINGHIENDSETAVSDDGLFSNTEEATEAPEADVPVKKVLEVAVPNFKSPASASNDVFHAHIPNFLSVEQTPYDPEQYAAEAEADAALLEHDAHWGQRIKHKVDNTVRWRLGPSGSYQSNAQIVQWSDGSYSLRIGNDIYDTQNKLISQPTFVTASHEAQHLLRVQTSFKSSFTFLPSAINTATRSKLPSMRLTTVQVPSRSVQEIIIEKDPELLKRQAEKYEEERSRARRRLEKRKQLNNYQNGTGEEEEDYSSFYGPRSTYSEQNEIIDSDRMDRLKRIKQEGAGQYRGYNKDLEENEEDDLGDFIAEEEEEEEQEEEQEEDEEDEEEVGAGSDIKGFDADKEASVARATINKYEDDEVIPSAVETDRSETVTETSVGDGSVQRRVKRRIVESDSE Q9P6R5 GPI14_SCHPO SPBC13E7.05; CHAIN 1..371; /note="GPI mannosyltransferase 1"; /id="PRO_0000246233" MRLVLLNYGIWHDRRSALKFTDIDYFVFSDASKYVSIGMSPYMRDTYRYTPMLAILLLPTQYGFPSWGKYLFSISDLIAGWLMIKLLSRRISYKRSLIYSSFWILNPFVAIISTRGNCEAILGILSIALLYLIEKKSVWLASLILGFSVHFKIYPFMYGIAFLVYFSKPKKGSTFMEKFLSLLSINQLKIVVGSLFMFTICNLLMYYLYGSPFLEHTYLYHFGRTDHRHNFSLHHLNLYYESSFGAKASSLFAFLPQLSLCMLIPLVFGKKNLPGTLFAQTFAFVTFNKVCTSQYFMWYLVFLPLVLPNSKLLSKKGLICLSLWIIGQLLWLISAYNLEMLGKSVFIPLWLSGLLFFFFNVYELKIILDSL Q9P6R6 ATPD_SCHPO TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000250" SPBC13E7.04; CHAIN 29..167; /note="ATP synthase subunit delta, mitochondrial"; /id="PRO_0000002670" MFRLSNYMLRKSQFPQGLVRAPFGIRGYAQAVQKNEKLVLSMALPYQTIYEKVPVTQVDIPAEDGEMGILKDHVPMIQCLKPGVISVTDESSNKSKYFISGGFAVQQPSNELSITVPEAYKLEDFSSSVANQLLEKHKAEMNSSDEGVAAEAAVRVSVLESLVRALK Q9P6R7 VTS1_SCHPO MOD_RES 673; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC13E7.03c; CHAIN 1..713; /note="RNA-binding protein vts1"; /id="PRO_0000081455" MEVVEGRRKTCLDVVDSPSSRQKQTIAVSLVDGKNYPTRFLNSRTIDKLKQELNTSNLSTGEMSTNETLKNAQEVAGKLLSEENEDSISEHFDEYLGADKPGISFLTRLKTLESWFQSLSLQDRLTTLRTLLHHLPSQEISTLLSSSLTSSPSNSGLSLDKSLPSSPKGDSPSLSSSLPSLTTKSNLSGNLNMVTPASTQGPAFSSKHGFSNALSTASPIPVRTSSVSSTYLTQDREASSKNCLSKALAFSSIEPPASSASTSPRNTPTPSNNGTSINANVTSSLTSNSTGKTSKTTDLLIAASKKSLPSNSTPSKPNTSFFETPHNNIWDSRDRGAFSAPPAPFFPLGFSPHLNDESSRSRWSNISYSPPPPPPPPELLNHSPKSRPLGDKPYLFYRNNQIGPRTRTEGRSSITEGKPFLSSSLRFEHVPSANDLNSVVNARVEKSTGQPSTPLNRQHYFNELPHSTTPVTLPSLIHGSEIDRRRSGFCLNNFNSTPPFQPYHYEIGSGLPQQMHATNTILTNPIDPNSNISTPVGMHLCTLPYTYQPFSSVEKIETPPNNSKNQTYRRSSRGSNKTRKSISHSKNTDKHVGNELPQDIPSWLRSLRLHKYTNNLKDTDWDALVSLSDLDLQNRGIMALGARRKLLKSFQEVAPLVSSKKMNENLKAAKNQSSESLTSFKGHTDSEDLPSGSMSNEISSNSTKQDVSSSSMD Q9P6S6 PGA2_SCHPO MOD_RES 77; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC27.01c; CHAIN 1..132; /note="PGA2-homolog C27.01c"; /id="PRO_0000116854" MGFDVAGYLQSYSLKDWIRIIVYVGGYMLIRPYLMKLGAKIQEREHRKSLLEGEVDGTLDPEMTHGTKPKEHGEFDTDDEEEEENPDAEFRWGYSARRRIRKQREEYFKNQDKSPLDAYADDDEDIEEHLED Q9P768 YI26_SCHPO MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P38085" SPAP7G5.06; CHAIN 1..583; /note="Uncharacterized amino-acid permease P7G5.06"; /id="PRO_0000310828" CARBOHYD 340; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSSPDRSIDIDLEKYPSTATKSVYGQSKDDKNVFDIHPTESEVIPGEVEYADTPSHQNFLQKFFSDFKPVKADREDGVALKRHLKGRHMQMIAIGGAIGTGLFVGSGSSLADGGPASVIIDYTLIGIMMFFTVYALGELAVSYPVAGGFYNYAVRFIDPAWGFAVGWNYFMNYFVTFPLELTTCAITFRYWTDINSCAWITIFLVFVICINLFGVRGYGEVEFILSTLKVVATTGFIILAIIINCGGVPTDPRGYIGGKIIKNKPFRHSFKGFCSVFTTAGFSFSGTEVVGLAAAEAEDPQKSLPRATKQVFWRIAIFYVVSLILIGLLVSPDDPRLMGNSSDGSTSPFVLAIKEANIRGLPSVFNAVIIISTVSVANSCTFTASRTLHAMAAKGDAPRFFAYTDRLGRPLLAMAVCLLFGFFAYINAAGDVSDTVFDWLLAISGISNFFSWGSINLCHIVFRLAMKKQGRSLDQLGFVSPMGIWGSAIGLAFNILCLMAEFYVSLFPIGSKPNANDFFQGYLAAPIVIAFFIGYKIYDRSHIPSLSKLDLDTGLRTYPPKDKESEKIRDAKGFFKWIWQSLC Q9P771 PRM1_SCHPO SPAP7G5.03; CHAIN 1..703; /note="Plasma membrane fusion protein prm1"; /id="PRO_0000337289" CARBOHYD 142; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 185; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 196; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 244; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 256; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 423; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 430; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 453; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 459; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 470; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 510; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 530; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 542; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 545; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 566; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MASSYLSLAARLSQCWISPWSLCCLYILMQFFLFTKDLNTKIGDFVNDEQATCNYIQEKVDILLDSPSLIANAAVRVAKDGIQSTVKIILSGISDSLIAAENVFIFFIEFSYGTYLCLIQLAIDGILDAVADVGEEIGTAVNDTLHAIADEIEDTVSSLNEVFQSAEDSLEKVASWLGEDINLPNVSIPEIQSLRNFTLSSSYDTEFEKLKAGVNFDSAINATKAAISKPFSSARNLILEKVSNYSFDTSMVSSPNKTHVVVCSTDDLTAISSFILSSIYKIRKVVIISLLIIIAGLFLISSIYEIWKWCRIRHKAFLLDEHIRSNKFEDTRDLISYIESPISWNLKYFISALPLPCFLSVQLRWFITYIFHPPAAMILFISCTSFISGILQLVLLNNIREDGSVISALAQNSFHKVESALANVSVAWANSTNQIILKNQENINNNMFGSIHNTTLSLNSTLNTFMNELNSSMTSAFGDTFLASTVQNVMNCLLYRKIENFEEVLTWVYNKSHIELPLLPTDILSKSIDNQTIYSSLYSSLNSSNSTVSFSGIFDRVEKSVISELNFSFLFFLLWLLICAFGLIGVLSSWLKSLFLSLLDLVIPNPKENITLPVQSLAFPVTKSCRPPPIPPRESHVYDFQNFQYEEDDCIDYKRSLGLISLSSDLAIDIPISPAIISDIQFNSITTESEETTYLLKEKQDRY Q9P775 YBEG_SCHPO MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 496; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 497; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1711.16; CHAIN 1..516; /note="Uncharacterized WD repeat-containing protein C17D11.16"; /id="PRO_0000316549" MSIVSSVAFVPRGYASEFPKSYDIDEIEYERINQLSKLKLEDARADLQSSMEDSNKANGNGEETTDGAEGVLQTSEEVDDELKVYNLDTYDDDEEEAETEGPAAMFSNIRGLAYHENGEKDPYITIDPQEQDDLEREEMQILPTDSLLLAARTEDNLSHVEVYVYEPTEENLYVHHDFLLPTFPLCLEWLDYKVGTSDNAPGNYVAVGTFDPEIEIWDLDIIDAVYPAAVLGAGASQVNKKKKKSKKINDSYHTDAVLALSSNRNAHNLLVSGSADTTLKLWDLSTCNCVKSFTYHSDKVSCLDWYSKAPSVLLSGSYDKTAKIADLRLEEAPSSFQVTSDVENVAWDQHSENNFFIGTDNGIVYYCDARNLSKSVWQLQAHDGPISCLSVNPSVPSFVATGSTDRVVKLWNTSDSSPKMVVSRDLDVGRVFTCSFTTDESTAFHLAASGSKGVVRVWDTATNPGVRKAFESRVTEEVTKKERIVQLEDRGAGEDSSDDDDYEDIEDDDDQDAEMS Q9P777 HISX_SCHPO ACT_SITE 335; /note="Proton acceptor"; /evidence="ECO:0000250"; ACT_SITE 336; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 132; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 194; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 217; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 244; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 266; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 266; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 269; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 269; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 336; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 369; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 369; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 423; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 428; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 428; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC1711.13; CHAIN 1..439; /note="Histidinol dehydrogenase"; /id="PRO_0000135908" MPEYEIQVPSYRAAALTAEERTRLLARPIQNTQKIRTIVQPIIEDVKSRGEASLIDYASKFEKVQLKSAVLKAPFDDDLMKISPMIKEDIDIAFNNIFAFHSSQLRPTIAVQTMRGVVCQRMSRPINRVGLYIPGGTAVLPSTALMLGVPAKVAGCPHVVISTPVRKDGTVAPEIVYIANKIGAEAIILAGGAQAIAAMAYGISGVPKVNKIFGPGNQFVTAAKMHVQNDYGALVAIDLPAGPSEVLVIADETCNPESVALDLLSQAEHGLDSQIILLTVSLSPEMFDRIQKAINDHALRLSRSYIIKHAIKKSVIVQVDNVDQAFEWSNLYGPEHLVLHLKNASSYIPKIDNAGSVFVGPWSPVSMGDYASGTNHTLPTYGYASSYSGVSTDSFLKYITTQELTEEGIQRLGPTVIRLAELEGLTAHADAVRVRGVRL Q9P778 DPP5_SCHPO ACT_SITE 535; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P23687"; ACT_SITE 617; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P23687"; ACT_SITE 649; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P23687" SIGNAL 1..19; /evidence="ECO:0000255" SPBC1711.12; CHAIN 20..683; /note="Dipeptidyl-peptidase 5"; /id="PRO_0000311722" CARBOHYD 53; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 69; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 103; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 116; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 126; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 400; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MHSLFKQLVFFLVMTLTAADKAAFDAESMLEAPRRSAVVSNPLGNLGIFIESNYSFADHKYNSGIYLLNESTRNHQELLVHGKSNKALTWITDSAFLYAREDNSSSSSILLFDVNNRSERIIYNHNSSISDIRIGEKNNHYRIVFSSVDNSLVKGPSNVHVYDHLFVRHWDRWNTGSRNTLYFIELDKKTENSNYFEISSEKAIDLLKETGLESPVEPFGGLSDFDSNYDKLVFVAKDPKLNPATQTKTVVYEINLNTRNLKSLSTAKGACSSPRLAKDGNHIAWLEMQTPQYESDQNQIMVYESESGAKKHIARHWDRSPSSIEWGVFKGGEPGLFAIAENYGKQILFFVSIFHHQVIPMTEEHSVSSISVPKSSSLWLTKSSLINPPYYAKINVETLNESVLLENNVGLSPTSYEEIWFPGTHGHRIHAWIVKPESFDKSKKYPVAVLIHGGPQGSWTDSWSTRWNPAVFANAGFIVFALDPTGSTGYGQRFTDSIALDWGGKPYKDIELGVEYIKNHLSYADSEKMVALGASYGGYMINWIQGHPLGRQFRALVCHDGVFNTLNTFYNTEELYFSIHDFGGTPWENRVIYERWNPSNFVNYWATPELVIHSSKDYRLTESEGIAAFNVLQYKGIPSRLLVFEDENHWVIKPDNSLRWHKEVLSWILHYTKDCNANEDETF Q9P783 RRB1_SCHPO MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 166; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1711.07; CHAIN 1..480; /note="Ribosome assembly protein rrb1"; /id="PRO_0000316544" MSKRAAEETVEFNSKNGPGQRGTVADNVDTEMGEFEDAYEDEIESEEEYIEADGEKDNGMDEEEQNDAQPSKIPWLPGGKINADEKLVADPSVYEMLHNIQVKWPFLSFDILQDSLGEERRAWPHQMYLVGGSQALDSNDNELTVMKLSQLYKTQHDENDDASDNSDVEEDPILEHKSISTKGACNRVRSARRPANSSKESLLASFHETGKVHIWDIAPHLRSLDSPGVMVSRKENSPLYTVNRHKTEGYALDWSPFEYSLLSGDNANEIFLTKYSNGGWQTDSSPFLSHTAAVEDLQWSPSEKNVFSSCSCDGTFRIWDVRNKQKTSALTVNAHPGVDVNVLSWNTRVPNLLATGADNGVWSVWDLRSLKSSSSVATPVASFKWHRAPIYSIEWHPNEDSVIGVVGADNQISLWDLSVELDEEEQDSRAAEGLQDVPPQLMFIHMGQQEIKEMHWHRQIPGTIVSTAMTGINVFKTITF Q9P784 RL4B_SCHPO SPBC1711.06; STRAND 7..11; /evidence="ECO:0007829|PDB:8EUY"; STRAND 13..15; /evidence="ECO:0007829|PDB:8ETG"; STRAND 17..23; /evidence="ECO:0007829|PDB:8EUY"; STRAND 69..73; /evidence="ECO:0007829|PDB:8EV3"; STRAND 81..84; /evidence="ECO:0007829|PDB:8EV3"; STRAND 92..96; /evidence="ECO:0007829|PDB:8EV3"; STRAND 150..154; /evidence="ECO:0007829|PDB:8EUY"; STRAND 208..213; /evidence="ECO:0007829|PDB:8EUY"; STRAND 222..224; /evidence="ECO:0007829|PDB:8ETG"; STRAND 228..231; /evidence="ECO:0007829|PDB:8EUY"; STRAND 250..253; /evidence="ECO:0007829|PDB:8EUY"; STRAND 267..269; /evidence="ECO:0007829|PDB:8EUY"; STRAND 272..274; /evidence="ECO:0007829|PDB:8EUY"; STRAND 283..285; /evidence="ECO:0007829|PDB:8ETJ" HELIX 26..29; /evidence="ECO:0007829|PDB:8EUY"; HELIX 34..44; /evidence="ECO:0007829|PDB:8EUY"; HELIX 117..130; /evidence="ECO:0007829|PDB:8EUY"; HELIX 134..138; /evidence="ECO:0007829|PDB:8EUY"; HELIX 156..160; /evidence="ECO:0007829|PDB:8EUY"; HELIX 164..173; /evidence="ECO:0007829|PDB:8EUY"; HELIX 177..185; /evidence="ECO:0007829|PDB:8EUY"; HELIX 193..196; /evidence="ECO:0007829|PDB:8EUY"; HELIX 217..221; /evidence="ECO:0007829|PDB:8EUY"; HELIX 232..234; /evidence="ECO:0007829|PDB:8EUY"; HELIX 237..240; /evidence="ECO:0007829|PDB:8EUY"; HELIX 242..244; /evidence="ECO:0007829|PDB:8EUY"; HELIX 254..258; /evidence="ECO:0007829|PDB:8EUY"; HELIX 260..263; /evidence="ECO:0007829|PDB:8EUY"; HELIX 289..293; /evidence="ECO:0007829|PDB:8EUY"; HELIX 296..299; /evidence="ECO:0007829|PDB:8EUY"; HELIX 324..330; /evidence="ECO:0007829|PDB:8EUY"; HELIX 354..360; /evidence="ECO:0007829|PDB:8EUY" TURN 45..48; /evidence="ECO:0007829|PDB:8EUY"; TURN 56..59; /evidence="ECO:0007829|PDB:8EV3"; TURN 85..88; /evidence="ECO:0007829|PDB:8EV3"; TURN 139..141; /evidence="ECO:0007829|PDB:8EUY"; TURN 174..176; /evidence="ECO:0007829|PDB:8EUY"; TURN 320..322; /evidence="ECO:0007829|PDB:8EUY"; TURN 332..335; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..363; /note="Large ribosomal subunit protein uL4B"; /id="PRO_0000129366" MAAARPTVSIYNKDGSVSSETLALPFVFKAPIRPDLVRSVHTAVAKNKRQPYAVSEKAGHQTSAESWGTGRALARIPRVGGGGTHRSGQAAFGNMCRSGRMFAPTKTWRKWHVKVNQNEKRYAIASAVAASGVPSLLLARGHRIEEIPEVPLVVDDAVQSFQKTKEAVALLKEIKAYRDVIKVANSRKLRAGKGKLRNRRHVQRRGPLVVFNEDTGIVKAFRNIPGVEIVNVRRLNLLQLAPGGHLGRFVIWTKSAFGLLDSVFGSTTEVAQLKKNYFLPENIISNADVTRLINSDEIQSIVKAAGPSRVKRAHVQKKNPLKNKAVLSRLNPYAKAYKANVKINSEKTPKAAGEKFLSVLHEN Q9P786 MTD1_SCHPO ACT_SITE 152; /evidence="ECO:0000250" BINDING 187..188; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 210..211; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methenyltetrahydrofolate + NADH; Xref=Rhea:RHEA:22892, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.15; SPBC1711.04; CHAIN 1..320; /note="Methylenetetrahydrofolate dehydrogenase [NAD(+)]"; /id="PRO_0000316023" MSNTNKSEPNHSCKVVYASRVAETFVEQLKQHVNLFEFAPKLVGFLSNSDPAARMYADWTNKTCTEIGFQYELREVPKDDLEDAIVEANNDPSVNGIMIYFPVFNDGQDQYLQQVVSPDKDVEGLCHKYVMNMYHNIRHLDPEKTKKSILPCTPLAIVKILEYLGVYNKIINYGNRLYGKTITIVNRSEIVGRPLAALLANDGAKVYSVDIHNVQCFTRGAGIRSKKHDVADTNFKLEDVAPISDVIICGVPSANYKFPSNLVRDGAVCICFSSEKNFDAASLKEHAGIYVPSIGKVTIAMLLRNLIRLTSYQLNKPVDI Q9P789 YN8E_SCHPO MOD_RES 260; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 506; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 511; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 515; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 554; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBP35G2.14; CHAIN 1..1065; /note="Pumilio domain-containing protein P35G2.14"; /id="PRO_0000310366" MHQDAMQGSIYEGSRRNTISKPSNNNPPLDMSSLNNDFGQQLDSLATGVGSGSLNGTTNPSSNFNDSNRSNISSSLRSEMEMSNNLLKNTQNDTWTSTVGLSVPENQEAMNFNEGPTGISSIASKNNSSITSKLQNNSNLSVTSSANRGRTSSVSSSYDPSFPWGPRMSSVSSGKQHLSSLSLHTHFNPSSSSTVSSDSLESSQQKAPSSSSTATPASAASEIISNKDPVVEPTHSASNAANSGSNTIRARQTTRTRSNTLPWSPRVFGPTLGYNTPPFGYPPTTSSALPNASGSSSSFFGLPTAVSASAGTSFSDISPAAPKASLENNIASNASSLLNPVGLDHFSAASGWSRDFNHLPASSLATARSSLTGNAKSGIDSSVTGMPSDNYARVVESSTAEFFDPSLASSFGLTNYRTKPLTTGFNHPRPQGHGLNTSLFNTSSGGSLKSPTFEVSNRLGDVDTVPDLPPLGSLSSRPKPSSSSRRRSQSLSAMLKTSNPYMPSPSLLSGSLANSSEHSSSPRLRGSPIHNQPVSSSKSTASLNTNNNGLRASTPEMANISTRSSSESNNTNSWPTVGDATIENLTQHEPTHALWVGNLPSGVSATTVATTFSAYGTVSSIRMLSHKHSAFLNFDSVETAKHVLEELNGKRIFFGSDPVCISFAKVASSSSESSHSAVDGLNKAFSNVSFVPSLREVYDDLINVVQSFGFKDLSKIYQILNAACELTDFAAQIPSISKAFSSRRLNAPKLRQVRKRIDNGLCTQEEVEDIAINWLDEVSDLSSDHLGNTVVQKLFDYCSDPVKEMMLERIAPHLAQIGIHKNGTWAAQKIVDVASTEAQMRLIAKHLQPYIPLLFADQFGNYVVQTCLKFGAPMNDFVFEAILNQFWVIAQSRYGSRAVRACLESPDVTEEQRVLVAAAITVYSVHLAMNGNGTLLLTYLVENMNYPHIPILLTRRFVQDIVRVCTHRLAYNSLLKIISISQGDTACGDLVVDAILDTQNDLNPNSLEKILFEQTYGPSFICKLLTHENISASHRQQLQSAVRNVLGTMEDRGSSELKKLAEVCA Q9P791 YN8C_SCHPO SPBP35G2.12; CHAIN 1..205; /note="Uncharacterized Nudix hydrolase P35G2.12"; /id="PRO_0000317227" MSQDQKPKVLEVSNLENQDAKWTSLKKIRWQDEKGKIRFWEMAERTTRSEANVDAVAILAIVPIDGSPHVLCQKQFRPPIGKFCIEIPAGLVDSKESCEDAAIRELREETGYVGTVMDSTTVMYNDPGLTNANLKIILADIDMSKPENQNPQQQLDDGEYIENFPIKLSSLQEELFSLEKKGFAIDVRLSTFALGLHAGLKYLSS Q9P792 YN8B_SCHPO BINDING 62; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 65; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 79; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 85; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 88; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 96; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 102; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 136; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 139; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 150; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 153; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 159; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 162; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 168; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 172; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 212; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 215; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 227; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 230; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 236; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 239; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 244; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"; BINDING 248; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" SPBP35G2.11c; STRAND 63..65; /evidence="ECO:0007829|PDB:7DDE"; STRAND 73..81; /evidence="ECO:0007829|PDB:7DDE"; STRAND 83..85; /evidence="ECO:0007829|PDB:7DD9"; STRAND 103..106; /evidence="ECO:0007829|PDB:7DDE" HELIX 86..91; /evidence="ECO:0007829|PDB:7DDE" CHAIN 1..397; /note="ZZ-type zinc finger-containing protein P35G2.11c"; /id="PRO_0000314634" MLCNRTCPSSDCGILCNHSVPSFPPFHSSVANIHFTKENNLKSNIFEHNNNSPTLRSSSVACNTCLKIIRNDSFHCTKCFDFDVCRDCYAKQAFLHPCPKPHFVLVRSSIPSVASLTCSVNSMSVSPQSNFMYAICDHCEQPIHNVRYKCSVCDDYDICESCLTDNSHSNTHAFVRITKAYPHGLPSFHLFPQFLSAELFESASTVHRSVQCDNCLAHPIVGPRFHCLVCEDYDLCSSCVSHVHHDHHSMLRLTREISASPLHLSKPEKPKVLNFDFKLVEDSILPLELSPGCPFYKIWHIRNTSCQSWPSPLYVKFNGGDKLFPGDNPYSFPITSSVHPGEDVNFTVALKVPEKSNKEIFTAFFNICSDDGSVFHKSLCAFLRVPKSFSRISKSSF Q9P7B0 STB3_SCHPO MOD_RES 194; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1652.01; CHAIN 1..391; /note="Protein STB3 homolog"; /id="PRO_0000352765" MNIDNMDLEMTTASDFAEKKESVDVKRENPSFTNSIKALPIQSELSAMMSKDNTLNHVKQEPSDGFSSVKWASTSFDSTVTAHKEETPYSSSLGSHDSSSLPSSTNNRYSSVLKELCNTYLPSILSTYGSLPIRRLLHHLSLMLPSFNELTPTQQRRLLTRALESKKGIQFEKIGWGRWVLRDSTIPANSHPQSLPSNSIPKTEPLDTPSLSNSQERFSKSPSDGQNVRSRAKKIPSGMSAEESDELLSSSGRKTRSFNTPFSSFFASLEETPGSYTAHLGGVLSPREQTPALFTGQYPDNGVYYEEEEEEEDDNDLFDEHEYGYGTLPPFVFDEDQMLDGGESTDEEDWRAIGTEALLRKVNTKKRRPSRVLVHRDQVAVEAMLMLSGSV Q9P7B2 RS8B_SCHPO MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 99; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 150; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 154; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 171; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC521.05; CHAIN 1..200; /note="Small ribosomal subunit protein eS8B"; /id="PRO_0000122257" MGITRDSRHKRSATGAKRAQYRKKRKFELGRQPSNTRIGPKRIHEVRVRGGNKKFRALRLDSGNFSWGSEGVSKKTRIIQVAYHPSNNELVRTNTLTKSAIVQIDAAPFRVWYETHYGILMGSKGKKATATPTPKSKHVQRKHSARLGDSKVDSALETQFAAGRLYAVVSSRPGQSGRCDGYILEGEELHFYLRRMAPKK Q9P7B3 YI14_SCHPO MOD_RES 129; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC521.04c; CHAIN 1..881; /note="Putative cation exchanger C521.04c"; /id="PRO_0000317131" MSQPADINQSESSAETITQGRRADRPEETPSSSVYEQNLRFGDFLMPTVGDADATDSLSQSTNDRDIYSPREIDQYTRKVSSRTDPSTSTISNARQHPRNSVSRLSRSSSNVRQQRDIPKQNFKVRPLSPLRGQSPASLRSEESFTLKERQNAINKTRAFGMRLWKPALYKKFRSINRDADIDIHDEPLKRPNTSISNVIWLICFGAPLFLVIFICYIFFTVLSFFNVPDAIVYSKLCRGLMFYLLYPFGQHVRHKVKRLSVRSPAHPIYQTQHSHYDETPTSHHPDPARLNFLSFSFCVNPMNQSLDCNTTPHRRNASSIIYTLMYYLIIAPTLLITSAICMFTIFFVPCARTLWAICRHLRTCPLSLSFRPNLALPLSMDSSDVVLLCVKKAASWKYYKYTIDGIYIIYFDMLALIIPTIFFGFFGSQGHWFTSSVFLFTASLVSIIPLAYFIGMAVASISAQSSMGMGAFINAFFGSVIEVFLYSVALRKGNAGLVEGSVIGSILAGLLLMPGLSMCAGAIRKKFQFFNIKSAGATSTMLLFAVLGAFAPTMLFRIYGPFRLDCEPCGANCQKCTKHYVLENDSLYKNRVLPFTYCCSIMLVLAYAIGLWFTLRTHASHIWQNFTADDISFLKAEEEVGEPVNQDTAGNMSDSSEGGEAVVNGNSQHHHNRDDASSGLSSNGSENESLEHEPTNELPQRPLVNQSQNSHGDDAPNWSRSKSAIILLSATFLYSLIAEILVEHVDTVLDKFAISEKFLGLTLFALVPNTTEFMNAISFALNENIALSMEIGSAYALQVCLLQIPCLMGYSLFQYYRSGDSISFKHLFTMVFPTWDMICVMICVFLLTYVHSEGKSNYFKGSILVLAYLVSMLGFTFFNY Q9P7B4 YI13_SCHPO ACT_SITE 158; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 162; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 11; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 65; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 92; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 126; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 158; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 162; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 191; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868" CATALYTIC ACTIVITY: Reaction=L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH; Xref=Rhea:RHEA:43524, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58320, ChEBI:CHEBI:58349, ChEBI:CHEBI:58585; EC=1.1.1.381; Evidence={ECO:0000250|UniProtKB:Q05016}; MOD_RES 42; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 43; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC521.03; CHAIN 1..259; /note="NADP-dependent 3-hydroxy acid dehydrogenase"; /id="PRO_0000372617" MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPSHQGGANHVYRKQA Q9P7B5 WSS1_SCHPO ACT_SITE 118; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 117; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 121; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 127; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; SPAC521.02; CHAIN 1..283; /note="DNA-dependent metalloprotease WSS1 homolog"; /id="PRO_0000351446" MIAILYLYYILTTSILLSVSFMLRINDDDHPNEKIGFISAIKGDFHDLSSDYLKRIAAMAFPIMKEHGFGVTSLDEVAYNAKFWGRNWNKGECIELVLRDASNRWLPFEFVMDVFLHELCHIWQGPHDRRFFSHLSTLRAALIALYAKGYKGPGKYMTWDSFVLANVVGNYNTVVFNGITLERSTMHGVETCGGSLQRKKKIRRKPTPSSTKKRKLTRTGQKLGTDMNIRLELLKSPAKPQAQSMRGREARIAAALLRVDNSNEYKPKDHNSSTTLENYFVVE Q9P7C1 YKU3_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPAC2E1P5.03; CHAIN 17..303; /note="Uncharacterized J domain-containing protein C2E1P5.03"; /id="PRO_0000310357" MSRIFILLLLFGVCLAWTSSDLEIFRVVDSLKSILKNKATFYELLEVPTKASIKEINRAYRKKSILYHPDKNPKSKELYTLLGLIVNILRNTETRKRYDYFLKNGFPRWKGTGYLYSRYRPGLGAVLVLLFLLISIAHFVMLVISSKRQKKIMQDHIDIARQHESYATSARGSKRIVQVPGGRRIYTVDSITGQVCILDPSSNIEYLVSPDSVASVKISDTFFYRLPRFIVWNAFGRWFARAPASSEDTDSDGQMEDEEKSDSVHKSSFSSPSKKEASIKAGKRRMKRRANRIPLSKNTNREN Q9P7C6 CWC23_SCHPO SPCC10H11.02; CHAIN 1..289; /note="Pre-mRNA-splicing factor cwf23"; /id="PRO_0000071128" MASEGDSIDYYELLGINEDAQDQEIHRAWRKTSLKYHPDKNPNDPKAAEKFHMLQLAYNALIDVQLRKAYDSERFAKLARKRREEAFNFQRKSMVDDLRERERQFYDSLEKKENERDRLQEKLRALQEESANLRRQRENRLREEQEQSKRRKQETPSSKISELDRSIRIRWKRKYADQVNDAYLRSIYSSFGTLQNVVIQKDISKEKKYVYSIIVFETLSSAYSAINAEKPSKIYDVQWLKPPKSNSNTPTEKDTTVEDYEEITIMRMKQKHKQKQKENERKATSTMNA Q9P7C8 SLD5_SCHPO SPBP4H10.21c; CHAIN 1..214; /note="DNA replication complex GINS protein sld5"; /id="PRO_0000255434" MEWDADDLLIEPTTEVENDYEDLCTQWVNERMAPDLLPFAEEIVSRVLDRIEAQRETLQLAIGTSSATSYRSVLMQTELERVKFVLRSYMRTRINKIDKYAQYIQSHPNLLLYLSSPERQYLLRHQQIVHRHYMDSFLREVPAKMNKLDDKVGNLSMVASPDMDTAVFCVVNESVEENFRVSENEYITLDKGDVLILRYSVISDYLRLGVVSLI Q9P7D0 YOFJ_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPBP4H10.19c; CHAIN 17..381; /note="Uncharacterized protein P4H10.19c"; /id="PRO_0000310333" CARBOHYD 133; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 192; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 225; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 243; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 246; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 287; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 118..149; /evidence="ECO:0000250" MQTLLFYFFFINLIFAHDLNVKTYKPCTIPSVFSEQFTSEDITTWRSRWRAPVNKDLGVWDLVEAPGSHLRDEYGLITLKSNKPHILISNLENPTTRQSSSVPIVLSFQVKPTKPWTCGHAYVSLVHQSNPKNVSKEPPSVIRFGVKKCGMFDYISLSIISYDGKVSCHLYDAPPSGLVEGRTSMYTLLLQNTTVVIRRDQSVVYTGDVGTNFFHSPTKWITHSNVSNGYYTSRNIMSFLLSNNTNTSSYPFSVNGVELDVWNENAGVFINNIYFGFSLSDAMKFENETFIAKKILENSPCPNQPSIQPFGILMMLVSTIYGNFKNLYNCIKRNTIGYIYNSIYDFWITEGMLFPMRNMDIFKITAISIGLSIPVFLWLLK Q9P7D2 PPME1_SCHPO ACT_SITE 153; /evidence="ECO:0000250"; ACT_SITE 178; /evidence="ECO:0000250"; ACT_SITE 304; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester + H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) + methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89; SPBP4H10.17c; CHAIN 1..341; /note="Protein phosphatase methylesterase 1"; /id="PRO_0000223669" MAFRKEELSQTLYENESEQSSETKELMLNNEESLSDWRNYFDEKLTIPGESGALNGTINGYLTLPQPDGCLLVLQHGAGSSAMSFAPVTQELLSNSDNKVGFLALDLRAHGETTLEPESDMSLETLSKDFTHAVSYVQRMFELDEKIILVGHSLGGAICAYCAFQKTIPNTSGLVVIDVVEGTAMEALGFMKTYLSNRPTSFKSIDDAISWHIKTLVTRNRLSACITVPSLLVQQEDGTFVWRTDLYKTSPYWMDWFKGLSDKFLRAPYGRMLIVAGTDRLDKTLTIGQMQGKYQLEILPETGHFVHEDVPAKISSLLLNFWHRNQPLVLPPKVGATPVLQ Q9P7D9 RSV1_SCHPO SPBP4H10.09; CHAIN 1..428; /note="Zinc finger protein rsv1"; /id="PRO_0000046884" MKSYECPFCKRVFHRQEHQVRHIRSHTGEKPFECSYPSCKKRFTRRDELIRHVRTHLRKALVTPEQTLDVNLHKAPDSKPEGDKSTGQEADKSQNQSKDGSITDPVQAAVLALSVAYAKPTSVSLSPTDLQAQSKLIEKPRRRSASNATGSLNKKNQDPLRRFSISESAGAAAPTPSPSNSKSPPSENRKNRLQNVLSPIASNNVPDFNQNYPTESNPMFLSTPRFQNTNGQRTLTVPVSVWDARQPPTSSRSGLPLSVMYNHFPSVPIPPATVNDTSMEYYLPNAYPHPTGISLPFYPFDSGIPVSPNIPVSPSSSFVPMYPTTFPSSKPQIVNAPPAPSYFSPGSSFGAQLCANGSTLLRADTKQYGLALPKITNSNLISPNQTFNPVKSSVKALPTLEPPSSPSHATATSSLHTLFHTAPSRSYD Q9P7E0 QCR10_SCHPO SPBP4H10.08; CHAIN 1..79; /note="Cytochrome b-c1 complex subunit 10"; /id="PRO_0000353193" MISFFPNKPMYHVQPHISFITPERTMKTIPAFSRWAFAAVAGVFVFAMQVPKVKTTILQPIAFIGDHFKDKTPEEDKWL Q9P7E8 APP1_SCHPO SPAPJ760.02c; CHAIN 1..857; /note="Protein app1"; /id="PRO_0000064640" MSFQLDTSTHGAEIRNVYEKVLSGADDCSWAIFGYEKGQGNILKVVASGNDNDEFLDEFDENAVLFGFLRVKDVNTGLNKFVLVCWCGEAAARKGLFSIHMATVSNLLKGYHVQITGRESSDLNMDDIIRRVADASGSKYSVHTSNSTPQSKHNAFYDASQTFGSTAKVAPAPAPSTKTPLANISKPVVQAQKDSKDNSWDDSSKQSNTQTANTTSNLRVPVNASWSDAGRKEKSQENKPKPTPFGSGGPSKPTPFESHGPAKQISVQPSEHPKPSISTTTTGSSYRSAESSHAPTTPDHFKLTPLTKLEPQPPSGSPSKKPVSELEELHTAGNVNLSARRALFEKKESSTKNVENPVSHHLKSPVRTSFPPASTTASKQDSPSTVPVDKQETAKPINKQVSSNETSAQEEPRESVAALRARFAKANVSENNDPPTFPKTAAKISSFNSKAGTSFAKPRPFTNNPNPISAPEKPTSGESLSLNPPPAMPKVFPERDISSASQKAAQPSVITPSVPQPPAAPVVPEAPSVHQPPAAPVAPEVPSAPQRPAAPVVPEAPSVPQRPAVPVVPEALSVPQPPVAPVAPEVPSVPQPPVAPVVPEAPSVPQPPVAPVAPEVPSVPQRPAVPVVPEAPSVPQPPAAPVVPEVPSVPQRPAVPVVPEAPSVPQPPAAPVVPEVPSVPQPPAVPVVPEAGQLNEPVVPPLPPHDETQEPQVGGDVKATEHTQPTKTPAIVIYDYSPEEENEIELVENEQIQILEFVDDGWWLGENSKGQQGLFPSNYVEITGPNETANNPPAEPQAGGPGKSVKAIYDYQAQEDNELSFFEDEIIANVDCVDPNWWEGECHGHRGLFPSNYVEEI Q9P7E9 YDZF_SCHPO ACT_SITE 719; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 795; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 828; /note="Charge relay system"; /evidence="ECO:0000250" SPAC14C4.15c; CHAIN 1..853; /note="Putative dipeptidyl aminopeptidase C14C4.15c"; /id="PRO_0000122423" CARBOHYD 96; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 102; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 472; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 483; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 613; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNAYEGDTLNNHGKSSTRQHWRKRSAVSSSLEFSSYEESNSPIENTEVLKVSEIEAKKRRRKKHRYIYLAVCLFFLASVLSCAIIFRFYLHTNRENFSLFKNDSYKQKEPITVSHFGESIFLPYHQDIEWITSTEGTVLYYDQSTFSLSLFYPDGKEYGSNVDSLITSFVLTCKNLHRKRYSSDMEYIAFSCSKDRRWRHSYYEDVYLVERATGRIEHLASDQSKKIVVAEWSPIGHKLVYGLGSNLFIWESFSEPPVCITDQSDLDGLFNGNSDWVYEEEILQSSKAVWWSPDGNCLSYLSIDDSKVPVHVLPFEQLDSKVEDQNRVNNFFHYSTPKDPIPFVKLFVNCFTDSGESIEVDSSFPLSTQHRYITDVAWAGNEKLMFVEVLRGNYERVTSLFDLSSRKTTIENTEVSEHPLALTSSLHLKYLSFESLGNLKERYVRQYFLSNKKRIAIYELDNPVPIYLTPVNISFLSDLYLINNTLYFTAISSGSPFSRVYRLCTKSLILSEINIQIGSGLFGIKVSNDQNYLLVNYLGPEIPKQFIYSIHEDKVSTSNDHSKNNLPSDSSSTSLGKVKLELCNSLETNEELIITKEKFAFPSVFFKVIKVKNITAYIQEIRPPNFNPRKRYPTVFHLYGAPQSALVTGKYEMDINELMASVYNFLVIKVDIVDISDVSGQHLFSDSHELIIKSWIELLRSYVDTPYIDRHRVGIWGWSFGGYLTLKILENADFIKTGAVVAPVTDWRYYDAYYSENLLGAYSKQTTAIYDKTAVHYSENFRKLCGLLVLHGTSDDNVHIENTMQLTKAMVEKGVYNYYPFIVPNANHEFSDPTDYTFLREKLSGHFHHALYC Q9P7G0 YKY4_SCHPO MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1142.04; CHAIN 1..707; /note="Uncharacterized NOC2 family protein C1142.04"; /id="PRO_0000326122" MVKLSSIIKARKANALAKKNDKIKKKDTDKGIRQKHSKKEGKDETLKRDVEKFIQNVNSEDTPSEDDSMSMDAFLEGGFEELDSANSNDAGSSRKRKNLPNENTQDSTSESSEEEEDGLESYQKQLEGLKEKDPEFYKFLEQNDQDLLEFNAAETDAMAKEIDENERLKSSSGKIVLTSDTIQQWQKLLETNHSLTTLQKVVQAFKAAAFLNEEEAEDLKYTISDSKVFNDLLLLAIQYVPKVLNYHVPIQEDAKGKKFINTDSKVLPKLRPVLKSYGFSILRLLEGMTDAKNISLLLREAQNVLPYMITYRKFLKQFTQATVEVWSSTRDDSVRFSAVVLLRTLCLTADITLLEFVLKEVYLGMARQSAYTTVHTLDKINFLKNSAVNLFLLDAESCYLIGFRYIRQLAITLRNTIHQPSKDSRKPVQSWSYVHSLDFWARLLSQAAWLSREKGVASELQSLVYPLVQIALGVIMSSPSSQLFPMRFHIIRSLIYLSRHTGVFIPLAPSLFEVLDSSYVSRKAKASTLKPLDFDVELRASSSYLRTKVYQDGLIDQLLELLSEYYVLYATDISFPELVIPAIVRSKRFAKRSKNAKLNRGLLTLVNRLEQQSKFMTEKRNQQKFAPIDSDSVEQFAQTIDWQQTPLGIYVVTQRQTREEQRKLIRESVQQDQEHKEQMRQKKKQALKSDDIELDDLSEEEAEDIDE Q9P7G4 OMA1_SCHPO ACT_SITE 196; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 195; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 199; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 250; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O75844}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844}; SPAP14E8.04; CHAIN 1..337; /note="Mitochondrial metalloendopeptidase OMA1"; /evidence="ECO:0000255"; /id="PRO_0000302811" DISULFID 265..321; /evidence="ECO:0000250|UniProtKB:P36163" MFLNKYISNYSRTRAVSCAPVLSYKKCSYRNFNGLLQARFQSNNLSWSNRNRVVYKSFQPNPRDKRFQWIFGALIAGGGVYYFTHLEYVPISNRRRFNDVSLDFEKRMAQDAYKEVMSEYGDRMLPSYHPTTLYVSRVLKRIIAVSGMSDLKWELHVIRDPTPNAFVLPGGKVFVFEGILPMCKGEDGLAAVLAHETAHQVARHSAEKIAFTRAVSCIVFLAAASLDLSGQLSHFLLNFGLLLPFSRKMETEADYIGLMLMSQACFDPNAAKTLWERMDAAEGQMGKALAFASTHPSSKKRIRKIEEWLPEAQVKRETSDCYHETWPMLQSFKEVHW Q9P7G5 BOS1_SCHPO SPAP14E8.03; CHAIN 1..235; /note="Protein transport protein bos1"; /id="PRO_0000207555" MSNTLYNHCTKLFQSIQRSLDELERGVQDESNTISLAGIQGQISASFLSLSRSIDDYDSMVQRELVPAKKKKATIRIQEFRQKHVQLLEKFDELKAHVRDIAQAKNRKELLGRRGYVNSLDSPYGNSTTDAEIVEGPSDLSRQDGLLKEHDFLGRAESQVDEFLERGRMILGDLVEQGSVLKATKTKVLNAANTLGITRHTLSLINRRSKQDKIIFYCGAFLVFVLFYLIYRWLR Q9P7G6 YK42_SCHPO MOD_RES 73; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 379; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 382; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAP14E8.02; CHAIN 1..566; /note="Transcription factor P14E8.02"; /id="PRO_0000353195" MNISSQNVLLPSPIPSSSPMASHKKSWLSKHPNQSMTFEKPQLGQFVLTPEPSSNTFYAPSSPASAVRREPLSPMSFVRMRSHRVNKIGRSSQQCDHVLSTVDKAISRVHAIVTCTQDRMIIECVGWNGMIVSDKMRKSVFHMKKNDRIVLVRPNSDACPVLDVFGYRVLLGWPSDSEDEWEGNLNAKNYEENREPMSPSPQEALPLMPSSPPSQDYQNDQNHLILYTNSESIPKLNLRSNELVYPPPSKDLLQKLLALEKDGQVEKSDCSKNTQLKPSFLPKNTDDLLNGTDDNNIVLREVKVSFENEKIESDDLDKNEEISEGEEYTPIEESKEPITVRRDSVIQIDESSAGLTDVISELNFTNHNDDSKNSNITTSNDSPVNEVEPMAPELSSAVVEKKEPEDYESISAVDENTNDSNESLPSSHDYSESTKENSAPDSLLLGLVLDELVFSTTSTTPLPALSHLFPSNMPLQLIQDKLRDLAAKHPYFEEVKRYGTDANGDPLWSEWFYNPDVDDDLERRMRYAPLMRPVRSSRRVHKQYYWKKPRARPRSSGHSSRRRRLS Q9P7H2 REXO3_SCHPO SPAC1782.08c; CHAIN 1..540; /note="RNA exonuclease 3"; /id="PRO_0000120935" MFSPLGQFKHIVCPFLRTGRKCQSRNCFFSHDFQNSTKISPPYSENVEGYPKVKIEKSLPYKYDNCKLSICVPIVTTCIPYHSVENLNFNIRQNISTTLNLEKTNDSIKETKNENFRMDVLETYKCKQLNHQTTHLPTNTVLKKRSLFNDAISIVPNKKKQLVSAISTNSDSQGASSNIIPTPKYDSNSPAGHELRKRMTHLLYESYKDLGYSNAESSMLALLDEKNICETANSKMIYSSSCKSKILSLKKAPKKNEIQGSTPDEKLESLVHSEEELILWGYNIGDVAPVNPPDELRECDRCGTRFADPRGPCTYHWGKLFREKQGGEKIRTYTCCGVKEGDSSGCIIEDNHVFKYRHLPYLASVHPFSYLPDSTNSKQLSHCALDCELCYTTNGMELARLTVVAKESIIMDVFIKPKGKILSLNTRFSGIHDAKELESGITMDQMYIKIKELGMNKNTILIGHGLENDLNAMRLIHKRVIDTALLFTHARGPPFRYSLKYLTKKYLGTTIQTSTHDSEEDAVSALQLVFYKTKSNESQN Q9P7H4 PTPA2_SCHPO CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; SPAC1782.05; CHAIN 1..352; /note="Serine/threonine-protein phosphatase 2A activator 2"; /id="PRO_0000226117" MLSREEQNRCFVPVRRILDNEDLKLFKEGDAYKLIDSFICDLDEAVKDKPISASIPQSSSIEHVLNILDRVGEIKQENPAIDNMGSRFGNPAFQSFYDQVYIETPKLHQVFGIEHNAAMEAGRYFYESFGNRKRIDYGSGHELYFMSWLLILKQLGIFTKNDYPALVVRVFVKYVELMRSLQIFYTLEPAGSHGVWGLDDFHFLPFLFGAAQLVNHKYLRPKHVRDPEILEMCRADYMYLGYVYFLNKLKPSVSLRFHSPMIDDISAVKTWSKVNEGMIKMYRAEVLGKLPIMQHYLFGHLIPASPGMSPAPQDGDDSEVTHVHSHYADCCGIKIPSAISAAKNNGSRIPFD Q9P7H8 ECM29_SCHPO SPAC1782.01; CHAIN 1..1679; /note="Proteasome component ecm29"; /id="PRO_0000116846" MAENELRLLNNAELKLALAESEDSFQSLVSVFLCPILLKLDSPHESVRNKTISIANHIMTRLNNNAQAILPLEALVSQYVEANQPLRKRFLLAFISIGEKRIPCSENLALLQICLNHVNEYPLVLLTLTIRLLRFSKPTSAITCSNDVILSLSSFYLIQKDQRIFSDLQFSQKTVDYRLSLLRWIHLSSWPSNWKWLAYFFASADSHSEVARLADEFTRDSGLPDLENLSHVNVLLDIALDKFRIEALHANFSVSISLRNKAIQHLLKSKIAANTDKAINCIEFILEAPPSMQPRLIQFTRWVVDKADPNFLKPKAAMILEKILSILSSNIIQSDLLRGFLYTTIGLLTKVDNHLITNSLLTNLLTSLQSELPDVRVSIDEALSIIIPYYSNFRFSNELLPVLEPFIFDSPESPAAYCALRFVLVAFPFDYLPARFICLKVQNPFVFHHSFIEEAKKGLNLSQWVQYNSVYSTNEAQEEDKVRAASYPSASEVISFILSDHDLKKFWESNAAEYCLAILEFIERCIYYSADRSLELYDNDKLSSIDALLIQDSKLREMVSEKCISLSNFNVFLEYVFYGTLLMHFEPTYALSRLVSFAPPEVTFSLPELDFLTSVFNFPLALRNTATRILGIILSTKDSTRISEVLSSCFTIISTSNNKNDNFFKAETALLIIGYTISYLAAQTNSAAVDSFILNSGSIKEFFSVLLEYLGSNVLHKKTTSLAIYKELFVYFTRDWITSYGVDFDEILNVLLRFLKEVEDTNVKVECLHVISRMSLSFSDDEMAEKILKAIYVTYHMDSPDILFASAEAMSILAGGHRNVFVKSTCPIFFQKQLDNYKADHYCFTLDFILTDCVNSPKPLLRRASSLWLFYIVRYCEPQTYTMTRLNDIYHSFLSFLVTQDDFVQDTASRGLKAMYDVLEGDERKSFTDNLISTIAADRVDEKTKAPLDADTALFTTNKGTVATYKDICSLASESGNPDLIYSFLSIAGNSSLWQARKGLASGISYLGIPEDQKRKTFSFDTSKSSSLLKKLYRFKHDPNPDVAKTMGEIWDTLVPSDLNLASHRKYLVEDCLEFMGSRSWRDRESSVNTLVSLLSNVPVTEYLNQLEDIWNMSFRTLDDIKESVREASFPLCKLLARSVIQSLEKTSHNTSPSGICKGKRIVSVALPFLLKHAYDQAKEVRSLTYSTITELVRTGNSTLTSFVPAIMQVMLEYLTEYESKAATFLDFHAKNYSIKQENIDNARTSAVQSSSMMDTLEKCIGLLDESSMQTLYPILNRMIAKPGGVPTKIGSAQVVMLLVIRRGPLVKQFASKLLQSLKSSCFDRNAAVSDAFASAIGYLLRVCPLEIASQTCQEIIDKFYDGNTNEQIISSKLTVYASRYAPDVFLNLGSLFFPFIFFGKHSSSISINGVLSKAWDELSSAGSSVNLYSEEIILLIQKNLIVTKWDVKRPAAAALLEFVNTSRLTYRQNDIYVLLNETMKDKSWPGKELLLEAYVKFLIKYPEFIKSQKMEEVHQVIVREFKRRNIVYKSHAMESVGELLSDENYRELDLYELSLNECGTFLQKEWFDKDDELNLEEKIALQRNSVYAMFNSSRPGNKNCNEMLLTYLSNALDENYLHWNVKLAILKNAPHLKKIMSNEEFLLYKDILYRCYEDNPSPKAKDYAEVIFGENYLSVLRN Q9P7I0 YIT2_SCHPO SPAC105.02c; CHAIN 1..170; /note="Ankyrin repeat-containing protein C105.02c"; /id="PRO_0000310321" MSTEGAKPSEMLIAACRSNNVDMLEEVVHQQEGDGVSFINNARDSLGNDCVHVCTKYGSLECLDWLLDISGVNLNNRCRMTGDTPLHFAVMFIKKDQETALRMVEMLMEVGADPLLTNNDGFRPIDLVPGDFHDVFASALEGPAPALQYSADVVADDDDEEEGSGESDEE Q9P7I9 EMP24_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPCC24B10.17; CHAIN 22..199; /note="Endosomal protein P24B"; /id="PRO_0000316579" MAFFNVFKAVLCAYFISVVFGHGITLKPHQRECFYENLRNNDQMSVTYQTNVGGDQLVSMSIYNPAGQIMHQEVPNSMAQYSFTVKNPGKYMYCFYNDALDGESKEVLFNVHGVIYISDEDLDANNPLLGKVRQLHDTISKVKHEQEYFVARERIHRNTAESTNDRVKWWSILQTVILVSVCVFQIFYLKRLFEVKRVV Q9P7J6 RS17B_SCHPO MOD_RES 43; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC24B10.09; CHAIN 1..132; /note="Small ribosomal subunit protein eS17B"; /id="PRO_0000141545" MGRVRTKTTKRASRVVIEKYYPRLTLDFQTNKRIVDEVAIIASKRLRNKIAGYTTHLMKRIQRGPVRGISFKLQEEERERKDQYVPEVSELEKDKINVDQDTKDMLKALGYDSIPTVVVAASRPERPFRYRH Q9P7K3 YJN2_SCHPO MOD_RES 420; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC24B10.02c; CHAIN 1..449; /note="Uncharacterized kinase C24B10.02c"; /id="PRO_0000316602" MATKVEEINKLKKKNLHFRQCSADSLSNSSMQFDLSGLNTPVGELATSNLPSPAHPPFGELHQESRTSNSSAMHIENVVASRLMYNEVANGSFALEPKNILVVTKPRKHSLVYKTAEITKYILTIGTPETKVYVDMRLARSKRFSAHNIAKEANTDIDRIKYWNPYICLIKPSIFDLAITIGDNSTLLYTSWLFQKIGPPVLSFSDDDVPGFLTHFSLSNYQQHLYQVLTQNVSLRFCSRLQCSFHKYDEKTKQYSLASTTYSLDEILISRGEHPFISNLNVYNNSELMTVVQADGLVVATPTGSTNISANAGGSLVHPALNAILVTPVCPHTLSFRPIILPDYNVLNVEIPLDSRSSAFFSVDRHESVEMHRGDYLSIVTSHYPFTTIQNPGYQWTKVLEDKFNWNVRERQKPFSRKPSLSDVKDTSDDKFDITDNSYCREFSADIDG Q9P7K8 SPT4_SCHPO SPBC21C3.16c; CHAIN 1..105; /note="Transcription elongation factor spt4"; /id="PRO_0000238553" MDKLNRTRSRACLICGIVLPHSVFANKGCPNDGVDDVETFTSPVFEGIMAMMSPTESWVARWQRIDTFTPGIYATRVQGVLNEDVVESLRRRGINYRPRNGTSWD Q9P7L2 UBX4_SCHPO MOD_RES 338; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC21C3.11; CHAIN 1..425; /note="UBX domain-containing protein 4"; /id="PRO_0000210996" MATIYACRGFHRVPVKLSPSSTLQEVILSSYKQLGFSDWHNLELLHGDKKVDTSLLLRLSGIINGAKLIVKESATNQSGKSSSSISPQSKKIKVALQLPGAARIIDEASSETSIKQLLERHSLLTKVSHVLINGRNFKSEEFDNPLLLYGIREGSILIRLFPIKAQQSIVSEQAPVSQTFNGDVKEKKNADLMDIESENKKDDIVESFPKYPVDAHKLLEPLPTPIPSLPSTPSSYQNLPSQSLTGESLPTVSNQEKDEGVIEKVAVNNTPSVSSKSPFPKKKSFSSMLAQVKKEKAENNGSDGYDLQPTKSQLELYQSILRKRANQVSSTSLTKSSSPKPLPSSAIVKFDFGNGKSIVHEFSKDDNIETLRAFVASHLSPEESTSFQLTFSNYEALPTTGLIVEHIGRAVVRVHTISDPVYAQR Q9P7L3 RIB7_SCHPO BINDING 68; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 72; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 103..106; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250"; BINDING 191..195; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:27278, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58890, ChEBI:CHEBI:59545; EC=1.1.1.302; CATALYTIC ACTIVITY: Reaction=2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NAD(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADH; Xref=Rhea:RHEA:27274, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58890, ChEBI:CHEBI:59545; EC=1.1.1.302; SPBC21C3.10c; CHAIN 1..268; /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase"; /id="PRO_0000135941" MESSQAYFPPSANKKHVLLTWAQSINGRIGYVVESPSLGQLRLSSKESFVMTHLLRTKFDGIMVGSRTAENDNPSLTAKLPDPANPDCLLPLNKQPIPIIVDSNLRLDYASLKVIRLARERLGKPPLIIVAPSIWQQVQHDSKLKEAVKLIQSVGGRCIIRNEDSPDSWSDYVALDKLLQNGVNRIMVEGGAELLAKAFGSTDIDAYVVTIVPKIFSCSNTTEIKNLNNLNLTTNSHWYPCGPDVIFTNYSDEFYESYKSLLTNSDAI Q9P7L4 OAA1_SCHPO BINDING 59; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q6P587"; BINDING 61; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q6P587"; BINDING 93; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:Q6P587" CATALYTIC ACTIVITY: Reaction=oxaloacetate = enol-oxaloacetate; Xref=Rhea:RHEA:16021, ChEBI:CHEBI:16452, ChEBI:CHEBI:17479; EC=5.3.2.2; Evidence={ECO:0000250|UniProtKB:P53889}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16023; Evidence={ECO:0000250|UniProtKB:P53889}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q6P587}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q6P587}; Note=Requires a divalent metal cation for activity. {ECO:0000250|UniProtKB:Q6P587}; SPBC21C3.09c; CHAIN 1..221; /note="Oxaloacetate tautomerase oaa1, mitochondrial"; /id="PRO_0000156842" MLSRAGKVVCIGRNYAAHIRELNNPFPTKPFFFLKPTSAIVEPGHGNLIIPPDVSAHYEVELGLIMKDRLPARRPVSSNSWLDSIGAYFVGIDMTARNIQNEAKKKGLPWSFAKGYDTFLPVGPIIPKHLIPDPHNVILELSLNGKVVQKDSTSLMLNKIPKIFSSITEAMSLNPGDLVLTGTPKGVGPVVPGDILSARLLTAQEQEIIPSKFEIKAEKCD Q9P7L6 TR140_SCHPO BINDING 83; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 87; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 125; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 150; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 176; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 177; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7"; BINDING 197; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8TCB7" CATALYTIC ACTIVITY: Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:27354703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50961; Evidence={ECO:0000305|PubMed:27354703}; SPBC21C3.07c; CHAIN 1..307; /note="tRNA N(3)-methylcytidine methyltransferase trm140"; /id="PRO_0000204457" MDTTPDNSEKKKTSSVREATFSINESFGGRLLTEEEDVFEQNAWDHVEWDDEHLALAKKCIEEQKLYPVTEKDAYMTHPERYWDQFYGKNEGKFFMNRRWIAQEFPELLDLLKEDAGEKSILEIGCGAGNTIWPILKENKNSNLKIFAVDYSEKAIDVVKQNPLYDAKFCSASVWDLAGSDLLRSIEEASIDAITLIFCFSALSPDQWQQAIENLYRLLKPGGLILFRDYGRLDLTQLRAKKNRILSENFYIRGDGTRVYYMTNEELVDVFGKNFKIIQNGVDKRLIVNRKKRVKMYRCWLQAKFQK Q9P7L9 RM34_SCHPO TRANSIT 1..20; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC21C3.04c; CHAIN 21..108; /note="Large ribosomal subunit protein bL34m"; /id="PRO_0000030522" MMFMQQFRNLLHPAMKGARNISILAGGGTMRGFPTRNPFNTATLYSSLPTMNIFGQMQQVRWKTYGNEYQPSNRKRKRKHGFLSRIRSVNGRRVLRDRRQKGRMYLSH Q9P7M5 NOP10_SCHPO SPAP27G11.13c; CHAIN 1..64; /note="H/ACA ribonucleoprotein complex subunit nop10"; /id="PRO_0000149012" MHLMYYLNDEGKRVYTLKKVSPDGRVTKSSHPARFSPDDKYSRQRYTLKKRFHVLLTQLPAKPY Q9P7M8 NU184_SCHPO SPAP27G11.10c; CHAIN 1..1564; /note="Nucleoporin nup184"; /id="PRO_0000204855" MGDYLLSWSWILDAFETSDENLSQNKFEELLDARIAAFQQIESPVTGTLNSNKTTEGEEAKLSIYDSSHSISKSQLESVKKISDITGYNEAQVAYVLLVHQYELNTQYFSQLDNDSVLAQEFQRRYYAEIISCWKVLAFLLQACTDADSKWHKMATRLIVSIFQTAQRSGENAQSTTPSIFCVRIIDYLSKMTSQAAPASLTFNGEEAISQWYFFHFNLQLQLLRVIFLSTYSLVVCNSEMAISWFNCMKKTRYLHDQEFMHLDIDTGFSMCKEITNVAIIISINFISLEKQVLSFKDNPSFFMLSGNTIISLHDMITQLSNDSIGAAVSLTWGIALHLLSNSPDNIPLIQNSSVVSSKILQNPQNSFQALIIAALKYDPFTLIHRIISSLEDDPYIDGYSKIMATLFSSAVSYVKFSDSTMLCATTLFKTPQVYQLFENNDSVTRLLNFARARFPFEYSQFVLLLIPTFACLTSKQLVSSELLHMTTFTQSLPSGFKAYEIIPEPNVTGNALIELQESLHLDSYGFFFPNAERSLPKGTRGRIVSVDTYPPVVMWDLNYSLWEAVGISLNYIVRNGLINSHKSFVLTVLSSSVPLFQTDVSGACELVHLASEGLDGELDFINVICDLLDYFLSLSVIEDADYQICVSSLRLLREFTRFAATDVWAYVTRSLVCVGSEKGISLEDVIFDYESINGVYDFTLAFFDLYEILLDNCISTSVVPDDFSIRLKTDFVKRAMRFLCEVFANYLDWKYARIIQQYQIGHRFASLITKLLNVTFGIEYFNPKTTVNKKTLPLRELSHYIVQRFLVQQDSNRYLHPLLSVMDLINLLYTDIFSTISSPRAKAAKMWLISSFCAMKTLICLRGFLNLKPSELERELFSRSPDLFNCLPRLLCCIAPILQLLSALILAPWPSETPSLLAYMINSTDIVGRVCIQILTNPIQSTNIEGSVWKFLSSIMKGQQQGLAVLLFSGKKFPLDRMKSLNHNVDVQLTSKSLISLAEKRLDSFSINDILSQVPVFEFIFLSRNFWTASLGNLQQEANFWNRIVDAIKLPLTVKLDGLSSVAQADLYILAAHATRITAIQLHMSKLNKSNSSKKIIIDPLKDSMKDLVQHAFTITAYDSNIHNALTRAFKHENGDLHISDLRNTGLFPLRYGDNYFYNIKLAKNMLLNTEDTSFKISMMMSANENLSLLDAQAALLRSWSIFICAFVEFVKEDATLSILELKIMKWVLKSLAEDTIDVNVVQELSAERAALVFRISQQTLAIPISNEVKEHLQSILLLTWKAITTTKFSIYEDSNGEMAYYRPLLHVLYNTLNRLLSEEKENLSLSVGFVSGLLQLCHRKLSQLFEKAVINPTIEVYGDIVLLNSLHKCIVNSHLIRGLQSLYISYINDSFSVDNCLRLFSWSHSLLVDGQPYFADAALSFLLICSSSPAGAEQIVMNGFFYSIMESPLSTALSTGGLGLDGSSIQYKIWIRGILPLLFNIVKFLGNRIMNDMREFVLLAFPQIQYALLNWCQPPSSISLASIDESFMIVLLFDLLQQFNPALLQEIRLAELKIEMLEASTI Q9P7M9 RIB1_SCHPO CATALYTIC ACTIVITY: Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25; SPAP27G11.09c; CHAIN 1..326; /note="Probable GTP cyclohydrolase-2"; /id="PRO_0000317089" MDKKEGDQVHHDKTLLQDLSLPENVASEKRLPIDDVQCVNSPMLSPALDIEPKPNVVGTAERLPKVRCVVRARIPTVKGTEIFLHLYKNDFDNKEHLAIVFGQQIRSDSLDAVQEGETEMDRMVRGAYVGTLYPGRKSSYIDVNSSKTTEEQKEEARKTNFVPLVRIHSECYTGETAWSARCDCGEQLDEAARLISEEGNGVIIYLRQEGRGIGLSEKLKAYNLQDLGNDTVQANLLLQHPADGRSYAVATAMLMDLGQRDIRLLTNNPEKVNSIEGPNKEVRVVERISMIPKSWRGEKGIESAEVVLYLKTKIEKMGHLLDLPDS Q9P7N3 VPS41_SCHPO SPAP27G11.05c; CHAIN 1..871; /note="Vacuolar protein sorting-associated protein 41"; /id="PRO_0000314101" MSVDESNSDSEIDSISSSDEDEEPKLIYERITEKFQGCFMNDTISACAISKEHFFFGSHNGAIYIYQKNGILLRKMILHSASVVDLSVDLESENLASCSMDGKMIISNITTRETTVHDFKRPLLSVAIDPYYSTRSSRQVLSGGRAGKVVLSEKGWLGNKDTVLQADCGAVYKISWYTTYIAWASDLGITVYSTEFGKVLGRLEPPKRLPNDEIFPYQLFWQSESRLVIGWSDQIMIVSIQRSNVANELPKISLQALLEIDSIVSGVLMLGFNILTLAYIANVEDFTSAIPSQRIEGCRPELRLIDSSFKELCGDAIGLANYSRLQPSDYHLLPDPSSNSHSFVISPNDIVYVRERNQIDHVKYLVSKEMYAEAIDAVKKLPEIPPSLQISELAKKYIFHLLGKGQYKEAGMVIPSLYNDNLAEWEQWVFVFAENDHLEDIADFLPTGENHLSPLVYEMILAQYLATDERTFNKKLHEWPTMLYSVSTIRNATLKKFKENQKSSTLTESLAFLYLEDNMPIDAFHLYLKLHSELCIDLILQHNLYDEARASVLLLMLISSKGKSSDTKSAMSSMLVQHVHSFPPQEVIMQIHSVPQFLYEYFCEFELMYPNSLMEYGDLKLDVFAEFDRKRFFDFLVNTQCYSLDHAAQICKQYNYLDELVYILGRMGNNKEALMLIINELLDIGRAIRYVKEQADRELWDDLISYSLDKPEFICTLLENIGTDENARNLLSKIPPGTKLPHMKKSISKLLADHQSQVQLYQSCYKLFKNESISMAIKYREQEQSGLEFLVKDNPFNSFGDEQLDYNYRKRIPMIYDLRTKKYIRPEDVRIDTDDVFKDDKIAYFKTRMHLKPEVQMRNKLDLLMMLYKQT Q9P7N4 TAD3_SCHPO SPAP27G11.04c; CHAIN 1..315; /note="tRNA-specific adenosine deaminase subunit tad3"; /id="PRO_0000310824" MVKTNISKNSPKEATVPELDWPFKLIKSHLETRKLETENVWIACFEPKYASKVTQYVKQIRSKQKESLLHCNRLRRIQDENGSLELQIIICPEKSMTANEIGKDFEDLGIVSKMIFLYAVPAFPPLTDEQFHEWNSVWPVSYRKHVQRQDVFTVHELKRIESILEDLINAAGASHKHGEIGCAAAIYDPTTDTVLAVSVDERSKLKNPINHCVMNAINLVAKRELSRRQNRTDGSKDRYLCKDLTVVMTHEPCVMCSMGLLHSRIRRLIYCKKQPLTGGIESLYGIHWRAELNHRYLAYSGWNKPVPSIKENIHV Q9P7N9 TRS31_SCHPO SPBC1718.05; CHAIN 1..209; /note="Transport protein particle subunit trs31"; /id="PRO_0000211584" MQSTNKELFRSSVSESLKSTAPLMGKSVYEQNLNKIRNSDVNLSSFAFIFSELIQRIQSQVSGIQEFEEKLNEHGYRVGQKLVELVVWRERNPKRETRILGILQYIHSSVWKYLFGKHADSLEKSKEASDEYMIVDNNPLLNKFISVPKEMNQLNCCAYLAGIIEGFLDSAQFPCKASAHSVPLSQYPYRTVILIKLDPSVIAREEVLG Q9P7P0 YOL4_SCHPO MOD_RES 669; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1718.04; CHAIN 1..675; /note="Uncharacterized acyltransferase C1718.04"; /id="PRO_0000317313" MQHTFIYDTCLWILSILIDFFFREVKTRGSFRVPRKGPLILVAAPHANQFVDPLILMLQLRREVGRRTSILVAAKSYRQRFIGLMSRAFGAIPVERAQDLAIRGEGKIFVVAEGDKTAIHGKDTLFTKHSVGDTLLLPNNYGSSHIASIKSDTLLYVKREFRGEDAERVLLSPEGSSYKVAPEIDQTYVYNEVRRRLVKGACIALFPEGGSHDRPEMLPLKAGVAIMALETLSQHPDCGLQLLPCGMNYFHPHRFRSRAVLEFGSPLSIPTEYVELYKAKKRREAIQGVLDMIYDALLSVTVQAPDYETLMVIQACRRLYKPAHIQFALPKVVDLNRKLIVGYNHFKHDPRVIRLHDKILLYNRQLYRLGLRDHQVQSLQYSRFMILYKLVYRCCKLFLLALGALPGAILFSPVFIAAHRISVKKAAAALKASSVKIQGRDILATWKLLVALGMTPILYSFYALLCCYYIYSYKLIPHSSIFVYTVPIISTFLFPMVTYAALRFGEVAVDIYKSIRPLFLALIPSKANAVYILKDERKQLVAEVTDLINKLGPELFPDFDPDRITTTIEKPERPSRFARRLSSSVASDVDNLSQLHDTDLNSEVSAPAPLQNVYLYSPNPSALPPSDEEEKDINDKAKLIRNALRQRMGQRMTEIRSRDTPPEEVFSESDEELSD Q9P7P6 PDC3_SCHPO BINDING 38; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 125; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 450; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 477; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 479; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 483; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2; Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1; COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Note=Binds 1 metal ion per subunit.; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Note=Binds 1 thiamine pyrophosphate per subunit.; SPAC186.09; CHAIN 1..572; /note="Probable pyruvate decarboxylase C186.09"; /id="PRO_0000090769" MKDNQQAVQLQQPTTIGHYLAVRLAQAGVKHHFVVPGDYNLGLLDKLQYNNYLEEVNCANELNCAFAAEGYARANGIAACVVTYSVGAFTAFDGIGGAYAEDLPVILISGSPNTNDIGSSHLLHHTLGTHDFSYQYEMAKKITCAAVSIQRPTEAPRLIDYAIKMALLKKKPVYIEVPTNVASQPCAAPGPASLITEPETSNQEYLQMAVDISAKIVNGKQKPVLLAGPKLRSFKAESAFLELANSLNCSVAVMPNAKSFFPESHPNYAGIYWGQASTLGAESIINWSDCIICAGTTFTDYSSNGWTSLPPKANVLHVDVDRVTVSDAEFGGVLLRDFLHELAKKVKANNASVVEYKRIRPESLEIPMENPKAALNRKEIIRQVQNLVNQETTLFVDTGDSWFGGMRITLPEKARFEIEMQWGHIGWSVPSAFGYAIGAPKRNVVVFVGDGSFQETVQEVSQMVRLNLPIIMFLINNRGYTIEVEIHDGPYNRIKNWDYAAIVEAFNAGEGHAKGFRVGNGHELAEAIRQAKENSQGPTLIECNIDQDDCSKELINWGHNVGAANGKPPAKE Q9P7P7 LDH_SCHPO ACT_SITE 192; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 105; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 137; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 137; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 168; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; SPAC186.08c; CHAIN 1..330; /note="Probable L-lactate dehydrogenase"; /id="PRO_0000168500" MTAGSKVFSNDSVRSSSFKSIKIVIVGAGNVGSTTAFTLLLSGLAAEIVIIDLNKKKAEGEAMDLNHAAPLSHETRVYLGDYKDCKDATAVVITAGKNQKPGETRMDLLKANISIFKEILREVTKYTKDAILLVATNPVDVLTYATLKLTGFPAERVIGSGTIIDTARFQYLIGKLYGLDPQSVNADIIGEHGDSELAVWSHASIAGLSLADFCEESETKYDEQALNECFKETKNAAYDIIQRKGSTEYGVAAGLVRILAAIIRDENALLTVSGLDSYSNIGDVCFSMPRKLNKDGAHRIINAKLSKDEDAKLVESVKSIKHAIESIGLN Q9P7Q0 YLY5_SCHPO SPAC186.05c; CHAIN 1..262; /note="GDT1-like protein C186.05c"; /id="PRO_0000316592" MINVESPLNLETTLGSLQFSHGSVQNIGMSISMIIGCELGDKSFIVTALLAYQYGRASVFFGSYLALFFMTSFAVLVGRAAPFLFPKSITHILGGTLFLIFGVKMLKESKEVRESQQSLENEFDKVEKIIVNEEDMKKTLELGLPASNRSSSTLKDKFFKVFSMSCFKNLFSKKFSRAFIKAFALIFVSELGDRSQIATIVMSAKEKVLDVFIGVNIGHMLCTMVAVIVGRYISNKIEMYKVLFFGGIVFMIFGILYIFQGF Q9P7Q2 PFL9_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC186.01; CHAIN 22..326; /note="Putative cell agglutination protein pfl9"; /id="PRO_0000353815" CARBOHYD 25; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MNVVKYIIFSFALAPLLLVNANTYNFTQIQKRSVNQAVLESSQDTNSVGGEASSTACPLFTTIYTNGITPGTTTIYPTSISTSGVSSNNIDETSVSSESIITSTITTTITSGSQLYTTTITGQNTPVDTVEVVIPTAGTFTTTLTSGSSYPVATTTVRTASGTQSGEVEVITPSCGCSPENSFHLKIDNDKISPSYVYMDPNAPVRTNGAGREGNMFASTNGDNEGLNLFYYDSTIQRVLTCDCQRPSYTVYIEDPIIGNGFSSAWNLIKNSDGIFTPVESRNNEPLHFHVDNNGRVWMTSQEYDTEVSSTDERNFRANDVTLQLY Q9P7Q4 SEC18_SCHPO BINDING 311..318; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 592..599; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 252; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1834.11c; CHAIN 1..792; /note="Vesicular-fusion protein sec18"; /id="PRO_0000084570" MDSRWKLPFMSNKGTPEQPMRKPLSGSYSHNSAGPTPNMSPFEQKPPLPTHMDVRRPSGPFRIVKATSTEDALTNCIIVSPMDFKQQYIIVDNSRVFSTKPVPGFPQGCLGASQPHREWASWSLNQQVHVADYDPYGPHGAPYLHSMTLEVDFQNRNRTTNEPFDGEEMAKLFCSSYQSQVFSPGQKIVFDFRSYNIKATVRTISCVDLLIGENQDAENTADTSKRGLLTSQTEIQFFKAAHSALRLKASMTRPASNAILQPGFKFEDMGIGGLDSEFSAIFRRAFASRLFPPGMVEKLGINHVKGILLYGPPGTGKTLIARQIGKMLNAREPKIVNGPEILNKYVGQSEENVRKLFADAEREYRDRGEESGLHIIIFDELDAICKKRGSSGGDTGVGDQVVNQLLAKMDGVDQLNNILVIGMTNRKDMIDEALLRPGRLEVHMEISLPDEHGRLQILKIHTSRMASNGILENDVDMEELASLTKNFSGAEIAGLIKSASSFAFYRHIKVGTTAAVSGNLENIKVNRNDFLNALSEVRPAYGVSEEELESRVQGGIINFGKHIEEIITEGKLFVQQVKNSERTRLVSVLLSGPIASGKTALAATIALGSEFPFVKLVSAESMVGMNENARVAHVNRVFEDSYKSPLSVIVVDEIERIIDWVPIGPRFSNTLLQTLMVLFKKQPPKGHRLLILATTSERTMLSRMDMTQSFDAEIAVPNVSNVTELDRIIQSIDSFADSNVRADTLQRLQNFTGTDAVNVGVAKILMIAETAKQDVDVVSCFVEAMARAIPME Q9P7Q6 MUG51_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P49842}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P49842}; SPAC1834.09; CHAIN 1..306; /note="Serine/threonine-protein kinase mug51"; /id="PRO_0000116748" MPALLKINKKKNGQTKIDRLFSKRRKTSLAIEKNHSKASMCTGQSPLNIISYNVPPLIVLRNKTIRNSIEVLVEEMFRDIQMRQQTNVLVAQCPRMIVETQLIGLFQSNYTSVAEELEQSIRTGDIRRLYLNRSDKFCGESCLILRPEFDKLFTYYLCKFKDQEHIYTLIFKLHKLLIENPLPSYTSEELKFNWEERRLLISMGFLILAGTDSYGISLPNLGIFTHILRNSRNDLSNYLKKRPYREVIESSLYNRNVSVACKKKNEAFFGWKFRLCDAIGAGLVDSFMTTCGRAFRLTKKGLEMKF Q9P7R8 YHV3_SCHPO MOD_RES 411; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 420; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC211.03c; CHAIN 1..1462; /note="Uncharacterized protein C211.03"; /id="PRO_0000303920" MEVPRASPNQEPLCSISPSSLVINEIITVVTAIRKTTRWRNSGVASILGVSTLKDEFLADGLESRWKTNGEKSSSIRYPLVMEFSQLKEDLTNRASLNGYDSLKLLSPFLRTIKSPRMTGYITSLCLSAILKFFSFRIISEESPNLALSMRNLSFAITQCRFESFDASQDEAVLLRVSRLMEELLRGPGKAVLSDDSICEIVETGLSMCCQSRLSQVLRYSAELSMTSILEKIFERLKYIDVKTDSEDFWDASEEHSIKGEEFHYKKITEGDEISNEIDPFGIGSIREVFRVLVSFIDFGKQKFSDNIKAMALRFINTALEVSGSHISDFPSLRVLITDTLCKSLLQLIRSDHTALLTNSLLVMTTLLQAMPGSLKLQQELFISYLISCLHIPSTTPRERNVETSLHKVVSSLDLSEEISPDRATPTSFTERKRFAFDTRNRPPEVRELIVECLGSLSRIPYFLIDLYVNYDCDPQMSDLAIDLLKVLTRNCLVDSARYSTANVPPLCLDALLNFIYYFHEHLQPCYNDPNNTFKDDVAKTLIESKKRKAIIIEGAELFNESPSDGIAFLTQHSIIKQSDNPTCIVEFFHSTNRLSKRVLGEFLTKGSNSHILNAFISAFDFKGKRIDEALRLLLQSFRLPGESQLIERVLETFSHYYMSANPDSMSSKDAAFVLSYSIIMLNTDQHNPNIKSQRRMTLDDFCRNVRGVNDGQDFDRNFLSEIYKAIKENEIIVAEEHDTELSFLYIWSKLQQSVKITEPFKRSSSNVHDKIVFLEVWKSIMAALIYVFSTATEDTVFYRVVNGIQQATEVAAAYELNEPVDYAIERFCQFTALDPSSVPGTQLNTAIKVEDRIITVSELSVRFGRDFRAQLALLVLFWISSKFGNIIDASWPLLVQLTICLARNNLIDNSFLPGFKLFGYQWFPFPEPPLNSGKPALSKEGGLLSALSSYLSSYANDEPPCPTDEEIQHTLCTIDCISSAKIDNFLTKLVDLKQPGLNKLLDSLLSLSNPSTSLLTDENTVDDNKVSSVEALSNIQSAIVADLLTSLFLGTRESLNKLERRTQILSYLLFQIEQSGDEKVINQLSLYIFEMFMDDDLKLSENSEDWGLFSKLCNLLNDKNIVVRNQSLSLFHQLVNKYPFLLESWIGLQLVQSAVNTNTADIDDLYRLLSKIPTNLLDLPMFQVYLGCVDTLIQTIVKQIAQILSKQKKGASKGLPFDKSILDNHSAELNDAFNLFLKAAVEYKVDSNESSEHFQDTRWKIIYDHVCKLCLSRSRSLRAASLSCLQRIVVEQLDQPHEVSYTMALFHLVLLPTMENMITVLTEKPEHKIFGLAQAQMFNIICKTVLIDMNVLSAQKEMLHTLWLKLMDVAIKLSSIHGSESMAEVMESIKNVFMILHGAGALAGPTIEVDPEIPDHLIKTWNTTWNNLFIYYPELSNDLNINNEAEMKKENLKNPSQTTTV Q9P7S2 RPN6_SCHPO SPAC23G3.11; CHAIN 1..421; /note="Probable 26S proteasome regulatory subunit rpn6"; /id="PRO_0000173859" MSSKSSLELANNAVKSNDIEKAIDLYKEVLNKGVSKDEKVANEQEQALTNLSDLYVRENRHNDLAQLVQQSRPLMANFSKAKSAKIVRTLIDKFSGEKKSLPLQIEVANDCIKWAIKEKRTFLRQALETKLISLYYDNSSYTDAINLINTLLSELKRMDDKMLLTEVHLLESKVYHAIRNIPKARASLTAAKTSANAVYCPPMLQGNLDLQSGILHADDMDFKTAYSYFYEAYEGFTSLDDDKKALSSLKYMLLSQIMLNSVSEVKSLLTGKHAIRYAGRDIEAMRAIAQAHENRSLADFEKALQDYKPELASDPIIRSHLSSLYDNLLEQNLLRVVEPFSRVEVSHIAELIGLSTVQVEGKLSQMILDKIFYGILDQGSGCLIVYDEPQQDKTYEAALEVIKNMGTVVDLLIENKASALL Q9P7S4 TAF4_SCHPO SPAC23G3.09; CHAIN 1..365; /note="Transcription initiation factor TFIID subunit 4"; /id="PRO_0000343443" MDLNNPPSKRFGDDDDIPANKRPKNEEYPEIPGYLGNRKPSYTQNPNSGPGKLHYASPRPNNVSSSVGVASGGDRQEADQLQDALISCGIQLKEEELNLSTSFYDPSSLNTFALTTEDRSRKSDFLNSFVLMQTVSNIVNLHRLKSMDSDIHALISMAVRDYLANLLQKMIVESHHRTSQLHTDNYKQVDNVRQTLANFAYKEYESEERRRTVLNIRRAEHEARLAELNSASTNEEGSSRRRKEQSSSAAAKNISEDAQNRMTNATASIMAGSALPSGGKKYSWMATDMTPMTPAVGGGFGIRKKDSNSLKPSSRDGVLPLQQEEKGIITIRDALAVLEMDREGAGRIFGRGAKAMMRAYIRLKD Q9P7S7 NOP58_SCHPO MOD_RES 33; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 441; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC23G3.06; CHAIN 1..508; /note="Nucleolar protein 58"; /id="PRO_0000350991" MFILTETAAGYAIFKAKDKLLKKRDALIEDLKSPEGASNLLKLQSFAKFESTVDALDNVSALVEGKVSSKLSSLLEGLSDSKSSTLVVADPKLGNAINKLPGLEFEIISDSSVQDLYRGIREHLSSLISGLAPSDLNAMSLGLSHSLSRHKLKFSPDKVDTMIVQAIALLDDLDKELNTYAMRVREWYGWHFPEMGKIIQDNLAYARVIKAMGMRTKCSETDFSDILPEEIEATLKSAAEISMGTEITEEDLDNIVMLADQVLELASYRAQLSEYLRNRMQAIAPNLTALVGELVGARLIAHAGSLMNLAKQPASTIQILGAEKALFRALKTKHSTPKYGLIYHASLVGQANSKNKGKIARVLATKAALSLRVDALSDKDTTNGNIGLENRIRVENRLRSLEGGKLLPLPTAPVQQSKVQINGTSAYSTATDAVTKDAEESQEDVEMDIVIEKKKKKSSKLKEADGESSKKEKKEKKDKKHKKSKRKSEESEDGESPKKKKKSKKSKD Q9P7T1 SIB1_SCHPO MOD_RES 752; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"; MOD_RES 2206; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"; MOD_RES 3288; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"; MOD_RES 4439; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" SPAC23G3.02c; CHAIN 1..4924; /note="Hydroxamate-type ferrichrome siderophore peptide synthetase"; /id="PRO_0000339124" MKNSNEEDAFSTQISQLGPMRPSSDAPYHVLSLPFSHPYSAFLDAWSWLFCGITGGEVSFFFFPVSDDVIPNTNPKNCQCYLYHSTNSQLEPLEVFHLHKLHSAVFTSRRDPSFADDLFESSKPCLNQLLSYFSDITAFRSMDVVADIAFVCSPNFLTLKWNSSLFDDDLARLLFFMINSKITNYDLPFSILNSPCSDLCLNSSSLANYLHGCFYHNTLSHPYQDALKFIYEIGDDLEDTFRSFSFLELHSLAIKLSKLVTCKNEVVPIMVSHSPALFVGILAILYSGNAYCPIDVETRTERVHFISKDVDASFAIVSEEFVNRFPNNTIILKVPEYNESMEIKVDDEIPPFPFPESLDSVAYVLYTSGSTGNPKGVAISHRAATNSIKSHGYLYPMFGLERGDAWLQFANVTFDVSVFEIFGNWNNGLTLVTSKRQNLIGNLEYLIYDYKIAALELTPTVANVISLDENKELFTSVRMLITIGELLTNRIIDFWGERLVNAYGPTEAAIHVTLNPSKALTTVYLVGVPLQSATICVVSLPTEDSQPHVLHEGFLGEVCIAGPQLSSGYINRPEINAKAFVEVQYNEQTLSIYRTGDLGRIINGKLYIFGRIAGDMQIKIRGRRIEIGEIESKLAPSVDSLAIEKIGDNLVAFYVGDEMKLRKHAESHLASWMCPTKYVGLPGFPRLASGKTDRKALKIQFSASDKHSTDFSSFNQSELLVANVLHEICEKRFNSVVSISRFSSIFDLGLDSLDIVYFVRKIRSLGFEANPSIVLTSKVVFKIAESLILLKPNEVQSKNNFLNKCTPLQKGMLYESFSNNGNLYFNHTVFKIAASPEKVKLAWEKLLDTHTILSNGFALDENEGFTRFILEKKPPLYSYSKNCLECIQKHFTTKEFDEQFLNSGPLDAAVIYDSSNCYLSIVWHHALYDGWSIDIIMQQLFMLIHDRRLTIVPQFEDYVQELESLRRLNYKNCISFWKKYLKDFKFKSLSYQREKMGVVELSSNISLLSVENICKQLQTTPLSFFLTAWSTVLSSYLKTNDFLVGTVVSGRVNSLLPNVDYVIGPCMQTLPVRIKLDDELSYKNLCQNLFKELSFVLKHSVMAISDFQEELLVSNLFESILIYQQSGIPSVDESFISLIHSTDHVEQPLLIEIEKNKGYKFKLTGYLSSELLNNLLNDFDKILNFILYNIESKIQTHASFNVTITEHNHVESKARTGFSKREEKLVRSCLSKILGNTVLSADVFENLQNYGFDSLCAMRFFSLLRKSSGIGNLKIPNMKSNPTIASLCELLVLPTETLSADNEITFYEVSDIQHEANLDIESFQYFPCTPMQQALLASSEKNGVEYYYNKYLFETGKSSQEEIYLLFKTLLNNLPILRTCFFVTRSKKYPYCQVVLNEPNFYFQVLPYKGESLSKYNLAEIPLLDSKKVPIQIFFLQGENKNYVLFCIHHVLYDAWAFQLIMDDINHLLRKENPKGSQSMLKFISYLHRYNKNVDLEIWSKIFLGFKPSKFPELCKDINPEQRTYKCNLSISLSQIDDLCNGFSFTTSTFLQCCWAKTLSFLLNSRDICFGNIISGRDVPVDEVVSLVAPTFNSFPLRVLLDSKLSFAEVCGQLQRLKETLQEHQMTSVQSICKSLTVKSLFDTVFIIQPQLLSDRTGPWKLLNESSSMDMRFIIELLLGSDDSPLTLVGTGTGKSGKLVCNLYKTILKHYVHYGLSTSVPLYTSLEKHNLISRSPSSPPPIHTNFDTNADIITLFEKEANEHPSSIALHFVYNVDKENIYSYKFFSEYSIKASYWLHSIGIKKNDVVAVFIDKSLDYYSLMLGVLRIGAFFFPLEHCSSLNFAKENLLRTNVKLLIVDKFLPFEDVNQVEIDKFRQVVDKLPTVEIPNESRSSAFIFPSYELAEGLTMMESSSFMDSIISFIDSTCFPSSSRWFQYAPSSTACQMFDCFMCWFFGCTLISGPQLFLKNNLKPLLLATHASHLITTSSIAASLKGEDIPSIQRLYCYEGPINNYMIKSWGSRLSYIYAFKPLICSCVPATEYLESNIMMVGIPLKGLIFAVVNSDTNTLAPIGSSGELCIASVKKSGNTMMDSQRVFTFENRSYYRTGDIVRILAGGEFEYIKKKSFIFIDSMPLDIEGKINVDKLRDLLNDDNYIFKVDNDEFPKNDNILDGFQEKVILTISDFASIPFEKLSLNTKLSTIGIDSISAIQLSKDLREIFHLRISALDILNSSTINSLIRKLKRRRTESHTRNDKIHESIDQFFKDIRKQILIPQTLCDKIEQILPCLASQCSMLSRFYTNGGKDYLNYSVFHLQKYNDPLLLRSSWENVISNVSILRTKFQTTKHKRSPFCQVTYSKVDIPWSMELHAASVEKVLNEYLELQRRDLLQGKNVLPYSLIFVRTFSQETFLIIIMHHALYDESSLRKILGLVEKSLNSPIGKFNHEPIVRQIELLKANYEEAKAFWIKQLLSFQPTNFPSLTACRIDNEDRMLTKKPCALNYTNLTKWCNAHDVTLQVLGQLVWAKILASYCAENYAVFGTVLSGKSVLTDVDDNIFPTVTTIPCVVKLQGTVEDCLRQLQKFNLDANKFQFTSLLDIKKWLNLGPSEKLFSSLFSIYVDNDIPLKLFNDECKAQGFIEFPVALEMRFSESTSELTLNSAVNYIPQAHASLILDQFNAILTTIFNNPLQQIEILENSLPTQLLSIKPAIVGDYPTEIKYLHQFVEYFAQKSPNSCALEFALDINQDSVQLIRLTYSELNERANKLAHNLKSYGFRVGSIIAVYFDKCIEAFISMLAILKAGCCFLALDVSAPTERIRYIVTDSTAVLVMSTGELYTKLLNASINVTILDASDPGNYSNNIENPYTKDFEDSNLAYVLYTSGSTGKPKGCCLTHHNVVQCMLAFQDQFAGEWDTNSRFLAFASFHFDVSVLEQYFSWSTGITLVAAPQSLILQDLPTAISALKITHVDLTPSLASILTPKTAPLLRVFITGGEQIKQELLNIWGDTRVLYNFWGPTELTIGASAFRKVPKNAKVSNIGPPFPNCSTYILSKETKVPVLLGGLGEICMGGNQVAKGYLNLPEQTDAKFYFDRRFNDRIYHTGDLGRLLKDNNSLEFCGRTDDQIKLRGQRIEIGEINAVIKSSSEKILGVYTLAVVHPVLRKQQLVAFIHVKGISASHLIVHDHKDPSLIGFINSACKASLAKYMVPSFYVFISSVPLTPTNKFDKKKVIEEFSRLSLGQLSSFAPAREENDNEGSNVVEPKLLKIIADFSDVKVTDISPQTSVFELGLDSISAVALSGLLRKSGYDNANPSLILTSSTISNLGFALNTQTNEELEDSIKVNSIIKLPSCSQFPFHQYIELINPCLPLVEGLLFELERSNNENYYNSFFFLFEKREQADQFINNFKLLRKQYEVLRSSFLKSDGEYFQVVWKSDFIAEVDVLNNDSLIKTVRYSLKCEKGFFLVTVTLFHGIYDGWSLDLLLNDLARLCSRKTLAPRPRYSKIVRQLLINTSLKKDTKEYWLNLFRSKNIYVPIFQGKLDMAITLGHKLSISSAKLSTICRSVLKASVNSALLTSWICFLNSIGAINCVGIVVSGRSEISMDCLEVMGPLFNTIPFPLFLEKDESFDCLVRRCQLTLASMIPYHQTSLREIKKWLRRSELFNVLFTYNLHPSVIKQCEFPWSFSSESTDTGYPLALEIEEDVDGTMNLHLSSNFKYIGQTEIIGLLDSYDCYLSSLLETSNAKISSRPNVLMPNQPEVKQYIPNVWNDVLKKLITILSPKVIITKLDFERDTFVHEFGIDSIDLIWLASKVSEAGIGKLDIGLLMEKPTFYRILQLLCETSANHSTSLKHEFGTLNTLLSKYLTDQDAEDCYPATPIQSGLLLETMNQKNLYQNDVLFSLDAEISLEKLQNSWKRLCQKNAILRTHFAISEDSSEPMVIQIVDKFEARSCLNQIKILPSRFTNIEDTLRFLRHDEEAKRFLDPFKNPPYYVQFFEIGAKNYMFVQMHHSLYDGWSLSLMYDELMQLYRDEQGNSRKPFKDYIIQLYSLKYDYDFWFKYFENLSIPKPLPFLSNNGKFMSSMMSTVSLPSVRLACQLYGVSIQSLVFFTWGYYIASVLNCPDIVFHTVLSGRTYIEGAETVMGPCMNTIPVRIKFEGALQTLKKTSRMLINLAKQQHTPLSWIYKTYGNVAAIPMESILVYQHLPDSSQSETFLNVVTDNSAVDYPIAIQFEIQGDTLNWLTSLDLARVDGDVANQLLQTIDKIFSNLTKGSFEKLTFNFSNFVKYRQYQINLKDFRENLLLTEEAISDCDLLIIDERVLVVFILFPEPDAKFPYLVLNEEIIRMLKSYIKKFRLTLSSAMVPDILVPVSYLPRSLDHSENEGKLLNIYNSISADNLKILSAVHEIHLNETEKILLEGFSKIICLPQDSVDISNNFFQLGMDSIRSIHLCSYLRNKGLNVSVSDILQHSSIEKLAHYLQYEKKESSSSFDIASFQLDEYLNTLPSNIPINLVQKILPCSAGQMYALNAWYNTEKKKYFHTFFYTTEEKIELLKLKLAWAKLVKSSDILRTTFIRSSSPCYPLLQIVLKSFECPWEHYITDNLHDTCLKIQKRELVTNTTLQEVPLRIATIETSGKFVFCLTIHHALYDGWSLDIMINYLSKMYYDDSLTIVQQNSQLFLSTVLDPAVGLSRKKFWNNYLTNYKPYTFLEKPSASQEITLFFPKLFSLDTVYSSVRSRGLTVQSVSFAVFARLLANEVKQEDVVFGIYVSGRTLDVDNIDELLFPTFNVVPLRVTDTFRPLGEIALEIQSFLNEISGNLQYISLLDLPVHGMMDIAVNFLSTGDNNEPSKVFSVYPLKLNNAELKINEVETTIDGCEILFGNKPKLDFELAIRDGYLEIGLFCQSSIFSKREASVFINNFVTIIKEIEL Q9P7T7 POF1L_SCHPO BINDING 40; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 41; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 48; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 97; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 129; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 131; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 165; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 206; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250|UniProtKB:Q96T66"; BINDING 214..217; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q96T66" CATALYTIC ACTIVITY: Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1; Evidence={ECO:0000250|UniProtKB:P25576}; SPAC694.03; CHAIN 1..249; /note="Putative nicotinamide mononucleotide adenylyltransferase"; /id="PRO_0000350758" MDQAKKYANLLDSFRSSTEDILLLERLEVSDKPIYVLDSSFNPPHFAHLGMCLSIPKGSQLLLLLSITNADKPVAPAAFNERILMMEKLKTLIHNCTVSVAICKHALFVDKCRSISNKLGPREQVYLVGFDTLIRILDCKYYKEKAMQQVLQPFFSCSQILCFSREVDGTTTDDQAQYLEKIKKSLLPNIPSQWSEKIKLTKLKGNVGFGVSSTRARQAIISGDEETQRKIIPQEILNVIKVIQPYRHR Q9P7T8 YIW2_SCHPO BINDING 757..764; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPAC694.02; CHAIN 1..1717; /note="Uncharacterized helicase C694.02"; /id="PRO_0000310784" MSEEIAKLTTVQNYRLVDLIGDFAGEELFLIDGDSLIFHILAKDSQFLAKNGVQILYAIYLLEKELARFKSARLNFCIVFFKNWEALYSQYDGILHASLLLFRRVAIRHLRKHVPVYVFKSLGDSQWSIFIAKHRPYGFMVLDSNQNTKEGGLVISDEQVMVFKSFIFFALSDGVPVALLGSYQFVDNKILVCILPSFFTRSSESVENASNLISDYLKKFGKPRQSIELPDIAVDACPSNASRIQTLSAAWLLLNEKSDLNVDLCKILIILTCMLEELSLNDRFQPAFPLYEDPAIQKFIISYLNATNTILQLLDSKVDGFHDIFDGRLFIRLVVDAALGEFCIPDICRESALSLWKLILDIAPDAGDLFDFPSLSSISKDLCVPIETPVSEIDISLTAYNDPVISPYYDTEEWNLEQREEPGIETVLDFSKLRINDKTMTSKRFDDLSATRKTGDNTKDRKQANKVRRQDQFFISHIQKYASSLTGAKGGQLKRQTIFTQGPNSTKESKQAVKEETSVKNSPKGKNTKNGKAEKEKPGKKSKAPKLSKAEQIRAEIAARKVEKEENKNEVIWNETKNDLGRIKDLNLRAGRLAQLLNTRTYDPYIENEMRLYRIRVLLSLWTACCVTDEGKEKNIKIAVEIFREISIVYPNPITKQVKAALDETLTALGFENVIRKMKKLESKPLSFPFVLPDLEDEEFDLEVPYTSPTFQLLHFGEYMERSMGSAPDSRVAFDPDEWQRETLDILDRDESVFVVAPTSSGKTFISFYAMEKVLRDNDDGVVIYVAPTKALVNQLSAEVYARFNKHYPHAGQTVWSVYTRDYRINNPTNCQVLITVPHVLQSMLLQPALANAWCPKIRRIIFDEIHCIGQMEDGLVEEQLLLLAPCPIVALSATVGNPQEFQVWLSALQRAHSYPIHLIVHEHRYSDLRKFVYGGAKEFNGLQEEGDLGQIAFIHPAAAMSFSDGSTTNLAFEPRDCLQLYYAMKLVSKGDFKISRKLDPDRYFEDIPFIKKVDAVGYEKKIKATIDTWASLPNAFAPNSPFQALIKHFCSEPQKVVNSQLELHNSAYSLDAISQNLLPMLKDLHSKELLPAICFNYDRQECEYLAEIVFKTLVEKEREWRENSEEWKEKMREYKKWQSTANQRAKQMEKFEKSATEKQKEQALKEAGDISWIEFFDPEEPSPEFSFAGAKSTYGKEELYRDLEALRRRQAVPEWYVDALYRGIGIHHSGLNRRYRQIVEVLFRCGQLTVVIATRTLSLGINMPCRTVVFLGDSLQLNALNFHQAAGRAGRRGFDLLGHVGFLGVPLHKIYRLLTTKLWDIQGQFPLTTSLVLQLSQLISGSQAGPFARDTIHALMDEPKFMANGSILSNQVNHHLRFVIEYLRREGLLDVYGNPINLASLTMHLYYTEPSNYAFMNLLKAGVFHKIAEKFATEKFEAMRDTVVILCHLFGRIRMNEQYVMTLEGSTDLAQSTVVLPPLPTEIADVLDAHDQRVLDLYKTYAWYYQKHGNIGVAANKLPLSNTTIEGSAKLPSSLSVGVMSEFCGLAGYNESMVGTTSSFLDKVPDGIFLKTSRLPIFEANKAPYNAYLLDFFTHGSVDMLIEQNNLKQSEIWFVLNDFSLVLATICSCLGNLLNLVTDEDIENAMSALEGSNAVQATTESEATGADWMQNMNGNYSTTLASPELEEKMDMNLFKVYCMFLEVRNQFDAKFRKMWA Q9P7V4 KTI12_SCHPO BINDING 8..15; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPAC30.02c; CHAIN 1..281; /note="Protein kti12"; /id="PRO_0000339141" MPLIIVSGYPSSGKTTRSNELKKALEDRIHQNIDNTKDYRVIIINDESLNIEKETYRESKNEKAARGLLYSAVQRELSKSTFVICDALNYIKGFRYQLYCESKSMYTTHCVIHVAVPQDLCRKFNSNKEQPYPDDVLEQLMFRYEEPNGMTRWDSPLFTVLHDDASCPIDDIWSVLIHNKNVKPNQATMVKPPAEVNYLYELDKTTQDVIMLILDNSNDTSLITVPGSKLQIALPSVTVSLPLLQRLRRQFIQINRQQSYNTNVLKEMFVEFLNGQFETLD Q9P7V5 SEC7B_SCHPO MOD_RES 44; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 122; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 597; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 653; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 654; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 669; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1110; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1606; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1609; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC30.01c; CHAIN 1..1822; /note="Protein transport protein sec72"; /id="PRO_0000120216" MQDASEPVINMPALPMNSVNEQHDRHEDLPEVGTTSVTKIINDSDNEDDENGMDLGRVASESLEGDAVVSIDINTEDSSLSPAKQENEKSPEGIEQKYQEEDLKDDKKSNETIATPVPDAASRASLEKQKSGLTNLEKSTHVVLIKCIEQLIQIKVCMKNEKMKNLMEQLKPLLQTECQFDKFLIVELFQYCFESSQDEVMNISLDTISKLASFAYFSSKDKTPASFGPPKSLLQCMVDMVCDSINDEVVDGNLQLNVVKALSAFILCSEQDSMLHGAILLNSVRKLFNVFLLGDSDTIQSVAQASLTQAVTVVYERLRASHTQSNSTSALPEEDASVTENWVHDEDEPDKKITLHSMASAGTSSLDHVKVDADDPAVTSVENSSIQDAFLVFRSMCRLAVRQTSPDKVSNIRSQAMRAKLISLHLIYRILEKNSDLFMDPTLQFRGIPALKGMTLVHASRQYICLVLSRNAVSPVPQVFEVCCDIFYLMVFSLRAHFKQEIEVFFREVYFPMLDLKNTSYNQKLHTLLIIQRICLNPRALVELYINYDCDRSSTTNVFEQLLFSISKVTTNGPSETISEDIEEILPSLESSERSSTPFLNTNSASLKSEVVQLTTFSDFQLKLKTLQCVLDILQSLSNWAESGLYLSRRGVSTDEQGFVGDYDALSRSDTPVTNPYYNGKQSFEANSHSSSSIALADPSQFESNKQRKKLLRTCINKFNYKPTRGLKMLSENEYVDINDPKAIAEFLFRADGIDKTTLGDYLGEGDEKSISVMHEFIDCLSFINLKFVDALRRLLQCFRLPGEAQKIDRIMLKFSERYMKENPSAFANADTAYILAYSIILLNTDLHSPRIKNKMTKEDFIKNNRGINDGADLDEDYLGFVYDDILKNEIAMKDDQELAAIAPLMNNFSTSSGFTTFTSNGRDLQRVACIQASEEMANKATSVLKKLLYQQKHGSQKTNVYYNATHFEHIGPMLEATWMPILAALSNPLQNSDYVNELNMCLDGFQLVVRIACLFDLDLIRDAFIKTLTNFTNLHSTSEIKLRNTMVIKTLLRIASTEGNNLKDSWKDILTIISQLERVQLIGVGVDETEVPDVINARVRRKNVNIGSSNSIRHVSGSTSRSTRTRSLSKPLSPEAVSELMSTEVVLSIDRIFTQTSSLSGSAIVSFFKALCEVSWDEITSSSDLEQPRLYSLQKLVEISYYNMQRIRVEWSSIWNVLGRFFNMVGSDENRHVAVFALDSLRQLSMHFLEIEELSLFSFQKEFLKPFEYVMASDTVVEVKELVLQCVKQMIQAKISKIKSGWKTLFGVFTFAAKARSEILISMTFDTLVNLFSEHYDTLMQQNCLIDMLISFTELCKNGTNQKISLQSLEIIREVYSSLSTMIKEGLSSKPSVNETFSKYVFPVLFAYYDIIMSAEDLEVRSRALQNLFYIFLEESDDFTEETWEVVSRKFIFPIFSIFGPEADEATVMLRDEEIRTWQSTTLVEALRSLVTLLTRRFDKLHNLLKGYLWLFSNCICRDNITLSRIGTNCMQQLLSGNAYRFEVKDWNLVADMFIELFKETTPHQLLLLETFSNGQGAPVYSENENTQLSHKRGGSLPETSRSISTSSISPEKQMEFRSMIRKCILQLLLISIVAELLDNEEVFNHIPHEHVLKITVAIYDSWQFARKFNEDKSLRITLLNVGFMKQLPNLLRQETASALLYITLLFRLLKTRDPLGKTETDQKIHKLLFPVCAEMLDMYASLVVEKHTRNHAAWQPVIATILDSILNLPLELFSENIHTLYFSCCSMIAKENLDDQLRELLKNYFNRVGHILLNLNAQQE Q9P7V8 MPCP_SCHPO SPBC1703.13c; CHAIN 1..311; /note="Probable mitochondrial phosphate carrier protein"; /id="PRO_0000310804" MSTPLIPPAPPKKTLQLYTPQYYGLCTLGGLLACGTTHSAITPLDLIKCRKQVNPNIYPGNIAGFKTILSKEGLRGLYTGGMPTLIGYSLQGCGKYGFYELFKHKYSTLVGAQKAHEYRTSIYLAASASAELLADIMLCPMEAIKVRVQTSNPRFANTTREAWSKIVTNEGFGTLYRGLAPLWFRQIPYTMMKFASFERIVEALYTYIGKPKNMYSKAEKIGISFAGGYMAGVLCAIISHPADVMVSKLNSNKKAGEGAGAAAARIYKEIGFSGLWNGLGVRIVMIGTLTGAQWLIYDSFKIMCGFPATGA Q9P7W6 MLH1_SCHPO SPBC1703.04; CHAIN 1..684; /note="Putative MutL protein homolog 1"; /id="PRO_0000178007" MDVNSRAKIRPLDQLVINKIAAGEIIERPENAIKELIENSLDAGSTSIDVLLKDGGLKLLQITDNGSGIQYDDLPYLCQRFSTSKIDNFNDLQHLQTFGFRGEALASISHVAKVTVVTKLSSDIHAWKAFYVDGALAPISPGMSPAPQPCAGKQGTVITAEDLFYNVRSRKSALKNGSEEFRRIMILVQKYAIHNDQVSFNCKKVGDTVASLSLSSRLSKADKIRHIYGPRVASHLRDFSLGEGQSSIVGFSANGFISNADFQDKKSNLILFINNRLVESVELRHALEETYAKYLHKGASYFVYLSLNMSPEQLDVNVHPSKRIVHFLYDQEIATSICDKLGEILERTDTERSYPLQAMIPSISNTKNAESSSQKAVRTYENYLVRTDPRERSIKSMLSDNFLQRSSNNYDNEIIEKVDSANSNKNATNDIKDLQTEEIVEEGNSIDLESIKSLQKQVINSMHVLATNILTEHKYVGLVCPTRRIAAVQHNIGLYVVDYGKLSYHLFYQICLTEFGNYGEFVLETPLSISDLFEIVNGDEDKSESEKFTRLLVSRRDMLKDYFSISVTSGGLLTAVPMLSPKYHPPFEQLPLLISSLTPKFFDWLDEKSCLNGIMKAIAKFYVPLPLSYEESDVKSIRSLESCLEDYLFPEFRRRVICPKKVFEEKCIYQITSLPRLYNVFERC Q9P7W9 RNP1_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; SPBC1703.01c; CHAIN 1..217; /note="Probable ribonuclease P protein subunit 1"; /id="PRO_0000128423" MADPLYSSLKTVNSTSKVTPESLVFQTKILTPEEAKNVINEKIAFKPLLLVPSLNLEKQGDRKESVASKKRKKLSSKEKKKLQLNVVPKIADYSQFKHLHSMWCSYILEVIAGCTGESLMAKLAKAEYQGAYMQVLRSKSTTRVGLEGICIHESKHMLSLITKENRVVRVPKQDSVMKVIVDVPQRKLVFELYTQHLLLRAGDRSNKRFKSKNTIDL Q9P7X1 MPPB_SCHPO ACT_SITE 69; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096" BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"; BINDING 70; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"; BINDING 146; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10096" CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000250|UniProtKB:P10507}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P10507}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP23A10.15c; CHAIN ?..457; /note="Probable mitochondrial-processing peptidase subunit beta"; /id="PRO_0000026783" MLRLQNLPKLVRRFATTALPKTETTTLKNGLTVATEHHPYAQTATVLVGVDAGSRAETAKNNGAAHFLEHLAFKGTKNRSQKALELEFENTGAHLNAYTSREQTVYYAHAFKNAVPNAVAVLADILTNSSISASAVERERQVILREQEEVDKMADEVVFDHLHATAYQGHPLGRTILGPKENIESLTREDLLQYIKDNYRSDRMIISSAGSISHEELVKLAEKYFGHLEPSAEQLSLGAPRGLKPRFVGSEIRARDDDSPTANIAIAVEGMSWKHPDYFTALVMQAIIGNWDRAMGASPHLSSRLSTIVQQHQLANSFMSFSTSYSDTGLWGIYLVTENLGRIDDLVHFTLQNWARLTVATRAEVERAKAQLRASLLLSLDSTTAIAEDIGRQLLTTGRRMSPQEVDLRIGQITEKDVARVASEMIWDKDIAVSAVGSIEGLLDYNRIRSSISMNRW Q9P7X3 FRG1_SCHPO SPBP23A10.12; CHAIN 1..245; /note="Protein frg1"; /id="PRO_0000220773" MSMRLTFKGDKKIQKKKKKNTKSLQSSLESAENDPFWTDANELNELEGPAVIYKIDDDAGVSLGIEEVKESCVLLPLDKVSLEPELTRQVFLLSILNNTILLKSCLGKYMSCSKSGDLYCTQEAVGSQEQWIAENLGSGFWAWKSVSTKKYLTLSREKQDQAIACVSDTVIPEAKWRIRVQTRFLKKNKSSLFDNPTIHSRQLESMAGRKLSTDEKKTLKKAFKEGVLHEALLDLRVSSRSDKYG Q9P7X4 YH6B_SCHPO CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000250|UniProtKB:P38288}; SIGNAL 1..22; /evidence="ECO:0000255" SPBP23A10.11c; CHAIN 23..507; /note="Probable circularly permuted 1,3-beta-glucanase P23A10.11c YJL171C"; /id="PRO_0000014203" CARBOHYD 480; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIAKSFIASFLFLCFAFSGVKADGCSEENGYYYCNQASEVEFTNVGYSSTYNEITNMDTSSCSCSSTPKSYGGNLAPFDEEFSFHFRGPIELKRFAVYYPDTSNALSSLRKRSNNQHMKRHPHHKRDDVIDSTLTVYETVMYTTAVYGDSATTPAASEAQASSDILSSLASLSSASTDNLAASVTPTTVAASVASSVDTDSASATISSVVDSATSSVSTVIPSSIISAAPPDSASESTPASTSYASSTTSATSTSTTSGSSGSSDWGRSSFYEADSGTSDNIVFLNNMGGSAGSGVWSSCFGNSLSFAASNGVDGASSSQVLENILVASDKEFSIWTATECNNDCGYYLPGIPAYHGFSGAKLVLMEFIMPHDSSSSYNQDMPAIWSLNAQIPRTLQYGNADCSCWTTGCGEFDIFEVLSTGNEKMIPTLHGSQGSSNGNGGGAGSSDYFARPTSSSMIGAVIYDTSSSGIYIIDVTDQNVSFDSTYSASDVDAWLQSGATIVQLSS Q9P7X5 PPK32_SCHPO MOD_RES 632; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP23A10.10; CHAIN 1..749; /note="Protein kinase domain-containing protein ppk32"; /id="PRO_0000256832" MLANALRLVSNSKKIKYDYDIQKENSVQVGPWTVYSASKKGTNEEVSVFTFDKKNLSTLLKRGSIDSNLKTNYVLELLRKDVSSLSRLRHPSLLQVVEPLEESKSSMSFVTRRIQSMLQDFIKSSNGGFSNYGSSANGKSSGNALEEVEIQKGLLQIIDGLVFLHGSAKVIHYNIRPSSVVVDAKGDWKLCGFSFSQSVESARYEFNDYDFGIPSSLQQSMDFLAPEYITHEIAGPESDVFSFGCLIYSIFNKNQSIINANNHLLSYEKEITSLNSPTFIESKNLPSENLKSLLKETLAVDPKQRASMFELERSPYFTGSAIAALRFLESFPEKLPSEKVSFMESLSKNLTTFPYRIQSQKILPTLLDHLNDQKLVPSLLPCIFEISKGLDSSIFSSKVFTAIFPIISAANSYPERVPLCIFQYMDCLKSKLPSGEFLSKIVPFIYGCFENSSLNVQTTSIQILGTLLDIIDVTTVKSSICPKLYHSFSVTNQLDVKVAILDTFNVFINQKFLDSFAIVDKLLPVLEKVKTREPTVVMGMVTVYISAGAIIPEETVHEQVIPRLWILSVSPSLSLEQYNKCMREIRSLSDAVQKSHAKKLQSKPSSVVPNRITTDPFSSQTKEATSKPSSISPNKATTNIFTSQASLSSQGVARETSSASSYRSYSQRASTPAVTAKSSFHYATPTSGLSNFNSVTPSSSASLYPPLIPSEARTPSVQPANRRVTTPVVNQNTVTSDSSNDLGGWKSLL Q9P7X6 PSF1_SCHPO SPBP23A10.09; CHAIN 1..202; /note="DNA replication complex GINS protein psf1"; /id="PRO_0000219039" MENGLGNRSNKLIRDSKRTQYLDYLPPYQADTVNDVVNEIRAADRESLGILQNVTHEASQPFQPQDHPSEAAALLMFHSSSIYNKRCLMAYHNLRLQRLRQYCWSGGKRMESCLDTSLSTYERDYLTRYSELLAAYKGAWSELDLTGSLVPPKNLFIDVRVLKDVGDIETEYGTINLTKNSQLHVRATDVERLIAQGFLAKL Q9P7X8 RPA2_SCHPO CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:P22138}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000250|UniProtKB:P22138}; SPBP23A10.07; CHAIN 1..1174; /note="Probable DNA-directed RNA polymerase I subunit RPA2"; /id="PRO_0000048079" MSFQTLERERTFKNPPKDGTSFPDLQKAVKPHVDSFNALTNAGLLNYAVKEIGEKCAFDSITQEEGGALKFGNKISFRVDEVQIAKPMLSSRERSSINRKVYPAEARERLTTYKSRLVLKFSWSVNGGPRQSEMREVGMIPIMVRSNRCHLEGLSPAELIAHKEESEEMGGYFIVNGIEKLIRMLILPKRNHPTAIIRPSFANRGTSYSQYGLSIRCVRPDQSSLTNTLHYLNNGVTMFRFHWRKNEYLIPSMMILKALLETSDKEIFEGIVGKDLGNTFLTDRVELMLRAYKSYGLYSQTETLQYLGSKFRVVLGVAEDLTDVEVGRFLLQKVVLVHLREAKDKFRLLLFMIRKLYALVAGECCADNPDSPQHQEILLGGFLYGQILKEKIEDWLNSIRAQINLDVRRSAPGVDFSDRKYLTRVFSKINNDIGTKLQYFLSTGNLVSNTGLDLQQATGYTVVAEKLNFYRFLSHFRMVHRGAFFAELKTTTVRKLLPEAWGFMCPVHTPDGSPCGLLNHLARKCEIVTHPSDVSQIPSLLLSLGVDPPSVVGHESGWGCVQLDGKIVGWCTYKLAKHVADVLRLMKIEYAVKLRNGTATEPAKVPLDLEIGYVPPSHNGQYPGLYLFSNPARMVRPVKHISTGELDMLGPFEQVYMDIACFPKEIVPKVSTHVEYSPTNVLSIVANMTPFSDFNQSPRNMYQCQMGKQTMGTPGTALRYRTDNKLYRLQTGQTPVVRPKLHNTYGLDHYPNGTNAVVAVISYTGYDMEDAMILNKSAHERGFGYGTVYKGESFDLSQKRRRGEPVVHHFGFAPGSTPRREWLQKLDADGLPFIGIKLEDGDPIVAYYDESTGQNFIETYHGTEPGFVDEVRLLGNDVGDSECQQIHVKLRITRSPIIGDKFSSRHGQKGICSQKWPTVDMPFTESGMQPDIIINPHAFPSRMTIGMFIESLAGKAGACHGLAQDSTPFIYSEQQTAADYFGEQLVKAGYNYHGNEPMYSGITGQEMKADIYIGVVYYQRLRHMVSDKFQVRTTGPIHNLTRQPVKGRKRAGGIRFGEMERDAVIGHGTSFLMQDRLMNCSDYAQSWVCRDCGSIISIMSTISMNGVGSASEVRCRSCAKPALGLEDTSDIWQDGSGKKFVGGTNTTLIALPSVFNYLTAELTAMNIKMMLEVK Q9P7Z3 EFM4_SCHPO SPBC839.14c; CHAIN 1..238; /note="Protein-lysine N-methyltransferase efm4"; /id="PRO_0000116780" MSGLPESKLGTKQYWDNVYEREVSNFTEFNDEGEVWFGEEAEERIVQWLEDHISTSFREVSEAAPFRVLDLGTGNGHLLFRLLEEEDTLLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIIKDSKFCSKDWDLILDKGTFDAISLSGELLDGRPLNSVYVDRVRGMLSPNGIFLITSCNWTIQELEERFTKNGFIVHSTVPVPVFEFQGSTGSSTSVIAFQIDPSFNRK Q9P7Z7 COX17_SCHPO BINDING 28; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:Q14061"; BINDING 29; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250|UniProtKB:Q14061" SPBC26H8.14c; CHAIN 1..70; /note="Cytochrome c oxidase copper chaperone"; /id="PRO_0000239059" DISULFID 31..62; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 41..52; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MSSSTEPSTATKVSEPAPIASEEKPKPCCACPETKQARDACMLQSSNGPIECAKLIEAHKKCMAQYGYEV Q9UQW6 ERG10_SCHPO ACT_SITE 90; /note="Acyl-thioester intermediate"; /evidence="ECO:0000250|UniProtKB:P24752"; ACT_SITE 351; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"; ACT_SITE 381; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" BINDING 185; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 185; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 230; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 246; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 247; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 249; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 250; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:P24752"; BINDING 347; /ligand="K(+)"; /ligand_id="ChEBI:CHEBI:29103"; /evidence="ECO:0000250|UniProtKB:P24752" CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037; Evidence={ECO:0000250|UniProtKB:P41338}; SPBC215.09c; CHAIN 1..395; /note="Acetyl-CoA acetyltransferase"; /id="PRO_0000310395" MVNTEVYIVSAVRTPMGSFGGSFASLPATKLGSIAIKGALERVNIKPSDVDEVFMGNVVSANLGQNPARQCALGAGLPRSIVCTTVNKVCASGMKATILGAQTIMTGNAEIVVAGGTESMSNAPYYAPKNRFGAKYGNVELVDGLLRDGLSDAYDGLPMGNAAELCAEEHSIDRASQDAFAISSYKRAQNAQATKAFEQEIVPVEVPVGRGKPNKLVTEDEEPKNLNEDKLKSVRAVFKSNGTVTAANASTLNDGASALVLMSAAKVKELGLKPLAKIIGWGEAAQDPERFTTSPSLAIPKALKHAGIEASQVDYYEINEAFSVVAVANTKILGLDPERVNINGGGVAMGHPLGSSGSRIICTLAYILAQKDAKIGVAAVCNGGGGASSIVIERV Q9UQY2 PSB6_SCHPO SPAC22F8.06; CHAIN 1..225; /note="Probable proteasome subunit beta type-6"; /id="PRO_0000148041" MSQSQFDPYVQNGGTTVAIAGDGFAILAGDTRSVNGYNINTRFQPRVHEVGDDLVIGASGFEADALALVKRIQQRIDLYHDNHERKMSAQSCACMVRTLLYGKRFFPYYVYTTVAGIDKEGKGEIYSFDPVGSYEREWCRAGGSAANFITPFLDNQVNLHNQYVPGSHGKERKPRRLLKLEEAMKITTDAFTSAGERHIEVGDSVLVKIITKEGVETRIIPLKKD Q9UR07 TF211_SCHPO ACT_SITE 271; /note="For protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" BINDING 502; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 566; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 567; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic; for reverse transcriptase activity"; /evidence="ECO:0000250"; BINDING 990; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250"; BINDING 1050; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic; for integrase activity"; /evidence="ECO:0000250" PTM: Processing of the polyproteins proceeds by an ordered pathway, called maturation. It involves the initial cleavage of a 27 kDa capsid protein (CA) from the N-terminus of the polyprotein, followed by the cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which does not seem to be processed further (By similarity). {ECO:0000250}. SPBC1289.17; CHAIN 1..1333; /note="Transposon Tf2-11 polyprotein"; /id="PRO_0000097506" MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQPGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQPQNKNLGKEFLPKKNNTTNSRNLRKTNISRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGTQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISIAPAHFQYFINTILGEVKESHVVCYMDNILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI Q9UR09 PSU1_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPAC1002.13c; CHAIN 19..417; /note="Probable secreted beta-glucosidase PSU1"; /id="PRO_0000033464" MRFFETLALALLTTGALAAPFRHPHHLLNKRDVSVVTSKVYAYTTVTLEAAASAISTNGAAKEAATAAGDAETTSSVAASVTPAASSSVAASVTPVASSSVAASVTPVSSSAVVDSATSAAASSSVIPTSSSVVASSSEVASSTTSSAAASATSTGSSSGGFQDGVYDCTDFPSDQSGVVALDYLGYGGYSGIQIGDGAGSSCVEGAYCSYACSPGMLKTQWPSTQPSDGETRGGLLCKGGKLYRTNTAYDNLCENGVGTASVQNTLGQGVAICQTDYPGSENMVIPTYVGGGATSPLSVTDNANYFQWEGKGTSAQYYVNKAGYTAEQGCQWGTSSGDYGNWSPLVFGAGMTDGTTWLSISQNPLTSQLANYNVKIVGADGASVSGTCVFENGAFQNGGSGCTVGITSGSGVFVFY Q9UR27 RM31_SCHPO TRANSIT 1..23; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC16A11.11; CHAIN 24..115; /note="Large ribosomal subunit protein mL60"; /id="PRO_0000374039" MLGAFNSTLARFGGLVHKVPWRLSQRRKYRHRQRLRAVDEVVDVLRTALQEKNQSCKRIESFVANHQPESQMSPKDKYTMFTRKTQGAGLQGFRKGVHKSPKWTRSTNRVNPTGF Q9URM2 TKT_SCHPO ACT_SITE 422; /note="Proton donor"; /evidence="ECO:0000250" BINDING 32; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 72; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 121..123; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 162; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 163; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 192; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 192; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 194; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 268; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 268; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 363; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 390; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 422; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 448; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250"; BINDING 472; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 480; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 531; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; SPBC2G5.05; CHAIN 1..685; /note="Probable transketolase"; /id="PRO_0000191903" MTSSSYTDIDTLAINTIRTLAVDTTAHAKSGHPGAPMGLAPAAHVLFSRIMKFNPAHPKWLNRDRFILSNGHACVLQYIMCHLLGYKLTIEDLKQFRQVGSKTPGHPETHNPDLNIETGAGPLGQGIASAVGLAIGKAHSAAVYNKPGFDLFSNYTFCFLGDGCLQEGVSSEACSLAGHLKLSNLIAVWDNNKITIDGATSMSFDEDVEKRFEAYGWNIVRVANGDTDLDGIEKGFREAMSCTDKPTLINLKTTIGYGSELQGTHSVHGSPLKPEDCVHVKKLFGFDPTKTFQVPPEVYAYYKERVAIASSAEEEYKKMYASYKQSYPDLSNQLERILSRKFPEGWEKHLPVYKPGDKAVATRKLSEIVLDALCPVLPELVGGSADLTPSNLTRWEGAADFQPPSSKLGTYAGRYIRYGIREHGMAGIMNGLAVYGPIIPYGGTFLNFVSYAAGAVRMAALNNSRVIYVATHDSIGLGEDGPTHQPIETFAHFRAMPNINCWRPADGNETSAAYYSALTSDSTPSILALTRQNLPQLENSTIENALKGGYVMLENKEADITLVGTGSEVSLCIDTVKTLETEYNLKARVVSLPCWEVFEQQPESYRLSVIPDGIPAMSVEVWATNGWRRYVHEAFGMHTFGDSGPAPKLYEKFHFTTSGVAQRAKKTVDAYKDIPYIRSPVRRAF Q9URU4 PFL5_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPBC1289.15; CHAIN 22..1283; /note="Putative cell agglutination protein pfl5"; /id="PRO_0000353810" CARBOHYD 66; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 84; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 99; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 115; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 123; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 143; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 157; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 174; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 196; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 266; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 301; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 336; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 406; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 441; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 476; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 546; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 686; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 721; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 1203; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MLVFTDLIFLAIFAHIGKATAKVWNRNVQGFLDLNLPNECSQYTTIYSDGPSEYTSTLPYTHSFSNASVYTTLITITNSQCTGNYSTLTISSQPLIHTNTSISKPSQTATPQNTNTTQVSLTNGTTTNSYSNTNSLPITDTINGTTELIIPTTSYNNQSHTLIYSTYTSTYLPNSTIDLSILPHSTISTLSTVSINDTSASLSKTTSPTAGTITETIVSGSVGYTSTFPASGTTSGTVEVVEPTAGTITETIVSGSVGYTSTFPANGTTSGTVEVVEPTAGTITETIVSGSVGYTSTFPANGTTSGTVEVVEPTAGTITETIVSGSVGYTSTFPANGTTSGTVEVVEPTAGTVTETIVSGSVGYTSTFPASGTTSGTVEVVEPTAGTITETIVSGSKAFTSTFPANGTTSGTVEVVEPTAGTITKTIVSGSKTFTSTFPANGTTSGTVEVVEPTAGTITETIVSGSVGYTSTFPANGTTSGTVEVVEPTAGTITETIVSGSKTFTSTFPASGTTSGTVEVVEPTAGTITETIVSGSKAFTSTFPANGTTSGTVEVVEPTAGTITETIVSGSVGYTSTFPASGTTSGTVEVVEPTAGTVTETIVSGSVGYTSTFPASGTTSGTVEVVEPTAGTVTETIVSGSVGYTSTFPASGTTSGTVEVVEPTAGTITETIVSGSKAFTSTFPANGTTSGTVEVVEPTAGTITETIVSGSKTFTSTFPANGTTSGTVEVVEPTAGTITETIVSGSVGYTSTFPASGTTSGTVEVVEPTAGTVTETVISGSVSFMSTITAHDTSSGAVIVVEPTAGTVTETIVSGSIPFTSTIPAQGTTSGTVEVVEPTAGTVTETIISGSVGYTSTFPAQGTTSGTVEVVEPTAGTVTETIISGSVGYTSTFPAQGTTSGTVEIVAPTAGTVTETIVSGSIPFTSTIPAQGTTSGTVEVVEPTAGTVTETIISGSVGYTSTFPAQGTTSGTVEIVAPTAGTVTETIVSGSIPFTSTIPAQGTTSGTVEVVEPTAGTVTETIISGSVGYTSTFPAQGTTSGTVEVVEPTAGTVTETIVSGSIPFTSTIPAQGTTSGTVEIVVPTAGTVTSTTGSGTSWFTTTVPATGTRSGSVIVVSPTAPACSSTPFAECPNLNFNFHSKNVNFPPADIRVISVTPKGNNMYDATVQFTTSSTMSKKSLSELKILGLSQTYLLYSYNSKVDNISNPGSWTSTVTVQGTSTGSYICMPHFQIQYDWCSAGVTDMSECNTWSYQKSYDYITGCNNYDNQGNSQTDASDYCWNVC Q9URU9 FYV10_SCHPO SPBC106.13; CHAIN 1..404; /note="Protein fyv10"; /id="PRO_0000292466" MNFRPEQQYILEKPGILLSFEQLRINFKHILRHLEHESHVINSTLTTLISQENASMDEKIEKIDSLLSRVSTVKKKMKHLHDCEALFIKQTKSRLLFMNRLQGIRDMESADFLDWSRVRLNRLVADYMMANGYHGAAALLCKDSQLENLVDLGIYKRYQLIHDSILQQELKEVLSWCSEHRAILKKNNSTLELEVRLQRFIELIKSKKLCQAIAFAKAHFGTWANEHPARLQLAAALLAFPEFTNGSPYSLLLSDDRWEYLASLFTSNFTAVHNIPSVPLLHALLAAGLSSLKTPLCYLDANDDNPLALQSQTVKQCPVCTPCLNDLGKALPYAHITQSAIVDSLTGEGLDSDNCPVAFPNGRVYGIQSLISWNEANGTREGFLRDPYSGKEFPFQLLRKVYVV Q9URV1 PLG7_SCHPO ACT_SITE 257; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 291; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q13093"; ACT_SITE 368; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q13093" CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000250|UniProtKB:P83006, ECO:0000250|UniProtKB:Q13093}; SPBC106.11c; CHAIN 1..438; /note="Putative phospholipase A2"; /id="PRO_0000316918" MGLGFSSKKQLPAYCGPLPVGSLVLELSVPEEFRCEYKTIEHKLRTVKVRIFYPLDPTKDVEPRTDELWLPFHEGIPEVAKGFRWWLLRAFASGLTNLALPVYKGELFHPPNNGKLPVFIFSHGLVGSRNVYSSLCGTIASYGIVVLAMEHRDNSAIISTVRDPLHPEEPPYVVQYREISDFYADATVVLQNERLLFRQQEIQIALQMIRNINDLGTPDENLPFLCSVDSSFYNSVFQSMKGNLNTAQGELIVAGHSFGAATCAFISGSSTKSLYNDYMFHTEFKCSILYDIWMLPVRQLHLSTMRYPTLMIISYEFRRFVDNFQALESWLVNKDSENQNAGESADEKMSVVPLKKYSHVFVYDGTVHANQSDLPILLPRMVLRVLKGKFEADPYEALRINTRSSVQFLRENHVENVQGDNDPSSLQTNIIPGWERIM Q9URW6 YIE2_SCHPO MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 316; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 324; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 325; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 326; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 354; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 406; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPJ696.02; CHAIN 1..430; /note="SH3 domain-containing protein PJ696.02"; /id="PRO_0000303942" MGLHNPLPSSLKSECKKAGKILTSFVDPRQTLGAQEVIPPSVLTNAKGLVIMTVLKAGFLFSGRIGSGLIVARLDDGTWSAPSAVMTGGMGVGAQIGSELTDFVIILNSKAAVQTFARLGSITLGGNLSIAAGPLGRNAEAGGGASVGGMAPMFSYSKTKGLFAGVSLEGSVLVERRDANRSLYRGDITAKRLLSGQVAQPAAADPLYRVLNSKIFNLNRGDEGDIYNDVPIYADDEPEDIWGPSSKSTKRRDSADRSSSYSRRGDSYRSNRSRAHDDDDEDDYSFSRSKSLSRKTAGGSLRSSKMDNRRSKYADTPSPRRSRSYSDEDEESVYSSDVSTESSSQFSSRSSEYSKPSRPTAPKPKFKQDSLGPNQARAMYSFAGEQPGDLSFQKGDIIDIVERSGSHDDWWTGRIGYREGIFPANYVKLS Q9URW9 YLX7_SCHPO ACT_SITE 263; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"; ACT_SITE 297; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007" BINDING 241..246; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" SPAC922.07c; CHAIN 1..496; /note="Putative aldehyde dehydrogenase-like protein C922.07c"; /id="PRO_0000310349" MSEDLFVSINFPNGKSVKQPIGLYINGEWHKSAETWETVDPSIEEVIAKVYLAGEKEIDYAVKSAKEAFKTWKKVPGSEKGELLMKLAELTEKHADTLAAIEAMDSGKPLVSNARGDVDGTIALLRYCAGWADKIYGQVIPTGPEKLAYAKRTPIGVCGQIVPWNYPLNMAGWKIAPALAAGNCIIIKSAETTPLSLLYFATLVEEAGFPKGVVNIISGLGTVAGSYMAKHPGIDKIAFTGSTKVGVIVQQLAASNLKAVTLECGGKSPFLVFEDADLDQAVKWAALGIMYNSGQICTSNSRIYVQDSVYDKFIELFKKHVIQDYIVGMPFDDNTVVGPVVNKTQYNRIKNYIEQGKKEGAKLVLGDEPLPLKQGYFISPTIFADCSENMTIVKEEIFGPVVAISKFKTEDEAIEKANNTTYGLAAMCFTKDLERAHRVSDELEAGMVFINSTENSDIQAPFGGIKMSGIGNELGSNGIEMYTQIKAVHINFNNKL Q9URX3 1A1D_SCHPO ACT_SITE 78; /note="Nucleophile"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 51; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC922.03; CHAIN 1..338; /note="Probable 1-aminocyclopropane-1-carboxylate deaminase"; /id="PRO_0000184511" MGLEQFKKYPLTFGPTPITSMKRLSKTLGGKVEIFAKREDCNSGLAFGGNKIRKLEYLIPEAIDGGYDTLVSIGGIQSNQTRQVAAVAAHLGLDCVLIQEDWVDYKDTMYDRVGNIELSRIVNADVRLDSSKFDIGIRPSFKNALEELTKKGKKPFPIPAGCSEHPYGGLGFVGCVEEIYEQEKQLGFKFDKIVVCTVTGSSFAGIIVGMALTGRQKDVIGIDASATPEKTKAQVLRIAQNTAKLIGLEKELTESDVNIDTRFAHPAYGIPNEGTIEAIKLCGATEGVLTDPVYEGKSMQGLIHLVRNNEIAEGSKVLYIHLGGAPALSAYSAYFKNT Q9URX6 RL31_SCHPO SPAC890.08; STRAND 14..20; /evidence="ECO:0007829|PDB:8ETC"; STRAND 54..56; /evidence="ECO:0007829|PDB:8ETC"; STRAND 74..81; /evidence="ECO:0007829|PDB:8ETC"; STRAND 94..98; /evidence="ECO:0007829|PDB:8ETC"; STRAND 109..111; /evidence="ECO:0007829|PDB:8ETG" HELIX 21..24; /evidence="ECO:0007829|PDB:8ETC"; HELIX 30..32; /evidence="ECO:0007829|PDB:8ETC"; HELIX 33..49; /evidence="ECO:0007829|PDB:8ETC"; HELIX 58..64; /evidence="ECO:0007829|PDB:8ETC" TURN 25..27; /evidence="ECO:0007829|PDB:8ETG"; TURN 65..67; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..113; /note="Large ribosomal subunit protein eL31"; /id="PRO_0000153787" MANTKKSAINQVVTRDYTIHMHKRLYGVSFKKRAPRAIKEIVAFAQKHMQTKEVRVDPSLNKEVWKRGIRNVPHRLRLRLSRKRSDEDDKALYTYVQAVDVANPKMETTVVEE Q9URX8 NG06_SCHPO SPAC890.06; CHAIN 1..1315; /note="Probable nucleoporin C890.06"; /id="PRO_0000204847" MDINDPSFSSTENGIYELLSRGYAAIEAATERDLKLPELGDIIGQVHAPEYISQVLSGWKPFYLRSVVNIPDRIFEQYNRTECFTQMGLFAEIQRAWITVDNRLFLWDYLSGQNFQAYEDLSHTIVNVKLVRPKANVFVSEIQHLLVIATSQEMLLLGVTIDEKTGELSFFSTGIQISVQGINVNCIVSSEDGRIFFSGNKDPNLYEFSYQLEEGWFSRRCSKINITGSVFDNFIPSFFSFGTHGDGIKQIAVDDSRSLLYVLRETSSVSCYELTKNGVNRCVFYSFSSMISQAQMLNATSPLLDPRTTQIVSIVPIPAYESQQIYCVAITSTGCRFYMRGGRGPISHYAPSNSTLSSTPPSTLQLTFVRFPPPMQVENYASSRNYPANPFFLQNQSTSQQQPERSSAVKTTPMKCSSLSNIYTSDLFFAISSSNTNEGDVVCCTAPEVGRIANAWQSGTQPSLIESSMYVPIKGFVQDIKCIQNSRERNELVSQFNTPPPTFAILTNTGVYVVVHRRPIDVLASAIRMGPSLSSGIDGQVQLFFESVGRAEGCATCLGIVSGCLDQGDFSHAAANFSGSTTKLAQADLLDIVKKYYIEFGGKAFIDQSRYNNQYDSSSLEFVRLSGCHDGLASSISRIIRNVWKNHVIIAKKMQNKRIHYAPAFNATEILKIQSGLLYLSTFLENNKSFIEGLNSPNTLIGSSNVADEIAVQAEHRALSALLLVLQQIVEGISFLLFLNDTGVSDFHEIVSSTSIDIQKSCSNMTFGEFFTSKRGREVTKELVNSLVNRHLQSGGNIDMVSQLLRKKCGSFCSADDVLIFKAVESLKKAKDTVDIEERQSLIELSYTLFKKAAHVFTPEDLRLAVEEYKSLNAYTTAVNLALHVASARDDRNQALSYLVDGMPENDPRREPFESRTKCYSYIFEILDSLESQMSNDSSAIKVDVYDTIQRSKDELFHYCFYDWYSFKGLTDRLIEIDSPYIQSYLERNSTKDMKIADLLWQYYAKREQYYQASIVLYDLATTHLAFSLEQRIEYLTRAKGFGSCHVPNSLRHKMNKVMLSVLEQLDVASIQDDVLIAIRGDMRIPTSKREELSKQLDGEIIPLSDLFNNYADPLGYGEICLSIFQCADYRGINEILNCWESIIKTTHENAIISPVGSSPVEAVSSTLKNLTLRFSQSENVFPIEQIIDITERYAFDQQGEAVATGWVIDTFLGAGVSHELIFIVLNQLYDRREKPWQGKDRLFFLIKEVTHLLKLWHEVSVRAGVAQTSKPSFDAPLVLEAIEKYKNALGAPDTATKSCKENLISLDSEIRQTY Q9URX9 PXR1_SCHPO MOD_RES 159; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC890.05; CHAIN 1..284; /note="Protein pxr1"; /id="PRO_0000303955" MGLAGVKKKQQIGVDPRNSKWAKDTNRLGFKLLSSYGWVNGNGLGEKQHGRIHNIKVSLKDDTLGIGAKATNDLEWSGLGEFNAIFGRLNGDESAYGVYAEKAKVQQLTYERQSANEKGLKSLELSRRFVLGGTFTSEFSEWMQKAEEDEDRVCEDASSSDEAKREKRKKHSSKKKSKKKTSTGSALDPKKLEKITKKKKKEHKKKDKESSSKKRKSGSSDKEEKKKKKIKLKDKPESTSSVEKVKEGNRPASIHFHTRRKFLAQKRAAVSDPVALREILGIKG Q9URY6 DUR33_SCHPO SPAC869.03c; CHAIN 1..661; /note="Probable urea active transporter 3"; /id="PRO_0000314768" MTETVLNQGYGYGIVIGLGFAFAIVMILVTYVLKRYVGEVQDSEHFTTASRSVKTGLISSAVVSSWTWPGTLLTSAGMAYEYGVCGSMWYSFAFTVQITFFTVIALQVKRVAPGAHTIVEIVKARFGQASHAVFLFYALGTNIIVSAMLLLGGSQAISAITGMHVVAAGFLLPLGVWLYTVSGGLKSTFLSDWTHTVIVYIVILITLFVAYTSSVHIGSIDKMYDLLTEVSKTNPSTGYKGSYLTVTNRDAVFVGWNIVIGGFATVFCDPSYGQKAIAAKPISAMKGYFAGGLAWLIVPWAMGSAAALSCLALTNNPVSVTYPDPVSSKQVSEGMPLLYGMTALMGKNGAAAGVLILFMASTSATSAELVAFSSVMTYDVYRNYFRPNASGKELVRVTHVFVTIFAVCMGALAVLFNYIGITISWIITFIGIALGPAVFGITLTLFWKKMNKYGMIIGCPMGSITGVVCWVGSCYKFSNGVVNKTTLNTPYANAVGNFTGLFSGLIYIVLISYFFPNKSDDLNNLNEKFVLGDDATAEEIVDAETEKKQLDRSLRIGIFVSWIIFFILVIIVPLPMYGSKYIFSKLFFRGWIIVIIIWTLIAALYITFYPLYESRDTIVYLCKLAIGKAKAPEPMNYVDAVEVEIESLSDDDKEKKANDFL Q9URY8 SULH2_SCHPO MOD_RES 823; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC869.05c; CHAIN 1..840; /note="Probable sulfate permease C869.05c"; /id="PRO_0000080187" MRAWGWVRNKFSSEDDYNDGASNKDYPDRFNEFDNSQNDHNDYTQNNAQFQNAQTTTFGRTISRVKAYYEIPEDDELDELASIPQWFKKNVTSNIFKNFLHYLKSLFPIIEWLPNYNPYWLINDLIAGITVGCVVVPQGMSYAKVATLPSEYGLYSSFVGVAIYCFFATSKDVSIGPVAVMSLITAKVIANVMAKDETYTAPQIATCLALLAGAITCGIGLLRLGFIIEFIPVPAVAGFTTGSALNILSGQVPALMGYKNKVTAKATYMVIIQSLKHLPDTTVDAAFGLVSLFILFFTKYMCQYLGKRYPRWQQAFFLTNTLRSAVVVIVGTAISYAICKHHRSDPPISIIKTVPRGFQHVGVPLITKKLCRDLASELPVSVIVLLLEHISIAKSFGRVNDYRIVPDQELIAMGVTNLIGIFFNAYPATGSFSRSAIKAKAGVKTPIAGIFTAAVVILSLYCLTDAFYYIPNAILSAVIIHAVTDLILPMKQTILFWRLQPLEACIFFISVIVSVFSSIENGIYVSVCLAAALLLLRIAKPHGSFLGKIQAANKYGSDNIANVRDIYVPLEMKEENPNLEIQSPPPGVFIFRLQESFTYPNASRVSTMISRRIKDLTRRGIDNIYVKDIDRPWNVPRQRKKKENSEIEDLRPLLQAIIFDFSAVNNLDTTAVQSLIDIRKELEIYANETVEFHFTNIRSGWIKRTLVAAGFGKPKGHAVDASVCVEVAAPLRDANLSAESSRNLSRIITPIYDDEEGNVSGHIYELDGKNNSDLSMHCQKGSNQVEIEFVEFNSRKYPFFHVDVASAVVDLQHRLLSPQKSDSFGSLKEGGTTTIKKIEN Q9URZ3 PUT4_SCHPO SPAC869.10c; CHAIN 1..552; /note="Probable proline-specific permease put4"; /id="PRO_0000310854" MDEKKALQYEESKRAEEITDIELVSVGGIDVEKKYGETKRALKSRHVQLIAIGGCIGTGLFVGSGSALSESGPASLFLSYVIMSFVIWTVMNALGEMCTYLPLSGASPITYIERYVDASLAFAAGWNYWYAYVFLVASEVTAASIVIEYWTYAVPTAGWIAILLFLVAVLNSFFVKWFGETEFWFAIIKVIAIVGLIILGVVIFFGGTPKHDRLGFRYWKHGLAFREYIVKGASGRFVGFWSAVIKSGFAFILAPELVIFSAGETEAPRRNIPKATSRFIYRLIFFYIFGSLTIGVITSSKDPRLLNAISSGASGAAASPFVIGIQNAEIPVLNHIINAVILTSACSSGNSFLFAGSRSIYSLAKEHQAPKIFKYCNRWGVPVISVAVTVLFACLAFLNASASAAVVFNWFCNLSTISGFLAWICVLVAYLQFRKAMILNNLWETRPYKTPFQPYATYLTLFLLALITLTNGFTVFVGHTFTAGNFIAAYITLPIFLVLYVAHKLWSRNWSFGKRIEEIDVTTGVAEAEALEQMYPAPVPRNIIEKIWFWIA Q9URZ7 YK72_SCHPO ACT_SITE 88; /evidence="ECO:0000255"; ACT_SITE 214; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250|UniProtKB:Q16875"; ACT_SITE 285; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q16875" BINDING 16..24; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 127..132; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 157; /ligand="beta-D-fructose 6-phosphate"; /ligand_id="ChEBI:CHEBI:57634"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 213; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 220; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 226; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 296; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 307..310; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07953"; BINDING 310; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 314; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 325; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 351..355; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P07953"; BINDING 351; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:Q16875"; BINDING 355; /ligand="beta-D-fructose 2,6-bisphosphate"; /ligand_id="ChEBI:CHEBI:58579"; /evidence="ECO:0000250|UniProtKB:P07953"; BINDING 387; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q16875" CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; SPAC732.02c; CHAIN 1..408; /note="Probable fructose-2,6-bisphosphatase C732.02c"; /id="PRO_0000318495" MKDIEGLLGLCVCFVGLPASGKTSSAMKLSRYLTWMSVSTHLYDTKEIDNSLSENSNSDSENLAKTLSPIFDNLESVFKKGTDVAILDFNQCTLKFRKSIVELAKARNMLLMFVEVVCTNQKIIDENITDMCQHSPYFKSFPFEESKNKILDSIHEYEKHYTPLSEAEECTFVRIVDFGAELIVHKLENYLESRIVYYLSNLRTRRRSIWLSRHGESQFNVEGKIGGDSSLSPQGLKYAALLPEYVAKFSIGEKGLTVWTSSMARTIQTARHLNCQKLEWRALDELDAGTCDGFTYDYIEQNFPHEAELRNNDKFHYRYRGGESYMDVVRRLEPIIMELERQGDVFIICHQAILRCIYGYYHNLSLEELPFINVPLHTIIKLTPMTYETIEERVTVPISAVSTQRGKH Q9URZ8 VATL2_SCHPO SPAC732.01; CHAIN 1..162; /note="V-type proton ATPase subunit c'"; /id="PRO_0000071787" MSSNLCPIYSSFFGFAGVCASMVFSCLGAGYGTALAGRGIAAVGAFRPEIVMKSLIPVVMSGIIGVYGLVMSVLIAGDMSPDNDYSLFSGFIHLSAGLAVGLTGVAAGYAIGVVGDRGVQSFMRQDRIFVSMVLILIFAEVLGLYGLIVGLILQTKTSNVCY Q9US00 AMT2_SCHPO SPAC664.14; CHAIN 1..512; /note="Ammonium transporter 2"; /id="PRO_0000278388" MSSVNSIPTATSTVYISVLPATATPSGGSGGNVLHEDLNKFYDYGNTSWILACTPLCLIMVPGVAFFYSGLARRKNTLALIMLSMLGLCVSFFQWYFWGYSLAFSQTGTSGYIGNLRHFAFIRTLADYSPGSNNIPELVFANFQGMFAAITVALFTGAAAERGRIGPMLIITFVWLTVVYCPIACWIWNPNGWAFKFGVYDFAGGGPVEVGSGFAALAYTVCLGRRSKFVEEQFRPHSVLNVVLGTSLLWFGWLGFNGGSAYGSNLRAAMAITNTNLAGAVAGLVWVIYDYIFRTRKWSTIGFCSGVVAGLVAATPCAGFVSPHASLAIGAITGLCCNWAIKLKSHMRIDDAMDIFAIHGVAGFVGTFLNGLFAVDYIAAMDGIYVGENKIRGGWFDHHWRQLGLQMAYICAVGAYDFVVTFIILFITDKIPYLQLRVSPDAEEIGVDADQIGEYAFDYIEERREYKHWKISPAGVPEEIIISNGVAQPTGNVAAPGKILESTNPLELGLTI Q9US06 PAF1_SCHPO MOD_RES 388; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC664.03; CHAIN 1..456; /note="RNA polymerase II-associated protein 1 homolog"; /id="PRO_0000318139" MENRRQDYILRVRYHNPLPPPPFPPKLINIPNPVKQYALPNFVSTLVQEKKIPIENDIELGMPLDLAGITGFFEGDTSWMHSDLSSVNLDPIDRSLLKVAGGSGSTHLEVPFLRRTEYISSEVARAASNRGNLRLTASTSKALAEQRGRSLREVPKQLEAINESFDVVQQPLEQLKHPTKPDLKPVSAWNLLPNTSMAGIQHLMLRVADDLSERSHSYSSLVNLQEGHNLTKRHEVALFMPSSAEGEEFLSYYLPSEETAEEIQAKVNDASADVHEPFVYNHFRNFDASMHVNSTGLEDLCLTFHTDKDHPEANQVLYTPIYARSTLKRRHVRAPVSLDAVDGIELSLRDLNDEESLQLKRARYDTFGLGNIKDLEEEEEKLRSVEGSLNEELSEEEKPAESREQLESAEQTNGVKPETQAQNMSASESQANSPAPPVEEGNTQPSPVEQLQNEED Q9US07 ARP8_SCHPO BINDING 339..342; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" SPAC664.02c; CHAIN 1..662; /note="Probable actin-related protein 8"; /id="PRO_0000089127" MAPKRKQPYTEEGIDFKFTQFQIVPPINQKNFYTEYLKRDDQMYIWRDSAGEKDAKETESESANGDTKQDDSKKSQVEEEEDGIEESELGEEKDNKTIVLHIGSQNLRIGLASNKTPTTVPMVIARKMRAPFAQERCLLKDICHVNEDGNVAFDSEFDSNLKLLDSELKSWLKAQKKRSVPNGTQLVKNYNKISKPETVPPDDDPEKPDWIHFEQDDHVDVICGKEAFLLPLNEYPEYKLFYPIKSGVFNESDYASSQQLLADIYEIFKYSITSLLQIPVSQLSQYSVIFIVPDLYDRVYVEKILDILFFDLHFGKAAIVQESLCTSFGAGMSAACVVDMGAQKTSISCVEEGVVVPNSRIKINYGGDDITLLFMKLLMRSHFPYQDIDLKTPYDWSLANALKIKYCGLSEATYNVQLNSFFSRTPDKGTRKFTFKSLDETMLAPLGFFRPDIFENENKLHDRYTLFPVPVDVYDNQPNNPESLAQTTLLQISTPISNIKANGKDDEEKKEESDLVTPSVKFKPPRVVYCGSLAAPEIKNEKLIYPLDDAINQSIFSACDGNLSDEKAKNLYSSILIVGGAGQFPGFAHLLEERIHSKRANIPTISVIPPPRSMDAQFVAWKGACIYNRIRIVSELWIKNSDWKMLGSRVLQYKTLGYFWTG Q9US12 YK66_SCHPO ACT_SITE 304; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 303; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 307; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"; BINDING 313; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion. {ECO:0000250}; SPAC607.06c; CHAIN 1..612; /note="Putative zinc metalloproteinase C607.06c"; /id="PRO_0000078180" MSQIILDNISQNETVYNRFVIIHGRVGPRASYCPQTINVKHHENSFPEQTWVVTDLYFKAIIHVVPGDNTILFTTDDGGKLELQVYYQLLVDNPFYCIAFIVGKDSDLSFDAPHGAKNDIDEGIRKLRCAAYLWQAFTAECMYRNGYGRRSFRIEESVQPDTMSCLSPWGTERLTATINILRSDKTAEEIRSVPPDQLFHIAGDAVDKLHLPEPWHYMCMFLDTRYDPSTQKIRGHVALGGGTDMHKLGVFGSHSLHSFPSALEYVVPVFSDARRIPSYLANDANESSTIWECANIGIGAMLHELGHTLGCPHQPDGIMLRSYPIFNRSFTTREFECVRTGSKGLAPVLAKDECSWHHLDMLRFFYHPCFKLPSDPTYPSDIETNYFVKGETITFVNSTGIFLIEIEYNGQTKGWKEFNPPVGEASLTDAEIRSLSNASSNQDYRVRVLSRNFKCIDLNNVPEIIKNAKVESSFGTVYRSERYGLRGCNGKELSNILIAPEKFKPTKIRVHCGLALDGIEVFFGDESVLLGNRGGSPHDFEIQGSQIVGFQIRCGAWVDGISIVLENGKTSPFYGNANGGGLKSYLVPKGFQLVGFYGTLGPFMDSIGFFIK Q9US27 LOA1_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; SPAC1783.02c; CHAIN 1..300; /note="Putative lysophosphatidic acid:oleoyl-CoA acyltransferase"; /id="PRO_0000356186" MEKFTRWRDPGTGIAPFHPINTETPSGFNFKWILIVVVMILRVPLCIISVTLWFLWSCFLKPILSIQPKLSFFIDSSLSRLLLLCFGCLKLSKSTSGSFVQGDSLQPGDILAVNHSSPLDVLVLSCLYNCTFAVCDSKTSNVSIISAQAYFWSCFFSPSKLKITDAKPLAKVAAKASKIGTVVILFPEGVCTNGRALCQFTPCFDSAKETDRIFPLYIKYLPPCVTLPVPSLLSFARSVLLTVSFEIRIRFSAEPLIPRNCTDVTESAQEVLSKLGRSRVVKLGKSDKLSYLDARSKKHV Q9US35 DSD1_SCHPO BINDING 204; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9"; BINDING 211; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9"; BINDING 253; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9"; BINDING 279; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9"; BINDING 280; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9"; BINDING 385; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9"; BINDING 387; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9" CATALYTIC ACTIVITY: Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18; Evidence={ECO:0000250|UniProtKB:P53095}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13978; Evidence={ECO:0000250|UniProtKB:P53095}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P53095}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P53095}; MOD_RES 68; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:A0A8V1ABE9" SPAC1039.06; CHAIN 1..415; /note="D-serine dehydratase"; /id="PRO_0000317093" MASNVDKFSSRFYLNVNKEELKKEYVGKTIQQVPTPGFVIDEAIFEKNCNRMLDRASDIGVTFRAHVKTHKTIEGTLLQLGDGRTKAVVVSTLMEGFSLIPLILEGKIDDLLYGLPVAKSRLPELYELSKIVPHLRLMIDNPKQLDILREFTSTLPDDAKPWSIFVKIDMGTHRAGVTNDSQVVKDLISTILSDKSLFDLFGFYCHAGHSYASRSIDAASEFLCAEIDAANTAAKFATSIDPSLKLTLSVGATPTAHSVSPKVKELLPTLSGKLEVHAGNYPMNDVQQMITKCISQADVADYVFAEVISNYPGRNGEPGEVLVNAGVIAMSRETSPEGDFGIVITPGFESFYVDRLSQEHGILKSKDPKATLPDASQVLCIIPNHSCITAAAFPWYYITKGSDVITDIWVPWKGW Q9US41 URG1_SCHPO ACT_SITE 353; /note="Proton acceptor"; /evidence="ECO:0000255"; ACT_SITE 355; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 268..272; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 273; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 284; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 286; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 315..317; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 377; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 382; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAC1002.19; CHAIN 1..439; /note="Uracil-regulated protein 1"; /id="PRO_0000353828" MLATEQSRPAECNGAHAHEKTEEVKKPLYSRPVVLTTYPSQSRIDPFPMNWGAATAEERGPITVARSIETLPHRNAVGAHGGSYSVYNALAVAGGFLPPDHRPNFELTEPTFDFPELDSWHDPKKIVAMDPYGHLTPSVFKKYLDEGYDVRPTIAITRAHLQVTEIQRSVENGSLPIDGKIVLNEKGDIAVTKVAVEPVWYLPGVAERFGVDEVTLRRALFEQMGGAYPELITRPDIKVFLPPIGGLTAYIFGPPEYLSDTSKSLAVRVHDECNGSDVFQSDICTCRPYLTFGIEEAAKEAQNGGAGLVVYFRKEGRALGEVVKYLVYNKRKRTGDSAENYFKRTEELAGVRDMRFQALMPDILHWFGIKKIDRMLSMSNMKHDAIVGQGIKILNRITIPDDLIPEDSQVEIDAKIQSGYFSEKKVTEDDLSCVHGRHW Q9US43 UPP3_SCHPO BINDING 75; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250"; BINDING 100; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250"; BINDING 126..134; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250"; BINDING 187; /ligand="D-ribose 5-phosphate"; /ligand_id="ChEBI:CHEBI:78346"; /evidence="ECO:0000250"; BINDING 188; /ligand="uracil"; /ligand_id="ChEBI:CHEBI:17568"; /evidence="ECO:0000250"; BINDING 193..195; /ligand="uracil"; /ligand_id="ChEBI:CHEBI:17568"; /evidence="ECO:0000250"; BINDING 194; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; Evidence={ECO:0000250|UniProtKB:P70881}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. {ECO:0000250}; SPAC1002.17c; CHAIN 1..204; /note="Putative uracil phosphoribosyltransferase urg2"; /id="PRO_0000309558" MSTTTTVSAIRTVEEMSNITISSHPVVNEQIAILRDRSLKPSQVRSVVDEISRFLAYESTKTLKSPSVSIVPVLRSGMSMMSAFSKVLPDVPIYHIGIFREKSTLQPIEYYNKLPKKSTDTAVILDPVMATGGTANAVITTLQEWGCKNIIFVSVLASEQALTRFSNIPGVEFVIGAVDKSLDAKGYLVPGVGDIGDRLYGATA Q9US45 MED6_SCHPO SPAC1002.15c; STRAND 40..43; /evidence="ECO:0007829|PDB:5N9J"; STRAND 75..84; /evidence="ECO:0007829|PDB:4H61"; STRAND 88..96; /evidence="ECO:0007829|PDB:4H61"; STRAND 98..100; /evidence="ECO:0007829|PDB:4H61"; STRAND 102..111; /evidence="ECO:0007829|PDB:4H61"; STRAND 114..117; /evidence="ECO:0007829|PDB:4H61"; STRAND 148..150; /evidence="ECO:0007829|PDB:4H63"; STRAND 154..156; /evidence="ECO:0007829|PDB:4H63" HELIX 11..13; /evidence="ECO:0007829|PDB:4H61"; HELIX 19..24; /evidence="ECO:0007829|PDB:4H61"; HELIX 33..38; /evidence="ECO:0007829|PDB:4H61"; HELIX 48..58; /evidence="ECO:0007829|PDB:4H61"; HELIX 66..71; /evidence="ECO:0007829|PDB:4H61"; HELIX 120..140; /evidence="ECO:0007829|PDB:4H61"; HELIX 193..211; /evidence="ECO:0007829|PDB:5N9J" TURN 30..32; /evidence="ECO:0007829|PDB:4H61"; TURN 85..87; /evidence="ECO:0007829|PDB:4H61"; TURN 151..153; /evidence="ECO:0007829|PDB:4H63" CHAIN 1..216; /note="Mediator of RNA polymerase II transcription subunit 6"; /id="PRO_0000096390" MASGAPPSVDLTSIQWRMPEWVQSMGGLRTENVLEYFSQSPFYSHKSNNEMLKMQSQFNALDLGDLNSQLKRLTGIQFVIIHERPPFLWVIQKQNRLNENEVKPLTVYFVCNENIYMAPNAYTLLATRMLNATYCFQKALTKIEKFPQYNPQEGYTYPKLSNDNLEVDHSNTNEPADENKNQSIENADYSFSPEDFSVVRAFMQSLHSSKEAPDVK Q9US47 SSDH1_SCHPO ACT_SITE 318; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"; ACT_SITE 352; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007" BINDING 296..301; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.16; SPAC1002.12c; CHAIN 1..547; /note="Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)]"; /id="PRO_0000310351" MTSLIQSIPRYIYESNSLPKLIRSGLDRKSPIGLSLLKRNCRNRSFAANMSTSSKLSTNIKDLSLFDLEEFPARSYIGGKWVTAASGKTFDVENPGLNETLAPVTDMSVEETRKAIKVAHEAFLSYRNSDIKERYAILRRWYDLIMENADDLATMMTLENGKALGDAKGEVVYAAKFIDWFAGEALRISGDSSMSSNPQNRIITIKQPVGVVGIITPWNFPAAMITRKVGAALAAGCTVVIRPAAETPFTALALAKLAERAGVPAGVLNMVTANSPSEHGIELTTNPLIRKVSFTGSTNVGKILAKQSSSTLKKLSLELGGNAPFIVFEDADLEKAADALMACKFRGSGQTCVCANRIYVHSSVYDAFVDLVTERVSKFKLGYGLDAGVTHGPLISEKAISKVKQHVEDAVQKGGVVVTGGKVASNLGPMYFEPTVIINAKQGMLISEEETFGPVGALFKFDTEDEVVAWANDSPVGLAGYLFSKDISRVFRVGEALQVGMVGCNTGLVSDVLSPFGGVKESGFGREGSKYGISEYLDIKSLTISTL Q9US49 ECD_SCHPO SPAC1002.10c; CHAIN 1..590; /note="Protein ecdysoneless homolog"; /id="PRO_0000220848" MSNLGNNITERIESDCISQNECRIDVYFSEKEKESTEASINMFLAELERLQLEYGKEHIWQNEELNLQRVEYQGKDCILGITNFGDCIDDEWYIVWLLREASKAVKSAFVRIIDEDGEFLLIEAALSLPKWIDEDNSDYRVWIHNGEVIILRPEDEFLKKMNRCPPLTREQAIFQISSGSNLYTSREVNDSISQRLKKFPKAANVKLRAICTVPRKIVHVLQKNKNLISSAVNAFYYRDPIDENYCDRMSKFNQNDLVTTTITFTPLLYAQLYQQRCKTFRPFHLPSDVHSLDYERAILGMKLSCGFEILYNSKENVEKRTEIDEYLQIQPLPTDEDIKKIPLIEDDTSFMNVNPDELEELLEKKLNSFCDDFGDDERSGFDNTDHDNTLVGEEEMVPGNHGGKSINEEITKNKQKQNFNESDLKNMASRIETFINDEASNNHREDFYGVKNSDTDTDSDSLADSDDEIFLNRNQGIDEVEFDETKFYDLLKGKDGKYQNQDVDEFSSGNEDEMDIPGDANMEEYMRAMDEELYGGLRGRDEGLEGIDDKDIDLNLMKNIIEGIEANPDLYGGPISTLLNSLKIQIPREK Q9US53 JMJ2_SCHPO BINDING 468; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"; BINDING 470; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"; BINDING 556; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" SPAC1002.05c; CHAIN 1..715; /note="Jumonji/ARID domain-containing protein 2"; /id="PRO_0000200598" MSKSTFHQTSPSFVQYTHATDKLKPAPHGMNTRGNNLSSMSKNTGQRKQRSKSIHGLPVAPVFYPDKEEFQDSIGYINKIAPIGEKYGIIKIVPPAGWNPPMQLDMNKFSFRTRRQDLHMMDLRFREIVSYDERVYRFFCNLGMELPESFFISNTSIDLYSLMRCIDSHASLSEKELKVHVWKRILRELSIPFTNASLKEASDLYLRYIFPFEDFVRKYQTSEDQCFETDLFPKFFTKDEHSNISIKDQKTSKQFNPETNESVGILQNQESKRNEQIKQQYMPADNFGSNDNHSHNKKRRLSSLSTNNNHLCDNCHKPVNCEVEDTCKEAYCTKCIINPYEFGFETGNYYTLSNFEKYCDNFKKNYFSKFKDSEITEDIVEKEYWKLVKDNNTSLEVEYGADLSTLDQGSAFPSLAKNPVNPYSKDTWNLNVIASTNGSLLSYIDNPVSGITCPWLYVGMCFSTFCWHVEDNYTYSVNYQHYGDTKLWYGIPGDQAERFERAALDIAPDLVKKQKDLLYQLATMINPDELQKRGVDVYFIDQGPNEFVITFPKSFHAGINHGFNINEAVNFAPKDWLLNGFSLNGVLKYQSLLKPPVLSHDMLVYNLATNPASEISVSELRPWVHEAVKRELGIRIMIRGRYDLKEILYRELMEDAENWQCQHCKAFSYFSQVACSCKSITVCPLHIEYLCKCDLSNKTLRLKVDDNELQKLLSY Q9US54 TAF11_SCHPO SPAC1002.04c; CHAIN 1..199; /note="Transcription initiation factor TFIID subunit 11"; /id="PRO_0000372420" MKRTGSASSVPRFQRSMSYDQSNSPTAGAHAKANTASPAAEPAPSSKEKENWNRQEENDLEEDDRDDFGTAAISKVAGKPGETDDEANEKLRTKYLLESFDEEQMQRYEVFRRANLNKTNVKKLANQILNQSVTPNVAIVISGFSKVFVGEIVELARKIQDQWGDTGPLSPDHLREAYRLSRQNRRLYPQSRHVSHLFR Q9US59 SKB5_SCHPO PTM: Phosphorylated in vivo. In vitro, phosphorylated by shk1. {ECO:0000269|PubMed:10593886}. SPCC24B10.13; CHAIN 1..140; /note="Shk1 kinase-binding protein 5"; /id="PRO_0000097777" MAEETEEDYLVVGRDYLYPPDHELHYGFHARVIEEEEERFVDDTFDETIEGSDDSESIDDTEVFYDAEESESTHPSASFNVLADAVALYDFEPLHDNELGFTTGQRLCILSESSDGWLIAYDDASGRSGLVPETFVKLEV Q9USD4 ALG12_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a di-trans,poly-cis-dolichyl phosphate + an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, Rhea:RHEA-COMP:19518, Rhea:RHEA-COMP:19519, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260; Evidence={ECO:0000250|UniProtKB:P53730}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29536; Evidence={ECO:0000250|UniProtKB:P53730}; SPBC1734.12c; CHAIN 1..546; /note="Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase"; /id="PRO_0000215785" MTSKESICWYLANILLVTCIGYYSYKTPFTKVEESFAMQAIHDIQTYRWDLSKYDHLEFPGAVKRSFIPSLFIAVLSYIPSWFVNPLLAARWTIGYLSWESMNSVSCSISKRFGTLSGALFILFSCAQFHLVYYMSRPLSNIFGLIATNHSLSLLLKNNYYGSISILVFAAAIVRSEIALLLMCLILPLLLQRRITLSKLLLVGISSSLAAVGASFLIDSYFWGAWCWPELEAFLFNVVEGKSSDWGTSPFYYYFVRLPWLFLNPTTLLFLLISFVYIKPARLLIYVPLFFIFVYSFLGHKEWRFIIYSIPWFNAASAIGASLCFNASKFGKKIFEILRLMFFSGIIFGFIGSSFLLYVFQYAYPGGLALTRLYEIENHPQVSVHMDVYPCMTGITRFSQLPSWYYDKTEDPKMLSNSLFISQFDYLITEDPESYNDTFDVIESVNSNTKIPILPKWLSNHIPREISIRNPAQPVYILANKKARATKPAAVDDYSSFIGHKVDEIKLWPPIYRVVSPDTLLTRDYREDRLNFFIDKDRILTHITQG Q9USG6 RL33B_SCHPO MOD_RES 98; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP31B10.08c; STRAND 9..19; /evidence="ECO:0007829|PDB:8EUY"; STRAND 24..33; /evidence="ECO:0007829|PDB:8EUY"; STRAND 49..55; /evidence="ECO:0007829|PDB:8EUY"; STRAND 64..76; /evidence="ECO:0007829|PDB:8EUY"; STRAND 81..88; /evidence="ECO:0007829|PDB:8EUY"; STRAND 98..101; /evidence="ECO:0007829|PDB:8EUY" HELIX 41..43; /evidence="ECO:0007829|PDB:8EUY"; HELIX 60..62; /evidence="ECO:0007829|PDB:8EUY"; HELIX 92..94; /evidence="ECO:0007829|PDB:8EUY" TURN 77..80; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..108; /note="Large ribosomal subunit protein eL33B"; /id="PRO_0000192806" MPAQGHRLYVKAKHLSFQRSKHVIHPGTSIVKIEGCDSKEEAQFYLGKRVCYVYKSSKAVRGSKIRVIWGTIARPHGNSGAVRARFVHNLPAKTFGSSLRVMLYPSNI Q9USG9 TYDP1_SCHPO ACT_SITE 122; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q9NUW8"; ACT_SITE 401; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q9NUW8" BINDING 124; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9NUW8"; BINDING 403; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q9NUW8" SPCP31B10.05; CHAIN 1..536; /note="Probable tyrosyl-DNA phosphodiesterase"; /id="PRO_0000340099" MSTLEPEKRRQHEDKSNEIIDSPIFLNKISALPESENVHCLLLKQLIGSPQLKQTWQFNFCVDLNFLLENMHASVFPTVDVRITHGYDSKSDSLARLTAQMNHCPVNVKLYSVYVPMWGTHHSKIMVNFFKDDSCQIVIHTANLVEPDWIGMSQAIFKTPLLYPKANDSLSTSSVPEYGNPSKIRKHEGSLDIKDDRNCDIIDVDSAFENFKHKSDTRSSDDLGVIGRQFQQDFLAYLKNYRHTYELIEKLKMYDFSAIRAIFIGSVPGKFEGEEESSWGLGKLKKILKMLEKDSKKDEKTKFEESDICISQCSSMGSFGPKQEYIAELTDGFGCQRGNWKFLFPTVKEVQQSMLGWQSGSSIHFNILGKTAASQVETLKKGKNLCKWVAMKAGRQRVAPHIKTYMRFSNDGELLRWVLVTSANLSKPAWGTLEGHKAKSRSTRGLRIRSYEAGVLLYPKLFEESQRAPCIMTPTYKTNTPNLDEKRREFYGKRVIGVRMCWDFPPVEYEDKDEIWSPVINRTDKDWLGYVWPPNW Q9USH1 MED31_SCHPO SPCP31B10.03c; HELIX 13..28; /evidence="ECO:0007829|PDB:5N9J"; HELIX 30..38; /evidence="ECO:0007829|PDB:5N9J"; HELIX 41..43; /evidence="ECO:0007829|PDB:5N9J"; HELIX 45..54; /evidence="ECO:0007829|PDB:5N9J"; HELIX 55..58; /evidence="ECO:0007829|PDB:5N9J"; HELIX 60..63; /evidence="ECO:0007829|PDB:5N9J"; HELIX 70..78; /evidence="ECO:0007829|PDB:5N9J"; HELIX 81..88; /evidence="ECO:0007829|PDB:5N9J"; HELIX 90..103; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..139; /note="Mediator of RNA polymerase II transcription subunit 31"; /id="PRO_0000212533" METKWLLSKVPDDKSRFEIELEFVQMLSNPWYLNFLAQHKYFEDEAFLQYLEYMEYWREPEYVKFIIYPTCLHMLTLLKNPQFRNDISRADLSKQVNDEIYYEWLGKGLQQYGSADDATLSQPQQEEDEKKVDVKKENE Q9USH9 YJQ1_SCHPO BINDING 308..315; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 627..634; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" MOD_RES 27; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 47; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 55; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 57; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 97; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 137; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 163; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC825.01; CHAIN 1..822; /note="Uncharacterized ABC transporter ATP-binding protein C825.01"; /id="PRO_0000310289" MARGKRSTQRDADLELESLQSEIESESPQPVTKSKAKKNKKKLNKASAFNSDNDSNYDLKPEDDEVDEEVVPVKKKPSKKSKKAKANAFEAFADEQSVEEEEEEDSEKPVRKNKKSSKKASPKNAFDALADDMDDLSLDEEESESSEKSKKKKKKSKSKDDGSEALDDGDIESSEKDKKKKKKSKENDDAPKKDRKTRKKEEKARKLASMLESENKDNDANAAPLNKTDAFKDGLPSGRLIFAYASGQKVAPDGSNPADGITVTGNLLSPPNSRDLQVEKLSVSAWGKLLIKDSELNLINGRRYGLIAPNGSGKSTLLHAIACGLIPTPSSLDFYLLDREYIPNELTCVEAVLDINEQERKHLEAMMEDLLDDPDKNAVELDTIQTRLTDLETENSDHRVYKILRGLQFTDEMIAKRTNELSGGWRMRIALARILFIKPTLMMLDEPTNHLDLEAVAWLEEYLTHEMEGHTLLITCHTQDTLNEVCTDIIHLYHQKLDYYSGNYDTFLKVRAERDVQLAKKARQQEKDMAKLQNKLNMTGSEQQKKAKAKVKAMNKKLEKDKQSGKVLDEEIIQEKQLVIRFEDCGGGIPSPAIKFQDVSFNYPGGPTIFSKLNFGLDLKSRVALVGPNGAGKTTLIKLILEKVQPSTGSVVRHHGLRLALFNQHMGDQLDMRLSAVEWLRTKFGNKPEGEMRRIVGRYGLTGKSQVIPMGQLSDGQRRRVLFAFLGMTQPHILLLDEPTNALDIDTIDALADALNNFDGGVVFITHDFRLIDQVAEEIWIVQNGTVKEFDGEIRDYKMMLKQQIAKEREEERRIELEKQKK Q9USI4 SAC32_SCHPO SPCC70.06; CHAIN 1..458; /note="SAC3 family protein 2"; /id="PRO_0000316864" MSTKVKQKQKQKHRPKPSLDRSDSTKRAARAARFSTTLDANFQALKKKRKDEQESFQAKQSTNWEKSSVLVGTCRQMCPEFELEERKLQHAIHPYELDPVSKQAHPSLAVKAYHRPAAGKGPILPSDVRPPSILKNTIDYLFKVILDRYSLREAHAFVRDRTRAVRQDFSVQSSFSQDSVYCHELIARFHIISLHELAHTPNFSRQQEIEQLSKSMEILYTLGQLYDYMHLRKEHCTHEAEFRAYMVLLSLGDPSVGLDTLSWPDFVFKKPIVKTSLKLYSLAQRNNHTITTSNSISLSLVSSFNTEATSNLYTRFFKIASSFRVSYLMGCLLDLFVPSIRTGALKAMKKCYLSAHSNIPFKDLMKILAATSEDELVQCCKMHGLKIEYIGEQPSAVVLNRKTVITEPLLSSEISCRFADEKKPGTNVSDLICLDTDGSSLHRKKPKLFKKRSIVRQR Q9USI5 STI1_SCHPO SPCC645.14c; CHAIN 1..591; /note="Heat shock protein sti1 homolog"; /id="PRO_0000106342" MAEELKAKGNAAFSKKDYKTAIDYFTQAIGLDERNHILYSNRSACYASEKDYADALKDATKCTELKPDWAKGWSRKGAALHGLGDLDAARSAYEEGLKHDANNAQLLNGLKSVEAAQTQAASGAGGFNPFAKLGSQLSDPKFMEKLASNPETASLLADSAFMAKLQKIQQNPGSIMAELNDPRMMKVIGMLMGIDINMNAGEGAAEEQEKKEEFAPSSSTPSADSAKPETTNPPPQPQASEPMEEDKTAEELEEAATKEALKKKADQEKQIGNENYKKRNFPVAIEQYKKAWDTYKDITYLNNLAAAYFEADQLDDCIKTCEDAIEQGRELRADFKLIAKALGRLGTTYQKRGDLVKAIDYYQRSLTEHRTPDILSRLKDAEKSKELQDREAYIDPDKAEESRVKGNELFKSGDFANAIKEYTEMTKRAPSDPRGFGNRAAAYLKVMAPAECIRDCNKAIELDPNFAKAYVRKAQALFMLKDYNKCIDACNEASEVDRREPNTGKNLREIESQLSKCMSAMASQRQNETEEETMARIQKDPEVLGILQDPAMQAILGQARENPAALMEHMKNPTVKSKIEKLIASGVIRLG Q9USJ1 THTM_SCHPO ACT_SITE 252; /note="Cysteine persulfide intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00173" BINDING 190; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate; Xref=Rhea:RHEA:21740, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57678; EC=2.8.1.2; MOD_RES 164; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4B3.01; CHAIN 1..298; /note="Probable 3-mercaptopyruvate sulfurtransferase"; /id="PRO_0000139401" MFSVGKKISFILPIKGVLQKLKDNAQKTVLLDATWYLPTDTKNGKKEYLESRLPGAQYFDIDEAKDHKNPLPHMLPPADEFASYVGKLGIDRNTNVIIYDRKGFFSSPRVFWTFKVFGHEHVFLFPNAFNAWKTEGLELETGEPRTPKPVVYEGAKLNKDLVASFDDIVKVIESPDAAGVHIVDARAHERFLGNVPESRPGLASGHIPTSINIPFTETTAAGITAPKPEEDLEKVFSSHGLTDKSVPIITSCGSGVTASVLFAALKECGFKDVRVYDESWSGYGKRANEDSSLLATGP Q9USJ2 GOT1_SCHPO SPCC4B3.02c; CHAIN 1..129; /note="Protein transport protein got1"; /id="PRO_0000218585" MWLSDLQKIGVGTTALGFLFMIMGIFMFFDGPLLSLGNLLLVFGFFMIAGFSKSVSFFLRKDRMLGSISFFSGLLLTLFHFPIIGFFVECLGFFNLFKVFYPLIISFLRTVPYIGPYIDRLTSYQQSPV Q9USJ3 YJ23_SCHPO SIGNAL 1..27; /evidence="ECO:0000255" MOD_RES 476; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 478; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 596; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4B3.03c; CHAIN 28..679; /note="Uncharacterized protein C4B3.03c"; /id="PRO_0000014205" MSLLRIRKASLYGFSTVFILLQSYAVAYPLRAFRQNDGIGIAMNPSQDGGFVSAEKDSDFEYWMKLIISAVLILLGGVFAGLTIGLMGCDDLHLQVLEQSGDASERVHARKVLKLLRRGKHWVLVTLLLGNVIVNETLPIVFDSIIGGGWPAVLISTAMIVIFGEVIPQATCVRYGLSIGAKLEPIVLFMMYLLWPIAYPTALILDACLGESQSTMYKKSGLKTLVTLHRDLGIDKLNQDEVTIITAVLDLREKHAESIMTPIEDVFTLPMDRILDEDLIGEIICAGYSRIPVHKPGFPHDFIGMLLTKTLIGYDPDDKWPVGKFALATLPQTWPNTSCLDLLNYCQEGKSHMILISNSPGEPHGAIGVITLEDIIEELIGEEIIDETDVYIDVHKGLPRVGENNDFWNRMLHRSHLSTMAALHKSQRSHDLAANEHAPILNPKNSALNPRLVTNDRVKVKSPSLIQSSTGYGSMSQSPSRSDLPSKISRVNAELQAHGSQRSSIDVSKENKSSVADGPSSQAHNGPSTQPPEALPNGTDPSSSKTTENNGNQQSERTESADGKKDNSGSISSNSSKTFTGKRVRLGNVIESNVVSPDGTNRIVIEPFERSVDPNNADIVEMVERNGIVVPKVTVTSHEDDVDSVHNTPMSVSSTLSVKTSSSKVPRNKRKRRKGKSKK Q9USJ5 DCUP_SCHPO BINDING 24..28; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 42; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 74; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 75; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 153; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 208; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 331; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37; SPCC4B3.05c; CHAIN 1..355; /note="Uroporphyrinogen decarboxylase"; /id="PRO_0000187576" MKNDLILRAAKGEEVERPPVWIMRQAGRYLPEYHKLRAKQSFFEMCQTPETACELTLQPVTRFKGLLDAAIIFSDILVIPQALGMQVVMLEQKGPHFPKPLVVPEDIDLLEKTPNISAKLGYVMDAISLTREKLDGQVPLMGFSGAPWTIMAYMIEGGGSKTFAKAKSWLFRYPEASHKLLKIITDATVSYLIQQVYAGAQLLQIFDSWAGELSPEDFTEYAYPYLVRICQEVKQHLKKKKRDEVPMIVFAKGAWYAIDQLCDSGYDVIGLDWTVSPKEAVRIRGNRRVTFQGNLDPNILYGTREIIEARTKEMIQDFGGGKQGYIINLGHGITPGVNPDDVRFFLEKCHQYGSA Q9USJ6 FMNR_SCHPO BINDING 22; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q07923"; BINDING 96..99; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q07923"; BINDING 126; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q07923" CATALYTIC ACTIVITY: Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783, ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.39; Evidence={ECO:0000250|UniProtKB:Q07923}; CATALYTIC ACTIVITY: Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618, ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.39; Evidence={ECO:0000250|UniProtKB:Q07923}; SPCC4B3.06c; CHAIN 1..200; /note="NAD(P)H-dependent FMN reductase C4B3.06c"; /id="PRO_0000315910" MTLPEKLLKITPKILVIMGSVRSKRLCPTIATWVGEMGKRETNFDYEKVDLTDWPLSMSDEPGLPIMGIDVYTQEHTKAWGSKIAGADGFVFVTPQYNGGYPAILKNALDHLYHEWNGKPLLIVSYGGHGGGDCASQLKHVAGFLKMRVAPTMPALTLPRDKIVQGVVDPAVEFTKHLGELKKAFGEFSQLFESNPERKP Q9USJ9 MNP1_SCHPO TRANSIT 1..33; /note="Mitochondrion" SPCC4B3.09c; CHAIN 34..173; /note="Large ribosomal subunit protein bL12m"; /id="PRO_0000311767" MFRIASRQTRNLRALSSSKNWARSLVNTRSFRAAASVQNNNAQIGEMVDKISSLSLLETSELVKQLKEKLNIAEIAPMAAVAPAVASAAPSEEKAPEEKKEEKTTWNLKLESFDAGSKAKVIKEVKSLLGLSLVDAKKFVESAPKVLKENILKEDAEAIKSKLEKLSCKVVLE Q9USK4 CWF20_SCHPO SPCC4B3.14; CHAIN 1..290; /note="Pre-mRNA-splicing factor cwf20"; /id="PRO_0000079615" MSLVSYPRSESESDIEEETPLASKSFDPTLFQHARRKLSVDSTKKSPKRLKRQVDLQKSSFNDKTFNESDVISNERFKSNDLLELLPAPKNQAELAPKSSKRSDLDLNENYLLPNNSVSDLTSTGSSETVKKSTYSEKSGNVSLFNIVGSESKQASLVDSDQKPYQPILIKPKARANPPKLRNQPENDFISIANHSVHSNAEDINIINEDYIEIGRHRKEKGRIIDVDINKLPKPTQEALPSAPTIKSVAPGRHQLSSLVEMAISQKDNFEAYFEQQRSNKKASSQKYGF Q9USK7 YJ2I_SCHPO SPCC4B3.18; CHAIN 1..316; /note="Uncharacterized protein C4B3.18"; /id="PRO_0000317226" MPEMDKSNDFFEENPCPNSLGDVSSLIEDFINLQSNSQNIAFVTSGGTLVPLEQNTVRFIDNFSAGNRGAASAEYFCKSGYSVIFLYRNYSLMPFTRRYEGPWTNLFERSNGSQEKPWIVKQEFQSTVFNALNELDTYTKHHRLIMIPYTTLTEYLWYLKAIAERLQIIASRALFYLAAAVSDFHIPPKELSEHKIQSGSGSNKLEVKMHPVPKFLRFLVDTWAPEASIISFKLETDPSILIDKARVALQRYNHQLVIANLLSTRKRSVAFVTSKTVEWLHLSDDDIVKKVEIEQYIVSRAISLHKERIQEFAKAP Q9USL3 SYIM_SCHPO BINDING 628; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5; SPCC18B5.08c; CHAIN 1..973; /note="Isoleucine--tRNA ligase, mitochondrial"; /id="PRO_0000339654" MKFSYISSLPKGHNHICCKQAGRFLSSQADLKKYSESLCLPKTSFPIKPNVKGNNEKYFKSITSDLYEWQKENLNKEDSFVLLDGPPFANGRLHIGHALNKILKDIINRWQLLKGRSVHYVPGWDCHGLPIESKAIKANAERKSSLEIRKIAKDFANSAVQEQLMMFQRMAVMGDWPSRYITMSDKFEIAELKVFLSLLQKDLIFRQNKPVYWSSSSRSALAESEIEYDDNHVSTSIYFTFPVNSFSIDGCEYNNVKALVWTTTPWTIPSNLALSYHPEINYGLYQHNNSIYLMSDNLVPNLDFMQGAKRLASCPSDIISSFTYENPLLPKQSFPFLQSNYVTNDIGTGIVHVAPGHGMEDYLLGLENNLRPFSPLDDYGRYTKEALDGSLEGLEVLGDGGKKVISIMKNQNMIVKVSPYKHRYPYDWRTHKPLILRATPQWFISLENERKTAIKALDSVKMIPPNSRARLLGFLNGRPEWCISRQRAWGLPIPVLYEKGTKIPLLTVKSVSYIIEKMEVEGVDSWFNDTENNGHAQWVHPDYRNKEYIRGTETLDVWFDSGTSWTTIAPRKNKPLIDLCLEGSDQHRGWFQSLLLTYTAYQSKPEAPFSTLFTHGFIFDERGQKQSKSLGNVTDPEDVINGKLLKGKKLPYGVDLLRLWVASCDSTNDTNLGPNILTQVGESLKKWRLTSRFCLGNLHDWNTSSSVDVGELRGIDKLALVQLDKFQTEIRELYESYSINKVVHHLNYFMNSFLSSTYFDAVKDRLYADLPNSVSRRSVQTVLYHSLLTLIWAISPITPLLAQEIWQSLPDSYLNSSYQTPFHAGETHLISSLRSKVDLLDRKFLIKEYLVLQQLKYSINLLITAARENLTIKNSLEAYVVIKSKSQSLLSFLKNYSSDLPFLFNTSKVFINEIPENLKLASVTQPEVQLDYGVANISLFFSNQQKCLRCWMHTAHEDGLCDRCESVLAQLKR Q9USL7 RSM18_SCHPO TRANSIT 1..31; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC18B5.04; CHAIN 32..166; /note="Small ribosomal subunit protein bS18m"; /id="PRO_0000317315" MLGRRIFSPAPNRGFILCNLIQSNNSTRRGFSDNRKFNERNSEASSNVGFQRRVRSNIPSYLSASVEEGDIYSPNDLLFETVKAKNQAKFYEPVREDCFKTVNENPMNYWKNPVILSRFVTELGRIKPRGDTGLTAKNQRLLSRAIRRARAAGIMPTKYKSVYSEN Q9USM5 UBP1_SCHPO ACT_SITE 288; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 806; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPCC16A11.12c; CHAIN 1..849; /note="Probable ubiquitin carboxyl-terminal hydrolase 1"; /id="PRO_0000080602" MASTATQNASTRYSQIWIDQPASLPFQDSINLIKEDKEKWKKEKTAFLIDYDWFEGYVDFIYGEGDNPGPITQWRLLDEKNELKHSLEESIDYSIVSASLWHMLVEWFGLEGLAIERKVLLVGLAAEQKPFVDIYPINFTLHVLFDPINGENTSYSPLYQIDEPYHSDEPYAFSFSRSDTLRSLYKQVMEAFQISDGTSFRLWYLNKSNLSSRFVSLSEFNDQPAIALLSEYAVCMTIFEIDIADGSLLLEFQHPNGEWLSDSITKEQNLTINKEIGLCGLYNLGNSCYMNSALQCMIHTHELTKYFLSDSYEKDINYNNPLGMMGKVALSYASLLKMIHHTADMHSVSPSSFKFIIGEFNTYFSGYRQQDSQEFIAFFLDGLHEDLNRIQIKPYFERPDLFDEHPLHVQRVANQCWDIHTKRNDSIIVQLFQGMYKSTLECSICYQKSTAFDPFMYLTLPLPTSAKWRHKVVYVPPFGTQSPVELYLELLMESTVIQMKFQATEKLQKMGLECGELTACDIYRGKVYKVLKNKDKISKKIHKWDHVVLYGSTANGLTIPIVHGCKRPAMPGSYQSNDVFGFPLQLNVRSRNVLTNDLVKEIVELYRVYAGIDVAIGTLQLGLKRMESKAGKWECIKEIEVKRFEIVEEEEIVIDDKTVIMCLWNDQQYEKLFYNCEWIFEKIQFHMESITLEDCLLEFSKPEQLDLQDSWYCPGCKAFRPATKRLEIWRLPKILVIHLNRFSGHGGDLRRRRKRRDLVVYPVFDLNLKQFLSPFIKDHEWLSSQKSMLYDLYAVDNHHGFMSNGHYTAYARDASSQTFFKFDDTAICEIDPEDIVTSSAYVLFYRAKN Q9USM6 CYB52_SCHPO BINDING 38; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"; BINDING 62; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" SPCC16A11.10c; CHAIN 1..129; /note="Probable cytochrome b5 2"; /id="PRO_0000166034" MAEKTITVEEVLKHNTRDDLYIVVKDKVYDISKFLDAHPGGEEVLVDLAGRDASGPFEDVGHSEDAQELLEKFYIGNLLRTEDGPQLPTTGAAAGGSGYDSSQPVKPAMWLFVLVMVVAYFAFRKYVLK Q9USN0 GPI10_SCHPO SPCC16A11.06c; CHAIN 1..506; /note="GPI mannosyltransferase 3"; /id="PRO_0000246266" CARBOHYD 115; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 395; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRIWFWLAILVFRWWNALWVKTFFQPDEFYQSLEVAHHFIFRYGFLTWEWTSAIRSALHPLIFAALYRVLQVLKLDSSYFVFTNAPKLLQGTFAAILDYGTYKFALVRYGSKTANWTLACSLVSIMNAYVGVRTFSNSLETTLTSIGFYYFSYYLKYENSSPEQRKKAYSSLLGFISVAAFACFIRPTNILVWIFPLLFWNKNPQTPIKDLLSFSNVFNRFRFLYALGYGRLFGIFVLCVSLFLVNIIADRILYGRFVFPIISFFQFNVTSGLSSLYGLNAWHYYLSQALPLICGGFLPFVLLTMDLQTAGTILCVFFPYSLIGHKELRFVYPISPILLTLAGKFFSSFSSWKRAARFFFLIGLGHALVITFLCRFHQFGVMEVMPLIHSLAEKNQTGLILAPCHTTPWQSHIHSPFAENGWKFLTCEPFEKPFDETDRFYENMPTFLDKIKEWPDYLIFFEERFYSLYSYLDSRGLKYEEVQRYYNSLIPESRERAGALLVYKKL Q9USN1 SNX12_SCHPO SPCC16A11.04; CHAIN 1..1010; /note="Sorting nexin-12"; /id="PRO_0000316573" MYQQHIFYFITGGIFILWILAHSFFVKIIYLWASGCLLWYCLETRTFENKNNLGTSEPFLVNPAIFQKRARQLALSKLLLRQPLYPGIPEISEEIESIISHFMQKYIKVWSYQIIPEPTISNSIESHLRKCLMVLLSRVDEIDLADVLVKTVLPLITKHLRLFVEAEQLVVGNKAVSFTDHSELSREVAAKYDHGRLHEAVLLSGNPMVAQKRYLRNWTTQVLSIILPNYYETSPLVLSLVTEVIINTTLLPLVSYISDPDFFNYLIIQASGSIIQRRRKIRRLKRAIRKQSNHFQVGARRLRLKDSQHSFEQYIHEIKKISNISDARRLRSELMVQRRQLEQTEAFDFEFKQYRERLQIAIITAEKRISLLSGTPFQHKEAVLFEQVQSLLQILSDSAAVSCFLEFMERKNRSRYLHFWLVVEGLKESQDDPLNAHMIAPFSDIVSDHTDFTAIVKSYFESVDNPLDIPKPLTNTINKFVNQSKDNLNPDLWVEARNAMLMAQEHVFDIMQNSDYSEFVNSEIYYRFLAQDVVSDHKSTNSSATFSRLEELGENIPAISKQPSYLSISSSSKSINSSPSPSIQLSVSSSISRDKNLSPLDLELDDPTYSDEEEVLFAPPGDLQLSESIDELNNNIEELKAQLNAINTLIKKAELVADQKQLKSLTKNHQEIEKAIHRKERQRDQYMSQEEDSKLFNRSRVSIDSFKISKEENTPDFAVYTIRIERLENGHVRSGWMVARRYREFAELHKQLKQTYPGVRSLKFPQKSIITSLNKNVLEYRRGALEEYLQSLFRMPEVCDSKMLRMFLSQQNITAPQMFNPKEVGKKWKQLLEVLGFEVNNSFNASNVNTNSSFSGPISEFLVELFSPNDDAKQQWLPKKTYISILEQLFGGALEKRIRLQLFQLFTPEKIYRKLREFRRGLEGKSNHDHSKDRRHSRARKPAYADRNQLKAEAGILLASMFPGYTPDIAVKRIFRILQNQSLNAHVIYTLLDEILLALKKHARSTNKAT Q9USN5 GDH2_SCHPO ACT_SITE 654; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2; SPCC132.04c; CHAIN 1..1106; /note="Probable NAD-specific glutamate dehydrogenase"; /id="PRO_0000310353" MYLTKQIPHYSRIHTTQLLTVVNHRTIPFKIRGSFSNCRRYSNFATVPLLERPFKNKSKHNTARASRPFSTQKMLLTKSHPPNMYKDSVFFGYRPIVFSGKQDQKSKVIQCLRTERKTIPDDLVEDEVDRFYNKLGLDDYYFQMEPVSIIADHIEIIYAAKIAAHASHAKEELNIHVKNENEDLAIYLDSSPVTQPELDQSSAVEESISTRYLDPFKLTDPTAYRVESFTSVTNIDRTSTENSNIYTYFVTKCDFVDNPKKDASPDVPTDIASVSDKTFLEKASDNTIEMYQDVMNSVLTRFGPVVRLFDYQGRSEIRLVVGYRRGSIFQYFPSLSKLFRYYGLHSTRTYVEQFSNGVTIISYNFKPELFKNAAVTSINELFSQITREASLLYCLPSTDFQPLFVSEKLSIQEVTYAHCVRIFCEHVMNKLGPEYSSLSAILDHSNNIHAEILETIKRRLSTLAFTRTKIHDTIMQYPGLVHTLFEQFYLEHAINHNSTPHLHRAKSATSLADEASTYSITPMSATALMDLIQKTCTNEEDVSVMEMFVKFNTHLLKTNFFQTTKVALSFRFDPSFLDSTQYKDPLYAMIMSIGNEFRGFHLRFRDVARGGIRLIKSANPEAFGLNARGLFDENYNLAKTQMLKNKDIPEGGAKGVILLGKDCQDKPELAFMKYIDSIIDLLIVNKSQPLVDKLGKPEILFMGPDENTADLVNWATIHAHRRNAPWWKSFFTGKKPTMGGIPHDKYGMTSLSVRCYVEGIYKKLNITDPSKLTKVQTGGPDGDLGSNEIKLSNEKYIAVIDGSGVLYDPAGLDRTELLRLADERKTIDHFDAGKLSPEGYRVLVKDTNLKLPNGEIVRNGTIFRNTAHLRYKADTFVPCGGRPNAININNVEQLIDDHGRPAFKYLVEGANLFITQDAKSVLEKAGVIVIRDASANKGGVTSSSLEVLASLSFDDASFKENMCVHDGKVPTFYADYVNEVKRIIQRNANLEFEAIWKGHSENKIPYTSLSNHLSTEIVKLDHDIYNYEKLWADVGFRNAVLRASIPKTLQAKIGLEKMLERIPESYLRAIFSTYLASRFVYQHVVSSDPFAFFDYISTEMKMLKDA Q9USP3 PPR6_SCHPO TRANSIT 1..13; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC11E10.04; CHAIN 14..443; /note="Pentatricopeptide repeat-containing protein 6, mitochondrial"; /id="PRO_0000353137" MRILGSLPNNIRKCTFKLILQKRYSHTDILKELLYDISDSQKFIPSASPIASNLLRVSSYGKLSSLFIEYSKARSKKEFDQLRTSDFQSILRSVVCPKNGKNIRHRDRDLVSLQIKLILQDADRLGIQFNIVDYTHILRVAMYTGNKHILEYIVARVKEKRIRPSVDYFNAILGVIGGNRWSLSKFQSPAFRGSPVTEPVSGKMLDMIEVDFPNYDLVPNSTTYDYLMVGLSRDGKIREIYDLIDTVWGINENSSSKKVDCGNVTFPTHHTVFSIISALGYLGDVSSAVSLSRKLTSVYKINFPELAWRYIIYWSIASLQFRAPAGHARIKNIELFIRLYSQMYRHCVPIIEIYDTSIKFYMKHGRFGLLEKVCESWTKQFLGSLEKQNNEVKKKHLQLLEKQISKLMRYAETERPHDTKRVSVKWSNVLNQIHSSVGDPAKP Q9USP4 MUG1_SCHPO SPCC11E10.03; CHAIN 1..351; /note="Meiotically up-regulated gene 1 protein"; /id="PRO_0000278483" MKEMINLDSSSEPSIVTKQFSVEECLSKLKEQHCYVPMRTIGRLRLRKSSDQTEKKCWKEKLMKIRSELEELWEQSMMYEEQKELTQLGEMLDRLWDKHINSEGSKSETISDTAISGNDDTMEKRLEQFSDDTLQDTLETEKNLNSKTSESLKSPTLSYPFDLDSLDKRIFKLESKIGYADEPLSELLNKCMEKLEIVEQDPQFWQSRIESWKQLLAKDFLKHHERNLCSIEKQTTLKNSSLKELCTEEDIVIMLEICSSQLPFVEQYMPILPLLLERLKSLQNMHTDAAEAISSWQGSKDVMMTMQSELNEWKNTVERLDHSKFYTQSVEEMRRLSDTVTQLEKRVLKLQ Q9USP5 GPI8_SCHPO ACT_SITE 145; /evidence="ECO:0000250"; ACT_SITE 187; /evidence="ECO:0000250" SIGNAL 1..19; /evidence="ECO:0000255" PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity. {ECO:0000250}. SPCC11E10.02c; CHAIN 20..380; /note="GPI-anchor transamidase"; /id="PRO_0000026531" CARBOHYD 307; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 73; /note="Interchain (with C-182 in PIGT)"; /evidence="ECO:0000250" MIVQFVALLLLNLLQIIAAESSHTNNWAVLISTSRFWFNYRHTANVLGIYRSVKRLGIPDSQIILMIADDYACNSRNLFPGTVFDNADRALDLYGEEIEIDYKGYEVTVEAFIRLLTERVPENTPASKRLLTNERSNILIYMTGHGGDGFIKFQDAEELSSEDLADAIEQIHQHKRYNEILFMVDTCQANSLYTKIYSPNVLAIGSSEVGTSSYSHHADIDIGVAVIDRFTFSNLEFLENRVDSKSKLTMQDLINSYNPYEIHSTPGVQPINLRRSPDDILITDFFGNVRDIELHSEKINWMLPGENTTKPSIKRNSFVFQAQNDMQDDGKGFGISNLKSFLPPTRELKYKKHPISRIISAVVCISFSIGFPYYASKYLK Q9USQ0 SPO7_SCHPO SPBC902.03; CHAIN 1..180; /note="Sporulation-specific protein spo7"; /id="PRO_0000315976" CARBOHYD 163; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 169; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSSYVPNTLSVYHNLLILEASFRKTYLQLQVRRQKYMAFYVSLLVWNFYFGYRVFYRISKYSLIDLTYKLCLLCGIVTLLLFYFSGLYRTTIVYPSRYVQQVNKAMRFFNIRLVITPVPWFQVRKPLDCGVHLILSSKRFDILVIEGWEAFRSSYFASIHRKNNSIQSNESSESPSSKQN Q9USQ5 OAZ_SCHPO SPBC577.14c; CHAIN 1..226; /note="Ornithine decarboxylase antizyme"; /id="PRO_0000220870" MAFRNRMYQLSNVDDADADILNSHFAPNPRGQNHTHGRRRNTLALCTTKDQMFVYGSTPAGGAEWCSEALERSRPRAAFKQQRRRHVPRWISDSFRTCLPKPSGILKEQTVNEEEGNSRHRGKYDCDERIGVAESMNYWHGIVRTEEDGSKTLFLIPESWEDVHLKEGLVAIIDLAVDRLHCSKLVLFVDKNNSSLPYLVKSLHWVGFEPLPHLNCSDHALFGMEL Q9USQ6 SYJ2_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPBC577.13; CHAIN 1..889; /note="Inositol-1,4,5-trisphosphate 5-phosphatase 2"; /id="PRO_0000359407" MQCYLKRKERSVAFITEKYAAIIQKPSVKDSDCIITFTCISLEEFEKIKEYELLFGGEKILGTLGLFNYVCEDMKEGVFLCVARKAKLVLRIGNRDPISKLENVSFISLDQELWDEELFEPMPRNSSPSSTFSTSTSDLNNIEKDNLVNSEYSSKYSSTTRIYPYHSLSQLTDLLTDGSFYVSTNISCFSRFQSEQPYGPKDIYCWNRFLITELDNHFSEAHILEKFPNLLLHCFRGYVERMFIDSMSMSIISKVSSYGSRQTYPPSGIDDSSYCSMFVETEFIVEIAQTVFSFVQVRGTVPCFWEEQFSSWYGPSISFLRSSQASQSLFNFHFSKLYKAYGDIYVIDLLQTKGFEASLYEAYKHHLMLLPFPAVVKKFHFTPDPARPDIDPRLETDLADDLKEMGYTQKSIENDMLESFQKGVFRINDLDCLGRTNVIQYQISRLVLKDIFFNLQIGVTFNILEYLRHLWSNNGDAIAKLITGVGSIGSSATRRGRKSIAGSLSDISKSFGRMYVGRYPDVESQNAILLLLGCFPNQSPVLISESVSSYIQGVLRQRRSEYRVERDFSIFSSTFNANGKVPSTDEFKRLLLPFGERTSAYDLYVVAVQEIITLNMSHLVSSSNQKLRIWEEKILMILNSRDSNNKYMLISSIQMAGVFLGVFIRKDDHLVVSKVTKTTRKTGFGGFSANKGAVAIEMNVCDSDFCFVSSHFAPKVNNISERNMEYTSISDNLVFPSGMKIYDHTNILWMGDFNYRIDSDNEEVRKLVELDDLDKLASYDQLCTEMKKGTVFHGLVEPQLTFLPTYKFDNGTNDYDTSDKQRVPSWTDRILATKSFTRNCYKSCDIRCSDHRPVFATFSLKIFSTCMDKKAGIIRDARIAYIKSKNSNK Q9USR2 UBP10_SCHPO BINDING 89; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 92; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 108; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 114; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" SPBC577.07; CHAIN 1..502; /note="Probable mRNA-splicing protein ubp10"; /id="PRO_0000351443" MSENKDKNNILKRHIEEDNNIDNGKRKKLELGKDMEDVHDIASKEMEEHETTPIISQNLYLDTINRKLLDFDFEKVCSVSLTNLSVYACLVCGRYFQGRGPSSHAYFHALTENHHVFVNCSTLKFYVLPESYQVESSALQDIAYVMRPTFTKLEVQRLDHTPQLSYDLMLKPYVPGFVGMNNIKNNDYFNVVIHMLAHVKPFRNYFLLKNFDNCPQLVQRLAILIRKLWNHKAFKSHVSPQELIQEVTVLSHKKYSINEQKDPVEFLSWFLNTLHNCLGGKKSTIAKPTSIVHYSFQGFVRIESQKIRQHAEKGEQVVFTGDRVIQTNVVPFLYLTLDLPPKPIFQDEFEGNIIPQVELKEILNKYNGVHTQELAGMRRRFHLMTAPPYFIFHIKRFMKNNYFTERNQTIVTFPLDDFDMSPFIDDSFIQSNPKISTKYNLVANIIHESVTHAEEEFHNFRIQIRNPSTNKWYQIQDLYVEEISSDMIRLGESFIQLWERSS Q9USR3 STT4_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; SPBC577.06c; CHAIN 1..1877; /note="Phosphatidylinositol 4-kinase stt4"; /id="PRO_0000314092" MDCIDKSIRRESLRKLGCLPDHGWNLFVQSSNRYSKLLEADSKLFKAQRIEDTVLSICEVTLENKASENALTLFQQLRFYLLNYLFLEDTSEYKSVLCSLDESVYPNLLPLTANICPCILKALLALVRQHRELSSDIVKFLNSIFLALTRILNTPHSSNNNPTHTKTTIFEKVFYASHLGFFFEEIADACISALPQDACLWAMEVCNTILVSDLPCKLIDLHNDSFLHHSNYYAGFGLSYYLYLSSMKAYINSSGCLWYEDATSFWDIVKHRPSSPEEKPFLTQFQSILNLSDKFLSKTGTLRLQEKLGTSCNLFFVLVLKLALLSSSYIGFVPYTYSDWINVLLGSISEDPELLPHLIELMASLACVFPTHFQFAMKRLRLIAIYAPRFDDGNVTYAQLASRKLAQLFNYSSRDTAITSIYQFANLLSPADTPDSYLAAPKERLSISDNMSSSSSQTATVNTISNYLNVIDSVREIALTVNDEKIYGLAISLLIQKFSRKFDSRVSTELVRTLADISTKANDRDFSILVQFYSIQNKMLVKNGDEALTIAICDSRCLIARGTESNSFKRSDLLKSLLEEIIHIGIVRDTPAPELKGYYFGMSKAVQALVECVAGTDWSSLPKEEMYPALFRDMWFTLVINRFRYSVDLGETLEVDLENIAKNSPLLVFEDFGSNFESNLELNTVLRTHIEHSVISQIKSELLVRVPNIDLKPLSTSEICFLSAVLLLESLRCKSNKLSALVEYLLDPSLRDSQLPQSIRAIALYNLTSFVESLSKERRVASSTIDEFQKLLCLCCNRVDCVRQLALECMNYIMETLPHLLGIKEILFSVLELSSLLWKARTEECTDQYVPQLLYKSNKLNLSVILSDIYSCREEVLFQFNRHARSWIQNSSKAIPYQVKNLLESYLADFVDFDDLEVVELGRSLAVELGTRIVSSDRDNFVLPAFGNWTPDTSSEFMAEYTIRQRYSHVDNSILNIEGDMSTDRIDLILNEKSKLFETHLAALKSLEDDILQGNTVSPQRLRNEVRKAAAHAVQEPIFQFSVLARKIVRIPFLDFSPSSFKLGITLWNWMMNQVPSFSSFLISNIIRNWKNEIVTEKRGYFSTAKSKSPLALPMTYSPTERASFLSYKNKVMSQMIPHLLLLQLIAGNFEGFWYGDRQTAKLIVHFMKFVLKKITSMEVNLNVLTRELHFKFVSFGLRIAENLLNSPLGSRFYNLCVDAGLCWFSGMPNWTYGADKLHVAAEISVMRSLRDKLDSFLLRYPLKVSTTLKQKLLIILLNNEMYMLYTWLTPVLHGRNVRMVEPIPDSDAASSPITLEMLQVAWNVSPNIVLYAPKRFQNAPLKQMALNFVIANPFTSVKHEVALEYLFEHYPSGEFPIDRKFILYWEPMYPVSGPVMFMPNVKWNPQLLQYTMRSMESYPVSVTFFYVPQIVQSLRYDSMGYAESFILETSGTSQLFAHQILWNMKANLYKDEAATVPDSIKPILDRVMDKMINSLSGEDKQFYEREFTFFNEVTSISGKLKPFIRKSKPEKKAKIDEEMKKIKLDVGVYLPSNPDGVIVGIDRKSGKPLQSHAKAPFMATFKIRKEKLVDADPEELAVNGTEEEAGDSAKKQTYEVWQSAIFKVGDDCRQDVLTLQLIAMFKNIFNSVGLDVYLFPYRVTATNPGCGVIDVLPNCISRDMLGREAVNGLYDYFRTKFGDEDSIAFQKARSNFVQSMAAYSVITYLLQFKDRHNGNIMIDDQGHILHIDFGFIFDIAPGGITFESAPFKLTTEMIAVMGGSNKSQPFQWFQELCVKAFLACRPYAHYICQAVEVMLDSGLPCFKGQLTITHCLERFALNLNERQASTFMLHLIEQSYANKRTLMYDQFQKATNGIPY Q9USR5 THOC5_SCHPO SPBC577.04; CHAIN 1..200; /note="THO complex subunit tho5"; /id="PRO_0000353829" MTENAISDCLNVLDSTRTLCLRIHELKQHSRDADDQNPEQIKRQLMSKLLILREANRKSYEQLVQAKTITAEHKSELDNARIRLQALQYKKLHLKTIIKNYEEKEHIYTALPLVSKEEFLKEHPEFKSSNDHDLMLAILEDELKERQRLSTLKQELLKRKAALISENKAKRNALQKGDEKLQTFLRSSVPVQEYYNITSM Q9USR7 RL38A_SCHPO SPBC577.02; STRAND 22..27; /evidence="ECO:0007829|PDB:8ETC"; STRAND 33..38; /evidence="ECO:0007829|PDB:8ETC"; STRAND 43..48; /evidence="ECO:0007829|PDB:8ETC"; STRAND 65..68; /evidence="ECO:0007829|PDB:8ETC" HELIX 8..16; /evidence="ECO:0007829|PDB:8ETC"; HELIX 51..60; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..74; /note="Large ribosomal subunit protein eL38A"; /id="PRO_0000215443" MPRQISDIKQFLEIARRKDATSARIKKNTNKDVKFKLRCSKYLYTLVVADAKKAEKLRQSLPPDLTVTEVGKKA Q9USS0 PNC1_SCHPO ACT_SITE 11; /evidence="ECO:0000255"; ACT_SITE 119; /evidence="ECO:0000255"; ACT_SITE 163; /note="Nucleophile"; /evidence="ECO:0000255" BINDING 53; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P53184"; BINDING 55; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P53184"; BINDING 94; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:P53184" CATALYTIC ACTIVITY: Reaction=H2O + nicotinamide = NH4(+) + nicotinate; Xref=Rhea:RHEA:14545, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:28938, ChEBI:CHEBI:32544; EC=3.5.1.19; SPBC365.20c; CHAIN 1..220; /note="Nicotinamidase"; /id="PRO_0000371807" MSFHPALIIVDVQNDFVHPVYISSGESALEVVPVINRLLENDYKWDTVIATKDVHPKDHLSFTTSHSSTPKPSGTVVNIEAYGHVYKQTLWNSHCVENTPGCEFPDSLNGDRIEFVIPKGSDRLVESYSGFYDAIGRDNGLKAILDKKGITDVFIAGVATDICVKETALHARHWYNTYIISEAVKGSSTESHNQAIKDFRDAKIEVISEKDPILQSVRKV Q9USS8 YNB2_SCHPO MOD_RES 290; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 293; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 296; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 418; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 428; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4.02c; CHAIN 1..437; /note="Uncharacterized protein C4.02c"; /id="PRO_0000116851" MSLNVDIGLGTYDFSKWGYIDVHKIKEVHIYDFDNTLFQTPLPNANIWSNQAIRILMAFNILANGGWFFDPHVLAATGDGVEVEEKRAWEGWWNEKIVSQARESIRRPDVLAVLLTGRNEGFRGIVEKIIASKGLDFQGVVFKLQAPDGFWPQTLNFKLWFFNEVYRHFLYINSTRIYEDRPSHIEAFSAWLTERKKKNKNADFEIIAVAEPPKYLKFKVEIALVRGMLTAHNLKAPSLKLPLYKFVKNVIATVVTVPVAELHHIRNAFFNIPIAEIMESVSANSSRRNSHDSNSTIICEPEYPPDTSFNSSPGRLWIVTAIGRYRDEYWTVRAEAAEGYDCEKIHEIDVADIPSLYGTILYVSMSTGIVKSEIGDIGAQQWKTLAPSERWILRTNIRKECTYDIRYKRPYVSSLKYSDDDLTAGRASPMTGPTKRK Q9UST2 IMP2L_SCHPO ACT_SITE 46; /evidence="ECO:0000250"; ACT_SITE 92; /evidence="ECO:0000250" SPBC336.13c; CHAIN 1..180; /note="Mitochondrial inner membrane protease subunit 2"; /id="PRO_0000259581" MANPFVRNQSFKSVFFKNLVGITLWVPVLMFVEQHVVSVGTIEGRSMKPAFNPETNMLQRDRVLLWKWNKDYKRGDVVILRSPENPEELLVKRVLGVEYDIMKTRPPKKLSLVPVPEGHVWVEGDEQFHSIDSNKFGPVSTGLITAKVIAILFPFSRAGRIDHEGFRKNAVFLSGKRSVK Q9UST3 VPS52_SCHPO SPBC336.11; CHAIN 1..508; /note="Vacuolar protein sorting-associated protein 52"; /id="PRO_0000317078" MQRASTQDVYDGSGDDLNKLDSLKSVLNDVLSSLERFQVDLDVATSDIYKVSERSNKIQVNLNNLKAVESALGAEIDGAILPPDLIKTISTGDMDHPSWNSALEKLTSFLEGGEDDSSLGNMFNSLQINKDQKKLVDKLRDKAIERIRNYIVVTIKMFRQAFVDVFPIRKHRLIANKNYYLFLFKFNRKLALELQRAYINTMNWFYLYHFEQYSRFLDKVHVLKGETIRVEEDRKGLFNLSKGAQQSYGNQMLSVNLRPQDFDMNSVLTASTMHHIESSPQYIERVYCSWELVLTEHVSSEYAFLLEYFNLSKDQQATVFAAIFEKTLHFSRKYITGLISSSIDCIGILKSIRFTQKLALQAQTNIVPVIEPHYNSMILFLWPRFQAVMDMHCESLRKTNLSVKPEEITSRPHPLSQRVAELLYSLSMLSVNVVEAEPVARSASRLAQDYVSMLQNLCKTVNDKRRQSRFLSNNYTLISTVLSGVSGNLAIEQKTYFEKLNENLTNFQ Q9UST4 IF5A2_SCHPO PTM: Lys-51 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function. {ECO:0000250|UniProtKB:P19211}. MOD_RES 64; /note="Hypusine"; /evidence="ECO:0000250|UniProtKB:P19211" SPBC336.10c; CHAIN 1..169; /note="Eukaryotic translation initiation factor 5A-2"; /id="PRO_0000142486" MGMFIQKEHKPTMAEEEHVDFEGGEAGASLTFPMQCSALRKNGHVVIKGRPCKIVDMSTSKTGKHGHAKVHIVALDIFNGRKYEDMSPSTHNMDVPVVKRDEYQLVNIDDGYLNLMTTDGTTKDDVRLPEGELGNEIEEGFEEGKDLIITVVSAMGEEIALACRDAPSA Q9UST9 HENMT_SCHPO BINDING 61; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 114; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 117; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 118; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 176; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide; Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.386; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; SPBC336.05c; CHAIN 1..378; /note="Small RNA 2'-O-methyltransferase"; /id="PRO_0000343141" MGVSSFYPPLHVQRRRKLFKILQGGFPVRSLLDIGCGDARFLSYLVPCNDQVPIEFLAGIDINEQSIERATEALQVRTEDFLQLRWRPLHIELLLGNIKDFTHYKHVDAVVASEFIEHCQVAEILAFEKLVFGNLKPNVCVVSTPNFEFNTIFEKLSTLTSSISSRTSTNFRHPEHVFEWDRKEFAKWAYKICKRYPEYTVEFTGCGLLNDLIDGDDLLHFRPSSTYGFCTQIAVFHQSKNNAASHCFLKDQNSSILLYKKITYPFMEQLFPPTVQQFMNLLKKAFFDHLFGRHCLLLFQVIAGKCALSVKLPFLFIWESSPLIRHAFHYDDSIYLSYCPELKKSKHKGIALANSFSFRIAKVLKKSRIFIITFHHYV Q9USU2 DIM1_SCHPO BINDING 31; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 33; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 58; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 79; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 107; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"; BINDING 122; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01026" CATALYTIC ACTIVITY: Reaction=adenosine(1779)/adenosine(1780) in 18S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1779)/N(6)-dimethyladenosine(1780) in 18S rRNA + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42780, Rhea:RHEA-COMP:10234, Rhea:RHEA-COMP:10236, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.183; SPBC336.02; CHAIN 1..307; /note="Dimethyladenosine transferase"; /id="PRO_0000101462" MGKIRVRNNNAASDAEVRNTVFKFNKDFGQHILKNPLVAQGIVDKADLKQSDTVLEVGPGTGNLTVRMLEKARKVIAVEMDPRMAAEITKRVQGTPKEKKLQVVLGDVIKTDLPYFDVCVSNTPYQISSPLVFKLLQQRPAPRAAILMFQREFALRLVARPGDPLYCRLSANVQMWAHVKHIMKVGKNNFRPPPLVESSVVRIEPKNPPPPLAFEEWDGLLRIVFLRKNKTIGACFKTSSIIEMVENNYRTWCSQNERMVEEDFDVKSLIDGVLQQCNLQDARASKCGQTEFLSLLHAFHQVGVHFA Q9USU7 YHHB_SCHPO MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 105; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 214; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 215; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 217; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 237; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 271; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 278; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 294; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 297; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 302; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 305; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC28F2.11; CHAIN 1..310; /note="HMG box-containing protein C28F2.11"; /id="PRO_0000311771" MAQNSTQLEKISGSFTRLAEAFQLALTACREIEESLPSILGEKSEVSKPFKPAVTDPSNAKKEINMAIESPSKKATSPKKATPAAVAPVEATSAVDTSEAVASMTPNKRKARDPAQPKRPPSAYNLFQKNQRSEIKESLGEKSNDVKEVNKAMHEKWGSLSEDDRKTYEEEASKLREAYEEEMAAYNASKENASVADSRVTAEETSTKPSEDLSSPTKKDLIDFSETRPLAQASRATPDIKEQHAKKPKRKHTRSTVPTSNVEPVSQPQPSPDKIVSSPNPPSAKREKKKRRKSSMSSSITTPPTAKVAN Q9USU9 TOA1_SCHPO MOD_RES 249; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC28F2.09; CHAIN 1..369; /note="Transcription initiation factor IIA large subunit"; /id="PRO_0000364025" MSNSIVGEVYHHVILDVIANSRSDFEENGVDDATLRELQNLWQSKLVATDVATFPWAQAPVGTFPIGQLFDPVSGLRTDSLDVTAPAVANSPILNNIAAIRAVQQMDTFAQQHGNSNYYSPPTPSLPQSATNISFDSSAIPNVQSNPNNTAPFPSYSSNSLQLPTNQTADSPIINDHSTANVTSTGQEHAPDSSSTNSFGGLLLPNQNSPKKSELGETESSNTTPANSRNDVPQTDGAIHDLDDAGSPSNFESNRFAIAQKADAEIYEVLKKNRILQIDGTIEDNEDEKKPPVDTPSDEAINSDLDDPDSDEAPETEEGSDIGQAIVLCLYDKVNHHKNKWKCVFRDGVVGVNGKDYLFFKANGEFEWI Q9USV0 HRD3_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPBC28F2.08c; CHAIN 21..713; /note="Putative ERAD-associated E3 ubiquitin-protein ligase component"; /id="PRO_0000350745" CARBOHYD 48; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 123; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 211; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 314; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MQLLNFLICLFFIFKRCVFTVIGGEFSYDNIDKKPILVASYPEGSRFNVSASIKTLPDLVTLTFPKLVKDPGYVYEEAEKGDPESQFLIAMLYAMGPDERLGLSFPRNEPLSRIFLELSATQNYTYALLALAYKHLNGLSTPMSVDKGVELYKQVAHQISCLVQPLSHFAPDIAAEYPVDLYDLSRTSSYSVQKKDDIVEYLKDYALRGNNISAHISLATIYQYGTPGKLKDIKLAVKHYLAAIRLVNSGIPDSPSEAIKSIHNNPRHAPTTKETANSLSIAAFRLGCMALHGELGKPDPSLAYAWFEYGVSLNHSSSKAAIAYMYFMGYPVAENTESITKLLENALASNDPLAFAVAGKVSLANGQIDEATVHLIRAVSNGHLESVLHIADIYYGSNNQLSIAYYENFISRVLELFDVKTISFDPLTRHFAHRLSAELGNLMSQILAAKDRDPSTSYLKTVIFPTNEQTHRNARIAMNYYSRAAARNHIHSLIKIGDFYRMGLGTSAKPELAFSYYSQAAAIHPSALAYWRLGWMHEYGVGVPVDFEMAKKNYDNALMHDTRAFLAVTLARLRMRLSSPDSWFSNIYRILGKVTYKFLKLVQYFIINIFDILSPAGPDSQLPPEPPTLQVDRTPQQPDPQETSESLPSPNTEEMGESYNDIRFTYDYIDGRFLETACVTLIVVVVGLVLMRRHQQHRLQERRERIIRRQNRA Q9USV2 YHH5_SCHPO ACT_SITE 47; /note="Proton donor"; /evidence="ECO:0000250" BINDING 110; /ligand="substrate"; /evidence="ECO:0000250" SPBC28F2.05c; CHAIN 1..276; /note="Uncharacterized oxidoreductase C28F2.05"; /id="PRO_0000310313" MKPFSPSQTNFEKEQLCFGVYQLKDCYQQVIEALSLGIRVIDSAITYRNEKECEQAIQDFCHQNVNIKREDITLITKIPDSLQGFERTWKAVEQSLRRTGRPKLDVVLIHSPKWPVRRIESWRALLQHQKEGRINKIGVSNYNIHHLEEIISLGLPLPAINQVEFSAFNNRPTFLSYCFNHGILVQAFSPLTRGYRLSDIRLLDLSLKYNKTPANILLRYCLQKGVSPIFKASSFVHIHENVKAEQFMLDPSDMDVMDTWDEEFVSKPTWNPIILP Q9USV4 MEP33_SCHPO SPBC28F2.02; CHAIN 1..292; /note="mRNA export protein 33"; /id="PRO_0000116773" MPPKKAAKGKGDPGKAAKKDPTKKAADATFGLKNKNRSTKVQAKIRQIEQNAAASGSKDAKRQEALRKRREEEKRAAEAAKAEVAALFNAIPKKQTPQNFLTRKEEVKESQKIDLYSDVRDQQTDLPLEKRPWINTDIVCKFFLEACETGKYGWLWQCPNGNMTCIYKHALPYGYVLSRDKKKDDTKEEISLEAFIEIERHRLGPNLTPVTEENFKKWSDGRRDRILKQAEERRSNRAVGRSNLSGREYFESNKDKTHEVVGDEEDWDFSALRRETEALAKAQDATAPIVSV Q9USW6 DPM2_SCHPO SPBC21B10.11; CHAIN 1..72; /note="Dolichol phosphate-mannose biosynthesis regulatory protein"; /id="PRO_0000220876" MIVYISTAAFLYYTIWVLIMPFVDNMNISQKLFLDREWAITIPVAVMLFGICLIGTFVSLLMIKSSKKKSDL Q9USX4 RL33A_SCHPO SPBC1921.01c; CHAIN 1..108; /note="Large ribosomal subunit protein eL33A"; /id="PRO_0000192805" MPAQGHRLYVKAKHLSFQRSKHVIHPGTSLVKIEGCDSKEEAQFYLGKRICFVYKSNKPVRGSKIRVIWGTVSRPHGNSGVVRARFTHNLPPKTFGASLRVMLYPSNV Q9USX9 ELOC_SCHPO SPBC1861.07; CHAIN 1..97; /note="Elongin-C"; /id="PRO_0000319984" MEKEYVRLISGDGFVFILEKEIACLSGTIRAILNEGIFSEAQKNECTFPDIRATLLEKVCEYLHYNYRYKNQLDIPKFDIPPEMVLELLVTAEYLEA Q9USY2 YOW4_SCHPO SPBC1861.04c; CHAIN 1..1014; /note="Uncharacterized RNA-binding protein C1861.04c"; /id="PRO_0000310819" MSQIQDLKDENVEMDIDPQEQNEKKPLLLDELTKFTILHPYNYDSHIKLIEELKRLDKKKELSEARKTFQSIFPLSEDLWVDYLLDECKNCRTLDDYVRIKTLFDLAVQDYLSIKIWCMYLEFTLNLMDTSSFEQEQSELNGVITLTDAHSLFERAYQTCKFHFSKSQCVWTLYLEFLQTFGDALFEGEEEQEIVFKNKIYDFHIDRLKLPHEQIEETFTSLSTFVTNNWSPSEYEDVMVKSNKVYETTLKRNAKIFNKELLLNSANHSLEAYMDLINDESRRSTAELQYITTLYERAIVLYPLIPELWLQYTAWLSKVDFSSSQASSVAERATRNCSWIGRIWSIKLTYMTLSGASTSAVCEEKDRCLNSNLLVNFDEVIDFFSGFLKACLYLSSNEDKPQEFLKHQIHKVEDYLRKNHKGSKDARMRIELSKIYLYSEISDFESVEKCWSDMFHDFQNQALYWISRYISTMKYNPELAAETLKKSLYKNVDQPQLLFQFYQSIMDLNNDCFTNTSHLYDVLNAQRISFKRQLDSFAEETKQTVENTEPLKVPQADDTAALSKKRKPGQEGDVFKKSKPIEQHRNREELTVLVTNLPSDISENELKIFFKDCGNIIRIFILEDNQKDVKVAQIEFSETSEVLAAKTRDLKSIRGHEISVQIHVDTNLYVTNFPPTYDELDITKLFSAYGNVVDVRFPSLRYNTNRRFCYVQMRKPDEAHNALQLHKKLLEEKYPIQVFISDPLRRTPRSGAVYEGRELYVTNIDFKVNEKDVETFFRDYGQVESVRIPKRFNQHKGFGYVVMTTNQDAENALSAAGKQLGNRVLNVVLSKPRESLEKTRVSSNDNRTLAKSFETTESNKMSTPKKSFEQIKSKSLGVTNVDGTVNEARLRSLFESYGKLYRVVLHPEHEGAVVEFLDIHDAGKASLALEGHEIGGRLLHITTVNEMMHNVPSSMNHSDYNTSATRPRRLGSRTFQGFNSNHSNINSKKDDLDDKEMQIDAPKSNDDFRKMFLK Q9USY3 NAA35_SCHPO SPBC1861.03; STRAND 146..149; /evidence="ECO:0007829|PDB:7L1K"; STRAND 180..182; /evidence="ECO:0007829|PDB:7L1K"; STRAND 226..228; /evidence="ECO:0007829|PDB:7L1K"; STRAND 252..255; /evidence="ECO:0007829|PDB:7L1K"; STRAND 302..304; /evidence="ECO:0007829|PDB:7L1K"; STRAND 372..374; /evidence="ECO:0007829|PDB:7L1K"; STRAND 377..379; /evidence="ECO:0007829|PDB:7L1K"; STRAND 536..538; /evidence="ECO:0007829|PDB:7L1K"; STRAND 603..605; /evidence="ECO:0007829|PDB:7L1K"; STRAND 653..657; /evidence="ECO:0007829|PDB:7L1K" HELIX 66..68; /evidence="ECO:0007829|PDB:7L1K"; HELIX 101..111; /evidence="ECO:0007829|PDB:7L1K"; HELIX 125..127; /evidence="ECO:0007829|PDB:7L1K"; HELIX 130..133; /evidence="ECO:0007829|PDB:7L1K"; HELIX 159..172; /evidence="ECO:0007829|PDB:7L1K"; HELIX 174..177; /evidence="ECO:0007829|PDB:7L1K"; HELIX 203..217; /evidence="ECO:0007829|PDB:7L1K"; HELIX 229..249; /evidence="ECO:0007829|PDB:7L1K"; HELIX 261..271; /evidence="ECO:0007829|PDB:7L1K"; HELIX 275..277; /evidence="ECO:0007829|PDB:7L1K"; HELIX 282..285; /evidence="ECO:0007829|PDB:7L1K"; HELIX 295..298; /evidence="ECO:0007829|PDB:7L1K"; HELIX 313..330; /evidence="ECO:0007829|PDB:7L1K"; HELIX 331..334; /evidence="ECO:0007829|PDB:7L1K"; HELIX 340..348; /evidence="ECO:0007829|PDB:7L1K"; HELIX 349..351; /evidence="ECO:0007829|PDB:7L1K"; HELIX 358..362; /evidence="ECO:0007829|PDB:7L1K"; HELIX 364..369; /evidence="ECO:0007829|PDB:7L1K"; HELIX 381..391; /evidence="ECO:0007829|PDB:7L1K"; HELIX 412..415; /evidence="ECO:0007829|PDB:7L1K"; HELIX 417..436; /evidence="ECO:0007829|PDB:7L1K"; HELIX 442..450; /evidence="ECO:0007829|PDB:7L1K"; HELIX 453..461; /evidence="ECO:0007829|PDB:7L1K"; HELIX 467..469; /evidence="ECO:0007829|PDB:7L1K"; HELIX 482..502; /evidence="ECO:0007829|PDB:7L1K"; HELIX 508..510; /evidence="ECO:0007829|PDB:7L1K"; HELIX 511..532; /evidence="ECO:0007829|PDB:7L1K"; HELIX 543..560; /evidence="ECO:0007829|PDB:7L1K"; HELIX 564..572; /evidence="ECO:0007829|PDB:7L1K"; HELIX 580..582; /evidence="ECO:0007829|PDB:7L1K"; HELIX 585..595; /evidence="ECO:0007829|PDB:7L1K"; HELIX 598..601; /evidence="ECO:0007829|PDB:7L1K"; HELIX 610..621; /evidence="ECO:0007829|PDB:7L1K"; HELIX 625..647; /evidence="ECO:0007829|PDB:7L1K"; HELIX 669..672; /evidence="ECO:0007829|PDB:7L1K"; HELIX 681..686; /evidence="ECO:0007829|PDB:7L1K" TURN 42..47; /evidence="ECO:0007829|PDB:7L1K"; TURN 97..100; /evidence="ECO:0007829|PDB:7L1K"; TURN 112..116; /evidence="ECO:0007829|PDB:7L1K"; TURN 121..124; /evidence="ECO:0007829|PDB:7L1K"; TURN 154..158; /evidence="ECO:0007829|PDB:7L1K"; TURN 184..186; /evidence="ECO:0007829|PDB:7L1K"; TURN 218..223; /evidence="ECO:0007829|PDB:7L1K"; TURN 256..260; /evidence="ECO:0007829|PDB:7L1K"; TURN 287..289; /evidence="ECO:0007829|PDB:7L1K"; TURN 396..398; /evidence="ECO:0007829|PDB:7L1K"; TURN 401..403; /evidence="ECO:0007829|PDB:7L1K"; TURN 437..439; /evidence="ECO:0007829|PDB:7L1K"; TURN 462..466; /evidence="ECO:0007829|PDB:7L1K"; TURN 540..542; /evidence="ECO:0007829|PDB:7L1K"; TURN 673..678; /evidence="ECO:0007829|PDB:7L1K" CHAIN 1..708; /note="N-alpha-acetyltransferase 35, NatC auxiliary subunit"; /id="PRO_0000316239" MSVKESLSLLNSMQGNVKIGNVEPAKGNEGYVDNAGYVDCTKSYFEATKSLKEEQLVCDPKFTLLDSISAFEIMEPKMDSGIDYQPLRVDFSRDLSYLEILALMDLIVSAEKEWHYGSPLSESLLCSAHVFSICKSPISQVGDSGFSSGSGRNTTDIVLFPFVLAVIKCCDIVHREFLMGNLYDEEDISSFSYHMSFLQNYPIEKLNYLLQSSIEYLASEVIKFSAELRQIIEGILNRIQLRIGILRVYERSDIKTTIDALHLIKNLVPEIQNTVSVVDSSIKESILKQYWDFRVQAQLVATAPVRNIPPTGIEHSYQRILYFADDMLLILNSHTLASSLAVYQFCLDFTRLNRTPEPYVRSSLQALITANNAVNLRDQPTSYMLECIREFSGLPSNFYNPNTRTVIEKNSISSAYGPLVESLIAHSTNIMVDLVRICSHNPCRFRRNLINLLPEITVAHFEAEALDLKFVAKSLPSNGPFSSFIYHVKLNAIEHILLSSFEQKLHQPYQWPHFFAVLDHVFSIHQTHLELHGKDRNTPPMAKTFVTYLHRILNAIKETYSGYLLLTVLCMRLNIIKTPSFTLDEKIQESYYMAHYRPLINLRQPKPLLRSEADCIIKNLQNFSTDDLIIKSNEKFTAAKNSLINVIKSGFEQNEFINPYFLQTNYLKNLLCCCITNLVSLAILSKDHSANLKIVEIPGNPLPSLSRT Q9USY4 ABP2_SCHPO MOD_RES 297; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 298; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 302; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1861.02; CHAIN 1..527; /note="ARS-binding protein 2"; /id="PRO_0000064430" MNFYSLLPSRHDVSADNITEKFCQFCLCCNPWYAGADTRQLANAFNMIPKSEGQKFEIWVLFLLVRQYHQKIINSWSKLVGFLGVERKDEQSTQKIQQYVVRLKRWMSQTHVDAFFDYLLNKPNPYYLEIPETQPQVRCNVNVTDDLVIKSLRAGLMSHPDVNSSSISTMRTSTSPSNWIHSASASLDDNTHNLGSFVTNPHADSQECPTPQSLLMRASHHMSERGSQQAHQTTPQNHSLPHPPNMFEPPDEDHQLPSAANNSHNHDHAFQTAEAVGVADSIDPDWHQWPDDLRDVSSPKESDGLNDSWSRQTNQVETENVENEAGVPRKRGRPPGARNKIKRLRSEPSVSLTLSISWYERFEKLMHAQNTMLRSAFSHVARLPMETVSQLLSHYTETISQYLPPSETSPIPKTPNFKFISSTLLALVSSHSEILEASTDRLIWTVHQGPLTATICHAFNLEKAPSMHSLAEAQMIPDVPISHSNSMEPLDTVSSLKLEIAKLNAALKEKNLELENLKRKIMNAVFD Q9USY7 FZO1_SCHPO BINDING 164..169; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q8IWA4"; BINDING 327..330; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q8IWA4"; BINDING 365; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q8IWA4" CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; SPBC1706.03; CHAIN 1..758; /note="Transmembrane GTPase fzo1"; /id="PRO_0000127683" MEKSARQLSVAEQNGESGRLNNGYTSNNIQQYKDETNRHQFEYNQNRNQLLRSIHIIQNLLNELDNYVDRSDCLFHSVWRTDKEKSKFSGNYYPFSPSKMNVITIDLSLRSSSTADEKLISQLGEEAHESLLKVHIEKANKHLFSLFSRVEDTSSKILITGDLNAGKSTLCNALVHKDILPEDQQPCTEVFCEVHDAELNDGKDCVHAIPHGLTYSHTDSSTYKVFPIEDLKRLVYETENWSMLIVYVNDGRPAHESLLHNGITDIALIDAPGLNTDSMKTTSVFACQEEIDVVVFVVNAENHFTLSATDFLRNASTEKSHIFIIVNKFDNIRDKERCKRLILEQIHTLSPGTFADAKDLVHFVSCRVARDPNNREDALYSSFFQMENSLRSFILENRSKSKLAPVRRYLSGLVGDILNICEYNIKLIDFDINHLQQRLTDLSPKFRKVKHEQQFTYQKNESLVEATVQSISQHTHSELEDAIDSLGSFASVKYSGFFFAYQYAISVRDAMQQYLEEKLLESEDYARKRTEEAVLCIQKDVKDNFDSAVLPVFHANQMFIKKHRLQLQKHFRFELGLLDFIDLDLTERLGTWSASLSTILLVLGKTTPSFTTLGAFTGNLGYPIFKYFQNNSLQHLLVPVLGLASICVFGYVIYDIPRALPLKVAEKIKKSLRETDFCHNASIWIGTESRKVLNIPLNDLRRMFHQQWDKQRETISVAENDLRICQKARKFFGEIESRTREAKKKIMMVQLEGCDINY Q9USY8 GEMI8_SCHPO SPBC16H5.15; CHAIN 1..166; /note="Uncharacterized protein C16H5.15"; /id="PRO_0000353136" MSSEITEGDLQKFHDEHFNAKAVNLWNVAFAQNDRGGNSESANVEYTQSVERYPDGTIRTLTDEQILWFRESEKRELMWKKEKEQLLKEKELRQKALDKERMVSSKPETNPKTPISLKELKDIEIYQNQFHYSAYEILEEEKILDNIFRKFTALPIKYWPATPIRG Q9USZ0 WDR6_SCHPO SPBC1306.02; CHAIN 1..984; /note="tRNA (34-2'-O)-methyltransferase regulator trm734"; /id="PRO_0000316567" MLVEGDKGVLEPVNFVGPVTSLALIHNDKFLCCAQGPCLRIYDVSESRHESDLIKSILLPFHNRIHGMLPCKQGLFVWGGTYFAVVDVETSQVYYDRISDWIFNAAELGEENKFCVVTSKNQVHLLSLSKGSWEVTNTISCEKTPLLFCATVQISGNEIYIASASAFQQIYVWKFNYNNPPSCVSIDTYLVGHEGACFDLKFSSDGRYLCSVSEDRTLRLWSIESSPFLIATGFGHSARVWRCVFLPNKEIATVSEDLTLRLWTWNDKTLTNTYTYTGHRGKHIWSLVVSSANPIIYTGGNDGSVRSWDYKTRIQESCISVSSLFTSKTLLASFCFVKCQKLLCLAKNGEMSIIDNKGKKAIPALTTTSDMSIIRSWKNSFFVAAASNKGTIYVFSYQNTNLLKAIDLHRGKIQQLLTYQVKERYFLLSKSFVGKNQFRVYLQEFDFEADKVNLISTIELELPATFDPTSLTVDEEYSNFLIGSRTGSLALYNIGESNYLSVWRRIHEFDAISSIHIKSSKRDYLLIQTVGRDGYVNLFSIPRVEKSAVPQELCSKKCCDGILSGGLCKKLKNGKENQWVWGFHASNFFLRDETNETNVFFIDCGGSHRPWAFSMEMDIQSFASYRANQLYIYSTALNLLQRNSVLQNGLHGREIRAMDFNPSGDLLLSGSEDTKVTLLEFQSNGNIIPLNSVKFHNSGIQSLTWFSDDILFSTGGLEELNVYRLIQKPEAYLKRIVHEKLCKPNKSNKTYDGDLRITDISVVKATHLGERVLWINTVQSDSTIKAFTYNVDTKQLNCIKSWKYKTVCLVFAEAVIFGSHLLLVVASTDGNVAIWNTFWRDPQIEPLIIWIKTVHQFCVKSLNISRDQDVLTISTGGDDGAISRSILLLEQISENSVVVNSLHNYFFAEAHASSVTGVLSITKELLLSVSIDQRILLWKVEGDSLKPILERYTHVADVGGMIRNNDFLIIYGIGCEVFRLGSLR Q9USZ1 EFGM_SCHPO BINDING 66..73; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03061"; BINDING 151..155; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03061"; BINDING 205..208; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|HAMAP-Rule:MF_03061" TRANSIT 1..24; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03061" SPBC1306.01c; CHAIN 25..770; /note="Elongation factor G, mitochondrial"; /id="PRO_0000007448" MLKLSFRSLTSRLPRLSTLVVRGYASVANTGIEASNTSENNLNIQEQLNDNDKKRLKQIRNIGISAHIDSGKTTFTERVLYYTGRIKDIHEVRGKDNVGAKMDFMELEREKGITIQSAATHCTWERTVDQIEANEKQKTDFEKSYNINIIDTPGHIDFTIEVERALRVLDGAVLVLCAVSGVQSQTITVDRQMRRYNVPRISFVNKMDRMGADPWKVIQQINTKLKIPAAAVQIPIGQEDKLEGVVDLIQMRAIYNRGSKGEKIEISQQVPENLIELAKEKRSALIEKLADLDEEIADIYVMEEDPTPEQLMGAIRRTTLARKFTPVLMGSALSNVGVQSVLDAVCDYLPNPSEVENIALNAADSEKPVSLVPSSEKPLVALAFKLEEGRFGQLTYLRIYQGTLKRGNYIYNVNSTKKIKVSRLVRMHSNDMEEIEKVEAGGICALFGIECASGDTFTDGSVSYTMTSMFVPEPVISLSLKPKSKDTTSFSKALNRFQREDPTFRVQLDNESKETIISGMGELHLEVYVERMRREYKVDCETGKPRVAFRETLSKKVPFSYLHKKQSGGAGQYAKVEGYIEYMDGVEDESGNVVDCEFINKVTGGTVPTQYIPACEKAFYEALKKGFLIGHPIKNCRFVLEDGAYHPVDSSELAFRLATISAFRTAFLQANPMVLEPIMNVSITAPVEHQGGVIGNLDKRKATIVDSDTDEDEFTLQAEVPLNSMFSYSSDIRALTKGKGEFSMEFLKYLPAPKYVQKELVDAYNKQQQK Q9USZ4 RPA34_SCHPO MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC11G11.05; CHAIN 1..251; /note="DNA-directed RNA polymerase I subunit rpa34"; /id="PRO_0000337684" MAKSSEFVNEESSEDESSVSSIEDQHSSKEPEQSVESNNHGESNAQEDVAEIAGLEKVQGKPVLTTNDLKKESNVFLVRLPPGMSADQISQLKVGSKPTVELKQENENTYQIREESTSSVRVFLPDEQGSYTSNEIKTGYVITETPKISQNIDTGITIPTQAPLVPQRKNLRQHFRPIGDAVGPESEPEAEPKSGIKEHILQETGDATVEELQNKGKEKQKELKKGKREKKDEEEKPKKKKQKKSSKKEKN Q9USZ5 TRS20_SCHPO SPBC11G11.04; CHAIN 1..136; /note="Transport protein particle 20 kDa subunit"; /id="PRO_0000372419" MTAYAAIIGTKDNPVYELEMGPINEKLDRSLNSHLNQFIVHSSLDIVDQLQWTSNAFYMKTIDQFHEMYISAYVTPSNMRFMLLHQNQSADNIKLFFQELHELYIKTLMSPFYQPNQPIRSQAFDLKVRSIARRYL Q9USZ6 MRT4_SCHPO SPBC11G11.03; STRAND 36..38; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 85..88; /evidence="ECO:0007829|PDB:8ETC"; STRAND 129..133; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 135..137; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 139..141; /evidence="ECO:0007829|PDB:8ETC"; STRAND 170..175; /evidence="ECO:0007829|PDB:8ETC"; STRAND 178..183; /evidence="ECO:0007829|PDB:8ETC"; STRAND 185..188; /evidence="ECO:0007829|PDB:8ETJ"; STRAND 222..224; /evidence="ECO:0007829|PDB:8ETC" HELIX 20..34; /evidence="ECO:0007829|PDB:8ETC"; HELIX 50..58; /evidence="ECO:0007829|PDB:8ETC"; HELIX 72..77; /evidence="ECO:0007829|PDB:8ETC"; HELIX 89..95; /evidence="ECO:0007829|PDB:8ETC"; HELIX 113..118; /evidence="ECO:0007829|PDB:8ETC"; HELIX 162..168; /evidence="ECO:0007829|PDB:8ETC"; HELIX 196..203; /evidence="ECO:0007829|PDB:8ETC" TURN 81..83; /evidence="ECO:0007829|PDB:8ETC"; TURN 144..147; /evidence="ECO:0007829|PDB:8ETC"; TURN 204..206; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..241; /note="Ribosome assembly factor mrt4"; /id="PRO_0000154814" MPKSRRSKVLTLAQTEKKGHEGKAALFSGVQQSLDSFDYMWIFDVTNMRNTYLKRIRDDWKGSRIFMGKTKVMAKALGHTPEEEHAENVSKLTKLLHGAVGLLFTNSKPDEVIGYFESFVQNDFARAGAVAPFTHVIPAGPVYSRAGQIPVEDDILLTHTLEPQVRQLGMPTVLKNGVVTLLADFPLCTEGQQLDSRQTRLLKLFGITAAEFKVGLLGYYSKKGASVEFLQSAPGADEAME Q9USZ7 END3_SCHPO SPBC11G11.02c; CHAIN 1..375; /note="Actin cytoskeleton-regulatory complex protein end3"; /id="PRO_0000349457" MDPQEKNKYWEIFRGLNPENGYLSGSKAAGVLRSSKLSSDKLEKIWDLADIDDDGMFDFDEFAIAMKITFDLINGVYKTVPDRVPEALVSTSKKHLVAARDALRGNDDIALLHKVPSLDTDPEDAVLKDGFDWYISPSDKIRYSDIYSLHCNKHGEVSFNGLAPVFTPFGVPNSQIQKAWKLVNPQGTETIQKDQCLVFLHILTQRSNGFRIPNDVPYSLKASFKRGNIDYNLDSYNSTNNYYSSPTMAPSTGGAKPKSDLDAPRDVRDSDWELISLRNELSKLDEKILSLQRETDDVNIAQNKSKLIQRDLQKVLDYKLGILQSLKNDGPNGPSASAIDNDLKMLEQQLNVLGRHLEGRKSQVAKLEERLRSLS Q9USZ8 FIS1_SCHPO SPBC11G11.01; CHAIN 1..160; /note="Mitochondrial fission 1 protein"; /id="PRO_0000256189" MTEKHTLRLADPSAIDSIISVDEFLQIKEQYDAEQPLITLQTKFNLAWALVRSDSTQHVQQGLSLFCSIYKDSPERRLECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGYIGMVVVAGAVVSVAALVGWASKRLFSKRRP Q9UT00 YKH3_SCHPO BINDING 1053; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1053; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1059; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1107; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1107; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1109; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1109; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"; BINDING 1115; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; MOD_RES 843; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPYUK71.03c; CHAIN 1..1225; /note="Uncharacterized protein PYUK71.03c"; /id="PRO_0000116827" MSSQAEPSKGASNADPNEKVEKMHLPTDTAGGGVKVKVKEQEASPSDKNNLNPQSAGVSEVQVQDDTGARGSGARDLKVPKQMQAPKSSEEKSDVDGVPTRPVSERELRKRDAMQFIQRHQKVRNILAQYCPWLTDERLQLCIELKILFMQHFQDSRLVLYTAVMSFLFGYLRFGFLSLFIIMAVCIQYYRICDRRVKVNFKDDYTRYLSTRKLENDSETVTWLNTFLQQFWYIFEPSLSERITEITDQILSENVPSFIDSMALSEFTLGTKSPRMGFIRSYPKTEEDTVMMDLRLAFSPNDISDLTGREIAACIKPKIALDLKIGKSIASAKMPVLIEDLSFTGNLRVKVKLIDKYPYAKTVGLTFTEKPVFSYILKPLGGDKFGFDIGNIPGLTTFITEQIHNTLGPMMYSPNVYELDIESMMGAAGLNTALGAVEFKLRKGDGFKDGLGGAVDPYVVIKNSADRVIGKSKVAHNTGSPVFNETFYSVLNSFSENLNLEVYDFNDIRSDKLLGSAVLPLATLEAMPVTNDAFVELTLKGKTVGRLNYDMKFHAVVPDSGEEITKVDGPGVLQFTVHQCKELSNDPSKRPTAYAKLIINNKEVYTTRKIKKNNNPSWEESFGTLLPEGKNATLGVQIFTEESEHPFGTANVSLQDLFAATKTGLLWFPLQHAPSGRVRMSVMWKPAQLNNDSISSMALATPIGAIRIHLRSANNLHSKIPGKKCDSYARIMSHNTKQFRTVVIASNVNPFWDEYMYAPVITKHDIFFLQVMNYNSSGEDKLIGQTPINISNFINQGENGALMEYHDPRELTVPLSSTRGIKGNATITFKCDFFPSAVTTSLSPDVTPAPKASSTVATDKVNIEVLPESQKTPTAVDNTSTSRGSTSVKTSKPKKISELLMPSEAVNAALDFESGFMGFDIISYKIAKPAQELAIFLDDLPHHIFLSSALNVTGGATLHEYGNTFIRQLEYSQCTFKLLDGDKEVGSKTMLSRDLISKGATKPLEIAFPDGASILVAFRLTPVPVKLEEVEMYENMGEMTVDVIKATDLPAADSNGKSDPFVVFELQGEEVYRTKTHKRTLNPTFNESFEVELPCKQTCNFVANVFDWDFGNKDDHLGSCVIDCKLLQQQQQTNYEIPLDSKQGVLYLRITLSPKWVLRSKRAGNSSLVEGILGQTASIVGMPLKGISTVGNVAVDGVASVANLTNKMRKGISRGFKGIHHEKAK Q9UT02 SEC7A_SCHPO MOD_RES 40; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 326; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 741; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 742; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4D7.01c; CHAIN 1..1811; /note="Protein transport protein sec71"; /id="PRO_0000120215" MTDLEIETVSRVSSNPDEVKGSSVVEEEPDSESTIKSRVSDEIDEHDSIPEQSNTEKSIEINDKNLEAEKDIESNLSLRPPEDDLDSRSIESEQTGTLSKQTTSTSEAPQDLKIWKNISNASNQNSGKLNPQLFVIEAFKHMSKAKATKRHKKLREAINNVQIELQKQPFLLPEVILEPLVMACQTNSTTLLTITLDCFAKLIDYNYFDSPTLNPSDITLMERVVNTIASCFCGESTPERVQLQIVKALLAAITSERTIIRHSFLLTAVRQTYNIFLLCKDSTTQAIAQVALLQMVDSVFQRLSTVLNHEREFSTINMNKSSSNGTPDRANSPIPSQLSENKLTLESFEHRKSFDQVREEAPLEEDSLEQQLLRDAFLLIRALCKLSIKNIPYEHEYDLKSQSMRSKLMSLHLIYHILRTYMNILSDINVKIRSPTSTPTPLIDAVKQYICLALAKNVVSHVLPVFEISCEIFWLILSELKNFFKSELEVFFTEIFFPILEMRTSSNQQKIVLLNIFHRMCEEPQTLIELYLNYDCISGNTENIYERAIVTLSRIASQSTSDPPPSFVFRDDQLVIDKPGFVYHTLNDIPQLNSSTIGSYVHSHNPPYFDYQIRLKSYRCLISTLSSLFTWCNQTFAPTVEITAKDDETESTSKGEEPQKSKSEPPSAGINSTSMDNLESSGQALATDDPSQFENLKHRKKQLQEAIQKFNYKPKEGIKILLSSHFIASKTPTDIAKFLISTEGLDKAVLGEYLGEGNDENIAIMHSFVDHMSFNDIPFVNALRSFLQKFRLPGEAQKIDRFMLKFAEKYIDDNLGVFKNADTAYILAYSIIMLNTDLHSPQVKNRMTCQDFIKNNRGVDDGANLSDSFLTEVYEEIQKNEIVLKDEQDPTSNFPEIPGTSNLSFAANISNALATVGRDLQREAYYMASNKMANKTEALFKDLIREQRERGKLSGNDIYYTARHFEHVCPMFEAVWMPILAAFSEPLQLSSDPALIQLSLDGFRLAMNVIFFFSMDLPRNAFMQTLTKFTHLNNTSELKWTNMHALKTLLEISLAHGDKLRDSWKDVLLCISQLERVQLISAGVDINSLPDVSTTKPLRKSLDKNIRQSRSGSISLKHSKSFQSASTHSTKSSSVEIVREYSSREVVMAVDMLFSNTRNLGSEGIYDFVKALIEVSWEEIECSLELSNPRLFSLQKLVEISYYNMRRIRMEWSSIWSLLGTYFTQVSCHENSIIASFALDSLRQFSMQFLEIEELSHFKFQKDFLQPFSHAMENSQDLKIKDLVLRCIDQMIKARYQNIRSGWRTIFHILAYASKIENLLVLQCAISVVSSLGHEHISCVLTQGAYIDLISCITKFAKLNGNQKFCLSCVDMLKNLEHELIKHLKHMKKESVYSKKLEEEYWLPFLLSFNEIICEASDLEVRSKALKVLFDCLYRHADDFDEEFWETVSNKALLSIFSILSITNSQRLYLAKNTEETEVWMLTTMVEALKAFIELIKNLFERLHFLLPKALNLLEKCICQENSMISKVGLSCFSQFVLKNKNQFKDVDWDEIINSINQLLQMTLPIELRDPSLYPQVNSDSSLEDVKENSFRPHEISRFNSQSVFKSKKHHLKSIVVKCTLQLLMLNCLWELFHSDNMLTNIPKRKMVKLLDILKQSWEFAESFNSDFEIRAKILSSGIVEHMPNLLSQEALCAKLYFYTAFECMSSLKSDSHDTEEYNDLMDVFQKKIYLASQLVLHGFQRVIGDNPVKGVAAFQPVIAALVSYINSLDEIQFSRGKSEFYQLLCAIVACGHIDQQLGTSLSNAFLRYAC Q9UT05 TPP2_SCHPO ACT_SITE 101; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 326; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 512; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240" CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide.; EC=3.4.14.10; Evidence={ECO:0000269|PubMed:9740805}; MOD_RES 606; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAP8A3.12c; CHAIN 1..1274; /note="Tripeptidyl-peptidase 2 homolog"; /id="PRO_0000310393" MKFRLNANFNFSFRRYCFVQCRNKYHSHVRYLSSAKKSGILRNSYNQRTERYFTNIMIPSDYSNKFYPVDGVVPKHETQAYEFLKKFPEYDGRGVTVGILDTGVDPGAPGLSVTTTGLPKFKNIVDCTGAGDVDTSVEVAAADSNDYLTITGRSGRTLKLSKEWKNPSKKWKVGCKLAYEFFPKDLRKRLQKLETEDMNKSNRKLLQDATDEYAKFKDKFPEAPLDKDNLQTQKELEARIECLKQLAEKFDNPGPLYDVVVFHDGEHWRVVIDSDQTGDIYLHKPLADFNVAQEWSTFGSLDLLSYGVHVYDNGNITSIVAVSGTHGTHVAGIIGANHPETPELNGAAPGCQLVSLMIGDGRLDSLETSHAFSRACSEIIKNEVDIINISFGEDAGIPNKGRVIELLRDELAGKRNVVIVSSAGNNGPAYTTVGAPGGTTFDVISVGAYVTSGMMQAQYNLLSTVHDTPYTWCSRGPTLDGDTGVSIYAPGGAITSVPPYSLQNSQLMNGTSMSSPSACGGISLILSALKAQKKPYTAAAIKKAVMYTSKDLRDDFNTGMLQVDNAYEYLAQSDFQYTGARSFTINGNIGNSKRGVYLRNPTEVCSPSRHMFNVAPKFEDGEEYEKSHFEVQLSLATTQPWIQAPEYVMMAGTGRGIPVRVDPTALAPGHHFGKVLAYDASNESRRCVFEIPVTVMKPSSISNTCFSLRDVSFEPTLIKRHFLVPPKGATYVEIRVKATSELESTNMLWISVNQTIPQTKLNEASTELIMPVTQNEVTTKLVSIDDSYTLELCMAQWWSSLEPMVLDIDVNFHGIKVVNGKEINLISSQGLKRVDCASIRRENFKPDITLKDYVDSFKPTNTVIKPLGDRDIMPDGQQLFELMATYSVEISEKTELKADFAVPHNMYDNGFNGLFFMVFDSQKQRVHYGDMYTSSHTLEKGEYLYKFQLLSVDPSTLERFRNVTLRLTKKLKKPITLPLYADHIDFCDNKTYERENIDAGVVESFVVGTNIEGEQYASELKENSLLTGELKFGDCEKGTVPVTLVLPPKISTKEDTKLGEKCANIVQLQVDLLSKLADQEKEKHLKYLQSSYKNSLEVQLAKLDIVKETNERLSTADSILSLIDTEALSRYYSCQQKVEDTIPRDVVLEKKMALQRDAFIRALVVKCETFSTQGHKDKDNYFQNYQLLLNWLENSDPRVWQIKKDYYKSQNQYGLALKALLELLKENGNSGKMDVAKLLSEEKELLVNLGWNYWHDIVFVETVKRVPPYSYALF Q9UT06 YLWB_SCHPO BINDING 243..250; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 295..299; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 364..367; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAP8A3.11c; CHAIN ?..419; /note="Uncharacterized GTP-binding protein P8A3.11c, mitochondrial"; /id="PRO_0000316233" MLSLRTSISRIQPCLFIRASSYQTEATQPKFQDKIRIRIQGGDGGQGCSSFIKEKFRPYGPPDGGNGGDGGSVYVAVKPGSFNNLSHLSQIHKASNGTNGKGGNRHGSCGKSVILYVPPGTVIREISAVRSEQSLEWVQMPGKTKPPKLKKGQISFVSEATRHGKELLYYRASSMISGAAEYSLEECDTTPQILCYGGVGGLGNVHFLSENNRSPKFATKGLTGEQKLIELELKTICEIGLVGLPNAGKSTLLNCLTASKSKVGEYEFTTIYPKIGTIKTTMPDDHSSFQYRLADIPGIIKGASDGKGLGYDFLRHVERAKMLCLVIDINPKAKIPADQAFQLLWDELNKYEKNLINKVALVIANKADTAAEQDLLLLKAIVERTTKGVAVLPVSAKKQEGLEGLVRGMTQLLQQRLLV Q9UT07 UPS1_SCHPO SPAP8A3.10; CHAIN 1..171; /note="Protein ups1 homolog"; /id="PRO_0000271268" MTAICTDKTELNASWNTVSSAWLTRYPNPYSLHVVSADVLERYVDDEGRLYTERLLVKQGRLPRWASDLLNVNKSYILERSVIDPSKQELKSETFNLDHVKILRVIEYSRFIQSSENCSKTIVDTIAKFVSPLRFGLGRRVQKYSLKRFQEQLSSSRRGLLYVIQQKFQPS Q9UT09 AROG_SCHPO CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; SPAP8A3.07c; CHAIN 1..372; /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited"; /id="PRO_0000314763" MSPVFLPSGETYDQEHLDDNRVLGYNPLVPAALVQQEIPVSETSRKVITDSRKEIQAILNKQDDRIIVVVGPCSIHDPKLAMDYAKLLKPKADELQDALCVVMRCYLEKPRTTIGWKGLVNDPNLDGSFAINKGIRMARQMYCDVTNFGIPLASEMLDNISPQFFADLLSFGAIGARTTESQLHRELASALSFPVGFKNGTDGTVGVAIDAIGATAHPHTMLGVTKQGLAAITMTRGNKDTFIILRGGKKGPNYDAEHVAAVRKDLEKANLPPRIMIDCSHGNSSKNHLNQPKVSKSIAEQIRNGDSSIVGVMIESHINEGRQDAPIRPGVKDTLKYGVSITDACVSWEQTAPMLDDLAEAVRARRQNQKSN Q9UT10 YLW5_SCHPO BINDING 287..294; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 357..361; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 417..420; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" SPAP8A3.05; CHAIN 1..695; /note="Uncharacterized GTP-binding protein P8A3.05"; /id="PRO_0000363371" MSRLSQLLNSKKAKQKPPSEHPIGLSSILKQDSSSSSDSPNFFPSSSTNDHQERDTINDTNFVVPEKQKTSKLALLAAERKKLHSSFPSTQQQPPKTEKEKEKEPIQAKHKKNVENDFLLQRFRKVRIAEKKDSEQPSSHEIHLTDDDDKTTLQKQMVESDQLKKNPQEVKLAPPSSFAKCLTGAKKRVFEDQIEIHLSKSSLLGFNAPSPDDIVLMAQSKSKSFQKHKRLDEQLLNSVKSMKKVSQQLKPQKNTNDSNNDHTLLSQDQLIELSKLVKPRTKLLLLGPPKSGKKTLLSRLFFQIGSFDPKTMQKCTVLNAKKESLSSVLKSTKTKWYDFETFSNSYSSTIIDFPLGIFTTNASSRDNFLKHSSLFQVMNTAIFTIDCLNPLEGLDGISSILQLMNGLSISSYMFAITKMDEIEWDENKFINLVNSIQSFLKESCGIIEKSKFIPISGLKGTNLTSISQEKLSQWYKSDTLLGKIDKEADTNHGTWNFLLNLPLSLTISHITPLPENQSHIYCSIHSGMLQDSQKLYVGTGRLETQITGLSSDENPKGFNVAGDMIQAKIPTLPNLCPGILIADSIDAFTSSKTAYVNATWFHGSLEKGKSMHVIALFGCHAVLTKLYCFTDSQEKAPNAIGNDLERNRTSLVKIELENAFPLVKESYINTLSRVLFVSEKWNSLIAFGTVLSLHD Q9UT27 PVG1_SCHPO SIGNAL 1..30; /evidence="ECO:0000255" SPAC8F11.10c; STRAND 92..97; /evidence="ECO:0007829|PDB:5AX7"; STRAND 123..130; /evidence="ECO:0007829|PDB:5AX7"; STRAND 151..155; /evidence="ECO:0007829|PDB:5AX7"; STRAND 158..162; /evidence="ECO:0007829|PDB:5AX7"; STRAND 181..186; /evidence="ECO:0007829|PDB:5AX7"; STRAND 188..192; /evidence="ECO:0007829|PDB:5AX7"; STRAND 212..218; /evidence="ECO:0007829|PDB:5AX7"; STRAND 235..237; /evidence="ECO:0007829|PDB:5AX7"; STRAND 260..265; /evidence="ECO:0007829|PDB:5AX7"; STRAND 297..299; /evidence="ECO:0007829|PDB:5AX7"; STRAND 330..335; /evidence="ECO:0007829|PDB:5AX7"; STRAND 351..354; /evidence="ECO:0007829|PDB:5AX7"; STRAND 379..384; /evidence="ECO:0007829|PDB:5AX7" HELIX 62..86; /evidence="ECO:0007829|PDB:5AX7"; HELIX 104..119; /evidence="ECO:0007829|PDB:5AX7"; HELIX 136..144; /evidence="ECO:0007829|PDB:5AX7"; HELIX 148..150; /evidence="ECO:0007829|PDB:5AX7"; HELIX 166..178; /evidence="ECO:0007829|PDB:5AX7"; HELIX 196..208; /evidence="ECO:0007829|PDB:5AX7"; HELIX 219..229; /evidence="ECO:0007829|PDB:5AX7"; HELIX 241..245; /evidence="ECO:0007829|PDB:5AX7"; HELIX 249..254; /evidence="ECO:0007829|PDB:5AX7"; HELIX 303..306; /evidence="ECO:0007829|PDB:5AX7"; HELIX 312..328; /evidence="ECO:0007829|PDB:5AX7"; HELIX 338..347; /evidence="ECO:0007829|PDB:5AX7"; HELIX 363..369; /evidence="ECO:0007829|PDB:5AX7"; HELIX 371..373; /evidence="ECO:0007829|PDB:5AX7"; HELIX 385..398; /evidence="ECO:0007829|PDB:5AX7" TURN 87..89; /evidence="ECO:0007829|PDB:5AX7"; TURN 131..133; /evidence="ECO:0007829|PDB:5AX7"; TURN 230..232; /evidence="ECO:0007829|PDB:5AX7"; TURN 359..362; /evidence="ECO:0007829|PDB:5AX7"; TURN 376..378; /evidence="ECO:0007829|PDB:5AX7" CHAIN 31..401; /note="Pyruvyl transferase 1"; /id="PRO_0000029851" MFANINIRKSVWLFLLAAVSCTLFIYGVTRTDLQTLKNPSSLTSPSSSTSVDKKKPLFTKSPRNSASCESTITLQSNLLFTYYKHYFAGIKKVALIGFPDHPNKGDSAIYVAEKKLLDALNIEVVYITAQEADYSASELKSIISDIPRDEFALAFHGGGNFGDLYPDHQHLRELVVRDFPSFTTISFPQSVWYNEQQLLEQASILYAENPNITLVTRDRQSYGFAVDAFGKHNEVLLTPDIVFFMGPIPEIREATPITHDVLILARLDHEGGQQHGAEDYYRDTLNAANLTYSVEDWLLWDPPVAQNPDSSFDDRGQARYEAGAEFLASARVVITDRLHAHILSTLMGIPHIVVENSQMGKITNYHNTWLHGCTLDGVSVVVDSVDKALSLLLEWNEAGYF Q9UT28 EFM7_SCHPO BINDING 58; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03223"; BINDING 84..86; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03223"; BINDING 106; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03223"; BINDING 137; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03223"; BINDING 162; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03223" SPAC8F11.09c; CHAIN 1..255; /note="Protein N-terminal and lysine N-methyltransferase efm7"; /id="PRO_0000096899" MADNDFEGFGIFEEPEGFRPSTPPPKEVLHTRVIVPNGPEEIKLRLVGSHSLWAHYLWNSGIELANYIDKNPDTVRAKKVLELGAGAGLPSIVSAFDGAKFVVSTDYPDPALIDNLEHNVKQYAEIASKISAVGYLWGSNIKEVMSNAGFKDNEVFDILLLSDLVFNHTEHSKLIKSCKMAIEGNPNAVVYVFFTHHRPHLAKKDMIFFDIAQSEGFQIEKILEEKRTPMFEEDPGAPEIRATVHGYKMTIPIPV Q9UT32 RL1DB_SCHPO SPAC8F11.04; STRAND 52..61; /evidence="ECO:0007829|PDB:8EUY"; STRAND 72..75; /evidence="ECO:0007829|PDB:8EUY"; STRAND 87..91; /evidence="ECO:0007829|PDB:8EUY"; STRAND 111..116; /evidence="ECO:0007829|PDB:8EUY"; STRAND 138..144; /evidence="ECO:0007829|PDB:8EUY"; STRAND 166..168; /evidence="ECO:0007829|PDB:8EUY"; STRAND 188..191; /evidence="ECO:0007829|PDB:8EUY"; STRAND 195..205; /evidence="ECO:0007829|PDB:8EUY"; STRAND 236..242; /evidence="ECO:0007829|PDB:8EUY"; STRAND 244..246; /evidence="ECO:0007829|PDB:8EUY"; STRAND 249..253; /evidence="ECO:0007829|PDB:8EUY" HELIX 15..26; /evidence="ECO:0007829|PDB:8EUY"; HELIX 43..45; /evidence="ECO:0007829|PDB:8EUP"; HELIX 95..105; /evidence="ECO:0007829|PDB:8EUY"; HELIX 107..109; /evidence="ECO:0007829|PDB:8EUY"; HELIX 117..123; /evidence="ECO:0007829|PDB:8EUY"; HELIX 127..135; /evidence="ECO:0007829|PDB:8EUY"; HELIX 155..159; /evidence="ECO:0007829|PDB:8EUY"; HELIX 175..186; /evidence="ECO:0007829|PDB:8EUY"; HELIX 210..227; /evidence="ECO:0007829|PDB:8EUY"; HELIX 257..264; /evidence="ECO:0007829|PDB:8EV3" TURN 6..8; /evidence="ECO:0007829|PDB:8EUY"; TURN 145..154; /evidence="ECO:0007829|PDB:8EUY"; TURN 160..162; /evidence="ECO:0007829|PDB:8EUY"; TURN 230..235; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..373; /note="Putative ribosome biogenesis protein C8F11.04"; /id="PRO_0000353842" MALKELLGSDAPLEKVCSALLEYESKRKSSENIDSESKKTNLLEDEQDDIEPVWLQLATLKFIGNNRKLIPYKIAIKNPVIPSSSEACLIVKDPQRVYKDLVNEAGLSKVVTRVIGLSKLKAKWNSYEQKRQLRDQFDIFLADDRVIPMLPRILGKTFYQKSKVPVPVKISKGTAEQLKREVVSAYGATYFNSAPCSSFMIKCGHVSNTSTELAENVESILQFVSKHIVPDGAKGIASIHLKTSQSIAIPLWNNPNLKELIASSRKVVTKETASSKRKSDEESLPSQKKQKKVEVAKESKDSKQQNVSDKKQVTVKEVPKKLSVKNAAKTTNRDEDSKGKKAKASPKVSQSSLKANGTTAIKKVKAGKNKVKH Q9UT34 YIQ9_SCHPO SPAC824.09c; CHAIN 1..320; /note="Uncharacterized protein C824.09c"; /id="PRO_0000318103" MINSKSKKKESNALVLKSLLREPYNKVCADCKRNEQPRWASWNLGVFICIRCSGVHRSLGVHVSRVKSVDLDSWTDEQTENMTRWGNERANLYWEAKLAGGHVPSDSKIATFIKTKYEFKKWVLYPEIPSPETLKPEQNTRPVSEVNASLDLNTASRSSSAHSVKSTSSATVTNVTSKKEAISATTSLAQSSPNLASLSKQPSTVHAPSTRQRDLKSSILSLYASPRPQVSSSSITTNATYQNLPSPVSTSTTSSQPYGAFHQPATTGSSFVADKWKMPMFTSNVTSAQPSARASPVQSNSSRPRSSLDSKIINSHDVWK Q9UT36 GLO21_SCHPO BINDING 63; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 65; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 67; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 118; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 139; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 139; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 148; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 178..180; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 178; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q16775"; BINDING 250..253; /ligand="substrate"; /evidence="ECO:0000250|UniProtKB:Q16775" CATALYTIC ACTIVITY: Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925, ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6; Evidence={ECO:0000250|UniProtKB:Q05584}; CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione + H(+); Xref=Rhea:RHEA:25245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=3.1.2.6; Evidence={ECO:0000250|UniProtKB:Q05584}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q16775}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775}; SPAC824.07; CHAIN 1..256; /note="Probable hydroxyacylglutathione hydrolase glo2"; /id="PRO_0000337689" MSFHITPIWMWKGTGNNYAYLLTCDKTKITAIVDPAEPESVIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKNASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVSSPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVLAALPDDTVTYPGHEYTKSNAKFSSTIFSTPELTKLVDFCKNHESTTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMKKLRDMKNAA Q9UT37 TIM14_SCHPO SPAC824.06; CHAIN 1..140; /note="Mitochondrial import inner membrane translocase subunit tim14"; /id="PRO_0000071116" MSSAILLGVGIAATAAAGKIGVDAFRKYRNLNGGVKAFLKGGFESKMSRAEAIQILSLNNRTLTRQKIKEAHRRLMLANHPDRGGSPYVASKVNEAKSLLDADRSIRKFSSWALPVSKQRSMPSVLEAVKWLEYSSIPKA Q9UT38 VPS16_SCHPO SPAC824.05; CHAIN 1..835; /note="Probable vacuolar protein sorting-associated protein 16 homolog"; /id="PRO_0000065890" MEPSIKYPIYEWELLQDTYYQKSAIGKAEWEYIDPVDFMFAVAPCGGAIAITRSESNLQSNYKYDQVPMYSICVFCLSGQLLQTLTWDKTSLVGMGWNENEELIVVSKQGQVRVYNLLGEFHQFSLGKGVENIGIRECQFSEGGVFALLQNDTFISITGFEEPWRKTYASIPFNTLEYYNIDSWALIPNPFSPDLGMDIVVTVGPHILQIDEQDSQLHSISSLQHVSHISISPNARYLALYESVGKVRVISSDFSKELLDLRLPETVAEASLKQMAWCGNDAVVLVHENLLTLVGPFGGSVPYLYNHTPIVSTEVDGVRILTKDSSEFLRKVPAPLENIFHIGSKTPGAKLVEAFQKMKLKSVFAEKMLLELKDELHDAVDTCVQASLNEFSIEWQKVLLEAASLGKNSLRMYNHQEYVDVCRELRVLNAARDPNVGIYITHEEYLHLGLERLIQRFSCRQLYGLAVQASMWMQIPCDWVYIQWAQTYIKQSSEPEEVVLDNIVKRLSSRKYISYEKIARTAYQEGRLILSTKLLDFEPLAKHQVMLLLNMEAYEQALKKVIETMDNNLIIYVVLQIKQQMAIASFFQILNEYPDAVKVYVEFAKKNDRKTLHDFFYQDDNKQGIAVLAVEDTLKTATVNQRITSLKSAAKVCSESKELSLEEKCLGDEIKLLQLQQTYEDQFTGNFVGLTVNEVVVKLIQINQTQRANKLRSDFQIPEKRFAWLKLRALVAIRDWVQIEQWAGSMRRSPIGFEPFVTEILSAGNKKEAAKYIPRCTQLTTQEKVDMWVQVGDVKSASEEAAKSKSGSVLGDLLERVQTMPESRFVQNALDQLRR Q9UT39 YIQ4_SCHPO SPAC824.04; CHAIN 1..341; /note="Uncharacterized WD repeat-containing protein C824.04"; /id="PRO_0000316562" MDIGILSSLKPAQSFRDNSLGSFINSIDYSDSGEYVATTCSADDTVQIYDALDPKQVHTITCFETGIEVARFTHHDHNLLLSTTKGNKDIQYVSIYDNKRISYFSGHTDIVSSIEVSPIEDQFVSTANDKTLKLWKMNQSSRCLGNLDLPSLGIPAYDPTGLVFAVACHSLSRIFLYDVRNYGSDPFSTFTIDDSRYLSRFSFPPMMPEWKHMEFSNDGKCILLSTRANVHYILDAFSGDVLSRLEDFQELPFSNNFHGGSTTFVPQGNFVIGSADDRTLNVWNLRHTFHHKGKTRPPEHRIVSQSIINPGLVKYNPRYDQLLTAGSQLVFWLPEKYALTS Q9UT41 BST1_SCHPO ACT_SITE 264; /evidence="ECO:0000250" SPAC824.02; CHAIN 1..1142; /note="GPI inositol-deacylase"; /id="PRO_0000277642" CARBOHYD 596; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 679; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1002; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1028; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1119; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKDDKGRSDTVNGYYISNSKLSSGFYKRNNANTASNDEKPNLEQNDIPSVTSSGSSTPSSISIEKEIKISKGNVIVKAIRSWSLYVAIIAILLLLVILHSFQGRPQDNGCGKSYVWPSYVRFVDFDERYTRFANKYSLYLYREKSVEESDEPSGIPILFIPGNAGSYKQVRAFAAQAAHVYANAYAEDADGTLNAGKLVPDFFVVDFNEDFSAFHGQTLLDQAEYVNDAIPYILSLYRQNRKISSEYDNEAFPPPTSVILLGHSMGGIVAQATFTMKNYVDGSVNTLITLATPHAMAPLPFDRHLVEFYESIKNFWSQSFLLSPEENSLDDVLLVSIAGGGLDTHVVPEYSSISTFVPPSNGLMVFTSGIPSVWAEIDHQAMAWCENFRRVLIRGIFAIMDARTSKCTVSLNLRKELLSRAYIQGSSFQNDITQISKPIAQYKALDLDLTYVYSEMPGQLLFLNQLGVSYIRHHIFPIPKPTSSIDRFELLTDQPIDLSSSNIKVLACRLDPKIDNTISALLENGNNKVINANCHLLRELVTLLPASTAYTSSPYGGDSFYNYVLPKEKMDDYHFILVSDDSKAPASGFVVGGFSNVSLDPKTIKGSQIELFKSGRKFQFDTKGSISKRFRFPGIQSSIMAYTISVTYELYPGAVPQKEFTPMLKQSIESPFETKYHVNMSNTELSVHGISPFMEFFGKESEKSLTLEFFLNPAIYKSVYVSIQPSYYRSAGRLLMRYRTLLASFPVVVISLAAYNQFRYFHYGSAYLSMSAALEVMIRKGLIKLLFLVSILSIAFSYLISRVELIVADGADPVASWKIFAMMVPKSFWKQNHLLFGLQTAQFWFLAPLLTLMFVGLVITASVIILCVMHLLAFIYGIYLRYKGLTFTGVCQAVKFSFQCLRTRNTRKLDHGEFKKLSSFLSQRNMYYANPSLCYVYGKKHMQARIIGIMLLLLMAMTVVPFQLVYGVALCTQTVTTAKALHLARFCTKSSHYRKKLWDFYNFSCTITILMLLLAPLDFPVLIVWARNLSMHWSIPFPTHHNFFSIIPFILLTEILRTGKMLPRLNDVEYYINNVFLFLLSFYSLIYGAEKPYLIHNVVGLYFFWLLFLYAKNGFFVQNISKWPIIPRMKYFIKHKFLRSIS Q9UT44 PROA_SCHPO CATALYTIC ACTIVITY: Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41; SPAC821.11; CHAIN 1..451; /note="Probable gamma-glutamyl phosphate reductase"; /id="PRO_0000189823" MSLEENVKEAKNAFNILQTLSVEDRDDALDKIVEELRIKKSEVLAANAEDMKAAKLLAESGKLSSSMVKRLDLSSSDKYDSMVQGVLDVKSLPDPLGRVTYARSLDDGLDLYKVSCPVGLLLVIFEARPEVIINITSLAIKSGNAVVLKGGTESAKSFAALSNVVRSALGKSKVPQAAVQLVQSREEVSQLLKLDEYIDLVIPRGSTNLVRHIKDNTKIPVLGHAAGLCSMYVHEDADMELASKLVLDGKTDYPAACNAIETLLINEAVLSSHLPKIAETLTEAKVTLKCDPASLKVLKDMPKVSALVEPSVDQDYNTEFSDLILAIKTVPSLQSAMQHINTHGSKHTDCIITSSEAAANRFMAGIDASGVYWNASTRFADGFRYGYGTEVGISTNKIHARGPMGLDGLTIYKYQLRGNGQVASSYGVGPGKRAFKHTPINIDNISQVSKK Q9UT51 CSN3_SCHPO SPAC222.16c; CHAIN 1..338; /note="COP9 signalosome complex subunit 3"; /id="PRO_0000120986" MVANMEFQGTLPFHPLEDPETLLLKFTDFVHQHSVEQCNQLSMYIIASVNSLAEAFYGSHPEKYNIVFQSVEYAAHSPAISVMHVCYLKELLRQGQYATSLKSFNDLEVSKHIPGSILLQYCMYAAYHCLGNNDLDSAKVWYFSILYIPTTTLTSFHEEAYYSFLLLYIITTGKKFQLDSATSSNVLPLKRHMVPYEEFLDAYLKDVNTLRTVIKEHWSRFLKDNSTAFILFALEVYPMHRLKKWRKTFSSLKLEYIAKQLAISQDVAKEIIQKFDNKTNFTVANGEIFLTFNALDDVSPEMHSDLCQQLIEASKNFEASIRLKSVIYSKIMAKKLNA Q9UT56 RS26A_SCHPO SPAC806.03c; CHAIN 1..120; /note="Small ribosomal subunit protein eS26A"; /id="PRO_0000204526" MTQKRRNCGRNKHGRGHTKFVRCINCSRAVPKDKAIKRWNIRNMVETAAIRDLSEASVYSEYAIPKIYVKLQYCVSCAIHARVVRVRSREGRRIRTPPPRVRYNRDGKRVNPAAIAKTAL Q9UT57 CFD1_SCHPO BINDING 13..20; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 201; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250"; BINDING 204; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000250" COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-SPAC806.02c heterotetramer. {ECO:0000250}; SPAC806.02c; CHAIN 1..608; /note="Probable cytosolic Fe-S cluster assembly factor SPAC806.02c"; /id="PRO_0000278883" MDKVQHVILVLSGKGGVGKSSVTTQLALSLHDSKVYSRPLKTGILDIDLTGPSIPRMFGKDAERNRIHQSSAGWVPVYTDETKEIGLMSLGFLLTSKNDSVVWRGPKKAAMIRQFISDVSWGELDFLIIDTPPGTGDEHLTIVESLLSETSTVRDVPIDGAVIVTTPQGIATLDVQKEIDFCKKASIKILGIVENMSGYICPHCADCTNIFSSGGGLTLSEKYKLPFLGSVPIDPKFGEMIENLTPDSNIVHLYSKTEMSKKFSFITNEFLNQLYGPRKLDTITTISGHTGRLWSVAAHPMLPLFATSSQDKSVRIYNSNTYNLVHVIDGFHTRSIRRVAWRPIERPVLAVASFDSVVSINEKIDDDWECTAALEGHENEVKCIAWSCNGNYLATCSRDKSVWIWEATEDDEFDCLAVLQEHTQDVKVVTWHPTEDLLVSGSYDNSICFWRDDGDDWALTCQLQGHTNTVWALAFSPNGNTLASADNDGNVFLWIKISSNEDVATIDSTNILRPALQEEWKQQTSLPHIHKGAVYTISWMNDATLCSAGGDGKIVVYQREKHDEALWHVAYEQDHAHGVYEINSLEYLRDDRLLSGGDDGECRVWSFK Q9UT60 XDH_SCHPO CATALYTIC ACTIVITY: Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867, ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.179; Evidence={ECO:0000250|UniProtKB:A0A024SMV2}; SPAC513.06c; CHAIN 1..368; /note="Probable D-xylose 1-dehydrogenase (NADP(+))"; /id="PRO_0000316231" MTSMSGASPVIHWGFLGAGSIAAVFAKDLVGVPERHKVQHEIVAVATRDSEHRASSFAKNHCAPCKPKAYGSYEELVKDDKVDIVYISSTHPQHYEVVKLALLNDKAVLCEKPLTINYPEALELVELARARNLFFAEGFWIRFYPIVKAAKTLLHEDRVCGDHFRLFVDFSQDFRFRELPSESRLRTVSLGAGVLLDMGVYPLTWSRLLLYDDPKNEKQEPTVSSNALTFEDHNGDIGDYTTAVTLVFPKTESIAMLCTSMDRGKMSDDFLKLDGENGNQLFISGDCYRPQSIKLIRASGETEVFDFSFDDATGFFYEQDAVAECLLKNMKEAPEIPHEETLKMMQLTDQIRRQINVTYPADLRYTTA Q9UT70 BET5_SCHPO SPAC3G9.16c; CHAIN 1..155; /note="Transport protein particle subunit bet5"; /id="PRO_0000211564" MTIYAFYIYSRKCECVFAHRWKPSDRNSMETLVSQLEQNSIEDDMEKLIFGVVFSLRNMVKKITADQDQFMSYTTSKYKLHFYETPTNLRLIFITNPKIDSLTHVLQQIYTTLYVEFVVKHPLYTHVPPSAEEGGINCEIFRITLDRFVRTLSCF Q9UT75 MOD5_SCHPO BINDING 10..17; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 12..17; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, ChEBI:CHEBI:74415; EC=2.5.1.75; SPAC343.15; CHAIN 1..434; /note="tRNA dimethylallyltransferase"; /id="PRO_0000316242" MLKPLCVVIGTTGAGKSDLAVQLAKRFGSQVINADSMQIYRGFDTITNKITVEEQENVHHRLMSFLNFDKEYSVPEFERDASRVIDEIHSQGKIPIVVGGTHYYLQSLLFEDTTLSAIDKLTNDSSPSKPPHPDSHILDDDPSAMLSYLKKIDPVMAEQWHPRDTRKIRRSLEIYFHTGRPPSEIYSEQKMKSSGSKLRYKSLIFWAFADSLVLMPRLDKRVDKMLSHGLVDEIKSMKSLAESEKFSPDFTRGIWQCIGFKEFMPWFEAPSDIVFNDCLERMKVSTRQYAKSQKKWIQSRFLPMCLAQQDLSPSSILFSTTNTTDLNNWEEQVEKACRVFQYFFYNGDAIAPSADDQHAFEKARDYLSIMNGRQSQKKKFVCEECLDKRGDPFTVIGEDAFNVHIKSRKHKTTVRRKKERAERQIRLKNIGILK Q9UT77 GATB_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate; Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_03147}; SPAC343.13; CHAIN 1..526; /note="Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial"; /id="PRO_0000316035" MSFGRWAASIGLEIHLQLATVKKLFSPAKVNPLAQPNTCVAYFDVSLPGSMPILNPEALKFAVKGALALNCEVANVCKFDRKHYFYPDLPAGYQITQKEIPIGRNGFIPLSAGLDNVPDTQIPIQHIQLEQDTAKSTSAKNPSRILLDYNRAGTPLLEIVTKPCFHDVNTVSAFLFKLQSIVRFAGISEALMENGGMRCDVNVSIAPVISSENLNELHFKNNGVISVEKSISHFPQLGTQLARVELKNLSNVRNVVNSIRHEVDRQVSLANMGVSWPSETRGFDDITGKTFPLRNKTTSDDYLFLPETDIPPIILSRSYVNSVLKSLPALPDELFQKLTTGSHAISHKEARTLLSVKEYYHYYRNAYHHIDSISHVNQSLKEDALRTLPYWITVELVGKVREIDPSPNINIVPPLQLADIVLLVSKKKLTAASAKLFLRSLIKSPSSKPISTLIQEKNFGTIGDSEKIKACVESVLSKHSKQFEELKNGKTSLIKWFVGLTMRELRGQASPKDIEMEVQSSLRREK Q9UT83 MUG28_SCHPO SPAC343.07; CHAIN 1..609; /note="Meiotically up-regulated gene 28 protein"; /id="PRO_0000278491" MIALEKLSEKNKRSTKKCEISIYVGNLPSTCQSSDLHELFEPFGNFSKFHMLSRKKNKSTDSKSPTLFAFITFENKCSADNAIASLNGSSFQGNTLKVEYTHIVERYKNKLENGVDQIHHSNNEKAKIRFSKIEKYTKETRPTVSEVRVSTKDKKEYSMNTSNLVQSNPPKVHDKENAFAEATGTSILSSKAVQTLLVSDFTENEPKHLSIRPNCKDNNTPSISNTFIEPYKENNTEHLHLKSAFEPCQMMPGMLLEQNPQFLYDNPSIFVIGILNLPLKVSPVELYNEFSNHGHILGVAINQSINEDMTHYAEVAVSTYESCIEIIEKFHAIAYEGSILQLFIKQPVQGFCSNLLNHPEGTMTNLLPPNMEMPQPFEIPVIAKTSALPNPFISFPSFQTSYETTVTPTPTSTPTIDPCNLFVKNLDDNIVGNTQQLEELFSKFGRIKSCTLASYPSTEISKGYGFVSFSHPFEAVQAINTLNGVLFGKKRLFVNYAEKREDRKKRLSAIFSQSYPPVVPSPSLTIPMATEPQILEYHQEWPQPLIQSIQQHGYSDPRQTLPTRLDSCAAKLREAVISNENLNPSHKFGIKHSTFKTSLSPLTNIVLNQ Q9UT88 ERG8_SCHPO BINDING 151..161; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate + ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2; Evidence={ECO:0000250|UniProtKB:P24521}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342; Evidence={ECO:0000250|UniProtKB:P24521}; SPAC343.01c; CHAIN 1..426; /note="Phosphomevalonate kinase"; /id="PRO_0000310369" MKVTCSAPGKVLIAGGYIVLDPQYSGLVIGLTAKGYASTTTLDDKCGTVRVKSPQFINAEWLYNIDWTVSPIRVHQIYENCELEKNPNPFVQLALFYVINYFFSTGRQPLCWQDLQVTLQVDNAYYHQPQLKPDQTSYPKFNFLNCTLGQVHKTGLGSSAAMITSLIGSLFLSLRRLTDDTGDKSLKIDDSTKVIVHNLAQIAHCSAQGKVGSGFDVGAATWGSCIYRRFDPKLIEQLLVPYDEQIKNINFSTELRKIVSKKWSDVVPFQLPATYCLLMGDVAGGSSTPGMVKKVQQWQKENPEESKNCFDDLYSRVLSIKNCFLSSESLDSELQSQFRSIRRILQRITVEAKVDIEPLKQTNILDNIEQLPGVIGVGVPGAGGFDAQFCLAINHTEIIENVIKTWKDDGVVPMDVSPAFDGLAVE Q9UT92 YL47_SCHPO MOD_RES 20; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 23; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 25; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 26; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC323.07c; CHAIN 1..533; /note="Uncharacterized transporter C323.07c"; /id="PRO_0000316590" MKRFFSKLFSKSPTSGRVPSPDSDYSEEEQRLLAEENGYFQDSNEYVEPNIPAVYGSMIPVAQQLQQHHVHTPGESFADNASGYPVIKHELSELLRLGSPTVIAYLLQSSEQFSTVFTLGHLGKEYLAASSLSTMTAAISAFSIFQGVISSLDTLATQAFGANKPYNVAIYLQRCLLILAVLHIPVALIWLNLEHILIFLHQDPMVAHLCGRYMRVFILAAPGYAVFEALKRYLQAQGIFTPITYVLCFAAPLNILLNYLLVWHPTIGFGFLGAPVAVATTFWFQSICLILYICFSSTPIPWPGFSRQALKNLSPMLHFSFHGMLMIVTEWAAYEMTSLGAGYLGTAPLASQSILLTSTSLLFQIPFAFAVASSTRVGHLIGSGRANLARLCSRVAYSLALCISIFDGSLIFCFRDVWGSLFTSDPEVLAVVKDIFPILSLFIVTDGLNAVGGGLLRGTGKQYIGGLISIGSSYLFALPVTVFVVVYFNTGLKGIWCGMILSSVTAITCQFTVLFNTDWHRVLQEARHRLTHV Q9UT93 ULA1_SCHPO SPAC323.06c; CHAIN 1..517; /note="NEDD8-activating enzyme E1 regulatory subunit"; /id="PRO_0000194961" MGTSAKMQKYDRQVRLWKAEGQNAIEKSHVCLLYANTVGCEALKNLILPGIGSFAVVDDTSVDFSMDGMNFFIQYDQEGKSRARCTASLLQQLNPNVEMEYLEMSPEALIDKNIEYFSKFSVVLSSNLKEKPLFRLEEYLRSHKIPLLHFNSVGFAGILRISTHEYTTTQSQPELPQDLRLKNPWPELINYVKSMDLDNMDSSSLSEIPYIVLIIHVLLKVSPAHAQNSQEADDCAMFRKIMEEYKGKCDSENIEEASSNSWKAFKEYKLPSNVYEVLHDTRCVKIQEDSESFWIMAHCLKMFYDETEFLPLSGLLPDMNCSTQQYVKLQVIYKEKSENDILKFKKYVQQTLKRLNRSVEEITDLEIKHFSRNCLNIKVMDFKTMKEEYQPTSNSVLESSSIDSNSLLPWYLAFRIYDTILEKHGKNYKEAFSDTTKTISVAQSFLSQIGLEKFFDVVYTAIQELERADGHELHSISSFIGGIVAQETIKLLAQQYLPLNNTFVFDGVHSRTETFKL Q9UT94 MTQ2_SCHPO BINDING 54..58; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 80; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 130..133; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 130; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; EC=2.1.1.297; Evidence={ECO:0000250|UniProtKB:Q03920}; SPAC323.05c; CHAIN 1..231; /note="eRF1 methyltransferase catalytic subunit mtq2"; /id="PRO_0000362148" MLSTPVTSQLRLKEFQDVYEPAEDTFALLDALEKDAKKLRQMAEMKNLLTAEIGCGSGCASSFLKSGILKNKPIVHFMSDISNSACRASKITALNNRELYKDDNGLFITVQTSFLDGIRLGNGVDILIFNPPYVPTEFEEIPSEAATIASAWAGGTDGMDVTSTLLNQLKDILSQDGVFYMVAVARNKLHSICEILQKDGFIVNETLKRKAGRETLSILRIYRIGNTIWDE Q9UT97 PSA5_SCHPO MOD_RES 55; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC323.02c; CHAIN 1..247; /note="Probable proteasome subunit alpha type-5"; /id="PRO_0000124128" MFMTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGVKTKDAVVLGVEKRLTSPLMESHSVEKLFEIDSHIGCAISGLTADARTIIEHARVQTQNHRFTYDEPQGIESTTQSICDLALRFGEGEDGEERIMSRPFGVALLIAGIDEHGPQLYHSEPSGTYFRYEAKAIGSGSEPAKSELVKEFHKDMTLEEAEVLILKVLRQVMEEKLDSKNVQLAKVTAEGGFHIYNDEEMADAVAREQQRMD Q9UT98 POS5_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + NADH = ADP + H(+) + NADPH; Xref=Rhea:RHEA:12260, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:456216; EC=2.7.1.86; TRANSIT 1..42; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC323.01c; CHAIN 43..386; /note="NADH kinase pos5, mitochondrial"; /id="PRO_0000316603" MIRAANGFRISVRNTAVCLAPNFRQLKGFSIINLGSLQYFRYNSVYSKSIRLVNTLENRIVPVYKECASPQSIGGKSNLKQLQWPKPPKNILILKKRMDERVDHCFETLVQHLQQTYPDICIITETDVAKKFSYLNLYTWTEISDLEQKVDAIITVGGDGTILHAASLFARSGMPPILSFSLGTLGFLLPFDFGSFQTAFADFYNSRSFVLMRMRLRVAMKTKLYNESIYAMNEMHIHRGLSPHMAVLKVFVNDKFLTEAVADGLIISTPTGSTAYSLSSGGPIVHPSINALLLTPICPNSLSFRPVLFPDTFKISIETSNKSRVRPQLSIDGRPLGLTDIGQRIDITSVKDNAIPCIIRSHKEDDWVSDIVSLLRWNHPFHRKGW Q9UTA1 YL8J_SCHPO SPAC25B8.19c; CHAIN 1..522; /note="Zinc finger protein C25B8.19c"; /id="PRO_0000046867" MSSDNTPSINRRNNENPPQSSLPTTSGIVYNMFPACPYPHVQNPAFHGSVDVPQVAQKAFDPQAATVSESANVSRPTPAPVPPAGNTNTPTTSNSNQNLENNVTSAASMPAILNAAGQLEFSPSTNNALCCCTTVHGHPHMPPNLLAASSARLRLPPISTILGGTFADPTFLAAAAAAAVPHYAHATTGSATDASNTSNGNSNPAAVPAGFLSGYSPLSYAYFVAKANELALANQRQSSEAAEQPSSKNNTSGANPPSSNNQEVTSAPIPAAPIVLPFQQPFYPIVCPGCAQGALPQHIPVPHNTEFAQYQPSSRDLQNHPTVDESRLSSVAPPASNTLNHANGNQAENASESSTSQSNDSQGPANTSYPVSVPLPNDAENNHTLSRNPYIPSLNFKDNMSAELSVVATLASNSAQAHPMGQQSDSNYSDHHNNDKRAHVSRRHSTSRKIAQSHTGSSSTSSAANVRYRCTECLQGFSRPSSLKIHTYSHTGERPFVCDYAGCGKAFNVRSNMRRHQRIHGL Q9UTA3 YL8H_SCHPO ACT_SITE 149; /evidence="ECO:0000250"; ACT_SITE 190; /evidence="ECO:0000250" SPAC25B8.17; CHAIN 1..295; /note="Probable intramembrane protease C25B8.17"; /id="PRO_0000316621" MEGVILASSALFTVYIGAKWSAQEEEPEEKQLINKRLAVLFPIFGGVTLVLMYLALRYLSKEYIQLILQGYASLASIICFVRSFNPKTTFGKITATMSSIAIALFYFKTKHWMASNILAWALAANSISIMRIDSYNTGALLLGALFFYDIYFVFGTEVMVTVATGIDIPAKYVLPQFKNPTRLSMLGLGDIVMPGLMLALMYRFDLHYYINSTSQPKKHSTYFRNTFIAYGLGLGVTNFALYYFKAAQPALLYLSPACIVAPLLTAWYRDELKTLFSFRSETEDETDEQDKCKST Q9UTA7 YL8B_SCHPO SPAC25B8.11; CHAIN 1..654; /note="Uncharacterized transcriptional regulatory protein C25B8.11"; /id="PRO_0000310389" MSNLILTPSNNGTERPYRSRKTRPCDNCRLRKSRCVVESIGNPCLLCTQLKIPCTYHLPPIKRNKQKKQQDSVSDDTPSEATTTTNDDRDPKYNALGNNLDAVRGKVISPTQGSDARGPDGRQVPLNLAGITEMYHTSDDKFDKLGLDDSLNYPYVLGPTCDSDIDLIREYFSFENGVCSFDNMTVKYVSTSSKSPVMYILDPAYENDRHSDFSRYDHALHDLLSTYIDEATGRTLVNLYFSHVHPSYPILHGPRFLLSYKNGSRNVPSILLAALYSVALTYWPSDSRSFGAPPLDQRKMWTIVEEGLNFHFTQPRLSTIQAALLYLISRPLHNMYSLSSILSRTTVLSQLLGFNHDCTEWKIPNEEKTIRKRIWWAIFIADKWYSMYFGLATNIHEDDFVVPKIESDESLPLEITSSHSFKTFLKMIELSSLLQDILQDLFTVRALTRHSKNNRSISYQIIGFFTRLNSIRPVEFTEPALGVASLKIQFDAVEILLWKTALRFNLPDFQSADDLFVCVEKSVSNFVQITANSSGDFFWPYAGFHFSTLVSLLIRLHLDFHTNNTYGARAFSLLDAFVRHCITLHEAGFDFVEMAIRRSSSLLKELGKDHPHLLALRDDIFNSNDSRGEEAYNHVPEQLFDPWNPHSWTFPKSD Q9UTB2 SYSM_SCHPO BINDING 287..289; /ligand="L-serine"; /ligand_id="ChEBI:CHEBI:33384"; /evidence="ECO:0000250|UniProtKB:Q9N0F3"; BINDING 317..319; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9N0F3"; BINDING 340; /ligand="L-serine"; /ligand_id="ChEBI:CHEBI:33384"; /evidence="ECO:0000250|UniProtKB:Q9N0F3"; BINDING 404..407; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q9N0F3"; BINDING 438; /ligand="L-serine"; /ligand_id="ChEBI:CHEBI:33384"; /evidence="ECO:0000250|UniProtKB:Q9N0F3" CATALYTIC ACTIVITY: Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evidence={ECO:0000250|UniProtKB:Q9N0F3}; TRANSIT 1..42; /note="Mitochondrion"; /evidence="ECO:0000250" SPAC25B8.06c; CHAIN 43..479; /note="Serine--tRNA ligase, mitochondrial"; /id="PRO_0000315879" MRLTNRRFSTFLGNALPSKKKGFIFMSQLLYLRTFSTHTSYLRSSWQAILNYKYIYQNAEAVQRNCINRNLQAIAETVPKIRSLIDEKESLKNEFFPLLSLKKEITLQIERCSDPNERGKLVNEAKGLKKKTEEYNKIISKVTNDLYQYCLAVPNTTLPTVPVGPEDKAVVVQKIGSPLVKKTGSLKDHLQIANEGINLEDAAQASGHSFCYTTGDIALLEMAITNYAMDFAISKGWCPVIPPTIVRTDIALACGFQPRDEEGQQIYELDSYTSPLVSSPKQCLIGTAEISLAALGFKKTFNNFTERKVVGVSRAYRREAGARGKENRGLYRLHEFTKVELFAWTHPSRSSEMFNEIVNFQKEFVETLKIPARILNMPTAELGSSASQKYDIEAWMPARQSYGEITSASNCLEYQARRLLTRYRNDKDSGFVHTLNGTAAAIPRLIIAILENHQQEDGTVKVPETLVPYIHKEYLFKAK Q9UTB3 YL85_SCHPO ACT_SITE 149; /note="Nucleophile"; /evidence="ECO:0000250" BINDING 208; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a uridine in tRNA = a pseudouridine in tRNA; Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; SPAC25B8.05; CHAIN 1..450; /note="Putative tRNA pseudouridine synthase C25B8.05"; /id="PRO_0000316611" MPASKYAGWSRDQLISRILELDGKLQKNTNSLPNKEIEGKNEVIKNKNKLDNGNEIEPQHLSQELVLQHALQDASSLPKLKPVRPFQLEKTVFVAFKFAYCGWNYNGLAYQLEPTPLPTVEGKVFEALLRAHLITDPSSCSFSRCGRTDKGVSAMGQVISLNVRHSERRPIIYCDVLNRLLPADIRITGYAFPPEGFDARFSCKQRHYKYLFTKDYPGGSLDIDRMNEAAALYLGEHDFRNFCKIDASKQITNYHRRILSSKVICIDPSTGLYAFDLQGTAFLWHQVRCMMAILFLIGQKLEPASLINDLLDIKKVPTKPIYDMASEYPLILYDCDFDNIEWTLPTDSPTTAPRIAKHTYETIYHQWHSLRIREQIASFMLDIADHNVKRYGKSEESSSTMNVGEGLLKRTKKYIPILSRQRQESVEVVNERYKRKKGLKDSDVKSENIK Q9UTB8 INI1_SCHPO SPAC23H3.02c; CHAIN 1..117; /note="Pre-mRNA-splicing factor ini1"; /id="PRO_0000218721" MSKHHPDLVLCRRQPGITVGKLCERCDEKCPICDSHVRPTTLVRICDECAFGSSQDRCIICGAPGVSDCYYCSECTRMEYDRDGCPRVINLGSSRTDWFYERKKFKNAGKEMPGATY Q9UTC0 ZYM1_SCHPO BINDING 7; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 15; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 15; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 17; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 21; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 21; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000305"; BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000305"; BINDING 26; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 30; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000305"; BINDING 30; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000305"; BINDING 32; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000305"; BINDING 40; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000305"; BINDING 40; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000305"; BINDING 42; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000305"; BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000305"; BINDING 47; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000305" SPAC22H10.13; CHAIN 1..50; /note="Metallothionein zym1"; /id="PRO_0000374047" MEHTTQCKSKQGKPCDCQSKCGCQDCKESCGCKSSAVDNCKCSSCKCASK Q9UTC3 PSF3_SCHPO SPAC227.16c; CHAIN 1..166; /note="DNA replication complex GINS protein psf3"; /id="PRO_0000132324" MDYYDIDSILSENQKVPCTSTVSIPGLGHEGRMVPTGSKVELPFWLAEVLAINSFVSIHMPAPFSSVVRNALKANPNSVSIRDITTHYYHFAEKMLHLISDDSLVQISLNTLRSRAMLIADASLNPQGALQQNSQFIEGLDDFEKHILRVSHNAHRSLINWQNSTS Q9UTC4 YIDF_SCHPO SPAC227.15; CHAIN 1..873; /note="Uncharacterized protein C227.15"; /id="PRO_0000358935" MSNKPDANDQCMVKETISRMSMSKEKPFLRRNYSSPSFNDSVNSVNDEFQTYQLPNGEFSDNMNDLYFPFRKGNESLMTENSNYPISEQDTQHNHISDFPSRRMQLDGMNHSNNDTYSTAIPFSKDSSVFDAVGQQSSVPIHINPAYTNSHQNSYSLNETYLSYDFFDNHRGASSSAVSKDGLASPRPTKDVDADDTTWYFTSSPSFQPLKDSDRSQTKNTHEETSPIVSSPEDDADAAFKPSSLPSTSISASSNAFYKPAAPDNERPLDPHITPYLRLQLLTTGADDNDIRKNALTQVDYLSYDWKETDIWASWREITKTKANYDNGIRLENASWRTWMKHKFKLKTISPETLNWLKECDVTWLYGPLLHTSMPSRHHSHRKKEKEKEKSKAPRVTPLTHKTNDDEANHSETSSGSSLAKKPILKRRTPQELLLSGRDLTPWPQIRRFDSLLARNRGDIFSNRNHATIRSALFSQRYPSHSKRHIHFNDRVQQCIAVDIDSLPSDSESASYNTDDANSVVSPSKDGISTTTVSSDATRSSQSSHFRIIEDLPDSKLKYSLEDQATYDQSSRYPGRHFGKTGRSHFPRAPEYYGENDFEEDEVYRDDRHYENEHDEYDPNLIYYDNEPTEENRLVFEDTNNTFIDTDSDDSNADESQFLEYANDSPNSSESLESLNNQSYSSSPYSVFSHPPPYMGRQSLNDSPQTSDFKASNLNDSSSNVHSIFQTRETTSPSVQNKTPTKYHRELKSSKDGHEQASPLVSSSPSGSFTSQISPAATTTATNLDAVSLSPSTVRTGSQISDIGNDAISTTRKTVRAFLENANPYSTNNDGNPSNNTSDVEVNETSMNDNSEEPISSNWLVDLFQKSLKSFRE Q9UTC5 YIDE_SCHPO BINDING 36..43; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48; CATALYTIC ACTIVITY: Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674, ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48; SPAC227.14; CHAIN 1..235; /note="Putative uridine kinase C227.14"; /id="PRO_0000358938" MALQVDAPDVSSYDELYNRAVELLKHQQRVLIGLAGGPGSGKSTLCAILAKAWNERFGSEIVKIIPMDGFHYSLEELDRFDNPEKARALRGAEWTFDADLFYSLVRLMKKITDRELYAPSFDHAIGDPVVDDICVEPKNRILIFEGNYLLLNKPPWSDACKLYDIKAYLPVEHSVARARVAHRHLVSGLCATEEEAIERTDRNDMINLTFVEKNMVTPDIVLQQLRLKTVKTSSL Q9UTC8 OS9_SCHPO BINDING 139; /ligand="a mannooligosaccharide derivative"; /ligand_id="ChEBI:CHEBI:71274"; /evidence="ECO:0000250|UniProtKB:Q13438"; BINDING 151; /ligand="a mannooligosaccharide derivative"; /ligand_id="ChEBI:CHEBI:71274"; /evidence="ECO:0000250|UniProtKB:Q13438"; BINDING 209; /ligand="a mannooligosaccharide derivative"; /ligand_id="ChEBI:CHEBI:71274"; /evidence="ECO:0000250|UniProtKB:Q13438"; BINDING 215; /ligand="a mannooligosaccharide derivative"; /ligand_id="ChEBI:CHEBI:71274"; /evidence="ECO:0000250|UniProtKB:Q13438"; BINDING 237; /ligand="a mannooligosaccharide derivative"; /ligand_id="ChEBI:CHEBI:71274"; /evidence="ECO:0000250|UniProtKB:Q13438"; BINDING 243; /ligand="a mannooligosaccharide derivative"; /ligand_id="ChEBI:CHEBI:71274"; /evidence="ECO:0000250|UniProtKB:Q13438" SIGNAL 1..40; /evidence="ECO:0000255" SPAC227.11c; CHAIN 41..310; /note="Protein OS-9 homolog"; /id="PRO_0000043274" CARBOHYD 60; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 97; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 204; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 208..241; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"; DISULFID 223..253; /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" MFSSSMFPHLILPAIGSSKVRTMVLPFAFVGFFIFPICLASLLDWNDAYEYPKYSFEWSNVSILEGDIDSIKEKTEKTKLSSLFYAGKHEYFCVYPNASLIKQNSTTEPSYDLQELRIQGTEKINELANVFLIENRGYWTYDYVYGQHVRQYHLEPQQGSDKVLANPMYILGTAPNTQTKKNLEENWAIGFVEGKAYLQTTFRNGTMCDITKRPRHVILSYECSTNSDTPEITQYQEVSSCAYSMTIHVPGLCSLPAFKIQEDIPSEKIVCYNVIKEKSNEVDHKDSQHVVDEVAQTSPPEVKEVETQSS Q9UTD0 FOLD_SCHPO BINDING 34..37; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 58; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 123; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 151; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 274; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P08192"; BINDING 289; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P08192" CATALYTIC ACTIVITY: Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378, ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216; EC=6.3.2.12; SPAC227.09; CHAIN 1..417; /note="Probable dihydrofolate synthetase"; /id="PRO_0000339137" MPIQLGLQRMLQLLKHLGNPQESFCAVQIAGTNGKGSICSYIYTSLLQAAIKTGRYTSPHFLEPRDTISINGQIASEEIFNTCWKQVIEVDRRFRTKATEFELLTATAFQCFHHSGVRVAVIETGMGGRLDATNVFEEPVLSIISRICLDHQAFLGNTLEAIAKEKAGIFKKNVPCVVDGLNEVNVLNQLKLSAEETRAHPFYLAKGKSGENKNEWIINTPNWGTNTFSTPLKGDYQGQNLACAVTALDILSSSFSIMLPHVQNGVKNTSWPGRLDIRSVPSLGDILFDGAHNKEAAIELAKFVNSQRREHNKSVSWVVAFTNTKDVTGIMKILLRKGDTVIATNFSSVSGMPWIKSMEPEVIKNSISSESSVECYTADNLTISEILRLAKEKNSSVIVCGSLYLLGDMYRYLKLDV Q9UTD8 ERD11_SCHPO SPAC227.01c; CHAIN 1..373; /note="Protein ERD1 homolog 1"; /id="PRO_0000116788" MALIEDLNHFINYFPLVLRLFFLVVFGLYSFTLILHLLVINRVDVFSLLHTPLPVNRSQQANAPLWQLSFSLSILGTLLFVIAESLYLISGSDELAYVPVFIFGVIVFMPVHKFWFFQRKVFTRQCLRILGGSYRPDYKFPDVIFSDLLTSYSRVIADLWLAGAILIYVTDSPNNSHRKQYENEVIMSMIAAYPYAIRFRQCLIERSSADNSSDKFWSTLNSIKYFTAFPAIFLGIFAKKRFSFLWFLWNTSSAINSTYSFWWDVSMDWSLPFFKQPLSIQNWKFGVRRLFPTFTFAVVSAIDFVLRMAWVVRVLPEHQSAFFTTDFGIFIMQFLEVFRRCVWVFFRIEAEASKSLAYVNISDRSDIPTIHPD Q9UTE1 YFMD_SCHPO ACT_SITE 235; /evidence="ECO:0000255"; ACT_SITE 266; /evidence="ECO:0000255"; ACT_SITE 527; /note="Proton donor"; /evidence="ECO:0000250" BINDING 150..157; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 300; /ligand="beta-D-fructose 6-phosphate"; /ligand_id="ChEBI:CHEBI:57634"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, ChEBI:CHEBI:456216; EC=2.7.1.105; SPAC222.13c; CHAIN 1..592; /note="Probable 6-phosphofructo-2-kinase C222.13c"; /id="PRO_0000318496" MSNTGSARTEEFTKGTGYEATKPNNDTDDDAKQNYPSKEPHMKLGDYTEETSFVDDSIFKREELTPDRNSPANDVEKMEVPKPTPQWMKLKDEGKLGKHRKNRLRRPGRFPVRQESTIDIPGLTVSKRTENDSNNASYGIREKLIIILVGIPATGKSYIGSKLSRYYNWLKYNCRFFSVGDKRREEGASTYSMSADFFDIKNEETFKFRENVALETLEDLLHWMIHENGVIGILDATNSTHERRKHLYDRISKEADIGIMFLESLCTDDILFEENIKLKIKGPDYEGYDTESALKDLRERVDLYKKYYEPLDERDEQLPFLQYVKVINVGIKVVTHNIEGFLAGQAVYFMLNLNIQKRQIWLTRPGESLDTVAGRIGGDASLTPIGKQYAQDLANFMDRQRVLWQLRYTNDLASTNKRFSLSEASSFNVWSSVRKRAIETIEFFNPDSYNVKKIRLLNDLNLGSREGLTLREFSEKYPDEFDVIKRKDYAYRFSGQGGESYLDVIHRLQPLIVEIERSSGNILVVSHRIVSNILMTYFLNYHPEDIIDVGLPLHTLFCIESDRYGTTCMAYRYDAANRQFIKDPMFDLRKRT Q9UTE2 HEM6_SCHPO ACT_SITE 118; /note="Proton donor"; /evidence="ECO:0000250" BINDING 104; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 120..122; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 271..276; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3; SPAC222.11; CHAIN 1..312; /note="Probable oxygen-dependent coproporphyrinogen-III oxidase"; /id="PRO_0000109877" MSDITVEPIGKQMEKLILDVQQEIVAGLEAVDGQKFFQDKWTKGEGGYGISCVIQDGNVFEKGGVNTSIVQGKLNQDAVQRMRANHEGIDRTAKELPFFAAGISMVIHPRNPMAPTTHLNYRYFELVNSDGKKIWWFGGGADLTPSILFEEDGKHFHKLHKEACDRHDPTFYPRFKKWADEYFLIKHRKETRGIGGIFFDDLSEKDPQELFAFVKDCAHTFLPAYVPIMEKRKNMEFTEDDKEFQLIRRGYYAEFNVMYDRGTWFGLQAPEPRVESILMTLPLHASWRYKYEPKQERHKALLKVTHTPIEWC Q9UTE4 YFM8_SCHPO ACT_SITE 101; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P37528"; ACT_SITE 208; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P37528"; ACT_SITE 210; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P37528" BINDING 68..70; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P37528"; BINDING 131; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P37528"; BINDING 167..168; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P37528" CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000250|UniProtKB:Q8LAD0}; SPAC222.08c; CHAIN 1..234; /note="Uncharacterized glutaminase C222.08c"; /id="PRO_0000316599" MSSASMFGSLKTNAVDESQLKARIGVLALQGAFIEHINIMNSIDGVISFPVKTAKDCENIDGLIIPGGESTTIGKLINIDEKLRDRLEHLVDQGLPIWGTCAGMILLSKKSRGGKFPDPYLLRAMDIEVTRNYFGPQTMSFTTDITVTESMQFEATEPLHSFSATFIRAPVASTILSDDINVLATIVHEGNKEIVAVEQGPFLGTSFHPELTADNRWHEWWVKERVLPLKEKKD Q9UTE6 MAK16_SCHPO SPAC222.06; STRAND 19..21; /evidence="ECO:0007829|PDB:8EV3"; STRAND 26..28; /evidence="ECO:0007829|PDB:8EV3"; STRAND 34..37; /evidence="ECO:0007829|PDB:8EUY"; STRAND 48..56; /evidence="ECO:0007829|PDB:8EUY"; STRAND 59..65; /evidence="ECO:0007829|PDB:8EUY"; STRAND 76..81; /evidence="ECO:0007829|PDB:8EUY"; STRAND 132..135; /evidence="ECO:0007829|PDB:8EUY"; STRAND 174..177; /evidence="ECO:0007829|PDB:8EV3"; STRAND 179..181; /evidence="ECO:0007829|PDB:8EUY" HELIX 4..11; /evidence="ECO:0007829|PDB:8EUY"; HELIX 67..69; /evidence="ECO:0007829|PDB:8EUY"; HELIX 73..75; /evidence="ECO:0007829|PDB:8EUY"; HELIX 86..96; /evidence="ECO:0007829|PDB:8EUY"; HELIX 102..127; /evidence="ECO:0007829|PDB:8EUY"; HELIX 138..155; /evidence="ECO:0007829|PDB:8EUY"; HELIX 157..170; /evidence="ECO:0007829|PDB:8EUY"; HELIX 183..193; /evidence="ECO:0007829|PDB:8EUY" TURN 12..14; /evidence="ECO:0007829|PDB:8EUY"; TURN 40..42; /evidence="ECO:0007829|PDB:8EUY"; TURN 44..46; /evidence="ECO:0007829|PDB:8EUY"; TURN 97..99; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..302; /note="Protein mak16"; /id="PRO_0000339417" MQQDEVIWQVVGHEFCSYRIKGEAQNFCRNEYNVTGLCNRQSCPLANSRYATVREDNGKLYLYMKTIERAHFPSKLWQRIKLSKNYAKALEQIDQQLLYWPGRQIHRCKQRLTRLTQYLLKARRLALKHQPALIPIKPKQAHREASRERKALIAAKLEKNIEKELVKRLKSGVYGDQPLNVNEEIWNKVLAAREGLIDEGEEEEEREEAELEFVSDDEDEEEISDLEDWLGSDQSMETSESEEEESSESESDEDEDEDNKGKIRKRKTDDAKKSRKKRAPHIHIEYEQERENEKIPAVQHSW Q9UTE7 MSS1_SCHPO BINDING 246..253; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 293..297; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255"; BINDING 363..366; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255" TRANSIT 1..19; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC222.05c; CHAIN 20..496; /note="tRNA modification GTPase mss1, mitochondrial"; /id="PRO_0000035780" MRILNRVFLNTFQACFRRFVHQIPTIYALSTPPGTSAVAIVRISGPNACKVAKTLAGSVPKPRIASLRTIKHPVRSEVIDKALMLYFKKPSSFTGEDVVELQLHGGTAVVDVTLEAIKQSGIPNIRYAKPGEFSERAFYNGRADLTQLEGLIDVINAQTAEQLYSANKEAHGSIYDICFRWRKKLIEYRAFLEASIDFSEEHELDDIETIKLFEELNEMKDEIDAHIEGGKCKEVLRKGINVAILGPSNAGKSSLINLLANRRISIVSPQSGTTRDAIEVLVDINGFPVLLSDTAGLRKGEDVQEIEKIGIEIAKARAEESQLTLFVFPINYHSFSESLKQSEILETIKDCLRQRKPIHFLINKVDCVSDYTTMFKPIKAYLQKNFLIPENRIHAVSCKTKEGLIDFLQALSSTFECMVNPLTNNKIQANLGWNERQRQCLSSCSSHLSLALQKSSDIVVAAEEVKLATEDIGRVTGAVDMENVFSVIFSKFCVGK Q9UTE8 IES6_SCHPO SPAC222.04c; CHAIN 1..117; /note="Chromatin-remodeling complex subunit ies6"; /id="PRO_0000339139" MEKNSSVDSLDISLLARPFRNPNYKAQPRRNRNLRQIIQNDPVQNEPSKFSYSSIEAPPSVLPQPKYCDVTGLLAIYTDPKTRLRYHNKEIYGLIRELPSGADQEYLKLRSSDVVLK Q9UTF6 COX6_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1B2.04; CHAIN ?..140; /note="Cytochrome c oxidase subunit 6, mitochondrial"; /id="PRO_0000006107" MKAVQRIFQTGRFSVAAGPSVRFQAGFLAANRQVRFSSNHGVSLEEINTKYNDFFSNVQDQFELQRGLNNCFAYDIVPSSDVIEQALRAARRVNDFPTAVRIFEGIKVKLPTKEQYQAYVKELKPVCNELGIVLKEDLFK Q9UTG1 PNPH_SCHPO BINDING 49; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250|UniProtKB:P55859"; BINDING 81; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250|UniProtKB:P55859"; BINDING 103..105; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250|UniProtKB:P55859"; BINDING 135; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250|UniProtKB:P55859"; BINDING 220; /ligand="a purine D-ribonucleoside"; /ligand_id="ChEBI:CHEBI:142355"; /evidence="ECO:0000250|UniProtKB:P55859"; BINDING 239; /ligand="phosphate"; /ligand_id="ChEBI:CHEBI:43474"; /evidence="ECO:0000250|UniProtKB:P55859"; BINDING 262; /ligand="a purine D-ribonucleoside"; /ligand_id="ChEBI:CHEBI:142355"; /evidence="ECO:0000250|UniProtKB:P55859" CATALYTIC ACTIVITY: Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; SPAC1805.16c; CHAIN 1..315; /note="Putative purine nucleoside phosphorylase"; /id="PRO_0000316221" MTATSFLHQAKQQPHHTEPYIKALEAREYIIEQVPEELSKPKVAIICGSGLGTLASGLSAPVYEVPYEDIPHFHVSHVPGHASKLYFAFLGEKRVPTMILAGRYHSYEGYPIEATTFPVRLMKVMGVEVMVVTNAAGGLNQGFKVGDLMILKDHINFPGLAGMNPLRGPNAHEFGVRFPPLSDAYDLELRKLVYDAAKAHKVSRTIHEGCYAFVSGPCFETRAESRMLALMGADCVGMSTVPEVVVARHCGIRVLAISLVTNNVVVEESPSAKDLVEVDSNVMSKGAANHLEVLEVGIAAAADVRTMVETIVNFI Q9UTG4 RS26B_SCHPO SPAC1805.11c; CHAIN 1..119; /note="Small ribosomal subunit protein eS26B"; /id="PRO_0000204527" MTQKRRNNGRNKHGRGHVKFVRCINCSRAVPKDKAIKRWTIRNMVETAAIRDLSEASVYSEYTIPKLYIKLQYCVSCAIHSRVVRVRSREGRRIRTPPPRVRYNRDGKKVNPTAVAKNL Q9UTG6 FMT_SCHPO CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:78530, ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; EC=2.1.2.9; Evidence={ECO:0000250|UniProtKB:P32785}; SPAC1805.09c; CHAIN 1..340; /note="Putative methionyl-tRNA formyltransferase"; /id="PRO_0000083096" MAPKIPLNVIFLGTDEFSIPILRKLIGCVQRVRVVSAGGKRQSRRGEIPLPPAAMEANANGLEYIKLQDGWKNFHMRPDDQLAITASFGRFVPFKILNQLPYGGINIHPSLLPKYRGAGPVYSTILNGDRLAGVTIQTMDSKQFDKGKSLAQAYLKLNGKETYTLLTKILSLGAAGMLEHVLLQSLYLPNCQTNTVAPQIHGRITDTGGLQLISKETFPSFQESWAKKITPEDAHVNFESMNTQQIYNMSRAFNHVWCILNNKKVFLYDVHPLHSTSAEDWIHMKPGEFALLEKNLLLVKTLDHVMVIKGGIRLSARKIVDPVEWGKTFNSGRGGRFQYV Q9UTH1 TRM13_SCHPO BINDING 18; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"; BINDING 24; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"; BINDING 34; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"; BINDING 38; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01141" CATALYTIC ACTIVITY: Reaction=cytidine(4) in tRNA(Pro) + S-adenosyl-L-methionine = 2'-O-methylcytidine(4) in tRNA(Pro) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32767, Rhea:RHEA-COMP:10397, Rhea:RHEA-COMP:10398, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.225; Evidence={ECO:0000250|UniProtKB:Q12383}; CATALYTIC ACTIVITY: Reaction=cytidine(4) in tRNA(Gly)(GCC) + S-adenosyl-L-methionine = 2'-O-methylcytidine(4) in tRNA(Gly)(GCC) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43192, Rhea:RHEA-COMP:10399, Rhea:RHEA-COMP:10400, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.225; Evidence={ECO:0000250|UniProtKB:Q12383}; CATALYTIC ACTIVITY: Reaction=adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43196, Rhea:RHEA-COMP:10401, Rhea:RHEA-COMP:10402, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74477; EC=2.1.1.225; Evidence={ECO:0000250|UniProtKB:Q12383}; SPAC1805.03c; CHAIN 1..368; /note="tRNA:m(4)X modification enzyme TRM13"; /id="PRO_0000339427" MARIKKIFTQEELKQIPCPYDHKHTIVRHRLEYHLKRCNARPVERTDPYYKKDINISTSTDASESSSFEIVDLSKEELSKWICLFNRISDSLPTPQKKVLFHPAMNARLEEGTKKKHAIQQASLLGHMEKLHYFDNQGSIYYEFGAGRAELSRYVQHCSQQENVYILIDRDSNRTKHDSRILKDSIKNNWPEPKIIRCKIDIKDLKLDFFASEFRNSGKPVFAYSKHLCGAATDLTLNCLKSSPPNALVIALCCHHHCRWRTLSTFAREQLSHWGISNPQEFQILRQMTGWAVNSLREHMHASGGADSHISGLSHEERVKIGLKCKHIINYMRKLECEKMGYESSLVYYVGEETTLENVALIAYKRIN Q9UTH5 PLB6_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SIGNAL 1..19; /evidence="ECO:0000255" SPAC1786.02; CHAIN 20..644; /note="Probable lysophospholipase C1786.02"; /id="PRO_0000024644" CARBOHYD 44; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 96; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 141; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 178; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 245; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 253; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 281; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 286; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 316; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 319; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 373; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 393; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 449; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 501; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 558; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 579; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 596; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MYFQSFYFLALLLATAVYGQVASPELHSLSRRNWKKPPPFPSTNASYAPVIRSCDSSEIMVNSLPRGELPDLENDFIEKRLSNANEALTTFLQSKNTTADLDLSSIVGDNGPRLGIAVSGGGWRSMLFGGGALAALDSRSNETTLGGLLQSAHYITGADGGSWLLSSLAVNEFRTIQNISKSIWYTRLGIFFIEETHFGDLKNYYTNVVDEVNQKAAAGFNVSLTDYWGRAIARHFVGQLRGGPNLTYSSVQNASWFQTAEYPYPLIVTQGLTGGLPDGSNGTATNSSIYEISPYYLTSFDNNVRSYTPTQYLGTNYSNGTAVDGKCVTQFDNVGFLVGTSSTRYNEALIDVSLRQSRMSRRLGFTLRHMRINGSSVSFYPNPYTDATDIAGNATAVSEDIVDTPYLDLFDGGYDGQNIPIWPLLQPERKLDVVFAFDSSGDTSNFWPNGSSLVATYERVTQRASDAVYDVEDFVHVPTPETFVNLGLNANPTFFGCDGRNTTRGDVPVDHNTPPLVVYMPNTPWTMKSNLVDHRYRIANSEIQALIQNGFVATTQDNSTDFASCLACAVVQRSLERRNQSTSAACQQCFSQYCWNGTVDNTPVDDDSKNPTYNPAVKTSSASGVHANILLSFFVLLATLLVTA Q9UTH8 SFP1_SCHPO SPAC16.05c; CHAIN 1..442; /note="Zinc finger protein sfp1"; /id="PRO_0000310835" MPSLALPINKPSHHNVNYNGNSFNSIHATSFGMSPQSWGNSFSGQAWLRDTIPSLSNVVESQTIPEEDSTSYLNRLEEAFCRDFRCCGQTLEDLHQLIHHYEEQHAVLATDSAVPQEYSLDSNNAAQSNHSHIQALKQRERIRMHDLADQLGTSEISDNSAVLPFAFPANGGAPGPYRVSVVVPAAAAAAAAAASSDMSSDEASSQAETTGTPKKMPESLVMDASSPLSDMSMSIDVGESAANNVFAFNQKDMVDSTYLPPFNYDHDVFSFAPSVASADQFTESSMSPTPEVVSPAATNSAISSPFVRKSSSDLEAKPSKKQRSTPAFSHDSPLTIDYPGSNLVVVDKPYKCPVPNCDKAYKNQNGLKYHKLHGHCSPITTPTPAPIPHQGFVVENKPYRCEVCSKRYKNLNGLKYHRTHSHLQVSMAQAQREVQMNFMRTA Q9UTI0 PYRC_SCHPO BINDING 12; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P05020"; BINDING 14; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P05020"; BINDING 95; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /note="via carbamate group"; /evidence="ECO:0000250|UniProtKB:P05020"; BINDING 95; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /note="via carbamate group"; /evidence="ECO:0000250|UniProtKB:P05020"; BINDING 132; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P05020"; BINDING 170; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P05020"; BINDING 240; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P05020" CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P05020}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P05020}; MOD_RES 95; /note="N6-carboxylysine"; /evidence="ECO:0000250|UniProtKB:P05020" SPAC16.03c; CHAIN 1..337; /note="Probable dihydroorotase"; /id="PRO_0000147290" MSLKIPGLADMHVHLRQDNMLKAVVPTVAEGGVSVAYVMPNLIPPITTVDACLQYKKEIEQLDSKTTYLMSLYLSPETTPEVIYEAAKKGIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSKDNTVFTAEPKFLPTLLDLHQRFPKLKIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDWQDDPYCFCKPVAKTERDRRALIEAATSKNPKFFFGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDFKESNIVLKKESFRVPESVANDLVPFHPNEVLQWHCSWE Q9UTI1 FUB1_SCHPO SPAC15E1.10; CHAIN 1..265; /note="Silencing boundary-establishment protein FUB1-like protein"; /id="PRO_0000116837" MNNPTSDDRLRFQQKCHKSMLNTGAIFKNCKLRNGDVLQEVTESLTEDSEFNYIVNESQNVSTRLIFWNKWIYILCANTSSNITATRIFRLDDDQPWNLESLVAEVCPVDTDNRLAEHAARTAKDTSANELNYESYQEKSRAPFGFAGPFGAMPGSQPMFPSIGASDLYPAGIGGSDMGNDGGMIPTFNHPIFHPENRSRNEQASANRTNIPPGARYDPTGPGDFRGFGRDERKPQFPFKGPRSQFPGEPDNDDFMPPGSSDMFM Q9UTI2 GLRX2_SCHPO SPAC15E1.09; CHAIN 1..110; /note="Glutaredoxin-2"; /id="PRO_0000141611" DISULFID 26..29; /note="Redox-active"; /evidence="ECO:0000250" MTSIAKAFVEKAISNNPVTVFSKSFCPFCKAAKNTLTKYSAPYKAYELDKIENGSDIQAYLHEKTKQSTVPSIFFRNQFIGGNSDLNKLRSSGTLTKMIAELKENKSSIL Q9UTI6 ECT1_SCHPO CATALYTIC ACTIVITY: Reaction=CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate; Xref=Rhea:RHEA:24592, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57876, ChEBI:CHEBI:58190; EC=2.7.7.14; SPAC15E1.05c; CHAIN 1..365; /note="Probable ethanolamine-phosphate cytidylyltransferase"; /id="PRO_0000208464" MASSSNIKHRLWLDGCMDFFHYGHSNAILQAKQLGETLVIGIHSDEEITLNKGPPVMTLEERCLSANTCKWVDEVVPSAPYVFDLEWMRRYGCQYVVHGDDISTDANGDDCYRFAKAADQYLEVKRTEGVSTTELLDRLLSSVPLEIYSTPVSVLSSQIDLLRRFATDSDGLTPFTDVFIYNTEKPETLISGTTLLRLNPEKNIIYIDGDWDLFTEKHISALELCTRMFPGIPIMAGIFADEKCFEKPMLNLLERILNLLQCKYISSILVGPPPASLFASSKYIKLCFDEQISKVYYPIFSTDVSIPALDISLSNTPNNSFYKFDKLGSDLIKQRVMLRRQHYEERQRRKMGKNATEQTTIKTYA Q9UTI8 RL44_SCHPO MOD_RES 55; /note="N6-methyllysine; by set13"; /evidence="ECO:0000269|PubMed:20444689" SPAC15E1.03; CHAIN 2..106; /note="Large ribosomal subunit protein eL42"; /id="PRO_0000149145" MVNIPKTRKTYCPGKNCRKHTVHRVTQYKKGPDSKLAQGKRRYDRKQSGFGGQTKPVFHKKAKVTKKVVLRLECVSCKYKNQLVLKRCKHFELGGEKKTKGAAIQF Q9UTJ2 PMM_SCHPO ACT_SITE 19; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q92871"; ACT_SITE 21; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:Q92871" BINDING 19; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P31353"; BINDING 21; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P31353"; BINDING 28; /ligand="alpha-D-mannose 1-phosphate"; /ligand_id="ChEBI:CHEBI:58409"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 133; /ligand="alpha-D-mannose 1-phosphate"; /ligand_id="ChEBI:CHEBI:58409"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 144; /ligand="alpha-D-mannose 1-phosphate"; /ligand_id="ChEBI:CHEBI:58409"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 151; /ligand="alpha-D-mannose 1-phosphate"; /ligand_id="ChEBI:CHEBI:58409"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 189; /ligand="alpha-D-mannose 1-phosphate"; /ligand_id="ChEBI:CHEBI:58409"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 191; /ligand="alpha-D-mannose 1-phosphate"; /ligand_id="ChEBI:CHEBI:58409"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 219; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P31353"; BINDING 231; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:Q92871"; BINDING 233; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P31353"; BINDING 236; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P31353" CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; SPAC1556.07; CHAIN 1..257; /note="Phosphomannomutase"; /id="PRO_0000199702" MAVIPIEERKFPKTLVLFDVDGTLTPARLSVSPEMLETLQNLRKVVAIGFVGGSDLSKQQEQLSVNGENVIDSFDYAFAENGLTAYRYGQQLASQSFIAWLGEEKYQKLVNFCLHYIADLDIPVKRGTFIEFRNGMINISPVGRNANTEERNEFERFDKGRKIRATMVDVLREKFKDYGLTFSIGGQISFDVFPAGWDKTYCLQHVEKEGFDTIHFFGDKTYKGGNDYEIFVDPRTIGHSVTNPDDTIAELKKIFNI Q9UTK2 RM19_SCHPO TRANSIT 1..32; /note="Mitochondrion"; /evidence="ECO:0000250|UniProtKB:P53875, ECO:0000305" SPAC1486.07c; CHAIN 33..144; /note="Large ribosomal subunit protein uL11m"; /id="PRO_0000318133" MASTRTTIIKLIVPAGKATPTPPIGPALGARGLKSIDFCKEFNARTAGWMPNTPVPCKITVTPQRTFTFTIHTPPTSWLISKTLDLEKGSSSPLHDIKGQLSLKHIYEIAKLKSTDPSLQGIELLSLCKSVIGTAKSMGVKVVP Q9UTK3 NPT1_SCHPO BINDING 15; /ligand="nicotinate"; /ligand_id="ChEBI:CHEBI:32544"; /evidence="ECO:0000250|UniProtKB:Q9HJ28"; BINDING 170; /ligand="nicotinate"; /ligand_id="ChEBI:CHEBI:32544"; /evidence="ECO:0000250|UniProtKB:Q9HJ28"; BINDING 220; /ligand="nicotinate"; /ligand_id="ChEBI:CHEBI:32544"; /evidence="ECO:0000250|UniProtKB:Q9HJ28"; BINDING 348; /ligand="5-phospho-alpha-D-ribose 1-diphosphate"; /ligand_id="ChEBI:CHEBI:58017"; /evidence="ECO:0000250|UniProtKB:Q9HJ28" CATALYTIC ACTIVITY: Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017, ChEBI:CHEBI:456216; EC=6.3.4.21; Evidence={ECO:0000250|UniProtKB:P39683}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q6XQN6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q6XQN6}; Note=Activity is highest with Mn(2+). {ECO:0000250|UniProtKB:Q6XQN6}; PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release. {ECO:0000250|UniProtKB:P22253}. MOD_RES 223; /note="Phosphohistidine"; /evidence="ECO:0000250|UniProtKB:P22253" SPAC1486.06; CHAIN 1..410; /note="Probable nicotinate phosphoribosyltransferase"; /id="PRO_0000205861" MSEPAVVSILDTDLYKLTMLQAVLEHYPDAQVSYKYTNRSPKMALNQEAYNWLREQIRGLRNLHLLPEEEQWLRKNCPYLKESFYEFMHEFEFDPENSISLNYDSETKDLSIFIHGLWKNTIFYEIPLLALVSESYFKFVDKDWSPEGQFEKAYEKGKRLIRAGCAFTDFGTRRRRDPHTQEIVLQGLMKAQEDFKGPGSFLGTSNVYFAAKYNLNVSGTVAHEWYMGIAAITQNYKQANRIASLKWVQTFGTSLLIALTDTFSTDVFLKSFTANSADDLANVFHGVRQDSGCAEEYIEKVVKHYKSIGVDPSTKVIVHSDALNVDRCIELYKYCEKCGIKSAFGIGTNLTSDFQKVSNPSEVSKPMNIVIKLFSAEGTKAVKISDDIMKNTGDRDAVIQAKHQLCLPIA Q9UTK6 YKR3_SCHPO SPAC1486.03c; CHAIN 1..797; /note="G-patch domain-containing protein C1486.03"; /id="PRO_0000303956" MQNEYVDMNSSSEDSDGDSILEEGRLRPSFRGQQKERDMLGIFGEEDEDGFHNSGIGSARLRRKNISFVEKSEQVKANKQVTADDLLEAHSIPQLKNKNDEVSQAKNIPKMKFNTTGFGAKMLEKMGYKQGQGLGANAEGIAEPVQSKLRPERVGLGAVRERTEKQRKEAIARGEISDSEDEKHTVKQKPLREKKKKPLKSSEEISKDMGSYNLPRFLASLIDASLNDTKEIEFVTSNKEELGLEGRDMSTSGINQLSRLARVECEHHASAWQQLQARRAYVKMELKRVTTEFDEKSVEISRLEKLLGKVMEVKSRSMEFTVPEAEIDVIEKRLQPLNNLIETLPVEFSEASMHFELDSVAVSILAFVLSEPIKNWDVWKHPYFMLESFLSWKNSLYSKDFRPKREESSTFMDIDVEFDDELEGQSLTHYESFMMFVWKKKIGEELKKWIIQDSLKALQLLEAWDPVVPEKVKDSLIQDDILPRLKDAVSKWNPKLKLKKNDSLHHCIFPWLPYLEKHADSLLQSVLVQFSLILSPWKIKNGSIDDFSVWRSAFANDALDRLLEKVILPKLEKLMDEELVIDPSNQDLEIFFIILSWKGSFKAMVFGQLFADHFFPKWLETLYQWLTEAPNFDEASEWYTWWKSVFPKDLLSNAYIQQGFSKGLDMMNECLENKSITAPLPFAKDSTKGVNLQFSKEKHEFTAESDDTTSYDEPLVSFRELVEEFCAENSLLFVPLRRSHLSTGSALFRISTQASKARGITVYLRNDIIWKKSPGASEDTPYDPIGFNEILLMFNNN Q9UTK8 GMT_SCHPO SPAC144.18; CHAIN 1..345; /note="GDP-mannose transporter"; /id="PRO_0000315880" MDNHMLNRISKSPILPVVSYCMASILMTLTNKYVLSSPGYNMNFLLLTVQSTVCVAAIGILKRLKVINYRDFDFREAKFWFPISFLLVAMIYTASKALQFLSVPVYTIFKNLTIIIIAYGEVLWFGGHVTALTLFSFGLMVLSSIVAAWADIQSSSFASQTLNSGYLWMVLNCLTNAAFVLAMRKRIKLTNFRDFDTMFYNNLLSIPVLVICTLFTEDWSAENIAQNFPPDAKFGVLMAMAISGVSSVGISYTSAWCVRVTSSTTYSMVGALNKLPLAIAGLVFFDAPITFGSVTAILLGFISGVVYAVAKSQQQRQKDPATILPMTHNPVSASSQSMRDSLSKS Q9UTL1 COG1_SCHPO SPAC144.15c; CHAIN 1..701; /note="Conserved oligomeric Golgi complex subunit 1"; /id="PRO_0000304070" MVETDLMSSHSSNWKEIFRTHSIAQTIQLEKFVSQQIEEKGRELQQNVCFNYQSFIEASENLSNIRNNLEKVLQNSYEFQSMVSLPKVDRVSKFLSDNESISQTSGDYFIFLQRFYAHAILFVMELFNKEQYLQSSKLLIFCLRILPADLPNDHQCHILVNRLESCKNYLNNRLKQAMTSSLSKVSVVTSWILLNQANISSGLDIFLQECEDQLLILNDAREFSLTFLNTLKLARDFPNEIRSYLEASKNFNIFKEKEILRNICLDECYLKAYFSAEDVKVTTPFETLQQFDGDNILQQWKLSFFSKISHSEKSFFSNATSLTTLYQILEGLLSELSEPQFKEFYELWNSILQNHFIISSRNIIDSLGLYVNKIKEKLQICFEIPPTNSFDPWSFQLKQQVLNELKQNILPACGMDDGFQRFWQSLASFDMVLDESLQVLKKLQTLHLSFTLGDIIPNYLTLADYLLNFVKTSFAQIYELVCSFVNNVAVMESSSEKQLRTSRCLKIVRLLKQFRHMDESVPFDDLIYKLQNILVRELTDFTTGIYINESKINLDVAACITGNFFGPSFALYNSLIMLIDKLEVLGFDIVSDKFKGLLTPNLFESLFILNLERLKAAKSMDHMKQNTFDMEFINYLSDFTNNPREVIDYQHFIELIDLHVQDEFSKEDFDTVRANVKECVPKLLSFFTVLLPRVKAQKVIT Q9UTL4 GWT1_SCHPO SPAC144.10c; CHAIN 1..459; /note="GPI-anchored wall transfer protein 1"; /id="PRO_0000215187" CARBOHYD 13; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSYKLEKEAFVSNLTGSSSIETCGLLLIGIACNVLWVNMTARNILPKGNLGFLVEFFIFCLIPLFVIYVSSKVGVFTLCIASFLPSFVLHVISPINWDVLRRKPGCCLTKKNENTFDRRIAGVTFYRSQMMLVTVTCILAVDFTLFPRRYAKVETWGTSLMDLGVGSFMFSSGTVAGRKNDIKKPNAFKNVLWNSFILLILGFARMFLTKSINYQEHVSEYGMHWNFFFTLGFMALGVFFFRRSLKKVSYFNLATFITLLHHCLLVLTPFQKWALSAPRTNILAQNREGIASLPGYIAIYFYGMYTGSVVLADRPLMYTRAESWKRFQRLLFPLCILLVLYLVSNFLSVGVSRRLANTPYVANVAFINMFFLTIYILIDAYLFPSSVPYGSRVPKLLEDANNNGLLVFLIANVLTGVVNLSFDTLHSSNAKGLTIMTMYLFIICYMAHWLAQHGIRFRL Q9UTL5 TF3A_SCHPO SPAC144.09c; CHAIN 1..374; /note="Transcription factor IIIA"; /id="PRO_0000047085" MCHFNELSIEIESKNLRSAKKIFHCPYEECGKKYSRPSLLEQHLRTHSNERPFVCDYTGCSKAFYRKSHLKIHKRCHTNVKPFSCHYDGCDAQFYTQQHLERHIEVHRKPKPYACTWEGCDECFSKHQQLRSHISACHTHLLPYPCTYQDCELRFATKQKLQNHVNRAHEKIISYSCPHESCVGHEGFEKWSQLQNHIREAHVPSCSICGRQFKTAAHLRHHVVLHQTTLEERKTYHCPMEGCKKSFTRSSALKKHISVIHEGNMAFHCDSCGTKFGYKHMLQRHLERGTCKKAHKPYINECGIKHDGIEGVAIHDQKEKELSSNLVSDVAKKIINEVTGHGYKEAREYSCSFPECNYRFKRLYDMHRHLNSHH Q9UTL7 GPN2_SCHPO BINDING 12..17; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9"; BINDING 172..175; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250|UniProtKB:Q9UYR9" SPAC144.07c; CHAIN 1..315; /note="GPN-loop GTPase 2"; /id="PRO_0000315978" MPFCQVVVGPPGSGKSTYCFGMYQLLSAIGRSSIIVNLDPANDFIKYPCAIDIRKVLDVEMIQKDYDLGPNGALIYAMEAIEYHVEWLLKELKKHRDSYVIFDCPGQVELFTNHNSLQKIIKTLEKELDYRPVSVQLVDAYCCTNPSAYVSALLVCLKGMLQLDMPHVNILSKADLLCTYGTLPMKLDFFTEVQDLSYLAPLLDRDKRLQRYSDLNKAICELVEDFNLVSFEVVAVENKASMLRVLRKIDQAGGYAYGSTEIGGDAVWVNAVRQGGDPLQGISPQERWIDKKEEYDKYEWELEQKSTMDEDENEG Q9UTL8 AP3D_SCHPO SPAC144.06; CHAIN 1..825; /note="AP-3 complex subunit delta"; /id="PRO_0000227680" MVFERTLIDLIKGIRSHANDEEAFIATCLLECRKEATSQDADLKSEAILKLAYLEMLGVDISWASFQIVEVMSSSKILQKQKGYLAAVQSFKPDTDVLMLTTNLLKKDLMSSKVPEITLAIDGLSHFSTLGLARDLYRDVLILLNHSVPYVRKRTILLLYRLCLQYPEAISACIPKLRERLDDPDTSVVNAAVSVICELARRAPKNYLEFAPDLFHLLTTSSNNWMLIKLIKLFASLTPYEPRLVKKLIPSLTDIIENTHAMSLLYECINTIVSGNMLVGHSQCDKLASLCASKLRGFFEDTDQNLKYIALLCLRKLANTHPSLVSAQLDIILKCLVDTDTSIRLRALDLVNEIVNKENIRTIVKTLMLQLIVSSDESAVEDIRNSTATRIIEMTSKSTYMNIADFEWLLTVYVDLANIPGIDTGTLLNNQIIDLCVRVKALRPFSVDIFSQAILDPSYVSTTDCSVSEKRTDILPAIIWCLGEYAEFIEEYLDILDALTRPSFKKCSNLAHRLLLQAITKIFCQWCLEEEPTWGVEKFGLVKLWVEKIVSFIEQFLNFQDMEIQRRASEFYILFNQVSDIVNTSDTMEVLELQKKPPYIVQNTMYKLFFGEPLNPVAVKAQRKVMPDENLDLNCPINGVIEVPKELLENIIQSDDSLINFDTEVPSSGIDTFSKKQFNSLESVPVQRDLSSPFYLSSNQHTTTTNSEPENLNVETSMSDEAFNADKVTKVTKNKRRRKIFTSPSLQAMVVAQDEVPEGISLADIENKENPSNSNVYSLISLDPPLSTNQGSMGDIVLETKSPIRVEKKKSKKKKKKKEKTSGKE Q9UTL9 YIV5_SCHPO BINDING 290..297; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPAC144.05; CHAIN 1..1375; /note="Uncharacterized ATP-dependent helicase C144.05"; /id="PRO_0000310750" MDRTKRRKIEKEASLLNERNNLLESDFANCYRAFQHQLKLDQQIWRGPEDELNRLKSTIYPVVFWVDGSEKLHAYSFTQRKISLAKNLIPLFSVDLNKDTYSALKAPLKIWSKLWEDNRRLKKIIKYTSYVTVKGSELILSFGISILDSFLAPQDAILSSGSSSSYTALLDYTFLPSEDEEYSCLDINTALFYDCARKLAKSLRFANVSRDPRLSSELLPFQMRVLEWMKRREEEKFLTSNDLPPLWYHCKSLFDDRMVYVNHVYGYMTFSKEKTYLLASGDIRGGILADEMGMGKTLEVLGLVLHHQLPISLTDTCTFDQVVGKNVKYSKATLIITPSTILDQWLSEIDLHVPSLKVFHYQGIRKSNGLKSAKIFLDCDIVVTSYSDLRFELLYTESHSRTLRHEKRHVSPKSPLIDVCWWRICVDEAQMVETSQSNVAQMIYRIPRVNCWTVSGTPVRSEVDDLFGLLFLLRYSPMYLYKKQAWMQIIEKKRVREFCDLFGSLVCRHSKQDVEEELKLPPQHRICMTTRLSVVEETNYQDLLSEAAKSLHFFKDRNLDLCDEESMRRWLVRLRQACCHPQVGFGNKSAFGGGPMKSINDVLVFMLEQTNSTFSSLNRKLYSDKIIVGQIYDHIKDYNKALAIWSEVRIPVELAVKELENVIYNSKYEDHGKNLPINYFGLDHFIHLRVWYVLLHKIYFFIASAYFSLKNEKFENEFYLLAQDLRRKIMSDVIIKTSKHLEEFSEKFIPKKLVKIPRLQKSYAKGLITGHGIIEDYNRLYKELNDQKEVLIKFRDRLIHLMKLPLLDQESDPTGDEYEESLNAQSEISYCIDVYRQMLSDRVAAVSGTINTFVSHETELEKYKLIESIKKSEKSLDKQAEERDKKYLLYFEEREEARPKADQYGSLINIVSRLLDASNRSTSSFETSKNMEEYERIDAMAKEQSRICQKLEKELSIIQLTYNSRIEYYKQLQEISDSLMPPPVSNISLNNYVKDDEKKQKFLNSVIIKASVILEKEISEKQDEASQTTNVAELVNQKISEMNIPGHIHLLRELEEEKSNTQRKIAHFESRRRYLTNLYEHIVLKAESHQICIICRDIIKQGFITTCGHLYCSFCLEAWLKHSSSCPMCKTKLNKNNAYYIGESRDIYSRQEFVTGFNKRDERLEILDDEAYRQISNMELKESFGSKIDTISKHLLYLKHNELYPKVVVFSQWLDVLDVLHKSFEANGIVFIRFDGKSKNTCLKRFKEERSLQVLTLHARSQSSGLTLTNATHVFMCEPLLNSGIEMQAISRVHRIGQTRPTFVYYYIVEDTVEGHILNLSLTKHEQLDKLGLDVPLVGNINRTTEASSGGEQVDAAEIKDCLKMALKRLTTEDS Q9UTM4 TCPE_SCHPO SPAC1420.02c; CHAIN 1..546; /note="T-complex protein 1 subunit epsilon"; /id="PRO_0000128353" MAGLDNAVMVRDDQGNPFILVRDQEKKRRLHGIDAVKSHILATKTVANIVRTSLGPRGLDKILISPDGEITVTNDGATILDQMEVEHQIAKLLVQLSKSQDDEIGDGTTGVVVLAGALLEQAEALIDKGIHPIRIADGYEKACQVAVKHLDAISDVVDFSPENTTNLFRSAKTSLGSKVVSKAHDHFANIAVDAVLSVADLQRKDVDFELIKVDGKVGGSVDDTKLVKGVVVDKDMSHPQMPHRIENAKIAILTCPFEPPKPKTKHKLDITSVSEFEALQAYEKEKFQEMIKHVKDAGANLVICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATNGRIVPRFEDLSSDKLGSAGIVREVSFGTTRDKILVIEKCANSRAVTVFVRGSNKMIVDEAKRALHDALCVVRNLIRDNRVVYGGGAAEISCSLAVTKEAEKIPGIDQYSMGAFADALDTIPLALAENSGLSSIEALTAVKARHVKENKAYLGIDCLQTGSNDMRKQFVIDPLIGKKQQLLLATQLCRMVLKVNDIIVAGSKDDDYN Q9UTM8 SSDH2_SCHPO ACT_SITE 264; /evidence="ECO:0000250"; ACT_SITE 298; /evidence="ECO:0000250" BINDING 242..247; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.16; SPAC139.05; CHAIN 1..493; /note="Putative succinate-semialdehyde dehydrogenase C139.05 [NADP(+)]"; /id="PRO_0000310352" MAPQFKRPELFGFDKSHAQSFVQGKWISSPNNKTFEVDNPATGEIIGKVADVSVEETKKAISAANEAFKTYKNFTHVQRSQLLERWAELIMENKDDLVKMLTLENGKPLSQAEMEVTTCSGYLKWYAAEAVRTFGDVAPSSLQSQNFLISIKQPVGVSALITPWNFPAAMIARKGGAALAAGCTAIFLPAFRTPYVCLGLVRLAQEAGFPDGVLNVITSSDASAHGKELTTNPIVRKVSFTGSTNVGKILMGQSASTIKKVSMELGGNAPFIVFPDFPIDQAVESFCTIKFNSCGQVCVCPNRVYVHKNVYDEFVSKLTEKVKTIKVGDGFDSSSAVGPLISQDGCKKVSKHIEDAVSKGAKITVGGKEISSSKGYFFEPTVLSGVTQDMLVASEETFGPLASVFKFDDTEEVIEWANDSDVGLAGYVFTNNLSTMIHVAKELEVGLVGANIEMVDEPFISFGGIKQSGFGKEAGRLGVQEFMVVKEINLKTL Q9UTN0 YII3_SCHPO SPAC139.03; CHAIN 1..625; /note="Uncharacterized transcriptional regulatory protein C139.03"; /id="PRO_0000310386" MSETTKSGSKKSGQTSRRAIHSCLACRRKKLKCDHGRPCSNCLKRSTIQSCIYIDPGKTNYDKRFERGSEADELIDQLLSRVSMLEKRLNEVGTKSQSDYENQQSHNLPSTPSADAETQRNIGSLSVLDDTKSQYANYSSSSHVLWHLRNYHYLNLDQDIQEENDSLISPFFFRISPNESAYDYLPPKKVSDILIEQFFFRCHMLINVLHRPTFYVRYNDFWEKPHLRKPAFTSLLYAIYASALLATPVEVQKTWALGEDERYLQVDYHQAFRYALASSNFLFEPDLNALQALVLCQVVFDSDRIRAPPSLVGLILHVALCMGLHRDGSLYGLNPVISEIRRRVWANIVLSDLRTSETIGYPPQIVEGNYDTRLPSALPDEIHNVDSSVIISEATFVNIITKVSRAYSKCLKVLLGIIAPNYTRLLELDRELSNFFKELIEVNIPTSNTMHERHIRLLVSYLSNRFPILLHFPFLLKKNSAQFAYSHSRALESATLALNQLYELGSNPEYSKYSWYLWRYPPFHPCIVLLLDLLNSQKIIYLDDERVVLLNKIFSLFPRSSGKEHYQKAWALLQTSRAKVWEKLGLSTVDVSTTDVRLTNFEFFDANNLDINWDDWDAIFQHCPF Q9UTN4 PFS2_SCHPO SPAC12G12.14c; CHAIN 1..509; /note="Polyadenylation factor subunit 2"; /id="PRO_0000051491" MERAENARIIQKPMTRRTVDYGSGLSKYIVNRHLRSNRYHIHVPRPNPNQIINLYPPYEYKYNNTSSLCTKYIHTSANKARHVINVVRWTPDGRRLLTGSSTGEFTLWNGLTFNFELINQSHDYAVRCAEWSTDGRWLISGDGGGMVKYFEPNLNNVKIVQAHEMEVRDVAFSPNDSKFVTASDDGSLKVWNFHMSTEELKLTGHGWDVKTVDWHPSKGLLASGSKDNLVKFWDPRTGTCIATLHGHKNTIMQASFQKNFGSNYLATVSRDSTCRVFDLRAMKDVRVLRGHEKDVNCVTWHPLYPNLLTTGGSDGSVNHYSLDEPPLLSQQKYHEKHPNVTLSASSYLLYPTAEIPFAHDLGIWSMQYHPLGHLLCTGSNDKTTRFWSRSRPDDKESTMDRHHLGEEQSEAMLSQRKAAIEEDDNYEPDENPLTETLANAHNPQFSGVLNLPGLGTMPSFPSPYQHGQPQIPGMLHASLSNSYAEPSTQNSFIPGLTSKSQDGYPQNYR Q9UTN8 UBC14_SCHPO ACT_SITE 91; /note="Glycyl thioester intermediate"; /evidence="ECO:0000250|UniProtKB:P15731, ECO:0000255|PROSITE-ProRule:PRU00388" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000250|UniProtKB:P15731, ECO:0000255|PROSITE-ProRule:PRU00388}; SPAC1250.03; CHAIN 1..155; /note="Ubiquitin-conjugating enzyme E2 14"; /id="PRO_0000361053" MASASPSSSRRLTKEYSDLREHPIPDIRVNLVDDNLFHWACTALGPSDSVYAGGKFHFSLKFPLDYPFQPPTIEFTTRIYHPNFDSEGNVCLAILKQQVFKPSIKLRSVLEQILQLLREPNPDDPLVASIAEQYRNDRPSFDKIARDYVEQFAKS Q9UTP0 RL30B_SCHPO SPAC1250.05; STRAND 55..59; /evidence="ECO:0007829|PDB:8ETC"; STRAND 80..86; /evidence="ECO:0007829|PDB:8ETC"; STRAND 102..107; /evidence="ECO:0007829|PDB:8ETC" HELIX 22..34; /evidence="ECO:0007829|PDB:8ETC"; HELIX 41..50; /evidence="ECO:0007829|PDB:8ETC"; HELIX 64..77; /evidence="ECO:0007829|PDB:8ETC"; HELIX 88..95; /evidence="ECO:0007829|PDB:8ETC" TURN 114..116; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..117; /note="Large ribosomal subunit protein eL30B"; /id="PRO_0000146141" MSAAPTTAPVAAVSKKGKKSGDTINSKLALTMKSGKYVLGYKSTLKTLRSGKAKLILIAANAPPLRKSELEYYAMLSRCSVHHYSGNNIDLGTACGKLFRVGVLAVIDAGDSDILAA Q9UTQ1 PDX3_SCHPO BINDING 20..23; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P0AFI7"; BINDING 74..77; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 79; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 89..90; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 96..97; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 119; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:P0AFI7"; BINDING 137; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 141; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 145; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 154..155; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:Q9NVS9"; BINDING 202; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:P0AFI7"; BINDING 208..210; /ligand="pyridoxal 5'-phosphate"; /ligand_id="ChEBI:CHEBI:597326"; /evidence="ECO:0000250|UniProtKB:P0AFI7"; BINDING 212; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250|UniProtKB:P0AFI7" CATALYTIC ACTIVITY: Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5; CATALYTIC ACTIVITY: Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; Note=Binds 1 FMN per subunit. {ECO:0000250}; SPAC1093.02; CHAIN 1..231; /note="Probable pyridoxamine 5'-phosphate oxidase"; /id="PRO_0000167786" MSENTDSTHEKLIFAPSRYQYEKSSLHRDALMGKDPLVLFNQWFQEATDDEGIKSPESTTLSTARLPSGRVSSRLVLLKELDHRGFIIFTNLGTSKKAKDLKSNPYASLSFWWEPLQRQVRVEGIIERLSREETEEYFKTRPRNSRIGAWASPQSEVIADREELEKRVEEYKKKFGEDESVPVPVPDFWGGIRIVPLEIEFWQGGKYRLHDRFSFRRNTLDEDYELVRLAP Q9UTQ6 RS15B_SCHPO MOD_RES 63; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1071.07c; CHAIN 1..154; /note="Small ribosomal subunit protein uS19B"; /id="PRO_0000130050" MAEENHDEAVRVAELRKKRTFRTFAYRGVELEQLLDLSAEQLVDLFHARARRRMLRGLGPNASRFIRKLRKAKSEAPLNEKPATVKTHLRNMIILPEMVGSVVGIYNGKLFNQVEIRPEMIGHYLGEFSITYKPTKHGRPGIGATHSSRFIPLK Q9UTQ8 HPM1_SCHPO CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600, ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85; Evidence={ECO:0000250|UniProtKB:P40481}; MOD_RES 333; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 338; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1071.05; CHAIN 1..339; /note="Histidine protein methyltransferase 1"; /id="PRO_0000339342" MQANGFSFGFYDEPNNLNGQDVGADSLPSVAIESDSLGHMLKYIPEKLSYARVSGLGHTFVQRELWDVKMQLMEQDDSIESDDKLKVLDGCNDLVPNVYEGGYKTWECSLDLANEIKKIDVVKNNLTTVLELGCGSAIPILSCFQEFYKHRIPCTLVFQDFNVDVLRYVTLPNLLLNWYFCTQEHDSSEKHGTIDVSPSLLQEFSDDLARTNIYCEFLCGCWSEEMQLLIQRTYGDHYFSLVLASETIYSLPSLENFLYMLLKNTKNLALVAGKDLYFGVGGSILEFNSRLQKLVDDPNSLKAIKTSTQNVGRSIVYWEKEFPPSNIDSSPQSPLPGSL Q9UTR1 MMS19_SCHPO SPAC1071.02; CHAIN 1..1018; /note="DNA repair/transcription protein mms19"; /id="PRO_0000356171" MSSNLVALYLFSIDRSQDEANDVVDRIVEEIVTDRMGIVDLVTSIGEYLTDNNISVRAKAVLLLSQTLGELPKDRLPAKHVSVLLQFYLSRLDDEVTMKENALGIGALLNMQNFPAQKIVDVCKALFSSTDMPKYAQATRLNILKVFETIIDNYLFFISSQTRDAFFSGICSTFAGEKDPRNLMLVFSMLKKILSTFPIDGFEQQFFDITYCYFPITFRAPPDATNLAITSDDLKIALRETLVANDAFSKLLLPALFERLKASTVRIKIDALNIYIEACKTWRVGAYLWSAKDFWESIKQEILNSTDAELQNLALGALNTLASKFYKEEGFSSSFTEFVDMILIQLSQRLLEDVNVKSCGSCAAVFASLASISVETFNYCSCNFLPSVLDLPMVNEPLEKQKGMLVFLEYVYKCLVLLYGKWRSKNQADIDNPLLVYKDKQLSFVSGSLMGTAKDETEIRMLALKVIFLMASIKNFLTESELTMVLQFLDDIAFDFSDPIKKKATECLKDLGLLKPDFLLLTSFPFAFSKLTDDVTAKSSSEETFKQYLSVLVSISEERSLFKALVIRLVEMLKDQFKSKEMSVDLVESIVQSLSVAFKERNDRNEQEIPFFFEELLKQLFTLCFANCESMNVRCLIYVSQTINEIVRVNHFEFQEKFVGQLWKLYMENSNSDLIETEGCEKAAERFTLAASLSDQKFLNLVVLLQGGLNGLSKKLHFIEKLNIELLNLLINVVFVTESPGVKISALRLISSLINKCEKDEDISSFISSKGVTSLWDKVYTGTPKESEAALDVLAWVDKALVSRKHSEGIPLAFKLLDTLNLQNVGDSSVKALSIIIKDDPALSKENSYVEKLLYKQRFYASVSPKILEHISTATGGEKSLYLMLLSNVIGNVPKEIVIPDMPSILPLLLQCLSLSDISVKLSTLNVIHTSVKELTSLLTEYLDTLIPSLLAIPKDMNNPTVVRLLALKCLGSLPEFTPTTNLQLFRDKVIRGLIPCLDDPKRVVRTEASRTRHKWYI Q9UTR9 ASA1_SCHPO SPAC1006.02; CHAIN 1..368; /note="ASTRA-associated protein 1"; /id="PRO_0000316564" MVVPTPFYVLRGHSSSVTSVLFDANEYLYSGDEAGFVICWCLTSMRPKCAWRAHTKTILGMQIVKGGALCTHGRDCRLVTWKIDFNCMTDNFMSLSKLAELQNYGPEASSETEKSSAFISIHSNIVVNSLTFCPFSYSPQSKIVVLCNTLNFEELDVYDDESLYHPQTHKEDCGKRLQTRIQPEESVGKTGSVMSTSVTVTDEKYVLLAAGYESGHVVQYICSLENVKTVTLDFKAVWKMVYAYKSHSQPVLSVEYAGSKLFSTGADDCICLHPTPSSIADDLGSLPHPIFRKTKHCGQQNIRIRSDNKILATAGWDGRGRVYSCQTLAPLAVLKYHSDGINSLAFHPGSNVIALASKDTRISLWKLY Q9UTS0 PSP3_SCHPO ACT_SITE 205; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 237; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"; ACT_SITE 394; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240" SIGNAL 1..20; /evidence="ECO:0000255" SPAC1006.01; CHAIN 21..451; /note="Subtilase-type proteinase psp3"; /id="PRO_0000027150" MRVSWISGLLLVAHLAPSSAFNPLRFFLDDTFSSGATEEHFMGPSDDGFALQQPTNYDPSMPFPLDESASAAVDAVSNNYIVMFKPSVDKSKLEQHHRWIEHLHEKRSLDFKDVSTFLMKHTFEIGDAFLGYAGRFSPWLVAELQKHPDIALVEPDRVMHVMTEQTFAPWGLARVSHRKKLGFFTMTRYQYNETAGEGVTAYVIDTGINIEHQDFQGRATWGATIPTGEGEVDDHGHGTHVAGTIAGKTFGVSKNAKLVAVKVMRADGTGTVSDIIKGIEFAFKQSKKDKESIASVVNMSIGGDASTALDLAVNAAIAGGLFFAVAAGNDAEDACGTSPARVSNAMTVGASTWNDQIASFSNIGSCVDIFAPGSLILSDWIGSNRASMILSGTSMASPHVAGLAAYFISLDPSLANHPVELKKYMLKFALKDLLNGIPEDTPNVLAFNNYE Q9UTS5 ZAS1_SCHPO SPBC1198.04c; CHAIN 1..897; /note="Zinc finger protein zas1"; /id="PRO_0000046860" MSNEESFTEKPLKKRSRAHRLGDPRFYCTYPDCPKSFTRKEHLRRHERTHENVKAFSCSFCNRAFARSDVLNRHVQQMHLQKQNLSERRMLNASCFLGFCVLAHDYVNLINARHFMIEHFLSLFAFCRTILFSLLTSFLLVPPPQFFHSEAGERPTPSVGAPSSLASSMDSVRVAPSMLAASHQIVPQYSENNPRVSNEPPRVTIENASLKPFSGYIKSHMSTSNFLNGEPDLNVNVDLSPFPNLPATVPITQAASTANAFQQPSNQFQTQKLPSGLDTRPVSSYPDELTQLESNPDSFSRLDLQGDCTCIFKNRSSIASSRTMDDVVRWLFSSGKRRQKYESSYPYQTQSNQIPSQDQYSDTDSNFLSYYFSASGPMYVPQKCPATVYNNLLNFLEGSFHLQPNFLAMFTLESVSSWLNAYWSMFHVRWPILHRGTFQITQAPLDLLLSMITLGMHSSNDLSIRSLAVEIHTTLRYNIYQKQEFGPPVSLWVYQALFLIQVFELFTSNLKQHRLAQMFHPVLIEAMRQAIPSDALTVRSETFGESNTPLTLQQWHKWITRESVKRIAFFVFALDSTSTLVFGNQPLLYVTDVSMPLLAEEHHWEAENFEVWAAQKPTIEPPTILHMLKAFVQCEQCESPLPKLSPWNMLLLLHGLLSVDISLKQKKFVPGMKLSKREIDGWCSLVFEAYQKWNRCYYSIFLNNNILPFGHPFVKECRSLYNLACIYSKTRLTYLQAFAKAVTDPVDGSVTSKTVAPLRYVKIWANTENARYSTSNALEILDMLLREKIESAPRYDTLIYHSWCYYVAALVLWSIGFALDEENKKTEEVTNLHSQMSRYVTKVRQALEQGEPLFAVVEKSKNPIILHVVLQALDVFPWDLLGEHKKIIQQLLSKGND Q9UTS7 ASPG2_SCHPO ACT_SITE 46; /note="O-isoaspartyl threonine intermediate"; /evidence="ECO:0000250" BINDING 93; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 126..127; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; SIGNAL 1..22; /evidence="ECO:0000255" SPAC977.12; CHAIN 23..356; /note="Probable L-asparaginase 2"; /id="PRO_0000002364" CARBOHYD 37; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 52; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 176; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MWGFIVTCGIFLVLLCQLRLLSKRKSKSTPYNALLPNVTVFAMGGTIAGCANSSLEIVNYIPGSVGIEKLIEAVPAIKAIANINGVQVTNMGSENLTPADVLKLAKLILAEVAKPNVHGIVITHGTDSLEETAMFLDLTISTAKPIVVVGAMRPSTAIGADGPMNLLNAVAVASSNQSMGRGTLVLLNDRIGSAFYTTKTNGNTLDTFKSYEAGSLGIVLNQKPFYFFSPAVPTGKVFFDIYNIKQLPRVDILYGYQGLNPKLAESAVHLGAKGLVLAAMGATSWTDDGNEVISSLIREHNIPVVYSHRTAEGYSSNSCLGIPSYFLNPQKARYMLMLAISSGYSIRDIEDLFSIK Q9UU76 PUF6_SCHPO MOD_RES 34; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 79; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 88; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP1E11.11; CHAIN 1..642; /note="Pumilio homology domain family member 6"; /id="PRO_0000362160" MAIGKRKESTEVKKKDGSMNKRVKVAKLPKKVDSFSPKKKKNTTSSGSSESDSMSQNDKKKDSSLNESEDEDFAGFGESASENDELESAESEAENDEESSSQKSNSKESHAQRKKLQKERKAMKPFADTSLKAKSLWDKLRQKTSIKAEERKTIIAELFDLIRTNVKQLVFKHDMSRVVQTCVKFGSKQQRETICAELAGSYVDLCKSPYGKYLAIKIFKYGTPKMKEVILGEMYGNVVKMIRHREAAYVVEDAFREFTNLQQQRALICEFYGPEFQVFKDRTQDIHIDKLLIDHPEKRPSIMQNLWKTIEGSIAKGSIGFTMVHRAMLEFINHADSNEAKELLNLTKELIYEFVHTRDGSQVAMKLFALANAKDRKVMLKSLRPYLIETAKDSYGHLVVVAALDCTDDTIMTGKLLQAEFEGELLKLSADKFARRILLYVLVGWEDARYFSKENRELLRSLDSLKAKTSKKDPIVRRNELKATIGPLLISLISKAAGDMIAESLASQVLVDALLYAPCEKEEAVDATLKAFDGNPEQDNHLIHQIHCSRALKTLVQNGHWSGAEKQVVKAEDDLKVASKLIVIIKKYLVEWASGDGAFVVVAVLEALSDSEKQEFLKILRKHKNQLNKSEFRGTKKLLEML Q9UU79 NSA2_SCHPO MOD_RES 78; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP1E11.08; STRAND 180..184; /evidence="ECO:0007829|PDB:8ETC"; STRAND 191..201; /evidence="ECO:0007829|PDB:8ETC"; STRAND 219..222; /evidence="ECO:0007829|PDB:8ETC"; STRAND 240..244; /evidence="ECO:0007829|PDB:8ETC"; STRAND 255..258; /evidence="ECO:0007829|PDB:8ETC" HELIX 6..12; /evidence="ECO:0007829|PDB:8EUY"; HELIX 19..41; /evidence="ECO:0007829|PDB:8EUY"; HELIX 45..53; /evidence="ECO:0007829|PDB:8EUY"; HELIX 206..211; /evidence="ECO:0007829|PDB:8ETC"; HELIX 248..251; /evidence="ECO:0007829|PDB:8ETC" TURN 174..176; /evidence="ECO:0007829|PDB:8ETC"; TURN 186..188; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..260; /note="Ribosome biogenesis protein nsa2"; /id="PRO_0000317314" MPQNEYIEESIRKHGRRFDHEERKRKKAAREAHDASLYAQKTRGIKAKLYQEKRRKEKIQMKKTIKQHEERNATQRGSDAQTQGAVPTYLLDREQESQAKMLSSAVKQKRKEKAAKYSVPLPQVRGVAEEEMFKVIRTGKSKKNSWKRMITKATFVGDGFTRRPVKYERFIRPMALRQKKANVTHKELGVTMQLPIIGVKKNPQSPTYTQLGVLTKGTVIEVNVSELGLVTSGGKVVWGKYAQITNNPELDGCVNALLLT Q9UU84 MU170_SCHPO SPCP1E11.03; CHAIN 1..426; /note="Meiotically up-regulated gene 170 protein"; /id="PRO_0000278516" MTEELFSNSETCSLSDPLTSKTLSSIENPFDDPYILSEESEILTIKTDVLRPNILNRKSSFYPEADAPVRKSNLQVKKIFENQVLNCDGIKVAITIPDTSLIAGSLLHGNIWLSYEGAKNVETGVWIKEMFLDFYGILNFKGHSEPFYSISEKYSFCNLKTSALILSKAASASIGNKGLFLKCSCKVGFPFSFIVPLDIGPGTYHSSKLELLYYISSTLTLTSLDQNIRCTRCTIPKRVITSMHNNIAELYNPISCIKSLPYLSLEEAKTTLEVHTDRSLFFSGQIIDFTICYTHNHHRRIHNIKARLLETHIFHPNTQNHYGGYCMNQAEETFASCGYLKRYQKTKTKTRAKSTWKIANKSVYSNLAPTLKNTIHAQIKIPEFCRSVNLKDQLKIDYTLEVCFSAFFKPRILSIQIPITILHSWN Q9UU86 SYG1_SCHPO SPCC1827.07c; CHAIN 1..682; /note="Protein SYG1 homolog"; /id="PRO_0000116894" MKFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAKNPSEGLYGTSGILGETPEEAIVKRGQIHRFHPLFQEFLDQQANKVEEFFENLVSDARERMDLISDQVDIYEKLRAFKKGTLESGSVVLIQKQHSKLRQRLDSILNFSRLQPAYHIPARKSVPTDAYTPMVSYRKLKSKLKTTLLDFYDYLKLVSQYQHLNQQAFRKIVKKYDKTLHTDLQGFWVDYMSRYTFTDFSITTNWQLHVEDIYARLFTNHNKKLALEHLKSFRQKEHFSANSMRFGLLFGAGLPLAIEAACYYNATEQSSYLLQIWGGFFLVIFAFVLFDLDCYVWEKTRVNYMLIFEFNQRKSLNWRQHLEIVGAVFFIFSLFFFLCMRNFFPGFTIYFPALFLGVVGTFLIAPVIVPYWRMRRYLIIQLIRVFLSGLSTVHFQDFFFADQMVSLTYACGNISLFFCLYKRLWRQPQLCNSSHSPLLGFFTTLPGILRVFQCFRRYSDSLKSFPHLVNALKYIFNILAQMFLSLWRIHPGLKYRVLYTIFAGVNSLFSYTWDILMDWNLLVRKDGRWQFREHRILKQLWPYIIAMILNFIVRSSFIFYCIFPNHIQHSSGISFFVTLAEIMRRCMWNILRVEHEEIYNRENLRAARELKPLDFVKPHSDVFVSHQISSDKNYTDDEDSMDDQTDVDEAQFS Q9UU90 POP5_SCHPO CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; SPCC830.09c; CHAIN 1..139; /note="Ribonuclease P/MRP protein subunit POP5"; /id="PRO_0000140014" MVRFKSRYLLFEVLYPEAKEFFDYPTIPSDSSITTSSLSKIIRTMVAENFGDVGIGKVASSLTVKYFSPNTSTGILRVSRQHFRLAWAALVLIRELYGKPVIIRVVRVSGTIKKAELAAIERNKSEIHNISLMDEPIEV Q9UU94 EPL1_SCHPO SPCC830.05c; CHAIN 1..557; /note="Enhancer of polycomb-like protein 1"; /id="PRO_0000214165" MSSVSKNARAYRQRKVGIKTVMPIYFERDIPDFDEEASLQRTVPLVESGVEKEEEEEKHLQQVINEAHEAIVRGSEKKLIIPTREAKNIGIIDKYYKKNFILPKTLIRFSLTVEECTNPEYCMDEHDTEYFLKLKQAQPSLSKFSELDFEIVMQTFEEEINQNQPFLSMDTSQILPLSELITSFELKDVLYLKPLASQVYPYWRERRISKGGLPIMAKAQVGDDKDDDDPYVCFRRREIRQARKTRRSDAQSYDRLRRLRQSMETSLQLLEQVYKREQKKLQALEDDYAIFQKRCLVKKLKRTLNIKDSDELLINPKRRPIEVKPAAPVPTPAPPVKTSPHPASYRPQPTRNVEVRPLLMLDDVQSAQITQFQIRLQQRLTKKEQLDRNWVDLLETPSTVIHTNYPDSFYRNIIPYYSGKETKQSHNQLSIPSSTPSTPLSDNGPTYSTPHSSLSNFNTCDSLSFSSNNSLYGYSTLLHPRNPICVRQRIGRGGRLMLDRTRALPVHRLSKPKSRVEDRWLFDIPFDADDTIILDDESDASIMFRASLLNDDMGTQS Q9UU99 YJX4_SCHPO MOD_RES 525; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 559; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 888; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 890; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC23B6.04c; CHAIN 1..1008; /note="CRAL-TRIO domain-containing protein C23B6.04c"; /id="PRO_0000210750" MKDSEHHHHGHNGFSKFLHKLGFGKSKGKSHKSNTSSIHERENTAAKGPASNVRPARPNVSTSSTSNEVRKSVPVGNPTVHTKTGSSSSPASKMRNTVNLQHIQAANQKTRNAEGERKVAQRRVQSDKAEANDAAMSSSAPTVDVSEGNSAAEPKITPDDSDTPRLNVDMNDKINVDEAAAKSDSKLNVDQINSTTESEKRVEKVNPNIANNPLKSPDAVAYSSETVSDEKQPTEHPVSANVPAKSEKAVCDENTKISLTNTEHYKFHSLRGDVEVVVGDLERDGRDTSLGDASVNEAAKETDVDSSRFISDEKAVTEDAMKTEHASNAPLTDERHFQFHSSEGDIEGIVGTMQRQRQSVSSYDTIVPSQFYKQKVVQNSPPSLLSTDNKIPESGSDHPSSQDNSSKASLVENSQTQSSTPRKPLPTTTSPKVNPEPHSESISDTRPSTPRKVPPSTVPKMNPKLQGGNSVTAPSTPSKVLPAMSPKVAPKFQGGRSSTAPSTPNKVLPAASAKAAPKLQEKAASFDIPNKSTIISTKSTVASPIKANENSPALKSKASFEFPKELDPDGTWNAPIPYPDANCPMAPTYRNLTSEQEEMYEEVLKYCLELKEIPVASNSSKKTDLIELERLWLTRECILRYLRATKWHVSNAKKRIVDTLVWRRHFGVNNMDPDEIQEENATGKQVLLGYDKDGRPCLYLYPARQNTKTSPLQIRHLVFSLECAIDLMPPGVETLALLINFKSSSNRSNPSVGQGKEVLNILQTHYCERLGRALVINIPWAVWGFFKLISPFIDPITREKLKFNEPLDRYVPKDQLDSNFGGSLHFEYHHEKYWPQLVELCKSRRLGILEKWRKMGSKIGTSEWDLKGGEEYVELMQQYVRPSLTNRSSSPTVTPTVNTDRQPKTLTNSADELSPQKRRVENPKPVVKDEGPVSIVEDEESTPVVTKKEDSIPVAQSTKADAGLDAENDLLPKSGSGVSETPAFSHARDVSTASFSDAVSFITADSIE Q9UUA1 YJX1_SCHPO MOD_RES 328; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 408; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 409; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 421; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC23B6.01c; CHAIN 1..479; /note="Oxysterol-binding protein homolog C23B6.01c"; /id="PRO_0000315947" MPHEKQDRDAEEIEDEGKNIILGIVSQLRPNMDLSKVTFPTFVLEPKSMLERITNFMSHPDLLLNVQKTADPEMRFLDVVRFYMSGWHIRPRGVKKPLNPILGETFTGFWKFPPSNSKDPNLQKLHGIAVYAAEQVCHHPPISAYFYLCPEYKVRIDGVVKPRSRFLGNSAASIMEGIASIKLQDLDEEYLITQPNVYARGILFGKMRLELGDHVTVRCPKTDLQADIEFKVKGFISGTYNSIAGKVKRVSTGEVLYKISGKWDSEMSVESVKTGETRPLLDVSKHDVYLVSARPLEEQGERESQRLWYKTCQAVIARDQTTATETKSAIEDRQREEAKQREIENVQWKPKYFKMIAPEEYILNFDIPNGKSDLEVLCALDEFIPIFSEVDRIAFHKFLSENTKPEDSSIHKHSRDASGDSTKGFAEHMPAPARRRRPQSTASFVTYRSDNGSVDEYHDAQLPDPNTLSKLHEEQDPAL Q9UUA5 MTXL_SCHPO SPBC409.19c; CHAIN 1..450; /note="Metaxin-like protein C409.19c"; /id="PRO_0000358933" MLQLFIYSPGLGQPTMDPGCLAALIYCALAVPKDEIEILRTANSGMSPTHKLPALWDGHVWIGSLKNILIYLKQKGYNLDNFDAKQLANVMAFTSLLEGSVNDLWLLEAFVNEENFVEAIRPAWSKALKFPHNYLTPNALQRQAKERLAQTLGIRDEEVSYEASRMPISHKWTNATRHRQALLRTQARRIRISSLARQVYGSLESLISDSKFIFGEKPTSLDCLFYAYLSFHAFTNELPQATLRPCLQFNSPKLYAYLKSLRETWFSDDSNILSPLSIKVQPENLLTIARLAWNNVTAKANDTRKSITKFSVPPERKLLWARNGFFIFASAFSFVWFVISNGIVVIETEDDEASFEEVDDAKESIQEKEIDETTESKATHDSSETSSSKELPKEEEKESSSFDLQPLSAQDLLFSGFAEDEIMDEEFGYDDDDDEEFDLDDLDDLEEEIV Q9UUB4 PUR7_SCHPO CATALYTIC ACTIVITY: Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443, ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6; SPBC409.10; CHAIN 1..299; /note="Phosphoribosylaminoimidazole-succinocarboxamide synthase"; /id="PRO_0000100928" MALLKTSLDAPFTKIATGKVRDLYECVEFPDDLLFVATDRISAYDFIMENGIPEKGKVLTKISEFWFDVLKPHVQTHLITSRWEELPPVITKHEELKDRSMLVKKYKILPIEAIVRGYITGSAWKEYQKQGTVHGLNVPTGMKEAEAFPEPLFTPSTKAAEGHDENIHPDEVSKIVGPELAKQVAETSVKLYKIARDVALKKGIIIADTKFEFGVDETTNKIVLVDEVLTPDSSRFWLASDYTVGKSPDSFDKQYLRNWLTANNLANKPNVSLPEDVVEATRRKYVEAYEMITGKKWSY Q9UUC1 RL21A_SCHPO SPBC365.03c; STRAND 139..141; /evidence="ECO:0007829|PDB:8EUY"; STRAND 144..146; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..160; /note="Large ribosomal subunit protein eL21A"; /id="PRO_0000149680" MPHSYGIRARTRYTFQRGFREHGQIRLSTYLKTYKVGDIVDIKVNGAVQKGMPHKYYHGKTGVVYNVTQSSVGVLIYKVVGNRYMEKRVNVRIEHVKHSKCRQDFLDRVKANEAKRKEAKAQGKTVQLRRQPAPPAKAHFVSTENNEPVTLHPVAYDTTI Q9UUC9 MDM34_SCHPO SPBC19C2.11c; CHAIN 1..452; /note="Mitochondrial distribution and morphology protein 34"; /id="PRO_0000351437" MSFRVKGWSDQFSESFYERATTLLTAALNKGTKHSMIADHITVKELDLGPQPPQLEILEVGDLAPDRFQGLFNLHYSGDASLVLQTKIRANPLSVQKSNVPSFSSRNTMLASRAPLTVPMFLRLSDLKLNGIVVLVFSKQKGITVVFRNDPLESVRVSSSFDSIPAIARFLQREIEVQLVSLFQEELPSIIYKMSRIWFAKSDSNLSFQKIPFTSPNQSHTSLANYNPDLLDGPPDYHESTKVDTHLPIKMGPLDVQTHPNIRSIASLALSRKALLPISSPSIPMSIYRSTPPDTIIQQLTTQSDDISAVSSPATQYSASDYLGSNDTTARPSIFGRSHGTSQFRRRERVKKRHVIKIHEASNKSASSSETFVGSKNVDLTESAFDSIPDTPTKIITNINKLKRNYTITNNWLENLQQKIPSEVDNGKVSGLQYSAFKLLMLQRLMAAKGSF Q9UUD2 PRP38_SCHPO SPBC19C2.08; CHAIN 1..210; /note="Pre-mRNA-splicing factor 38"; /id="PRO_0000328925" MADFLARDYRSQGEAAHEMLPTFLIGKILRERIVDSIYWKEQCFGLNACSLVDRAVRLEYIGGQYGNQRPTEFICLLYKLLQIAPEKEIIQQYLSIPEFKYLRALAAFYVRLTWDDVEVHQTLEPLLRDYRKLRIRTNSEIRLTYLDEVVDDLLNAEVVCDISLPPLRSRLQLEDLDLLEPLSSSSDEEDDDEEQISKLESNEGAVDRNI Q9UUD6 UBP11_SCHPO ACT_SITE 59; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 302; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10093" CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPBC19C2.04c; CHAIN 1..350; /note="Ubiquitin carboxyl-terminal hydrolase 11"; /id="PRO_0000080611" MSTTPLSISRAKKYKTVFKGAAILTTFAALYIVTSPSTGKRLVKNASIKGLYNVSGNDCFLNCVLQSLASQESLLEILKLRCSSSTLYATLYELLQKLNSGPGNPITPGSFLNSLEIATNKKLVRSIQQDAQEFLQHLVETLELQKPHTYKWSKVLSFPVDSPFIGTMEQKVQCCQCLAISISYSTATSIQLCLPPEYSGNSNVSLLSLMEADREQHISDYKCDSCFKSSPKHSKTSCIRTVDWKNPPTILQIQLERTSYTCQGLTRNNVSISFPSKLILKNKHHYILRSLITHSGSVTYGHYLCYRLQDDIWWKANDSLITKSSLNEALSQTRSACLLFYEMESPLALD Q9UUE1 PYC_SCHPO ACT_SITE 326; /evidence="ECO:0000250" BINDING 150; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 234; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 269; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 578..582; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 579; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 651; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 747; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /note="via carbamate group"; /evidence="ECO:0000250"; BINDING 777; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 779; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000250"; BINDING 912; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1; COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; MOD_RES 747; /note="N6-carboxylysine"; /evidence="ECO:0000250"; MOD_RES 1149; /note="N6-biotinyllysine"; /evidence="ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU01066" SPBC17G9.11c; CHAIN 1..1185; /note="Pyruvate carboxylase"; /id="PRO_0000146823" MTSKYDALLHNQSTNTNPFSKLQDRSSLLGEKFTKVLVANRSEIAIRVFRTAHELSMHTVAIYSYEDRLSMHRQKADESYPIGKVGQYSPVGAYLAIDEIVSIAKRTGANLVHPGYGFLSENAEFARKVNEAGMQFVGPSPEVIDSLGDKTKARAIAIRCGVPVVPGTPGPVEHYEEAEAFVKEYGLPVIIKAAMGGGGRGMRVVRSADTLKESFERARSEALASFGDGTVFIERFLDKPKHIEIQLMADKAGNVIHLHERDCSVQRRHQKVVEIAPAKDLDPKIRQALYDDAIKIAKEVKYCNAGTAEFLLDQKGRHYFIEINPRIQVEHTITEEITGVDIVSAQLHVAAGFTLPEIGLTQDKISTRGFAIQCRVTTEDPNNGFAPDIGKIEVYRSAGGNGVRLDGANGFAGSVITPHYDSMLVKCTCHDATYEYTRRKMIRSLIEFRVRGVKTNIPFVLRLLMHDTFIQGNCWTTFIDDTPELFQLYRSRNRAQKLLAYLGDLAVNGSSIKGQNGEPALKSEIVMPVLLDSTGNQIDVSHPSEKGWRKLLLDNGPAAFAKAVRNHKRGLIMDTTWRDAHQSLLATRVRTIDLVNIAPYTSHALASAYSLEMWGGATFDVSMRFLHECPWDRLRRLRKLVPNIPFQMLLRGANGLCYSSLPDNVIYFFCEQAKKNGIDIFRVFDALNDVNNLSLGIDAAKRAGGVVEATMCYSGDMLNPKKKYNLDYYVNLVDKMVEMGIHILGIKDMAGVMKPKAARLLISAIREKHPELPIHVHTHDSAGTAVASMAAALEAGADVVDVATDSMSGLTSQPSFGAVLASVDGTDKQLEFDNNQLREIDSYWAQMRLLYSPFESEIKGTDSDVYNHEIPGGQLTNLKFQATSLGLGTQWAETKKAYIEANKLLGDIIKVTPTSKVVGDLAQFMVQNKLSAEDVENRATTLDFPASVLDFFQGLMGQPYGGFPEPLRTNVLKGRRQPLTDRPGKFLPAADFDAIRKLLSEKFGVSSDCDIAAYTQFPGVFEEYRQFVDRYGDLTTVPTKFFLSRPEMNEEMHVEIDQGKTLIVKFVALGPLNPRTGQREVYFELNGENRHVTVEDKKAAIETVTRPRADPGNPGHVAAPMSGTIVEIRVKEGAKVKKGDIIAVLSAMKMEIVISAPHSGVLKSLAVVQGDSVNGGDLCAVLEHE Q9UUE2 CSX2_SCHPO MOD_RES 625; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 653; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 655; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17G9.08c; CHAIN 1..870; /note="Protein csx2"; /id="PRO_0000074223" MTGHVDPVHFERLKIQSVTFGSANDNASLQVHNVSKSPEYSKYSYSRKNNEPIEFIQLREEEGPIVKVEEEDGLTLRFQLEFHAQEGKRDVTNLTCVYGTSPQQLDRLITREFSSDANFQNNHQVFLIGNIEFHSNENSKKIEWTWSNQSLHTLYFRNGGSPIYLCFAEYDKRLNCLVPLKTFQFYVTESDQDSTPATPFPMPMHLAEETATSPEISDAPPLSGNVDPLPINSPPLTNPVARDIDQTEPEDGPLFRATILNYERTTHDMRMVLKKLIKRIEHVAHSHGLLYMSYKELMSAFERVATINPPAFKPFLDHYYAAAAQSFDSFNIDRARLLRNFLIEPLRKIYDTDIKNVSTKKKDFEETSRDYYTSLSRYLSKSEKETSSDKTKESKFAAKKRDFELSRFDYYSYMQDINGGRKGQEVLSVLTSFAANDYNLIHSSLTDIDALRPSIIQLQDIVTEANKEFQLLRAEREERRRYIETSSRELEDKDAEIAAQAYKAKVDQDTSAKQGLLLAFSKSTSDLQVVGKSGWHKYWVVLDHGKICEYANWKQSLELHTEPIDLLMATVRPAQSVSRKFCFEVITPQTKRTYQATSKAEMHSWIEAIQYSISESIVQKGKGTSMNSEETSVKHGPTSTIGKALQRVASVTSPSRHNSDSKEKKQTKSPSLVKTLKEMHSSDQSCADCNTTARVEWCAINFPVVLCIDCSGIHRSLGTHITKIRSLTLDKFNPETVDLLYATGNSFVNEIYEGGITDWKIKNFENQERRVQFVKDKYLYKRFIKSSFSHDPNTGLLESIEHSNLKEAVLCLALGADVNYQRAVVKALLKNNYLIAELLTLNGASLNVDEVTMETLSARAQAFVMNRATP Q9UUE6 SYKC_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; SPBC17G9.03c; CHAIN 1..591; /note="Lysine--tRNA ligase, cytoplasmic"; /id="PRO_0000315953" MSEEQVNGVTQAVKALVLDPVTGEQVSKTELKKREKQRARELAKAKKQAEKAASAPVAAPKSSSKKEEDLDPSQYFENRSRTIMELRQTKDPNPYPHKFQVTITLPEFIAKYEGLARGETKPEVEVAVAGRVLGLRTAGNKLRFYEIHADGKKLQVMCQAQDADTVDFAAQHEHLRRGDIIGIRGYPGRSNPKGRADGELSIFARQCVLLSPCLRMLPKEHYGLKDLEIRHRQRYLDLIMNRSTRDRFVMRSRIIQYIRHFFDSRDFMEVETPMMNMIAGGATAKPFVTHHNDLDMDLYMRIAPELYLKMLVVGGLDRVYEIGRQFRNEGADLTHNPEFTSIEFYQAYADYYDLMDTTEELLSGLVKDLTGSYKVPYHPEGPEGPKWELDFSRPWRRINMIEYLEEKLNTKFPPGDQLHTPEANAFLRDLCAKHGVECAPPQTCSRLLDKLVGEFIESECINPTFIIGHPQMMSPLAKYHRSDAGLCERFEAFVATKEICNAYTELNDIFDQRARFEEQARQKAQGDDEAQIIDENFCTALEYGLPPTGGWGMGVDRLVMFLTDSNTIREVLLFPHMKPEVQAAEPTVVKE Q9UUE7 CDC73_SCHPO SPBC17G9.02c; CHAIN 1..371; /note="Cell division control protein 73"; /id="PRO_0000339173" MDSLLLLKKSIAEKKDVKLLASSEATSKVEKIEDAQYILFDENTSPILIDEPTKFIKLENDSHFSLRSVYFAWLLRDTSIAEYIQQCSELGIQNLTFLERTDLISWLEGSSDSEHIIGLEKPKPEGSTDAATSMDVDLHKKSEEVNWLFENTRTVSNHNSVLHGIKPIDFISLRKDVLDYIHANKATASAHADEQERPAKKRNRDPIILLSPSASSLLTMHNIKKFLEEGIFVPPAEAAHAAGGGRGPELIALSHKSSNSKFGTMRFIIVEGTEKFKPDYWDRVVCVFTTGQAWQFRDYKWSEPHQLFHHVKGFLVQYVGDPPHPATHDWNVEGIFVERLRRHTDREVVSQLWDKLERWMENRWPLWNGRR Q9UUF1 YNF8_SCHPO BINDING 124; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 124; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 161; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 187; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 235; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_label="1"; /evidence="ECO:0000250" COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; SPBC17A3.08; CHAIN 1..312; /note="Deoxyribonuclease Tat-D"; /id="PRO_0000317086" MASIRQAFVKSLRFYDIGYNATDPVFRGIYHEKLKHPDDFDSIISRAKAVGVEKMMITGDNVENSEEALNLATNYECFTSTVGVHPCQAQCFLRHSEGPEDYLVKLEALANKGKASGKVVAFGEFGLDYDRLHYAPADVQKMYFEEQLKVAVRVQLPLFLHSRNAENDFFAILEKYLPELPKKGVVHSFTGSIDEMRRCIEHGLYVGVNGCSLKTEENLEVVRAIPLEKMLLETDAPWCEVRPSHAGHQFLKTKLPFDSCKKERFKEGCMIRGRNEPCNTYIVAEIVAALKDISLEELSEQIWENSINLLSK Q9UUF2 SYMC_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215; EC=6.1.1.10; SPBC17A3.04c; CHAIN 1..782; /note="Probable methionine--tRNA ligase, cytoplasmic"; /id="PRO_0000139268" MATYKVQIPASFKTSYSFAESLKVSIAISAFSVKVPCEGAANCNSVRLVNSKEPEKYVSDANAIVSFLYWKQEEDLFNSFISSKLSILDWEALQFTPKAYTAKTKEDFAYLLSQLETIFKENEILNEFTPVEVALASDIYFCVLNGAPVREYPLLSAWYLKIEKQKPFVQALKLTFEKTLGQPAVTSTEKIPVSETTRNVNSQHLMRERVPGEKILPKSNERNILITSALPYVNNVPHLGNIVGSTLSADVFARYHRARNHNTLYICGTDEYGTATETKALEEGVSPKELCDKYHALHKEVYDWFEIDFDHFGRTTTPKQTGIAQHIFTKLYNNDYMAIDTMTQLYCEVHQGYLADRYVEGTCPKCGYDDARGDQCDGCGGLLNAFELIDPKCKLDRATPVKRETKHVFLSLDKLQPAVESWAMQSAVEGKWSNNGRSITESWLKEGLRPRCITRDLKWGTPVPLEEFKGKVLYVWFDATIGYISITANYTDEWEKWWRNPEQVKLYQFMGKDNVPFHTVIFPSSLLGTGEKWTMLHHINTTDYLNYETGKFSKSRGVGVFGNTAQDIGLSPSVWRYYLLSSRPETSDTMFTWKEFITRHNSELLANLGNFVNRTLKFTTAKYNGLVPHYLTDPSVGAGKLKADFVKDVNALLAKYNAALEASKLREGLRLAMEISARGNQYLQDNRIDNKCYLYERQKCADAIGYALNLIYLLAAIFYPYMPSTSTSIYKQLNAPAAAIPDTWELCLLPGHRIGEPEYLFTRIDESMEEEWRSKYGGNGSN Q9UUF7 COPB_SCHPO SPBC146.14c; CHAIN 1..940; /note="Coatomer subunit beta"; /id="PRO_0000193838" MSCWTLVQQDFLEAPSVDALKTSLESKNDYVKISAMKTILRVVINGDSLPSILMHVIRFVMPSRNKELKKLLYYYWEVCPKYNNDGTMKQEMILACNSFRNDLQHPNEFIRGATLRFLCKLKEPELLDPLIPTVRQCLEHRHAYVRKNAILAVFSIYQVSNHLIPDAASLAEDFLAAESEGTCKRNALIVLFTIDPEKAKAWLLANFEQIPSLNASSLLVIIEFIRKVVLTKADGLEKLRFQSLLVSLTATNNSSVVFEAATSVINVFPDAESLKLAASRLLALADREADNNAKLIMLDRISQLAARDKSILEDLITDVIPFLSSSDFDVCEKAISIIMGLVSSRNVEDILNHFQKELTKSNGETEKDDGRRRALTKAIHSCAINFPHTAATAIQYLLSHISDFQSKSASSVLSFIKEVMEKFPDLRSSNITKLLLSLKELRAGKIFRGVIWIAGEYCLTEDDIRVAWKSIRASLGEVPILASEEQLLKDVSNVPEDDLLIDISAPASTSRKVLPDGTYATESAVTSEALSAARLEAVKASKKPPLRTQILSGDYYLAAVLASALTKLVMRFARLSFDKERLNALKAEACLIMTSIIRVGQSKFVKYTIDDDSVERIMNCIRAIYSFEELPEFQTVFLDDMRKAFSSLVAQSDKRQKEADLLVNGSDAVQADELLNIRQFQRVIEEKQDLNFESDIIQATNDGMVVEDLASKLDHIVQLAGFTDPVYCEAYVKIQQFDIILDILLVNRTDTTLQNLSVDLATLGDLKVVERPPPMNLGPHAFKSVQATVKVSSTESAVIFGNIVYGGKASDEDKIVVLNGIPVNIIDYIKPAFIPESQFRSMWTEFEWENKVDISSNEDISLYDFLHKIMKKTNMNCLTPDASLRGDCGFLSANLYACSIFGEDALMSLSVEKSVSGPISGHVRIRSKTQGIALSLGAFV Q9UUG2 YFT6_SCHPO MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 271; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 274; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 290; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 292; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC926.06c; CHAIN 1..621; /note="Uncharacterized leucine-rich repeat-containing protein C926.06c"; /id="PRO_0000312229" MGSTVDGEKYIRNLASYIRSHEKRFARAPYRAPNHSIFSDRPVQLQLTVHHLYYLLTKFEELGVNTGPLNIRIENLHSETFPSDYTSFLNQSPKKNDFDDNMSLNSIVTMGSILSNVSSVWSIFSTAPSEASETRNKQRILAILRYIYSCFTKLPAISLVYNPKTPLISQYEEFPLDTAVPITVFKNLSSLEIRGYDIRSIFGWDFLSTTLKSLILHHCDLADLSEVLIKLVLDDAELYRFRSSRQTYPQQPNSQPCEQHPAHANLRRSVSLGSKDYLKSSHPPVHKTLSQSVLVLSKDGNASSSGGTENQSANSSSSLMEKDAILSSSSWSQLLYLRCSSCKLKSIPKNVFLSLQSLVSLDLSGNELTEIPYALGELPQLCSLNLASNKITGCRTFYHISLSHLQILVLSRNHLTSLSGLENVPSLEKLDIRDNSITDVVEFRRLVGNTNFEEAYLSLNPFTKTYSSYRITIFNYFREYPGSKDIMLDGRGPGMLEKMYLSEKASAPERVISLNPVNQKSHSPAIKSSSTLRKASKTRIVDLSAPNSAVFSKNASGGDTSSNVSLLNGSASEEIPQNTESGQVFRKKIEMLRQEAGPEWVDALMKESVVKHKFRNKDESV Q9UUG3 DPH4_SCHPO BINDING 97; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"; BINDING 99; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"; BINDING 121; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"; BINDING 124; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00456" SPAC926.05c; CHAIN 1..139; /note="Diphthamide biosynthesis protein 4"; /id="PRO_0000071152" MNHYSVLNLKDGKTYTDDEIKEAYRKALLLFHPDKCKEKPSVVYTIDQVKEAYQVLSSEKDRQQYQIKQEEESSHYYSIVDLSEFEELDNGSYYYPCRCGDLGGYVVTEDDLENNRSVVPCMGCSLTIQVDYEIAESDS Q9UUH1 VPS55_SCHPO SPAC630.11; CHAIN 1..128; /note="Vacuolar protein sorting-associated protein 55"; /id="PRO_0000316619" MSDLRKIIGLSSVLAVGFMLVILSCALFKNWYPLLIVIPFILAPLPNLLTKKYSTSHDFLQEEDRNLLDFGRFTFGATICTGFALPIVFVNVGLIGTAAATMSCVGGSIIFLVITLYSQAFVQHEEEF Q9UUH3 MUG58_SCHPO BINDING 32..39; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:Q97QZ1" SPAC630.09c; CHAIN 1..277; /note="Uncharacterized kinase mug58"; /id="PRO_0000214077" MSSLEIIVDKILKFLEKQPKPEGRPFILGISGPQGSGKSTLASALDTELTRKNESVVKFSLDDFYLTHAEQVELAKNNPNNPLVQHRGLAGTHDVTFLNNVLNAFVKGSDEEVSIPFYDKSKFGGYGDRGDESQWKKANPKTTTYVIFEGWMVGFEPLDSCMLSVRARSTRWQNIEGSLLWVNRKLADYQPIFQKIDSLVELEAQEINYVYRWRLQQEHALKARIHKGMSDEEVIEFVNHYMPQYVFYLGTLSNKVHLNPHCLEIILDENRYPVVMH Q9UUI4 NOP53_SCHPO MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 249; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 252; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 256; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22F8.09; CHAIN 1..419; /note="Ribosome biogenesis protein NOP53"; /id="PRO_0000218964" MGIKERNAPSQYKQSSRKNKRAWRKNIDLEDIESGLEQTRDEEIKGGNVEHKPNDALFVIDTLGDDRIAKRSRKKIKPLKVDQILENKSSIEKVHSHLTNNSTESNKKGKIFSRKELNRLQALVYKNKDGLTATSAASELKNTKQPKESYDVWETNPTVTIPVKRPSTLSKLPESLTENNAKVPNVVIADPGMSYNPDAAAWMKLLDTKGSEELKKEQKRISELEEKERIQKKAFEDKGLVSDQDVNHSIDSDDQSEHEQAETPIPSSKNKRKTRSQRNKIRQRREEELRLLEQKKNEELLRTIDKAPAISKKLQQKDKAEKFSNKAVSSSTTEIKLKKKKFGKHRLPNNPLEIKLGDELTSSLRELKPEGNLFADRYLSLQQRAMVPPSLPVLKKSKYRAKIKEKYSHKDFHLQKNSI Q9UUI7 TPSY_SCHPO CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; MOD_RES 88; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 108; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 109; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22F8.05; CHAIN 1..891; /note="Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 100 kDa subunit"; /id="PRO_0000122513" MGRQFICSIYLPYTINFHLDELEGNHESHPAITHQEKVTQTHRDSVKIDDILTRLSISKSESGQATPVLTPQLEGMNDYFSLGPSKRTGGSMTPGLGAMSPIPGSGRSSPLYTQPRSRATSPSRVRQADRFAAPGIGAGALPIRRKRRDSLAKSVALFESARWSVERGVVGNSGLFHAVDAAVRDHGLQNPLWVGLLGMPTESLSEKTKNAISGALLVKHQSLVVYTSDSNFEGHYNHYCRKILWPSLHYQHNEIFSFFHEESNWDDYVAVNRAFADALIKNYKTGDTIWVNDYHLLLVPNMVRERIPSAIIGLFIHVSFPSSEVFRCFARRKELLQGMLGSNLIGFQTEEYKRHFLQSCSRVLYAESTFDRILLDDRYIDVYAHPIGADPVLVDKWLENPETLEVKEVLEKRYANLNIFVGCDKMDPIRGIREKLLAFEQFLYDNPEYQKNTILIQTSTFTEEQKEYGVAISDIVTRINSAFGDFSLDHLPVTILSSDLSYPQYLALLSVADAFIVTSLREGMSLTCHEFILTQRQKKSPLIVSEFIGCASMFSNGAFIVNPWSTLELSLSMKKALTLSTNERNQRYSNCLDVVLTHSASNWVTGFETKLKKSWTSQQKRDFSRLPRFTLNFIGNRYDHAKKRLLILNFDGNAVTWEGRHEFVDFHYGYMVSILSKLIADDRNIVYIASCLEEDELESLFMHVPGVGLIAENGCYVLPHYAENVHQSWIRLYKKQQMDWREPLHDIIQYYSERTPGSSLIDHGFAMEFNYVKAENRENGLRSAGELASSINETQHGCRAVPLDGRVLCEPTTISKATAANYIMTHLIKNPEELDLILVAGNNRTDESVFAWANKSKVSSFTVSMGVGNTEAKAYTDGIPSFFNVLNSLCA Q9UUI8 YIY4_SCHPO SPAC22F8.04; CHAIN 1..383; /note="Uncharacterized transporter C22F8.04"; /id="PRO_0000116799" MSSKLTVNAHYSPLKDEDPLDHIDSQTALDSMETDSTGKSSLYFSKSDDPLSKDIEDGISTRKLEEMSVLEANAKEPDSENAPVSRLTIFFAVSSQIVFAILVTILNKQALNIINAPLLMLSFQMAFTSLMVKMYWRFSSVHFQTLRLASAIQLKKFIFVKILGIVSKTYCLAFVPVSFYQISRGLLLPFTILLSFVLLKQKTRLFPFGGCLLVMLGFGFGVRFESHVAPIGIILGVWSSFTTAIESVAVKHYVHEYPTLDLIYIFSALMSVFCLLLSVASLELLHTVQEVVGMQAIKFFIVLILSSLSNFYLNIATFTQIKVTSPVTYMISVSARSILQTLLAVAFLGETLYGNRIYGVILILVGTLLYTLAKEHERRVASA Q9UUJ0 PVG5_SCHPO SPAC22F8.02c; CHAIN 1..372; /note="Pyruvylated Gal-beta-1,3-epitope synthesis protein 5"; /id="PRO_0000076297" CARBOHYD 38; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 128; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGLPLRIFAGNGIGGWCLRLFLFGSLILLLRPLIFYSNTTMKKLKTEYPIYHRHLSALKRNFYYTMDAQLGGIRNVVLINRPCFAASDNFLTLMGQNWYLKERNINVLSDICFPLSNNAHDSLPTFNNGSDLFNPLYFAVLNAATPARFTFHLFNHVMDSVVPFDEAKKFKVRSFPINYAEYADDECQLALKKIRPIPDKYLVSTRVLSDSRYLELSGAVVAFAPDASSSLLFELADIKQHKKTSADILIFLSKDHNLPVSFYDNYKLKYTLHFWQPPSFPDSSTIDDQAKLLFDYVVSQVVKYPYFVTDIYQIHLLGVYLNLKHVYLLENDDVEDAYYERQWMQAFQRKNVVAVAEELQTALRIIEQWKQL Q9UUJ3 RGA9_SCHPO MOD_RES 640; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 645; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1952.16; CHAIN 1..670; /note="Probable Rho-GTPase-activating protein 9"; /id="PRO_0000097317" MWDGFSNSFWSRDYITGINRAQRLINEGVEQNEKLLQLLHIRAKSASSCSDLLFKSFSKFNKHHPLNEESNDLPSDAAIHQLYESYLMEASLHKKLGEQLNILVINPFANWSKKYSRRVDEIVSAAIVKINNYNSRFSHVNSKKSNLTDRKPIPTSRKSNKSDSLASALSQLDINPSNVNKFDGLINIVDHPYTAEEFANVLLKLMKASTVKRKSYSHLGDYELVTNCSLLFEAIKTTFGLEKDSYVVKAGNQLIQHGLIRLLGIRRVFENDPEIDAQFTTKSQQLLKSYHLSILEVDPYFQVNDPITATNDDPVLQKYNLAYDNLEQCRHELELYLFMVFKDLEQAELDRLNAVKSVLVECSNYSGNFIPSLNSIFIDNLNSFKNLDSLRDMSTQINKHYTGYFIPVSNNELSTKDEYLFLQKSSLTEDNLIVSLVPKILAYLLDAYSYERDEEVLSCVWTTEVPLKDAFDLKSVLRKTDNVESVLNACVEKYTLSSITCSLRLCLLEFPDSLIRSSFYDYFKAIYTTYTDFEDLDHRLYSIKKCLLHLHSTPLHILEEIIRHLSAYAISIRMKDGQIRHLAKIISPCVLRPPDDLNIIPVEDTHPTLLVIDLINEFENLFADLERPSTPPVEIERALTPITTSPQKLKLPRSSSPCKNPSPTRRFRPF Q9UUJ4 REC24_SCHPO SPAC1952.15c; CHAIN 1..350; /note="Meiotic recombination protein rec24"; /id="PRO_0000300499" MNGTNTEDNSKQILIQTMYTYDSSGETLKIAIAWKIILKKPKGKNIKDYIEALRKGIEDQEHCEKYASTLLEPRPKTKKDVVLKNSNVTECVALKAKPFSKKIEDMDIFLLTNVHENLQEKRQTSGSLAHLDIEYTFNGLFRFLKCTADIKLKQTKVYEGADFLRIKTLFEEIFMFLKRDCKSPLVLTRLVELGDYVLDLIIITQSIMQNNANNGTGVISRAKFLEFYVFLEQLIFNKLSFASVEQLEKLLDQIVKRMKICFTYCKNDNPSIRLLYSECFFSYAEIYFPCLHSFDAQLSSAASKCVQILRDIITNEELQTDKQELSKSAYSAPSILLIGLKDMLFPEDIS Q9UUJ7 CSN7_SCHPO MOD_RES 183; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1952.12c; CHAIN 1..205; /note="COP9 signalosome complex subunit 7"; /id="PRO_0000121005" MEEKISQAIDDPNVFCFQELWIECQEVQKSQPIDSAVLRTLEIFCRGDIRDASSEWNELRFKKLRLLTLIDLANRHVGSSVSFETILVHLQLDRLPPSDPTFTVEYYIMQAMMNQILVGKINAKTQTLHVSWALERFLDSKRIDEMKYSLDRFIERCSNILFQLDAGTPSVSKSFKRASRMSSSDGIDYMVFDKRPRPDDTDFDL Q9UUJ9 ACH1_SCHPO ACT_SITE 301; /note="5-glutamyl coenzyme A thioester intermediate"; /evidence="ECO:0000250|UniProtKB:B3EY95" BINDING 276..280; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:B3EY95"; BINDING 391; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:B3EY95"; BINDING 395; /ligand="CoA"; /ligand_id="ChEBI:CHEBI:57287"; /evidence="ECO:0000250|UniProtKB:B3EY95" CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1; SPAC1952.09c; CHAIN 1..521; /note="Acetyl-CoA hydrolase"; /id="PRO_0000215522" MPSLLSSRIRNAEFAKKIVTDPAKLVPYFKNGDYVGWSGFTGVGYPKMIPNALARHVEENNLQGKLRFKLFVGASGGADTECKWAELNMIERRCPHQVGKPISKGINSGRIQFFDKHLSMFPQDLLYGYYTRNRESNTIDTAIIEATAITEDGGIVPGASVGASPELMQLAEKIIIEVNTAIPSFEGLHDIVEIPNPPHRTPININRVDDRIGKPYIKVDPKKVIGIVEADYGDITCANSPQDETSQAIAGHLVDFFHHEVSVGRLPKNLHPLQSGIGNIANAIIGGLAHSPFKDLEVWTEVLQDTFLPLFDSEKLRFATATSTRFSPQGFEKFYSNYDYYKERILLRPQVISNHPEIIRRLGCIAMNTPVEADIYAHANSTNVLGSRMLNGLGGSADFLRNAKLSIMHTPSVRPSKKDPTGITCIVPMATHVDQTEHDLDILVTEQGLADLRGLSPTERAREVIDKCAHPDYKPLLREYFDIAENYCLARGAGHEPHILANAFKMQLNLLEKGTMKIDHW Q9UUK1 CTBL1_SCHPO MOD_RES 39; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1952.06c; CHAIN 1..564; /note="Beta-catenin-like protein 1 homolog"; /id="PRO_0000372369" MDVDSIFKNTEETNKKRNPEEADSLEPASSRRRLAEENSDEENEEFDEEGGRFFGSGLKKSEKTVLDFLDEQEAQEEPASLTPTELKRMVVRLEKTINNNQELRIKYSTSPQRFIESEADLDLEIRSFNVLSEYPILIPIFLKLDCVSTFLELMNHENADITITVLELLIELTDEDVDPDALNSLFTSLIDSGLLPLLSNTIKRFDESNEEDRHGVYCVLSLMENLLSVDNSICSIIVENTTLVEWLLSRSSVDETSISTNLQYAVEILAIILANSKEAKLKVCNLNGIDLLLRRISPYRLRDPTQGSEEEMMENVFDCLCSLVQETKGKSLFLKEEGIELCILNMKHKGKSRYSTIKVLDYLLFGPLSTPYCIRFVEAGGLKYIFAAFMKISAADTLEHILAILASLFRSLPADTVERVRFLRKFIENDFEKMKRLFKIYDRLRIQLKGIDQSRKLDFSPDSEEKSTKWFLQQIDHGLFPFQSTVLILSWLCVENTVTLKKIKMLFSEASIPIDELTDALKNYHENLEEPTVESEEVEANDSYYRIDEKPMVTVLLGSMQASV Q9UUK3 OTU2_SCHPO CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; SPAC1952.03; CHAIN 1..324; /note="Ubiquitin thioesterase otu2"; /id="PRO_0000318138" MRCPLAYYYTQTTIPTQQKRKSKKMEELLSKQREECKELQSKITNLRKQLKEGNKKQKRALQQKISQMEADLSQKHATERQKLDKGDEETNETQQEDLLNTLLQQMEDTKITTAEKSSVQSSLNTKENTPQQPKKSRNRQKERLERRKAEMKKMSEQAELESEKMADLKNEEKKKFSKILEEAGLVAVDIPADGNCLFASISHQLNYHHNVKLNSQALRNKSADYVLKHCEQFEGFLLDEESGEVLPVSDYCNEIRNNSKWGSDIEIQALANSLEVPVHVYNTEGPVLKFNPSTVKFEKPLCIAYYQHLFGLGAHYNSLLYRDN Q9UUK7 PUR3_SCHPO ACT_SITE 122; /note="Proton donor"; /evidence="ECO:0000250" BINDING 13..15; /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"; /ligand_id="ChEBI:CHEBI:143788"; /evidence="ECO:0000250"; BINDING 100..103; /ligand="(6R)-10-formyltetrahydrofolate"; /ligand_id="ChEBI:CHEBI:195366"; /evidence="ECO:0000250"; BINDING 120; /ligand="(6R)-10-formyltetrahydrofolate"; /ligand_id="ChEBI:CHEBI:195366"; /evidence="ECO:0000250"; BINDING 162; /ligand="(6R)-10-formyltetrahydrofolate"; /ligand_id="ChEBI:CHEBI:195366"; /evidence="ECO:0000250"; BINDING 191; /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"; /ligand_id="ChEBI:CHEBI:143788"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366; EC=2.1.2.2; SPCC569.08c; CHAIN 1..207; /note="Phosphoribosylglycinamide formyltransferase"; /id="PRO_0000074953" MVASLVVLISGSGSNLQAIIDATLNGVLKGEAAVTHVLSNRKNAYGLERAAKAGIPTSLHTLLPYKKEYGPEIGRKKYDAELAEKIIKLQPSLVVCAGWMHILSPEVLIPLETNKIGIINLHPALPGAFNGIHAIERAFEAAQQGKITHTGAMVHWVIAAVDEGKPIIVQEVPILSTDSIEALEEKIHAAEHVILVQAIHQIITDNK Q9UUL4 MOK12_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378, ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.183; SPBC32H8.13c; CHAIN 1..2352; /note="Cell wall alpha-1,3-glucan synthase mok12"; /id="PRO_0000080330" MLFFSIPTILLIFFLFIQIITAAFLTDENEPWNLNRNWTAQKILDYSAEWNSHEYFPSPSNWRALPFYTIILDKWTNGVPENDVAEDTVFESDPYEVTFRAGGDIVGLVTPRSLDYLESMGIKAVYIAGTPFQNLPWYPDGYSPLDFTLLDKHTGTLNQWHEAIMKLHERGFYVVVDFTISTLSELSYFVNSSMSFANTSAPFSTKGYKMKYKHPEYHYTDFQLSNGSSYSCNAPTFWDVTGLPINNTEDLNSISEVMCLSGDFDHYGDVEAFGNHPPWWRQLSNFASVQDRLRDWDPIVAKKLKHLGCLAVKMLDIDGIRVDKATQITADFLGDWSAYIRQCAREIGKENFFIPGEVTSGADFGSIYVGRGRQADQRPNNREIALQTGYNESKYFLRKESDSALDSVSFHYSVYRTLTLLLGLQGELFAAFDLNRHDFAAMWNQMLIQDDMINANTKKFDPRHLYGLTNQDIFRWPSIKDGRFKQLLGLFVVHLLMPGIPLIYYGEEQNLKLLDNQAANYIFGRQPITSSIGWQKHGCYQIGTTQYTDLDFGPASEACRDDWNSLDHLDPTSPTKHYIARMNEIRSYFPQVRDGWDLKLIGKWTHEGTFPGNELYGESNPTTWGLWSMIRGPLAPYQKFSDQNDYIWLIFTNENTTKTYDMDCMRQVDNKFPPYPALLGPYSSGSTVKNLLYPYEEIDLSTSTIDSPDIGNIGCIPHLTIDAYGSKIFVKKEDWIRPSLYLTKFLPGHDSRIYSATEVTSFKISLGFSEEVDCKDLFKRIGFNSRTLNSSFAPKILEDSISCGYLDQPAPQEYTNAPVTKWFFNATLDSVPNGMHELLLNEVKSTSNQTMQSKIARLIFRVGNEENPLVYPNNATFSPSLLYKASNGDLYVNHTGAGADKYRFSLNYGGTYSKWKTVSTPSEKLRKPTWNGTNLQKWDGDHLIVQYWSSIALSTAHVQHGDTLNYSRQFPNLFVQGAFNRFGYDGSMPSKMSYNLENRTWSYDLISTWPAELVLNVWGMNPDNNADQGWVYGDLDNDTIIDRVPPGSSRISNFIRFLDPPPKPYLSYKMYLNDFTRQLHYIPKGSWTVQIVAIVLLILLPPLFGIFSVALYSGAFSRVTIFNGSHNRGIKVAKQKIKSIMSRIFPFSVHLPLDNSSELLKQLPESEKRLNVLVATLEYDVPDLGIRVKIGGLGVMAQLMGQHMEFQDMVWVVPIISGVEYPFDKLCTEPKIAVKIGDDEFVVNCYSYKSGNITYVFLQSEVFYKQSSKEPYPLKMDDLASAIFYSVWNQCIAEVWKRFPLDIYHVNDYHGALAPLYLLPEVIPVAVSLHNAEFQGLWPLRTSAELECVCSIFNIEKDICTKYVQFGHVFNLLHSIISYVRKHQGGYGVVAVSDKYSKQTLSRYPIFWSLVHISGLPNPDPSDLKLLNHLTDDPVDVDFVLEAKRKLLKKQTQEWANLDVDPSAQLLVFVGRWSHQKGIDLIADLAPKLLTEHNVQLITIGPVIDLHGQFAAEKLEQIAKRFPTRVLCKPVFTAVPPFLFAGTDFALIPSRDEPFGLVAVEFGRKGVLCIGSRTGGLGHMPGWWFQMASPNTGHLLTQFENAITKALHSNGELRARLRVEALRQRFPVCIWKQKSENLLKSCIYVHEMETLKHASPTFKAYQFVVRICHYLTSKVKSINKDQVFNAFSPDVSERPPLFEVASCSNETDSVEKLTPELSVSPESDMHFKDGNSSKLEIVESKEIYASDSDISNSTSEDINKDECVSKDIEVDNFALNLQSQSYEGDSNDFGIREVPLSDANQSSQADSTSIDRYGPYSSQKVNFSKYKDFVESRPTFFQSSVTFTDADGSTRKTFSKRLENLTTSNTLKSLSVDHFIRKHERKYFNGLRKQEIDVKLKSRSDKEKSCTVSESYKQIDCDTYEATRLQKLLLHSIGGWPLYTIVLAIGQILGASSYQLTLLSGESAQSTVSMYILLSIFSFFSLFWWFLSRVVQARYILSLPFFFFGISFILVAITHFFQKTTACSVIQHIAAYVYAISSSTGSLYFAWNFGAEGGIATHHWILRACLVHGIQQIWSAILWSWGDLLSKKDLTQNVGPGIFAGGLIASFICFGLSYVTFAGLPAFYRQAPSIIPAFYRSLGKRNIVIWFFISQILINYWLAVPYGQAWRFFWNTSNTPLWSIIILLLIFFIVVWAVLLSVIKILSLNNVWFPVIFGLGLICPRWCLEFWSSSGLGINLPWAGKASALLTKSVWLLLALWDGIQGVGVGVMLLQTLARDHVAFTLMLAQVISCITIMIAKPSLPVSDRVFPNLGAWNPSEGPGPCASPCFYIALICQFVAVGGLLYHYRKSQLAL Q9Y700 EFTU_SCHPO BINDING 60..67; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 122..126; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 177..180; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250" TRANSIT 1..?; /note="Mitochondrion" SPBC9B6.04c; CHAIN ?..439; /note="Elongation factor Tu, mitochondrial"; /id="PRO_0000007464" MNSAKATSLLFQGFRKNCLRLNRISFASGLINRFTVPARTYADEKVFVRKKPHVNIGTIGHVDHGKTTLTAAITKCLSDLGQASFMDYSQIDKAPEEKARGITISSAHVEYETANRHYAHVDCPGHADYIKNMITGAATMDGAIIVVSATDGQMPQTREHLLLARQVGVKQIVVYINKVDMVEPDMIELVEMEMRELLSEYGFDGDNTPIVSGSALCALEGREPEIGLNSITKLMEAVDSYITLPERKTDVPFLMAIEDVFSISGRGTVVTGRVERGTLKKGAEIEIVGYGSHLKTTVTGIEMFKKQLDAAVAGDNCGLLLRSIKREQLKRGMIVAQPGTVAPHQKFKASFYILTKEEGGRRTGFVDKYRPQLYSRTSDVTVELTHPDPNDSDKMVMPGDNVEMICTLIHPIVIEKGQRFTVREGGSTVGTALVTELLD Q9Y704 MOK14_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378, ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.183; MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC63.04; CHAIN 1..1369; /note="Cell wall alpha-1,3-glucan synthase mok14"; /id="PRO_0000080332" MNIKKKSFLFQFLFGWIVLSSAQWLSVLDEAENLNSSFSLESVDSFAPVRPRFIIDEDFAEDYNLTVDILHRPLQENFDSFFPNVEAYVESGNSNGDLMSDNGKLDDLNSRAAYSALKALQNSYGSSHLYRFTPYELFGQSIWIEEAPEVNHVGWSIMFDNLGRYFLLELRGLREVTFALFITFSIVPIITGILTVYIYKKKYCVIKFNKSGRSKKKDSWLKRSKDELLRTDSANLLTLNDNDEPVMIRHSCKRTCILFATLEYNIPEWNIKIKIGGLGVMAELMSKTLKQYDLVWVVPCVGDITYPVAETAPSLVVKVVNQDYEVKVFYHYKDNIKYVLLDSPIFRKRTSHDPYPPRMDDISSAIFYSVWNQSIAAIIRREKVDIYHINDYHGALAPIYNLPEVIPCAISLHNAEFQGLWPLQSSIDEREVCGLFNVSKTICREYIQFGNAFNLMHCGVSYVRRHQSGYGVVGVSNKYGQRSWVRYPVFWSLKKIGQLPNPDPTDIGLSVNPVNQQLPDFAEYASVRKENKRKAQEWAGLTIDDEADLLVFVGRWSVQKGIDILADLAPTLLEKFNIQLIVVGPLIDLYGKFAAEKFMYIMERYPGRVFSKPEFVHLPPFIFEGADFALIPSRDEPFGLVAVEFGRRGAICIGSRVGGLGEMPGWWYSVESSSTAYLLKQLEKSCTLALKSTPEMRHKLRIAALQQRFPVDEWVALYDRLIRNCIKAHNKQQQRRSIKSFFSCITPNKPTKDVNDILSEKSAFSPADYEHSIDIREHTSYDANSMDNDSDEDNYEQAESIISSLSSSALSELSYISESSMNIGSRLDERFIDANGVAIRDFSAELTYLTPENSKGKLSIDHFLNKVQSRWHDEEHHYYKTGFRKRVYKYLKIKDKKSKDVDPDDDLVNQLPLNAYTKPRYKSAASTRLNIYQRILYLKVFTWPLYTIFLSLGQILSISSFQLSLLSGFEDNNQISLYVITGVFILSTIVWWGLYRNLPSVHSLSLPFAVYALAFLFTGISSMSLPYHIRGWLSYAATWVYAIAAASGPLYFTLNFEDEHCSGLGSSITRACVLQGVQQLWLSFLWLWGTLSSRLDYNYKVLLQPINSVYVVAGVWPVSFVLLSVCILLYKGLPPFYRQKPGSIPAFSKSLLHRKVVICFLISVINQNFWMSTLISQAWRFFWGSKLTKLWKIVVMTVSFLVGAWLIIFYVLRKLSNKHTWMVPVLGLGFGAIKWMHVFWGTSNVGIFLPWAGIAGPYLSRALWLWLGILDSIQGIGNGLILLQTLSRRHVTNTLMISQLAGSATSILARFVSPTKTGPANVFPDLTGYTPVDRAKPVANAPFWICLILNVALCIMYLRCYHRENISRP Q9Y719 MOK13_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378, ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.183; SPBC16D10.05; CHAIN 1..2358; /note="Cell wall alpha-1,3-glucan synthase mok13"; /id="PRO_0000080331" MRNKNILVLNLILSIPRLVFTAKYDERESLWNLNQNQSATDPLDYWGKWENHQYHPSPDDWQVPFYTVILDKWKDGDPRNNEANNTIYEYDIYETGFRNGGDIIGLKDSLDYLEIMGIKVIYIAGTPFLNQPWGADQYSPLDYTILDHHSGTIAQWRDTIEEIHRRGFYLVLDLTISTLGDLIGFRKYLNSTTPFSLFEHEAVWKSNVIYPDWNFTNKYDPKCELPRFWGEDGAPVVIDYVGCYDSDFDQYGDTEAFGTHPDWERQLSKFASVQDRLREWRPSVSEKLKHFACMIIAMLDVDGFRIDKATQITVDFLASWAHSVRGCAATFNKKNFFIPGEVTGSSSYGSIYYGRGRQPDQRPPSILTSLNSSSLKENYFLREPKANALDASAFHYSLYRAMTRFLQMDGDLQVGHDLPVDFTDLWNAMAVNEDFYNPNTHKVDPRHMLGITNHDVFRWSAIEFGLERLLLGTMITYFLFPGAPSIYYGDEQGFYVLDNTANNYLYGRQAMPSSIAWKVHGCYALASDQYPELPVIKAYQGCNDDWNIMDHFDFAKPELKMFKIFNFIREQYPALKSGWKSVKLRNWTEYVHFPNSGKTPTEVGVWSIVRGALETLQNFDARNNTAWNGDIWILYTNQNRTTTLDYQCSSSNSVVSPYASGLTLKNLIYPFEEYILQESNKYSSNLKSYYGCIPNIEFPPWGFKILIPKKYYVRYPPQITSFNPQHDSRIYNHNGKQKLVISFTETMDCNEITSKLQFSSKTESGKVMKVDKETVKCSVSNNSADSYYFGLAPARFHWSGDLINIADGIHEIKLQRVHSQDHQSMSDSMYKLLLRFGKLDNPMVFSTANRSSSILSQENEKLYINHKAPGADLFRFSFDYGLHWSEWIDYLSNKTECTEFANNISLKTWKGHHVIVQYWSRLTASANYIQEGGLGSLSSFPHLYMNGPYNQWGFDSGIPNRLIYKNCSWHKTFISDVFPTKFQFNVYNFDESGMPDQKKVYGTIGNSTVLVRLPPSELKESVTWIKEAPPSNFLTWEIIISDLTRTYHLIPRGSSTVSIILFSLFLVSPLICALATMLAFQKFFYQVRLNKGIEKKQEWKEKLLGPFSRISQSNINQGFSHQVALNNSVKSVHPKISRKLILVATLEYDIPDWDIKIKIGGLGVMAELMGKHLTHHDLIWVVPRVGDVNYPDGQELAPLEVVVLDQVYEVRVYSHNLRNITYILLEAPVFRKQTSAEPYPARMDDLSSAIFYSAWNQCIAGIIRRYPIDVYHINDYHGALAPCYLLPNVIPCVLSLHNAEFQGLWPLRTQAEKNEVCAVYNISTKICTKYIQFGNVFNLLHAGVSYIRIHQKGYGVVGVSNKYGKRSKARYPIFWGLKKVGKLPNPDPLDTAQLDDPTNITEEITIDLTAEAEKRAFKRDAQKWTNLELDDSADLLVFVGRWSMQKGIDLIADIAPTLLQDFNAQLITIGPIIDLYGKFAAEKLNALMKKYPKRVYCRPEFTHLPPCIFSGADFVLIPSRDEPFGLVAVEFGRKGALGIGARVGGLGQMPGWWYSVESNATSHVLQQFEEACRKALSSSAEKRALLRAKSAKQRFPVLEWISKLDHLMDNCIRLNVGQRQQGSSSHSMKFRSKNDLSSIKLSTKEGLENEENELKDKAPPNEPNVGSLFLFNKSSMGSVGGPGHYKATDLSQELETNDQDIEYNEFYSQLDTSTSDIFQDTSVDGFPDLQVSSDINVRNDRLSSFVMSSEDLRSSDGHPENSDSVLETISSVHHRSPINQVVRNLNESQLSLDSVISMNLNKEFALTKTENDFTDDNGRALNYFSQKLEELDPKNSVNELCIETFILKMKKEWYDGLRNIRFGIQRPNLLIYDEDKKFINTEHFLGSKVNLNSVTSLGNFNGSSPNSFLFLLKNRTMRIKCFMQMRIGDWPVYSIFLSVGQILAATSYQLVLLSGSSAQFSTQLYIVGSIYTVSSVFWWYLYRMLPSVASLSLPFLLYCASFLLIGISSFINENMYLRLWISHIASWIYAVASASGSLYFSLNFGDEAGAGVVSWIVRACIVQGFQQIWACCLWYWGSYIDRSMQECHSFPHEVYPLGLIAVFSWPLALVMLLFAILLIFGLPDYYWESPGNIPAFYTALLRRKLVLWFFVATILQNYWLSTLYGRSWKYLWGGSLLAPWKMLTIAFFLFLSMWIIMLMFLGRKSLTHSWLLPVFGVGLGSPRWLQMMWGTSNIGVYLPWAGVAGPIVGRILWIWLGVLDSVQGVGVGMILLQTLTRRHIATTLIAGQIIGTLTSMLARATAPNRLGPGLVFLDLTSWRFEDGAKIFRSAPFWICLISQIAVSAGYLLFFRRENLSRP Q9Y7I8 ZUO1_SCHPO MOD_RES 55; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 57; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 76; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1778.01c; CHAIN 1..442; /note="Zuotin"; /id="PRO_0000071159" MSAGDSIQLFPPTTKQAIEASFVPHGKISPLIKRAVEPVGPLFLAHARRQRHGRTFSEDERLEVKNKVQEEVKEESEDEEEDPAMLRADPKEWKQQDHYAVLGLSKYRYKADTEQIKKAHLKKVLKHHPDKKAASGNINDDSFFKCIQKAYEILSDPVRRRQFDSVDENADVEPPESTTKETFFELWTPVFESEARFSKKQPVPSLGTIESTRAEVDNFYNFWYNFDSWRSFEYLDKDIPDDGESRDNKRFQEKKNRSERQKNKARDNARLRNLVDTALASDPRIKLFKEQEKAAKAARKWEREAGAREAAAAAQKKKEEEERRAAEEAAAKASAAAANKKAKEDKKKAQKRDKKVVKNALKDFNYFSATDVPSAEHVDSVLKDVDVIMSKLGEGELGQLAADINAEKAAGAASVQAVFDKFAKMFIERGSMSSADVVFFAQ Q9Y7J2 YOI5_SCHPO SPBC1778.05c; STRAND 22..25; /evidence="ECO:0007829|PDB:8FW5"; STRAND 31..34; /evidence="ECO:0007829|PDB:8FW5"; STRAND 93..100; /evidence="ECO:0007829|PDB:8FW5"; STRAND 102..108; /evidence="ECO:0007829|PDB:8FW5"; STRAND 123..128; /evidence="ECO:0007829|PDB:8FW5" HELIX 4..12; /evidence="ECO:0007829|PDB:8FW5"; HELIX 43..67; /evidence="ECO:0007829|PDB:8FW5"; HELIX 73..75; /evidence="ECO:0007829|PDB:8FW5"; HELIX 81..85; /evidence="ECO:0007829|PDB:8FW5"; HELIX 135..152; /evidence="ECO:0007829|PDB:8FW5"; HELIX 153..155; /evidence="ECO:0007829|PDB:8FW5" CHAIN 1..160; /note="Uncharacterized protein C1778.05c"; /id="PRO_0000116872" MIKPKKLSSLMKQAVEETVPSIMVFTTTGSLLAYVSFEDPKDGLKRLDLAKRVRSIAALAGNMYSLYTATNPSPLVAESTDDVIAHQRDVLFETIIEFERGKLLIAAISIDGAEDKLYSKDPLLLGIVGTENAKEGMMQIKSELLKECITNELSTLGKPV Q9Y7J3 CARME_SCHPO BINDING 110; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 113; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 154; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 175; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 242; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 243; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 262; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 266; /ligand="carnosine"; /ligand_id="ChEBI:CHEBI:57485"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 274; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 297; /ligand="carnosine"; /ligand_id="ChEBI:CHEBI:57485"; /evidence="ECO:0000250|UniProtKB:Q8N4J0"; BINDING 356; /ligand="carnosine"; /ligand_id="ChEBI:CHEBI:57485"; /evidence="ECO:0000250|UniProtKB:Q8N4J0" CATALYTIC ACTIVITY: Reaction=carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:14205, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485, ChEBI:CHEBI:57856, ChEBI:CHEBI:58445, ChEBI:CHEBI:59789; EC=2.1.1.22; Evidence={ECO:0000250|UniProtKB:P53934}; SPBC1778.07; CHAIN 1..373; /note="Carnosine N-methyltransferase"; /id="PRO_0000337252" MEYDEEEVKVLKEVLSAFFLYRQYAHTITQQKRKSMSRLSFEHKDLLLQDSDNNFLKHLSRIDQCIEQNSVLAEAIANAAIPVFCSDFDQNELFHVNVDMMQKVSSTLKQIARDWSTECVEERRTTYAPFIEELNSLFPSDSIDRSKIRVLVPGSGLGRLAFDIAVEGFACQGNEFSYFMLLTSHFILNCVKQENQFLVYPYIHSFSNHVMRDDQVRSLNIPDAVPSQYLRNSQNFSMAAGDFLEVYGTEESRDSFQVVATCFFIDTTKNILDYLDTIKNCLVDGGYWINLGPLLYHFESEGTSNSNSDSQQQPFVELTLEQLFYVMDSMGFEVLKHNSVDTTYMGDKRSMLEWIYHPHYWVCRLQKSKLRFQ Q9Y7K1 YGL4_SCHPO ACT_SITE 122; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"; BINDING 52; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"; BINDING 97; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"; BINDING 100; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC216.04c; CHAIN 1..138; /note="Uncharacterized protein C216.04c"; /id="PRO_0000316245" MGFPLEKSEDEWKKELGPEKYRIMRQKGTEHPGAGRFTHQFPKQGVFVCAACKELLYKASTKFESHCGWPAFFDNLPGKVKRIEDNSYGMHRVEAVCANCGGHLGHIFKGEGYSNPTDERHCINSASLEFHNEATNDN Q9Y7K6 YGI4_SCHPO SPBC2A9.04c; CHAIN 1..741; /note="Uncharacterized RING finger protein C2A9.04c"; /id="PRO_0000310484" MDSNTNENNSHASSNERQSSEGHDDYLNRNPNSEATEGEEGTHPTTGTQPVAFSIGTMFIITPQANFEGGENDPFANPFQPPVKRAVKEAWDSFEPLSNDQLMDLTCPICYDDMNENDEKQATKMPCGHIFGKNCLQKWLENHCTCPLCRKEVPHETVGSAHPPILFIIPHSHTLRGNQGNTAVSQENASNGVHSDFHPSEELNNANTDGRTGVDEPARQLHRIAFNRIRFILAPNRSATNTPVENTHPENPDSNTSTPTTRSEPLAGEGASIDAENASSRQETTPSDSRPSTLTSLFNAFFSSMPDRPSSNEPMTSNLTSNSGSMTNSTSTDLPTSNLPSQNAPARPVEPSPSIQPPNLLNLPTASPESTSWLPGSQTNIPANTNRSERPFTQLMTFHGLPSLADLPAVLESMFRPSGNNNLLNLNGIFHPDHNAQTENGQTLPENTDDTNSNATSAVPNLQNLNQQNAVTMGTNTPNNGSSPAVHPVIHIYLSRPPLQPAVSEQETPSEAVSREGTRSTDATMEDSSRPPSNGSFQGPGITHLSEMGQRILQRFQEEMENRMNQTRSESSTPAQQSAAGSSINVDTAGRQPSDEINIPGEYENSSEVAGSRNQTPTHSSIAVDTLSNVAVDQPAISTPSDVVGSDAGDTSKVSSGTSTPRMAAPIARRSNRHHPYSRPSSTRPQCQLEDQGICDPNDRFVHFECGHSVHERCQQSTSNSENQMDEEIGECPKCRNEEHK Q9Y7K8 UPPS_SCHPO CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = a di-trans,poly-cis-polyprenyl diphosphate + n diphosphate; Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:19494, ChEBI:CHEBI:33019, ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763; EC=2.5.1.87; Evidence={ECO:0000269|PubMed:25066056}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q96E22}; SPBC2A9.06c; CHAIN 1..258; /note="Dehydrodolichyl diphosphate synthase complex subunit nus1"; /id="PRO_0000353827" MYDDIFFYLALWVIQSVYGAWDWAKNWVFWTCSYLLNFLYHHHCSRDLIRRDTKKLKKKPKHIAVIIECVEDGGIEGLIHDACELSAWCVCSNIRELTIYERKGFLKQSPEAVEKAIYSHLPFYLGGDKCTVHVTNPCSPDEKNQNDCVDLKVHLIAKEDGRDAIIDLTRGLADLCTKKVISSTQVTLELIDKELKESVIPEPDLLIIFAPLLKLQGFPPWQLRLCEIFHDPILYTTNYLTFFKALVHYSNAEMRLGH Q9Y7L2 BIN3D_SCHPO SPBC2A9.10; CHAIN 1..268; /note="Probable RNA methyltransferase C2A9.10"; /id="PRO_0000289271" MSNFQHGNYHSYYSMRGGTSIIDPRLKCLPDSLFYEASVLDIGCNNGTVSAQIASIFGASFVLGLDIDHVLIQKARKHLEFVSSRIGPVRNPGSIVEDQFNYYPISSIKKFSRIPVQLQPPLNKQNFPHNIEFETADFLRWESKRKFKIILALSVSKWVHLNNHDEGIIKFFGKISSLLETNGVLILEPQGWDSYLKAAKKISVFNQTPENLKIQPDAFEHLLNQAGLVLEYSIEPQVNNSEYKNFAKRTMYIYKKKGIGIIKLLTST Q9Y7L6 AP2S_SCHPO SPBC685.04c; CHAIN 1..143; /note="AP-2 complex subunit sigma"; /id="PRO_0000193813" MIQFILIQNRHGKNRLSKYYVPFDDDEKVRLKARIHQLISQRNQKFQANFLEWENSKLVYRRYAGLYFCFCVDSTDNDLAILEMIHFFVEILDSFFGNVCELDLIFNFYKVSAILDEIILGGEIGESNKKSVLERIEALEKLE Q9Y7L7 GPI15_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705, ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198; SPBC685.05; CHAIN 1..160; /note="Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15"; /id="PRO_0000351441" MLTIKRYPGAIEFTVHTSKSYGTQMFALCFISFVIGATSLAIGRSPKIIITLVELSFLLSLFHIISGVNHESLFVIRDLGVQTNCHSIVPWKSSSKLIPLDSIRDIFINEGFRKFDVCYYMGIAIESETEIHVVFPTLLPRHDVLQKVYKETVILLANNS Q9Y7M1 PXP1_SCHPO BINDING 49; /ligand="thiamine diphosphate"; /ligand_id="ChEBI:CHEBI:58937"; /evidence="ECO:0000250|UniProtKB:P40149"; BINDING 447; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P40149"; BINDING 474; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250|UniProtKB:P40149" CATALYTIC ACTIVITY: Reaction=an (R)-2-hydroxy-long-chain-fatty acyl-CoA = a long-chain fatty aldehyde + formyl-CoA; Xref=Rhea:RHEA:67444, ChEBI:CHEBI:17176, ChEBI:CHEBI:57376, ChEBI:CHEBI:170012; EC=4.1.2.63; Evidence={ECO:0000250|UniProtKB:Q9UJ83}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67445; Evidence={ECO:0000250|UniProtKB:Q9UJ83}; CATALYTIC ACTIVITY: Reaction=a 2-hydroxy-3-methyl fatty acyl-CoA = a 2-methyl-branched fatty aldehyde + formyl-CoA; Xref=Rhea:RHEA:25375, ChEBI:CHEBI:49188, ChEBI:CHEBI:57376, ChEBI:CHEBI:58783; EC=4.1.2.63; Evidence={ECO:0000250|UniProtKB:Q9UJ83}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25376; Evidence={ECO:0000250|UniProtKB:Q9UJ83}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHM7}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHM7}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:Q8CHM7}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|UniProtKB:Q8CHM7}; SPBC725.04; CHAIN 1..568; /note="2-hydroxyacyl-CoA lyase"; /id="PRO_0000315628" MSISFSELVAKTLLDLEVKVVFGIVGIPVIEICEAIQASGIRFVGFRNEQSAAYAATAYGYLTQRPGVCVVVGGPGVVHAMAGVFNSKTNRWPLLLLAGSSETFQQNCGAFQELDQVSYLSPHTKLAVRPPSPKMVVDSIRRAYRVSMTGTPGTCYVDLPANYIESTVDDFPKDPLPPIPSSPKCAPDPTQLQKAAYYLKNAKAPLLVVGKGAAYACAEKQLLEFVEHTGIPFLPSPMGKGLLPESHPLNVSSARSAALRNADVVLLAGARLNWIFQYGLPPKWSPNAKFIQIDTNAETLGNNAADLDLAIWADVGLTIDCLFKLVQTWKYSVGISTPYLRTLNETRSKNEKKALESRKSSIPLQMNYALYVVNEELQSLSLKSKRNITWVSEGANTMDRGRQLLEVTHPRGRLDAGTMSTMGVGMGYAIASAFAHSSDKIVVVEGDSAFGFSAMELETAIRNQLDLLVIVINNNGVYHGLDTDAYETLRDNHQLPTTALGTSIRYDQICEACGGKGFFVKNEEDLRSSLRKAWQTSSVSLINVMVDPEAARKLTFAWMSSTKVKPKL Q9Y7M3 PIB2_SCHPO BINDING 178; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 181; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 212; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"; BINDING 215; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" MOD_RES 259; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC9B6.03; CHAIN 1..293; /note="Glutamine sensor pib2"; /id="PRO_0000357025" MTTVHQLSGHGPLSRLNIYSGASPYTQRVRPSYELIEAPTRQATNGTGSVSGSPNSSSNSTPANQGSLPSHTNPQLYSSITRKERPELFRSYSGNPRLSKPYASSKLAASSRTASYQAMSYSVSPTSTNSSVATSLNYQSSRETGISKDHWKPDSDVSVCSFPSCSVRFGLFDRRHHCRRCGDIFCALHCDRNIPLTMDVKFCLAGSLYRSCVSCFYEYLKWKQSIDLASSNDITVIESTIAPQQATTHPPSQPKNAVSVPIPKMDSTDSKGELPSESLVLGTVPDNWVWSTF Q9Y7M7 MDL1_SCHPO BINDING 517..524; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" TRANSIT 1..112; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC9B6.09c; CHAIN 113..726; /note="ATP-dependent permease MDL1, mitochondrial"; /id="PRO_0000093470" CARBOHYD 66; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 113; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 132; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 502; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 584; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 598; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 668; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MDPIRFGLSRVPFAHCYNKRVIFRANYLVPLTWLKNNVAYKSTNTLLLPTPNAEYYSTSKLSSQVNVSLNSLSQKASSGSKIYPFKNSFPLPFSRSILPIRSLAFLKLCVRHNSTVPSKDEQAQDISKINTNGTLQTPNKKVNVFRLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQLGKVEP Q9Y7M8 YNTB_SCHPO SPBC9B6.11c; CHAIN 1..502; /note="Probable RNA exonuclease C9B6.11c"; /id="PRO_0000316917" MYTCPKTCTLTLKFFIDRFHTDYRLSKLAISFFDQKKNKMADSIPVKKKGSAKGPPSFVTPEYIEKQRQKKLEKMAKKAARKPIAPPSNAPPEFNTDFIKREMLSIPNYAPFETEKSALDITIMTYNVLAQTNIRRSMFPHSGEALKWKNRSRMLANELTYYSPTLGCMQEVDAEFVPNFYKKLLGGLGYELHFIKGEGKTHGIMIFWKSSLFKKVQDLTIYYDDHDELPGRMNTKNIGCCVRLERVDDPSRGLFLATTHLFWHPYGSYERLRQGAILVKEVNKMAQSHPSWPVFIAGDFNTEPFDTNFPALTTRPLSICQRATDIIERSMNYVFGESELEEKNASTKTENDSNEDDKEECQSSSTSSVPESTASTPKKRILHVQNDYVPHYRSFYQQHEQNPVLFSLYSVGYKLVHPENAKNTFDHPAFTNWAHAYQGHLDYIFVMNRDTSLQTPENQVVEGIKLKALLRVPLPSEMKEAEPLEGRYPSDHVALMANVQIV Q9Y7N1 YCK3_SCHPO MOD_RES 231; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1450.03; CHAIN 1..240; /note="Uncharacterized protein C1450.03"; /id="PRO_0000374048" MAATTGNIIKFEENADSKDLLEQCLNCSDVGVVSNTVRNMDGTIAADLARTLIPAMLINMQPSLAIWLHWIIVTHGGYLTTVMDLQDSLVQLHEKLVQSAHLMTKIFSLSGKLNMVLSQEEMRQRRLDFSSEDGEEEEENDYIDEDVDEAGYDIEVVDEAENDDMDNDLEANADAFDESNLEASLSPNAELSPRKSHIDHDFVIPEDEMLSEEEEQEVEKQILPKFVVPESPRKTSRKSR Q9Y7N6 PLB5_SCHPO CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; SIGNAL 1..19; /evidence="ECO:0000255" SPCC1450.09c; CHAIN 20..623; /note="Putative lysophospholipase C1450.09c"; /id="PRO_0000024643" CARBOHYD 118; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 153; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 187; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 232; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 256; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 264; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 293; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 331; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 360; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 367; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 400; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 403; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 474; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 508; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 513; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 537; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 564; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 586; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 603; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKLSSFGLFLALQLLPALGLPSRIDEVDVSDPELIGLLKPDNVDKPANSIPLSKRSTSPSYAPYTVACPSGSLLRPASDGLSTGEQEFVDKRVSKVNSALESFISKTGLKIDTKSVLNDTDGPRLGIAISGGGFPAMLTGAGAINAFDARNGNTTSLGGILQSSMYLTGLSGGSWLVGSVAVNNFANITFLHDDVWNLDHSLFAPYDDAFENFYIYQEWFEQVLQKKNAGFNVSITDLWGRALALKLVNPLTGGANTTFSSVTNETWFQDGEFPFPIIIADNVIEGETVIPLNDTVFEFTPIEFGTWDTGVESFIPMEYTGTHLINGIPLNESCVRNFDNAGFLMGTSSNVFSGILPATNASLTASNNTFNNAVLSFLEMLAEDQLDVGLYPNPYQGYGNASNTTTTNPLEPYPIIELIDGGSDSEGIPFWPLLHPQRDVDVIFAIDGGYQSATSGWPDGSSLVSTYERVLATNSSGVRGFPYIPDTNTFLALGLNTHPTFFGCDGRNTTAGNHTVNDDTPPLVVYFPNYPWTMYANVTTYTVQLEDTLSSGMIENAAVAATQNNSDSFAVCVACALVQRSLERKNMSTPSQCASCFNQYCWNGTIASTTVTTYAPTVLSAKI Q9Y7N7 NAR1_SCHPO BINDING 19; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 64; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 67; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 70; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 218; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 273; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 453; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 457; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /ligand_label="2"; /evidence="ECO:0000255" SPCC1450.10c; CHAIN 1..538; /note="Cytosolic Fe-S cluster assembly factor NAR1 homolog"; /id="PRO_0000316027" MAKLSVNDLNDFLSPGAVCIKPAQVKKQESKNDIRIDGDAYYEVTKDTGETSELGIASISLNDCLACSGCITSAETVLVNLQSYQEVLKHLESRKSQEILYVSLSPQVRANLAAYYGLSLQEIQAVLEMVFIGKLGFHAILDTNASREIVLQQCAQEFCNSWLQSRAHKNQNQVTNSVVNEHPLIPHSTSQISGVHSNTSSNSGINENAVLPILSSSCPGWICYVEKTHSNLIPNLSRVRSPQQACGRILKDWAVQQFSMQRNDVWHLSLMPCFDKKLEASRDEFSENGVRDVDSVLTPKELVEMFKFLRIDPIELTKNPIPFQQSTDAIPFWYPRITYEEQIGSSSGGYMGYVLSYAAKMLFGIDDVGPYVSMNNKNGDLTEYTLRHPETNEQLISMATCYGFRNIQNLVRRVHGNSSVRKGRVLLKKRVRSNAQNPTEEPSRYDYVEVMACPGGCINGGGQLPFPSVERIVSARDWMQQVEKLYYEPGTRSVDQSAVSYMLEQWVKDPTLTPKFLHTSYRAVQTDNDNPLLLANKW Q9Y7P0 RISA_SCHPO BINDING 4..6; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="1"; /evidence="ECO:0000305|PubMed:12377123"; BINDING 48..50; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="2"; /ligand_note="ligand shared between two trimeric partners"; /evidence="ECO:0000305|PubMed:12377123"; BINDING 62..67; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="2"; /ligand_note="ligand shared between two trimeric partners"; /evidence="ECO:0000305|PubMed:12377123"; BINDING 101..103; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="2"; /ligand_note="ligand shared between two trimeric partners"; /evidence="ECO:0000305|PubMed:12377123"; BINDING 137; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="2"; /ligand_note="ligand shared between two trimeric partners"; /note="in other chain"; /evidence="ECO:0000250|UniProtKB:Q2YN92"; BINDING 146..148; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="1"; /evidence="ECO:0000305|PubMed:12377123"; BINDING 160..165; /ligand="2,4-dihydroxypteridine"; /ligand_id="ChEBI:CHEBI:16489"; /ligand_label="1"; /evidence="ECO:0000305|PubMed:12377123" CATALYTIC ACTIVITY: Reaction=2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin; Xref=Rhea:RHEA:20772, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:57986, ChEBI:CHEBI:58201; EC=2.5.1.9; Evidence={ECO:0000269|PubMed:14690539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20773; Evidence={ECO:0000305|PubMed:14690539}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.7 uM for 6,7-dimethyl-8-(1-D-ribityl)lumazine (at pH 7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:14690539}; Vmax=158 nmol/min/mg enzyme for the formation of riboflavin (at pH 7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:14690539}; SPCC1450.13c; STRAND 8..18; /evidence="ECO:0007829|PDB:1KZL"; STRAND 22..28; /evidence="ECO:0007829|PDB:1KZL"; STRAND 41..44; /evidence="ECO:0007829|PDB:1KZL"; STRAND 47..54; /evidence="ECO:0007829|PDB:1KZL"; STRAND 56..63; /evidence="ECO:0007829|PDB:1KZL"; STRAND 81..86; /evidence="ECO:0007829|PDB:1KZL"; STRAND 94..96; /evidence="ECO:0007829|PDB:1KZL"; STRAND 105..115; /evidence="ECO:0007829|PDB:1KZL"; STRAND 118..127; /evidence="ECO:0007829|PDB:1KZL"; STRAND 139..142; /evidence="ECO:0007829|PDB:1KZL"; STRAND 145..152; /evidence="ECO:0007829|PDB:1KZL"; STRAND 157..161; /evidence="ECO:0007829|PDB:1KZL"; STRAND 179..184; /evidence="ECO:0007829|PDB:1KZL" HELIX 30..32; /evidence="ECO:0007829|PDB:1KZL"; HELIX 65..70; /evidence="ECO:0007829|PDB:1KZL"; HELIX 73..75; /evidence="ECO:0007829|PDB:1KZL"; HELIX 128..133; /evidence="ECO:0007829|PDB:1KZL"; HELIX 163..166; /evidence="ECO:0007829|PDB:1KZL"; HELIX 170..173; /evidence="ECO:0007829|PDB:1KZL"; HELIX 187..198; /evidence="ECO:0007829|PDB:1KZL" TURN 19..21; /evidence="ECO:0007829|PDB:1KZL"; TURN 199..201; /evidence="ECO:0007829|PDB:1KZL" CHAIN 1..208; /note="Riboflavin synthase"; /id="PRO_0000068173" MFTGLVEAIGVVKDVQGTIDNGFAMKIEAPQILDDCHTGDSIAVNGTCLTVTDFDRYHFTVGIAPESLRLTNLGQCKAGDPVNLERAVLSSTRMGGHFVQGHVDTVAEIVEKKQDGEAIDFTFRPRDPFVLKYIVYKGYIALDGTSLTITHVDDSTFSIMMISYTQSKVIMAKKNVGDLVNVEVDQIGKYTEKLVEAHIADWIKKTQA Q9Y7P3 TGL3_SCHPO CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P40308}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P40308}; SPCC1450.16c; CHAIN 1..545; /note="Triacylglycerol lipase ptl1"; /id="PRO_0000317234" MTALFNFWRIMYANISSIWLLVVSFFEWLFSATSISQQRGSGPRKGKVVMNKDCRSWEDWKVLATTIDKASGRWKWRFTPASDKYDYLLIDRCTVSLKRYRQRKSVYPMLMFLRSSLLRNFGNIGNSSLYTENYSGTKILIEEYVREVNNCLEFLYHTKRLSYDVKCDFFSAARISFGTTCLYFNGGTAFGLYHFGVAKTLWKRNLLPQILAGCASGALIASLLSVYRDEELNGLFDTFPSELWKICQQTSDYSLSKVVEYGNMLDISMIASFVRQRLGTITFQEAFERTGRIVNIVAPPSAVSGSPQVLNYFTAPNVLIWSAVCSSNSWAAIYRSSPLLAKLPDGSTEVCTPKNFIWPYAGLPNTGRSNPYARISEIFNVNHFVITQSRPSLFPTFYDELHHHRVSGYSLKMIRLVGLEMAYRFRQLDILGLLPPRLRRFFVDDYVPSAYITLTPTFSFSDIKHAFTKPSLSDIQYWILVGERATWQAIPLLQVRCKTEISLRHLSKNLTNSYVEPLSVNNLASPFVTNLEENQEKMLKIFKVK Q9Y7P4 RML2_SCHPO TRANSIT 1..23; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC16C4.15; CHAIN 24..362; /note="Large ribosomal subunit protein uL2m"; /id="PRO_0000318134" MLSYNRFRGYLIPQIHALKLFRYASTASTSGEKIESSERPYDVGMLLRPKTKFEIKTYKPISPGLRHLKRPVSDYLWKGKPFRPLTVAKRKKGGRNETGRITVRHQGGGHKQRIRLVDFERKVPGVHRVIRIEYDPGRSGHIALVEKLNSETANKSYILACDGLREGDTVESFRSLLKTGSNGEPVEMDPVLAAEIEDGTFAAKNLKPGNCFPLRLIPIGTVIHAIGVNPNQKAKLCRSAGSSARIIAFDGKYAIVRLQSGEERKILDTSFATIGVVSNIYWQHRQLGKAGRSRWLGIRPTVRGTAMNPCDHPHGGGGGKSIGNKPSQSPWGVLAKGGYKTRRGKNVNKLLVRDRPRGKEKR Q9Y7P6 MUG72_SCHPO MOD_RES 343; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 392; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1902.02; CHAIN 1..574; /note="Meiotically up-regulated gene 72 protein"; /id="PRO_0000116550" MSEEDTSKLRILSVGSNAISAFISWRLSESKACHTTLIWRNRCESVLSEGIRIRSSVFGSTKWKPDVVAPTVEQLAMNSEPFDYIFVCLKILPSVYNLDTAIKEVVTPGHTCIVLNTTGIVGAEKELQHAFPNNPVLSFVLPDQFAQRGPLQFEHTTFAADSAKSVIYVGLTEEEDDVPDSVQDAMIETLTLTLEAGGVSCDFLSKIQKKQWETGVGHMCFYPLSIINDEPNLALMYRLKSFAKVIDGLMDEAFSIAQAQGCEFEPEKLDVLKRHIVNRMLATPRPSYPYQDYIAHRPLEVAVLLGYPVEIAKELGVSVPRMETLLALFDAKNKRNLTVRAGTPQSSPNFNPAMRRSPVGAASRSPSRSTIGISNRIGSVDDLLNTRQFTSSPIGGSMPKGPNSIYKIPSASMVNLSSPLVTSPSGLNPTGRPSRFGGRVRGNPLTMNKAGSVSDLLSTSTNMASSDALETASMIGVPSAMPPNSFDMLTLTQRRNRRNNQSSSPPAPSDRRYTMGARRPVQTRGMTDSVIPILEDPMSTLYDTSRYPTRNSKPATPKASRPPSIASTVHRRMD Q9Y7Q2 GST1_SCHPO CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; SPCC191.09c; CHAIN 1..229; /note="Glutathione S-transferase 1"; /id="PRO_0000185984" MAQFTLWSHAHGPNPWKVVQALKELDLTYETRYVNFSKNEQKSPEHLALNPNGRVPTLIDHHNNDYTIWESDAILIYLADKYDTERKISLPRDHPEYYKVIQYLFFQASGQGIIWGQAGWFSVYHQELVISAITRYRNEIKRVLGVLEDILKDRDYLVANRFTIADLSFISWNNFLEIIFAEGKFSIEEEVPQLDFEKEFPRTYSWHQRLLARPASKATFEERSKALDN Q9Y7Q7 DENN_SCHPO MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 318; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 726; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC297.05; CHAIN 1..973; /note="DENN domain-containing protein C297.05"; /id="PRO_0000316866" MESIADHFFLAGLSNGFVSVSNSQFRADRLDEDAISVSSSIIQNNTRKSPLKRVSITSESSFYKENTFAHHNTTGSNSVGPKKPFLDYHHSTSNTPTKKKKDSFDHASVTSLHRRSLSSNTSTPRKYHSRKPYSEPSVIDKEHLQNRVSIGTTHTQNDLYQSYVAYPDALPLFAATHPFERRYPPSLLHQFPSSKDIKNETPTIDRCDFPNYVPMFAFPNDITIKESDVRPVSTYHSFALTSDNNSHLYGICVVVWVAMPQSMQNDLEKECEVWRANNTTVEDREVAEKLLSSLETERSKLSSLLLKMQEKELEGSDSIDPILLEKIDVCEENIILYTELLRPMRYKLPRFVHGLTNNRTLWIPNAYGLLSKHSHLQSFCRDWLRIVCSSIQAEDLDFIPSSDLNSLKSLNLQSFVKNICCDVPLPPKGLLQLQVNVGPLNLYAFRSPVNEIPGWNDVDLYPLFRALSIPNILVLFEAALMEAKVIFLSENLGMLGYASQALLHLLYPLTWQGLYIPVLPRRLISCFEAPCSYIIGTLSYFFHMDDVPLDNIPLVVCDLDKNSVSTFGKIVRLSRSLRSKLQAHLKLAAPLHDKFYVPHSPPKYTMETYPNNVLSLSTVTCFPLREKFSIPALLSFRSSNFSKRPYVLSPILNGFLKLQDNPSSIYFAKQTDSRQSSASKLLYARLQAPEHARNFSSPPFTRPASPSSSKFRFSSSSFQSTIRRNSLTSPYSVPELRSSESNQNKAGSINTGSAVNLVSSKPGEQKVHIMYKEGHKLRRIYKMFPADSAGSICAVSGYALGDVHVQCDNCGLRVNLDFIKHISMPCVPACFNSQQILVTFLKFFIKILGSYRNYLRKPHMSRENFGISKGSGGLIGSFDFNKFTRQASKVHGSWISSLCSSQAFAEFIGDRCELDLNDPRVALFDQLLLCERNHGKPRLFGKATPFLRDKSLEIQRIEVAPIPASLKNDNALH Q9Y7Q9 YCX2_SCHPO MOD_RES 267; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 289; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 290; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 292; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 330; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC2H8.02; CHAIN 1..583; /note="Probable metabolite transporter C2H8.02"; /id="PRO_0000372719" MGFKLNPFSKKPKDEEPLPLEQYEASEQKILGLVTKKEAKLLAIAGTGFLLDSYDLFIINLVSPILAYLYWGGLTGHQDYPSGIRGVVNAATNIGNIMGQLLFGFLGDFFGRKFVYGKEMMVVIIATILIICLPDRIPTPTAKMMWLFAFRVMLGIGIGGDYPMSASITSEQSLINRRGALLAWIFSNQGWGTLAGCVATLIILACFEKPLNDRGEYTKLNGVWRIQFGIALFPAVIVLIPRLRMQESEQFKNSKNMKSPGEGDLDSASQIELHDFKKKESLTAEFTTSSPSTASLSDKKNPGSVHIRPNNEVAPSSAPSRAPSTTSVESNTEGKESDIQTGSSFVSYFKEWRHAKLLIGSALSWFLLDIAFYGINLNQSVILQEMGFNKGVNEYHILQKNAIGNLIIAVAGYIPGYWVSVVLIEVMGRKWIQIQGFLICCLLFGVLAGTWETISTGGRFACVALAQFFFNFGPNTTCFVIPAEVFPSRVRAFSHGICAACGKAGAILSALLFNKLTEVIGFGNVLWIFFGCMVAGAVVTLILPETANRDADLIDRLEIAAMQQGRTSIIDRSEKWAWWKHGI Q9Y7R5 INS1_SCHPO MOD_RES 28; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC306.05c; CHAIN 1..281; /note="INSIG family protein"; /id="PRO_0000339168" MSRKEIYEPRPRYPDGYNGNRAVKKSLSVLSLDNMKSTLSGLFAPLKLDEEQAEDDESLSSYEDYASRQIDDDLKKQRKKGITFIDYSSLITFFCKLCVIFGLGFVFTYLAEQIVQDAKLPLLTVNLKSWKFEPPWPAIFGFVAVILGLSYRRMDTKYPLGAAPLRPSQSSKWQWISRYLAAFATLLLSMKKLLFISNSHSIVALVASSASIWYIFDRSRNGIILSTITSVLGSILYYNLVDTSKIELNGVEFPEIQFRLWIPMILFSASTIVGNAGRLLF Q9Y7R6 VOA1_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPCC306.06c; CHAIN 18..311; /note="Protein big1"; /id="PRO_0000343134" CARBOHYD 150; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 189; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFSWSILFIVCFSLVSAFKDTSPIFLFSTNSKLPKSSDDSSISTCPMMFFDAAIEALSTCNTATLIIHQPGLEVNDFQLGAFKHLKRVSLQSPYSLLLPYSKESLDSQELVHSAKQNCDVEVVYLGGSFNAFPPLQNDRITVVYMNELSNESYHRSAQLMELDEMFYNLQSTLEQDAQWNVIIASSPLNNSDFEGFKVDANEEEANAEFVIQTLGGLNSGKSALQHGQLASLPDQNEGSQTTLAMHQTRKHPVTDNGATGLFTEYQFFTPGLYMGYLALAVLVPTLFISCRLLSSIQISYHAFDSPRRKQL Q9Y7R8 MDHM_SCHPO ACT_SITE 205; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 35..41; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 61; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 109; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 115; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 122; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 147; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 181; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 254; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC306.08c; CHAIN ?..341; /note="Malate dehydrogenase, mitochondrial"; /id="PRO_0000310436" MFAKVAFKNFTPLKSIAPRSFSTTSSRAFKVAVLGAGGGIGQPLSMLLKLNDKVSELALFDIRGAPGVAADIGHINTTSNVVGYAPDDKGLEKALNGADVVIIPAGVPRKPGMTRDDLFATNASIVRDLAFAAGETCPEAKYLVVTNPVNSTVPIFKKALERVGVHQPKHLFGVTTLDSVRASRFTSQVTNGKAELLHIPVVGGHSGATIVPLLSQGGVELTGEKRDALIHRIQFGGDEVVKAKAGAGSATLSMAYAGARMASSVLRALAGESGVEECTFVESPLYKDQGIDFFASRVTLGKDGVDTIHPVGKINDYEESLLKVALGELKKSITKGEQFVA Q9Y7S4 YQO5_SCHPO SPCC569.05c; CHAIN 1..576; /note="Uncharacterized transporter C569.05c"; /id="PRO_0000372794" MSTNPNAGIQPLTNSISQSASAHPELYHTTSHESVSTYQLQSQLSHSATSNLSTAANFHTRPPIANDENAQNLSTVNSSHSSELSKANLVDVEKCIQDPLLQIFPTVEDPDRFVFSIDPKSPLIAVNWPFRKKLKITCVYSYVALCSTFASSVFSVPAEAITTIFHISLTVSLLTMTVFLCGYIAGPIVWAPLSELSGRKLPLLIGMFGFGIFNISVAVAKDIQTIMMCRFFSGFFASAPLTVVAAAFADMYSNKHRGTAITIFAALVFDGPLVSPIIGGFLTKSYLGWRWTEYITSFMGFFALVIVYLFCDETYSKAIIRNKAKEYRAMSGNYFVHAKSEEEVLTVPDVAKNYLLVPMKLLFTEPIVFLITLYSSFVYAILYLLLEAYPIIFSEKRHFSMGVAELPYIGLLVGVFIGSAINISFEPWYYRRCLALGGKPDPEARLPPMMIGCFMFPAGIFWLSWSGYYSYVHWIVPTLSGLATGCGILLIFLQCLNYLIDAYLFRAASAVAANTIMRSAMAAGFPLFAVQMFHNMGVGWAGSLLGFIAVALIPMPFAFFFFGRKIREKSKMAVVL Q9Y7S6 AATR3_SCHPO CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P00509}; SPCC569.07; CHAIN 1..470; /note="Aromatic amino acid aminotransferase C569.07"; /id="PRO_0000308491" MDNLKKKYQHHLSLESASREYGPFQMLGRIQSDSDIKMLSFAGGEPNPSKFPIHKLSVSFPEVNSWEKDTNKDATVSYELSNNANEGSLDLLGALQYGQCQGIPELVKFIKDHVGQIHMPQYKDWDIKITNGNTIGLEYCLRLLVNRGDCILIEKYTYPAAITAMRPLGVKFIPIDMDENGMLPESFEKVMETWDSSLGARPHVLYTIPTGQNPTGSTLTLERRKKFLTLAKKYDIIIVEDEPYYFLQMEKYDANWKPDKQAFNISSFKKKLIPSLLHLDTDGRVLRVDSFSKLIVPGLRLGWITGNSLFIDRITRYAEVCTESPSGVSQVVLYAILNRWGQNGFLEWLQDLQNSYTMRRNALLLAADKHLPKSVCKYHSPKAGLFLWVELDKNRLICSNMDKSISEIEMEIFVELVNNGVKPVCGQLFMGEPNSADKIFFRFAYSLADLSTFEAGLERFTSTIQKYFQL Q9Y7T3 THG1_SCHPO BINDING 29..34; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 29; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 29; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 30; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 75..76; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000250"; BINDING 76; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 76; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate + H(+); Xref=Rhea:RHEA:54564, Rhea:RHEA-COMP:14193, Rhea:RHEA-COMP:14917, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:138282, ChEBI:CHEBI:141847, ChEBI:CHEBI:456215; EC=2.7.7.79; Evidence={ECO:0000250|UniProtKB:P53215}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; SPCC63.07; CHAIN 1..261; /note="tRNA(His) guanylyltransferase"; /id="PRO_0000284993" MAKSRFEYVKQYERLDRLLPETYIVIRIDGKGFHKFTKKHDFEKPNDLRCLNLMNAAARVVMSEFTDIVLAYGDSDEYSFVWSKSTELYERRESKLVSHVCSLFTSAFVFNWPKHFDIPLLSLPSFDGRAVLYPNMKVLRDYLHWRQVDCHINNLYNTTFWMLILKGGFTNTQAEEYLKGTVSAEKHEILFSKFGINYNFEPEIYKKGSIWIREPIDQEWHQQDKKFSVKQKKKMVLSILHVSLIDDDFWTSRPFLEVLLQ Q9Y7T6 SEC59_SCHPO CATALYTIC ACTIVITY: Reaction=a di-trans,poly-cis-dolichol + CTP = a di-trans,poly-cis-dolichyl phosphate + CDP + H(+); Xref=Rhea:RHEA:13133, Rhea:RHEA-COMP:19495, Rhea:RHEA-COMP:19498, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:37563, ChEBI:CHEBI:57683, ChEBI:CHEBI:58069; EC=2.7.1.108; SPCC63.10c; CHAIN 1..504; /note="Dolichol kinase sec59"; /id="PRO_0000316236" MYIMSKKCYDTSEKIDREQECVEVNYQHRNFESILEIFSVLFIPFLCNSGKKFLQISNASFFLPACFYLLGSSSIIQLYEPLLWLSSFPFCILYVGFGENSVLYHEMYTVCLYNALLSLTQRWKWLSIVLDGLGNSSVNLKLHETVILAFLEITQNSFTFIEGILICTGLTGLCFATFSYEVSPVVSVLSGVLLISLPTLILLNLCILKLAAKLHLSALFTTCLIYFFSALLVFLVSRSWVAGQLGQAPEVWLFNQIFSHRNSLTRIKIIIWWIICLGCFIFILLRSNRNNPLGKYFTTEDEVLNFRRKTYHALVVFLFLPVCCLDPHFLHLSFSGVLFIFLFVEGIRILRLKPFGKMIHEFLWEYTDNRDHKGPLIISHIYLLIGCAIPIWLSNALKGPVASVELLVGVLCLGCGDSMASIIGKRFGKHRISKTNKSIEGVFAFSISVFLVLHLTQAFHVCPSVTFWKTLFMSLCTAILEGVSTENDNLILPMYMWVLYQALD Q9Y7T9 YCJD_SCHPO SPCC63.13; CHAIN 1..208; /note="Uncharacterized J domain-containing protein C63.13"; /id="PRO_0000310355" MFKDYYAILNITPKASAEEIKYAYKKAALETHPDRVSPSARARATEQFQLVNEAYYVLSDNSRRAQYDRESASSSAKPRQSFFSRTNPQPQSQSQQGGPSFGFRQSFSDSQFEQVFNEMMNETSTRGIANAFWTIVGTLAGAALGFITFDVPGVLVGSAAGAKLGRIRDTHGKSAYSVFQDMPAVEKARILTQFLSHLLNSSKQFTSS Q9Y7U3 GEP4_SCHPO CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; SPCC645.02; CHAIN 1..209; /note="Probable phosphatidylglycerophosphatase, mitochondrial"; /id="PRO_0000351427" MLINIEGIQAFCQTIRNPRRIIPHATFPTFSQIPCNINYFLEQKFQVPVDIRALVLDKDNCITLPNETTIAEAELKKIREFQNIYGEKNVILLSNSIGTRKLDPTGELAAHFQQKWNIPVVRHSKLKPLCTEELYTYLSNNSHVSSASQILFIGDRLLTDITLANIMGSWGVWLTRGVGNTTNMMMEVESWLYKRIHTQNPYIPTNRKS Q9Y7U7 SND1_SCHPO MOD_RES 316; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC645.08c; CHAIN 1..878; /note="Staphylococcal nuclease domain-containing protein 1"; /id="PRO_0000315882" MSQYVSSMIKYAQSGDSFNILIKDNAKKITEKQFSLAYVECPRFRREGDEPFAFEAQEFSRRLVVGRPASVSTLYVIPTSKREYGRIRTSEFDLAESLLREGLAKLRPEATRNEGTSENSYFVSLEEAQDHAQQYKLGIWGPSDDVVVTEKANPANPAKFLKAHKGKKLNGIVETIRNGDQVRVRLFLSPKQHQLVTISLAGVRCPRSTFTATSPEQTSSEQEPCGDEAKQFVVTRLLQRNVVIELLDLAPNGVSFLGNVLHPAGNIATFLLSSGLGRVADNHISALGPETMQSLRTIERKAKISRLGIWKNISVSIPDINSLSLKDYSAVVSRVISTDTLEVRKDNGVECRIQLSSIRHPRPSNEKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLPAINNCTVKLSDGTNVALMVVKSGYATVIRYRMDSVDRSPIYDFLIEAEKAAQEGRKGMWSGKKPAYENIVNASESSLRSRQYLSSLQRTRKLSVIIENVISGSRFRCFCPKENCYFMFACAGIRTPRTARNDQEKGEPFAEESLSLAKSLLQHDAQVEILSVDNNGCFLGDIYVNHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHDYVPPEKKAASTEKESENTVKEPIYLDIVLSDIAEDGKFSFQIIGTGIQQLETLMSDLGSLKKSFKPSEKINVGMNVAAISALDNAMYRGRVLRCDRENQAADVLLYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLSYVQLPPPSSDYYEDARLVFRELAMNKGLVAKVDGHEGNVYSVTLYNPSDGSDFSDCINAQLVALGMASVIPKKKTSHFEKDTASLNILEEHQQEARLNHIGFWVYGDPLEYED Q9Y7V0 MU117_SCHPO SPCC645.11c; CHAIN 1..186; /note="Meiotically up-regulated gene 117 protein"; /id="PRO_0000116548" MWKFCCVTEKLTLFLFIYGICIYICIAVPIRSDLSTVFEPEAKGSRITSNYRRSLFNMLGYDNSVHPNNCKGSFLCPMLRGENRACPNAYMKYNRSLIYHGYSSYTASSCTAIYECEGDYPARTGNEIIDEFDQLNLQCSACGTRFFNNDNENTRCYVKLNYCYPDCTEITPSTSEYDYREPVRDW Q9Y7V2 BYE1_SCHPO SPCC645.13; CHAIN 1..721; /note="Transcription factor bye1"; /id="PRO_0000116549" MVRKSTRRTAKASEKPPETVVRCVCKSQEDIGDTWVQCDGCDCWQHASCVGLADKDIPESYYCEVCHSRSDVSSQVQNSPNKDEEHQTADLLASNEGNEKNNEENNVVSSDSKEAITKESGAELESSEPASTNSNVGMTTRSGRQSPRTPIGSTTPKSSHSPPSTRKRRGSVGTTATHTKRSKNAPKTSPKDASNETADQEKELSLHTSIDEIQNPVRKSVAKAWVSVFEKIIEKAKLEGVQGLEDLNSTSLALQLEHIMFMVLSYTTDHSLTPNNKYREKFRALRFNLVDDKNPAFRARVLKNEISFNDLVNLSSEEMANPDLKNLAEEIRQQSTENTVIKQHLIAPRDRLLDEDKLTQQDELGIAENDDAMFPKPPGELVAPISIAEEEPTIDSKSPTLPEHNPLSEDDTSNGDKAAKRKGSFNDTKPIVNVPSIVEIDDPTILDIVEEEPLARNDSFSSPYSPAEDMAEESEFFGMKEKIWTGKVKMATVSEFHANALNLFGDVSASHLFEILSATALIEGRISVSSVLQYFHALRKTPSKEIIAVLFVPTEQNSQGFDILYDYFVKRNRYGVLHSKSNSVKDAYIIPMPSGNSVPELLDLLPKVDLPKDRNFQYFMGLFVLNKSSSRHESVERATPITTSTNGIPSTYQSASGTPTNPVHSYPSLESIINALTPSDMLLIKDVVENNPQIRANPSLAINPQFMQNAISAAQKKASKQ Q9Y7X6 ISH1_SCHPO SPBC365.12c; CHAIN 1..684; /note="Stress response protein ish1"; /id="PRO_0000221231" MRSRSVASLGVLLAIVFYIFTYGFSTYRKNDTSAVKTWLEEHSIPYGSRSSPSDFQQFISESYDSLVPNLDKWSGHNLNSWLGKKTESSYLDAISNKIRKTGRKLSGSVEDARDATQEAWESQKASLFESWSDSQLRAFLARHSPQFAAKEKKGILEKLSPASLRETAAKEYDALTSKLGNTGDWIYDTWSDNELRTWLHDVGVPISSHESTRSHLLRKLKNYISTKADEAQPSVEAVKGKASEKAKQAGEFVSDKAGDAKELVNEKSSEAGQYAGQKMEEGGELLQEISKRRGRFGNWWANSGLKAYFDAHGIPAYQPSPIDQFYAHLRRQYYLKTNGYQALKSKAYEEASNVADSASSIASNVASGATEAYQGAASGASRFTEGAKTAAESVTSAFEHNKDTATSKAKQMKGKAASLGSTASEKVGEAADYAAETASKVASKAASKVRETIDETIIERWQDSKLKEFLFLRGVPVPQRSTKDQLLDLVRKHFNKGAVPNWAAYFDTLSSKELSAWIKEYKKHYHGKLHPSKDREHLFQNACNIYRAIAEKADKSVLQSIQSKFPKATVPGYDSWSNEDLKSALKEYGDSIGKVFNRKDAIERLKRHDILFYGPVVADKAKSGVSGFLRRVASFMGFGTRDVAEIKLGENIQKVKDTASKASSAVSSAGDYVETNVKKAQRVL Q9Y7X7 YGRB_SCHPO MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 202; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 204; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC365.11; CHAIN 1..266; /note="GRIP and coiled-coil domain-containing protein C365.11"; /id="PRO_0000317082" METTVSAKNSLENENFLKEKSETVFLDEAAITKPPASKKKRKNRKKKKNNGPSEQFVGNNDLEEQRSGSIDSKDKEKPLDEKVKELENANKTLSDLVRRIQIQRDEAEQKAEIYNRDALNTKQEHLDIKKRLEKSDETVCKLKEENENLQDMLRNVGNELVESRDEIKELIEKQKVQKESVKSHESELSSVMSSEILPKASSDSAGSFEPPVISNISKELINKEYARNVLLQFLENHEHRDKILPILSTALDLEEVHQHLILKNLN Q9Y7X9 KIN17_SCHPO SPBC365.09c; CHAIN 1..304; /note="KIN17-like protein"; /id="PRO_0000351449" MGRAEAGTPKAISNALKSKGLQRLRWYCSACQKQMRDENGFKCHTQSEGHIRQMNVIAMNPGKRIQDFSNQFLRDFISLLRTAHGEKKIHFNQFYQEYIRDKNHVHMNATRWHTLSEFCKFLGRQGMCRVEENEKGFFISYIDKNPANILRNEANKKRERQEKSDEEQRLRLLDEQIKRAYESAQNNEDNKDGSSREQPVLHEIDLSKKGNPIQLNLSSSSDSHSAQNEFFQTRNTPTFSFSSSSSQTSLKHKPKNVFAELNKSRKKNNKDSLDQGQNVKRPRSAVEDIIAQETMREKRRNIKL Q9Y7Y2 SLU7_SCHPO SPBC365.05c; CHAIN 1..379; /note="Pre-mRNA-splicing factor slu7"; /id="PRO_0000218552" MSYMNNTFQSNYDYSKDKNFMSTDIGPSMREMKAQKRRSRPMDNPDADNPYIPKFISTAPWYAQDDDAVERLAHQRIGKKETPSGGRSSIEGSWYVRGKKLGPAATKYRKGACENCGAMSHKVKDCMERPRKRGARWTGEDIQADEVIQDINVSWDAKRDRWNGYDATDYKKVIERYEKLDELQNKGEENRDASENSAVKASRNSTVSGSEDSASITTPSLRMREDVVAYLRADNKNLQYEPKSRSMRDETGYHMVDDSSGGAGFVKASGGEKEDFEKLQMFAWEAERSGTRVHVVANPTAGELEFRKNKASRMTTQKHIDQSILDRYGDGTSKVKDKKAKNNEKEVPDLAILDKSEKSKGESNTDEESENLVIVEGDL Q9Y7Y4 COX10_SCHPO CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o; Xref=Rhea:RHEA:28070, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:60344, ChEBI:CHEBI:60530, ChEBI:CHEBI:175763; EC=2.5.1.141; Evidence={ECO:0000250|UniProtKB:P24009}; TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC365.02c; CHAIN ?..387; /note="Protoheme IX farnesyltransferase, mitochondrial"; /id="PRO_0000045420" MFHILNKGSSKSCIYTRPCLKRFYHQHYEHTGKLSRTFFSPTHIKYNRLSTLDTSTSTANAAPDPQVLTFLSKRMQAAPLYPKPSAFLELGKPRLTVLVVLSTMSSYALAPYPGLSFNTLAWLTMGTALCSISANAFNQSMEPMLDCQMARTRSRPIPRGAIRPEYAWLFATLTGIAGTSMSFLVNPTVGWLGLGNIVLYMGIYTPLKRISIVNTWVGSLVGAIPPLMGWAACSGGDLLSHPGGLITAAMLFAWQFPHFNAFSTMVKDDYKKCGYQMMAWKNPALNARVSLRYALAFLPLSYAYISTGLVGPWYAVPATGTNMFLIARAWKFYRNRNYQNARSLFFASLLHLPLLFTLTLACHMIKVWNDSDSKNPVLGSEEDTLKY Q9Y7Y8 SYQ_SCHPO BINDING 270..272; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P00962"; BINDING 276..282; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P00962"; BINDING 302; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P00962"; BINDING 447; /ligand="L-glutamine"; /ligand_id="ChEBI:CHEBI:58359"; /evidence="ECO:0000250|UniProtKB:P00962"; BINDING 466; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P00962"; BINDING 495..496; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P00962"; BINDING 503..505; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250|UniProtKB:P00962" CATALYTIC ACTIVITY: Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662, Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521, ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000250|UniProtKB:P47897}; SPBC342.02; CHAIN 1..811; /note="Probable glutamine--tRNA ligase"; /id="PRO_0000195865" MDQDYEELRAKFTKIGLNETTVKDTLKNKKLSSSLNKVIEETNVGSSGCDRTIGNLLFTLANASLKQKDPKSNAHEAFIASKIVSGDLKTNLQVNAAITYCKDKDTIDESEFDKETGVGVVLTPEQIEQLVGDYVAENKSKILEQRYQLLNPSASALRQHALLKWAPQLEVKQTLDRKFLELLGPKTEQDAAAGKKKGAKAKNSKQKTVDSGKAKEQKIVSEQSKKYNMFEEGFLAKLHKPGGNTQLIPERMKEHLQATGGGVVTRFPPEPNGYLHIGHSKAIAVNFGFARYHNGVCYLRFDDTNPEAEEERYFESIKDLVAWLGFQPYKITYSSDYFDKLYELAEELIKRDKAYVCHCTDAEIKKARGGEERGPRYACVHRDRPIEESLLEFRNMRDGKYQPKEAILRMKQDLSDGNPQMWDLIAYRVLNSPHPRTGDKWKIYPTYDFTHCLVDSFENISHSLCTTEFILSRVSYEWLCNALEVYCPAQREYGRLNVVGTLMSKRKIMKLVKEGYVHGWNDPRLYTLVALRRRGVPPGAILEFVSEVGVTTAVSNIEVARFENCVRKFLENSVPRLMFLPDPIKVTLENLDDSYREQIEIPFNPKDPSMGSRSAFLTKHIYIDRSDFREEASSDFFRLTLGQPVGLFRASHPVVAKRVVKNDEGEPIEIIAEYDASSSKKPKTFIQWVSRDKESNSPVLIAETRLFNNLFKCDNPAALKEQELAAQLNPESEVVLKNSIIEPGIYDLIKSAPWPKTDSSAGVDKAENPESVRFQAMRVGYFCLDEDTKKPNHLVLNRIVSLREDSAKNKN Q9Y7Y9 YOD2_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPBC18A7.02c; CHAIN 19..457; /note="Uncharacterized membrane protein C18A7.02c"; /id="PRO_0000339415" MKLLISLLWSIFFSIVYSEKTLLNFKHYELCNGIYSKSESGGSLNPAIYVNWTEPWGQEDEVEVLIFNWKEIRKLGAFRSDDQFTYICDYDAVYTDHLCEADQLGLYLWNSTSAKSIRSYIIPTNADPQNIIYEISQSGYYCIWSHSKKMLPYQALVNWQNAYGGLPASQFPRMPISGGITIAYSVILALWMFFRFQYKHSIVTVQKAIMFLLIFSCAQQAVTSIVLDTENLRNRGNFTWLGETLVSILFACQLVLDLALLLILSWGYTRYSTNMRDRLFTEAKIPLIICFFALFVVRFFAITIQSIHLGLWFCFFFLTACISALYILFGAFVALPSTLRALVEQRYYTLHSIYKIFRIMVLCGVVTIFSFSLVALIFCSNTNNNSTNKLWKIRWYFLDGWIDGVHLTYLITLSSLWRPSQENPDLDPTGLSYPVLDPRLEEELDLLEEDIRADKSK Q9Y7Z1 NOP16_SCHPO SPBC1539.10; STRAND 12..14; /evidence="ECO:0007829|PDB:8EUY"; STRAND 42..44; /evidence="ECO:0007829|PDB:8EUY"; STRAND 186..188; /evidence="ECO:0007829|PDB:8EUY" HELIX 4..11; /evidence="ECO:0007829|PDB:8EUY"; HELIX 34..39; /evidence="ECO:0007829|PDB:8EUY"; HELIX 46..52; /evidence="ECO:0007829|PDB:8EUY"; HELIX 121..124; /evidence="ECO:0007829|PDB:8EUY"; HELIX 136..151; /evidence="ECO:0007829|PDB:8EUY"; HELIX 161..174; /evidence="ECO:0007829|PDB:8EUY"; HELIX 180..184; /evidence="ECO:0007829|PDB:8EUY"; HELIX 195..206; /evidence="ECO:0007829|PDB:8EUY" TURN 175..177; /evidence="ECO:0007829|PDB:8EV3" CHAIN 1..209; /note="Nucleolar protein 16"; /id="PRO_0000320385" MANPRQRNKQRSGKPRLTRRNANKKAKAKIYGNFVIQQNWDKHATLRQNYARLGLLATPNYVTGGVEKLYPDPKRENEDRELTSEELDELKKSLPPGQAIVRRDDDGNIIEIIHGEAKTLDDVLDKEISIAPAKTEVVRQLEEEAVKKAARQSNKMLPLSAFEHAYIQRLINKYGTEDFESMAKDVKLNSKLFNGSKLKNLYIRMKATK Q9Y7Z3 ACBP_SCHPO BINDING 13; /ligand="an acyl-CoA"; /ligand_id="ChEBI:CHEBI:58342"; /evidence="ECO:0000250"; BINDING 28..32; /ligand="an acyl-CoA"; /ligand_id="ChEBI:CHEBI:58342"; /evidence="ECO:0000250"; BINDING 50; /ligand="an acyl-CoA"; /ligand_id="ChEBI:CHEBI:58342"; /evidence="ECO:0000250"; BINDING 54; /ligand="an acyl-CoA"; /ligand_id="ChEBI:CHEBI:58342"; /evidence="ECO:0000250"; BINDING 73; /ligand="an acyl-CoA"; /ligand_id="ChEBI:CHEBI:58342"; /evidence="ECO:0000250" SPBC1539.06; CHAIN 1..87; /note="Putative acyl-CoA-binding protein"; /id="PRO_0000316197" MSSTFEQAAADVKELKETPNSDELLKLYALFKQATVGDNNTEKPGLLDLKGKFKWNAWEELKGKSKEDAASEYISFVDELKTKYGMK Q9Y7Z4 COG3_SCHPO SPBC1539.05; CHAIN 1..735; /note="Conserved oligomeric Golgi complex subunit 3"; /id="PRO_0000316217" MFDQLEFYPAVNYEDNETQNDIKLPEVAKLENIETVHSISKERRDSLTEILNDSSSLPARPFSLPNPNNSTVEKQSLFPFEEKMNPIWIISRPTFSIEQDAEKKINELQTFTNIIDQILGQTNNIESTLLSMKEKFESSEKKLSEFSEMCENLSTDEMRFSEIADGIRKGLTIFAPLKELTRVFRHPPPDFAGKVSFKEHITQLNTCIMFLEENLDFQESPHYLGQYKKLLSQAMDIFKPYFIRIIKQTTDQVLKDSKKMDVHKQLHSSLFYARFSAVGHNLCPTITELCKLCSKESLDAFLPAFYDVYFQCRTRLLKPVLDYHLKSFFMEKSISSYIQKSLALLQLTFFDENKLFREILIMDDFRFMHYWNNLCQSFFENSRSLILHEKNLTELCEVCSYIQSFQNAILEGEREDVDKKVVEFLNPLVLELQERLLFVVQTAIETDIQRYSPTEEDLNPIADDKSLLFDLEKLRLNNDEEKLDPDVPQKLAMAQGWYPVVQKSLIILSKIYRLVNSQVFDEIALELVHSCIRSLVDAYRYFSRNNDKQLARLFLIKNFLVLKDQLNSFDIHYACIEAGVDLRKVWDSVREWRSNLRGVLQLVYETFPKFITNAVDTRQELNQQLRVAVNGYIETAVIHYTECLSIGNLESITEFQNRIQKFPELRQQISLYLSETWIIELFLQAIREEVVSKFQNFYESIVANEDITGSDHNKSGTTSLKHLNEYVEDIYSVMS Q9Y7Z7 RM15_SCHPO TRANSIT 1..59; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1539.01c; CHAIN 60..210; /note="Large ribosomal subunit protein mL57"; /id="PRO_0000351439" MLTRHCNRLGLQIENKFVFRSSSWNCVRRIGKIACNENKYRYEMTSTEEDIDSFFSRVFGEKNYISDKSLREQIVTHKSYKHGLKRYNEPFVSVGNAVIDVCLLNHYLESGNFSTIPSYKDLVNLRSPARLAEVAKKWNPETATQCILPLKGPNSPSSSSFEKIYSSIVSGLVAVVYFQKGGVEAMNFCKKSIISDLTKDFVRPNTVHNQ Q9Y7Z9 COQ6_SCHPO CATALYTIC ACTIVITY: Reaction=4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20361, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58373, ChEBI:CHEBI:84492; Evidence={ECO:0000255|HAMAP-Rule:MF_03193}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03193}; SPBC146.12; CHAIN 1..479; /note="Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial"; /id="PRO_0000207582" MSSLVLRGVSRVEMPTISPTLGIYTRKFASQKILQRQFDVVIVGSGPVGLALAAGLQSNPVTQSLKVGLLDIQDTMKLKDWKFETYSNRCSSLTNHTRMFFDKIGAWDFARKDRIQPFQHILASDGLTNSSIHLDQKPGSEPMAFMSENVNLQYALLNSIIDKMNNNIKKPNLEFLMPCTITKLSKGENIYRTHIHTTTHGELTTKLLIGADGRNSIVRKYANISMPGWNYLTHAVVGTLKIDPLKGPAVAFQRFLPTGPLAYLPLPDNNATFVWSTRPHIASKLLRLPEETFVKFLNASFRLDYPDLSYLYQMDFSEPSKVNEQLDWRLQVKRNSNMQVPPVITEIVSGSRAAFPLRLAHVDEYVKEGIALCGDAAHNTHPLAGQGLNTGIQDVESLISALSFAIKHGQDIGSVFSLQPYFRDRYFKNHVYLGVVDKFHKLYAMENPVVTSVRTLGLSLFDRSASLKNFILSTVANGI Q9Y801 YFAS1_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPBC146.10; CHAIN 25..189; /note="FAS1 domain-containing protein mug57"; /id="PRO_0000008799" MMKLFCLNIFRFLYTTSFISAVLSFNQRPINMQEVREPRLFELLAETRDCNIFSELIMQFPDYVHLFQQKDQHITVLVPNDAAFQQCKVKPWAIEYKNGVAVKSTDIVHITEQQAQDNILKFVERHIITSSPIEWNNEYKTIDGTDVHVIKKEEEIYINESIHVLCRKKASNGEMWVLNATLSTPSIRE Q9Y803 YN98_SCHPO MOD_RES 124; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 126; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC146.08c; CHAIN 1..127; /note="S1-like domain-containing protein C146.08c"; /id="PRO_0000317699" MSKKYGGQISFDPPARLEKDQVVAKVVQLKGSALFMVVENNGQELLVEMPPKYRNKIWVRRNGFVIVDKSEFLEKDNKIDGTILYVVQSPLKNWKKQIYWPKEFADESLNQNDSEESSSSEEEYDSD Q9Y809 NAA25_SCHPO SPBC1215.02c; CHAIN 1..811; /note="N-terminal acetyltransferase B complex subunit arm1"; /id="PRO_0000353830" MRRSGSKESTIVYSALSLAQAGRGPEALALLEPLKSTPINSLELLDIIQAVYDDQKKGEESFVFWEKFLQTYGKQEKNLLAYFKASIRIKSLSHQRKAAVELQKNFPSRKHTLWVISSLYLLSKKSENEVEQRLLKALAEKTAKLIFEKPTGYIDSCEEFHLYLDVLLLVGDKDRALDALIHQDADRFVDADADLLLRKLELLASCARWDSLFTFSLSLFQTGNTDWKVCKALLDSASNDDSKLVPLKDCILKALSTSSTKRNLHLLWIEASARFFPEEHESALLGYIKKLYMKPIVFEDLRPYLLKLNVDAQHRLLDAFKLADLGESNESQKVDKLYAEVLLLKIHFLLFESFTAESVVDYVRRCFVAFEKGLSLSKGLLPTDFTHGYEALLLAVHSLIYMWEGNKDLKPAEKQALIFDAICLLEKGITYSQHNFHLKLPLIRLYLLLDGGFPAAAKVYDTMSIKQIQNDTLDHYLLTRATTYYPSSVTSHYINSSLKIYGSNEFETPEMISMAYEDGAYSQIEDMRNFRSRLDHSTWKSISLVERARIHYLTAFKPPKQYLPKCSSPKDNRDLKVFADYGSDKLPTVEESLRNSPKPDTLWIHLTVIGHSLVQDSIVNGDFEKAVLSAKEMEVLCENNDLSKQLTSEEIVHMKLLIQLGLLSVKVKNGDYENSSFETIENLIESFDYENSTPLSQLTKYTEIINDLITCLNSFLYHVSATKKKEFTRQYQLLKNISSNKLGSISGITKHKKKAARKYVSELLSNSWLSNLSETQVPYDPKFAKQVGEGMIDSYIQTTDAVSKLPKFVKF Q9Y813 RPR2_SCHPO BINDING 59; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 62; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 93; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250"; BINDING 96; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SPBC1105.16c; CHAIN 1..107; /note="Ribonuclease P protein subunit rpr2"; /id="PRO_0000317087" MSTKSKDQHARVSYLYQASQLLFRNVQEPTLSRHYISTAKDVSQKSVMRIHPDIKRTICKGCNSLLVPGKSCSIRFEEPSRKNPSIDRVLWICKKCAFKKRFSDKSC Q9Y815 RSV2_SCHPO SPBC1105.14; CHAIN 1..637; /note="Zinc finger protein rsv2"; /id="PRO_0000310841" MDTTNNTYARSISSNGNDNFPTPDWQFNGSQLQQNRKSKMNGRSVTNVFPNAFSDAEFEQISMPELNLKRFNPTTLEENNSDLSDMSSWDYMMNVPIRVYNDADTMDPFSLDTIPDSSMDMPFDPLASDYGNAANFPSVPSSLGSNHQFITTPPVNGSNEPTSAQTNHIITANSSPSGNAGSNASASMSVPPPLTPSASTINDQPFSNSFDLPSQVIADGTGAISDINGNPFPMNSPPLDMEPLPSISMDASDSVSEQLVKDASLPSGPFSTDYLENGSDLKRSLGHNQKSDRVSKDVSPQHQANPSTLNNPLKTQNFDSSKNLYTDNKDSSLVSPTGLQSRMEQNPEVRAHPMKDSATSTALRRSHALGAAADSLLPQENSAQIYDGKDVSMVNDNMHSDVRQDSFNKESIKQRIPSLSPPITRSYNAKHRPSLVLGTSVNPHSLSPSQPPVVVPSNTTISSSPPLTSPVKTSANIPNLLPTSELDSSNAPHSQSAATHDLNDVKSYYNTRSSHSVVPNPTNQKVSITGAAADGPNGSAPVDTTPTNSSTTATGAQRKRRKFKFGKQIGPVRCTLQNRVTGEICNTVFSRTYDLIRHQDTIHAKTRPVFRCEICGDQRHFSRHDALVRHLRVKHGR Q9Y818 UBC15_SCHPO ACT_SITE 90; /note="Glycyl thioester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133" CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; SPBC1105.09; STRAND 25..31; /evidence="ECO:0007829|PDB:5KNL"; STRAND 34..43; /evidence="ECO:0007829|PDB:5KNL"; STRAND 54..60; /evidence="ECO:0007829|PDB:5KNL"; STRAND 71..74; /evidence="ECO:0007829|PDB:5KNL"; STRAND 87..89; /evidence="ECO:0007829|PDB:5KNL"; STRAND 101..105; /evidence="ECO:0007829|PDB:5KNL" HELIX 5..17; /evidence="ECO:0007829|PDB:5KNL"; HELIX 92..94; /evidence="ECO:0007829|PDB:5KNL"; HELIX 117..129; /evidence="ECO:0007829|PDB:5KNL"; HELIX 139..147; /evidence="ECO:0007829|PDB:5KNL"; HELIX 149..167; /evidence="ECO:0007829|PDB:5KNL" TURN 49..52; /evidence="ECO:0007829|PDB:5KNL"; TURN 63..66; /evidence="ECO:0007829|PDB:5KNL" CHAIN 1..167; /note="Ubiquitin-conjugating enzyme E2 15"; /id="PRO_0000082589" MPSSASEQLLRKQLKEIQKNPPQGFSVGLVDDKSIFEWEVMIIGPEDTLYEGGFFHATLSFPQDYPLMPPKMKFTTEIWHPNVHPNGEVCISILHPPGDDKYGYEDAGERWLPVHSPETILISVISMLSSPNDESPANIDAAKEFRENPQEFKKRVRRLVRRSIEMI Q9Y819 YON8_SCHPO SIGNAL 1..26; /evidence="ECO:0000255" SPBC1105.08; CHAIN 27..629; /note="Transmembrane 9 superfamily protein C1105.08"; /id="PRO_0000315979" CARBOHYD 157; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLLPSIPSCSFSFVVFVSVLLQTCFSFQLTPLSPKNYPPGASIDTTVNTISPFIGDGRGSDIFNYEYYDERFHFCRPENIAKQSESLGSVLFGDRLYNSPIEIKMLENQDCVPLCASIIPSSDVSFIRDLISKNYVVNWNIDNLPVATYLEGTNSKNYSLSPGFPLGKNTEKGVILFNHYDIVIEYHTTSSDQHRVVGAYVKPVSKESTLVDGNPVCSSSSNPQYLPEGADLTLVTSYSVSWKYSDTPWATRWDKYMHIESRQIRWIFIIHSAIIDTFLIFVVSIILYRTLNRDINKYNSAFVDQEDVQEDFGWKLVHGDVFRPPRRPMLFSILLGTGAQLLFMSSGIVLFAIFGIVAPSRRGSLATATVALFIISGFVSGYVSALSYKLMQGMLRKRNLLLTPFVVPGFMLAAALFFNMVFWSKSSSSTVPFSSWLLLIFLYLLFTVPLSFVGSLIGFRSREFVPPVRTNQIPRQIPSHSIWLSSFPSAIIGGSIPFLVILIELFSILDSLWFHPLYFMFGFSFFCFGILVTTCIMVSIITVYFQLCSENYNWWWRSFITPGFCGIYVFIFSVFYWFFKISSSSLATAVLYFGYSLLISVLVFFLCGSVGFFGAFLFVNKIYASIKID Q9Y820 YON7_SCHPO SPBC1105.07c; CHAIN 1..442; /note="PCI domain-containing protein C1105.07c"; /id="PRO_0000317134" MSLNDFLQTLSNAVGEKNSNTLEKCIILDPSEPSFQQLSKTLFLDRKGKNKLNGTIQKEFGRIRGWKELVTTYFEYVENAASSPDQRKWELLQNLYSNLTTCFSHIDGAWLCTIVKRVSKLYVKLSLQLDTSTPTLEDSFDGNGFIQRKYVSDASRNVLRTFNSILSDRQQNINPSKKDAIFCIANLLCLLYFRLKQIRLCQTIQANVISSGADISRATMAELVTFRYYLGRCHLYQRKIHQAKDHLLFSFLQCPDECYHQKRLSLIYLTTCLLILGKSPTKGLLEKYKLTAAFEPLIKALKSGDIKSFRLSLEDNSRRKWFIKRGIYLTLLDRCEIILWRNLFRKVFLFTFEQSQKTPHVSGSYLLTAARLSTNDNSYDMDDVECICVSLIDQGYIKGYIIHASSTLVLKKDPSFGFSVIESLMPIARNDHAEKEFFHANA Q9Y825 YEC6_SCHPO SPAC25H1.06; CHAIN 1..408; /note="Uncharacterized WD repeat-containing protein C25H1.06"; /id="PRO_0000316553" MNTELDMQNFEHIKFLENQISEDHFRWKKNSKHLYNLLITRTLTWPSLSIQWLSAMESITEKAVLKNRLLLGTHAAEGMPNFLQLADLDLPDFNQTILDPVKHYNEDTGELGGYSMQHSCKFQISQRILHNGDVNRVRHMPQNPNIIATMSSCGNAYIFDRTKYTSMPAEEFLPNISLIGHKKEGFGLSWNRQQNCRLVTAANDSKILEWDLNNFSRDTRCLTPVKDFHYDDSPVNDVEYHPHHTNLYIAVNDNGIAFICDNRLQQTCSKTVKASNPLFSVRHNPSIATLFALGSEQDLQLWDLRNLNKSVFNTSEDLSDNRLKVPSRLTLGGTSLSWSWRHSGRIVSACQEYCYVWNFNKANPLEFVHAGHKGTVNEVDFDPFEAQCIASVADDNELHIWKPNVIVN Q9Y827 TGL5_SCHPO ACT_SITE 174; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"; ACT_SITE 327; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:Q12043}; SPAC1A6.05c; CHAIN 1..483; /note="Triacylglycerol lipase ptl3"; /id="PRO_0000317235" MSKNEIKLQMEYASSYETWLEAAEKLDVIEGKYQWREQKESDEYDYVLVESRLHELRRHRLSKNTRLLLGLLRNSVARDFANMDNSRLYNYAHSGTKKLIDEFIQEVLMCLTYLEETPDLSLDEKITEFSRLKLTTGNTALILSGGGTFGMTHIGVLQSLHEQGLVPKIICGSSAGAIVACAAAVRNKEEQEILLRQFHTGDLSVFTDPNAAPPSVIQSVKQYFTRGCVLDISHLERVMKLLIGDFTFQEAYDRSGYILNVTVSCGSLFEMPSLLNYITAPNVLVWSAVVATCSVPFLFKRATLWERDPLTREVSAFCVTDAPLWMDGSVDNDIPHAKLTELFHVNHFIVSQVNFHIVPFIMDPTSHNWVERCCKKAIDLAAQEVSLTFRLFAELGIFSVLFTKLQSVITQKYSGDITIIPRLNYREVNKVIKNPTPSFLLDAATRGKRGTWTKVPVTRNHCAIEILIAAAYTRLIKRSKSLK Q9Y876 SHR3_SCHPO SPBC409.20c; CHAIN 1..215; /note="Secretory component protein psh3"; /id="PRO_0000097739" MAKRSIFRFADEKGLKVAARYGVLMSTSFIFALLFHSSVADVNTLWSPGPESAFDAAETYYTLVAGSHFIVKYTVYTIMGLNMIFHLIQATGAKGDDKLFFYSSTLLYLTALILFIVNVAPSMLVVKLQNYVQFPRNMHLSVLAASHVLVEFLLAGVILIQLGYVFGYHVQSIQQREYAEDMREQELAEKAKLESESATTQSVETVSTESVSKRK A6X972 GON7_SCHPO SPAC6B12.18; CHAIN 1..73; /note="EKC/KEOPS complex subunit gon7"; /id="PRO_0000303984" MNNLELTYKCETDTTRPFLKSLPVGFEPVEVDDYYISLKEQVRAMQDHCNEEFTKKMQTEGKNDVPEEKPIIL A6X982 YOGD_SCHPO SPBC15D4.13c; CHAIN 1..204; /note="Uncharacterized protein C15D4.13c"; /id="PRO_0000304127" MRYPNLLFLALPISEHYIEESLKYFKLTSNDPMILSGFRGPRVSHLTIGMIPVKNDEDVLKCMDFLYNKEDEIRKSYGEKKITIDLKGTSFFGKSPQEAKVLYATPVDKHNEWLKVIFTEHNLFTKDARPLTLHCTLLNSRYIKYQGRRIRFFNSEPFMEKYGQFLWAHNIELDKLSIMKTGAVGEPGNMYYEELASIPLLVND B5BP45 YP51_SCHPO SPBC460.01c; CHAIN 1..572; /note="Uncharacterized amino-acid permease C460.01c"; /id="PRO_0000415919" MSHNNFELSPDYKDIDKKDDLNPSIVEKGYVEGVVDDVQPERKSFITKFFDDFKPAISTDEDGSALKRSLKARHMQMIAIGGAIGSGLYVGSGSSLSDGGPASIIINYTLIGIMMFFVVYALGELSVAYPVAGGFNTIATRFIDPAWGFTISWNYFINYFITFPLELTTCAITFRFWTDINSAAWISIFLVIVIIINLFGVRAYGEVEFILSTLKVIATLGFIILAIIINCGGVPTDHRGYIGGSIIKKDPFRHGFKGFCSVFTTAAFSFSGTEFIGLAAAEVDNPQKSLPHAVKQVFWRIAVFYIVSLTLIGLLISPDDPNLMGNGSTSVSPFVLAIQEANIKGLPSVFNAVIIISVVSVTNSSTYAAARTLHGMAGLGHAPKFFKYTDRLGRPLIAMVVVLLFGFFAYINEADKNGNDVSDTVFDWLLALAGLSNFFSWGSICLSHIIFRLAYKRQGRSLRDLGFVSPMGIWGSCIGLFFNILCLMAQFYVSLFPIGGKPNANDFFQGYLAACVAIVFFVGYKIYDRSHVPSLDKLDISTGLRTYENSDEEDETSSGFKHVLKKIYGAFC B5BP46 YP52_SCHPO CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; SPBC460.02c; CHAIN 1..220; /note="Putative glutathione S-transferase C460.02c"; /id="PRO_0000415923" MFLGTIYSFKTNTRTPCLLELAKRLDLQVDLVETYHHKFPTDLAAKFPLQKLPVFIGADGFELSEVIAIFKYFYEKGKHNDKEGLGPINEIEEAEMLKWMCFINFDIVTPQIVRPWVDMFRGSVPYEDKAFKESAARAIDSLKIINELVKDRTYLVGDRFTLADLFFGSMLRRFFHSIIDEKTRKELPHLTRYYVTMFHQAKLEAYYPLELPLTVTVPNN B5BP48 YP54_SCHPO BINDING 204; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 206; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 231; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250"; BINDING 338; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250"; BINDING 353; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 364; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250"; BINDING 368; /ligand="2-oxoglutarate"; /ligand_id="ChEBI:CHEBI:16810"; /evidence="ECO:0000250" COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; SPBC460.04c; CHAIN 1..391; /note="Putative alpha-ketoglutarate-dependent sulfonate dioxygenase"; /id="PRO_0000415922" MATLTETISKADKHDEKLTDFQYSKKIFNGVHEVEDDKQRTDFTTVRFGDVEKKFAVPKDYKYKNVLPTFPNAVYNLTGELAFEDKGLLADPKFSNLLKDVTKVEHLARDLGTVLYGIQLSKLNDAQKNELARYIAERGVVYFPDQEQTLEEFQELGQYYGHSHKHGSNSRPFEDKFAEFQVVYSDRFSPYDQHAKNNSLRYWHSDVSFEKQPSAQTFFKALTVPEQGGDTLFISGYAAYEALSTPLKKYLEGLTVVHSGKEQSEYHRRSGQHVRLDGDTNAHPIVRTHPVTGWKSLFISPGFTRYIPGIPRGESDAILDYLYQHIANLSQSTVRIKWTSNGVAAWDNRIVIHRATYDHLPQTRHLVRIAAQGEVPFFDANSHERSEDLRE B5BP49 YP55_SCHPO SPBC460.05; CHAIN 1..530; /note="Uncharacterized transporter C460.05"; /id="PRO_0000415920" MNNMSLKFPDIAINSSESSDDEDPSSKNEKKDGSIKVVKGLTDEKKVFEKAKNDFDEALAIIDDDDFEYTKSEDDKVRRKIDFFILPIMCITYGMQYLDKTAVSYAAVYGMKQEAHLSGYVYSWLSTIFYLGYMIAQYPAGYLLQKFPISYFMFIAAFLWSACVLLMAACSNRHGLLTLRFFSGVFEGCVNPAFVALTAMWYKREEQPVRVVSWYAFNGVAIMVGALLGYGTGHIKGSLQNWKYPFLVIGAISTAWSFVYLFFPQNPVLARFLNAREKRIAVERVRKNRTGMETKKFKPSQALEAFKDPQVILIVLYNGLCQVTNAMSVFSALIIQGIGYSGINATLLTLPSGAFAVAGMIASGIFTHYFKKGRIPLAMTTSSLTIVGSIMIWKIPHSNPWPRVVGVWLFCTISSGNAVILSLLSSNISGYSKKVTVNATMFLFYSIGNIVSPQLFKAGQTPEYIEGIQASLVSVCLFEGVLALLAFYYIFENARRDKLLENNPALGGEIKNEEFLDKTDREQIKFRYVW C6Y4A3 ATP19_SCHPO SPAC25H1.10c; CHAIN 1..68; /note="ATP synthase subunit K, mitochondrial"; /id="PRO_0000389140" MSVYTIAGRQFQAHQLSLAVLGSVFVGPVIYSKLFKRNKPLSAKDVPPLNAKSKEEEEFILKYIEEHK C6Y4A7 EMC5_SCHPO SPAP4C9.02; CHAIN 1..106; /note="ER membrane protein complex subunit 5"; /id="PRO_0000389151" MESSTINAKKISVLLTLFSIIGYTAYSAHESILEIRQDGKLPLDIKCEVILVTLLFTFTTVIIASPLRSIQLNKWSHQRSDLAFLNSRTNFLRIKELKEKIEKVKN C6Y4A8 YAEP_SCHPO SPAC23D3.16; STRAND 15..17; /evidence="ECO:0007829|PDB:8FW5"; STRAND 19..33; /evidence="ECO:0007829|PDB:8FW5"; STRAND 37..40; /evidence="ECO:0007829|PDB:8FW5"; STRAND 49..56; /evidence="ECO:0007829|PDB:8FW5"; STRAND 62..69; /evidence="ECO:0007829|PDB:8FW5"; STRAND 72..79; /evidence="ECO:0007829|PDB:8FW5" HELIX 3..12; /evidence="ECO:0007829|PDB:8FW5"; HELIX 41..44; /evidence="ECO:0007829|PDB:8FW5" CHAIN 1..81; /note="Uncharacterized protein C23D3.16"; /id="PRO_0000389143" MDSQLSENLLKCVNETYRGAMLVRNGLPIATAGDVNAEEQRVICEWNSNAVSEVLHLHDSNTKILIATKESCVLGLIYRNT C6Y4B3 PGA1_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC167.09; CHAIN 21..178; /note="GPI mannosyltransferase 2 subunit C167.09"; /id="PRO_0000389147" CARBOHYD 48; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 49; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 106; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 115; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 122; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MREFRLIFVLLFFLPSFAIANTEIINVETGDSNKLLTSNSVCDIELSNNSSIPLLLKPNPTIPQAAGAPQQSKYTFSVCGLKPLQKYQIRASWPAVYPSDIILNYNITHIIVEINASFYSHNESLMKRPPLVPLRLVVEPLLLGFLPKSVLPIVGFVFVIILIALICMTNLFIKHKRD C6Y4B6 NCE1_SCHPO SPAC12G12.17; CHAIN 1..58; /note="Non-classical export protein 1"; /id="PRO_0000389167" MSQPYLISKWMDPLFGIFVGTYGYYLYEKEHRPRGRSLRELALRKWNKQAVSQQSMKN C6Y4C0 YFMR_SCHPO SPAC222.18; CHAIN 1..111; /note="Putative splicing factor C222.18"; /id="PRO_0000389142" MSNAPSNTPTGFNYKPGHTLYIRNFGTDMRARTLGQAFEKWGRIVRCDIPISSNPQAHRYAFVEFEEREKAELAHEKMRNAKIGNDIIFVEWAKSRERYHRDDKRRLSNYA C6Y4C1 PT117_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1604.25; CHAIN ?..88; /note="Protein pet117, mitochondrial"; /id="PRO_0000389139" MSTASKLCIVGAGVFSVYMVYFVHNNQIIEREKMSAGVQKDDERKRIKKERFEDLKRQQELRKFYESQLPVEEDEKGLRQTTQTTVND C6Y4C3 ECL3_SCHPO SPBC8E4.12c; CHAIN 1..89; /note="Extender of the chronological lifespan protein ecl3"; /id="PRO_0000389116" MDLNLCLLCGNSIDAEGLYCSNECRIQDKATTELFSDPLKSPSLNETIDYLALNYFDLFSRRSSMCSSSNSSIYSGIYYTELKNYSVEN C6Y4C4 SDHF4_SCHPO TRANSIT 1..31; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC26H8.16; CHAIN 32..100; /note="Succinate dehydrogenase assembly factor 4, mitochondrial"; /id="PRO_0000389141" MFNRNLRAVILKNYNKALTRCLHDAGNLKRPTPPRLPKEQQEEWDRLQKESSKRPVDVMRREKHKDFEGDVNPKTGEIGGPKSEPTVHGDYSYEGRVTDF C6Y4C5 ECL2_SCHPO SPBP35G2.16c; CHAIN 1..84; /note="Extender of the chronological lifespan protein 2"; /id="PRO_0000389115" MDLDYCIICGKPTTGNLYCSRECHLQDCPGCGSTSEQCSYSKSADLHMLSSQYLDHFRRRSSMPSPSTSSSLLNGFVASRLAVL C6Y4C6 YGSQ_SCHPO SPBC29A10.17; STRAND 100..102; /evidence="ECO:0007829|PDB:8FW5" HELIX 43..59; /evidence="ECO:0007829|PDB:8FW5"; HELIX 82..87; /evidence="ECO:0007829|PDB:8FW5"; HELIX 106..124; /evidence="ECO:0007829|PDB:8FW5" TURN 64..66; /evidence="ECO:0007829|PDB:8FW5" CHAIN 1..153; /note="Uncharacterized protein C29A10.17"; /id="PRO_0000389149" MGNCCSFLFNNSDDIDEQTPLLNNDGIQRTPPSAEADMSLRKREEEEEWESKVYDVAKNKFIDVFSLRLRTEAPQRDPRDNIYEEVLDQIDSLNLDPKYDVAKPTEQETEFIIRKLGVLIDDINNIKLSDKEIKGKMVINLSKVQPNITGSPS C6Y4C8 VMA21_SCHPO SPCC1235.16; CHAIN 1..88; /note="Vacuolar ATPase assembly integral membrane protein vma21"; /id="PRO_0000389110" MERKSQVSDTNNNSIPTNVLLKFVGFSVALFTLPLITYFWTLKTLFKGYQTLYAGLSAAVMVNIILALYIVAAFREDSGTPKKDIKRE C6Y4D2 RM49_SCHPO SPCC1442.19; CHAIN 1..135; /note="Large ribosomal subunit protein mL61"; /id="PRO_0000389113" MSSIGGKLQKSLHKIRAGALGIPLPKHIQEVSIQYSLDSRLGHMGAKKFVKECLPSLYYNNYGLKFNVNHRLPNDQTPTFSIISNNKVIYSYDMRSKQLETISSDIQKALKELHHESSPENIKEAHKQDYSPPSN G2TRJ4 TAM1_SCHPO SPAC222.19; STRAND 10..14; /evidence="ECO:0007829|PDB:8FW5"; STRAND 17..19; /evidence="ECO:0007829|PDB:8FW5"; STRAND 61..67; /evidence="ECO:0007829|PDB:8FW5"; STRAND 75..77; /evidence="ECO:0007829|PDB:8FW5"; STRAND 92..94; /evidence="ECO:0007829|PDB:8FW5" HELIX 2..9; /evidence="ECO:0007829|PDB:8FW5"; HELIX 39..53; /evidence="ECO:0007829|PDB:8FW5"; HELIX 54..56; /evidence="ECO:0007829|PDB:8FW5"; HELIX 97..100; /evidence="ECO:0007829|PDB:8FW5"; HELIX 104..116; /evidence="ECO:0007829|PDB:8FW5" TURN 70..72; /evidence="ECO:0007829|PDB:8FW5"; TURN 101..103; /evidence="ECO:0007829|PDB:8FW5" CHAIN 1..117; /note="Uncharacterized protein tam1"; /id="PRO_0000416513" MSVSQQLSELASKEKTVLYVADQNLEEVLCFPESTDRTTLVQLTDACLHANELAKHLEFGKPLSITNQYSRGSCVLQIAKEKKDGSGMVVSTTIAAHNALRGALKCSNALDQVISQL G2TRJ8 CMC4_SCHPO SPAC4F10.22; CHAIN 1..70; /note="Cx9C motif-containing protein 4, mitochondrial"; /id="PRO_0000416511" DISULFID 4..35; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 14..25; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MVDCQKEACNLQSCIQRNQYNQGNCEKFVNDLLLCCKRWYDKNSLTGNEAPHTCPELKPLLRQLSSRNLT G2TRJ9 COA3_SCHPO SPAC1B3.21; CHAIN 1..69; /note="Cytochrome c oxidase assembly factor 3, mitochondrial"; /id="PRO_0000416512" MNQGNQAFENARKPFRRANLITALGLGAFAFATFAYSVYRVHEDTFEDVVMTPELEKKIAEDRDLSKKN G2TRK9 NEW13_SCHPO PTM: Myristoylated. {ECO:0000250|UniProtKB:P53139}.; PTM: The N-myristoylated protein is further palmitoylated. {ECO:0000250|UniProtKB:P53139}. SPAC4D7.14; CHAIN 2..121; /note="Uncharacterized protein new13"; /id="PRO_0000416507" LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000250"; LIPID 8; /note="S-palmitoyl cysteine"; /evidence="ECO:0000250" MGQVLSICSSKSKEKKVVNEKPTVKPKPAVNVQKPAKAITKASSPPRTGRKLAETGNTSNKEHLSPTEAARVAAEKRNIEKKKGNGKLGRQLEKERAKPMKEHLQDISTQRQQEREQIKWD G2TRL1 YLY4_SCHPO SPAC186.04c; CHAIN 1..175; /note="Uncharacterized protein C186.04c"; /id="PRO_0000416653" MNTSSRIQLPSSNDAHVYDGRSNEPKASKRSYVNLTRQMRPKDALKMNISSPNLKDLSKFADPDAQQWLEGYLAGKLEDNSKTPRSNFVDPLYEELNARRKPNKPVWSLSGPLPHVLGNSVVEKLEARSRASSVSNSRLNSRTNSSVSLKGMDGSSSWKNKIKNAVSNVTDQSKR G2TRL3 RSA3_SCHPO SPAC6B12.19; CHAIN 1..80; /note="Ribosome assembly protein 3"; /id="PRO_0000416490" MATNDQKIDNKSTVSNMLENPMFQTFSKKETEKPSLSEYMEQLTSEFGEELDNLRQKEIFDHNKLQLLIESLRAGHKIYE G2TRL7 SPD2_SCHPO SPAC3F10.19; CHAIN 1..102; /note="S-phase delaying protein 2"; /id="PRO_0000416677" MSETFKLPDHDELPQLVQTTLFDVGARVRKAVQTGYKFDQQLFPSYHKDQTDRNELPQQKHDPNLRLDDLKQELAADSIFWDTASTQEIADSFAKPDFLKSH G2TRM0 FMC1_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1486.11; CHAIN ?..104; /note="ATP synthase assembly factor fmc1, mitochondrial"; /id="PRO_0000416488" MSTPTTVYRSLLRQLREMNVIYKTSTLKQKKGFTKTQKDFLVYTKACLRNNKVEQLSKFQEVVAFLKSGNQHELLFNRHHPLANVNELEKVKLAARRVGLESPE G2TRM8 COA2_SCHPO SPAC15A10.17; CHAIN 1..86; /note="Cytochrome c oxidase assembly factor 2"; /id="PRO_0000416489" MFRTLKASQKRSLVNLMFGTTALFATATVIFPSLLPCPAMKNPYLDTQSDPGYEELPENSRVIVIDQQSPKSSLVASKQNNPPSKS G2TRN2 NEW9_SCHPO SPAC926.10; CHAIN 1..57; /note="Uncharacterized protein new9"; /id="PRO_0000416505" MLRWSSTYTFGLLWLIIGSEAFHLNALKQDHLERMKQYDAKIRLAKHEFDDTSNETK G2TRN7 YM06_SCHPO SPAC212.06c; CHAIN 1..147; /note="Truncated RecQ DNA helicase-like protein C212.06c"; /id="PRO_0000416670" MGVRLVVHYRLPASSMDYVQETGRAGRDGKYAIAALFYEKYDSTWSSYVEDSMKNFLNDNTMCVRSFLASEMDGECVCYSLLGEESTVSTMYGVKPTLPETPKPAIATHSRYNASFSSSPPPQPGSSSGMSAMNTNTTSTTPVSGKT G2TRN9 YAOB_SCHPO SPAC11D3.11c; CHAIN 1..357; /note="Uncharacterized transcriptional regulatory protein C11D3.11c"; /id="PRO_0000416587" MRSLSCIVCRQKKIKCDRKNPCTNCEQAGEKCMFKEYDSRKIRHPHSYVKALETRLAGLEAFWKRVKYAPVNEKLELLKTISFNDHLSPDISVSKTDTTFEFPVSLDIRGPNTIAFYGPTNVYGPPLTPSSPETPSFPPQNPSFSPLITDCLKLFFKWQYPQFLFINREAFLVDYYYRYHEGRYCSEHLLYAMCAIGSRMSVDPNIAALAKNFYQIAWNKIIEYGLGKSHITSIQCLLCLGYFNIGMGNTSLGWMLSGMAFRMGQDLGFQLNPRNWSVNDHPVVSPADAAVRSRIYWGSYVTDIFISFVLGRPTTLKKSDTSIPDSESLPDFDGVNEYRVNNALLLKEYLCIQSSVY G2TRP2 RN35_SCHPO TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC8D2.23; CHAIN 19..86; /note="Large ribosomal subunit protein bL35m"; /id="PRO_0000416494" MLVVFQRVVRATVLVGRKDTIRTVKTHSGAKKRWILTEDGKSFKRKHAGAQHLNRDTSSSTRARQRQWEEANTIQKRVLKRLLPFK G2TRP3 KGD4_SCHPO TRANSIT 1..?; /note="Mitochondrion" SPBC21B10.14; CHAIN ?..89; /note="Alpha-ketoglutarate dehydrogenase subunit 4, mitochondrial"; /id="PRO_0000416666" MVRKILIDFTKHITKSSLERHPHPAASFPLPASFTTVDSGPAKHSTAPPATPETSILVEDRNELPLRFHRLPVSEAEMQAVESGGAYAF G2TRP6 COA6_SCHPO SPBC24C6.13; CHAIN 1..90; /note="Cytochrome c oxidase subunit 6B-like protein new16"; /id="PRO_0000416495" DISULFID 15..56; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 25..45; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MAGNGALRRSAREKCWEARDAYFGCLDRHSILDGLKDDTKAAQACSAEKTAFETDCVKSWVNYFLKFRVQQHQQQEAIKKLEAQGAKKLN G2TRP7 TOM5_SCHPO SPBC19G7.19; CHAIN 1..49; /note="Mitochondrial import receptor subunit tom5"; /id="PRO_0000416679" MFSGAGRPSKEQIKQYDNLAVGEMKKGASVAAVLLLTPFVISFFQKMRA G2TRP8 MZM1_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC30D10.21; CHAIN ?..100; /note="Mitochondrial zinc maintenance protein 1, mitochondrial"; /id="PRO_0000416496" MSAAKQCFRNLWRASNSVFEGDPMILAAARDKIRTGFHNHRCCSPEEAKKEIQNGNAVAEILRRNVVQAEKQSNDTYSLKIRKTTEINTNRQFTEKKFPR G2TRP9 COX20_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC25H2.18; CHAIN ?..120; /note="Cytochrome c oxidase assembly protein cox20, mitochondrial"; /id="PRO_0000416667" MSTPNEPEKPGIIDAFKSLKMSDFAHMVHHPCFKESLITSVVCGLGVGCIHLFLRAPISRAANWGFGTYFGMSIVSWEGCNYRKQLETNNFNIKITEAAEKTPKHRSSRSAQEIDEGFNE G2TRQ6 TAM11_SCHPO SPBC17D1.17; CHAIN 1..62; /note="Uncharacterized protein tam11"; /id="PRO_0000416520" MEREGKEDVRKADHKIVYGIERVRHGINNFFDDVGKAVKSESDTADSKRSAEAKADEAPAKM G2TRQ8 RM36_SCHPO TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1711.18; CHAIN 19..86; /note="Large ribosomal subunit protein bL31m"; /id="PRO_0000416518" MKCSLRLFEKAGRLSVRSQTVQTFQQRIVLANGASYLVNTTLPKPYILSIKDITNMPLNNPKVNALSSIRGQESRRSKFEERYEGL G2TRQ9 TAM10_SCHPO SPBC14C8.19; CHAIN 1..168; /note="Uncharacterized protein tam10"; /id="PRO_0000416519" MGSSKSSKKDKQIHPFGTDVSTFRKLSSKEKKKLDEKELKQYKKLKHKVKKLKKEERERSSIKNTKTLAEDPMVKNVAENDHDQMKNSLSRSQDKGNTDYWLAASLSGGNQRKSKFLKMLGIKNAASITESSPSAQSNKTNDKQREKELEQQYMHGVLHKGTKKGLGM G2TRR4 SPC1_SCHPO SPBC887.22; CHAIN 1..78; /note="Signal peptidase complex subunit 1"; /id="PRO_0000416499" MNYLEGTIDFAGQLRCQKYMNYGLCTSAVISYIYGYLVQDSYCVIKLFLILASLVALVCLPAWSMYNKNPLKFQKKKE G2TRT0 YHX4_SCHPO SPBC3E7.04c; CHAIN 1..530; /note="Synembryn-like protein C3E7.04c"; /id="PRO_0000416682" MELEAYIQSLGLGIESYSQSATQFHDEANQSFNIPISTIIKLKEACRELETSKVVAKSLNWSHLLRVISLLWEKDVSLELMKLLANCLRQVPSISVQIVHNESLKQLTTSVFEVRAPKVLSLISTFNDDLERRVVFMRFLFILLSTQTDDICLDMRQVRTQLIQMLKKMWTLNSSPSNNSQDNEMVLTEILRLLFPISKRSYLKEEDEQKILLLVIEIWASSLNNNPNSPLRWHATNALLSFNLQLLSLDQAIYVSEIACQTLQSILISREVEYLEKGLNLCFDIAAKYQNTLPPILAILLSLLSFFNIKQNLSMLLFPTNDDRKQSLQKGKSFRCLLLRLLTIPIVEPIGTYYASLLNELCDGDSQQIARIFGAGYAMGISQHSETMPFPSPLSKAASPVFQKNSRGQENTEENNLAIDPITGSMCTNRNKSQRLELSQEEKEREAERLFYLFQRLEKNSTIQVTNPIQQAVNSGFIDVVFCLIFQMSSESFIYHCYHSFVGPIHILLLMFSTFKFHEILHFIKISKAS G2TRT1 YI4C_SCHPO SPBC1348.12; CHAIN 1..383; /note="Probable transcriptional repressor C1348.12"; /id="PRO_0000416668" MHLSKASFLFDCSRFILNFHERCLKNGVRTKKACVICRSKKQKCDGQLPCLYCKKYEYQCAYEGQATSTCNSEASLFNDANFKIGSDYRSKRIKVVSDTNNNKEDGDGKLSFTQCNPRMDIHHEAENFTAMVPYYEPKKFRFFYENSAIVFPRIYVFIYFEEVHPIFSMFDQKAMEKKIQFLWDNKSTDSCSEYVVISVKGKLVEHITQVLESSLSTTILSSIQLTVCWVLRTIYLHATTRPHLSWIASSVSMHYAEIVGLHQEITAEYGTRGIELTNITTQMVEEDGPAYQLVLLFKIIMEYQIISEDSRFVYLQAFQRLDQLCDIHSPALVLLKATVCFHLYRNLFLARIKPFCVIVSILFSVIDRALESCKQLVSQRKAW G2TRT3 TAM14_SCHPO SPCC330.20; CHAIN 1..70; /note="Protein tam14"; /id="PRO_0000416523" MPTVQTPSQRRANTQFQKNITRRVKTNSKERYVAKHPPTKIPRNIAMFFILLMSGGIILGILRFLLTFFS G2TRT6 NDUA4_SCHPO SPCC417.16; CHAIN 1..52; /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4 homolog"; /id="PRO_0000416672" MPFRAALRKVPVELYPLGAAVATAVGFATYSMGKKLLADPNVHIDPTVRRTI G2TRU0 OST5_SCHPO SPCC18.19c; CHAIN 1..94; /note="Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost5"; /id="PRO_0000416669" MSLNELIVAALKLFFYNKEQKSDCIFFCQVQIVIQISSSMFSLVIRRIHIRKLWYITVFTINASMFSGFFNNPSLLTPNENLLFQVGLHYSFAV G2TRU5 COXM2_SCHPO SPCC4B3.20; CHAIN 1..89; /note="COX assembly mitochondrial protein 2"; /id="PRO_0000416498" DISULFID 24..56; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 34..46; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MNKSPIEEEFDLRKQHQKLLKKNCQKEIEDFVKCATGRTFSVTWKCRSENKTMKDCLTKAADEISEWQIRSEYNKAKQESFIGKQDEKK O13598 YNI8_SCHPO SPBC11B10.08; CHAIN 1..204; /note="WW domain-containing protein C11B10.08"; /id="PRO_0000358322" MAYQTREGLPNGWVAQWDERYKCYFYVNESDPKAKPQWECPVRGLTIPPPPSVDHSAPPSGPPPSYSNSAAPATPAASASSAAPAPAPAASQNRAYGAAPQPYPPQGGYPQQPYYYPNQPNYYPAQPAYAQPVYAQPATSARRGRSGVLSNPMVTGLGGLLVGGLAMHEMDEAFDRPEEVVYVDDNNYNNFDDYGGNDFGNDFF O13602 RT28_SCHPO TRANSIT 1..50; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC11B10.04c; CHAIN 51..288; /note="Small ribosomal subunit protein uS15m"; /id="PRO_0000030612" MRLFEGAFQPWKLASTNLMQQCLLLNKKSQFHTTCILQGLKKQKANQRRKQNLKRREELRKQNLDTLADPIIGHSSEWIARLLKPYEILVERKKPNFPIRSIKFPASMETINLIVEKFEKIRASATEETKDFIKLNEVNEFPSSDTSLESNQDGFERLHPLAERLERMSQLSDLRKESIHRIFNIENSNSKTLRLNNKQLAVESFARNERDTGSPEVQAAVYTSRILALSDHCKNHKKDQTGKRMLRYYVHQRQRMLKYLRKVNFDRYVHCIKNLGLTDELVLREVTQ O13621 YNG5_SCHPO SPBC691.05c; CHAIN 1..668; /note="Uncharacterized protein C691.05c"; /id="PRO_0000116853" MNEKLQSYEKQLTSDIVNNCDLIIEVNASSKTCQETLSSLLRELQLSHFSTAVRPGSDTSIFVFVKVQNDYLIELAHNDRTSSFLCGALDDLNHVNVNSVTDIDSSERIRLVYDKITGSKTEDSLGICPGENPYADIISIFPLHQPKFDIKWSKYWYQLLLGNKKQLDSINAEYGSQVALYFAFADFFKTGVFVLSFWGILGYYFLRPYSYIFAIGVALWGAFFIQFWRVQEHKLTNHWSTVNCQSLAKSMTEFKPQSYRVDSLLGTARPYYPQWEIIVRSTIANVPLFLISGCILLFLIAIAFIVDVTLSEVYSGPLKSIVSLLPAVVFQVLTLPFTFIYSIVAERLTKLENRRTKTDFQASLSGKMFLQNFMLSYTALFLISYIYGPFAEYFVPHYIQNRMSQSFFSVGYIAKSTFKLNPLRLRNQYIYFLTNAQVINYITILAVPQLISYVKKHYMSKPTRELHIQDIPSETVTLKRARSEAEKIEYDCYNDYKDFVLMFGFLVMFSPIYPLAPIFSLVNCVLYIRSSVYRFTKMVKKPVPCRVDSIAPWDQRLSLLSWLGCITMPSICYFYSSTTKPSDKSMVIAAVIGLLSEHLWFLLRMFISSVFPVDKTFFAPAKERQHLLAERSFSIPPVADVPTSTTTAFEEADETLSIYRTAENKKTK O13640 YGWH_SCHPO SIGNAL 1..32; /evidence="ECO:0000255" SPBC8D2.17; CHAIN 33..328; /note="Uncharacterized alpha-1,2-galactosyltransferase C8D2.17"; /id="PRO_0000339339" MFNFRLFSRRGKSLGLLAIVLLLFGFYSLKSSMPVYSNSIGSPSAHSSSYKGVSKAKTSPQDPDSVVMLIVSFDDHYDSSRSDSSSVFLDKVLSDRTEYALRHGYTLVHKKARDIQARYGVYGTWSIIPALRETLAEYPDAGWIWLLDAKAVIMNPSESLKDRVLKPEKLSQHLLLNSPIDPLKNYIRTRRKMDPSDVFVITTSDYNGISTRSLLIKNNNFAPFLLDAWNEPLLKSAGFDQAERSALSHLLEAHNTILDHVALVSPKVLNSYTNSAVDLNYEEGDFLVILQDCENAAACERIFDNYYQQRKLPAIKKQLSEETVDEQS O13641 YGWG_SCHPO SPBC8D2.16c; CHAIN 1..315; /note="Putative methyltransferase SPBC8D2.16c"; /id="PRO_0000317094" MEKESEIQSLPPTRRYTISLALPISSLNVAYNLQLKTSFVWKISRIVSLYGIDEIILLEDPEYVQNTQVHTLSSDAYLKDPTKFLTDLLCYFETPFFMRKELFPLNPHLKYTSCFPLLPLRNDKASTVNIEFPYREGIVTHPSPQAKNKYIINAGLSHNVIVSSPSVLAPRTRVTVRLKAQSPNEEGQLQGDIVSFSAPREKGGHYWGYKVRSCLSSQLCKSSPYKGGYDFVVQINSQTSAITSKELEASLPSSFRHAVLVLQDNVVQKELVDSTAKSISFNPFPVSFLNDPIPEEILLAAMTRLSDMLLMHGRR O13650 SFC9_SCHPO SPBC8D2.07c; CHAIN 1..673; /note="Putative transcription factor tau subunit sfc9"; /id="PRO_0000361655" MGKDVALDFLPSSLYSCTCSCDGKLAFCDSEKVQILVPSTEANTPKFMKALAYLDDVEDELPNCQMLAPNELRLGDLTPSVISRYVVWSPTGLADNYDPLLTVLTNRHRVYFFSSSSRVLHQKWTCVAQMSTHLPSDPLELCRIHSVAWSPLVSLPSSSPWGVCLFALGAESGHVHLSIMSHSSTPFFKSFDLNCSWVVQLSFSSWNVVGDSATCLLSCSSRNGEIRILKIAISSHSDTFDTAMQELPFSLDYRPFSPLLAWSSPLANVEYLALVYPGHLFAFRYDKSLGKFCSFLNHNLLSLCSPSGVLFGHNDIDTIYVYILTHSGTLETFSLLDNSISMLDSPERHVLEKFLNNHLQNYGSVSDDSIKTLKIHGFCPSPYLSSAALHFSISYPASFTYVVTAAERSYFNFIPSLFSKSVFSHMITSSLNNLCVAPSAGCLLEISLMNDTLKEKTDIFTMLTNSLSSFLVTDYDFFLELKHLIDISSLSNLYLDSSLNAMRLLYGWSVYKQKALDATLLNSLRYRLTLYIMLYTLSQISLDPSYLTSDCKAVLRNFVSFTYKELAEVPIAMEVANEIAKSLEVSSDFSETCPACEATVQFNNTSLATCDNGHVWRRCSVTMLLLSQKAAKYCAVCNSIVAIFNPSQTKCLLADLQNELSICFYCGGHFLVS O13660 YBC9_SCHPO SPBC27B12.09c; CHAIN 1..277; /note="Uncharacterized mitochondrial carrier C27B12.09c"; /id="PRO_0000310790" MDQAIAGLAAGTASTLIMHPLDLAKIQMQASMNQDSKSLFQVFKSNIGSNGSIRSLYHGLSINVLGSAASWGAYFCIYDFSKRVVMSMTPFNNGEISVLQTLCSSGFAGCIVAALTNPIWVVKSRILSKRVNYTNPFFGFYDLIKNEGLRGCYAGFAPSLLGVSQGALQFMAYEKLKLWKQRRPTSLDYIFMSAASKVFAAVNMYPLLVIRTRLQVMRSPHRSIMNLVLQTWRLQGILGFYKGFLPHLLRVVPQTCITFLVYEQVGMHFKTQSSKSQ O13674 MUG24_SCHPO SPCC74.09; CHAIN 1..654; /note="Meiotically up-regulated gene 24 protein"; /id="PRO_0000082024" MAIMHKIGCAGSEVETDRVLEKDQANNGHFVDSDCCFQETGSTGTANSICTLNDSEDDNSSLNSVDNNECTNLDCGGKKHKNLSPNPSFHVNINAAEFIPKSHNGYAPKSMNPPPEQLDSPCYPHFDQDSSSVIYPSPPSTYYPNMYVSANTFIPMPYAHYTDNMYHAKPVNRPNFLPREGTPPPFAQQPAEQFSPFNSEYESLLDFRALILGNLPVDYKISELLSLIHSGPLEKIQSNPGKRRIIITFLDSADAFFFYERYHPRGFIFHGRPLKLTFARPSPLPESIQNFCSNTAASRNVFIGNLPSSYHEKEIEEAFGKFGKIEHIKILSKKNIAFVHFLNIRDAIKVVRTLSCDPDYHSWRIFFGSDRCANHPPSFDERSCFTSKQNPDTTSDRCRQQESKDNGNRTVFLGNLHTKTKGHEICDLIRHGGLQDFHYIPEKHICFVTFITYSAANAFHDYLAEEEVLLHGRRIKVGWGKESGPLPRVLEDSILMGASRNVYFSHISDSLTTEELELILRQYGEIESIKYLKNRSSGFVAYTNISNAMKAVNGLPIHPLFKKSKIRYAPDRCEQELQKSKSNSPIQQNVPLQQFITPPFSYPVAYCPAIPPGSDPILNFGIQYQPFIPFTAVPSFPFNCNVPNYPQTSDHEND O13679 YJ15_SCHPO MOD_RES 260; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC737.05; CHAIN 1..264; /note="Uncharacterized protein C737.05"; /id="PRO_0000116806" MQNELNPILLSQNSIRFATRVAIFFIIRDELVEAVTWRHPVKSMCLGLTITLLYLHPVSFSAILLLVFLTMMPISMTHDVTTNLKDLQNFMASYSSSYDQLLYFRQNYYHHITPSAISSGLLVSLVLIFLLAYLRISIDRYLPIAIWIGLISLHPKLRSYLIQFYSAKRDHVPYLQIRNELAQVWRHVDISGSQTTTRYTSFPKFNPENSVTSLDLVEPPENYSWAPQSDWTFVPPNEFRRFILWSPQPPKMNRKSSHGSNLPL O13687 VATE_SCHPO SPAC11E3.07; CHAIN 1..227; /note="V-type proton ATPase subunit E"; /id="PRO_0000117309" MSLSDEQVQAEMHKMVSFIKQEALEKAKEIHTLSEEEFQVEKAKIVREQCDAIDQTYDMKLKRASMAQKIAKSNVLNKSRLEILNSKQKVIDDIFSRVEKKLDGIEQKKDAYTKFMADLIVQAMELLGEPVGIVYSRQRDAEIVKAAIPKATEVLKSKNGSIDYELDAETDDFLNDSVLGGVVLVGLGGKIRVDNTLRARLEIVKEEALPEIRRLLFGENPNRKFDN O13691 NDUV2_SCHPO BINDING 88; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255"; BINDING 93; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255"; BINDING 125; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255"; BINDING 129; /ligand="[2Fe-2S] cluster"; /ligand_id="ChEBI:CHEBI:190135"; /evidence="ECO:0000255" COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255}; SPAC11E3.12; CHAIN 1..162; /note="NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial"; /id="PRO_0000020009" MKPIRFFKPENLQLAKAILARYPLRFQSAALVPLLDLAQRQHGTWIPPTAMYEIASLAGVSIDYVHSLILAYPNDFFWRPKKPRVRICNSWMCQQAAEEQGNSNWDSQCRSVATKYGFDVENTGCLGNCFQGPAMWINDKIYGVNTKEKLVDIMEALTQKKN O13693 YDYE_SCHPO SPAC11E3.14; CHAIN 1..588; /note="Uncharacterized protein C11E3.14"; /id="PRO_0000116679" MFNIKNHLRLPIIGKREPEEQPDPIDHDLHVQRLRELLYGLDLMLDDDAQGVKSAFSDDTVESAVGRSGSAFYNAILGLEPKAIEEATEALYHAEQVTEERKKHFEHHDRPIGSYPAGMELQLCLSDIYLMQSALGFVSDSIVDSMKAAYRIRKTFLSFSKMMEHVRDVQHKKETGEIKSLSPNATFIDEFIESGVITGYGVLTFLVSMFPPSLSRILSLFSFHGVRKESLELLWRASKYPNIQGAIALLCLYAFNAMIQSLGSIPPSNYDQELEHCLQAVKDIRKRYSKGALWAVMEAKIYFLTGESQMALEMEELSIDSSMEQIIAMKGFDTAMLYVGMRKFKQAADAIIELEDLNSWSHAFYRYFAGCCLLQHGKEILGSGGSEEEAKASIDHGIEYLKNAPTLVQKKKKRRTLPVEAYLIRKVQKWEDRAEKLNISIADAMDVPPYAELIYIFVICSLKDPKEAEALRADLETCKCSEEDEAGLKEFLLGVIDRHLKEYDSCRVRMEHVLQLDQGYLSRDNRELWILPFAYYELAALYWDMHGMAAEKEVNHYLKKAQEFNDYDLQNRLSMLAQAATQTLQSEK O13699 MU132_SCHPO SPAC11G7.06c; CHAIN 1..430; /note="Meiotically up-regulated gene 132 protein"; /id="PRO_0000118858" MLSFGGSLLSHSDIASRNKFSIDYSQFKAFFPGNWKFSNSKDKKPVRSPTLDEPVGDVDIDIFDVSKFYPLKRLSSIPEKIRANYHEELQTTSYDLVRNPFTHGLFCVVFYHQNKSYLKMGVTDNFNAFEEDSRVYQYGVNHKLSCKNLLLAINYSPKTYTKIFDFLRNGRAPLQVLVHHCMLYNFYPEDFQDALWCAVQAHVMNQVRLGRATLLHARACYQKIGDIRMYLIDPHDLYFSPNSLKWLIICSKQFQALVHLEVKMDTLKIFRRRSKYFNLARSCVSGFELSWLIMMTSIGSNASAVPVHAYLASKRILYPSIIPEEIFFMRKFDSSLFKDIKNIHELLGFLGRLFMDLQDCEKFHHDYTEYHCYRIGKPLYQNYEEEALRKKSQGVKDADFIKPLVTNTRTAEKYKAFFEYKRNIVLKKQS O13704 YEU5_SCHPO TRANSIT 1..24; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC13F5.05; CHAIN 25..363; /note="Thioredoxin domain-containing protein C13F5.05, mitochondrial"; /id="PRO_0000303924" MLFRIPTLFTLFLACFSLVSGVFGYSPMFGSNTIELNSKNFRKFVKAKGPSLVVFYAPWCGYCKKLVPTYQKLASNLHSLLPVTAVDCDADQNRAVCSQYQVQGFPTIKLVYPSSKGSSLSSTDYNGDRSYKSLQKFVSDSIPSKVKILTSEAKTQKFIQDAQNSSKVILISQKMKPTLLYKSLSNEFSSLPFSFMPAKANVNDLFNISAYVDTSDLPILFIKHPNNGTSFFSNSLNRDSIVEFLQSSIKDNNFSEYLATFCSKKSCIITIQDKDSDSGIDESIRKKYPKLHFVRLGRNTTVAERLEDTLDLGYSDTFLLSLKKSHYNAKPYGKPLRRWLEDIQVQQAGPSVSLPNDLLSKIK O13706 YEU7_SCHPO SPAC13F5.07c; CHAIN 1..165; /note="PARP-type zinc finger-containing protein C13F5.07c"; /id="PRO_0000304025" MEQGGSGYRIEIAPNNRAKCKGSLCGRSKILAGTVRFGTFVDSGRFQSWAWKHWGCVTPRMLKNIKNRLGEDDIVNSLDGITALSQEWIDKVVDAINEGHVSESDERESRKLGEKMNVNSQKLKTSSPPKVVRKNKRHHTTVKSVLSDSDLDAEFTDGSEAYEDD O13714 YDZ7_SCHPO MOD_RES 28; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC14C4.07; CHAIN 1..644; /note="Uncharacterized membrane protein C14C4.07"; /id="PRO_0000116683" MSSHDDDHTPLLISDPSVNKPFRSRTPSPEREYCSDCPLQAKGSACNGNSHSLKHETNGASSSNNNVAKSSSHDSFKAKPKNYDSTSNSNEPISFNEPDSSNSHHNNESICNNDNCCREIARRRSLSPLLILPLNFINAFSWGMIEIPLLFLLRQELCAIHYNLDPTQLSPDDPICRLAEITTGVSKVRAAFGSLAAFLGLFSTAYYGTMGDIYGRRLVLFITVSFLLLGDLWLLYQSYAPKHPYFVLFAAALKGLGGYISTVVASQNSFVADCSKTEFRAWYLGLNFAAYHLGTALGPSLSGFIVQYTPHMYYVFYITSTFWIIYLLYVWLILPESLDVSESKEQQNKISGFSSIWRSCLEPLIILWPRSLCTEESCEFHQYDINADTHAGRRHWDVLLAAILISLTLLGAGSMGLLPLYTDYKFGWGPMKASLILSTDSFASSITLVALFPLLSKVIEKIIEKLYSSEGLFEDPSRADNTSSLQGIRNVFSYLVRPGYSRSSILRGRTADEKYTIVKRDVWNAQLGYAIALSAAVLLAVAKSDVALFTAVIIQAISNMVVPCVQSIALNGVQSEYNGRVLAAFAVFEAVALIIRGPIYAFVYTESMKVSYPNMIFFLSAVIYGCCFIIIFFMRLYRPLNRKR O13715 MUG5_SCHPO SPAC14C4.08; CHAIN 1..185; /note="Meiotically up-regulated gene 5 protein"; /id="PRO_0000116684" MCYLSRMSSQQMQLTISGFENRIKILEDLMNEFDSNLYIRLKRECDFKLPKEYDVSIHALTILMKRHLSNMEPIDCYQDLDTGTLQTMLIFCCTLRMIEHYEKSLSNINFFSLSNDLKRLEEYNTSCSVLLSLYQRQLKKISTTIESYYLADTLRHNQNILNLCERIYNIQKLLNKREKASVLRH O13717 YDZA_SCHPO SPAC14C4.10c; CHAIN 1..329; /note="Uncharacterized protein C14C4.10c"; /id="PRO_0000116685" MELELDLLTGLQLLSEYCPRVTPNAPPRRASVAVIIAFKESQDFSNPKWPQCIPITSVPYVLLIQRSFRDTDRWSGHMALPGGTRSLTDKSDIQTAHRETLEEVGIDLRKEHAHFVGALDERVITSNWGQFPLLLLSSFVFILPYMPSLRLQESEVFSAQWYPLADLLLPECQTRIQIDSSRALKKTYPRFIKTLFHLAVGNLMYSAIRLEFDPSSATYSLPPYQRPFLRGITHSIFVDLFIFLSPSSARHCLCWSLPYFQHYDLRFIASFFTQFYRLRLHQVYPRGNWVFTCLNGYYPYLKLTLLVGFLFRLFLVYLLFLIISAYYKS O13724 ZPR1_SCHPO SPAC15A10.04c; CHAIN 1..459; /note="Zinc finger chaperone zpr1"; /id="PRO_0000119039" MAEEKKEELFTSIGNAAQNVSTAEDREGNGVQEVESLCMECGKNGTTKLLLTVIPYFREVVLMSFECPHCGFKNAQVQHAETIQPEGSKITFHVEDKEDLNRTVVKSQEAIVSIPEIQLEIPGRLGQLTTIEGILSNVVDDLSKEQESRKESAPQLYDQINAFIEKVNSLRSGSVPFTITVDDITGNSWIEMKPGRDGDRWSQVSYKRTLEQNTKLGLVDTDQPEDVKTQTNNASNTLKHDATAVEVDPNEVHTFHATCPSCSHQCDTHMKLLDIPHFKEVIIMSTVCDRCGYRSNEVKTGGEIPPKGRKITLKVMDAEDLSRDILKSETASLKIPELGLDLFPGTLGGRFTTIEGLLAQVYDELYGRVFSQETDSMTPEQVANWQQFLCNLTAAREGATQFTLILDDPLSQSYLQNYYAPDPDPNMTIEEYERSFQVNEELGLNDMKTENYEKDGGKK O13732 YDOC_SCHPO SPAC15A10.12c; CHAIN 1..148; /note="Uncharacterized protein C15A10.12c"; /id="PRO_0000116646" MVKPRLVFLSIAGPKDEQLYLEIIDPKEKHLLARYQYLGELSLDVINDLVNDGERTSNDCFLGLLGVEEDISTYAFYSNTKVKFILAVKAPDYVVKETEIRQLLRRIYTIHTHAVCNPFSMDLTPETLKTSIYFKESLHQLISDWNIH O13733 PPK3_SCHPO SPAC15A10.13; CHAIN 1..637; /note="Protein kinase domain-containing protein ppk3"; /id="PRO_0000116647" MDFIKSAASFIAKAGSQFPYDLNEKIPLSSNSVWTLQTGSIRESAQPCSVFSISLSTHPEWAELADRACETMKTLRHPCIIKYLSTYKSSTHLYIATETVRPVTTELNELSAEIKTYGLWRVSAALSFLNDKNIVHGNLQMSSVYLNSADEWIIGDFFLAGDSPQFIKDNHDKILNWSRLVPFEIQSSTLNSASFIYLDSYELGKFISHLYNGTPGDLSQRGNIPANIFVSAKKLLNVEGKQKLLASEFLKLGERPGGFFRTHLITLYELLSEVRINEEEDRVKLKQLLSSKLEVIPKNYIQKVVLNILFLLLSIDTHSDVVELLFKCAQIVKGRPDIEKDFGVPLLSLLKQQSVPIRGLLLSGIINNPDVLPKNIYEDTSFSVFANLVRSNSPTLKEHAIVVFSIIAPKLSKKTLNNELLRSLAVVQNDQHPTLRTNSTICLGKIAEYLDASVRKPVLAAALSRSLKDPFVPAREAALKVLLSVQNYFDTKDVAIKLFPSVVPLLIDENEGIRRTAEDVTDQFLSRIKNFNLGEKENVSAPAKFNGSFWSKFIHSSSASPSPSIDMKKESLELKNDTTEIKEKKNSKSRVVGNTENSKDEFNNPLFETEEQIDESWMENWNDEEETENNVEESWGL O13743 YDR8_SCHPO MOD_RES 200; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC16E8.08; CHAIN 1..269; /note="Uncharacterized protein C16E8.08"; /id="PRO_0000116657" MAFSPANSFLINKSICESKEVEPLEANLFGKLHNKLLICKAKKENLEKKLAYQMMYSKLLKSLPKLSSLEENKLTKLKAPIEDMENTKKELEEIRKQSTETELRYLKSLSNTLSFGTLSLSNEINKVGPSASFMLKEVHDSVQVLEQRLEKMGLIEKPSESSESSIYSILASLKHTNDSLQKKELSPHEIAESPSSHSTSPMGRNVDTETLSFLLIDWQRLCAEQNTFLRDITNNMSSSVPQDVLSQLRQFFFRSELLSDKLSNLCSES O13746 YDRI_SCHPO SPAC16E8.18; CHAIN 1..107; /note="Uncharacterized protein C16E8.18"; /id="PRO_0000304006" MEVTSFILNATFKEFACFGNNYLIILPGIMLERNVFRHLNYSTNSICSHYQFFGGHYESFELLVVIVYYFSHVGSFSLAEIYRITWDKRIVLYGTTTTLVYCSEGSD O13747 EPT1_SCHPO BINDING 262; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 265; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 274; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 277; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 282; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 289; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 293; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"; BINDING 299; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" SPAC16E8.13; CHAIN 1..547; /note="RING finger protein ETP1 homolog"; /id="PRO_0000056332" MYYYLEIECESPVKDIFTCNKRRASKVVGNSFGGDHFNFRLGEIKLLSMDFPSSKVPEVEETSLGHGVVHLYRVFPSESHEFDAPGLILAILAIPLYMSPSDVLGFLGEKHCKSIQHIRLLKTKDPNRIMALLKFKDQASVIRFYTEFNGKAFSQIDPETCHVLHIDKVNIKYPMESSDSSSTEQQLVGPSSKPFASTTPALIELPTCVVCLERMDSSITGLITIVCQHTFHCPCLQKWGNSSCPVCRYTQKVQSSEFQSKCTVCCYDKDLWICLICGNIGCGRYHDAHAKQHYVDTAHCYAMELETQRVWDYAGDNYVHRLLQSETDGKLVELSTDGKSSGWTGSSATESKLRDKMGLEYTQILVSQLESQRLYYESHLSNMSQKLSRVNEELVLKTKIATASSNANTDLRSRVDISESKLKKRDDKLKRVSSQLEHLKHNYEEEKSMNENLLVRIQTLEKQNTTKSDQIVSMQFQINDLNEQLRDLMFTISASQEIQKMGQSEELQNGTIVLPNNSTVRSNSVKSKKKKKKKPVVPSSSGSLGTD O13752 YF22_SCHPO SPAC17A2.02c; CHAIN 1..290; /note="Uncharacterized TLC domain-containing protein C17A2.02c"; /id="PRO_0000343434" MSSAVTPSDQGLLPRGPIALEEFVKPFCDRFGLTKLPRHMHVILLSALFYQIINILSPVISRHLSTHYAKLSKKTRLNWDAHVVSSVQSIVLICLGYTCLKEVNAFPDKLFGYSVVAGDIYALTAGYFVWDLYITVRYVHITGIGFVIHAIAALFVITFSYRPYLMYYGPTYLSWELSTPFLNIHYFLDKTNRTGSKFQMINGFILIVTFICVRIAWGWFSAYSTAIEILNHINVAPWALSLFYLAANMSLNCLNLFWVSKMIDAIRRRAHGEKKSTPLQVTSEYAKKNI O13757 YF27_SCHPO SPAC17A2.07c; CHAIN 1..177; /note="Meiotic chromosome segregation protein C17A2.07c"; /id="PRO_0000373866" MALKRSYYASKDDYSTKRILEIIERPLKKLTIEDTSEYDDSDIEMPTCKRVAYYKNEYTIVVEDLDAELEEDDSINKPTEEADEAPRTQLSVISPLEKKLKRDFLFLLLNSNRQPGKSSGKSSIPSPDDFKLSVKYSSSSEDLGAVTIESHLNVSSDASIKYKSSGTSQSDLLMEIG O13758 YF28_SCHPO SPAC17A2.08c; CHAIN 1..361; /note="Uncharacterized protein C17A2.08c"; /id="PRO_0000304056" MRRYLKKAKPKIVQTSDNEEEKHEENLNVSQSNKNANRRKTKAKEKNSGKFRVKYENEEGDDDGEDSQIPLIPKVKKQSSFHSVDDLISRRMDALSHESGYSNAYVDELKRKSRQTPSEFTKKEEDSSTKESELQTRSSPPLPVNTSLEWNMLNQGIPEEAMIKELKDREGRKRNIAMMTDNYISLETGDQLMLAQNHKEEKLLQTEDEIQDEGYSGFENYVEESEKLQEIYHHSSESLRTRSIQMAVDQKNMEMELDDEDIAEPIQSWEHTQIKKGAFGESPAFTNGLSVKLPNILTMDEQIQRLKEAIASEKLQQEERSQIIKSLMEEELEINEQEEKIKHSFIDLDKTLLNNLTKSKS O13760 YF2A_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPAC17A2.10c; CHAIN 17..230; /note="Uncharacterized membrane protein C17A2.10c"; /id="PRO_0000304010" MTCVNVCFFLFPPCHRNKITEADKSLVDLLIPSLCCSLAVFPSIPLINTHSNLCLFSNFSHSCFLFCTHPDTLPTSLSINPKKLSLSFSFPLSQKRPFPNFLHPFTGSELSLFRCLLLFFFFLLFFLSFSFSFSFLFFLSQIFIVYFSSFPILHFLFFFFLCVCVFLSFLFSLSHLLSLAILFLPLLLRVFSTLSRLPRLFCLCLQKKRRVLIPFAFTSFRKIASLPCVC O13771 YE99_SCHPO MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17A5.09c; CHAIN 1..310; /note="Uncharacterized protein C17A5.09c"; /id="PRO_0000116708" MKVKSILKHSRMSSPSLETDSMESGQQQNMVSSTPSIDMNESDCSGTGTPSEERIRRLRWDEENLSKAEQQKSAKMKITEPKTPFQRFLLPDDEVPEINLDETDSKDDFTAGTLGDTLGTLPSTRVSKDSKDDNVSFSSDKKQFYVKKEPFPVPCTEPTTSGDRYTVRMKAPTPKYSTDNHLPSKKELFPRETKPQVEVVHARINNPDDHLRTHPSVNNLGKDSDHADKMYNEGVILGEDEAMEEEALSEAEENIPKKKPDFNELRKKHYFAMAKPLKRDELESSGTESDLERDNSDSGSASDVNMNENE O13772 HUA1_SCHPO SPAC17A5.10; CHAIN 1..224; /note="Proline/serine-rich protein C17A5.10"; /id="PRO_0000116709" MTDDSVPPPSYEEVLRQEGVIDSPNSSNGQTSTSAGHPSSSSSTLPNYAASSLNSRPVSSSGSGNAYSQAPYPPARPTSQRPNSWQPGNASTMYASPPPSSNYNTAKPPYQTSQFYARPQSSYAPPPSGRPRISYPYPPGYMCYKCHNTGYKDSGRPCGRCARRFGRSYDVQFSRPPPGALVVYPGDPRIPGRVCGNCKGSGQLDFIFFTEICPVCNGVGKIPY O13781 YEO3_SCHPO BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 47; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 125; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 260; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 467; /ligand="substrate"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; SPAC17G6.03; CHAIN 1..635; /note="Uncharacterized protein C17G6.03"; /id="PRO_0000310953" MKPAHTFSLIFSLLFVINPCYSATLPLAIRRELTWGQVNILHTTDIHGWLAGHARDKRYSGDLGDFASFVQHMKHLAKQKDVDLLLVDTGDLHDGTGLSDLTDPPGSWTDSLLANMDYDILVAGNHELYLSTVANDTYHNFIPLWEGRYLAANIDIYDEHVSSFVPFGDRYAIFSTPHNVKILAFGFVNSFSGATDTVRVLPVSQFSLQPWWNDMVSNKDIDLILIPAHVPVHNASELDIVLSELRIHFPTTPIQVLGGHSHIRDYAIYDEKAVGIESGRYCETVGWVSINGIPSFKSLVKLSGISSLMGVESYLAERLRFIGESIRRSSQQIFSSLQSAKSASVSFSRSYIDWNPEGFMFHSKTKKSSFNTSLGEFISNGIYEARKALGLLTPIGCSPKKFAFSEVPFNDSNSIYHLFQSELFPKIVVNESRHHIPHYIIVNSGGIRGGLNSGAFGLDEVFQVCPFKSNIFYVLKDVPWSITKYLPQALQHSGYLIAEDTLQINTPQVSDAKFEDFYEHSIRKTYGYTTHDDLGDDGDDTAHLTTPHYEPLRFICSQVGFDDSFSGDDKQVVDVVAPSFVIPRLDDILNKIADKPLYSPDDWELYFTRPDGKHSMTDLLPLYADLYWDHDCLYK O13783 BRO1_SCHPO SPAC17G6.05c; CHAIN 1..775; /note="Vacuolar protein-sorting protein bro1"; /id="PRO_0000218869" MEKLATPFFYLNKKETKHSDWVEPFTTFVSRIYGNSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNGINISFEWSDILDPDADFVKQSSLAFEKASVLFNLVSLLSRMAANHASAYTVDDYKAAANCLQCASGIAKLLRESFIHAPGRDLDSNFLLGIYNLFLGQAQECVLGHMSFSASDSNMNYSLAAKIASSAATLYDSCVHAFESMEPACNPNFIRLASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDFIHKPSLSDYPQTISTFIKSSLSHLLKTAEKDNDFVFHDLVVKEVELPKISPLQALPPLPLEKLYGSQDGFETAKKIVGDDLFKAFVPSAVTTASSLYSEETAKVFRAEQAEVERQNTQMATVFASLDLSRLQEITHSDSKTNFIPKELIEARSQLISFNPTFKIHELFAKSTKLKQIIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQQYALVKDDVETLCNSSKISALLESSISSTDNSGQSLLDIPIEQEEQERDMKIQLDLLEELQSRVQKLVPERQTTLQALQQKCLQDDISESLMQNSKRKDSALDTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVTQKLKQNPEFLRKMEVYNNQFSKNKELCSNLLSSSLTAKAISEGVSKGLEYYKTVEQRLAEINKTLGEQLLLRRKQGATCLSKLSSSSSSHTSISSNMRNLHI O13785 USE1_SCHPO SPAC17G6.07c; CHAIN 1..222; /note="Protein transport protein use1"; /id="PRO_0000116727" MSKDLISRLERQFKLKRDEFQDPLELLKFEKNLDYARKLLWEEGKCQLDKVAEPQGLSKRIMDLQGRIYDLNVTMEKKLKIEEKKIKSKQEKEIAHALQSIQERELRERQQMSNVEASNAQLLTNQRSMQTEISESLLHLASVLKENALSFTNALVTDNQVVERTGSLLDKNAHSLRHANHGVQSYSKSKRLSFWLQLGMIIAVVVSFIVMIFILQFTKNQN O13791 SLT1_SCHPO MOD_RES 227; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 229; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 409; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 415; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 418; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17G6.13; CHAIN 1..433; /note="Protein slt1"; /id="PRO_0000071961" MATLFHLIDVHGNEYQNVQDHSLQMALEELNQQIEVIQRQEEQLALRKKAIEDARQEVLQQIQHRKFRQYLHEREQEARLQEYYLEQLQERRAFENVVRTIIRKRFEDEERERAHRREKAARKLLRRILVSDSPNMQLVVPNNFQQMFIHHPVVDTIYSPEESSESQAEVADQQTGPYSTSEYAGAQQSQPFRIFIQNDNAPEQQSGPDVAELNTLPNRSKTSSQASVSDEELSRTELAELNDYLLAAQRRSNKRGNARKHIDLTARESPSTSFAQMSKGALNPDPEVIEPEDEPTTFRNPLEALLSTGQYSVVSSDEDVESVRDPDDGTLPIHSTQTVEEPIDTKAGEKLTDSSKQPSPPVAEHFSNETFSASPKGAETDVKSEGSNNHEQGSFNEPKSNVDSNDSASPKRPSSQASLRHNVTVEEVPDEDA O13793 FSF1_SCHPO SPAC17G6.15c; CHAIN 1..322; /note="Sideroflexin fsf1"; /id="PRO_0000318075" MSSNKLPTSKYDLSTYWGRVRHAMDITDPRTLLSTSQDLNSAVKTLEDYGAGKIAQLDETVWHAKKIVDSTLHPDTKEPVFLPFRMSCFVLTNLVVTAGMLQPNLGTAGTVFWQWMNQSVNVAFNSANANKSTQLTLPQMTKSYIYAVSASCGVAIGLNKIVPRMNFLSSSSKAVLGRLTPFAAVASAGVLNVFLMRGEELRQGIDVFDKEGESLGKSKKAAFYAVGETALSRVINASPIMVIPPLVLMRLQKQNWLRTRPKLTIPVNLGLITLTSLIALPLAIGVFPAREKISPFKLEPQFHHLKDKSDQPIVEVEFNRGL O13798 CID16_SCHPO SPAC17H9.01; CHAIN 1..1202; /note="Caffeine-induced protein 16"; /id="PRO_0000089747" MLFAKLLLKPVQILFAYAKAKSKEISIKEANLLIFQDETDNLRKISTPNKLAVSLAGGLKALLSSNQLCHAFHYHNKKIRLVDTSLNNLPVPILLPKLINYLLARKSQKSAAEWEEIERALLSCCKRSKDPSILFPTDVPCSLDDDVSFLTFKGHKNHLENRSFFHDSESDNFKVVLSNCAINSKEDNNLVTEDRVNLGAKLLLVPVQNLIKLLKVSKISVDLAVIDHSFQDQKLTLEVGNGGLEVVKLFGGWIRILESECLGHVFSFKKTMKRKEVALVNRKADIDTTDLFIALRQLVDSKFKSYGIKAQKHAINRISKLGKMITSNHAEEKLTTIPITEAKKESVSNTALIARKNIIRERKYLSRMFDIFEHIDSYFNHEINMLLVDLLLEPLQVAFVYKNLARRWISLEEIENLWLKVFDSSHPLGKSITSTLQAIGTRKILTQLSINMIPRYNQDNCSAGDIYILCFSENCWLYSVLQKTIDHWVNENVELFYKKFEILKSLLIEDIANSTFSKEVSLNSSLRWYCVAILVTPLQLIINHLKDKTEMLSLDAVMTLILGKNTREVNSSIEELKITDCLSFLLEHNIFNTFLVYNEGIVKLNKDFDDFTPLNLLKCVNYSLMEFQKNSTFDMLEKLYEIGREIDMSKFSTLKYNLQLPNVDLLKESEAVSETKNTKNNTFILKSDLKEEERLTNFTIEEINKHKAIGVALRKLLEEADTSSNFSSSNNHVLDSSKHTVSSASTSSRKFIENYKSLESIGLTSFVKDNKLKASKELQKLIEENVFPKNLILFIFRKCVIGIKSFEKLQSYVFTYYCERYPKLILKRVLRFLEEIGFITSQYPRKLTDTGALFLKHPSEWGVLQHTFISSNFFENVPCYISLEQSLQNFQNDIRPDTVRTTAMKAIIKKLLKSLRKLEGPVKIACFGSYRTGLMTKNSDLDLVIYSSKEALLPYYDRVKSIIKNEFSNVMPIRGARIPIIKFTGQYNIHCDLSFDNLLPIHNSDLILNYSLIDERVKTLLMLVKYWASNRLIDKTHHAFPSSYTWCIMVIFYLQQIPEPILPNLQKLSTQYSKIVRDNDYGNVNCWFNRDTECYRGSMQKGRKNIALLLRGFFCYYGLTTQYSFDWEAYMIDISSSQLKRKSTEFKDCPFVVLDPFLKKKNLTKALTQKSVKVVRYELERACRILSDPKCNLDHLLDPLIQ O13803 YE06_SCHPO MOD_RES 236; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 238; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC17H9.06c; CHAIN 1..601; /note="Uncharacterized protein C17H9.06c"; /id="PRO_0000116689" MVSNQDNVQRNDVQKYPITRFVKRKSNVVLKKNKGAMKSNSNSRSRGNKKLKESQFSSRDNFRTTQTQASSSSEPSDNTNRLVPVVIIDNNTPKKEESNAEKLKLDKDSSSVNYENQISKPLITFSDIHETVNVPFLCLDKHDSKNEVAINSHEDSPVCLEDITGSLSSTYGNDSLGESNLEELPTSDKIKGENMGSRKKRKGFVIDSEDSDTGIPREENVTITRKTKLSSNILYSDSDTERQSDSGSKNVARQFSRIKRKRKVLSSSSEDDESSSPEDLLKPIIRSTEEMENLNELEQEVQDLDPIDEGFEEKVPRFRNPSKKAFYEKLHSLRNRSYSKLESLTSEKSDTLITKSELANESEEDDFIVDDEDTEVMMNARSLLPAEFSMTSHQGLKAHFRNFMMFIVQQAIDPIDASDISDHYLFSRRTIRKQLYSSVDSNIISSIWQSEFIKLIKTVPNMKSAKIDATYGCDACNIHTRMSTQIVYFKGMPYNEHNYKELDSFEPITKEAWMLGNSCFNRARIAHSIYHWEYKVSRHIQVELKFREASNTSEQGKNIVESIYEDLKDSNFFETTWVELCNLLKLASSSFESNFHSRSSM O13804 YE07_SCHPO SPAC17H9.07; CHAIN 1..120; /note="Uncharacterized protein C17H9.07"; /id="PRO_0000116690" MVYLQTVNEFFTQSKSLTEAYPKTTKLSIKYRTNEQSQNYLIAKAFESASGICLKYRTDKAAELGRLLLIANKLSYVSTGNEIPPEPEQEVVASPVTEQKKAEPSAPPKGSKKKKRGKKK O13805 YE08_SCHPO SPAC17H9.08; CHAIN 1..326; /note="Uncharacterized mitochondrial carrier C17H9.08"; /id="PRO_0000090703" MPNSTAQYPEKDSWEFLVKSGIAGGTAGCVAKSVVAPLDRVKILYQTNHASYRGYAYSRHGLYKAIKHIYHVYGLHGLYQGHTATLYRVFPYAGIKFVAYEQVRRVLIRDPEHETHARRFLSGSLAGTCSVFFTYPLELIRVRLAYITNTGKNPTLTQVTKDIFHERDFLCNKKYPGLSRLSKICNFYRGFSVTLTGIFPYAGMSFLAYDLATDFFHKQKIDEWVSTKKSDKKLKTWPELLCGAFAGVCGQTVSYPFEVCRRKMQIGGIRKNKSFLRLKQVVQTTYKEAGMRGFFVGLTIGYIKVIPMVSTSFFVYNHSKALLGID O13809 YE0C_SCHPO COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; SPAC17H9.12c; CHAIN 1..266; /note="Uncharacterized FAD-binding protein C17H9.12c"; /id="PRO_0000310846" MSSSTYRKLPKILAAGLAIGCAGGYYAYKNSNKPPGLNPEIYAPFTVNKITELTSDASLFSLVPQSPSEHLTTLEPIAKVTIRDPSMQVQRPYTPLYLDANELKFFIRKYEEGPVSSYIHSKKEGDTIELRGPFKTTKLDCTKYPRIVAIVAGTGIAPIYQLAQSVKSPVDIVYCSRPGQPPLLKEELEKECPNVRVKSVQNRLVNIHDILDWDNVTVPLKDTLCIVCGSQKFVSTIAGPKADYGARQGEVKGLLSNNPFGKVWKL O13815 MUG52_SCHPO SPAC17H9.18c; CHAIN 1..105; /note="Meiotically up-regulated gene 52 protein"; /id="PRO_0000116691" MHKISLQFFFVDNYFFFWKQSKYQSIYAIQIRCFFLTVNRTPIPKQTFSLIVFYILIMIIQHLKEIHYLISASAKLLLASNYLLELLISHNIQFSPIRSFFIIMV O13818 YEE2_SCHPO SPAC19A8.02; CHAIN 1..1213; /note="Uncharacterized PH domain-containing protein C19A8.02"; /id="PRO_0000310806" MAAPANASSKKDHVIPVLLNECSIDSPSFRASMYYLGNQIKAFNEWSHDFLCCCNKFIESIMAIEPIVASMSLNAMPSNVASGFFDPDYATTALLHGQDLFRSSYMVQLQQAKNLRKFIVAPLDLFRDSKVKPLLQLNDRFKAEQAKYDAEVLRYSSLGHSKDLSQMRDEAKSLYEARKSYFTVALQYVVRVTSFRSSIDFIVIESICKFSIETFRLTDRLHESNRHINDQLIRLLSYETKLKESYPSLKRIVSNVFDRIEKEILKRVQPPTNLDAYRFDPQQICQTNATKRQGWLLRNISSSKADNKAIWRKYWFFVDNGYVGYLINDANGGVFESEKIGVLLCKFSVLPSNHRKFCFQIKTKSVSYILQAETHMEMLEWGSVINNAREHCINSGISANRILSPTLPSFSAKATSIINPQVNGRSNSTGKIGKNYRPRRTYSGRLLCGPNNYEVSTIMRSPTISTVPPPKYLSNSINGAKFLNPLAPWTLVNAPLITNLTHETITSLLDQEAFFHGNSPCALLANFWGSVNYGHVLERQNVYIEDLSNPSYKRLAREIHIEKLPSELKLRNAEFRGIFGESEASTVLFVCRVCSKREDQIRMPGRMYCTMKGIYIYYNINGLVLIEHFPISSILNVKQFASTKCDYFYMNIQNIGTVRFRLYLDSSKALTDRLNVLLCNYIADKPNSSIQLLSCIKRLNDDVKRFERGGDDNALKSYGVQPSQEDLLIRRGRSSRALTNLINKNESNDSFMEDLRDFKIAMLPKETVQVVRSHHLDDIVFDRVYNVSTKALFHIVFGDRSTVLSGAYNLHGVDDVEFLPWGKDPKTNLSRRYINYKVYNYDQEGQCQSYHYEDCQIMDVRNDYHLYIMTWLHHSWTLPYRDYFKIVTKTSISHLRREKSRLLISVGLEWIVKPFAISKVIEAECRKLAIKYIKTEVNFLEKATRRARNQPLIAIINQYGRVGDYNESMVYRRKIPFNCELKNLSIIDIIRNNWWLFLQGLAIDLLKLPWAVFHIFLRYLFSHSFLVIIFACSVILNLSLMFCFGAKYWDERQNNKFVGQVFDEFKNIETSARYVYMKDVDDLLVGLPTYLHPNVTYPSECLQSFALKSSPQKSHWLRKRNYIAEKRKKILENLASLNYYEYIIHEDAVYQYIQQELLGCDKAREFDLYPPSMQRYCDSCTQDWRNRTLFFGKDTLATRLLTLETVENADYAA O13822 YEE6_SCHPO ACT_SITE 254; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 87; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 136; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 199; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 254; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 291; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 293; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPAC19A8.06; CHAIN 1..397; /note="Uncharacterized oxidoreductase C19A8.06"; /id="PRO_0000310782" MSVVCSCLLPTPSTDFVNQRNMPIPIIAHIAQFKYEHLITHWAQYTKAAIAVSTIAAFKFWTSGRTTTWERKMNGMVVMVTGGSSGIGQVVVEKLASLGAQVVILLRTEPDQFTVDYIMDLRKRTKNQLIYTEVCDLSSMLSVRKFATKWIDCTPIRRLDMIVLCSGVLLPPFMDRQTTEEGVELQWATNFLGPYQLLRILRPVIYGQPGHREVRIVAATCSSYILGNIDFNDLDLSNHPYPRKSPWKVVGNAKLALMTYLYDFQKKAEAHERPDKMPCNLHTIMANPGVVRTPGFRRVVSFGKVWGLFLYLLLWPFWWLLLKGTIHGAQSFFHAICSPEFASITQPVLVNECSIVEYSRKEITDPEFAEKLIKAADAQIDEVEKQYKKKKIKKSKK O13825 YOS1_SCHPO SPAC19A8.09; CHAIN 1..81; /note="Protein transport protein yos1"; /id="PRO_0000116716" MFGFGNILYVTLLLLNAVAILSEDRFLGRIGWSQSAALGFGDRQDTIKSRILHLIRAIRTVMTFPLIAINTIVIVYNLVLG O13827 YEEB_SCHPO MOD_RES 194; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC19A8.11c; CHAIN 1..246; /note="Uncharacterized protein C19A8.11c"; /id="PRO_0000116717" MRVILVIGRSNSGKLDFIKALTGSLPKGLDDEAFNNDHSGLIHKYNIRNKYFEASVGIWIEEYSNLAETLDAYSSEEAKEVIDSLGAIVYTFRSFDEAEWSLFKNFIDKLQLEIPVIGLHMSDEKLLEPPDVFTPEYISISEEGVNEFNEKVGLDRVREILDCCEWNLSQVDKSFSEEKDDAGDFYLPERFKGSPDMQSTDLDNLMKEMNQIRDADLEKNEKKAKALNLLEKLLGDEFEENDYESL O13844 YFG5_SCHPO SPAC19G12.05; CHAIN 1..291; /note="Uncharacterized mitochondrial carrier C19G12.05"; /id="PRO_0000311180" MSTVAKTNPKSSNKPGPVKSIIAGGVAGAIEISITYPAEFAKTRLQLYRNVEGTKAKLPPFGLEWYRGCSTVIVGNSLKAAVRFFAFDSIKKSLSDEHGHLTGPRTVLAGLGAGVAESVLVLTPFESIKTAIIDDRKRPNPRLKGFLQASRIIVHENGIRGLYRGLAATVARQAANSGVRFTAYNSIKQSLQSRLPPDEKLSTVTTFLVGSVAGIITVYCTQPIDTVKSRMQSLSASKEYKNSIHCAYKILTQDGLLRFWSGATPRLARLILSGGIVFTVYEKVMEILKPF O13854 ADG2_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPAC19G12.16c; CHAIN 20..670; /note="Serine/threonine-rich protein adg2"; /id="PRO_0000014200" CARBOHYD 77; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 159; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 204; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 224; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 274; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 297; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 327; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 351; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 370; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 381; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 405; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 424; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 435; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 459; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 478; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 489; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 513; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MRRLTISGLLISLAKLCAGMEINVPSSSDVWTSGHIEPLEWSVVSTDPLQANVWLINEVEYPPTSRYIMTINTFDENATFPALDLSPGYGYQISFTSIRDDSVIYAQSGTFYIVGGEGISSTTGSTFQSMTTFTSSQTNSGHASASTSIPSTAITVTANSTIYSSATSSFPYSTDVSVSTGTSTDIVTLPPPASSTSSFSTITNTSMIPSSSSFTTTTGSPYYNTSSFLPSSVISSASLSSSSVLPTSIITSTSTPVTVSSSSLSSFTPSYSTNLTTTGSTTTTGSATVSSSPFYSNSSVIPTSVPSSVSSFTSSSSSYTTTLTASNTSVTYTGTGTGSATFTSSPPFYSNSSVIPTSVPSSVSSFTSSNSSYTTTLTASNTSITYTGTGTGSATFTSSPPFYSNSSVIPTSVPSSVSSFTSSNSSYTTTLTASNTTVTFTGTGTGSATFTSSPPFYSNSSVIPTSAPSSVSSFTSSNSSYTTTLTASNTTVTFTGTGTGSATATSSSPYYSNSSIIVPTTVSTSGSVSSFSSSPSPTSSFSGTSALSSSSNEETTTTTQVTYTTSPEETTTTMTTTTCSSRPEETISTVSTTSTVSESGSSSASITSTYPSSTLSMTTSHLSSSSVHSSSAHSSSSRSSSMSLPPSAGSSTSLQRISLLCVFIPLLFLF O13856 YEX2_SCHPO SPAC1A6.02; CHAIN 1..361; /note="Uncharacterized WD repeat-containing protein C1A6.02"; /id="PRO_0000051486" MGGTINAAIKQKFENEIFDLACFGENQVLLGFSNGRVSSYQYDVAQISLVEQWSTKRHKKSCRNISVNESGTEFISVGSDGVLKIADTSTGRVSSKWIVDKNKEISPYSVVQWIENDMVFATGDDNGCVSVWDKRTEGGIIHTHNDHIDYISSISPFEERYFVATSGDGVLSVIDARNFKKPILSEEQDEEMTCGAFTRDQHSKKKFAVGTASGVITLFTKGDWGDHTDRILSPIRSHDFSIETITRADSDSLYVGGSDGCIRLLHILPNKYERIIGQHSSRSTVDAVDVTTEGNFLVSCSGTELAFWPVDQKEGDESSSSDNLDSDEDSSSDSEFSSPKKKKKVGNQGKKPLGTDFFDGL O13859 MU125_SCHPO SPAC1A6.08c; CHAIN 1..285; /note="Meiotically up-regulated gene 125 protein"; /id="PRO_0000096287" MILKDSLEAKSCFKSSQTSHLAARVAMENPQKGNVINAQSSRQPSSENEFRENLFFKEMRTNGKNEHETSCRSVVLYRNSKSAKRYPLSTKCARISYMQGNKDTKTALTKKYKSNEDVSRMRKKGNKYPQCKSKNLYDSLKLEECIESWSLNQKQNENFYEHTHLNSRDDSNPSSCDRETFFLSDEDSEISLMEGLSSIENGYPDEKETLAALDNVKLSDENAAHLGYLVKYFQNYTDKIILKETLMDWEDKEPSLQELTESTKYLENLADTDHRTSNKPFLFLR O13861 TCD_SCHPO SPAC1A6.10; CHAIN 1..485; /note="tRNA threonylcarbamoyladenosine dehydratase"; /id="PRO_0000120582" METLQVEVFFLFDFTSIMAGFKVPSWITYKSFWIAVSSSVTTACVILGTLEFRKHRSIRRLQSMIVPEAGKSIQLSSSGVPIEIYDAGEEDEGISKGVPYDENLIREQLARNYAFFGEDGMERLRNSFVIVVGCGGVGSWVINMLARSGVQKIRIVDFDQVSLSSLNRHSIATLQDVGTPKTLAIKKAIKKFAPWIEVDARNALFNPDSADDLLSGNPDFVIDAIDNIQTKVDLLSYCYNHKLPVIASTGSACKSDPTRVNIADISATSEDPLSRATRRRLRLLGIMEGIPVVFSTEKPDPRKASLLPLSEEEFEKGDVDELSALPEFRARILPVIGPMPGIFGLTIATYVLTSIAKYPMDPISTMTRPRLYEEAVKRLHAEARKAGVNLDKTFNASEMSYIIEEVYVGRSALPPHESQKVTVVRWNPQLPFDHTNLVAMTRNEARYHEDNVLAKNVDPSTVYGKDVIEVVHSFLRRLRMWEMLY O13863 YDU2_SCHPO MOD_RES 72; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B1.02c; CHAIN 1..537; /note="Uncharacterized kinase C1B1.02c"; /id="PRO_0000120718" MEPGSKLSEDETFSQTFNEEEQEDSRNKDILAFDPSVDNEPLLTKKLSSLSIYSEPSPDEASNLQELKFVSSPPSVRVPRSRRNRRNSRVDSEARKRQFDRVKHSVSNSCKLHLSLQGQEAAQLRSDSLYLEASDKRDLTSLVTRVKELARKLSAARLAFRFRKVLLICNDNKESIERSVELAQWLLDTFSFTPSSSHNNMASSNTQSNTQLSEMESEEKSFNKDVYPNDEYTPFTPKNQFVIYLEDTLASLDVVESLSPKKNVRFWTSELCTQCPNLFDCVITVGDDSAALRASWLFQDVVPPVLSFSTAKAGFLSILPIAEYTKTLDLIFHRGFTVNLRMRFQCSIMRYVGEHSTHICEGQYSVLNELLIDRGPNPFMISLDLYVENEYITTLQSDGVCVSTPTGSTAYSVAAGGSLCHPGIPAILISAICPHSLSFRPIILPDSMTLRIVVPLDARSNAWCAFDGHHRIELGLGDYISISASSFPFPSVIRSKYSKDWFDILRQTLNWNDRKGRQRSSRYKSHVHKTNTSEEQN O13871 YE16_SCHPO SPAC1B3.06c; CHAIN 1..278; /note="Uncharacterized methyltransferase C1B3.06c"; /id="PRO_0000339158" MSKPTDQLYYANGVDSYIAETHAWRTPETCSTYMLKYVKKTDRILDVGCGPGTITVGFPKYVPEGEVIGVEPSQELLDKAEEALRKEETLKKEKINNCSFRLGSIYKLPFPDNTFDIVNTHQVLVHLQDPVAALVELKRVTKPGGYVCCKEADLLSACVYPKEYEHDLLLQSQARINLHGTNPTAGRSLRGWAIDAKYVAENIHSSASTWCFADEETRKWVSRLFIQRVLHSNERLDDDDAKDQSLRKRVAEAWQRWKEDSRGCFFMTDGQIVYKKEE O13873 CSN12_SCHPO SPAC1B3.08; CHAIN 1..423; /note="Protein CSN12 homolog"; /id="PRO_0000121044" MSERPLPLNVYFSTINSAVARSNSVLLAKNLSIPWGKTLTSVLNFDIPGTYSSDDVLKLTVERSISKNWTDIVLLHLQVLLYLVRDHDPAAAFKQQTELAQHLYREFSSGRCTGVHLPVLFIVCKDLRFLAINAHNAMLRRKQQLKVISVDESEENEQLEATARLINRAFTICINDRAPLSTSRKWGAYYIMGLLFKLYLRLDCVHLTNNVLRAMKVVELPDISLFPKSHVVIFHYYLGIVAFLNQNYKNASAELEIAFSLCHKGYNRNLELILSYWIPTRILVNHQLPTKNLLSKFPNLASVYIPLTRALKSGNLGEFGKCLQKNETLLAKTKIYLTLEGTRDLCIRNLFRKTWIICGKSTRLPVSVFQIALQVAGTDLPKLHVEAILANMISKGYMRGYISRNFETVVLSAKDPFPKNVST O13874 YE19_SCHPO SPAC1B3.09c; CHAIN 1..528; /note="Uncharacterized NOC2 family protein C1B3.09c"; /id="PRO_0000121053" MGKASKATKKFTKNHLKNTIERRKQLARSKKVYGTKNRNSHTKNKLESGTNDNNKNKEDLSKLYSDVTTSNTSHEKDGSEDISVLNVNSKGASLNQVSTQKRRSEKDLLAAIAYCQKLSGTNQADALWKNVEKDLKETLDNVDFDARSKILQDLRLEYAEILLTKFNFEKKGYQNLSSALDTILHIKKFSKFPNGLVTQLCNIFVNHSKAREDIQKAVNHICKIDSSLSVAVFQVFYSPLLDFFKSSPSEVNDFDTLEELQLFLIELLSLNSRFYQKIAFAYLSQLDAHLKRCLKESESSDAYKLIYNWQFTLSLRFWLHVISFLWNDYESISKEISPIAINLTLDCIRLIPTEQYYPLRLHLLKSLVNICRSTRLYIPLSSQFLEMIPFVLRRSSPLSDDKEVMYNFDMYSTLHVPKECLLSKSYRNNVRKEVILLMTEYFAIFSNSIAFPELSAPIIAQLRGLVNESAPGKHVLTFLNKLESTFSFVESRRMNVDFTLNDTSQVEAFEKDLDWRSTPMGKLVSDTT O13875 YE1A_SCHPO SIGNAL 1..35; /evidence="ECO:0000255" SPAC1B3.10c; CHAIN 36..664; /note="Uncharacterized Sel1-like repeat-containing protein C1B3.10c"; /id="PRO_0000350744" CARBOHYD 101; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 138; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 300; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 371; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 454; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 537; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGVSVLTFHVSLFLKRILSIAFFLLSLSTLLRIVNAQQYVDNNIGSMVLSDYDFAETPSVRVQRALEILRYYYEQEDVTYEEIIIQRNHAIELLRSASHDNNTDAMLYLANIEFFGLFEIIPEIEDSVKYYDMLQKANGSAFANNMMGFFYSTSFSEYASNNPALARIHWELAAKQGSLDAHQFLAYHNLIALNMPQSDEEAVKHYKFISDHLFEEECGSNVTYLKCIWPEIQDYNFAGENGMGVYGAASAYTYSDAYQALHTRSQYLREMSNSIEDWDYELMFEVAKLRLHGMYKYPRNYTVSDVLFRKVSRQYWPYTSENSVLANTPQSIISLAAQSCGYLGLLHLFDKGPLFDIDKAYWWFKRGATKNDSNSYYGLGYMAYHGLTSNGVDREKGMRLINLAVMNENPHALMFLGLIRLEEARYEEAYHLFLRAATQKSVISYKYLADCYYNGTGTSRSMISASLYYKKFVEAIRASATSMAIALEEIDEYGYFHNSFVYYLYAAQMGYALAEINAAYLMDENKFLINSVFRYFNYTQSEQEAAHDKFAYEFYSRAAAQGDIDAIFKLGDYYYYGIGTPKDYSKAYTCYKIAYEQSSIGMGLWNMAYMHEYGIGRDQDIYIARRLLDELSSNQNSYFPLKVAIFWINIHQLYIKLLKLLRLR O13879 YE1F_SCHPO SPAC1B3.15c; CHAIN 1..628; /note="Uncharacterized transporter C1B3.15C"; /id="PRO_0000121375" MDTNTLPPKPSISPSIASSFPTVKPFSSQNSTTSNPELSHIEKESNASSIIISQQPLSPSNISSAAPLDETHIATKASASLRNNNVSPHIPSPSSFSSSSSSDLDKSMLDEKHPDSEDITAVSLSTPPFPESIDVARFSSEEKKILSRIRRKLDLRIITCLWITYFLSRSVTYSISLSLTMNKHQGHSLLQTVSGLNYHTLSVGTGLSYVSLIIFDLPSNLLMTRADPRLWLSRIQVTTGIIGACHAVLGTKGSSASGFIALRFFNGLAIAGMWPGFAFYTSRFYRDQHLGKRIGWYYTAAQISSVATSLLSAAFQKMDGLHGLYGYQWMFLIWGVVAFTQGLFLPRWLPCIKHNQHNEKWISWIRIPKFLGFLKASENTGLTPEEEEVHAIYMAEMQVGKSWTLTDLADAFLDVRLWPPIFMFFGVVGISNGLVNYSSLIISEINENFSSVTVSLLVAPIWVFDAIAILTVLPLHDRFHKKMLFFVGSCLFVLAGLLITTFVSNVWGRYVGLLILGFGLGPTVPIIMTWVSSAMGPSHGDVGVAAGLAIVSGLGNLGSVVATSALYSGWKADTTFRRSNETMCGMVGIAIVASIVMHMVQKFNIRRFPFKRIYACLSERRKKELSVT O13882 RT18_SCHPO TRANSIT 1..38; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1B3.18c; CHAIN 39..223; /note="Small ribosomal subunit protein uS11m"; /id="PRO_0000116692" MVLKHSVTYNLSFFISFTFSSIFFSSLILFLVYKSVLSKLFFIKYLMLNLTKVGLRRFWSQSPRRNAPKKELSSLLESTITPKAFSKRTEEPNPIMQGTDTIPMPFYLHAKCLKNNTHITLCSPERKIIFRASGGTCGFRKGKRRGYDAAYTICSKVLEQIQVKRLGIENLHVIFHGFSQAREAVQNCLLGQEGAVIRDKIVKVMDRTPIKFGGPRGRRERRI O13883 PIGU_SCHPO SPAC1952.01; CHAIN 1..408; /note="GPI transamidase component GAB1 homolog"; /id="PRO_0000121397" MIPNEKLKLLGLLSISFFLQWYLANTWIAEFLYRRIEVSTPVSGFLRVREGLYLYENGLDPYSGGVFYQSPLLLILNYCCELLGGISVTRFVYTSISTMGGLFVYLIAKQARVLDPNQVLSTCSPLWISVIYLLNPLTFLPGIACSADMILNFTTLMTIYFASCGSYAIYACCMALTVFINPNALLLFFPSYLILRKCNSSIKFRQIFVVFLFYLAGLIITSGFFLNSLSFLKIPFRVYLDSHDLTPNLGLWWYFFTEMFNEFRTFFLFVFAILPLMFVLPVSIRLYYLPLPITIALIGLHSLFKAYPSICDLSIFLSLLPIFNKVQDRMRYSLLTNNAIVFALVLGSAFYHSWITLGCGNANFYYASNLILALGLSLKIMDFLKALLLVDWYANHPQHENIPLKQVQ O13894 MU103_SCHPO SPAC22A12.02c; CHAIN 1..124; /note="Meiotically up-regulated gene 103 protein"; /id="PRO_0000116733" MEQFEIIRESDADPYYFNKNLRLEECEIDGFTSIYKAPPPYSFVAGLSKNTSSNSFVIHKCLPPLQRNNTIRKRKRNPFLADRPYCINSEDMPLSDDRDMLKERHVKSRKLLLKEKGNRFYRRS O13904 MUG84_SCHPO SPAC22A12.13; CHAIN 1..195; /note="Meiotically up-regulated gene 84 protein"; /id="PRO_0000278614" MTLTHHSTFIKGIEGSAEGEIEDVRQTTVFDPPFYGHPMLVPPSPSLTTMFRTRSTTPDEEGTAIAEIDQQDWDIMVKVPTYEYYGFVMYLVSMLGFGVYIVWALTPAPVLKFFEIHYYLSRWWALAIPTWLFVLVIYIHVVLNAYNTEVLTKPFSSLECIVDQYALVGEEDGAAHGRVVDLRLCDVNKQQLEET O13905 YF3E_SCHPO MOD_RES 123; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 125; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 241; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 246; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22A12.14c; CHAIN 1..347; /note="BSD domain-containing protein C22A12.14c"; /id="PRO_0000310330" MDLYDYMAPTTTTEEDDEEGYEKLKEEMGSALNNLTNGKFGLFWNSMKEKSENFLDDTKGKASSGMQQLKSQLEENIPVNSAMENLRKVEETAGSFWSGFGSTVNGFLDQALQISPKEDDVSTPTHEASSSVFLNRHERQLLELVQNENTFTQIISEPSHGITFESWEKEISIDGKTEEISLLLEEYPDLRKQMESLVPSEVSYDDFWKRFFWHKEVVQPIKAIQSGNDEEEIFSWGDERSDEEESDNEQVNDEKKQSSEEDTTENNSAAEVIDETVNDLESAVSKGLQIETQPASHDGEVDGEVKEEEENKVSSSSNIEASQSSLEVKDEANRKVDDDDEDDDDWE O13908 YF3H_SCHPO ACT_SITE 157; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 172; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 176; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 33; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 78; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 105; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 172; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 176; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 206; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPAC22A12.17c; CHAIN 1..261; /note="Uncharacterized oxidoreductase C22A12.17c"; /id="PRO_0000310837" MVAPAHNYESRNILDLLSLKGKNAVVFGGARGIGHAICSVFAEAGANAFIVYNTTPGEKAAKEIAQANGVKTYTCKCDVTIPKEVEHAFAEIQKVFDTIDIVVPNNGICTGKSAIDMTYEEFANEINVNLLGVFNVAHNAGPIFQKQGHGSLVATASMSGVVVNVPQQQCAYNTSKAGVIQLIKSLAVEWRKFARVNCVSPGYTTSDMTGGKFHKEWEPYTPFERNGLAKEIASAYLYLASDAASYASGTNLIVDGGYTSI O13909 YDW1_SCHPO SPAC23C11.01; CHAIN 1..441; /note="Uncharacterized protein C23C11.01"; /id="PRO_0000116670" MDQEIRSNNYDISVSTVEDTSFEAMDDSILEIIDDEAPEIQGKPKANISTHFRNMLAMFGNFLSLGFFLVIIVLVGIAFEIGGRFCGLILTLALEVYFFSTALLKLFGLRKIALTLHFFEPLLVFILLIIALNASPSIEQNKYASFLASAWNTALLHFTPLFNLLEGMASLLVVQALGHLSRWLVHNKSENWMFFILLNASSAISMSLYLLYRVSSFSISNPNALMIGFSLATVIVISIYGVASGRANLSEASLMFLYIAYTVYMVCTDFGNPNTSSLEKPKFDYLPPNILQSVHYLISTISATLPRTLYNIVLFMVAAAKTVAPSVFATFAFRISVMYAVTRILPAIQNNIIFLEYSRTSKQGMWSILSPCILIAVYTNLLLQHLYPTPSFTSPVNQILCSAEIWRWVSAILTLLLYAIELAYSKESDTGQALASHFKLD O13912 YDW6_SCHPO SPAC23C11.06c; CHAIN 1..535; /note="Uncharacterized protein C23C11.06c"; /id="PRO_0000116671" MNTSQDVNAEAANERSALLPRFLGSHRGNVPENTDTYALTPLFYWIRSTSVGLLLITIICHLFLLLNIFISIPIISHLSPGFMPVGFTALAAILLAMQIMFVYSPNAPERVTQRIICFLLAIDVLVVFLSPILRHREGWRSNAFVLWAFLMSLWIVITDLMLFRQYKEEHPDYDAIAHRGYYWSWSPSTWPWRQVGSLTASTILSVILTILTIHTLVTLIMRAYDGALSAPGQLYTVTDSKARVHLECFGSSSSNNKTTVLVEGGEVSVHPFKEWLLNLQHTSPDLYEESKDFEGYENDVKPYLSPDTRVCVWDRPGMGWSDNIGSPSSVGIVMDLLTEALAQADVSGPYVLVAHGIGGVYSNVFAARHLSEVKGIVFVDAGSVQTLKDSGQFLSRFLLFVRGWLSPLGINRIFGSIFMGKTRQDRVYGMYSWTSDRWVKSKIEESLTGPSFSRYELQSAQSVLPKDLPVSVISAGKSMKRFKKWPDEQRQLSKLTQRTVWDIVNNAPHDVWLSDDGGDLIMKRLGEIIYGGWPN O13926 YF66_SCHPO SPAC23C4.06c; CHAIN 1..327; /note="UPF0665 family protein C23C4.06c"; /id="PRO_0000352829" MTFYYIRILRLQEKLEESFKYALRVVFTITSDLGEVSYPQDATVRVEALDRQQSHSRITISKQCVSWIGNGHAAETTLYFPASHQQIQLTLHLENQNSIVDSIHINADTVLPVWSEAFSPKSTLPNMVWRYIQGPEKKSPNDGLWFLEQMGNSIAKHLWDAGVVFSKKILSDDWHYSFSNRKDINVLELGSGCGIVGISIASKYPRALVSMTDTEDAIEFMEKNVEKNKSAMSNNITSDILVWGHDIPRKFRRHWDYIVMSDVMYNESSFSDLEASLQELMDKNTKLYIAYKKRHDNEKTFMSNILGWLDLVYEERGPITIYILQKK O13927 THT2_SCHPO SPAC23C4.07; CHAIN 1..201; /note="Twin horsetail protein 2"; /id="PRO_0000297690" MENQVSSFLIDSPMEWKTYMKSLSDDNPSFGDVTVNLTKISVSSKNAKSYAEEMYNYVTQEMVFISERSRLLLRAKRRLYKNQSLMKKTSVSTSNTVKMVFMSLAKQIEQMLKFCMMVYSKLCEAFETTLKVAKEFQICDSSQEWFFQFQLGYHRKQMELQMLSFVAEWLVLTQHYTDALNDSAKTLYDIMESSHKAAQKV O13929 YF69_SCHPO SPAC23C4.09c; CHAIN 1..131; /note="Uncharacterized protein C23C4.09c"; /id="PRO_0000121549" MDEELQAIRQARLAQLQAEHGSAPSNIASGPSSNQQQQEVQDEMRQNLLSQILEHPARDRLRRIALVRKDRAEAVEELLLRMAKTGQISHKISEPELIELLEKISGEVSKRNETKIVINRRVQDDEDDWDL O13938 YEP4_SCHPO SPAC23H3.04; CHAIN 1..353; /note="UPF0658 Golgi apparatus membrane protein C23H3.04"; /id="PRO_0000351424" MFWDFKHRIEQSVTNFRETTYEAFSRCKLFLKTLPKTSIFFLTVIILECLLIICFEGYCIGQFRTVELLKNLGIDSLPISLTLFIFACFFILYLCVEALSSKNIIEIIGLLCIHVALFIYSIVQISELAEIQKVFLSKTQSSLNPITLILNRHEAGNEGIYFILEVPKRIKPFLIALPVILGVASVMLGFLAHGMNKAYGWVIYKKIGPELRMRRRYLVYKIYVTLLKIDIYFFLGVTVQYVMVLPEDAVVEFVLTILVLPLTVLILTLSFNSVSSENMFLMMTVQFFYVCGIPYILFKIIRMYTSTQKEYYASSKQMITTFSVITLLLLLFTIAIGFACSHNFKKGLKEYCM O13942 YEPC_SCHPO SPAC23H3.12c; CHAIN 1..226; /note="Uncharacterized protein C23H3.12c"; /id="PRO_0000116728" MRIIALPLPNQRVFLHCYPSEYLAKKVTIHDKIINRIYKYWDSWSASKSYTKQKVVSLGNRILHATPYEENFLRAIAPVKKLNDTELHQTLYIEHPPNLESSTILAELNRSKQLQKTHTNYLIGNIIGLPLTIPFILIPLIPNIPGFYLCYRAYCNFRAIQGSIQLARVMSIENIQMQESEKLEKALKLFTNGDATPLNALIGHPDFVDRYKRAVAQEQRKSKIIK O13943 AVL9_SCHPO SPAC23H3.14; CHAIN 1..469; /note="Late secretory pathway protein avl9"; /id="PRO_0000353134" MDENGASFQVLCLATIGFHHLRGPEIEHLFPESMDFPKEWSILPFLSLPDGAHSSEKDFVYFTLPFPNDEGTVFGLSCTRQLNASSLKNIPSDVTRSSVQKAVVVITTSPPFGHIKDNLDIVTNAYFSQGDFSNLDVLRDFFHVLTRKEQDVHIALNINLKSFLCEWRQNALVLLKVLLLGKRILVYDKSAERLGNFQYSLLSLIPCMMSHLQDVSSPSAHSLEKSLHKPASLQTSDKRSLLAYTGFPLIIFGEGSMFSPYTPLQLVHVLEAKSSTSWLAGTTNTLIMLNQNKMAEVIVRSDTHQIEFVDPTIKNLTSLTYTDKSWMEDIISRVESSLEMELPGFEGSDDWIRNQFELYIFGMLATVKYYNFLKKQDDSILSQYHYLPSTSCISDYGETFLLEWMKTNTFRIWNNIADDDLFDVILPKHPCKEEHKVPISARIATLFSAVKITPKSRDGEDEGSKEPAV O13951 IWR1_SCHPO SPAC23H4.08; CHAIN 1..277; /note="RNA polymerase II nuclear localization protein iwr1"; /id="PRO_0000339140" MPLPVLRVKRKASEDPVNALYLELGNNPNSVSSTKRRKFAGRYYFKLSQTLKQDDRYIQINDESSEPTHEDVRNIHSHTKISSLKKNNYGIPVVQTSEDVVKAPTHMDLGSRENTKGILSFSSPRYTIQNLPSTQSNRVFDAIRVEQGHTTYHPHPQLDSMIQEYLSNGDLPLQQSTEDYVYDIYEASSKEPNKPTFAYGVIDALSIPDAFRSSLEQELVSETVDSDKDDPLHDEIDEDSNAESFYQNSYPDEDEWQDSSENDEFAYSDDAEQDFYD O13954 YEHD_SCHPO SPAC23H4.13c; CHAIN 1..184; /note="Uncharacterized protein C23H4.13c"; /id="PRO_0000116718" MSSNSAVQSKSPLLPKENPPVKAFPDNIQVSSSLLSFLIYILYTFSISGLSTFVITKYYIRPQWLYTLALRRALIKLYYNFMDGFNKRTDTLQHRVDDKKILKTIEKWSCIKEKLRRVANITEQEQQCIPAESSLDLSIQAMKGVVNAELYQFGSQISGSLEFDTPIGNLQKQIVSLKSKMINI O13964 YE44_SCHPO SPAC24C9.04; HELIX 17..33; /evidence="ECO:0007829|PDB:5N9J"; HELIX 44..61; /evidence="ECO:0007829|PDB:5N9J"; HELIX 70..95; /evidence="ECO:0007829|PDB:5N9J" CHAIN 1..121; /note="Uncharacterized protein C24C9.04"; /id="PRO_0000116695" MDPAHHIKDTSAELLSQQDFSILQSRLLEFLASQEARETVTASKELTLLRQGIRQLKEKVSKMEPEEMTVKEKKSIIEILKARIALKKAFLKMALSESNDTVVKKEDVRESPVDTFMENAT O13969 SYTM_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; TRANSIT 1..27; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC24C9.09; CHAIN 28..474; /note="Probable threonine--tRNA ligase, mitochondrial"; /id="PRO_0000035826" MMKLKKFQLHTPFAHSCNRVEIYTARFGPTPFSTKANNLKQPESTLNDHRTIAARQKLYTTSILTPGSIFFLPHGTRIYNRLVDFLRAQYQIHGFEEIITPLIFKKDLWEKSGHWQNYEKEIFRVEESRNVEDEHSNATYGLKPMNCPGHCIVYASTERSYKELPLRFADFSPLHRNEASGALSGLTRLRCFHQDDGHIFCSPESIKDEIKNTLTFVKQVYSLLGMNKLKLYLSTRPEEHIGSLDTWNEAENGLREALQESGETWIINEGDGAFYGPKIDVMVADARGKWHQTATIQLDFNLPQRFKLYYRTDAGDNAGSEKLIKQPVMIHRAIFGSLERFMGILIEHLNGHWPFWLSPRHAVILPVNQTDRILTYAKQVQKELSNQEVNESEFLPLNKNTYYVDINAEAQSIGKRLRESRLLNYNYEIVIGEDEVDKEILSVSSRHNHNSRDTRKMTIQQLKKEFIENVKAYR O13970 RT04_SCHPO TRANSIT 1..15; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC24C9.10c; CHAIN 16..263; /note="Small ribosomal subunit protein uS2m"; /id="PRO_0000311720" MLSRKLSPEQLVARRLKIRDWNHKIGAVVAPHYSPTLSIRNPAPPSQLSLPLLLSSGAHLGHSTSIWNPYTQPFIYGKREGIHIISLDQTMVYLRRAISVVRSIAKENGIILFIGTRNGQKDSVVAAAKRARGYHIFDRWLPGLLTNAREVQGKLGGSILCKDNRGKLIQTDKKPSYVFPDLMVILNPLENKSACLEAQKTHVPTIGIIDTDADPRMVTYPIPANDDSLRCTDLIAGLLSRVAEQEYQKANQAFEKDKFTLPL O13971 SGD1_SCHPO SPAC24C9.11; CHAIN 1..775; /note="Suppressor of glycerol defect protein 1"; /id="PRO_0000316029" MRPIKKSRSLKLPKSILEEIGESDSSARRGKRNHNLPHREKRKFARISRGKNGYENRKITEEGDSKSSELNDDYLDAHRKSSTKKKSSQNKQAKESKLLDPIAFQHKIALEEDDREIAHLEKMLGIKSKDKSAHSKIDKEFGWLLEDLDQEIDDIGVPGTEDPSYGHSEDSEVSDDTGDHGSVDELESEREGNSGEEEEEFHGFESNSDEFHQPETKPIRMDPLKPAVPSLPNANVGSKYVPPSLRKKLGGDKESEDALRLRRKLQGSLNKLSIANISSIIKEIEVLYMENSRHSVTSTITNLLLQTVMGRESMLDQLAIVYAALATALYRIVGNDFGAHLLQTLVERFLQLYKSKEKEPLSSHKETSNLIVFFVELYNFQLVSCVLVYDLIRLFLRSLTELNVEMLLKIVLNCGGQLRSDDPTSLQDIVTEMNLLLASADPSTISVRTKFMVESITNLKENKKTKVANASAQSKFEAVNQLKKFLGSLGNRSLNAREPLRVTLEDIEQIETKGRWWLVGASWNNVPSGDNTLSTEALQDKKKSEELTAHSKILQAAKKLRLNSTLRTSIFVALVGSEDYIDAWERVLKLHLKRNQLPEIAYVILHCVGNEKLYNPFYGLVALKCCTLQHNLKKSFQFSLWDFFNELQPDDDSEEREISMRRIVNLAKLYASLVIEAAQPLTILKHVDFMAINAQMQTFLLVFFTDIILGVKDDLQLVKIFENCKAEKNLSSKVDWFLKTYVRKNPLVDNSKKALFKSNLAMASAILQSISKEEI O13973 MRP10_SCHPO SPAC24C9.13c; CHAIN 1..88; /note="Small ribosomal subunit protein mS37"; /id="PRO_0000116697" DISULFID 30..63; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 40..53; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MSKKIVNPPRLQGLSRLRVRPKREKNTIPCGQEMAALLGCWQNHGGQTDTAQCANLVAALENCMKTTHRKTKSENTINYHLARLGKLL O13977 JMJ1_SCHPO SPAC25H1.02; CHAIN 1..464; /note="JmjC domain-containing protein 1"; /id="PRO_0000316594" MVYRPTAHEFDDLPKIEFIDSCPYQVFLEQYLKPCVPVLIGPKLTAQWKANTTWITSKGDPNILHSYILPDKPCTSRDNTSGNSLLNDNDIKNFIRSYAERIVNNEDKNVFLDSLLLSPNYEYLEENYGTIPVPLAYCNEKDRYGSQRRETVPLKSALHELRDEQVQLQCRQAPSNQALKSLYAKDMHLFRHLDPADFPYSTPDIFADDWLNAYVIDCESDDFRFAYLGSHLTTTGLHTDVYASHSFSVNLCGVKCWLFIDPKDLQTIASLYDDQQLPSWITKDDLFRGPLVNHRHLIKILFQYPGQTVFVPSGWYHQVLNIGTTLSINHNWCNASCILQMYTALKEQYEVSAESLKDLLEDGIVTKDRFSQVVTEVVEANYGWCWRRFWGMIKHQLKRRDAILHSSEYFSKWPIQPEFLPPLSWEYSILKNILLNDEPGSTFDSGSPPSSIVTIFKSLGDFKE O13980 MEU29_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC25H1.05; CHAIN 22..217; /note="Meiotic expression up-regulated protein 29"; /id="PRO_0000045813" CARBOHYD 84; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFVVKTAVLLFFALFIGNTYAYTYSLDRIQALKFSSESSNVDDGPRLHCKGPACSSHSNDLAICQHNQLNVAPHLLKWTCVWPNQSSHVEVIDYNIECKKTVALSMDSITKTCILNYKLEWTYSGVLLHRPWKLFSLKPFTAAFVLLLAASYLATACFRMLGYLGTPRSRFHDNRRWNEQKFMELAVSAVEEQLSNGIQLFSNVKQRVPVPVLDESV O13982 YEC8_SCHPO SPAC25H1.08c; CHAIN 1..399; /note="Uncharacterized WD repeat-containing protein C25H1.08c"; /id="PRO_0000316554" MAEEEENQELYIAENEVEEVIKDNDKLMDQGVTEDEAEQEQNDTMNNMVMDMSVQGFFEHKDSVFSVSINPVHSNLCASGGGDDLGYIWDITTGEQICQLTGHKDSIVAIDWSFDGTYIATGGMDSQVRLWKSSTGFEFITAFETVDEIVWLSWHPKGLFLAAGCNDGSIWMWSLPSGKVVQVMYGHTAPVNAGKFIPPGVGKRLATVDDSGTLIVWNPATGAPECRMSSDDHRFDPGNEETAAGWTSFDCNAEGNVLFLGGSSGKVKVVNINSSHILASLEAQTESVEAIALCTALPICACASVDGTVALYDSASLKFRKSLPHEQAVIDCKFLPNTPYLLTACADCVIRKWDVRSGQLLGEYTGHQEPILCMAITPDGKRVVTGSDDTELLVFDCEH O13986 YEG4_SCHPO SPAC26H5.04; CHAIN 1..789; /note="Uncharacterized protein C26H5.04"; /id="PRO_0000352824" MVAINDSTDSSFFKENPKIFKDEHELLRYIVPFKNWVIGRPDRKEYAIRNGAPKLLLNLFSLENLSMNEKYQVFVVLNSLMSEDQDPFVQFLRHEDLLSVMQMISKRDSTPYGMLNITLKVFNTMLSFDKAAEYVTQLHSDSIINQMFDLYTLPLKEQPSLDVLRISNLSSKILHRLILYNSKVGDSPRFCSALFQITNRATQLRLYSRRRFWNDCSILITNSLGTLNAYLKQHVKSYKQREKTRLESNGHVSPRDMDLDEIENVFEGNKDKVALFKSEIFGPNGDEYITQLFCLVRQFDPCIRLLSISCLVTLYKAGILSKNQTKEIQMIVTPILIRLFFESREAKQIAPRILAIIINENEIMQKTAVNAGFIDAAKYLLEYATKEEENEINFLSDELQSSVCFNLPATKKEQKNLILESVLLAVAALTTSKDEYRKLIVDAKYLPVIINALKINSNSVKKAACECLLSLSRSVYILRTGLADADVSEPLIKLLSDPDTRVKSTATSAICNLVLKFSPLREKFLTTNFIDTLISNISTKDSSLRKKTVWVLRHVVFGDDETIQLEPLKKIGASKLVELCNDEDLGVQEQMLQVLRNFTCQKEESVDFLLKMVPMELLAKILLEKLESKNPILIEPSIYILVHIAASDGELRDSILRQTKLLLLVKEIMLQEAQRLKPEQMSTNVSSPESDSEMDLQEDDFDREMRPPFDIYEEDTYEPNSEILLAGIWLCINILWPKQCTSPSQEDKERASILQNLGFGECLQMLQNHSSPDVRERVKDALMYINVTD O13989 YEG7_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAC26H5.07c; CHAIN 23..505; /note="Uncharacterized protein C26H5.07c"; /id="PRO_0000014196" CARBOHYD 25; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 114; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 342; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 454; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAILKSALVGFICFLHFFIVNASDNKSLLTEDIMASQVCNGMFAKKGKTSEITLKIDSYTSDFGGAIRLLIFNWKDVNAIGMEDDDGEKHYICNYEDIEAGVCKDDDYGLYLINQTAPHDSIYSAAVDAESMVSPLKYPVEQSGLYCVFTAPLEGSSEAYKITVTWENYFGNLDATDYPHLFLNPILLAINCLIGIWWSFIMFRYRHDLLQVQKYISGVVALSIVCTMVSTGYFYFANSKGYTTGSKVFAFFLSLAQSARQSYFGFLLLIVSLGYSIVVPSLGSLLRKCQILAGLQFVSSCFFLSSLFISPSNKESLVILFAAPVFLITLFAMFLWIVLALNNTIRDLRIRKQTVKAQMYTRLWIVICFGIVAYASIVAANAILIGIYGQMNYYLKYWKLLWFLNYGYTDILVLILMLTILYLWRPTENNRRFAMSEQVAQDVDEFEMTSSLSNDSLHLHHERPTSPANPHIIHGSADEHQALFAVDDESDDDASTLATSKQKPA O13991 YEG9_SCHPO SPAC26H5.09c; CHAIN 1..369; /note="Uncharacterized oxidoreductase C26H5.09c"; /id="PRO_0000091790" MAPIKTAVLGTGMSAFIFHYPFLKALPNHFEVYAAWERRATSTESKARAAFPNVKVYTKLDELLADSNIELVVISLPPNVHYEVVSQALNAGKHVLCEKPFTPTYGEAKELFDLAKSKNLMLTVYQNRRFDGDFLTAKECIENGRLGEVVQFESHIDRFRLFRKGNWKDVPNPGCGLVYDLGSHLIDQAITLFGTPHSVTAKLESQRQIPPLEVEDCFRIVLHYLPQEGRLPLDVIVCSSSISCGLDMRYIIKGTRGSFLKFGIDPQESQLNEGMSPMDPGYGVDSSHHYATLWTLPPDIDVRHPPKPTKSTLMTIAGDYRRFYLEVHEALVTKTFETSVKPHQVLLVEKIIEAAYKSSQSSTSIPLSE O13999 MU155_SCHPO SPAC27E2.04c; CHAIN 1..187; /note="Meiotically up-regulated gene 155 protein"; /id="PRO_0000278510" MRPTSGCSKDDTIQKQNRRHNTVDNKQEKLPLSIEIFLNKQINKISFDTIRSKQNCRLKEIYCRLKIRCRLKKKFIKSLSKKIISYHFISFHTIVVLLLLPPFSHLLVLVYPSVFTTAFYHQKWALRLNPCLPTYFFHRQRQCVTLLIRNANENMRARRVNSVMLTKPKQFLFLLEFITLFIFTYCL O14009 NSRP1_SCHPO SPAC29A4.06c; CHAIN 1..355; /note="Nuclear speckle splicing regulatory protein 1 homolog"; /id="PRO_0000116648" MSGTGFRYGLNVMKKKKPNESSNRITFTEDDSSSSEQEHAPIPNSFSSQITAASDASKDDNYDASIYGFDEFYDSMKSAEREQMELKRLESKDRRPKYMENLIESAKKRKRDLLLARERALLKKNELEGDDATEKFVTSSYKKHREEVQKAIEDRKEEDEKSITDTTTGMKDFYASMLDRQEKIHQAAVEGVQNSKKTGAEIGDAMKGQDTLGSDNLILEAKKKGLKLELNDNNEIVDQRQILTAGLNIRKSSANNSMRDDKKRNHKSSYKRSLSPSTRYHQDRPDKRHGTYSLEEIDKQRKEFENRQRLQKEKEFQKSREAALKIHASRNTTETQVQSARERYLQRKKKAATNP O14015 MU108_SCHPO SPAC29A4.12c; CHAIN 1..150; /note="Meiotically up-regulated gene 108 protein"; /id="PRO_0000116650" MANRFTSSDQTQETHGHHVDKHSFSGRQRHPSMGVHSFNEYMNEYPEAGPLVQEEEDDMESSSYHATQEDIGDDDSRSESTRNRSSQHTGRVNFSSLGGLGSIFGGKKSRSKSANGTQKKNANNNEEQLDEEEQNDPYLDRDISLLGSTI O14016 UREF_SCHPO SPAC29A4.13; CHAIN 1..235; /note="Uncharacterized urease accessory protein UreF-like"; /id="PRO_0000316578" MTDSQTETHLSLILSDTAFPLSSFSYSYGLESYLSHQQVRDVNAFFNFLPLSLNSVLHTNLPTVKAAWESPQQYSEIEDFFESTQTCTIAQKVSTMQGKSLLNIWTKSLSFFVTSTDVFKYLDEYERRVRSKKALGHFPVVWGVVCRALGLSLERTCYLFLLGHAKSICSAAVRLDVLTSFQYVSTLAHPQTESLLRDSSQLALNMQLEDTAQSWYTLDLWQGRHSLLYSRIFNS O14017 YDPE_SCHPO SPAC29A4.14c; CHAIN 1..346; /note="Uncharacterized protein C29A4.14c"; /id="PRO_0000116651" MLKSFEKHLNAVSRKCCNFILGSSIPVLGFYCADTCIRNAFMEFMETRNSKSKYVEAFNTVQSNGATSAISTFHILKDEIIRRIPLLPIIQELRETRMSEVSAEEKILLWNQLKFMSLVRMFTTLAVLAQCNLLCKLALTVLGREAFKEQMVKEFDPSNTLRPSGSDEDPAVFTGIAYILLNNQLDELIQQVQLAVTLTFEEVSPTDIVDRKLIEALTTRVVEVFVNNYQFSIDGNKEVLLAEIPKQYIVTGNLLYRVLELEDFATQMDASIVMKNELIALNEHMLTYLPSIPQEGIRLAKILTTFTKISENVFEAPFQEQFFQSLQMVSDVNRYMAIVFSSFDDC O14020 YDPH_SCHPO SPAC29A4.17c; CHAIN 1..147; /note="Uncharacterized protein C29A4.17c"; /id="PRO_0000116652" MNCLLLGRGFLHRFHPFRPVLCEDSASAATTITSQFKLNYRQIFIGSSLGLAAGFALGKLGRLFIVACSAVFATIAYINSKGLIRINWPQLQQQVIGPTEQYTGFHFPSSGRFNTQSTFPTIRNWICTNPNFKLSFFSAMYVGFVSS O14030 YEM8_SCHPO SPAC29B12.08; CHAIN 1..689; /note="Uncharacterized protein C29B12.08"; /id="PRO_0000304058" MTKEWECRREQIIELSKINGMTIRELQARMSKMYKFDASIRSYKRVLARWGIRVHRQRFVSPRTEEAAARTASGDVSKALDELVTQLFHARQSDKDSLAQIEANFGLKLSKRALHYRRKRLALKRPPPDSHDSPNNSIPLMANSCLLSADNSSSSTTSNPNVAPPISTLPDPVATISSSSSSHLDMGAIHPPHHSSLPPHMGVDPSTMADAHNAHSSLTPPQSGYSSMPSLPYLQQPFQIPSQRFSRQQQSHPFPAAQHAVNGQPQALYPFIYQSRNVPMGSTMFASSNQSAAHPDGNNALPMDNTHANISYMQSSQSMPVNSYSYDRYTPNQPSYLESKPGNHQPSYTSEQPMYSTASVPQQISNGPTAVNGLPMNSYTPHSNHLHSPSPNSNSGPTDSLSAPNSTSSPSMAHANGASFASQYPSLNKSIFPASYSSSAEDGQNMQAPAHAYMQSSIYGVNQEQKSEYPSNLSMQSSMSIKDPSQLQRIHLYPQHSQYDPNGMTMRDHYSERIEPEAKPSDETLTVRSSRDLSVHNVGTLPVLSAAAATQAAMPHTMGPSAHDSASAPSPHMQSQQALPYQYYNPLPAMADPAQNVPQQLPPPIHSHLSDDQHIQYSYPNTFVNRFPQNIHHPSANLLDASAALNPVQNPLLMPQQNHEHSPLVRSDAALHDHGPLLPVYPDVDSRFV O14032 YEMB_SCHPO SPAC29B12.11c; CHAIN 1..174; /note="UPF0664 stress-induced protein C29B12.11c"; /id="PRO_0000352830" MSINWVTYKEGSESDILLLENECMFDCFDGVAISILCKPPSLKSWTCTKGLLCLTNQRLVYIAKDTDCDFKDFQSPVANLKDTKLNQPFFGANYYSGTVMPVPNGGIPCEAEVKLQFNEGGIFNFVEAWNRLIQRFQEVDSVSRVQHLDPLPPYHRPSSSQDQPPHYEEAVNKS O14033 YEMC_SCHPO BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 25; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 46; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 49; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 73; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 94; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" SPAC29B12.12; CHAIN 1..113; /note="Uncharacterized protein C29B12.12"; /id="PRO_0000310737" MQTPTARSSTNVYGKLVDNETRCFHYHSKADVVALRCGQCEKFYACFQCHDELNTHPFLPWRKAKFHIPCVICGACKNSLTVEEYRSTVHCKYCNHPFNPKCKNHAGYYFEDA O14034 YEMD_SCHPO BINDING 8; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="structural"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"; BINDING 10; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="structural"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"; BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"; BINDING 29; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"; BINDING 32; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"; BINDING 71; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="structural"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"; BINDING 74; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="structural"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01239" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01239}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU01239}; SPAC29B12.13; CHAIN 1..137; /note="Uncharacterized lyase C29B12.13"; /id="PRO_0000372335" MPEYEGNCLCKAIHLKAIIEEPKLSCCHCETCRIWCSSPFMAFSCTQKPSVSENENVGKYASSSFAERIFCKNCGTTLYFAYTNGKNPYFINAWLFKGIENITFDAQVCIDDKPDCYDFANKTSMFTVDEVMKSIVK O14038 YEY5_SCHPO SPAC2C4.05; CHAIN 1..134; /note="Uncharacterized protein C2C4.05"; /id="PRO_0000122238" MVSAWIYFTSLMLTCANIMLQMYFTVMYSDLKDDFINPIDLSRKLNWYVLPEMGFQAFSALLLLLSGAWITFLLNVPMLAWNAKMIMSNTHMHDSTTIFKDVSSRQKRSFFKLACFAVFFFVYLFLFVSRLVDE O14042 FMP32_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC2C4.09; CHAIN ?..216; /note="Protein fmp32, mitochondrial"; /id="PRO_0000363390" MYLKIPCNSIYHQFQPLFRARTVHKVRSLGLNGFYRKYHGFNSLRFVRVLQEAGIDDKKSETLMRLISNVYSDMHEKISDFSVTKEQQDRVMYQQKVDFAHLRSELQSIERQEMVALHSQVEQLFSDVERLKTSFRDQLNNSTSEARLQLNIDRLNHYDETASQDLKLRELSAEIDTEMSNFRTQLASFKTQTLQWVFGIVTGSGALLLAYVRLII O14045 TPT1_SCHPO CATALYTIC ACTIVITY: Reaction=2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide; Xref=Rhea:RHEA:23324, Rhea:RHEA-COMP:11106, Rhea:RHEA-COMP:11107, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:76596, ChEBI:CHEBI:82883, ChEBI:CHEBI:85027; EC=2.7.1.160; SPAC2C4.12c; CHAIN 1..365; /note="Putative tRNA 2'-phosphotransferase"; /id="PRO_0000316237" MYKNMNSHELIEESNNSGTPATKSSSKPTKKIRPRNDLVHYSKALSKVLRHTAKANGLQIREDGYIEVDSILKLPQFRGMGMELLLSIVKGNDKKRFTMEEVEGVLYIRANQGHSIKAVQVPMARIDNASSIPKVVHGTKKELWPVISKQGLSRMKRNHIHCATGLYGDPGVISGIRKSCTLYIYIDSAKAMQDGVEFYRSENGVILTEGVNGLLSSKYFSRVETSDGEVLLDAKASPKNNRSDESDQSDPESIDPFCDNLQALSMHELELLEEKHSNFGYSEGIIKGKMQVAQSGFDDGFKHGSRLGFQMGKTIGTLKAKLYIFEENEQMEILKQELDRLQESAEFHIFVANHKEEILKCIREK O14059 HIS9_SCHPO CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate; Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15; SPCC1672.01; CHAIN 1..306; /note="Probable histidinol-phosphatase"; /id="PRO_0000122321" MPISSHSHSGQFCLHAQGKLEDVIQEAIQQGFQSFSFTEHTPRDRVEDLYPEELHLQPEDLFKTFDEYVNEARRLKQNYGDQINILIGAETEYIRPESVELLKSLNTKYNLDYFVGSVHHVNSIPIDFSPELWQKALQHVGNNPEQLFIDYFEHQYDLMQRLHPLVIGHFDLICLFAPEDAKEVFKNSKSVWELIQRNIKYAVSYGGIFEINTSAFRKGWKTAYPQQRLLELMVEQGAQLTLSDDSHGPHQVGLNYHLAKSYLDKCGITSLCMIEKGPDGNGTVVKNVTVDNVWSKFVGTNGITNT O14061 AST1_SCHPO SPCC962.05; CHAIN 1..519; /note="Asteroid homolog 1"; /id="PRO_0000116536" MGVPRLGRFLEPFGKPVYFSSYPEVPLNCSLVIDGPSFAFWLWFSQGIVCSDFQGYQKAVLDFHHLLSRLRFKEIEYIFDGGLPFSKHQVRVNRYQQKINDLRSAYINLCVPIAQHVLMGLAKAKVIVCNEEADKYCAFQAKKLDAVILSQDSDFLLYDIDTPHYGYIPLQSLDVTSNGISGRKYRFDEIQKDFHFDLHILAAYLGVEGHPLDLVIDYHNTFEHICKILENSVKDKFIEKLVSKEELTRVHAFYSLNDLKLETSTINTFMWGRVQELLNSQLQPAEIWLPQLLELPSKHCSWLESAPLRLQAYANFSKQMPEFGTEVLEYFRLSDRLSKRLISVDYDYATVCETLDSKFSNWNLPHRLVLWTLRCMKNLNNITATSFLLMHVSLFLGSPMNLQPVEPTQEDIASVSRFIATIYSICMLIFSEDKEQSSISFQEFVSFSPLSSTLNFALFHQAASKLKTGKSPLSIVTDKTTASLTYKMYKDLTNDYSDIYMIMDIWKPKRKRKTKKDQS O14062 RS12A_SCHPO SPCC962.04; CHAIN 1..145; /note="Small ribosomal subunit protein eS12A"; /id="PRO_0000122338" MSEQGDQIEQVDVVEEVEVEAAAPETVSVEDALKEVLKRALVHDGLARGIREASKALDRRQAHLCVLCESCDQEAYVKLVEALCAESETPLIKVADPKVLGEWAGLCVLDRDGNARKVVGCSCVAVTDYGEDSAALQKLLESFSA O14065 YC31_SCHPO SPCC962.01; CHAIN 1..1429; /note="Uncharacterized protein C962.01"; /id="PRO_0000116535" MEGENSKSVHPILSHSTSVVSERASSSGVNGTNGGMKQVSPVSTARTSIARRPPSTVGSQTGSLVNAPPKRSSGIERFDHVTGTAENRPQTPSTKASVANVKPAGAAESAQNANLISSKSENVPEPAGEKVSMPEKQDLQSALPSDAVSNAVIGWKSIYHASDVDVHDHFANVLSALQWDSHRVEPSILETYSSYKLTGQWWQSTSILLAVSILSWIASKLWFRFFILFFIIITGTIVYGSCMISVRRNIREEVVQELSKKNGDVDYETMSWFNTLLQRFWMLNEPEISKSVSTSVEQSIAEYLPSFIKEAAFSTFTLGSKAPRIDRVRTHPPVERDVVLMDVDFSLTPNDNYDVNDSSLKCRVNSLISLVIKFGFGKYMFSFPITIKDLRLSGKLRIRWGLSSDYPFIQTASFSFLETPIVYANIRPIDIPFLDADIFYIPGIGQFVSEQLGLLLNSMVLWPNMFDYDLSAMMAGIASGTAVGVVGLKIYSARRGEVSDSSIDRKPSSFITVTTSGREHGRTPIRSNTFSPTFDTTIYVVINSLNDPLKLSLYDNSGKSPILVGTTYIDPRSLYERGFIGDIYQFLYNAVNVGSVAFDATFFPSLLPKKTMDGSKIEPPESSKGILNVNLGCVNNLTELTELTKKSSLKYVLYVDSKEVASKTIKFVDRTPISLQTNAYIENNKKSSIKVAVFDVKSPEKAIATVSVPLPELLHEGYDTFHFVENPKATIDIESFWTPVDVVEEKSAKTYIDNLVGVMRLSVIKANDLVNVELPTRKSDPYARVIVGNSVVARTVYTPNNLNPIWNEILYVPIMADTKTIDLEAMDYEESGNDRSLGYASINVQKYIRNAKRLDRSALASTVFGTSEVNALTLTSRKGQSVRGTISVNCDYRPCLRLNTDNSSKQSSENVQSATDPTTPAKDNSTSNAETSSITSVISVNEALQYPSGFALISIVSADLQDVGVDLRVFTDNAAFPFITTPIAKTKTPRWSSFGISMVRELQFSETTFQLTDGAKKDPKVVCEHSVKTLDLVSEALGRPYSVEIPGSNGQLNHVRLSITYMPVPMTLNPMESYINSGSLHFMLQDGQNLPIGDIRSSDPFVVLKLNGESAFKSKVIKKNLNPVWNEEADIVVQNRVLDVLELVCYDWDMGEKPDVLGTSNIDLLSLEPNVESQQSIKLDSKTGTINASLRFVPGWHRRKAVLDVTLADNFLHAANKGAKLVVGGVGAAGGLALAGVTTIGSVGSKAVTGVADGVTGTGKHIISGAKGISKMGMFRRSLEKNPSRSDLTTTQEASSSASVPPAIAPESANAALTSTIDKTTGAPELAQKKYKVYVGQGKNMPHKTIKIIVTDNQDHSFKTKSRKGPSPSWNEEIPVKWSLGDELRISAVTSNLLGHTKLGEAVFQEDAIGTFRVVIGGSSSVEIKVEAE O14074 YEA9_SCHPO SPACUNK4.09; CHAIN 1..339; /note="Uncharacterized protein UNK4.09"; /id="PRO_0000116711" MQMNSLNDPKHLVKAVVRGEIKCLDVRAQSKYEISHLRKSVNIPSEKISKCWYQLPAKQEELFVVEDQGDKIETEETGTCAQQLKKRGWNIAGHFMFSHKIWEDLSLPQNELLESGPNRNLLFEPCPYLKEVMPVVEKGIKTNNARVLDIGCGSGRDLAWICFRESGKHWMVSALDAEKRAIQRFSELFSGLGLEDRIEGKKVAKVDASGLWKLYTRDGKQEPNATAISLADMLADFQNVPEGDVYKYDLVLQIRFLNRALLRQSSSLLRNNGFLFLCTFVNDGVHQYEHPRGSDHRFEKGEAAAIVSESDGRIRVLKDEIGFIEDGRPVQILLAQKVE O14075 YEAA_SCHPO ACT_SITE 246; /evidence="ECO:0000250"; ACT_SITE 275; /evidence="ECO:0000250"; ACT_SITE 293; /note="Proton donor"; /evidence="ECO:0000250" BINDING 166..167; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 244..246; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 270; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 293..296; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" SPACUNK4.10; CHAIN 1..334; /note="Putative 2-hydroxyacid dehydrogenase UNK4.10"; /id="PRO_0000076038" MTLSGKPAALLVGTLKHAHKEWEALGKYAELKTYSDGTREDFLAKCKTEFQNVKAICRTYNSKFYMGIFDKEIIDNLPPSVKFICHLGAGYETVDVAACTARGIQVSHVPKAVDDATADVGIFLMLGALRGFNQGIFELHKNNWNANCKPSHDPEGKTLGILGLGGIGKTMAKRARAFDMKIVYHNRTPLPEEEAEGAEFVSFDDLLAKSDVLSLNLPLNAHTRHIIGKPEFQKMKRGIVIVNTARGAVMDEAALVEALDEGIVYSAGLDVFEEEPKIHPGLLENEKVILLPHLGTNSLETQYKMECAVLMNVKNGIVNDSLPNLVPEQRGDIE O14078 YEAD_SCHPO BINDING 55..60; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 249; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" SPACUNK4.13c; CHAIN 1..407; /note="Obg-like ATPase homolog"; /id="PRO_0000122461" MRGIVTRIVLSTQKCLPSVNCTRRYYSKQKDISIVRQRLGRPGNHLKIGIVGMPNIGKSTLFQILTKTNLGNPANYPFATIDPVHAKAPVLDSQYELLCEIYQPKTRIPAQLTIYDTAGLTRNSSKGEGLGNAFLSNIRSVDALFQLVRAFPEAQVPHVEKSVDPVRDLQIIQEELLLKDAEFLESYLKKEGRSPKTCAKALDTARRALEVVLGKGRQISKAEWNDEQIPILNSLNLLTAKPVVYLVNMDQDDYLSDEQEALKGIKEWVEKNSFGDQVIPLSVLFEEQLFMLTPEEAAQECASLGKNSQLSEIICAGYSALNLIHYFTASEKIVQAWTIADGSKAPDAAGIIHSDFKKKFVAGEVIKFSDFEKYKSVDACKSVGKCKTKGKDYTVEPGDIIFWKIAR O14080 YEAF_SCHPO SPACUNK4.15; CHAIN 1..208; /note="Uncharacterized protein UNK4,15"; /id="PRO_0000116713" MPQFFRTQPLTDRTTSHGFAEVSSEDHCYCVWLVPAISSDIELRYRTFVDWAVCHKVDFEEMQLPTAPHITLARGIKLKPNQSFKSVLQYIASKRKSPLNIKFGKVAIGDSFYKRVYIQVEKTPGLEELQNAAYDLADTSDPFNVIEHPYMPVIYAKSICSDYSTSDPIETISSIGQASWGKACFLELIQLNKANHQGYVCDRIEFTV O14082 YEAH_SCHPO SPACUNK4.17; CHAIN 1..406; /note="Uncharacterized protein UNK4.17"; /id="PRO_0000116714" MMQNIKDEAYKTYQNVKDEISSHLPQSAPEPTGPPFKCAIFGCGGINFGTAEGPWNNSQKLELVLGHRLQVVALLSPHKSSHERVLKQKAETEYASSYANTREFYSADEYLEYLDSHPEEKPDAYIIGIPPETHGSTQKGADLELAILKRFPDASLFIEKPISAAPVEDAFAVARRLPSESVISVGYMLRYLKTVQKAKEIIKEKNLKVVSTVAKYNSAYIHNSKKFWWIMSESGGPVVEQGTHFCDLSRYFGGDVEIDSIKVNRVEWDDPSGKLNAMPVDEKTIPPEERIPRFTAASWKYKDGGVGAFTHNITLQGAKYDTCIEVQADGYYLRIVDLYEEPVLYVRSPDSDEEKVYKYPNDDPYYSEFKIFLDAAEGKGDKNLIHSDFLDAVKTYELTKAITEAK O14087 RIM1_SCHPO TRANSIT 1..22; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC2F3.04c; CHAIN 23..150; /note="Single-stranded DNA-binding protein rim1, mitochondrial"; /id="PRO_0000223929" MLFLKSSRAFSKRLFSSSTVRYRDIQRLTLTGNLTKDVERLQSQKGNEYMRYTVASNNGKDVAPTFHSVYVFDSYNFDRLQTILRKGTRVYVEADAVWRSVPAGNEGSQAKMSLRHVSADVLFYPRNKNGDESGEETHPELDADPMINSF O14097 YERE_SCHPO SPAC2F3.14c; CHAIN 1..331; /note="WW domain-containing protein C2F3.14c"; /id="PRO_0000316542" MSSSKDCKATSNVDQTIPASNVNSGDFISSNTSSSNSENSNIQGKHYTQVGEDADNSFISENTPKNTFESTQTYENLESISKNEPTSEASKPLLNELVPEEPLPREPPLPNEPVPEEPLPGEPPLPDEPVPEEPLPGEPPLPNEPVPETNCHKESPLSDETVSETSKNDTSNSPTNENQAQPSIAWSEGHRIAAIWDPSQQAYYFWDTLTNTTSWNNPLEDEEQTSPLDYTAKVQFNRLSGKFMPKWASPELRSEENKAHKHMEQYFDINSSLNSHNGQSLLAERRNKRYTRKEMEQMKRRTKEKKEMKRRALYDIASDEKDFRRRKIIRY O14099 YERG_SCHPO BINDING 142; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 144; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 153; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 156; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 162; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 165; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 166; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 172; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 184; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 187; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 197; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 200; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 209; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 212; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 225; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 226; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 229; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 232; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="4"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 244; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 245; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 248; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 251; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="5"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 260; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"; BINDING 262; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="6"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" SPAC2F3.16; CHAIN 1..425; /note="Uncharacterized RING finger protein C2F3.16"; /id="PRO_0000310483" MSLSEYLREFAEIFEEAAQELTSIFELPPDLLKDITEEDVGTDDSCNKKFLEVQKQKEDEEDEEILKGVDLTQQDSVREKIHEIQSMSQLSEKRKALLMQKMLMSGYLKYRRTHKKESDENQLSSSDLEKTYYDKEQEILGCSHYMRNCKVQCFDCHEWYTCRHCHNDACDHVLERPAVENMLCMICSKVQPAAQYCKYCKNCMGRYYCNKCKLWDDDPNKSSYHCDDCGICRIGRGLGDDYFHCKTCGLCLPISVFNTHRCIERSTDCNCPICGEYMFNSRERVIFLSCSHPLHQRCHEEYIRTNYRCPTCYKTIINVNSLFRILDMEIERQPMPYPYNTWISTIRCNDCNSRCDTKYHFLGHKCNSCHSYNTCISSIYKPLDHPQVSIPRLATAEDAGMRRLMGHSWDNSDEDFNIFGIHSFI O14106 RGG8_SCHPO SPAC31G5.06; CHAIN 1..234; /note="Protein rgg8"; /id="PRO_0000116720" MTIKKIISKNDPLISILSSPLRQDLATHFLFPRELLAKFPARKDTNPRKFCLLPLEGKNHLHNKHVSLYCLLSDRYLQPPSKRIFKRWNMELNNLNCPDIKRYILESLQDSLLKEISSLKETSTQNHLHCNDIKILQDCLRRPNISNGGIWVQWNLEEINQLKKFLSFRKLYPRQSFISLLQILPEPFLKSQLSHTLPVGSKYFFVPCDKKHHTLGLLLWKLFFLKDMPAAYSS O14108 ETA2_SCHPO MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC31G5.10; CHAIN 1..569; /note="DNA-binding protein eta2"; /id="PRO_0000197087" MMLAIDMTINENQGTRSNLESPTLSCSSKGAMQERDVMFTDHNTFNITNNKSRPGSLMKSMKRKDVYEFDEDNEFEFEMGSLIHKPSRAHSLGGTSEPVSDDHKDCMEATRQLLENSPLSSVVVKTCSDHASKRKIARSSSDDSESKVESTNSFNAKKRKDAWTEEHEKWFQARIDELLTIRSISREQMIEILEDEHAGSRLQGFLESVASFLNRKENSLLKYMRAFFQVAGYEKIDIGSLAAEEDSQLNFSLEDAQVIQKVVLSYCNNEGVDLQEFGFRMSSSSLRHTNINFLYNELRELLPTSISRKGIIRYLKEIYKPLDPKDRNAWEESELKKLYTLVEQEGTRWNSIANKLGTSPAACMSQWRFVVGTSTQETIDRRKLWTNEEEAKLLDLVKSSYRSSFHTKKMTSLFTHNNHTTSNIQREIPASDSIAWHSISKKLGTKSPESCRKQYEKTIASYSSNQRQEEDQGKKRKKRKKKKSKGKRKFYVADSLKLLEHVQRQCGEAISINAIDWKGIVKQMPKWSEEELRAQATNLVASVRGWKKTRLSESVRIAITDLKSLPPDV O14116 YKX1_SCHPO SPAC328.01c; CHAIN 1..1234; /note="Uncharacterized protein C328.01c"; /id="PRO_0000116834" MDEKGLSNILQALNVVHSPESSRETRFSAQQLLDELKDSYSSPSVAIQLLELNEQAFSSLGCKLDIHIVQHFSLSLFETSVGMNWKSFSNKEKESVTSFLCKISLEDNNLLSVHFVRSKLASVFIEIAKRDWYNTWREEFDSFLQSLWSLSLQHRQLSSLILRGIMEDLYQYDDPVASLRSHILFNALISILSSSSTLHKLYPSGLPYSVTIPSNNEGWLIRWGNALESQDDALECLKCFKSCLSWVATDSIREANIVSHICQILVQGPIFLKTHAIDCIYICVTRTMEIDDPLWEIVEEMLSPSSLYTLHQVYTATSESINIKTLSSTTPEYILLKKLSETIVALGQYNYLDSNRRKCIKLTSLDTYSLLVLEIMKHPSLLISAISQHFWVLALRDPIISKHEKFQIVYPELLSIASERLLRFEDAVVELIPESATAKYLQEDVEGVSAVHSFCGNFRRFMFDIVRLTVSITPIESLNWIQNRFQSTVLGNMEDIQSQTEFFSKTSPLYLTMDVGFSTIEAFLHGVTRWNENTSDDPATYEIILQNLFLWCKQLVEINFKDPMLITRLISVLVLFTSILARENTTLLGVVLEKIISAVTYDNTSASYGFSDVQKINEMRSRCCFELVRLGELMPNPLMNIFDQLQSIIDQLDNATTLTGSEIVMLKTFLFVITQFSDVNIEVKNEYFEKLVGPVVKTWLDVQPPVNSPMEFLNHIGFPQMAEYLSAKYPYNADYTQFELDADAASYQSNLETGRKWLWPIKCLGRFCEATCSNKHIHPSEFEGQKNLWQVILPNVVPNLLKLVEQLHCCYEPSFISGLGMHNSSILQKSIVERFWLHGVSQISKNQFLEESYKMDVSANKLIHSFGHFLRRLREYCYYAIASFMRLGQAFFCVPGLSKQFLTAFFSHAAGLSLHQWTSMVNVVIKPYCVNCPAELRDECLLPLLPALLSELDHKLVSEWRRINDRGLLVEEDAEETGEDDDLSEEMIEESLLRHLTYATAKLITETFLQITPTQSRSNVSSSLIGKETVEGPVKLSEYVLDNAIICEPLLCTLCHLLVIHDSRTVGLVVNAFLAITPLLVSEQAHSLVREFICQQVFQSVILAIHDPYFESMQSDFIRLACIILSYSQGITDSAFQLLASIPALANQENLVPAFFNKFREASTLKIQKALLTRLLNSGRIVPRTDRRAVNAAILDVSAKEMLKRFEKSVSLQDEQKNDVLSRDEDTGLANLFE O14118 EFM3_SCHPO BINDING 125; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 150..152; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 171; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 198; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867"; BINDING 212; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250|UniProtKB:Q9H867" SPAC3A11.03; CHAIN 1..289; /note="Protein-lysine N-methyltransferase efm3"; /id="PRO_0000372361" MHGAPEFLTKVKQQYLQQVDLYRFQWVSKPTDWPILFNDYAQVFLSEIVTPSAYTRAFLKSYFRFLDSIDSGHNERNEALLYTYIESLSSTYIPPVQYSLGEYDILIRESRHVLLREGTTGARTWEAGMALAEYIYQHPVQSGMRVLELGAGTGLVSILCAKMGSIVLATDGDTKVCDGVRENARLNNCDINVKKLLWGVDPPEFSDIVFASDVTYDCDLRCLATTLTQIITINPNCKIILSASLRRQETFFNFLKLIQNLYARQLEVWDSPKILYYDSPPIVFYEVSK O14119 BSCLH_SCHPO SPAC3A11.04; CHAIN 1..249; /note="Seipin homolog"; /id="PRO_0000341580" MGYLVKLFKLVVWMLVIGLFSIPSLVSYVIFYDTVIPHSVIQYPVYFNYTTGLNFPTAEVRLDHFSIDPRLPGTSLLQIKMPHSPRNSAMGNFMVSVDFQDRNQRSLKQVKRTVLLPHRSPIHEYLKLIVCSPLYFMGILEETDIVNVRLFESETFAKSFNSITTLSVRFSVKNTPAQAIVKIYSKDIEFYEATLAFASKLHGMRWFMYTHKVSAFLVFTSLFWFTGITSTIITYLIVSSTSETKATRR O14125 YEZB_SCHPO ACT_SITE 52; /note="Proton donor"; /evidence="ECO:0000250" SPAC3A11.11c; CHAIN 1..334; /note="Uncharacterized oxidoreductase C3A11.11c"; /id="PRO_0000310311" MPYINNFLVGPIGLGLKSLTWTENPVPDEEAFRIMNYALSHGCSFWDAGEFYGLSEPLANLQLLSRYFQKFPDSIDKVFLSVKGAFDPETHRVHGTRECITKSIKTVRETLKKVKTIDLYQCAAIDPDTPIEETMACLKEFVDSGDIRCIGLCEPSVEEIKRAHSVVRIAAIEVHYSMLFREIEYNGVKKLCHDLSIPLVAHSPLAHGLLTGRVTTMADIENLKKHHQCNEQPPSSTFSSTLPCIQALKELASKYDMSLAELALSFILSAGRGRILPIPSATSYDLIEASLGSFSKVLDTYQFAEVVSCLEKTLPPPASPNSEPQVTGGCSSMC O14127 YF51_SCHPO SPAC3C7.01c; CHAIN 1..611; /note="Uncharacterized protein C3C7.01c"; /id="PRO_0000116734" MNQDVRVFPDSIYLSCSKKKASLRIDRVDGCLSLSNSLDLSKTPDYNNVQLYGFIRLKIYKYVVLVTSCDLHAAILGNNIYRARKFAIFPITRTLPFSTGLLNIKDEEELHYISLLNKHLSKGQILFSPTLDLTCSLQRLRVLTQSFELTSKYNYRFFWNKYAFHELIELTNKDLGFQEWIQPMIQGNIAITNSFLKTYNLRLCVITRHSPDYAGTRYFTRGVNAQGSAANFNEIEQIIMIESPITLEEQMVLSFTQIRGSIPMFWAEVNDLHYRPLLSLQPLDYSETVFGKHFQELANDYGDNLVVVNLLDQKGREAPLRSGFEKLCKRNKNPPLSYVYYDYHKQGSRNLPLFLAEIQSLLIEGKYYAEHGSKTTAMQTNFVRTNCMDCLDRTNVIQTSIAQFILNMQLHDIGVLSSSESLEEYDSFLQDFRLIWANTGDYISDLYTGTPALKGDVTRHGTRTIFGAFKDLLNCFRRYILNNFFDGMLQDSYDLGLGVFRPYDSLSIPDLPLRFHWTRFVAPGIFLFTTIILTIQELFGNPSLFCRLLYSIPMVNAGIYLYFHRRQYVNWPRLVLPTYAKGGWFSFRNHFRNITLKVFRFLRSGSFKKSV O14128 PIL2_SCHPO PTM: Phosphorylated by ksg1 and ppk21. Phosphorylation is regulated by sphingolipid long chain bases (LCBs) (By similarity). {ECO:0000250|UniProtKB:P53252, ECO:0000305}. MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P53252" SPAC3C7.02c; CHAIN 1..383; /note="Probable sphingolipid long chain base-responsive protein pil2"; /id="PRO_0000308181" MGTQPSYSIHTLRAPPKAKQNQIPPSTTRRAVNVNKLGRQFRYPSVGMFTPEMAKRLAALVKMEKDLLRSYENVAMERKECANQLSYWGEDCDDDISDISDKLGVLLYEIGELEEHMVDRYDQYRVSLKTIRDIEASVQPTRVKKEKLLNSIYDVRSRDPESPKLITMEQELVREEAACLVAEAQLTNITRENFKRAFTLHIGTLLEHSEKVAILCGYAKKILDLLDDTPIVPGEPRPIYDGYNITRDYIVEAERELANWQNPFQTPEPLTDIDGLPSQSHYQTQFQASVVPRTDVINEPPRRYSHANGVTTSGTTHSYTSTGSKRYSQMGTEDYQPSFQPNILQSTQVVDNFEIGEEDDEEVGSQGVAETSMPSTSAQPIAA O14130 YF54_SCHPO SPAC3C7.04; CHAIN 1..783; /note="Uncharacterized transcriptional regulatory protein C3C7.04"; /id="PRO_0000310380" MSHEFSPENTAVLFEAMKQEQHNRRRRVPMERRRRVVLACFNCKARKVRCDGANPCKACASNNLECTYPVKDEKEMDYSKDYFIDLSKRYKCLEYIVERLCSTKVSTYTTPSLIEVCNRISNQKSLLSSDVFSLNSESTNSQRDVDTLTQGALVCSQIQQDPTVVAEDTNNGINADASDQSVDEIMKLIGKIKVDSNGESRYIGASAGEAFVDSVQSELLVDPSFSELSAYSHTHHSYPPNEHDVNAVQKALSLLPPPEVSDFLIKSFYGHVQANFFFFHETLLRYRLNLIMSFQNPSVDPGFLCLLMMIFALGSMFAHMEIRSASNPFDNPGKQFFDTARLLLPQVIQQCKPSLVQASILMGLYLQSTLSQKSSYTYFGLSLSAAVANGLHRSCENPNIDPKTKELRNRLWWSVYTMDRLISIATGRPLSIADSECDAALPTVVPELEIEGSASNVHNIISMSKIAKIMGKTMEQLYGTVNYKKNPINIIESLRADLEEWKRSLPPFQILENLDAEDPLFRANVHLHMTYDQAIIIMSRPVLLHKMKNAKNSPRVDRINEDCILAARHLISLVHLLQNHSQLSCYSFFDYNYTFSSALVVLLHCVTEPCEEDDIAMQYAYSALDYMAEGNEAAKNCARVIRLFDAHLKGARSDGNGNTSQSGFMAWQRWIAEVSAKDEPEKLMSPYNKSIGGGRNSNSLTPNANLGADVSFFPTDDTSFLLDHSKLDDDLEKFASTLDPIKTTPDLANDSSLLNWANTDQGMDIEGSWLGNMHPTWLDYVCP O14135 SET8_SCHPO SPAC3C7.09; CHAIN 1..429; /note="SET domain-containing protein 8"; /id="PRO_0000303896" MDIKYNELVNQFAPGAKQITIKKIRKKGNGIFSLNRYTSGTVLLEVPLENIICRKTVEQFRNSCDKFASIATLEEWNDMSFRTQAMLFLCYLWLGIQPRTNKWDKFLTVLPLSINTPAQWPEKEVYSLQGTSIFNPVCVKRKILQQEWLSLNQRYSDSWPSKITLPKWVHADALFHSRCLESPFKDPVLAPVIDLCNHSSKSNAKWSFSEDAMQLYLDKDIDENEEVTINYGSEKGSAEFLFSYGFLPEPEGDRITNVMKLLIPEDSNDSLDLAKRRSCKTPPMIEFVSDSSGELWWHAPFLFFSVLNVEDFTNFKMVCDESKAQTVDWEFEGQKCSVEDLPKLVQLSPKRDLYILRVFCLAEQLADAALNTNIENMYNPTERRSESVELLKRESFLLKKVLLYLRDVISKLLKSKVVVEFIHSQTIES O14138 NDUF7_SCHPO CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320; Evidence={ECO:0000250|UniProtKB:Q7L592}; SPAC25A8.03c; CHAIN 1..467; /note="Protein arginine methyltransferase NDUFAF7 homolog, mitochondrial"; /id="PRO_0000116736" MLNLYMWKLSRSQVYQASLLFGSRVISALAFTNTGLVLHGPRRWYTTDNGFLLHRDSKVSLADYIHESTFDPSKGYYSRLWTGSTNNLSHSVHVLRKEGHKCSKEFDPFLHGIPIPQKALNIYEKQRSLFSESISNYLVLQYKLRYFPVFDLKIYDFHSGTGIIALDILDYLYKNHLEVYGRTTYNIVLHNSWQASWFKSMLTSVRYAKHGDHIDIYVSDPLTWNHTDTNPCFVLALQVISSFGHDLFRQSNGAMMMERCWLGPEHFLNEFFTLNTHQKVSSLNYHLAFQQARINVQQGFSDSRAKRYFSGVKQVFWSFFSTQKLTYYPTKAIRFFERLSKQFPHHSLLLMDVCHVDKSLPGINAPSVLSMENDFSTKKMSSNIGHVFQNETVKYVFPTPLYLVSDILQLATHNRSFICSLPHFLRRWSNEHGRKFFVPVEPSSKNLKVPYSFNNYYVVSSMPTYYY O14142 SYM1_SCHPO SPAC3G6.05; CHAIN 1..206; /note="Protein sym1"; /id="PRO_0000317316" MFSRFATRYNALFEKAPIMTMCLTAGTLGGISDAVAQGLTIYQTNKNAMIGLDGVRLNTHPEIPSIKRVLQFVTFGFAISPFQFRWLRLLSAKFPIEKGAINVVKRVLLDQAVFAPFGTAFFFSWMTLAEGKGFRGAYDKLQAVFWPTLKANYMVWPFFQTVNFWLMPLQYQMPFACTVAIFWNIFLSLKNASSMQESGSQEIELF O14158 YE76_SCHPO SPAC4A8.06c; CHAIN 1..578; /note="AB hydrolase superfamily protein C4A8.06c"; /id="PRO_0000363392" MLKKEQLTVESINDGISKTFSQAFRFLAHHELRKNRTFMLDLGVSILKKFLIDSRDYKVEVVQDFCSRSLTDEFKFKFTSQPIDSKSESDSASYIRNYLGPEGIKQFGGSNWWLYRKSPLKSWWIERRHHIRHNLKCDKVIFYVHGGAHYLSTVRTNAYHIQRHTAALGARTFAPDLRLAPQFPFPCSLHDVLSSYLYLLKSTKPENIIFMGDSSGAGLIVASLVLIRDSKLPLPAGVVYDSPWVDLTHSLPSVVADDAADYIPSEGFHHRASRYWPITNLDSFSTISEKELLNYSKKQELTNFIENSIRKKIQTIKNLIPVLQEMDKEHARIDFDNVDSRLDPNILTTFPFQVQFYTSNANLKHPLISPIFTENLGGLPPSLVLGGSGERLRDEIVYIAHKMNTDVYNGKRTKVRLEMYDDCCHVVTALPFVKEAGIMVRRAANFAYWCLKQHDSSFVSPNKHLDGNPSHANEDMVRLRISRNGEERLMEPKDEIQCLNLPKSALGTIQVKALIRWIDVELILLSKDTKKPARYFAEFKHADLNGYLVKPKEYTMEGENPPLSALVANCKISPEKKQ O14162 YE7A_SCHPO ACT_SITE 390; /note="Charge relay system"; /evidence="ECO:0000250" SPAC4A8.10; CHAIN 1..785; /note="Putative lipase C4A8.10"; /id="PRO_0000116704" MNVYVQRDDVGLGQIHRFRIFVQSGGNLHSATSSTTVPPTVNLNSVTKKESGSIEDRAGSGGMTISSGENISKQISENNSSTNPKHANSESSPLLSSDFSSSSKDYHKVGAFTDNTNAINIPEQTRGVSHTSSSPSVGTSFSSINLREVKNPLAGSDSTAPFINSTNSVLWIRVRNREARFRQAAYLQGPFTLCVSVWNDQFFDEKNSLLNFDPQVQPSTSFWVCVPYSCFSNQQPIYIEIASQAIFKDRSINFELAISQSQHSIRAMSAADIDTLHAFPALHVEHQTPENLWRLPYSSFHSKNSHLVVLTHGMHSNVGADMEYLKEKLIESSKSVKELVVVRGFTGNYCQTEKGVRWLGKRLGEWLLDITGWGSASFPRYSHISVVAHSLGGLVQTYAVGYVHAKTHGAFFQAIHPVFFVTLATPWLGVAGEHPSYIGKALSYGIIGKTGQDLSLTPLNHSIESRPFLVLMSDPSTPFFQAVSFFEKRILFANTTNDYIVPFGTSAMEVSSLGKVEEAEGSDKVMPTHMENGISPTLKENEQTVQSVGDNAKKIHASSEESGSSFSKALKSFVGLFSYSASKTTDTEIPLVKNEDENARKPTEPNCLGSDELDVSNSSNQFFCSAPKLDPTSTFSGVAQRVVNTFTNLFIPAVPTDSYFFKYHLHKVVVSDNVHDPAASFSTFDGITELNNMNNGFLSNEITIAKNWHRLAWRKVAVRLDGDAHNTMIVRRRFPNAYGWTVIKHLTEILFEQNTSTAYMNPISFDETTTAAWLSEIYEDNSISV O14165 YDX1_SCHPO SPAC4C5.01; CHAIN 1..249; /note="Uncharacterized protein C4C5.01"; /id="PRO_0000108070" MAAKHVKYMACLFDMDGLLVDSETIYTKTTNLILDRYGKDPLPISVKAQMMGRPGSAAAKVVIDWSNIPMTPQQFVDEQQVIRAKFWSSLKPMPGAESLINNLSNHGIDIGLATSSNTANYNMKTAHLKHIFEKFGKNVITGDNPSIAPGRGKPFPDIWLKVLNLINESRKQRGLKALTPSQCIAFEDSIPGVKSAKAAGMHVIWVPDAAIKNLVGDQLNEIVDSQCETLPSLSEFDINKYLNINSKQA O14173 YE57_SCHPO SPAC4D7.07c; CHAIN 1..601; /note="Uncharacterized protein C4D7.07c"; /id="PRO_0000116699" MMSRKRQASSNDFFDMEQLLIANDALVHQNHSTPNHASDELSVNDPSPLSRGLQSDVNSNISRNISNTFFKKSIFFFVYYCKQALEFISTVFSIIKFLLNRRKVSFLLSFLLLFSLFLLIPNDGRVNIKFFYKDFVDRIPFRFIPSNFNISFGKHLEQAKSLFKSKFGNSSSTYNERDSIMPLLKLQSNLTEAKTLLYQNPISPEDVLLHFWDRNLMSTYDLKIQDINDSVNPLLNTYLDFIEKDIYLVSHLPVSEKHPGNIPISLVNKSVQAICSFAEHYNLLRNPSYRGFLRINNGESIFNLLCIEDLHESVNLDILCLKDILRNIAQSSKEAMYIVKRHNSSQSFYGNRSTTNFSIINSGLYLKKDAAKNLLAKQFDATYSYYHKDLEESVHQKLNSNLEKRVEKYIKHSCSQRNVADHPDFALKVVGAVVDYGWTFPKPKFSDILRDYWGKKANLPTALLDTSINSNWCNYEDTVQVSVRLNRPMYVRHISLIFPIHGDDSYFPREIQMFGLINDINYQILSNMNNLVLLATIPVSLSSVFEVNYYYLPKFSDTPGLLEEAYFNTFVFRAFSKNESLTSQICLYHIGIHGKEINEEF O14181 RM28_SCHPO TRANSIT 1..35; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC4F8.05c; CHAIN 36..118; /note="Large ribosomal subunit protein mL40"; /id="PRO_0000087691" MAKASKGKHQSGPSNHSESIDLVRKALYGNKKVRSLKMNPDMWEKHEVINRAWRIHEYRQEKQRENLLKNQFSAMKIACEELKHTSETLYKAAMSDSINRRFPVETRTPTDTPPRLSK O14183 MU114_SCHPO SPAC4F8.08; CHAIN 1..151; /note="Meiotically up-regulated gene 114 protein"; /id="PRO_0000116660" MDNKKGGLFKIAKKLRNGTKVWARAGYFKCKLLKITTTGAPCLFAGRLKRRYDATFQSMVEIFRQEIANDVTCGRVETALLYFVNKFFRSVGCFGKGKEREVKTDRQRDTGSGEQRIRLERDTETLYQSQLRINQVNGWMSGWMQISLILQ O14186 YDSB_SCHPO SPAC4F8.11; CHAIN 1..846; /note="Uncharacterized WD repeat-containing protein C4F8.11"; /id="PRO_0000051494" MPSRNSNVLQRPTYAQLASTSVKSSKGLVSYQDWVVDVKASISAISVNKSRTKVGVAGRELLKVLAVNPNSSKPPVCISDLLQKSTQTKHISCNDVKWGSSFASNLIFTCSPLGNLNVWDVNLEALLYDFNEHSRAVHKLDISSFHPSYVLTASQDGLIKLWDYKESSSTITFRGNSEAARDVVFSPSEPNEFVAAYDSGILQKWDIRFPKLPFLKLAAHNGVVLCVNYSPNGVFLASCGRDKTIRIWDSTSNKKKSLITINNVSPLNCVRWRPANQQSRGSNQLASSSLVGDTAINVWDITRPYIPYRTVSCHDSIVSTMHWASTELLWSCSKDGIFSQTRVENAFNCIDMLPRATSSWSTKNSLVFSSNPISNQRLSSLNRVASFESNISSLKSALYASQNSDGSTSNPVPFVPHNFVGIPQELGILAYRSEDVAQFCYLAKNYRISGDISSACKENAFFARNVGAEFAYQIWDALYFSLGVLNNSDKGISELINIPFVSANNSMADDEKGRNLKNLTQISTSSTPAHDNLSLNDFFEPREASTPSESSNSSIESEDNLDKAVLNKQSQWHDLENPIVLKKGQAPVNNFSTDSRASINSSYLLDSAASNYSGTSHNEMFNSFHRSSVTSASIKSREAVLSAGNSSRRASIFLDQLSLHGDTDSEIPIDDLPPIELPYVVTSIISDCISRGDVQTAACVCSVFSYLTIDLPRIQLDDLLESYVDLLRRFGMFSEATLLINMSGSKNLKYIHSSSRDLIFEMENKKATGNEQSEKGKENAKTVTSLKKCVYCELPLRGVLVYPPVCGHIGHESCLRSWYFDNTDDALPVCPVPGCGVKLLDKRALI O14195 YF07_SCHPO SPAC56E4.07; CHAIN 1..235; /note="Uncharacterized N-acetyltransferase C56E4.07"; /id="PRO_0000310296" MVKTVNGEPLRHRPLQFNDIERVTEVSLLAFSDSATWKWRFKGMSSETMKALTMQLTRDAYFDPHVTCIVAYTDSNPYVGFLAFKKFPPDPNVSYRDWILKSLNKYYSNFLYWWYGAQIVQKRFHYNELQYGAALYKTGLLKNPKGFIHIHFVCVDPALQGNGVGGYLLDMAHDLADEYQIPCFLMASKMAFKMYEHLGYKTSVIANLVDEDTGELIRESPGMIREPKQPSSHET O14197 YDQ4_SCHPO SPAC5D6.04; CHAIN 1..452; /note="Uncharacterized transporter C5D6.04"; /id="PRO_0000123808" MGFFSSLGQINVWSLLRPIIESDLEVIVIALGGYVLAKKGFLPRDAQKVISSLNVYFFTPCLVFEKVGNGLNLKMLIDLSLLPVFYVIISAASILISFLLAKLFRLTPRQRNFATACITFQNSNSLPLALVSSLATTVKDLLWDKIPDDTPDKVASRGIMYLLIFSQLGQALRWSYGYRILLSPNQPEDPLPIGNRSWSHSDVNEEEIQNLLASSANVDGVQNSVQANEGSTVQTDSSAISKNDNVQVETSNEEVGGFGAASSKISKFIVLLLDFFSPPLYSLFIALFIAVVPPLQRFFFEEGSFVEGSITSGIRMAGQVAVPMILVVLGASLATDISKTEPTQEVRKNNDTRVIIVCLLGRMVVVPLALLPAFSLLSYFSEISTVDDPVFVVVIFLLVGSPTAIQLTQICQLNGVFERECAKVLWWSYAVFTPPNSLLLAFASLLVVKWTK O14199 ALG14_SCHPO SPAC5D6.06c; CHAIN 1..210; /note="UDP-N-acetylglucosamine transferase subunit alg14"; /id="PRO_0000123816" MNTYVLTAIAVLASLIILLVGRNAIKSSKKKPFQKHLLVFFGSGGHTGEMLNLLNALDDKLYSVRSYVAGSDDTMSVSKASLLSNSLPSVKSKIFKVPRARYVKQSWLTTPFTAFWSLLGSISVIFWNPFGIPDVILCNGPGTCVFICLLGYLAKFLGKNVKIVYVESFARVKSLSLSGKILMPFVDRFLVQWPDLATKYKRAEYIGIVA O14202 MU116_SCHPO SPAC5D6.10c; CHAIN 1..135; /note="Meiotically up-regulated gene 116 protein"; /id="PRO_0000116655" MVSRVESVIVFALYKFLQRYFHSFHCFFLLCFTVMLCVVQQCSSAMTSFRCPTFSLSKYTCVLPASIPEMILFTFSSHTFQTPTKKGNKTKKKRKKEKKKETIVEKNKVLKSFALYKKINNYRSTRCVLVCQCKY O14204 YDQC_SCHPO SPAC5D6.12; CHAIN 1..314; /note="Uncharacterized protein C5D6.12"; /id="PRO_0000116656" MRVCRTLKISIKSFPSSLSLLSLYKRRLHKSTSHSSTATSSHYSKNNLPSDSPDLLFDYFIDGHKIHVNPNAVEPLHLRRNADVVGFSLPHGVKQSFENYIQKYPLSDQVENSSNIYDPSSPPDSPRKQQTHLGTIPPEHPDVFFHNLKKKLDSLHTHSSPLTVYRNHLLTCETDSALAQLFKSEIYQQLSDFRRDFPLSHALRDTMLIARLNFLNPMLALSFFQAVKKHSPNAYVRGCSAPVYNQAILSVWQGCKDPNFVLHLLGEMRENVVMRDSETREAINIVYKDVNEWPKQLLFSQNRILEKLKIFLLP O14206 YDD3_SCHPO MOD_RES 377; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1B9.03c; CHAIN 1..389; /note="Brix domain-containing protein C1B9.03c"; /id="PRO_0000120262" MGGIGKKRVKKRTHLKADPIQEAAIPKSMVIRSGASEVGRSLSLLTRDLRHMMEPHTAIRLKERKANKIKDYLTMAGPLGVTHLLVLSRTDNNANLRIIRAPRGPSLHFRIHEYMLNKDVRRLQKNPKSPTTEFLTPPLLVMNHFNQNSSKDSPHEALLTTTFQNMFPPISVQHTNINSVKRVLLLNRRDDGYIDLRHFIISTKPVGISRPIRHLLKGEKKDSDIPDLHNVRDISDYVLHGDGISGAASDSEIEEDATVEIDRPVPTKTEENLLSASQLLKPKQQAIKLIEIGPRMTLELIKITEDAMGGKVLYHSHVHKSKEEIKQQDNFHEQSRALKEKRKKEQDENVRRKRENKKRRKDQKKEGITSSNKNDDSGNEGSSAYSDTE O14209 YDT4_SCHPO COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305}; MOD_RES 249; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC6B12.04c; CHAIN 1..421; /note="Uncharacterized aminotransferase C6B12.04c"; /id="PRO_0000123931" MAFRGIRPSNKVAASRPDVWTLVNQATAECKVPPVSLSQGFFNYNPPKFVLDAAKKSIDEVACNQYSHTRGRPSLRKALSEAYSPYFKRTLNPDTEIVVTAGANEGFFSVFAAFLNPGDEVIVMEPFFDQYISNITMNGGVPVYVPIIPPEEGSVKPVSAGAWKLDMNKLRNAITEKTKMIVINTPHNPLGKIFSEEELNEIADLVLKHNLLVVSDEVYDRLSFVPFVRLATLRPELFKHVVTVGSGGKTFGCTGWRVGWLIGDESLIKYSAAAHTRICFAVNSPCQEALAIAFGEAEKHNYYEEYKSSYKKRFEILAKAFDQLEIPYTIPDGSYYTMANFSKLKLPKDYPFPEEIANRPRDFKLCYWILKEIGVATIPPTEFYTDEDAPVAENYLRFAFCKTFETLEEAARRLQKLKDYF O14211 RRG9_SCHPO TRANSIT 1..46; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC6B12.06c; CHAIN 47..117; /note="Required for respiratory growth protein 9, mitochondrial"; /id="PRO_0000116665" MNIFNYTTLIFRRLSSTFKASNKASIEWKKQNIAVKRKIGGYWNPKKKLPLESMDEIRRLKKEKSSMSCSELAKLYGVSPESIRRILKSSNRPLDDREKSRKEKRWLNSLKSNRDFA O14218 YPI1_SCHPO SPAC6B12.13; CHAIN 1..104; /note="Type 1 phosphatases regulator ypi1"; /id="PRO_0000116667" MELTRPLGDISSSATVTIESTEESASISHEESENVLHLQPEPVRRVRWTVSTVDNEHMNKKKSKVCCIFHKQRKFDESSSDSDSDSDSDSSCSSCCSRNAYERA O14223 TVP15_SCHPO SPAC6F12.04; CHAIN 1..132; /note="Golgi apparatus membrane protein tvp15"; /id="PRO_0000339145" MDKTKMFSAINLGVGGIFVLSGFIKLFSFSFVNALLALFIIVFGLGTIGLEKEIPPIAIKYGSFMFSFLGRGFFYAFMGTLLFSYSGFTSFLGFLVLLAGIAYCGANYVAGLQDYAPRSMRDNDWDDNVDEV O14235 POF5_SCHPO SPAC6F6.02c; CHAIN 1..348; /note="Protein pof5"; /id="PRO_0000058506" MQSFPPEIWHHIFDHLISFDKFEAKNFGGLLRICRSSYVGGLHAIYYFPKLNPRNYHKFVDTISRKPTRKLVHHISLNNVSYASKASITSRLLRRCATNLETFSGPQSGLGFTALRAFSQCQKLKKIDLSILSEKIDLQYLFGGIQHLKHLEYIILPYLSIPAPMCTECWPSSLTFVGFSGGLTDDFLAESVFPPSLKSINITQCPLLTDAGIFSLLSKIGPNLSSVCVQYPMPELSRSGLDCIFQLCPNATTISIPANYITSTAFESIPESGHNVRSLEITYSGSLLTNISLIKADDLVGALVDGKLPNLHRLQWSIRLGWREESQDVQDLLELIDDQDGEVFITVK O14237 YEL4_SCHPO SPAC6F6.04c; CHAIN 1..489; /note="Uncharacterized membrane protein C6F6.04c"; /id="PRO_0000372359" MVALVNNMRKITIPSVGGKLVSSGQFQNFIASCILFCCPGIYLAVTGLGAGGGHPDAYHMADVTNSLLYALFTVCGWAGGPILKYLGPRWALALGATGYPIYIGGLWYFDNTGKQGFTIFTGAYEGIAAGLLWASTAYISLSYSCANQKSQFIATQWTILAFGSTVGSFIAFGINYHSTSTGVPMAVYIIFIIIMACAVLLAILFIKSPSDVRKSDGTSALSPSNKTFGQELWGLFEAAKDWRLLCLLPASFASQSTIAWQSHLNSYYFSLRTRSLNNVLFWVIQFFVPYLFTLILDAKALKRRTRGIIGLTIQAVVIMATLSGELGWIVSKHIDLHDTSPDLDWTQRGYGGALVLYLLMGIQYGSSIVSVQWCISLLSSDPDKYARYAGLYKGTQAAGMCVSFGIDAAGVSFLGQGIIYFIFLFVMCASQLIMTSIFGKETDRLSTKEHFTDDKSYIDGVMPSTDTYMNEKTSDELDKKSLPSDQVYV O14244 YELD_SCHPO SPAC6F6.13c; CHAIN 1..778; /note="Uncharacterized membrane protein C6F6.13c"; /id="PRO_0000340087" MPISSPGTRCSSDLKDPTLQQYSAESVSTEQSLGTFEESKGSITENYVQDSSVDEHDDGNWQPMEVISLEPTHLINDIDDDNEIIEEKKETEKVEESELEPRYTRVFRDEDDDQKHQLDSEAIKLLDIADHGNEEISMDSQLEITGNILSETEKMAYAGVCRLLILKMVDKIACFTTLPWYRGECKAALEDTIMWADKTTSCIYEHLGVTVEEQKMIENLHKHSVQIDDLSKILVSAHRAQTVSSLDAVLVDEVESSDSLSSLGKEKPVQIDVRWTVLCDLFLVLISKSLYDCRSRSLLMAVGEVLDINEFDVAKFEKHIVETIQIDDTGELEAGSSANTEAVMKLRRKVSRRKKYILMGLAGIGGGLVIGLSSGLLAPIISAGIGAAFTTVGLSGVATSGFLAGGGSAALITAGGAISGAHIGTTGMAHRKADVKTFEFRPLHAQRRANVIVTVSGWMLSKEDDVRLSFATLDPIVGDIYSVFWEPEMLASAGQTMNILATEVVTQSLQQVLGSTVLVSLMGALQWPLILTKLGYLIDNPWNNSLDRAKATGQLLADMLCYRSLGVRPVTLVGYSLGARVIYYCLRELEKKKEFSIIENVYLFGTPVIFKRTSWLKAASVVSGRFVNGYKKNDWILGYLFRATSGGIGRVAGLRQIDCIPGIENIDVTNLVSGHLAYRESMPILLAAVGFEVLDEEVDLVSEPIPEPLRERQSQLLYEIEAEECQNKQKELIEKSLMQKGRSLSPKKSNAFFDSKKIREELKKVKKKYGSSFNSRWY O14250 PSA6_SCHPO SPAC6G10.04c; CHAIN 1..272; /note="Probable proteasome subunit alpha type-6"; /id="PRO_0000124075" MFRNQYDGDATTWSPQGRLHQVEYALEAIKQGSATVGLVSKTHAVLVALKRNAEELSSYQKKLIRIDDHIGIAIAGLAPDARVLSNYMKQEALSSKTLFTRPIPVRRLMSKVAEKAQINTQEYGRRPYGVGFLVIGYDESGPHLLEFQPSGLVLEYLGTSMGSRSQSARTYIERNLDTFPDSSREELILSALRALRDTLSKDQELTEENVSISVIGKDEKYTLYDQNDTKEWLDKLGDKGPAAARASRAAAEEPQAPTAEAILDSADAMETD O14260 YFP3_SCHPO SPAC7D4.03c; CHAIN 1..886; /note="UPF0592 membrane protein C7D4.03c"; /id="PRO_0000339166" MGDFQSRYEILAAIMGPPNTASFKEEEHSGSQTKNYPVVVKCIQEHDPVDTTNVLVADDLDSNFEPFSITDDYGKYENTLVSHSSTILNEPYNESPSSSSSDSSSRSTSPFSQLSSQSLRLNAEEIAPSSLINKAVQSTLRLSEPLVSPIKCPLSEQFINFINQQDSDKVVLIRGFLLPHLASLTTKNVSEPELDKLRHSLYNWWVSILRRLQSNISTSERITYTKAILAIAKHHCWNKVEHSALLYLEHQLILYDTLTFVVHLLSQKSLPYSLTTFCASILVLSFFQLPLFADHFLSALDVKKKYIDALGSSFDEKIMIISHKYLAPFFTDQFSSTMHPYYPKRTSTPFTIGYNRQPIEFTRAWMRRFKSSTGGFFFEFLSCYHSFLALQFSFELPDNVIYFAPGYICLHAYLLELTISVIHISDKKPLMLPTGHEQFPCKTLPEVNPSMEEYNPKMPVTATTLSTLQQFVGHIKDAFKKIGDCRQEQMRLLAVLEQVLINVAKNTPAFNLQSCFLLCSLVEQCFGVFNDFSHRFDFSFWISVAKRLISTSHNMSIVRSITFIYAVWPYLDIKSKELVTLQWLLEENTFQELFLHWSPLVRAYFQRLVCWRFLKLDDMEEFQFKGTVTLRVKNLLKHYFTAQALYHEECLVNGRASPITKPSEPVPMRRLTIVCNHYQNYGNSESTEFELSNYKQDDGTIQALVTDVVSISNSFSSGLKKAFGSLFKNVSGLPAETEIAYHHTLSASNSYVFTDLVDNPDSMLKSTLKYRFVFKFSPSQPLSSLGKNKEKYDALLERSSHGVLPVQSKMLLYNSNHISCPLSSIKGVSVNGKRLVYTSRALVEWALVVNEFDHALSLRKGNETEDMEAPTLTVRIPKSYASNIYN O14262 YFP5_SCHPO SPAC7D4.05; CHAIN 1..228; /note="Putative uncharacterized hydrolase C7D4.05"; /id="PRO_0000314095" MIPSKNIQKIKLVTFDAFGTILHLSKPVPIVYSEVAQKYGVHATIDEIEHNSNKAFKDFSEKHKNHGKKSGLNPHDWWIKVIEHSFPTPVPAEMAEELWSYFSKKTGYTIHPLLIDFLKRNKEERKYIIGIISNTDERIRTVLEDYGIDHLIDIYAFSYDVGFEKPSREIFDYAMEKAVKLLGQEIQPEECMHLGDDLIKDVSAARNIQWNAEYCDIKTNFLKYFEQK O14264 YFP9_SCHPO SPAC7D4.09c; CHAIN 1..274; /note="Uncharacterized protein C7D4.09c"; /id="PRO_0000317696" MQLLNNWYSLLLTEVAAYFTSTTLFVSILKNAPSLSWLMKYGGHDNFGLKPPLIATKLEVPKRWFWHFYAFISLLNPLFTFFILNTNFPIPIFKNIKEDLMYSKKLQVLLLIYEIHTLRRLYENLRFRKSGSKMLAGHYLLGYLFYTHTFLALLLCGRRSYENTMSSMQFVGLGIYAIGSIWQNASHEHLIAQKNHSQYLVLKKGCFKWITGPHYLGEIIVYTGIALIAQHWLIWLVLGWVLCNMVAISSSYACTVKNKEQSLDFRWTLIPFLY O14266 SEC39_SCHPO SPAC7D4.11c; CHAIN 1..769; /note="Protein transport protein sec39"; /id="PRO_0000234108" MNEDKLESKWLFSLTESQKLYLLISLIINKKLPEAKFVYKLLDYTKGNWLSLLLRFLPETTDPECYIPYIDIDSHYGNIKASVNDIEPIVLPDEELCQLRLTNMKLWNCKLPSLKDEAEFYSLFSKKIVEETDLVDLAYQLTKNSQAPAEIQQWNSGTFTVFHKLSQFAAVPINLEEMEAATIRDVISLAFPVLDSKNCVFIMDEIITVFINNSSNDPNLISENWDFVWKKLLQLVKTDGLAVVHTLVLNWNTIEPKLFLKLAKVALASCYISDDSSLYSVSLARDITEAIQNKLNFSDVNFGDLLKKPHDFSADGLLSLQNDLTTPSSLSTSLLMEITKAIALLTQLKVPAPTFKTSVSISCSNFDSQIKYLENVLLNALGTIQSPDYKDWHDLYSYIERFKQLSLFFLNISEDAISVVFLKQMLQEKSFLALKQMRNEIGLKDIEPKVLIDCLKTSFYENFRAASNMNKNRGKLALACKVLDVFVDCEPTIDLRRRLNSLVNACSLIQPFKLILEPGKPLSPSLVEANLNPDKLIKTIFSQNPSAYTLYDDILALDIELHKAAGDFDYSQVFTELRRITEHMITLTIDVSLEKDDIEYAKQIVEDRLMTLAEASEDVKFFLYEIAYKIGKFPSNHPNAKVIRLDMLQIAIANAPRQKLDEVVSYWTDFQSNSKVLEENLNTTDVEFHSSKKIKDYEDLEDANFDEEWSKAADLMSDDPENQVLYEGNLNSSLSLNEDPSVSDENLTQKVTSKLTNGLGWVLGVPPRK O14267 YFPC_SCHPO SPAC7D4.12c; CHAIN 1..759; /note="Uncharacterized protein C7D4.12c"; /id="PRO_0000372379" MDGNRRVRFNTDRRPYLSPLQTSFPSSTSFQTPTFLIEEDDEDTEDDDGPQVLPVHRAPSPAAFRKRGSITSMDQYLVNMPAVPSPTASKVGLLDARNTDVESYAASYKTQSSSNSVNSLPMRRPTLDRSYSAPMIAAKNLQSDPEKMSNVESTNELPSTTTEAYKLVAAHTAARLEHMRLNALKAANDEGEDVKDNEQDDNIDESDPFANPKASYRGGVLSNLLKLYTNSNTVTSSRISLKHTDPTKWQKHAKRTASSNSLTDLLHASNQTFMAPASGLQSTEEIPQFSKTGHSRGRKFNFHHHSRKNSGLNEEYKITIHLADILQRQKYILKLCRALMVYGAPSHRLEEHMASAAKVLEIEGQFLYIPGCMIVSFGDVNTHTSDMHIVRVNQTIDLGRLKLVHDIYKAVLHDRMGVEEAIRGLDEIFKSPPYFRTWILVVFYGFASATILPMSFQGGWIDLPIAFILGCLVGILQHYIAPRSTMYNSLFEVTGSIITSFLSRAFGSIRYSGGRRFCFSALAEGAIVLILPGYIVLCGSLELQSKNIVAGGVRMFYAIIYSLFLSFGISIGAALYGWMDHNATDSTSCPVSTQMDDKWKILFVPLFTLCLLIVNQARPSQWPVSIFISCAGYVVNYFTAKHFGSNPIANAIGSFAIGCLGNIYSRLGRGVAFAAVLPAIFVQVPSGLAAQGGISSGIEVATSLTNNTYNTSSSSTLDVNSLKFGLVMVQIAIGISVGLFASALVVYPFGKRRSGLFSF O14276 FYV7_SCHPO SPAC8C9.07; CHAIN 1..144; /note="rRNA-processing protein fyv7"; /id="PRO_0000339136" MANHSSSSSDQGTKKKGFKFRQLPEHAYQGKAKRIKQDLILKAKTKKHFYKNVRPEEYIKKGSGERKRKFSKKSHLQELYERSEEKRRIQQEKEDAKVQKRLEIEKKQKDREQTRNMLSKKTKRGQPIMRNQINHLLAKVKQTS O14278 MU129_SCHPO SPAC8C9.09c; CHAIN 1..302; /note="Meiotically up-regulated gene 129 protein"; /id="PRO_0000278625" MLWRILTCCKSPEEDKDEHKKKPPNVGHAHLSVVSPLNELASEKSRSSLCIEWTIDSLRQFVQQLSVRQNMSKDRREALTYFINSYNDLFHDVYYGDGRSMSKTEEAQTIVTFTIGSYLYKYTHPSELFWQRLSDNMANIEDDGTCTEAQLAFRKRAALSKLGHPAFHFLPMNNKESFHYAWSLFTSTYFQKAATVSPSPNQQPVDSVANPQLRKASEITTISSRSDVDILLGKFKALIQESPDEHCNSWIQRIYITCVLPRNHYIYLLNEQVDFLTSIEIMKNQVTEGKLCLLNEDLGTLN O14281 YETC_SCHPO SPAC8C9.12c; CHAIN 1..303; /note="Uncharacterized mitochondrial carrier C8C9.12c"; /id="PRO_0000311179" MTYAAEDFDYEGLPIGSPMYAHLLAGAFSGILEHSVMYPVDAIKTRMQMLNGVSRSVSGNIVNSVIKISSTEGVYSLWRGISSVIMGAGPSHAIYFSVLEFFKSKINASPDRPLASALAGACAITISDAFMTPFDVIKQRMQLPSRKYKSALHCATTVFRNEGLGAFYISYPTCIAMSIPFTAIQVATYDTCMSFLNPNAVYDPTSHIISGGLSGAIASSLTTPLDVVKTLLQTRGSSSIPEVRKCKGSLDVVRFIYNYGGIPSFFKGIRPRMVVAMPATAVSWAAYEAGKEILIRVSKTSQA O14290 YF14_SCHPO SPAC9E9.04; CHAIN 1..188; /note="Uncharacterized protein C9E9.04"; /id="PRO_0000116732" MTIYYMIVFMLLMVEIVSFVILSLPLPLKVRRAILNAISNSPFAGRVKHVLKITIICILILFADSVRRVVRVTKEYDLAIAAPSTTESARSGYKASQFYAQRNLYLCGSALFLSLVVNRYYLALEAMIAAQDKMQALQTQVEASTNNAKAVEELETLRTKLETRDKEYETLAEKYAAVTKTVEKKKDI O14297 YF1F_SCHPO SPAC9E9.15; CHAIN 1..219; /note="Uncharacterized protein C9E9.15"; /id="PRO_0000341601" MLVLFGQPENWHEQDFRAVDDRVRGGSSISHLTEEKDSDGKSRAKFWGTLDTKTLGGAGFCSQATNIKDRTWNLKEFKGIELDIAKSDSYKYTFIIKDCHQDWETSDEKSSLSYEYDFTPIYSKEDQVVSIPFSEFKPTYRGRPVEGAPELDVSKITQFSIMIRSFFNSQSGDYELVLNSIRAIPKNVPFTTHKMSNEKQRLFDDYEKEIAGGSWCICQ O14304 YE88_SCHPO SPAC9G1.08c; CHAIN 1..241; /note="Uncharacterized hydrolase C9G1.08c"; /id="PRO_0000102279" MSSLNSVLPSNACAEIIEGKDKVHNVVILMHGLGDSHKSFANMAKNVPLPNTSYISLRGPYRLPLDFENPGGNWMWGEDVHFDQNGELQSEADFSKSFTMISNLIGNLLSYGILSSRIFFFGFGQGAMVALYSCYKLSTKYQLGGIFSFGGTLPLSITLPNHPFHVPVYLFEKRLHCSCSEYEESRLRKTFKPFHLTCWNRDDKTDMPSSPREWYTFVQSISKHLYIHNTLFEDAIPLTSF O14319 CUE5_SCHPO SPBC16E9.02c; CHAIN 1..569; /note="CUE domain-containing protein 5"; /id="PRO_0000310345" MASEQSNPRLPRRPPYMAEKARATLKEAFPNTDDAIIRAVLAASGYKLEPAFNALLGLSDPQVAEEMEQAETSYAYDTAAHDDPVQRQLEEDERCARELANRYNSHRPERRRKTNNDRRNYPPQNRTAKPNDNDGDDYSFFEDDLPVIKDTFMRGFQSFKQRSMEWVENIASKFDGEEEDDDDEKYSAPSKIYPSPRRSTAATLESAYEERPPSLPRRKPSRPGTAITLPPYESDPHMLNEKDFERLRLESSSSPMMRRSSLNSNRRSVESSSSAAFVEGQSFILDSNGAIEVANSAFALDDSDLESAYNEELEMKKDTSKPTASTKEVVVEKKPDESRKQAARTLETVSEEQMGSSNAKSKVLTSEPKDSTSVEAEKTETDEPAVGKGASDVSDTAEISEKTEAKNADSEANLEEKSDVGEEKESKDENNKASLHKDVEEKDTKITNEDTGKTETDVKAKETDSIEANDKDEKTDSKETEDKVEETESKEADVKAKETDSIEVDDKEEKTDSKETADKVEQTDSKDTNEKPAKDDNKEANEKAEKVDSKDVKEKIEEAADLQNSGKET O14320 COA1_SCHPO SPBC16E9.03c; CHAIN 1..249; /note="Cytochrome c oxidase assembly factor 1"; /id="PRO_0000373998" MISSKSLDYTRFLPFFAALVRGHCLTVKSPTHNCGSGVKTIMDKSSIFLKNRYPISINRFVQQRKTFCGASVCLHKVLVQRQFGFEEKSHGLKYKKLFRRNIGTSEKKNRLPDLLELSSSPRRLPILFAAFCLLWGTCAVLAIQYGKQNSNVTQVVMYRVQHSKEAQDLLGSNIDFKYPFPWVPGKLHKRQGFIDINFEVSGSLASGTVHYQSQRFGPIAHWVELDCTLTSNGKTIKIPTGVSKDTQWT O14322 MU100_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC16E9.07; CHAIN ?..313; /note="Meiotically up-regulated gene 100 protein, mitochondrial"; /id="PRO_0000278619" MYTTKRFQQLLKEFEVALLLKFSKQLLLLGKIESYLNNGSSMKHEECKSQIYDCRMAVKIYVCSITANKSTNLKHFVRLFFLLGDSERVNLCIKRLIYTFIGSINSVIDKKEDIEQELYSSCMHCSIMSPKLQKVMLAQKSLILNKVFDYLFFLYGLSGTSILYTAGDHIRKLDFKDSGFITPFFQLLLLVLLFTLTFKSKHSLNAYSLTASQFSGHTVCNESSLKPNENSCDLNLSRTATIKLESAEDDACQRVLGLIKSYMRPRTLEELKLEFRFEHKSVQDITTCILDEVDGVQMARVLEINPDAPILAF O14330 YB7F_SCHPO SPBC16E9.15; CHAIN 1..75; /note="Uncharacterized protein C16E9.15"; /id="PRO_0000124809" MSASVRGNSKNPQSTSAITTLTDKLLEDISGDFETLQKQFSEKLETMSTRLDQLEESMREAMNKKSSVSPVTSTE O14334 PFD1_SCHPO SPBC1D7.01; CHAIN 1..112; /note="Probable prefoldin subunit 1"; /id="PRO_0000124833" MQNLASQIQEKAVDSQQQLRTIMVQIAAKERALKISELAKKELEDVGEDKAVYTSLGKMFMKSDLASVRTHLDAEMASLREDIEALQKKQTYHETTASNAEQHLQKIKESIS O14341 RM35_SCHPO TRANSIT 1..17; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC2F12.10; CHAIN 18..308; /note="Large ribosomal subunit protein mL38"; /id="PRO_0000317293" MKRVWPRIPTISNVCRARSIYSAAQENAYRSSVKLIQEYSEKVHKKLQAKLLENPSETSPEIERLQVLSQINLPEVRSKFHKKEIDYTNPVFLYMLKQQWEDYQKLLLLQRLEQMKVIKDSGIGSFSPSVDVQLGFNPENNDSITPGTILPSTVTVKTPWLSVLPFNCKKNHYSVITLDLDVPNYETNRFETHCNWLLTNIPIEASKRVPIDTSKAFFQYRPPIVHRGEDKHRILTLVLRQKSSSISIPSNALVRERFDLSEFCSIYDLEPVGAHLWRSGWDSDAVALLSKHPSVHEYRDIRVERIPA O14351 YB45_SCHPO ACT_SITE 136; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 150; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 154; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 11; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 85; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 119; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 150; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 154; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 181; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 183; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPBC30D10.05c; CHAIN 1..247; /note="Uncharacterized oxidoreductase C30D10.05c"; /id="PRO_0000054876" MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVGKASIETAIKKFGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPKLTGQFVEWKSFV O14358 RT27_SCHPO SPBC30D10.12c; CHAIN 1..93; /note="Small ribosomal subunit protein mS33"; /id="PRO_0000116500" MASKAILEELNILSSKIFGTQYKSNNSRTGRKFVVQELKGAKLKSYYPATINYRQLRTLLNDKTFPDSDEELRMEIRKGRIRQGKGASKSKKK O14359 YB4E_SCHPO SPBC30D10.14; CHAIN 1..249; /note="Uncharacterized AIM2 family protein C30D10.14"; /id="PRO_0000116501" MASCCPTSRGAAASNKSYTFKGKEIENFGGLTTYVVGSTSNTRVLIGFMDIFGLSDQIKEGADKLADDGFTVYLPDFLEGKPLPVTALPPKTPEDQKLCNDFFSTRISPNLHWPKLAKVVEAVRANHGPNVTIGTYGFCWGAKVLVTYPATIDFVGIASCHPSFPDSADAANVHCPVLFLCSKDEDAKIIKEWEEAFKTNPAYAKSSFETFSDMFHGWMAARADLSNPEQRKRFDEGYQKVSSFFQSLM O14364 YOHB_SCHPO SPBC13E7.11; CHAIN 1..298; /note="Uncharacterized protein C13E7.11"; /id="PRO_0000116871" MNRLNFQSLLWKFGQKRFYYRPWIRIENIKPTPLWKPITFAVGVGSATFYTANYLDKRRKNYPKSSYGFPIPQTSSRSLVLSIIGINVGVFALWRAPRFSHLNRFLQKYAVMNPIFINMPSMIVSAFSHQSGWHLLFNMVAFYSFAPAIVDVFGNNQFVAFYISSILFSNVASLLHHRLRFGTKVTPGSLGASGAIYAIAAATSYFFPNASVSIIFLPFIPIKIGVALLGLMAFDAWGLISRGFSSFANFTLIDHAAHLGGGIFGWLYAKYGYSTYNRSTRPRPPSLSKPFFSRSVSF O14367 GTI1_SCHPO SPAC1751.01c; CHAIN 1..720; /note="Gluconate transport inducer 1"; /id="PRO_0000083874" MTEPGNLQPTFVGFIGTTVDALLLFEACRQNYTHFVDRRPQDRERERLIRSGSVFVFDEVQSGIKRWTDGIAWSPSRVIGNFLVYRQLCKKNSVSDRKRSSKSRSDSDEEEVSAFTVSVPVDVDVASHVNISSPSAPSLSDNLFPGSSFSASSQQNPSSPGSNDIKSEFAAVKNEYVLSPTSPTTSAAFPSSFSSLPLVSSKPTGTPFVPKSPPSSSPSTTNVSNASTSSAPINPRAPQTRRESISSTSSIHYCSSSSLSYLHDTERALVGSLTDSYGFKKSGLIKKTISLMIDGRLHHLISYYTPEDVLNGKLQTPSSFNLFQQLTISKDLLEYKSFRIPPLVEAAESEKISQLSTLEKRTLPSFPYNPFFSSSTAEIDPYHFQGLTLSTSPISGVESSSLSSAISRNQSNLSSFQQQQQFSALQSISNNALNENIEQPPIKMAARHSYPNFLQTLPQYMNDVYNPSGLAFNPVNPNANNSFVNLNLIQFTSPSQALFDYGEGPYVDQKSQYLQPKQPSSNTDSIDQSSYNMSLAASKQFLTSDTQPDVNENYSFISNSIPKNLSTSWNQNMGYHVTNSNSELASQNPLYAQQAVSMESMGNAIQSSAYSAMSTPHGGHYDHYAATAKGKNPLAAENHASGGRLPKVPIPPLSNMRRGSVPIIPSSASLPMRTSGNRFCHYSSLNGNHNRISARTNPYPINNQTMLFTEPLSKERGSLS O14450 PFD6_SCHPO SPAC3A11.13; CHAIN 1..114; /note="Probable prefoldin subunit 6"; /id="PRO_0000124854" MEELAKKYQNLQTELSTYVESLKKLETQLQENTTVLNELEKVAPDSNIYKQIGPTLVKQSHEEAKTNVKTRLDFINKEIARLENQTKISQEEFSKVKGAIIQAQAAAAPPNPAS O36018 BUD22_SCHPO SPAC4F10.06; CHAIN 1..388; /note="Protein bud22"; /id="PRO_0000373991" MVFTSHKGVKRKSHHSQLSVDDVPKKIPLFKKKISQALKKASTFERQKLVRRIKNCRASEDADTLGRFEAEFEFAKQFDFTKFVDYCYYKKILKNKDFRKLLNENLHVDFPADLTEDAQRNTVARILNSKQLSDAIRNINSILEKYLRFLNPDLQELSDKKAVSSTQKPIKTIGKVDLSNKSTSNQDQVDNTHVQNSTDGVNQDTGMILDNTEDKEINKSMSYSMKNEGVKESSLQNATLINRKSIIDDEMLEIPLGKHNNTNLPALTAGFLDPVESDDEFVEKELEEVDIPKRKNRRGQRARQAIWEKKYGKGANHLIKKATEERSIREERQRKYEERQAKRAARENAFTEHQTPQKPEQLHPSWEAKRKQKMPSSAAFQGKKIVFD O36020 MU126_SCHPO SPAC4F10.08; CHAIN 1..398; /note="Meiotically up-regulated gene 126 protein"; /id="PRO_0000278623" MGEMLNENTSSTSLSSFYVLENETIFNVQEEMEEDGSESGNIQKTLLEDPCPENVNDENEDEQNRSSRSSSPLVKHEQRHRMYNLKEVIKSFILTKSKEKPCDLEMGIDSIEMGRMQSFESDQQESHTGQANFPTDQEDPRNPQLDSQYEAFITQGESQTDKKKTSTVQEEELQNAGKKLETVQENPQAYSKVTQQEPQAGQKAVPQEPQANQQETSSNQEESSFDRQETQDDKQKPKTTQQEHYNLRNRNQATITNSNSKPQTRRSKIFVISLLGYGVYLLAFLDLIEYVSKEYGFEATVSAQIFLWCLFGVLMIARGLIYLALFRNFLNILKRMAIYCGACFWVYACIFFLTRVFCFLIDTPYPQFEKIPLEIYSIFAAINVYIIELGAIYCTSGR O36021 YEK9_SCHPO MOD_RES 744; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 748; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4F10.09c; CHAIN 1..860; /note="Uncharacterized protein C4F10.09c"; /id="PRO_0000173492" MATLYPKPKRGQKIIFNEEGEGTIDTKPQGVMFDPGVPWYNIPLPELHEDKKFVNVDHVSELETRGLLLLKEDSERFSETLGHGTADKRMLQTLISSGTTSDRISALTLLVQESPIHAVKALETLLSICSKKSRNEATQAITTLKDLFIGGLLPDRKLKYMKQQSCLGSKNVTDKHLMVWAFESFLKSFYFKYIQIIEALSFDALLFVKSQMVSTIYDLLKAKPEQEQNLLKLLINKLGDKENKIASKASYSILQLEASHPAMKLVITKEIERFIFAPSTSRTSCYYTLITLNQTVLTHKQVDVANLLIEIYFVFFTKLLFALEKEEVADAPTLEKKSLQSDSKNKKSQKRKKDEDLRKEAEENVNSRVISAVLTGVNRAYPFAEVNSEKFDKHMNTLFAITHTASFNTSVQVLMLIFQASASRDFISDRYYKSLYESLLDPRLTTSSKQSLYLNLLYKSLIIDNNIPRVRAFIKRMVQVSAWQQPPLVTGLFHVMHQLVIATTALRSMFTNAEIHDFDGDEEEVFKDVEEDDVSEDQKVDSDKDGKLSDKQSHSAYVVGNVSVSTKKEHLSYDGRKRDPQYSNADGSCLWEIHPFLNHFHPTVSLLAKSLVYGEKILGKPNLSLHTLNHFLDKFAYRNPKKSAAARGHSIMQPLAGGLSKGYVPGSTYSGVPMNSEQFTSKKQEEIPVDELFFYRFFNDKYIKGKQARKTKVDRDEEGEIDEDEVWKALVDSKPQLEMDEEESDFDSEEMDKAMTDMGSDSEQSADENDNESMASEEKPMFSDEENLSEIAHSEDEFDDTVDFFEDENDLLPFNETDDEEEIQTVDHSETHSHKKKKRKAIKDLPVFADAESYAHLLEN O36031 YEKJ_SCHPO BINDING 4; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 7; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 16; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 19; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 24; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 28; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 32; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"; BINDING 36; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00453" SPAC4F10.19c; CHAIN 1..154; /note="Uncharacterized zinc-finger protein C4F10.19c"; /id="PRO_0000173560" MTTCSICNESEIKYKCPKCSFPYCSLPCWKIHQSQCETVNDNNTTTFKGVKEPLNPPEPSPNVIYVNGRIPSLAEEALPSESLLESIVEDPSIKNLIESNAELLHIMKELVNLDREEEGSVPLKTLDAIQQQRLHNPSFEKLASMILEKYYAQK O42645 YF94_SCHPO SPAC10F6.04; CHAIN 1..351; /note="RCC1 repeat-containing protein C10F6.04"; /id="PRO_0000341579" MLLSLGSNGNFQLGLNNDEDVYSPQIVPFDRAIEKISCGGNHTLLLDEDSQLWACGDNRKGQCGYEVKEPLYNPLSPDYLRIFTRVSHERWVFLTCGWEFSVIVHADRRRVCSCGEGLSGELGQGNRSNSQGLREIDIPYLDDKEFIIDISAGLRHWICVTNEGNLYGCGDGRKGQLGPVVMKTVNKVSFLGRIEHAQAVVCGVQFSAVLQETGHVIVLGGEKWNVAAECDAWQANNSELSSSICSISANWSTLSLLSTEGCVYAFGRCDRAQKAHTKASDIVQIASGTEHNILRTKKGSVLIYGWNEHGNASNDDKRDVYDAKTLQLPGWAYIVAAGYATSWIVIEENHK O42647 MUG94_SCHPO SPAC10F6.07c; CHAIN 1..188; /note="Meiotically up-regulated gene 94 protein"; /id="PRO_0000278615" MDFNKIGDENVVFQIFKLEMLIMSEFPSFIEEKDKLLCLNVLANLLGGIFENEDKIIPNYKEAVIAALFERLLLSSNQKSTSKSNQMIKLLNNSLAHNNGLPSQRCNHDSKLVYMSLVQNNGLPGQRSNYVCCPLCMEQHCIELLTYQLFAKWRNFPRIDFSPVLQGNRGPRFFYTCFLCNSTFLASA O42654 MU134_SCHPO SPAC10F6.15; CHAIN 1..432; /note="Meiotically up-regulated gene 134 protein"; /id="PRO_0000118859" MNYNANVVKFHSTILHKFALKISKFLILCMRRNKRQLACMKCQCENPMAAITYADIEYPHNTHFLLLDSISWIPCTCKILKLKEFELPDRFDIPNLFYDGWLSYVFHTFSGVYLKIGYEMDESGFCLPDQVYHLIDNHSCIQTAVSHLLRNHQALFKYLCDYLRSGEFPLTVLIHHVMLYQYYPKSLQEALWAAVEHYVNNSGEAYSTVQKLAVQKKIGNIRMYLVNPRDIFALGSTCNCIVVSSSNFQSYVQLRKPLLENNLPYEIDGFDKILQCANSEADIGWIAMIHCIGSNGYAFPIHLYLNMKKNIFLGKLPESTLLLYNSDGAIFKNPPSSKKECDFYNQLLLDLCKCRQFNAEMECNMKKLFNNPTGLHSLPNLPNFSEAGSAKSSNFCSSKDNCLTNRLTLNCLDTPSDENGEDIAIQLIIPAE O42657 YF82_SCHPO SPAC27D7.02c; CHAIN 1..750; /note="GRIP and coiled-coil domain-containing protein C27D7.02c"; /id="PRO_0000317081" MLGRLKDQLNMTLAQGQEEAKNRRRQFQEEDQLRRNNKSSNKLSQNEEDAKNMDSVVQKLNELQNNVVAFQKLLQEKTPLSSIQDLEGFREFMENLEHRYEMTVSEVRRLSHEVNDLQTDRENLKHQFEDQIEKLNSEISNQNSLILQKKDELEKSIQRCSELEEKINSLESAQSIEQEVISSLKDDKTVETKNDVPEVSRPSTDTIGVSSALSKKKKKRNRKNQKKKSTKQNIEATTENDALSESISTPDIQKVAQSEDVDAEQDTVADSKEEERRDIANDDLIVNANAKEPMHHFSFTDLDTLLNWPKYVFHHHKIHLADTIPLVFLDLKPKEYTVDLETPKLVEELTKQLHVAESTLKENSEKFKQNSESLKSRVDNLNDYITKLQNEIDECRRNLLWAESSCETIREENQKNIKKLNDAESLKSRLLQSRTQMQTELDSYITSNSQLKDEITSLKQTVSESEAERKRLFSSAQEKQLQMKETVNKLTSLQEQNNEFDRQLKEQEEDLQNKEEELTELRKLLREQTQDSQKLRLLVEQLELERQDLKQAGENHYSNLSSDYETQIKSLESSLTNSQAECVSFQEKINELNSQIDELKLKLNEANKKYQELAISFENSNVKTQSVEPDNGLSLEALKNENQTLLKNLEDSTARYEHLQKSFKNVFNQLRKQQPSNHGRNSSVSRSSSSVEVNSKHPGSDDMLIDKEYTRNILFQFLEQRDRRPEIVNLLSILLDLSEEQKQKLLSVKY O42663 YF89_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPAC27D7.09c; CHAIN 24..383; /note="Uncharacterized but2-like protein C27D7.09c"; /id="PRO_0000372622" MKLTSIPIASTLLSLLAASGTLASPLHKRDDPLNNKQFGLMSIHSGNSYVHLHPFYVGDSGAIYLDPTDGTSTSAVFSMSNGRLVVGNLYASVDSNGTTIFKSDANAASTKFSAGDATNVGYNLLYNGTQSAVACPASDNDQVYQVYFGAGNGNPNCAGIAIEAFVSPSSSSSSSSSAATSTSTRVSSSAKASTSSGAIAYTTKCVVVPVTASATATAKAASAAASSAVYPLFPHGIRLIDSANPSSNSGNVYSPVVFQKQNNHTNTIFTFDVPQVSGSCELNLHLDTSGFPITVEGSNGVGQFILFNLSSVANDSTVYSNRPNRIAEIGRFNCSSSGCDYATNVTCPNSYTAVSYEMMALTDDSYLSFFEEADPLEGLTLRV O42665 YF8B_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPAC27D7.11c; CHAIN 24..463; /note="Uncharacterized but2-like protein C27D7.11c"; /id="PRO_0000372624" MKFSSIPIASTLLSLLVASSVTASPLRRRDDPLNGRQFGLLALHSGNEYVHLHGFYVGDSGSVYLDPADGTDDAATFTMSNGQLSVGNRYASVSANGEIVFKSDTNSTSSGFSVGEAISSGYSLKYNGTESAVACPSLVNNQVYQVFFGVGNGNPSCVGIAVLAVLPQPISSSSTYNSTTSSYHNSTSTPPPTITSTKASTVTSTEATTVTTTTAVTVTATETYTVTATNGGSTITSTGASTVTSTQPSTVTSTQRKNTATTTKTTTYVGPSPSASSVVAYTTKCIVVPVITTAASQSEAATPSPSAAVYPLFPHGIRLIDSTKPEANSGNVYSPVVFQKQNNHTNTIFTFDVPQVSGSCELNFHLDTSGFPITVEGVNGTGRFILFNLSSVANDSTVYSNRPNRIAEIGRFNCSSSGCDYATNVTCPDSYTAVSYEMMALTDDSYLSFFEEADPLEGLTLRV O42826 PDH1_SCHPO SIGNAL 1..26; /evidence="ECO:0000255" SPCC1235.08c; CHAIN 27..226; /note="Protein pdh1"; /id="PRO_0000022033" MNHFSKFSVTKRLLILEVLFSAISFGISIYIKVFGRSSIVTFFLLCFHLVPNALFLFPWTIITTSFVDANVFTLLSSILILSVYGVEIERSWGHKEYLLFCQFLTVIPNIAVLIPCFIAYKITDSHYLLVAIIQSTTAIQAGILTAWYQLYSCKKEESSNKFLCPLSKYLIYLFLSIHLFYVFQSFPWTYFCLAVSGTCISELYVLFVHPVVQELFHLESHTQLPI O42841 YFH2_SCHPO SPAC23A1.02c; CHAIN 1..430; /note="Uncharacterized protein C23A1.02c"; /id="PRO_0000310838" MFARHPNLLWLNKQLSILHYLCLVFLAVYYAYPLLFGIMPRKLQLEDENSFVIMGVADPQIEGNHKIEANGFFKGTLDLWGNDLFLRHLVHMNQFWGQPDAMILLGDLVSFQHLDNEEFNKRAKRLKKITGAKNFWQVGNSSLPARTFENGNIPVWTIAGNHDIGYGCESSDAQISKWEQAMGPVNWVSHFNVSKFPVRVIGINSLSLDDVQFYDANPSDIINSKSFSSLGILALSKEARDAWQFLFDIALEPSIPTILFTHVPLYKPANVCVDEPRIVRQLDFRVKSQNHLSYNTTMKIFELIPSIKLVLSGHDHMGCDYEHPNGAIEHTLPSAMGYFGGNIGFVKLIATNDVLTESSKNTPSVVTFLIQKLIGQRWKKASLKQSKFSSDIYATYTLSHGGPSYIWWALHISVCVLTILRLLVISLQHI O42843 YFH5_SCHPO SPAC23A1.05; CHAIN 1..101; /note="Uncharacterized membrane protein C23A1.05"; /id="PRO_0000304036" MGNPVVIKAKKDYDCVFEPEPMSWLRLQYYRYQVTAGTYLFTYKEAFVFNTVVFIIVFLTGWAAKSIIVKLLPSLWRLSTLIPSFFASFFMSLLGKDASSQ O42845 YFH7_SCHPO SPAC23A1.07; CHAIN 1..251; /note="Uncharacterized RING finger protein C23A1.07"; /id="PRO_0000310839" MIESELATSRWSLMLEADIATQTTRSLTNELSFIVAGLRPSTKESVLHFLELIFINLKYQSKKWLYSLVICKSLIALLGRKRLSANVRKIVRFLNVIICVIGLWKGLSAMSGKNTFINGLQSYLISETALPELGSFQELSTSSLGSFRMFQQIAVGFVDALFCTRIPASLWIKYKEYTTSAETTVPQECGLCMMCVQRGDERVAITTPYTTDCGHTYCYACIMSRLKLVNNVSCPICKHRIRFALPDQTMG O42851 YFHE_SCHPO COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 212; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC23A1.14c; STRAND 89..94; /evidence="ECO:0007829|PDB:7YEO"; STRAND 109..113; /evidence="ECO:0007829|PDB:7YEO"; STRAND 138..141; /evidence="ECO:0007829|PDB:7YEO"; STRAND 143..145; /evidence="ECO:0007829|PDB:7YEO"; STRAND 154..160; /evidence="ECO:0007829|PDB:7YEO"; STRAND 183..187; /evidence="ECO:0007829|PDB:7YEO"; STRAND 204..209; /evidence="ECO:0007829|PDB:7YEO"; STRAND 223..226; /evidence="ECO:0007829|PDB:7YEO"; STRAND 300..303; /evidence="ECO:0007829|PDB:7YEO"; STRAND 324..331; /evidence="ECO:0007829|PDB:7YEO"; STRAND 344..348; /evidence="ECO:0007829|PDB:7YEO"; STRAND 355..361; /evidence="ECO:0007829|PDB:7YEO"; STRAND 373..377; /evidence="ECO:0007829|PDB:7YEO" HELIX 16..22; /evidence="ECO:0007829|PDB:7YEO"; HELIX 25..27; /evidence="ECO:0007829|PDB:7YEO"; HELIX 72..85; /evidence="ECO:0007829|PDB:7YEO"; HELIX 95..106; /evidence="ECO:0007829|PDB:7YEO"; HELIX 122..135; /evidence="ECO:0007829|PDB:7YEO"; HELIX 170..180; /evidence="ECO:0007829|PDB:7YEO"; HELIX 230..243; /evidence="ECO:0007829|PDB:7YEO"; HELIX 249..285; /evidence="ECO:0007829|PDB:7YEO"; HELIX 287..292; /evidence="ECO:0007829|PDB:7YEO"; HELIX 297..299; /evidence="ECO:0007829|PDB:7YEO"; HELIX 306..308; /evidence="ECO:0007829|PDB:7YEO"; HELIX 313..317; /evidence="ECO:0007829|PDB:7YEO"; HELIX 333..342; /evidence="ECO:0007829|PDB:7YEO"; HELIX 362..364; /evidence="ECO:0007829|PDB:7YEO"; HELIX 383..396; /evidence="ECO:0007829|PDB:7YEO" TURN 49..51; /evidence="ECO:0007829|PDB:7YEO"; TURN 67..69; /evidence="ECO:0007829|PDB:7YEO"; TURN 116..118; /evidence="ECO:0007829|PDB:7YEO"; TURN 162..164; /evidence="ECO:0007829|PDB:7YEO"; TURN 193..195; /evidence="ECO:0007829|PDB:7YEO"; TURN 198..202; /evidence="ECO:0007829|PDB:7YEO"; TURN 210..215; /evidence="ECO:0007829|PDB:7YEO" CHAIN 1..398; /note="Uncharacterized trans-sulfuration enzyme C23A1.14c"; /id="PRO_0000114765" MTHTPSFDLSDIKSTLSTNVLHADDAYALENDVAPPIHISTTYTYPGTPDTLQPFTKLAEEDFPYYARISGNNVDRAEASLSSVLGAPSVVYSSGLAAIYGLLSYLNPKHIAVHKPGFGGYSGTIQIIARINRLTGLETSFIDGKCDAIGEGDVIWLETPLNPLGIAFDIPFYKELAKKKGAILVVDSTFAPPPIQDALVLGADYVVHSATKYLAGHSDVLAGVTASKDRSKILDLKADRAYLGTILHPQQAFLLLRSLRTFPLRIAKHSENGFLVAQHLNKLATDEQFATSLGIDSSLILEVYHNSLQTKEFVAKNLTGGHASCFSVLLKSDTVAKHLCCELKYFHHATSLGSVESLIEWRRMTDSKIDPRLVRLSIGIEDAADLIADLNRVFASLS O42855 RT51_SCHPO TRANSIT 1..13; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC23A1.18c; CHAIN 14..303; /note="Small ribosomal subunit protein bS1m"; /id="PRO_0000116742" MSFAQILRGSRAMASPKCLPESNYSTSHLRFPRLQSITSKKNSRARGDWGLKRTLPKIKTRYICVRQQDSLYKQADFQSSAKFVRLVRNWFDAGFVRDPSEVALLQELLKETGLKDTRDINKVFSPSKQSDENDNFRRYGVSGGIQYSNVPLINSRVTPNCESNCSNIRRRLTAHIISSDASTAYYGLGGLILRLPRTVVFNRNRSSPLFSQEQRISYTVYKNGRLRLVPFSGPELETHLAYPSEDSEVESFFNRDIQLVAKRDSSLDAPVSYQRGIMKFFMAPSQTSNNEANSSEKDNLSNS O42859 RT02_SCHPO SPAC23H3.07c; CHAIN 1..105; /note="Small ribosomal subunit protein uS14m"; /id="PRO_0000131016" MRALGHLKHKAFRDLLCRRLFAEHEVERQSNLYIYRNPELPLRVRLEAKKRIEALPTNAHPTKIKNRCIETGRGRGVFRAFGLARFPFRLKALANKLPGVRKASW O42877 FCF2_SCHPO SPAC3G9.15c; CHAIN 1..230; /note="rRNA-processing protein fcf2"; /id="PRO_0000374004" MTEIGLSVDLATISKLLESAKSTLQEKQASDDDKHGQQKLLTKIPKIISSSFELPSYFEKKFVMGLKKDELVENSESYINDASFEPTVPIYESHVSAPGISKKKKNIKDTAGSNWFDMPATELTESVKRDIQLLKMRNALDPKRHYRRENTKSMPKYFQVGSIVEGPQDFYSSRIPTRERKETIVDELLHDSERRSYFKKKYLELQKSKMSGRKGQYKKLQQRRKPSYLK O42882 YFQ5_SCHPO SPAC8E11.05c; CHAIN 1..338; /note="Uncharacterized protein C8E11.05c"; /id="PRO_0000372362" MASPPILSRESPVLGLEEEKKSDGGNSEVNIDPSASSSLKEDVDGEEGADTKIDPHLLEEDDLNPVEDYDSKNQKVVEASKLDLDATSTVWAESLSINREASISQSGIVDNEMEKKVEEEEEFDEFDDFGEFEHDIPICTFMGDWQDDFQDAVNSVFGLPETPKTIEESSLDPDRILSLWQKLIEMPVLQRPDWLRSSIRHIFLVTMGLPVDLDELLPTPSTQGSFNSSRTIELSSVTLPKSEDEPYLDYSAARRLCSINKDALTHRSHESLQQHIELLESTLQQAVEVARYWTDKRDSALSDKLLYETVVDDLVQHSKRLRNSGRKFLSRRSTSSHK O42888 YBN4_SCHPO ACT_SITE 59; /note="Proton donor"; /evidence="ECO:0000250" BINDING 117; /ligand="substrate"; /evidence="ECO:0000250" SPBC8E4.04; CHAIN 1..325; /note="Uncharacterized oxidoreductase C8E4.04"; /id="PRO_0000310309" MSIKEFAKNAREAYFTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISKLIEHKTLVDIANARGEGITPANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNIGVVRRFSHGKFAPKPMFVGLQDGTPKQTHA O42889 YBN5_SCHPO SPBC8E4.05c; CHAIN 1..447; /note="Uncharacterized protein C8E4.05c"; /id="PRO_0000310362" MPVSVSDSFVFRNIFGDAEIRKIWSDENRTQEYLNWEAALARAEASLGIIPKYAGEEIQRVCKVENIDFSKLEEETINIGYPVLGVVHQLANLCSGDSGKYCHWGATTQDVTDSATVRQMIDSFKIIKGYLEKAIELATVLVIKHRETTMAGRSNLQQAVPITFGFKMARFVATLRRHHQRLCELLPRVSVLEFGGACGTLASLENKGLMVQQKLAEELGLLQPEIAWHTERDRIAEAGCFLGMLTGTLAKFATDIKLLMQTEVAEVFEPFKANRGSSSTMPQKRNPISCVYITASTSFVRQGVAALLDAMVEDHERATGAWEIEWIVLPDVFVHTVGTLKQTVFLLEGLEVHPSRMNENLSITNGLIVSEAVMMALAPKLGRDEAHDLVYRLCHLSIQENKPLVELLLAERQVTNYLSKEEVTSLLNPENYLGSTFEMIERALQIP O42895 YBQ2_SCHPO BINDING 125..132; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPBC115.02c; CHAIN 1..454; /note="Uncharacterized protein C115.02c"; /id="PRO_0000279525" MLQVLRVSAPCFAFVDTIGSIGVCRVVRFTTFHNTPIEVYNKKVNDGVWKRDPYQETAVKAINRLYTELESYTQPPITQDSMPAEKGSILSWISPLKKMFSRKKSPTLTSSLPVPGMPKGIYLYGDVGCGKTALMDLFYHNLPPNVTRSQRIHFHAFMMQVHRTSHDLQDRYGFEIDFIDHIASGIAKETTVLCFDELQVTDVADALLLRRLFEALMKYGVVIFITSNRAPSDLYKNGIQRESFIPCIKLLEHRLQVICLDSPNDYRRLKSKTEDTYLYPANSPEVKKALENWFLCYADEKDPAHQDEVEVFGRKIIVPKASGNVAWFTFEQLCGEPKSAADYLSLASRYHVFIVSDIPKLSIESKDLIHRFITFIDALYDTHGKLILSSEVPVQEIYPTAPSEVLSSTADPAAKGKIESHYHGAFGGIEEVFTFTRCLSRLSEMKKQSWIHSP O42896 YBQ3_SCHPO SPBC115.03; CHAIN 1..368; /note="Uncharacterized oxidoreductase C115.03"; /id="PRO_0000091789" MPPIKTAVLGTGVSAFVFHFPFLEALPSKFEIYACLERRATVTQSKARSAYPNILVYTNLDELLADVNIELVVVSLPPNVHSEIVKKALNAGKHVVCEKPFTPTYEEAKELYELAESKSLLLAIYQNRRWDGDFLTAKKIIESGRLGQVVEFESHFDRYRLGRKSGSWKDEPRPGNGMVYGIGSHLIDQAVSLFGTPYSVTAKLEAQRQIPPLEVEDYFRIILHYPAKGNKLPINVILSSTNVSCGCEMRFCIKGTRGSFMKFGFDPQESQLHSGMKPNDHGFGTDRFELYGNLWTVPLDADVKALPEPTKITVPTVQGNYRDFYDAVFEEILKKANEFPIKSDQVLAVEKIMEAAYKSSESSSSIQL O42899 SCO1_SCHPO BINDING 130; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250"; BINDING 134; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250"; BINDING 222; /ligand="Cu cation"; /ligand_id="ChEBI:CHEBI:23378"; /evidence="ECO:0000250" SPBC119.06; CHAIN 1..263; /note="Protein sco1"; /id="PRO_0000173873" MFRRGLVFSRHCHYSLIRPRFPLNRTCLARFADGRKNLATDNRTQTYQSWRGMISIRALLLAAATSVGLYAYFQHEKKKVLERQNDKVLATIGRPQLGGAFSLIDHHGNRVTDNDFKGKFSLIYFGFTRCPDICPDELDKMSAAIDIVNNVVGDVVYPIFITCDPARDPPQEMAEYLEDFNPKIVGLTGSYEEIKDICKKFRVYFSTPKNIDPKKDDYLVDHSVFFYLMDPEGKFIEVFGRNSTSEDLARAIGSYYLSRKKQK O42901 YBA9_SCHPO SPBC119.09c; CHAIN 1..186; /note="Uncharacterized protein C119.09c"; /id="PRO_0000116508" MGSSSSRRRSSSLVTKVPKPTIDDRLDQGSATNYNSNWVNYKGAWVIHIVLIAALRLIFHAIPSVSRELAWTLTNLTYMAGSFIMFHWVTGTPFEFNGGAYDRLTMWEQLDEGNQYTPARKYLLVLPIILFLMSTHYTHYNGWMFLVNIWALFMVLIPKLPAVHRKRIFGIQKLSLRDDDNDSIPR O42903 YBAC_SCHPO SPBC119.12; CHAIN 1..401; /note="GRIP domain-containing protein C119.12"; /id="PRO_0000372423" MAENAGNETKLVENENLQEDLSRLNLEDEKNELKLNEKGGVLKENDEHLECSESFKKLAEKEEAYQTLKNSYNSLKQQHSNLLGKVSGIKSTLGERLKKDSQELAQNRKRIQELEKSLGDAEEALKLSNEETVTLTAQVESLTQDITDLRQQNASLVEENQLLSTQSKQWERRARDEHEMQESLAVRLADCEEQLARETERQEQYEVEIQRHLTNQHQLEIELESTKASHTENLGELTRNWQKAMDDVTEKFASKSKEYEDLQNELDATQKRLSRVSDLEHEVKEKTLLIGKLQHEAVVLNEHLTKALCMLKDGNNAEKIDKQLISNLFVSFLTLPRADTKRFEILQLISSVLDWNDTQREQTGLQRPGSSVNNWSIPHSASSNSLFSDHSFSKRRSFHDS O42907 YBAG_SCHPO SPBC119.16c; CHAIN 1..448; /note="Uncharacterized protein C119.16c"; /id="PRO_0000372350" MSIQAIVLATFDAKEGYNVENYYPGDFNVEGIEYLLFPSGIQELDNCTIFFRFQDQLCLSVFSKLQHPSFERSAFFTSVGLILSDDINFGEAVVKYGETLLYIANGLSLATLKYKFGEDASETYASEKCTSHQLSDSDFFKSLQTSAVNLEFDSLFEKLQGNKFAILGANSKELSQSYATILLDHLGPAFYCLYKFALQRKRILLISSHDDQLYSIIDMIVRLSSIKRSSDASIPILLSDLHPFYSVGLANTSTLLDNDLEEGWIACTTDTVLLSKSSLYDLALYWPDNSFNANKYPQIFNSNSIRIKPSYDDLINFKGLSRYLSFDGESSWGLTTYSLASKYIFNTSHHNLTDQEFLNENMLDYFQRYNQKLLTVLSSNAESFNVSDMQTLGLNPCHSLDKSFVSEISQIWLKKHINWQYGKYFWLRRVSLIFLASTCFLFILWKLL O42909 YBI2_SCHPO SPBC16A3.02c; CHAIN 1..347; /note="Zinc-type alcohol dehydrogenase-like protein C16A3.02c"; /id="PRO_0000372424" MSSETKSEFGTKSAWLYNRTGKPKDVLYLEKGLHIPNPAELGPYDVLVEVVATSINPLDYKLMNTYQMIAKALFKLPNIPGYDFAGRVLAVGSEVKEFSATQRVWGCQSFPRAGRQGGSCATHIVTGDKDVWHLPDGVSFNEGAGFGIAGLTAWEVLVRQMKVKPGTKLVIEGASGGVGTFAVALAKALECEVTTISSTENLDLCKSLGATHTLDYKKDNLVERLADLGPYDFVFDCVNDNVLYRASSKFVKPDGAFFGIGGDITLSYVGSRLSRTLRPRVLGGSSHSYYNILLHVDQEMLRDFVDFVMKHNIKTVIDSVYDFEDTVEAFNRLMTHRCKGKVIIKTD O42911 RT25_SCHPO SPBC16A3.04; CHAIN 1..220; /note="Small ribosomal subunit protein mS23"; /id="PRO_0000343560" MPKFNANGLLRSFAAEMKKPWTAESLWYETVAKHPPTFQYARRIVPLYDPNKVKSRGKRLRKSMYQPQEIQWPEDKLRKRFYRDHPWELARPQIIAENDGNDQQYCDWSHMDQPRKALSGESVVQRTLWLIENSNMPVENAYDQARKEFYHLRAEQEIQQRVAHDQAQALGAVFTKSDLELGYEMDQNALNSWFDNASQYAEANRTKFTDPSVDISKTTQ O42919 RT01_SCHPO TRANSIT 1..23; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC16A3.14; CHAIN 24..268; /note="Small ribosomal subunit protein mS43"; /id="PRO_0000310776" MLNTGLRKGLALSPITHLLKRCSSVTDNVHRVNYCYNYHTVPNLSQRNLLPLFSPEALDIAWDQHQRQVVKELNDRVKGTELEDSSVFNIIFQTAALPEHAATFQFASQAYNNHFFFQSLIGKRAADAKKNSKYEANAAINKAVNENFGSKENLLSKIHELASNSFGACWLWIVIDDYNRLNLLRTFQAGSPYLWTRWQSNDPHLISSVPDYSARPRKYAHVPILNLCLWNHAYYKDYGLLNRSRYIDTWFDCIDWSVIEERLTNSLV O42921 PT191_SCHPO SPBC16A3.16; CHAIN 1..85; /note="Mitochondrial protein pet191 homolog"; /id="PRO_0000325874" DISULFID 21..53; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 32..43; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MGRSCKVIREDLANCLLHSDCMFVKKKSARECLKNKDELPEECKNLIEAYGECKRQMLDMTKRYRIAPEKNTDQDTEKPSNVDEQ O42922 YBIH_SCHPO SPBC16A3.17c; CHAIN 1..599; /note="Uncharacterized MFS-type transporter C16A3.17c"; /id="PRO_0000343518" MSSSSSHNSFSGSKTNAAEGQNSIDGLSLKKTTSPFILTAYPSNEEKEVKETDIVPDENKVNELDVHKQSTEFSKQESASNDDDTNIQLIPENNMKIVVPALILTLFLAALDNTIVTTALPTIAEDFNDTSSSSWIGSAYVLASNAVLPAVGVFCNILGRKIVLYICIFFFMLGSALCGASQNMIWLIVCRAIQGLGGGGIISLVNIIISDITPLRTRPMYSGILATAWGAALVAGPIIGGAICQRTTWRWIFFINLPSGGIATALIVVFLHLLPCERTSFKKFLKTFDFIGLVCVITGIVLILLGISLGASSGKWRRANILCYLIIGGCLFVFAFIYDTFTKRNAVLPPPFFKNRSSAALLACSSFFYLNYMLFAYYVPQYFQRIRGDNPIMSGVHTIPCAAVLCFFCTTVGMVLRKLGRYLPLIYVGYISCVAGMGAMICVNATTSMSKVMGLTTIFMFGSGFLFLPPLIAMQATFPPAMTSMATATLMFIRTMGGSIGITVGEVIFNERVTQSFDGNTTYAQLSYKQVERLPQELQIRVKNTYASAFRVIWIFCTVVMAIGFASIFFIKSRPLISNAQSVPAKKKGDSDEKPAEKV O42925 YBD1_SCHPO SPBC16C6.01c; CHAIN 1..473; /note="Uncharacterized protein C16C6.01c"; /id="PRO_0000116510" MNNSKQFLKYQPLLEWLAKHEAYISPKLYIASSGVAGDGIFSTFDIDELEVLAKIPRRIILSPRNSRFGDSLYTHFNESNRSDDINFDNRDQVGLVMLVITVILENITDSPWNAYLNTLDETCMPDSPLLWKDKTCLEGTSMLDVINTNLRVYKNQYDQLVRPYFYKHADLKQLCPKWNQYLETCVLVQSRCFYVNSYYGLSLIPFFDIFNHKSGPAIASLHCQESNDHKGDIKIEFISFQYIRKMSEIFNSFGNFAADELFTQYGFIDTACKVWRVDMTMIAYETNRNFYMEWIHKKRIINTQELLVTPTTYANDKSETLRSVMIRQPMDLYIITDHGPSYGLYLYLFFCIYKIKFQKCDMNIVMLTKYFNEIWAVFIAHKEGEKEKVVAQLSGFSFYCKAIEFLQMLCQKRISRFKNGGLTAEAYKTLLCDPTLKRENRSRLVLQIFYHELNLLEKSMQETIYLCTENFED O42927 YBD3_SCHPO SPBC16C6.03c; CHAIN 1..207; /note="Uncharacterized protein C16C6.03c"; /id="PRO_0000303927" MNPTSFIYDKPPPPPIINKPFEQTNSSASLTQKNSSSETENVGRHGKRRMDQDLSFKPTKRGSGRGRGRSFRGGSHAGNTRGACAVDGIEYLKRRNISINTPEEIEAWIQERKKNWPTESNIRSKQEKEKVMENLGAADTSQSIDAQPTPSQHPLAHHEPHEKRGPPKKKSLYTKLLNTQLEQENIFFLQFMKLYLKKMGMVVKPVS O42928 YBD4_SCHPO SPBC16C6.04; CHAIN 1..350; /note="Uncharacterized protein C16C6.04"; /id="PRO_0000303928" MDSFHPTPGKPTTATSNSSLNFFVRNREKSIRCSSLHQTFTAPSPEASPSIGLRYVNYSMSDETDESMFPLDSELTDMEDDDTEYISDSTTDLPSAAMARGTRQLSYNENLDQRSFSKTPNKHIEVKNLKDLCSPSHSGRISKSLCPVLRRKSLLPKPKMFQRVASALYEESSPLELEIRSESEFSKMFFEPKKSSSFVSRAASPAMVGPGVPFYSSITGANGNVLAPSGSLKAVENSDVIESSAEDSSNTDNPSTKPSNEMPISPLLSSSVFFKDTEMSTPNSNHSRSRTPSSKKRTRWGEEIIDLSKRRAVSPSIYYDLDKKCSPIHSVMVSPLKIKDTHEVLMNLKL O42929 DENR_SCHPO SPBC16C6.05; CHAIN 1..190; /note="Translation machinery-associated protein 22"; /id="PRO_0000130608" MASQTIPKLKSVLYCDVCTLPVEYCEFEGTLKKCKEWLKSSHPDVYDKLYGEQDLSKDLENTLNVSGTKDSNAEEQPAKLTKEEKRVEREEAKRMASKVLIKTIERTKRKRVTTVQGLDAFGIETKKAAKMLANKFATGASVTKTADKKDEIVVQGDLNYDIFDFILEKFKEVPEDNIKIVEDTKSKKKQ O42940 PHO88_SCHPO SPBC16H5.04; CHAIN 1..194; /note="SRP-independent targeting protein 3 homolog"; /id="PRO_0000372626" MVSRWEKLKNNPQTKSIGISIFLMMITRVIDFSRPSLLWPLRILYATVNIVQIGIFLYTKIIIEKKNDLTVLKYVEPATPMSGREHSKFVATTVRDYDLSKLLTSFKQMLVTIATTLFMHLYMGYAPPLLLQSVSAARGLFDNSEVQIHVQNKPAIDELRRPFKSSGGLLGSFGQVLTDKKSVDEAELTKLKPT O42947 YBPC_SCHPO MOD_RES 456; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 458; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC16H5.12c; CHAIN 1..737; /note="Uncharacterized protein C16H5.12c"; /id="PRO_0000372354" MSVDTAKSDIQAEPSTGTLENKSSKTYSDSENNSTLDVSAQVLTLDNKSRILCIADVRGELSLINSLVEETNASCVIHTGDFGFFERSSLPSISERTLRHIVQFSPLIKKLPRSKNFDYYPSNPIGDLKNSIASHPDCLLSELPQFLSQEKKFSVPVYVVWGACEDVHVLEKFRSGEYSIPNLNIVDELHSYLLQIGDMKIRLLGLGGPYVPFKLFDNGDGKGTIAGGQGTMWTTILQMGELIETAKSLLDREEARIFITHHPIGREGVLSQLATACQADLTLSAGLHFRYGASYNEFCVNHSPEHYLQKLSAARAQFMEVYDTVKAEVEKMVTPEQHHLINNVVRLVSRMPDATNSYAMNNMLPGTAFKNLWNFNLLDASFGWTVFVVENGHVQVESKSHGFNLGYRRMASRRNENYASHIPRSTSENTGTYYYANNRLVESQAQFTKNREATATPTEEEQIEGYDQEHTDELGMSRANTTEESAETHEVIEEKSGPPAAEEEPISGVAEKPSPNEEEQPAIGGKEEVDVEEVTKGTGNLELGETTTEVTILEQENAANVTRSQAQEGRRTDMQKGNDREFRQYSGEQRYERCGFHITPCNSEEEARSYFKDGTDSLITNIQIRTSLNRYKSPQAPQNVNPTNYAYVFVENQNAVSKALGSIKVPEGVRVNIMRDDSYYRQNRGWYRNNRMEGHGTGMRTNRGRGRGGRMNRMQHPRPLQSGGSVNKQSAEPTTHG O42953 YGM4_SCHPO SPBC19G7.04; CHAIN 1..362; /note="HMG box-containing protein C19G7.04"; /id="PRO_0000311770" MQVSNSMSLNDEEDDIEFINYIPLLASPINSSTCSTSIHDKCPFKQHISENGQNFGSAISSNISQRNFKTLRASHLSQYRDCNRENNTEDKNVISTGIAVNEKYQSVLKLKEKAPQISSAAKRKSFIKERGMLAKCFLARLEDEVFQGRLTSSLEKKEIGIVWSKSFSTTAGRANLKRNNKDAPLGKKTYAYIELSDKVIVTKERLYNTLAHEVCHLACWIIDNEMQNPHGACFKAWGKRIMNNMPYIEITSKHNYDIDFKYKWLCINEKCNKLYGRHSKSINPQKQVCRLCKSQIKQICPKIKQPNAFQIFLKENSKRLRKLHPHITHKELMKKLSDEYHRTKDAKQNVSKSVSLISSSDL O42965 YGMH_SCHPO SPBC19G7.17; CHAIN 1..475; /note="Uncharacterized protein C19G7.17"; /id="PRO_0000116763" MGGARFINFIKPLSSLLPEVEGPKTHLELVEKLGWMAGCVVVYQILSIIPVYGAEKTDTLDPINNFRVLDGSSASGLMITGLAPIYLSSFLLQILASKKKIAVNFNLIIDRVLFQNAQKVVSALLYLILAVTYVSSGYYGSFSDLGIFRFIMLILQIFLPGIVCIYLCEIIEKGHGLGSGPVLLLGSHILGNIMWDVLSLHRYPVNESGDSQYQGALVGFAFNLFSFKNKFSSLRSILFRSEGLSFVQFLVCIAVFATFMYTLNIRIDVPIRSSRVRGVRQNFPLKLLYTSVIPLIYFYSILSHLLVFAYALYSLCPNSLITRLLVQYSPIDTFAEHKLQLVGGLVYFLYPPLGLSEALLHPVHTVIYTITLICITIYFSLLWMNATAGGPRDVLLFFKENQLVIAGYREATMLKELEKIIPIAAKLSAFFVSILSVIAGIFASTFGVGVLIASALVYASFEMIVGANTSLGNGN O42970 YB95_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPBC1E8.05; CHAIN 17..317; /note="Uncharacterized serine-rich protein C1E8.05"; /id="PRO_0000014192" CARBOHYD 42; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKLSFILSTLVAGALAYNEFSAPGPNAVLQEGGGVNTVSWSNLTSSTVTLTLYRGGNSALTPIETIASDIDNTGTYLWNIATYYEAADDYLLGLSFDGGETYSQYFTLQACSTCTISTSSLSYSGTISSTSIAPSMIGTRTSSSYFITSSSSTPSSSSSSSSSSPSSSSSKSSSSSKSSSSSSSSSKSSSSSSSSSKSSSSSSSSSKSSASPSSSKSSSKFSSSSFITSTTPASSSSSGAIVSNAKTASTDDSSSASSATSSVSSVVSSASSALSASASSASASVSSSASSDASPALKTGINALVAVGVVSAIALFL O42972 YGZ2_SCHPO SPBC20F10.02c; CHAIN 1..600; /note="UPF0588 membrane protein C20F10.02c"; /id="PRO_0000339159" MHRAAAVDTTPKIVFYYKCLLNKNWNEPINNIFWGEFFLLQPRLEVLSQLLRECPKQELTVNGPKFHSMYLYISEILKSKAESLRIRNSLATLQTFLAELSVRKPTDVNFTIFLLLGNIDSIDIQFSAFIKNLCQLVKDSEDVQSVEISLRFVLHFVSFLYNSSFISHIYGNYDVFSTLYTVILKRKFGFETAVYAIGLLSACDKFETVNTFRLGLSKIVDEEFFSSVLSSSAQQLISLRDFYVSIKPDNPLTGSFFNLFSLRSSSNNPDSDQESQFSRLPDERATMFFTIYELCCCNKLFLKKLVEGGEKNGEAPLEALLSLLSYINTHQRQSERSHHFSILSLILFHIIIDDRSLLYRLTDKKFKISVRVCSQRYPYPPNATKPATPLGYMLDICCIGIQHNMKLNLSATMYFLYFSFVYRAMTSLVQDGIRMEYHWLELWRVLFSFLDFVSVLINTSPTEDVTRLLELILDVLAYIISNGDALVIRSDELVDLFYKLLHSSKNFSSFSSKIPDERLGALNYLLEVTEYLTSKTVDLPRSTADEVESVIKLELESIPVAKQNAFGGVPPFKESQYRLFHKRASRGMADLLRRKSEAAN O42973 YGZ3_SCHPO MOD_RES 393; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 397; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC20F10.03; CHAIN 1..446; /note="Uncharacterized protein C20F10.03"; /id="PRO_0000339410" MGKKDGKRQLMSDDDSFDTISILSGSMDQLSVGSMEDSGILKGSKTWLEELESTIDDLIEVKKIGAKEREEHLEKIYVICTRHYAKRISENVASLEELLLKIFNGPRSDKELILTIRIMCTFCLASVFQVEELWTKTEGRFNALANDAESSGIKCESILCFSLLTALLDSEADVIEFGDFLISILESDGAVVNSEDDEGVVGCACQALGLLLTCVTTESEFLASAAEALSEQLDAASIDVQLAAGQALAALFERVNEIRPDKDEENDESDVSQTSKFDDIIPDRNQLLITLRDLASESSKSIGKKQRKVLHQVFRNVLQTIEEPNARNILRNSVRIGQSTVQLDSWKKILRAQMLRYVLGSSFSEYFAKSTFIRYFLGYSGYVAGLSSRDPDSDFDSDNVDEYIDDHKRGLSSTERRDLDRVRDKQKKQDQRVRADYINSVYFSQN O42977 RTP1_SCHPO SPBC20F10.08c; CHAIN 1..747; /note="RNA polymerase II assembly factor rtp1"; /id="PRO_0000372364" MDANQKLLDFAKLLNQKNDSRPVIEKLKDNISGDLLNYFLNLLEEISKLDTDQPLSVTSLRCLQLFVHLTFLLGVYTQLPKEMLSQAKIKALPIYTPKKNLVQIYNILLPLLLTPSLLQGPLNLHYADLLLLHLYLLNCHEQGSLIEEPRPLFLDPSWKEKVTSIMSPQMVDPSKMISSCLSLLQPNVDNWLQDKLKHYLTTCLCRETGVQGFLKVYMQAQPNSIERARQAAHLISSVPKDISPQKYFSCILPQVWSLFSTQPRLASQLIIAVTNTHCDIVTSFLLKKLQILEAPKVIDLSPFENALDVLQVLVYIQNDDIIRICESCVPSLLHLQENTTLRSKVQDILLRIISVCGTKSLLRNLTNAKHLRIFCERLTKSQLAMFLPNLLEIWVQQPPDKRLELLELVQYALSNVDSDEIPSNVMLSVCTNLINEVASQNKYSSTEISQITTNREVEEENEEILLVLLNIISSVIGRNAELDLENPISSLLPALEQLSNYSNREISDLAKDVYKTLIQSKDDYSLALSYTQSDLVPVRGQGVYMLRKLIEKKDDRINPVRVLHVLINLLRDENSYVHLNVISAVVSLCDKYDDSLIRLLKEYTNTNKFTVDETLLIGQAIYQTMERQGELVAKFYGQIEQTCLSMLNNENTDIKISSLNIARLLCQMTSSDAFIESAKNILILEMGSDKQFLRRAAVQLLDSCKHLPDSVITTLSYVGSHDKDDFIKESCLNILANQADAAKYYLQ O42996 YBC5_SCHPO SPBC27B12.05; CHAIN 1..482; /note="Uncharacterized WD repeat-containing protein C27B12.05"; /id="PRO_0000316547" MQRDLTVDEFLNYLYINVKELFTLKEKSFHFWRNSLISCSKTKNFLFVVVGDEVLVYDLKEISSDASEPEPCFYLHCPHEASSSRQGDINQDMPNVINNVRCELIGDLEYFITANDCGKVAIYDVQKLNREPIIYDVQHSAWGLAVSPLRILGISSNSHNVNLFHLSPEFKRFKEDYHSPWFRQETLVLEGHEHNIPCITFNSSGTLLLSGSIDRSLQIWDITSLSCLCKFYTKLSIWGVKFIDKNAFYHISILKHKPGSLIPAQQFGQSPWKPPIMSSSAFLLSHEEDFDDDAVFEGEYYVHIQDELPKTKVKNYFRTYLRQKPEELFIFTTKFSIVLCAYMGNSQIFPLVSSKNCFEEPITPRFQALHRINMIECIPELQSVVCASQSGQLTLLRLICTTKILNGNPIYVYSFVPHKIRLTHLVDAPLLGMSVCPLYPGEENPFKRFKIMLTVYTGKVISVEVQLSENLYDTSHIGNIPL O42997 YBC7_SCHPO SPBC27B12.07; CHAIN 1..290; /note="Uncharacterized protein C27B12.07"; /id="PRO_0000372351" MFSLLRKAIDVNRSRITLHGIKVHSINTFRLIPYSLSLTKQIRFYASEGTDAGEMEKGLSVVNANHENRPFRDLEGYHFNTFTFLKTLMDKGYTEKEAEGLLEVTNMFVTDMLRHSHLNYLSEADFENCSYLFRTALSELRSEKINMRKDQISSLRSGLFSNQREVESLEQLVHEQLNKLNTESKMEFENRKNDTKNEVQQLSARIVELHNLLAVSLGKLRAENERQKWDQIRKAAGVVMAFTGFLVLVIPFGLGVRSRKKEKQDELDNLGSFNLDNKRDDYTDTNLSHM O43006 MU178_SCHPO SPBC2G2.07c; CHAIN 1..225; /note="Meiotically up-regulated gene 178 protein"; /id="PRO_0000116520" MKFPDLLRCSRAVSLARPDLPRNSPDVYDTKIPILQAITAKKCQRFRGDWGAKRKLPILKNRHISIQKFDTFEHQCAFISSDRFVRTLKRIYDLKLPVPLNDYEQISPYLLQKYNTFSSSNPKSRPTLPPGILYAKLKLLDSFSDSEKKRLSLVSFIQTKKVPLPFTYGKFAPDSKECLFGVSGVIAATSLKGITSTKNRYVIRSLNVDETGKTIPNITRENRSI O43009 MU110_SCHPO SPBC2G2.10c; CHAIN 1..248; /note="Meiotically up-regulated gene 110 protein"; /id="PRO_0000278621" MVESSDENDQASSFASTEDLKELRFVFWFSVLIPIFFIALIIIKRYHSCTYQKNRLLRSIFCCMSIDDEEELETDMYDLPIVEPSITLPKYSASLQENERLVGIEGEREGIDVVLNFSKAGEGGVNPYPSFDTPNARILQLRQLAKLKKHGPRISYHGIGIGRCNGNRVLPPYPEPALLPEAPNTREASNNTYLYGFSNNFINISRTLNLRYPSASASISDSLPPPYQVLSVPSVTSTHAFSNNANQT O43015 YBOH_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPBC2G2.17c; CHAIN 20..319; /note="Probable secreted beta-glucosidase C2G2.17c"; /id="PRO_0000310373" CARBOHYD 36; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 39; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 45; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 48; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLFNNFLCFAVSAIPLVSAMPLGNAPYHHHHHAGLNASNITVGVNVTNTTAFSKRDGGFPDGVYDCSSFPDDQNGVVRLDYLGFGGWSGVQKNDGKYGTASTCQDNTYCSYACKPGMSKTQWPSEQPDNGVSVGGLYCKNGKLYLTQKDNSNLCEDGKGTAYVKNTLSSNVAICRTDYPGTENMNIPTNIDGGSKQPLSDVDEDSYYNWGGKKTSAQYYVNKSGRSAEDVCVWGNEGDDYGNWAPMNFGSGYTDGKTWLSMSFNPLSSAKLDYNIRIKSDGGSLSGDCYYEDGSFHGSTADSSGCTVSVTGGNAYFELY O43020 RT16_SCHPO SPBC354.06; CHAIN 1..96; /note="Small ribosomal subunit protein bS16m"; /id="PRO_0000167325" MVVKIRLARHGVRNRPFYHIVVANAWKAPQAKPIETIGTFDPIPKKIDSQDSIPRIKDIQLNVERFKYWISVGAQPSDTVRSLAEKFQLLPKKPVS O43021 YGV7_SCHPO SPBC354.07c; CHAIN 1..397; /note="Oxysterol-binding protein homolog C354.07c"; /id="PRO_0000100393" CARBOHYD 186; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 195; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSETSEQMEETVQSGNEPISKSTWMGFIKNLATFTGDLSTLSAPSFILSGTSLLEYMSYWFEFPELFVTIVDFPTPKERMLAVLKWYITGLSREYASRNKNYGTEKKPLNPILGELFYGSWDSSKGKVELTAEQVSHHGPESAAHVVCKEAGITVDTHNKYRSGFSGRTVYVNQLGQLRVHLEKYNETYYITLPNISLEGLWFMAPYIELYGSTYIVSNTNYITKIDYSGRGYFRGTKNSFKATIFEKNEDPDYIVEGVWTGESKLTIPSLKSTIFFLSIPSLEATPITVKPESEMGDWESRNVWKEVSAALASGNYDIVSSKKSTIEQSQRDMRKKEEAEGAVWARRYFKWEEHDSDARNALAQAVLEVIEPGFWIYIGDTHPSLPAGEQPVKRME O43022 YGV8_SCHPO SPBC354.08c; CHAIN 1..865; /note="Uncharacterized protein C354.08c"; /id="PRO_0000315636" CARBOHYD 128; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 147; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 151; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 624; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 802; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 853; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MVIEKRESFIEVVINSLLNDNPAQAKFDKYSILVSLGFSSLLSVILLCIFTLLRTKFNTYDRCIPPMKKSLWGWIEPLWSIKVEDCLYNMGADAVISLLFSRFCRDVFLILAAICCTILIPINIVATNKTLANSDSQNAYAKLSIQNVTGNWTWAHVVICYVFNVLVLFLLARYYQIVMRIRQRYYRSPTYQQSMSSRSLLIMDIPTTMRSNNGLSILASRLKSSEAPMHVHICHAIKNLPKILKKHDNAVRSLEAVLAKFFKNPKKLPDDRPVRRVKQGLLTSEKVDAIDYYSAKIENYGLRVDAARESLYENEFEHYGFITYKSSYIAHDTARHNSRVAGASVSMAPEPSDFLWDNLSLAWSTRLFNRMIGNILFIILIIAWIIETALVAIFISNLYHLGSVWPWLQQQLTSRSGFWSIVQGILSPAVAGFTFMILEIIMRRISYWQGSFTKSSRERGVLNKLHIIFTLDNFIIYTLMAVFWRLGVIIAYKTKEEGNFAEGMSAFATFDTVGLSVSSFVQFSTFWIMFIAHSTCSFFVEIAQPITLTIRLIKTKFFSPTPRDLLEWTAPTKYVYSQVLNKLIYFFTIAICYACINPLVLLFASVLFCVNYLTQKYILMYVSNSSTESGGGYWRPVVNRILLGLELANIILFLCLWVQGGRVRAYCIIPNFSFAIAFKIWCMFALDPKSHYMIEDPYMKVVEPLENEISESEMCFGHPSTYAPLLVPMVRSDARALLPLFYSGRTETHNKFDFATDSDDASEKHLRGEEEPLENVDFVDIDNVDTAKEVHDQQQVQQLKKNLSRSYTRSRGVSLRARLNEEELPLTESITQDSQISIPETLESQSTEITPINVSEHYDKYYHIF O43023 YGV9_SCHPO SPBC354.09c; CHAIN 1..794; /note="Inactive zinc metalloprotease C354.09c"; /id="PRO_0000174141" MTDEKHVYVPPPKDPPSYEEVALHSALNNSAPPNDGEQNETSMEEMEIIEPPSEDSSRFPLLRTKLAAIHEGWESACHSFEIRFASTFHRIPFQFLYLAVIATVIILASYYGYFDGVPAWRSVHHYGEDVLLNYIKGCDISDTRQQVMTLSSIPHLAGTVGDSSLLQMIMNRLYYEKGTIVDFREFYAYLNFPQLVSLSIDGDDSFHPSLIESYQVGGYDGVSIPTPATFGGSPSGFVNAPLVYANRGRIEDFEWLVNSGIYVESSIVLVRANQSDFALATANAEKYNASAILIFEDTYLTSLDNLNQVYPAGPYPSANSLYRGSVANHYYYVGDPLTPGWSAHEETNRISPKDANVLPSIVSIPITFNDGIELLKRLQGHGHLVKDSNWCQDLAPVLSEVWTGSKISSPGLEVNVLQDIEDKQKIINIMAQIDGYESDQILVVGAPRDSWCTGASDSSVGTSLLIDVISTFANMAQDLSWKPRRTIVFASWDARQFNAIGSTEFLEYWKESLEAKAVAYINVDVAVSGDTFTARTVPGLKKVIQRAFDVANEEDEMKAANIITDDFDYTSDLTSFLTFAGIPVVNLAFERNEENPTPMPFLGSCEDTVSWIDTFGSEYWENAARLGKIWSYLILFLANDPVVPYDLEDEINGVGEMLKRIPEIPGANALDLRKINEEFSELLESLIRFEDEIREWKSLMMHNSYTVSVKKHPELEGYNAKLARFERSFLDEAGLPGHEWYKHLIYGPNLRNSHSQLFPSIFDALLYGDVEAAQKEVKRIALALDRAHNEIRFA O43033 YGU4_SCHPO SPBC3B9.04; CHAIN 1..248; /note="Uncharacterized methyltransferase C3B9.04, mitochondrial"; /id="PRO_0000339156" MGILKKTIFIGGIYGLGVYIGAVAWRLRKDVLNYESRQKSDLLIPNSNSISIYNQIADKYSRKITREEIFSGIYFLRYFLLRNAKGDVLEVGSGPGTNFPFYKWKKINTLTLVEPAEKMREIADARAKKKVPPNVLYRQFADLRQLPPNQSYDTIIQTFCICSQEKAVEQLNNYRSLLRSDGRILLIEHGKGKYKFLNRILNAYAESHYESWGCVWNRDIEQLLEDSELTIDSCKRFNFGTTYVIEAH O43034 YGU5_SCHPO BINDING 2; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 4; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 16; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 17; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 23; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 26; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 33; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 45; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 48; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 67; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 70; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" SPBC3B9.05; CHAIN 1..116; /note="Uncharacterized protein C3B9.05"; /id="PRO_0000310738" MCKHVLNAQVSIRTACCRRWIDCIECHNEIADHPLLKTSELTLICKKCRKAFRIQFDQTMDESDEYCPNCDNHFVIDAITKVEKPKAPISPKLDLRMLNQEEKELEELLDETTRLG O43037 MGN_SCHPO SPBC3B9.08c; CHAIN 1..147; /note="Protein mago nashi homolog"; /id="PRO_0000174155" MSDFYVRYYSGHHGRFGHEFLEFDYHSDGLARYANNSNYRNDSLIRKEMFVSELVLKEVQRIVDDSEIIKESDESWPPENKDGKQELEIRMNGKHIMFETCKLGSLADVQNSDDPEGLKVFYYLIQDLKALCFSLISLNFKLRPVKN O43045 ISA2_SCHPO BINDING 131; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P0AAC8"; BINDING 196; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P0AAC8"; BINDING 198; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P0AAC8" SPBC3B9.17; CHAIN 1..205; /note="Iron-sulfur assembly protein 2"; /id="PRO_0000077037" MLMKSRVNLLFKGPFFFRERCFQTLLNPVIAIRQLSHGSLRNSRSCRIDAKSNTLTKEIFPKINNEFKIKNRFYSSKLANDQFTLQEQCDEKGIPFILYVKDSAKKQLEKIAERKPEENSVLRVTVDGGGCHGYQVSFRMDNKIGNADTVFVRGKARVVADNISLPLISGSEIEYTNELIGSSFQLLNNPRAKTSCGCNVSFDVE O43048 YH51_SCHPO BINDING 589; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 591; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 593; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 595; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 600; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 625; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 627; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 629; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 636; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SPBC215.01; CHAIN 1..834; /note="TBC domain-containing protein C215.01"; /id="PRO_0000353839" MSSLASLIKTKLKLPDSSKNLNKLRWKFRLLESQFALYSLPCQLRFVHYNNLEDPNSFNGLLYLFTDYIAFQGDDESNQFCMPYTIIRKVSRVKSNDLEQLLSVSTSNGYEYRISLQVSETTAAHFCQLLREELVSHKADMQRSSEFSKQFFSERLCKPNVPEPETKDSYGFGARYGYPTDPRISRERAKLRMWKEYFLLYGANLSLIRVSLFSKLVRIELPNKLRGEIWELTSGSMYFRLENSDEYDHLLKVYSGQTSFSLEEIEKDLGRSLPEYPAYQNEEGINALRNVLVAFSWKNQEVGYCQAMNIVAAALLIHCTEEQTFFLMHKICEDYIPGYYSKTMYGTLIDQQVYESLVQRSMPNLHAHFVSKDIQLSIISLPWFLSLFLCTMPLPYAFRLLDFFFLEGPRVLFQIGMAILYDNEAEIMKATEDTMLISILKNYFSSLGDKAYKDATDKRVASITKFQLLLVTAFKKFSHITHSLIEDERKKHYEGVMNSIESFAKRTQIRSLQNYGTLTRTDLSNIYDRYHEVLSSKHRVGLGSSTDTRLEFDEFCIFLAGVTEWAKGLDAAAINNSSSFLRHLFLRFDKSMTGSLSLQDLVSGIAELKFRDVMRNISFIFELYDFNGDGFMDKPDVLKVSEAILWLTRFMGDEYLSAVSEFIQRCFHFADEASPDGHSDTLIDISDHMSSTGSENRSVGANSDIKVSLPTFRMVVLSIGLLEQLFSGGLADSIVLAPVQEKSSTTGGLRGLLDSLVIDTNRIGKTFRGHKPASRPSTANGTSNQNTTSEITTSETTATEKTPSNSSDTEDDVGDVVENDKDLLQFDPYKKNDA O43056 KHSE_SCHPO BINDING 93..103; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" CATALYTIC ACTIVITY: Reaction=ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine; Xref=Rhea:RHEA:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57476, ChEBI:CHEBI:57590, ChEBI:CHEBI:456216; EC=2.7.1.39; SPBC4C3.03; CHAIN 1..338; /note="Probable homoserine kinase"; /id="PRO_0000156655" MQKFQIKVPASSANIGPGFDVLGMSLEEYMTLDVEVSTESGPCVLTYEGDGKEHVSLDVQKNMITQTSLYVLRCNNISTFPYATKIHVINPIPLGRGMGSSGSAAIAGVMLANEIAKLGLSKLQMMDYVLMIERHPDNVMASMMGGFVGSFLRELSEEEKNAFSPSADDLLKNEALTLPPKSLGTFARLPWASELKAIVVIPEFHLATSKARSVLPTSYGRTDVVYNLQRLALLTTALGQTPINPHLVYEVMKDKVHQPYRASLIPGLQNILATLNPDTQPGLCGICLSGAGPTVLALATGNFDEIAHAMLSIFEKHGVKCRYLVLSPAFDGATVKYF O43057 MSS4_SCHPO BINDING 8; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"; BINDING 11; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"; BINDING 73; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"; BINDING 76; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01132" SPBC4C3.04c; CHAIN 1..100; /note="Guanine nucleotide exchange factor MSS4 homolog"; /id="PRO_0000174179" MSNLRIVCQHCPSVVFNNKRPDVVKRPTMSAMLHSETQEDLETDDFFLLKDPFAFDNVSVSKPLANNYKLLACADCEKGPLGYYDSKNNEYLLLCSLEKN O43067 YGA3_SCHPO SPBC6B1.03c; CHAIN 1..272; /note="Uncharacterized protein C6B1.03c"; /id="PRO_0000343220" MGKNNPFVHSNANFPPLQTHNFEDIPEKGYTIFSSPRIDVFNEERPHSGINLNQYQHHEDDAELQSNNPFLNKDSGVDLLKLHSRSNSRIYEAKPKRVIKPKIAIIECNEMAENPPFWNQNKAFERKVSSKESFNMLGYDKIDKLDSSNSYLGDFGVHHDGPFDPCSKHRNLDAATSPIAAFSSQSEANSLPAFLLPNNSKGVEKSEENEDGVTDNDSSNVNSSTNESPNPTDINVCSNDDATDNTENNLKKKASFIYRLRKHLKRNSIETE O43073 YGW2_SCHPO SPBC8D2.02c; CHAIN 1..170; /note="UPF0220 protein C8D2.02c"; /id="PRO_0000174186" MTLLDSSIFRFRLSSLHVSSRSLGVYFAGIMFASAVWVFVDAALYSAFDYARNLHITFIDWIPFLCSILGIVIVNSIDKSRLSGDSFAYTDESLARKARFILFIGFALLAGGLGGSFTVFILKYVVAGYEGKSLLMGSANIISNILFMISATALWITGNMNDDYHYNLQL O43075 YGWC_SCHPO SPBC8D2.12c; CHAIN 1..293; /note="Probable transcriptional regulatory protein C8D2.12c"; /id="PRO_0000357023" MNALNKIPFTRALYHFSRFRSFTTSGWIMSGHNKWSKIKHKKSANDQARSLQIGKLSQGIILAVRQEGANPELNMRLATLLESAKKISMPKSGIENAINRGLGTAGSEGSQVHFIEYEAMHPSGVGLIVEAVTDNRARAASSIKHILRNHGASLSTVKFLFSKKGKVEVNLPPEKRDSMKFEDVLDDAIEAGAEDIVNRPKEYIDEEDEGEFLILTEPSSLNQVAHHFRSKNYEIKDSRLIHIPLEETAIDVPAKDSVREDIQKLIDDLYENEDVMFIHLSILNSHFLPILDE O43081 YHS6_SCHPO SPBC947.06c; CHAIN 1..498; /note="Uncharacterized MFS-type transporter C947.06c"; /id="PRO_0000343519" MKENDHLNSVSSSEIEKCDEDVEEELYSYPDSDFLVTFNGEDDPEKPLNWPVSIKLLNTALYGLTTFAAQFNSTTMSPTTSHLVNAYPIGHEVAVLPTCLYILGIAFGPMIFAPFSEVNGRKIGVLVPFFLSILFTIGTASSDSVAAIMCTRFFAGLFAGAPVVSSGGVMADLWCPAQRGTALIFYAFFVVSGADFGPIISSLVTEHSDTAWRWPLWTIVIIECFILTLDVFLIKETFGPVILATKAKNLRLTTKNWGLHAAHDEYRLDFKEFVTLHLVRPFAMLATPIVFFIAMFASYVYGILYLVLTTIPYTFGMTKNWQGTISTLPMIAMFTGVVIGGSFNIMWNQRYAKLITANGGKPLPEQRLPLMMAVGWLMPAGIFVFAWTNSPNIHWIAPFIGISMMGAGFFVIFQGCLNYLVDTFTKFAASAIAANTFTRSIFAGTFPLFSEIMFKKLGVHWGGSLVGFIALGMIPIPFIFYMMGDKLRRKNRFIKLIT O43084 HSP33_SCHPO ACT_SITE 162; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 163; /evidence="ECO:0000250|UniProtKB:Q04432"; ACT_SITE 196; /evidence="ECO:0000250|UniProtKB:Q04432" CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000250|UniProtKB:O74914}; SPBC947.09; CHAIN 1..261; /note="Probable glutathione-independent glyoxalase hsp3103"; /id="PRO_0000317305" MPAKTRNVLIACSDYYGPFYKDGENTGAFFLELLHPYLVFRDACFNVDIVTESGKIQFDDHSVAGPAIDKGSKGEEFLSYDDHIASGPELSKAEKYVLENKDDMFWRIVQNSKTADEVNPDKYDIFFVAGGHATLFDFPKATNLQKLGTSIYENGGVVAAVCHGPTLLPFMKRQTSDGSVSIVCGKDVTAFDRVAEDKSKLMEALKKYNLEVLDDMLNDAGANFIKSPNPFGDFVIADGRLVTGSNPASATSTAKTALRVL O43089 CBP6_SCHPO SPBC947.14c; CHAIN 1..103; /note="Cytochrome B pre-mRNA-processing protein 6"; /id="PRO_0000116781" MSLNQKITKAVALWPKDELRPWLSFPKTLDTSIRARLQKMPPQQANKQLNALNNLLDNVYWNKYIPKQVVLKPQFKPSYYESLTQIRRKEEKAPLWKRLFKRK O59668 YB83_SCHPO SPBC29A3.03c; CHAIN 1..398; /note="LisH domain-containing protein C29A3.03c"; /id="PRO_0000372348" MNIDEWQRIEETAPGNKCLAKLNELESILKDAKKSCLKDPTTSMKELVACSEKTQQVFDDLKRTEKKFHTSLNRFGKTLEKKFNFDLEDIKLHSSFESKKREIDTALSLHFFRQGDVELAHLFCKEAGIEEPSESLHVFTLLKSIVQGIRDKDLKLPIEWASQCRGYLERKGSSLEYTLQKYRLVSNYLTTKDIMAAIRYCRTNMAEFQKKHLADIQKTMIALFFCSRNEVLSGTNDSHDSIHHIISNNAQLNIPQEYIDVLDLDWKSLELLFVREFCAALGMSLESPLDIVVNAGAIALPILLKMSSIMKKKHTEWTSQGELPVEIFLPSSYHFHSVFTCPVSKEQATEENPPMMMSCGHVIVKESLRQLSRNGSQRFKCPYCPNENVAADAIRVYF O59670 SF3B6_SCHPO SPBC29A3.07c; CHAIN 1..115; /note="Splicing factor 3B subunit 6-like protein"; /id="PRO_0000310809" MPPSTVNQEVNSILFIKNLSFKITAEEMYDLFGRYGPVRQIRLGNTVQTRGTAFVVYENVQDARRACEKLSGYNFMDRYLVVHYYNPERAKVDGQDLAARYAALEQVKQKYGVQL O59672 YB89_SCHPO BINDING 215..222; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"; BINDING 551..558; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPBC29A3.09c; CHAIN 1..736; /note="Uncharacterized ABC transporter ATP-binding protein C29A3.09c"; /id="PRO_0000310285" MEQVIQNNCSEVDPHVLSYCTGYANDAIKDVDEASDHTISLIRNLLLDAGAREEAVQLIQNELEKQFKEREEHLDTLQTNGLVRLKETIRMDSQSEISSTMGLVGEKMELDAVKGRKVESRVDRRKLEKAERKIRAKWEKRTIKAEYESSKLVQPEQKSYEEFYMAVNPLDLSGSNQGKSKDIKIDGIDLAFAGHRILTGASLTLAQGRRYGLTGRNGIGKSTLLRALSRREIAIPTHITILHVEQEMTGDDTPALQSVLDADVWRKYLIQDQEKITNRLSTIEKELEELSKDQTADQAISRRLERERDELDLRLLDIQNKLSEMDSDRAESRAATILAGLGFTQEMQSHATKTFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAFLSEYLQTYKNIVLVVSHDRSFLNEVATDIIHQHSERLDYYKGNFSQFYATREERCKNQLREYEKQMEYRKHLQSFIDKFRYNAAKSSEAQSRIKKLEKLPILEKPQTEEEVEFEFPPVEKISPPILQMSDVNFEYVPGHPILKHVDIDVQMDSRIGVVGPNGAGKSTMLKLLIEQLHPTSGIVSRHPRLRIAYFAQHHVDTLDLNLNALSFLAKTFPGKGEEEYRRHLGAFGVSGPLALQKMITLSGGQKSRVAFACLGLQNPHILILDEPTNHLDMESMDALTRAVKRFQGGVILVSHDVDFLDKTCTSIWQCDHNVVSKFDGTISQYKKFCLSQQPTMTIKT O59673 ATP14_SCHPO TRANSIT 1..26; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC29A3.10c; CHAIN 27..103; /note="ATP synthase subunit H, mitochondrial"; /id="PRO_0000339126" MSRILKSLSRSYSTTSPRLYVDVVQGLYISSLKSYKPKAVPSETAAEVKEWSMPSAPTAPKYDVDFTSALNSYKYEGETIPTKAAGESNKFDFLESYENEKEH O59674 YB8B_SCHPO SPBC29A3.11c; CHAIN 1..297; /note="Uncharacterized mitochondrial carrier C29A3.11c"; /id="PRO_0000310789" MGLPVHNQPHKAHSGSPASTFSAALVSSAISNVIGYPLDSIKVRQQTYNFPTIRSCFQNAVKNEGLKGLYRGLTLPLISATLSRSVSFTVYDSLKLTFAHVDPTLRYFISGLGTGTFISLFACPFEYSKLYSQIDMLLRKTNMGRRQETNSKLSVRPPLSSFQSASDIVRRYGFTALWNGYRYHLTRDALGSACYFTIYETFKKNLIANDVKPHFAYAFSGAFCGALSWILVFPVDTAKSIVQRNTLLSIKTPLSSIPWLSFTIYRGIGISLMRSALINSCNFTLFELFRETKVLSK O59681 YBS1_SCHPO SPBC18E5.01; CHAIN 1..342; /note="Uncharacterized protein C18E5.01"; /id="PRO_0000171147" MKLVIGTCTDGPVLVFDMETKSITEKLEGVSSPTWVEWEKKSKRLYVANEIEEGYVAVFEWDNGKFSLVDRFTIDGHSPTSLCVLENGSVLTANYNSASISRSKAKDEKPHVWHHEGKSLHPERQTSSHPHQVTAHKHLVCSVDLGLDRFSIFDAEDTSSDPVVVVNVPAGYGPRHIVFHKTLPVCYLICELANRILVYDTNTFECLQDVSTLPPSMTLEKDPKFPQPPSAAEVAVVHDGPFLVASNRYLNHGQCDSLWAARLDPVTGKVIEGTEMQIMLHGICPRHFMFNRGASLLAVAMQDDDLVHVYRREPKSMCLHLLFTIPAPKPTCVKFLEDEDLA O59707 UPS2_SCHPO SPBC36.10; CHAIN 1..184; /note="UPS-like protein C36.10"; /id="PRO_0000346780" MKIFESCHLFQYPFEQVSAAHWQKYPNEHATHVIAVDTLDRKVLDNGVLYTERLITCHQALPRWILKLIDGAQDCYIRETSYVDLKARTLTLLTSNLTFSDRLRVDETVTYSPHPELEATVFQQEARIEALACMKRLSNLIEQWSVDGFGKKASRGKEGFESVLEKINMSVFQTRPFGSSEATA O59708 YN4B_SCHPO SPBC36.11; CHAIN 1..343; /note="Uncharacterized protein C36.11"; /id="PRO_0000304102" MSISNDSLASTVPGDELPSSYPVFSSDFSYIKPSHVLDVVTVTSTAGPEATDDPSYSGFYSTVISTQNPEPTSASTPPSASASSLPNGAQKHNHTGVIAGPIVGVLGGLIVLVIIFYCLRHFKRKKFLAEQQEFERQFEEEKSRLAAVRKNTEQEKMGYRGGYQMHSTPWASSPRNSTIPQRSQSFYNDTRRSSDLGANAADFVTPPGNVANSDNIRILKRNSIATIGNYRSPSALEKRRSISYGAVQSVQGRPLAPIPGRRPLSISSDLYNDSNSGSHSNDDSDETKLKQSSTESSSELLDEKDKFDKNSLNDPFVTIRKSSYEHEISEEHKKHSKKRSEHF O59714 YBH6_SCHPO MOD_RES 147; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 161; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3B8.06; CHAIN 1..511; /note="Uncharacterized membrane protein C3B8.06"; /id="PRO_0000372353" MDGMHMNSTGDNPIEIDFENYANHMNKFLMAHIICMIIAYVFILPAGIVLAMAKSKAHIPVQIVYVILTLIGYIFAHISHHKASPENYYKGNIHRPVGRFFMWITFLIAIVGITTSILKKRMLKEYQPAAEAPGAMEDPEQALQRNSLDDGAPLLPREGNSSDEYLPPQSSRRDVSSEKPSIPSISFINIRSWRTIPKKWCVLQVLRYFHRILGHLWLYVGFFESCTGIVLLAGIFKGQHIFNGLAHWIKGAIFLWYGILSFGEYLGAFSEYGWAWNVVPKQLSEKRFAKYVPTKEMVESFLLFAYGVSNVWLEHLGNTDGKWNHHDLQHASLAFMLWWAGLCGILVESKVVHRLLNATLSATLGQRRSEDSEHSENGLPSYNVFPALTVFFTGIMMSAHDQTNHVSTVIHVLWGRLLAAAAIARICTYIMLYLKPPSSPWPTRPPTEIITSFCLICGGAMFMASSYDVVNKIRLNEMSPMLIMNISVAFTCIVMGLEVMFLILKGYASSR O59716 YBH8_SCHPO SPBC3B8.08; CHAIN 1..153; /note="Uncharacterized protein C3B8.8"; /id="PRO_0000372378" MLTQDEVSAQLGQYMLRGYTLLDTICPKCEKVPMMRLRDNPMFCVSCINDLKESDASEHVTVAESAPKIASLPISKTNDAERSQQTTKAPVMERTESSHQATLSVYSRLISELESQLDDRLPLPHNTEFLDVSLQRIERILNLISLAKSLMSS O59719 YBHB_SCHPO SPBC3B8.11; CHAIN 1..868; /note="Uncharacterized protein C3B8.11"; /id="PRO_0000303929" MSTWPIDAISKKPSVSLDYGIIGACQLLNPSGYHRAEKVENNEWTFARYDSYTGVELVDLDKRWDILSLNPNYKLPKLTELPAEATNSTRKATSSSFGLSVCRYVPRNLFSTLAKESQLASSAESIYNPHILNTFCLGKTAPSDKNRYTTTECLACSKISNETAENLLFLCLSSPWIFRASPTLQNTATFEEFPFYLNVSAFEFAEDPIWKFSQPVRQLVFSNGEPSLLFALSSCELVIFQVTYDLMFLDEPNTPGCLSAIPLRFLYADDVYNSDSFANVSVHPTDNSFFLTTSSSGRWTIWQFLDDGYRECFGSSFKESLQQALCSAPTSSIAYHEEEINPDNTIYRAKWEEYFGGVILHNAFFILHVSLGEVPDFHLLFHCSSDVRILQVVNESMPIKSEFFILTTESVLWMDIQHPQKPLLEWKHNRKLDPTLKITVTATFSQNIYVSVYSQMNGVVQQIHFSKDRALPVSGSHPFLLLNEVQVPIRSLIIQPCYFFESSEFDRQGPFDSPFWSAIIDKADGSLSLHILCEKSSLKIYNLEELTGSSQVAMKFKTITPSVNTSEDDSANDQEIISTPNSDFQQLSLSRLYHVLCSNRNKKNTITLDEFASKVPDFVEAFDSINHDVIITLSELYDGFPLKGTFTNVAEIISHLEGTELSFYFPYMFGINYNNASFFYTSVDSIASLIHRRWESNTDKSVEIPCFQSSQRRSIKNVIHYLFLSSIGVSREKIFDPSLSRKEIDSTDLLTFIKPFYDTEGLELNEDVRNILENWEIGKISSTYVIGDSAVETEDPSSSQFSDFYISQQQSSVLPSSQIATVFSQEDVPNFSSLYSESSSQTIPIMSQVVSGKYGSRPSKKKKKRSGF O59727 YHX7_SCHPO SPBC3E7.07c; CHAIN 1..147; /note="Protein PBDC1 homolog"; /id="PRO_0000339881" MLSTKIDAENAENAAEIEMQFAVKAVEQAQIYWSLLEMRKGSELKLTKYDDEIFEDLINTFPEFKDPKTASFVNEDEMKSAKGKAAWRPFLMRYEKKVDDYNFGTLLRIKNTDEYEQETTIFVPRMQFLAYEIARNRYGLNDWIKKD O59731 YHXB_SCHPO SPBC3E7.11c; CHAIN 1..355; /note="Uncharacterized J domain-containing protein C3E7.11c"; /id="PRO_0000310356" MVQRVVDRDYYDILNISVDADGDTIKKSYRRLAILYHPDKNRENPEAAREKFQKLAEAYQVLSDPKLREKYDKLGKVGAVPDAGFEDAFEFFKNLFGGDSFRDYVGELNLLKELCKMINEEPELKAIEDTEESKKQLQREESKEADRLLQERIDVLCKNLLDKLSIWTETDMSDRVTDAFKQKMQFEAELLKDESFGNEMLHAIGSTYVQRANILIQSQSFLGIRGVWGSLCAKGTLLKDTWNTVVSAVDVQSSAAALAKAEEGEEQWSKEKRDEAARELTGKVLSATWKGTRFEVQSVIRTVSDKILYDKAVPLEKRINRANALLMIGQVFLKVAPNEKSDANYFEDLMNDRGK O59732 CHR1_SCHPO MOD_RES 227; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 230; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC3E7.12c; CHAIN 1..456; /note="Chitin synthase regulatory factor 1"; /id="PRO_0000076205" MPASTSIPETPSKLPDALLVNSDPASKVDNVSVKIEQESPLALEGSPLPTVSDVLPETNNAHEEVSSSSWSLSSSDSIMSYDSLSDDVSVLSFLDCPLTTFETAPSIASFSNSAADVSSHSRSSSSWSAKLSRFTKHASKPSLSSNSSDSSFSKSGSESNALSSRGSFELEPHGIHRHVSRAKRLLSKFYSKFHHKKEDSSFDPLAPLVFAPNTSRVLRVTNEANASAISLEKATSLSSQEQPGSEIKKELSLYDHEFDQILDLAIKAKKDGNLENAIEFLEYIMPEVASQQNFVPYELAELYKQRGTSQDLKSILPLYMLAASLGHDRSSFLVGEAFFYGTYGARENKLRALQYYHLANDKGNADAMLALCKLYLRGLPGHIFPSSRRAFEYAHRAAMLGHAPACYVLGKFYETGVGCVKDLAKSEAGFRAGLINDSPITDADALQIASTLVLLQ O59738 YN22_SCHPO SPBC530.02; CHAIN 1..541; /note="Uncharacterized transporter C530.02"; /id="PRO_0000372791" MDLYLLASGRKFGVVKSDCISNNGVNVKDVGNALNEGVVGAIDATRKMVVSLGTVMPEIQKCGVTFEESSEDVSDFYLVRWDSIDDPLNPKNWPMWKKWIVVVQISLIAFVVTFGSSVYSSGIGNVSMDFGVSISVSSLGSCVFLVGFGFGSLPFAPLSGIYGRFVVYFCTLLMFTLFQIGGGCAQNIWTLVILRFFQGFFGSTPLSNCGGTLSDLFTPIQRTYVLPGFCTFPFLGPIFGPIIGDFICQSYLGWCWVFWINMIMGAVVIVIIFFFMPETHGDTILDYKARYLRNKTRNMKWHTIHERQRNPRSAIYQACTDSVSLLITEPIVVCFTLYLTVVYIIGYIDFEGYPIVFAKYSFDQGEIGLSFIGIGIGIVLAGACTPIIYVHYNRVYTRRNGVMSPEDRLYPLFFGSIMLPISMFWFAWTCYPYHPYVHWIVPLISSIFFGWSLLFVFFVSYNYIIDSYQKLAASALAAATLVRYAASGGMSLVGRPMYVNLGDHWATSLLGFISVGMIPIPFLFFIYGKKIRGLSKHAYKL O59741 YN25_SCHPO SPBC530.05; CHAIN 1..762; /note="Uncharacterized transcriptional regulatory protein C530.05"; /id="PRO_0000115013" MENLKSASPEEDSPRHGDNMGKPKRIPRACDMCRKRKIRCDGKQPACSNCVSHGIPCVFTARPKRRTGQRQMYIKSLVSRLEQMESTLRSVIPNYDQQPDIIHPSSTPKNYHDLNCTKGETSSDDSTDDIAFLNEKMGTLVTTPIGSQKYFGSSSTFSIIQHAAKFASGVESDKVLEHLSMAKSGCLFDPDESFDGSKAELPSSEIANIYIDAYFKSYNPLFPVFTRENFYQKFGSPNCFKKPDGSIDLVNYASYVVVLSLGCLAIADTEEQVSRANALFKNTLGISIEVTKDMSFRTLVFNFLTSVYYCAVSKPNAVWLNVGVVVRVAQTLGLHRNSAMWSIGKEDAEEKARLFWYIYYLDRVSSMMTGKPVAFQDDDIDQMVPFYSIYCYYGLKPPEGDPLGTFNFLEAEVQLTRIVGQVLKELYSVSGMKSNSSQVMEKILEFDLLLNNWYNSLPDCMQPRNRFKIPKFCSSNLILTSAIYYSCLILIHRHSLTKNLQVNCVHRGTGSITDSQALCIAAARSITNLFVESVDLQPLIMKIIMYHAFTSSIIIFISILKRPLASICSEDLNCLISVKNRLISFETHGFVRLNVVMDALESMISTAQAAMQKAKQIAINFSSNLATNEDVTNSGMPDIADVSLKSQSHVPPRISSNHSDTSVKSNSPSSIFDNSGYLNSLNNSILQMHQNLQNSSNTNDQYKFDSVQENELHANITPVLDQTMSMFPFKDQLDLNFAAANVYNPNVFDDMGLDCSFYGNGL O59742 CLU_SCHPO SPBC530.06c; CHAIN 1..1173; /note="Clustered mitochondria protein homolog"; /id="PRO_0000123556" MSTIDLPTSSLPGSSGDPSGTEMSHSDVDVSVDIDVIFPDHTQTLSFSLLLSNTIHDVRQVILELMLAPPHTCFHLEYKREKLHSFLEIGQIPHLKLSKTRKIVLEVVLDPYTERESKYHIYTLLEFLSRKLPSSSTSPGIRAGFCIFPSLNIPSGENLQIKSSSSLEEINKIPENIVTQSLSYTNLLKKFETSPNPSNNGCFRSLALSGWNPVPAEFVIQGHLLYLTVLTIEGKTYNITSHVSGFYVNNCTSTKFDPSPCDDLQSHSLVLLLEQLSPLFKERLHLSLNDYKSGDAIAQASITGTLPQAPWITFPVPHRADLSRTQKSELFPYIENQGNLRDWNEEIQSTREMDHEDVQDRVLRERLTVKTLQDFTDMAVEGAIDMVNGNIPSLNPLEPTASQMFVHNNIFFSYGRDSVGIFSTKGGDSAAYSAVGKDILAIRLLNQFDLSNPSLLGTCVVDYAGHRVVAQTIVPGIFKQLENGSSHLIYGKVEGESDFRFDESFEGELSRISDLLHIKKHFFVDGKEKSFPLYTSMDAKALKGSDGRTYLMDLYSLFPLDAQFLEVISDEKNEEFPAYPHKLVHVRPELVQLFYEMKLQAFVNANHNAPKKKNLNDSLKSVELEGNGIKLSSEKGKNNVNKVRNDNARFDCGFNPDCFRSDYIFPPDNKELYDKDIENSYALSQYLHAEVIPNFVKSLSEPSSFLPIDGVALCRAMHRSGINIRYLGEIANIILQKSPNNVILLKLVTSEIFIRSIKHVFRNFLAVVPQVLRSHLLSHLLNNLFTVYGYVEPTKPLINENIANLFFQATQVIYSINSTSLYSSIKKEASSRFRFNLTDDLLHSLNPICILRGTCLRLGIQISCKDYFSNKSDDKICEEHAVPNGSTKFTGKKGNKKKRNLGKSQNTTNRQVESEQINIFRPKDILNLMPVIKTCIPYSGLAQESLEACKACLLQGNKELCYNLLNESLSLHEQIYGVLHTEVARAYCQLAMIYHQLEKKEEAVELARKAVIVCERFLGFDSSETSLAYMNLSLYEFSQKNEMQAVMHMQHALKLWYLVFGPDHPNTINSFTNLSLMLHGSEKFIQSQKCLQIAVDLSDKIFGKTTPTASLYLQLAQLMVLNKDSRSALHAVRVAYDILKETLGPDHQNTKEAEHWLSEFTALAVNQERQSRT O59743 YN27_SCHPO SPBC530.07c; CHAIN 1..242; /note="Uncharacterized protein C530.07c"; /id="PRO_0000372370" MDPYTVAIIKKLGIEEQVETAATKSPFIEGLANGTAPPGAFKRWLYEDRIYVQGCSLCLAKAINAITHEKGFPKEALDLFLGAYNVITPELAHFEARCKESNVEMPKLKPVPTSWEQALQDNKPEEYYHLSAPDCKSYIQFMTQELFEIPGTSGIDYFMAFYLNEVIYHRAWKFVRESKQFQKNCPEEMEFVKWWGQPSFGKFVENLARSIQDVPFTSATVDIAKKICNFEYRFFSTAFEKA O59758 YJM3_SCHPO SPCC1020.03; CHAIN 1..397; /note="Uncharacterized metal transporter C1020.03"; /id="PRO_0000317148" MLKTFNSSARSCRAMPRFLPTLCSRLHEKSGFEIRNAVRMHSVGSHTHTHDHGSDKEMLELVKALKKEGKSPELKLAWLGLYSNIGLAAAKGIGGVALQSSILVADAAHQLGDTLSDLVTLATLKICSKKPTQKYPAGFGKWETIGTFTVSGLLVAVSVGIAHSSLSRLYTILFPYAGSEHTHIGHSHNPSQLLFEHPFMALGLIFGSVVLKEWLFRKTRTVAQKTDSNILLANAWHHRADALTGMVSLLALSGTYFLNAPWLDPFFGCLVSIVVFSAGFNSSKKAFLQLLDRAPSEELRIAVTDALLKGEKLPYKIVTILGNAHAMHVIISVPPSFTSQQSSELAQKVEKTVLDAIPALSSCIVTPLSSDSNQVHRWQHLNGSSGEHSHPSHEHTH O59759 YJM5_SCHPO SIGNAL 1..32; /evidence="ECO:0000255" SPCC1020.05; CHAIN 33..509; /note="Uncharacterized protein C1020.05"; /id="PRO_0000310850" MMLPKRNIIHFLRKRAIFIVAAFIALLTVDYSLNTIEITDSKSGPFSLNTPIEDIRLVECFSFSPFCRPVLEFWKWARTSRNLYRSRIPWKRAYLYVKRPALYIPGETVLVEQVYVDRQLEKRNKHGIQIRYGTDGDICEFNTLLGEDVVELREGWSAVLNDFIYLGQPVLLTQRPCETPPTPSIEALKRKELSSVTLTYDDEEKKTIKILQLSDLHYSNSDRPCRDPYPYETAEDCMADAKTTAFVNELLQLEEPDFVLLTGDLINGDTSRDARSSLMKAVSPFVDYNVPFAVNFGNHDDLGDLSREELAKILSQIPGSMGLIGNVSGVGNFVLHSPRKFAIYVLDTKGDTSNRRLCPGYDAITEDQLEWLSSKVADFKYEPIQMAVLHIPLKEFCETEDLVGAFREPCSYSICDPNTAKALKSLRIPLAIAGHDHVNDFCGIHPDYNTYFCFAGGAGFGGYGGHGGYVRRARVFELDPVERAVRTWKRLEWPPEDRKLMLDVQTILV O59760 YJM7_SCHPO SPCC1020.07; CHAIN 1..236; /note="Putative uncharacterized hydrolase C1020.07"; /id="PRO_0000314096" MIPEACLFDMDGLLVDTESIYTKSTNIILKRYNKGPFSMEVKAKMMGRTSKEASRIFLDWSGIDLTCEEYIALQRETQAELWRHTKPLPGVMNLLSKLKSLNIPIALATSSDTHNFEKKSAHLSHLFDHFDGNIITGDDPRLPVGRGKPHPDIWFIALKMINDKRKAQGQAEILPENCLVFEDSITGVQSGRAAGMKVVWVPDVNILPFFSLSPEQAADKHITKVLSLENFDVTKV O59764 YJMB_SCHPO SPCC1020.11c; CHAIN 1..108; /note="ER membrane protein complex subunit 6"; /id="PRO_0000340112" MERDKGVAPIVVENVAYNEQVVSFVRNLTSSFFGCAAGILGLTSYEGLALYVLGYFFVSFLLFALKMRGNLTKYYQPGYKFWIAKILDGAPSYVLTWTLFYSLVYVYE O59772 SWS2_SCHPO SPCC1795.07; CHAIN 1..151; /note="Small ribosomal subunit protein uS13m"; /id="PRO_0000315966" MVYILGVAVNDDKPVRFALLSFYGIGHAKAEEICAKLSFHNTLRVRELTNVQLTTLSQLLSGMTIEGDLRRQRNADISRLVNIRCYRGMRHVNGLPVNGQNTRTNAKTAKKLNKVPRRGYMTLSPASTRPITWSFCLPRMVSVFQKLKHIH O59776 YCCC_SCHPO MOD_RES 51; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 53; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1795.12c; CHAIN 1..112; /note="Uncharacterized protein C1795.12c"; /id="PRO_0000303937" MYRPTTTSYSPVYTGNPLYDISASQSDPRQRIRKNVRFQTEVDEFPDFDDSDSDELQFENRDPRKRIDPIKHMLLVQRLKRVSTSSRRLFIFTLSMFLIAFILLIAFVSFRD O59780 YCN3_SCHPO SPCC320.03; CHAIN 1..867; /note="Uncharacterized transcriptional regulatory protein C320.03"; /id="PRO_0000310377" MDLNTLPFHSINSVNVSSAPTVNERSYPFLLDASAGVSGFNPVVSSPEKKARMKYKKNSTSPNMDVKSRKKVSRACDFCRQKKIRCDMDQSPRPGNACINCRKHHLDCNFTRTPLKRGPAKGFNRNADEKQKRASGSAKSSSPAVNGSVFSGNEASPSSRAPSITPVDSVNTTTSAIQVPSVTLTAPAPLGVDQKISQDQKPDSWLTYNAQFAQNSPQLAPSIPSPMKLSPANQQAMPPYPQMLGPGSISSYTNSNLGPSAGFRPPTFFSSPSPQPYSGPILASTAPTLDGSYLSNPSNSNPAVMSLSSNFPSPPKPNNPVYLPPRGNPTVNDRVSNVLPSITSFDSSVTTVPSNSPATLNSYTTSVPSGMSRHPMLMNPSTPEPSLGVNSPSLRPLQSLNNVQNSYRVASTQAPPPHPLRNYTSDAESISMRSKSTQASDAATFREVEQLYQENVEWDDAAIDRYYLLIHSTLPILHHSKARLKSELEKAPINLRSSCLHAIYSLVNRPPFATLGHVFHNTPMKAIGLLNLICSNVQDLSNRILHLQTMILLAIESDQRGPTTITGRNGLPQGMWLGAAIGLACNMRLHIQSHLSLQSINEDMDSDEALCRRAWWVLVVLDRWHSMSTCSPLFLPETFINLTIQDQKLLGTFPSQLVRLSLIVGHISDVFQSPDPTDRQSPIVTQQLRSEIDAFRQSVDVVWGQMNLLTLAVTHVKVLLELCINARPSTVLVPAMKMATILSSSSTPMTPLNHHFFSLATCVLIGVFDLPELQNEARRGLEHIRECIEKRRDIVSREDHEDWDYIVLKLINAKMQGMPINSDPSIPPHVPPSSAFAYSNQEMDSATFKDAYLYTRLCNLGYLGFLI O59784 MDE7_SCHPO SPCC320.07c; CHAIN 1..761; /note="RNA-binding protein mde7"; /id="PRO_0000081625" MSQLYALNGQPLAGKSDDLANKLAAFGLSQPNHSSLSEQQSTNSLLHGSGAFNKPPLSRNSTTNPLNLLYTQTQQPARSTTPFLLNPVGSSPGKLPVPSRNNSYLQGTAESNSGNFANNSISNNCWNSAYNSNSFEGTGSSPNFPPQNQFLSDSRSSIATLNAIPSLDQSVLLNPNLRARTPSLVPEHYFDDTDKSVHSKSSSGSNSLSEASNDDLESSIIQIVGGLPDDFDDRELSGIFTFCEGYDFSKIESENGHRKAIVYFRNAIAALKAKNMLNASSTNNFTIIQRDVVRQQENEYHKGIPPLTTPSLYSQRLSNNYDSTTPGFPRFSPANFDSVINKDVTSESRMSTSYPAVLEAFKSFNPIKAPKAEYLNQSRASMGNPSPSNWNNRLLQPSSKEQAVYSFQTQKNSKGLQFTSNELTNPTAKYSQLPNNIANIGESNSLSNQPNNFAQTSFDYQPNHPNAISPKAKFSLPSRPSYHKDNSFISKQAIDKSNPFEEALRLERTSPVKELPAIRPRTIPLNGVAPYESELRPPPKWKPMPDLKVVRSRPSLKQRPLRSAEYVRVCELKCLQEEEFDNKVLLEQVESNVQTDHNSPCNTIYVGNLSNPDQEKKLRLAFSKEKGYRRLCFKIKGNSPMCFVEFEEVCHAAKAMEKMQGAALDDKIKGGIRLSYSKNPLGVRSTENLSTTASLFQQHGPPKKSTDCYSAKASAAVERKYHFQNMTPKPNGTNSVTTLNRTQTHSSEVNDLFDIFEFPSK O59785 YCN8_SCHPO MOD_RES 463; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 466; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 467; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC320.08; CHAIN 1..505; /note="Uncharacterized solute carrier family 35 member C320.08"; /id="PRO_0000343536" MVDGSIHVPVQSHEGQHDNSSSLNEEIQTSQDPLGIVESYQESSTSDFDKSHYTHNSSIAAADSEYGSAFIQGQSSNGSEIKSERPSIDKKLDVNIDSHPIEPPPFEHDIGLPASQVPAAEEEVESTPKAKPLYFLLDKRFWIVFFLGQVLSLCITATNTFNGYMSGISNIPAFQTFLVYALLTLVYTPYTVFRMGFKKYFEMIFRHGWKYIIFAFFDVEGNYFVVLAYQYTNMLSASLLDSWATVAVVILSFIFLKVRYHWSQILGVVACIGGLVLLVVSDVISRGDYSAVNPGLGDGYMIIGATCYGVSNTLEEYFASKLPLYVVIGQLSLYGSIISIIQTFIFDRHHLYTLHWTSEMGGYLAGFILVMFLLYSLAPILFRMSSATFYNISLLTSDFWSLVIGIHVFGYHVYWLYPIAFVLIILGLFVYHVFVDATRESIKPWLKKGQGVDGVGTVRRPPSLVSSNDELNKKNDIVVAHHDNEVKERIYDAYLSVKNVFVRKS O59792 CIF1_SCHPO SPCC364.01; CHAIN 1..320; /note="Calnexin-independence factor 1"; /id="PRO_0000303995" MSEEIITESIVKNFGSAETSVGEKQPKRKRSEVRAEKLKARKLQKAAEIVQKQKENRKILKDVSLKRLSKSLDRSLPSENTIDQISFNHAMSEEDASGYQIGDKHKNLLLYKLSSSSGSVFTENLYSTIQEFLSAQKVDIADSKNTYVFGSTFDKKSHALVKTSDSVRSLKYGSFVKACAPLFRFASGIIKAHAPHFHQALLKLELAPSALRFGVFPNFSLQSVSNGYMSMESNFSSIKYGFVVIIIVGELNDVELKIPAISHSLKLKDGSILVLRSSLLHQWYSLPKQSILYEIRLFAMSSLWHYEKNKSIKIAKKDDI O59795 CASP_SCHPO SPCC364.04c; CHAIN 1..633; /note="Protein CASP"; /id="PRO_0000310337" MAVASEALLQKLTESWKNSRFEELQREADEAAAEIEKMQKTSLDERKELSSKTKEFRKQPDEVKLGEMKGLLKLYQSGIDSLTKRAKSAEATFFRVYETLGEVPDPYPLLIEAANNLKTQKQIEDLKKEKEEMEGSLQGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQENASTIQKLTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEQKSGSSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDYDEIKRELSVLKQIEFSGEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDLADVDVEGSVYLSNTTYRREGTSGQLSPTSSIMGGNPSLFNGSVLSRNSVNETGSAIVDVIKQQRDRFRRANVTLVNQVSAANDKIALLESKLEEVEKSNTLLYEQMRFRDHYQKHVEPSSSHLQTAAAYENSISPFASFRKKEAERAYSRMGSFERIVYALLRTLLFSRATRGLFFMYLILLHLFIMIVLLKLGIAGNTAYTPMNY O59799 YJV1_SCHPO SPCC550.01c; CHAIN 1..77; /note="Coiled-coil-helix-coiled-coil-helix domain-containing protein C550.01c"; /id="PRO_0000310851" DISULFID 27..57; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 37..47; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MDSIEKTPDGEEEEKDVWDTALEKGGCVEEHLRLNDCYWDTHDWRKCTEQMEEFRKCWEKRHGPLPSISDKKNKNLS O59806 YJV8_SCHPO SPCC550.08; CHAIN 1..247; /note="Uncharacterized N-acetyltransferase C550.08"; /id="PRO_0000351077" MAAKRVEAKDYKKAAATLVDAFFDDPVCVYLCHTTNEQQFKKLMTEMFEYIVYAHIIRGLVLEVGDFAGISLWMGPGNNMDDWYSILRSGLWRLKYKLDGEGRKRFFNEFLPILNDTKADVLKERDDHSWYLVYVGVSSKEQGKGYLRKLIEPIFNICDQEGLPIYLESSHLHNRPIYEHFGFVYQQSIYLTRDNQKVPLEIMIREPETESKAEQSAKPKAALSKTVSASIAEKVEGSLAVSSTPVC O59807 PEX32_SCHPO SPCC550.09; CHAIN 1..535; /note="Peroxisomal membrane protein pex32"; /id="PRO_0000356187" CARBOHYD 374; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 377; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 418; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MIRAHLFSEPDNSKLWAKSTGSDAFDLILKVLLWTAPWYYCLTTLFFTWLIILYPRPTLACSVAAWLFWFTSLDTLEPDDRKNTLKASEAVSTSAKTSEETAKPSETREDGEWNTLKNTLEADAQNLMSGFQMLQRRWSQPKTTTLKTEVKEQQASQSPSVEGENEPAGVKSNEATKPSVTEEKEKNAEQNKRRERLSISHIVTELAKKDEVSSESGSNEIVNAKLKNEQLDSNFTLLDAYLEPLVHLHEYSRRSNTLFFFYLPIVMSILIFCLPTQALFIVLSSVFLAWHSPPLQAVLFCIRRISFFNLLYEKFVIGKTKEPAKPVPQPSSNEPPAPSAENKQPSVSSPEKKESPATHLLKVIGSSPYVVHSNHTNNTLTDKESSDPTEKCLYLIEHQRYWVGVGWLNRTLPTDPPNFTNAGSTDPVAEPTAQLLPPDGLAWIDDKWSISPWTFTDTFWAQPAKTQFRTAFTRSREWRRRYRVAPPAENEKPHTSRTNTASSLSSTSEDQVSTHGSISSAKVTAIPDSNGAEAL O59814 YCT4_SCHPO SPCC794.04c; CHAIN 1..547; /note="Uncharacterized transporter C794.04c"; /id="PRO_0000372787" MDYIFLITGYKYRHLNLEAYNAKSRAIENEKRYLGNDRNLPFHREREKVESNPNSSDEEDLTSTNNTRSSDNTTSDTEDDSGEDSYQVEWESGKDPLAPKNWPMWKKIYTLLVASFIAIVITANSSIFSDGGGIAAQQYHVGATVGDLCSATFLLGFAAGSVLFAPLSEVYGRLPLYSVTLVIFVVFQIGGGCSKNIWSLVIFRFFHGFFGCTPMSACGGTISDLFNPIQRTGALLVFCAAAFVGPLVGPVMGGYITESKLGWRWDFWINMIWAGLTWVIVCFTMPETHSETLLDFKARYLRKKTNCDKWYNEHEHQRDPAYAIRTALTRGVRLLCTEPIVQAFCMYLVFINILLYICMVGYPLIFYQYGFNAGEVGLAILGILVGILLGLALTPIIYVHYRRRYEMRDGNICPEDRLFPLFFGSFFIPIALFWLGWTCYPSVHWAAPMVSGIFLGWGFLYVLAVCYSYLVDCYHEMAASALSVATFTRYAAGGGMTIVARPMYNNLNYHWATSLLAFVGCGLVPIPFIFFFWGRRIRQRSPHAYKG O59815 MAE2_SCHPO SPCC794.06; CHAIN 1..431; /note="Putative malic acid transport protein"; /id="PRO_0000310766" MDIVKQRYHELFDLRVRGPRMKMADRLEHFTWAWFASAMGTGGIGMVTSLYHFRFYGLNTLGKIIFIFQLSILTLYICCITFRFIRYPGTLSKTWKNPSEVLFMPTALLAIATSISNLYPYAFPYTGEWMVWLIRILYWIFVAVACIFVISLFYSLFHAHPFRINTIIPALVLPIFPCMICGVIASAIVESQPARQAKNMVVAGIAFQGLGFWIYIIVYAVNMCRFFTVGLQPAADRPGMFILVSPPSFTGLTLLDLAFGAKAKRPYIFVGDNSSEYLEFVATFMALFMIGLGIFNFCLAFVSVVAGFCTRQRIKFKVSWFAMIFANVGLVMDVQELGRAIDSKAVCIVGQVCGVTITIVWIILILLTLRAVYVQELLYPGKDEDIDTILPNVLEYYRHLEEEEKDEAERSKRKAEESDGKTTRELTSGGL O59830 YCUA_SCHPO SPCC965.10; CHAIN 1..525; /note="Uncharacterized transcriptional regulatory protein C965.10"; /id="PRO_0000310378" MTSTSHFVASTVKKPRSRYGCLICRSMRKKCDEVHPQCGRCLKAGKQCIWKQPGTERKNKTKWRKAMQNNSIPIQDLADDFELDFPDTLDLTNPDALPVLGESIVNPISLPVDVASPFLPSECYPSKVELPYFPLLSKPNTLLSLLNDEEISCCEYYCYSVAPITTILPGQPNFLPQLLLPMALHEESVLYSLVASGYRLKYGNDNSLALQKSKVFVNRALLTLPERRSLNLSKSEFVVSLACYILLVYTEIAFADTTEWATYFLNAYNMINKMGGFKILKECSSEGKLLAECFAYFDILASQSNLNGTYYSISDYTDVYGVDELQLFESLENCIKPLVLIIGDIINLLVESRRAGFDDLQHTLNIYEKSQTIEGKIWSCVPQYEDMKSNKLDSEKSEPLQLFKLYKTTTEMYLRQVISRMPPVSLEMQVLLHKQTQLIDLLLESSLRNSLSFPMLIAGLNAATDLQRTNFKNRVNCLCQNYTIGSLKKVWIVVQEIWKMNQNGNICIDWYEVVQKFGWRLNTGV O59831 YCUB_SCHPO SPCC965.11c; CHAIN 1..537; /note="Uncharacterized amino-acid permease C965.11c"; /id="PRO_0000054178" MEAAPSEKVPAKKLSSSENLDIGVSEVVTVDAAENNSNGIKRGLKTRHVSMMALAGIIGPGVFIGMGSALHIGGPVGLIVGFAIVSIVVFGVMLSIGEFNSLFDFNFNTHAARWVDPAFGAAIGWNYVIVWLTNIAAEYTSLTSILQYWGPHVPSYGFFLIFWGFFTCYQMLGVSVFGESEYILAFIKLLFITGFYIFAIIYAAGGIPHHKPPNLFKEMPLAHGFGGIVSAFVYAGVFFSGVESVSMTAAESKNPKKAIPLAVRQTFWRILYVYFGISISYGITVAWNDPNLSSGSKTLKSPMTIAIMNAGWNHAGDFVNAVILITCLSSINSGIYIGSRSLYNLAKDGMAPKIFKRVDKRGVPWVAVHSVHLFGFLSIMNYSTGAVKAYGYIINLAGVSAFIVWTAIIFVHFRFRRGWVKQGYALSDLPFKSPLYPFPQLIGFVIGIILTLVQGWTVFKPFAAGDFVDAYILLPLFFVIWLSYKFIKKTKWVSYEDMDFINGRRVIEPTYSNEQSSDKETEDGKKTSFWNRVWKEV O59832 DPEH2_SCHPO BINDING 29; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 31; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 144; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 144; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 215; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"; BINDING 236; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073}; SPCC965.12; CHAIN 1..416; /note="Uncharacterized dipeptidase C965.12"; /id="PRO_0000314655" MTVDLREEKELAQQRFKEICKHAKIVDTHNDFPYLLRVQLRNKLQLAEFDFENGLTSHTDLVKMRQGQVGVQFFSCFIECKNPNYLYQDFDTPTTVVRDTLEQIDVTRRLVCKYNNDLKFVDCADDAIAAFRNNGKIAIALGVEGLHQVDTSLAVLRQYYSLGVRYITLTHNCDNPFATAASSITGGLPDRGLSAYGIECIFEMNRLGMMVDLSHVSHRTMHDALDVTKAPVIFSHSSAYTLTEHERNVRDDVLERLKTNGGVVQVNFYQDFIRKPGSDRATIDDAADHILHIIKVAGWEHVGLGSDFDGIPQGPKGLEDVSKYPDLICKIIERTNATNEQIEGLMGLNVLRVWKKTELVALQLSKKLEPIESSWSGRKWEFYSYAKEFPELFPDAYKLNEKSTVWNYDQPLNIEK O59856 RM33_SCHPO SPCC1919.08c; CHAIN 1..97; /note="Large ribosomal subunit protein uL30m"; /id="PRO_0000104618" MSFFRVRLERSAIGLSSKVRSVLHSLRLTKRHSVVYCDVNPINAGRIFKVKELVSVSTVKQKLAAGQEKKSLASSSGFTVIHRYNNGLKELNNMFES O60053 POF12_SCHPO SPBC56F2.01; CHAIN 1..440; /note="F-box protein pof12"; /id="PRO_0000119977" MTTDVKAKNPASIFSHETLLHVLNDLSAHDLAALERVSRSWNSIVRRSSVWHNLYLSEFGTKHLRRHGRIEKKRRNWKGLFRRQSNWKDGRCKKVESMLPQLLNSEKSVGEDRLGLTLTHQNNIYFCNDVQISKWSSVGNSLKCQAISSFRDETVKSGPAVMCLDNASLYIGLKDGNLLHVTVHETGFGNIENLATFSTKFVALSSHKNYICGLTNDNNLYILQHSHQAGTKLKVLGKYHVSSIEKQVAIHFQQSKEGYEVVHVVFNDYVLSGGWTVSLQEFVFNEYCVKSSRLALHDNKDIEYSQQPASAIFMYGSYILTSHPDNSLILQRLYSTNNELRIKFLGRLLGHVCGVQISKLFSCGRIVSVSKNCADICVWDLHDTNYQSIVSPLMLTCTNIHNKPVSDYEKECKVQDIGLYEDTILITLSDGRILKFLFNI O60054 ARP10_SCHPO SPBC56F2.03; CHAIN 1..380; /note="Actin-like protein arp10"; /id="PRO_0000339114" MRKNCDISTVVVQIDEFGIYIGNASDKEPTWKVDLVPYKQSWVPISIVTTIIQRYCLNTFNCLAEIVRVVLVLDIFVTRKQKKELCDGLFNTLNVPITLWICAPLTAILSTSTRDAIIVDIGMKETKFIVILDLCILMHYTKTSKRSLSTVLERMADCFKLNNKKNSQKLLEDEEFAVTEALMKSLLKSRVPSKPTEELYQLTDQEAYFRYSDILPLAETTCQTNKTERGSSFNDAEKIRVPSWIANAGIEALFEGSDAGGSDIADQALPNVLLSLYRILPIDIRRIMSKLIVFNGILPSLPGWYQRFQNEMTSRGLAIKAVPGQTTADMMAWNGASTTCESQLDYDPDDPKHLRHSIVESPLLYGQDQYFNGENAPEWW O60056 YG55_SCHPO SPBC56F2.05c; CHAIN 1..397; /note="Uncharacterized transcriptional regulatory protein C56F2.05c"; /id="PRO_0000351073" MDLHSILQPISTPSASVVTAPLPATIALPSPNYYYPPVAQGHYPVNNMWSLPSNVRVISSHGAPGHQTSASQPSTVMPALETNASNAQYYPAYSVINGNNSVQVASPAYTVSHSPHSFSNPRYVAVPQKSTSPNQVCSYCEPLPNHLTKTKSCSIPPILNSSDRSPLSLPTPYPVQYSTQPVSLPQPIAAPAPPSAESSKSTISDEDVAWQLIRLGALSSNSVKSSPSKSFVSISSPVQSTVKPTKASGVVKSEKVEKRSLPPQDFGNASSSTSAKRRRPDHNHTSTLDASSSNTSLASTGPMTVSSSTVERKGKEASEVNPNSTSSVTFSDFAAAISRSRCSRCKKSKKGCDRQRPCGRCRDAGLNSEDCISDDDMPVSNARKPRGRGRGRPKTKN O60057 MU147_SCHPO SPBC56F2.06; CHAIN 1..411; /note="Meiotically up-regulated gene 147 protein"; /id="PRO_0000278507" MLAQNSREVLDKDLESHIPGAYSPAPPSSSLPTQNESNLQQSEKPLKHFENKKFKGEDVFAHSISKPFDGQNDEEKPSLYSHLTNELYETHDSSDYFGTYMEREESGHDEEEADKDASFTGYYNSRNNDEEGSELADSQMLPMTESFADIEDIHHHQHEDEFSSSNKDKGFTYEKPVTELPPKRPPYHYESSSTSISFVNGGPNFRKVKSGLLKPDADAASNLSTTSLVNQEYVMKQVTPNEYSMEYLRESFPQTPMGTEASGYSFDRTPHKSDIQASDRLNALNEKLLQGIQQSHQPYHYTNVKDSQGSHQTKVTIEENMEAPSHQAANRTTLTDSPLGIVEDETTILTDLEPSGPGLQKRASETSMSTNVSLPYYQNGRRVRNILTPYPTVSLASTMTSETEDVSEERI O60068 ISD11_SCHPO SPBC13G1.06c; CHAIN 1..102; /note="Protein isd11"; /id="PRO_0000339460" MSVSKQHVVRLYRNILKTSKLFPYTYREYTIRRTRDKFKELKVESDPAKFEQGIKDSEKLLEIIQRQSIINGMYNKRNLVVEGIDDTAEGEVKKSFENASQS O60076 TAF13_SCHPO SPCC1494.02c; CHAIN 1..111; /note="Transcription initiation factor TFIID subunit 13"; /id="PRO_0000317146" MSMENRRGRPPTRRQHLFTKDLKSLMYAFGDDVNPAPDSINVLEEIVVDYINEMCLEAARIAGNRNKVKVDDFKFALRDDPKKLGRVEELLVLQKMIADTRNVMKYNKDHF O60077 GDS1_SCHPO SPCC1494.03; CHAIN 1..492; /note="GTPase-GDP dissociation stimulator arz1"; /id="PRO_0000116890" MTASDTVYLFQSLADRSKNPQERSLFRNYISEALELLRETPSSPTVVHEQCFRFLANSCSDNNENRAAFFNLGGIDVLKPYCSKDNEYSALAFAVIHNCILDSREYRAQVADAQILNLAITYWIDWQHKLKAPFFNMLSFVCEMLYPFCKDCSLVFMGLQLLPSMVREGIDPFTIFAKAFDNSLVCVSFAQNPSMLIDSIDLVRNMPDFTKKTDMLNLFPRIAEHDAVLSTSLHADPQFLDFLESCFRSDDSNSITMASLFIGNLVRRDDIAKQLMQKDFLNMLISCIMQEKDVDGNVERVYACCAALRHFMIPVSSRAHFAPTAILLQEKLASSRFTQLHYISASMIRLSMPYILCELADHPERFYKLKDWSKSPDFNLALESNRTLLGFVKHYLTVPKSKEKISAFFKNNINLFEESVVTVLSTESKYPIVIGEAVFVAILMIKHGYANVAQTIIASPVYEALKSYRDDPNLAYQLKQNVRSLLVLVEHR O60090 YO29_SCHPO SPBC14C8.09c; CHAIN 1..297; /note="IMPACT family member C14C8.09c"; /id="PRO_0000316615" MNKRQSQLKFGNEGISLAVPKQSLQECSYMSNLITDRESTFLSYFVPSKDPKMLPVYRFMFQESADLKHCNHKMQAWRFPNEIEAFNDDGEEYSGQKLLNVLRKEDVYGMVVCVRWYGGQLLGPVRFQHITNTAKQSIDKYKSVLEEERKKQLLRTETGLLRQSSSRSSSLLDQRIRQITAKDKTVNLLRKTLNRPLLHEVDYHGKSLEILDMLLQSRNSMISSLRSELQEKNQKDKKKEVNKLEEKMTNAKEPNVNVPSMKASSAISVETPETIESEASVDHKEASKIIKDVEKEE O60091 RM24_SCHPO TRANSIT 1..8; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC14C8.10; CHAIN 9..176; /note="Large ribosomal subunit protein bL28m"; /id="PRO_0000317083" MASKLLRKLAYPTLPVKGKIYDPFSKFQQNLYGGSKTEAGNNKIPKFGHKTRRVWIPNGHSKWLYSNVLEEKFHLYVTSRVLRTIDKEGGLDEYLVKSTPSRLKSLGLRGVELRALVLHKLGAKNPILEKLPSDSGAQKRYLEKVKDVVLKLNRSKKLYQQIKSLVGKERSVNTSV O60093 SRR1L_SCHPO SPBC14C8.13; CHAIN 1..251; /note="SRR1-like protein"; /id="PRO_0000186126" MDFIVVKRSRKKKNGRGKFPKVSNTITQGDTDLWSQDTLQRKLDNSREKLEYSEFLKSVQSQLSEFKDPIHKCIILGLGRIHTLTASLQLSLFFEIMKIFNLQPRFCSFYDPAFLKDDVEFLENKGFCVLPDPPTPSCLKYTLLYMPHCPTSLYETWLAAYVNDDPRHFIMCGNNLQLYVDNKPSKEIVSTYPNVYKMCTKNYYTRLLFPEFPNVYAFNDLSFHFHDAQSFVEKKQPSKFVDASSVAEHPS O60099 YOX2_SCHPO SPBC14F5.02; CHAIN 1..515; /note="Uncharacterized protein C14F5.02"; /id="PRO_0000304064" MRNLNTELDFFVSFSALKEENISQLKVYWAQSNLVELYYGESFYINIVCSRPIVDENVTTWPENEGFRIEGTLLESLVESVTSASNYPKVNAFSLMCSGIPSFIWVEDDKQYALWACLAQLDSYSYPNHKLEIHVYKHILPDLPQSSEVDRNSETEGTREENSNTSDWDEQNEYVSEVEGDYNLLGSLSNDIQFRSNPPVISGAYVFGESDVANELKDPSRKTKTRKKVFECSVPVVLKLRSYALNESNQYITSIVSPDSSCENIRILGFKAETNAATISLFAPKTPEKLQITLSSSDVFTIIHLLQIPDNIKHIELQCFCKVIVAQKLSETLVESMPFTYKHPPVLITRRTPTKTHTKQLSSSGNVSAAQSISSLNLLEISASSPSYVPSGSSFSVRANLYNPLDFSIDLLIRIPLYCYDDCLTNKEHSTSKSEEKSSELLKYPNGHTISPGIIALSTKLYTGSIFPKCEKDFDLHFLAYKPGSYDLSSISIEDVNHVVHKPRKLSKELQIIVT O60106 YOXA_SCHPO SPBC14F5.10c; CHAIN 1..486; /note="LON peptidase N-terminal domain and RING finger protein C14F5.10c"; /id="PRO_0000310493" MRKERPGVLFNKIRSYFICPGCNCLPDWPVTLPCGGTVCRKCFRNAYSSESSGKVSPSRCCFYNHKKPHYSVETEVKDVIISKVVELIKTTEFQISQQSLVPLELKEEICHDDCLSSSPPCTSALTEITLLPPTFHNLIPSSSSYETAVAEFLHMEDLLQENVSRELECQICFGMLYDPVVSPCGHTFCGPCLMQALTQSPQCPTCRFGLPSPVVLEHAKSHSITTFLRDFYPDNWLERQKSWEEEKEQESWLPLFISMLAYPRMPTFLHIFELRYHIMIKKCLETSKRFCIAMPLRARSDGHNEHRELRNARGQRLFCSEYGTILEIIQVEPLIDGRSLVEARGSYCVRIIDFRADGLFPRVKIEKHYDTPLRATPLQFPEPEYLLMYGNLSNEELVERIDAFYMNARRTYVHWVVPLIDIKMEARQSIADLSYKITNLLPISELEKTRILQVDNPTDRLVLVLIWLTQLQESWWYRVGSACTIA O60108 CBH2_SCHPO SPBC14F5.12c; CHAIN 1..514; /note="CENP-B homolog protein 2"; /id="PRO_0000126135" MPPLRRQALTLAEKKAIRKHYFESATKPSQQELISWFEEHFHKKLAQSTVSSILSSKNEFLDNLDAENSQIRRNRQGKYPILENALIDWQTRLQKQDGAITGNAIKKSAAELWRRIPEYSELPIPEFSNGWLEKFKKRCLKHGLKLQGESTSVNQGTYEENMVQIQELISLFDPKDIFNMDETGLCWKLIPNQSPASERVKGITRDKARVTVTICCNATGSEKAPLWVIGYAKSPRAFRQANAHPDSMDFHWRYNGTARMTTSIMEEWLRWFDDLMKGRKVLLILDKFVAHECALENIRNSERKLVNTTVVFLPVNSTEIYHPCGQEIVYAFKSYYRKYWLNYMLEEIRLGKNPSKTMNVLKAVRWMIRSWNVDFEPSIIYNCFLRSGLFQNQQPLTGPSPETIRIAVNLQELIGKYLGDKDIFQIENFINPIEENSADTNDDIVNQVAAQFLDEREFETDEEEEESQYLLSTKDAINAINTLLNFQEQSEDGNVLFTRTLLQFQKVLESRSIV O60111 MCP2L_SCHPO TRANSIT 1..33; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC15C4.02; CHAIN 34..557; /note="ABC1 family protein MCP2 homolog"; /id="PRO_0000310291" MFSRFSWPRITRCFRSYPKKKSSCISFTHHAREHTNFKKPAVVGASITLMASVALVDFDPVKHAGVSSKRAYRVVLAGFLCFSDYKKVLGSSYASEEERQLALSECHLRCAERSLKVFEENGGIYIKIGQHLSAMGYVIPKEWTNTMVKLQDRCPSTSLKDIDHLFRVDTGKGLDETFDEFDPIALGVASLAQVHKARLKDSDVWVAVKVQHPSVSLNSPLDLSMTRWVFKAIKTFFPDFKLMWLADEIERSLPQELDFTREAKNSIETKEHFAHLSTSLYVPEVMWSKPRILVMEYVAGARIDNLSFMDEHSISRDLVSVDICHIFNEMIFGKGGHLHCDPHGGNVLIRSKPKNSKSPRNYEIVLLDHGLYRDIPHELQVDYANMWLNIINFNEKNLKFYAKKVANVSDENFPIFATAITGRPYKSLKSLPIGGPNHEEEQKKFISALQKGGMLQSIIRLLSTMPRLTLLLMKTNDLVRSLDENLKTKSGPEKLYLIMARYCLRCVYDDKMDSLWNSRSFWVSKVFKGTYYRLSYLFSSLKYTLAENYFYYKHMYL O60112 YG63_SCHPO SPBC15C4.03; CHAIN 1..459; /note="Uncharacterized Rab geranylgeranyltransferase C15C4.03"; /id="PRO_0000317152" MDDPNSYDVIIVGTNLRNSILSAALSWANQRVLHIDENSFYGEIDGSLTLRDLEQINEKIKKVDSSQILNDNGSHKSPLKRFEVQFLNKDLIPKNKGSVIQFHPQEIFASSELVKLLSETKIYKYLLLKPARSFRLLTSNEEWIKVPESRADIFNNKNLSLASKRIVMRFMKFVSNIADEQNQNLVKEWESKPFYKFLEEVFQLSGAIEESIIYGLCQSLSKDIPTKDALDTVLKYFHSFGMYGDYSYLLAMYGTGSELCQGFCRSSAVMGGTFMLGQAIDKIDESKIVLKDGSTLSAKKIVSSVDEGKLPHQQIQQRYLLVKGDCQQLFQEDGFFAALDASLIHFSPFSISENFGNSVQAKLYGSGSGDCPEGYCIWYLKTLNDSPCNEVFNLATKKLCSFSGCDDLEIIVQVDETLNQLRHIDYDDTLHSAKSLFYEILGQNNTFLQREGLFDEDDE O60113 YG64_SCHPO SPBC15C4.04c; CHAIN 1..542; /note="Uncharacterized amino-acid permease C15C4.04c"; /id="PRO_0000310826" CARBOHYD 6; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 394; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MDSVSNVSVNEQGKFNDKEEGFSNLKSLKHVSHSETDFEVSNDEDNQLLELGYKPVFKREFSTWATFSFAFSISGLFATVVTTYSYPLISGGAPSAVWCWLIAGAGCMCIALSVAELVSAYPTSGGLYFTCKDLVPARSMPVVAWVVGWLNLLGQAAGVSSTDWSCAQLLLAAVSISTDLKYIPTNQHIVGVMAAVIVFHGLVNSLSTRWLDRITRFYATFHLIVLVVCMICLLAKCPKFNTGKYVFTDVQASSGWHPIGFSFLFGFLSVAWCMTDYDATAHIAEEIENAAVRAPNAIALALSITYVLGWVFNIVLAFTMGTDLDSLINSELGQPVAQIFYNVLGKKGSMAFTILSFIIINFTGITAMQANARTIWAFSRDQALPFSRYWYKINKTTTTPVIAVWLNVVFCIALNLIGLGSIEAIEAIFSVCAIALDWSYVIPIACKLIFGKRLNYKPGPWNLGWASHFVNAYAVCWTAFVSVIFLMPTVRPVTPQNMNYAVVVLAGVLLFSLVYWWSGARKSYIGPRINVDMESEDPFKTE O60117 YH73_SCHPO SPBC16G5.03; CHAIN 1..268; /note="Uncharacterized RING finger protein C16G5.03"; /id="PRO_0000310485" MKKQFLVRKNSSNSRYLRRDCVICLQKDGLRAQLSPCGHDQFDYSCICRWMDQSLTCPICKRHVDCVFYGFHGSSLYKKWYTQSLGSNQYSISRQLLRQPSFSSSENTDRLADLLRVRRFIYQKAWKSYENPSLSSHRQYQIPTPIQLASSASLLKKVESFIAKELLLFEYLDGHQINFIQIFLMGLLRVQNIQHPQTIDELAEFIGHEESSILLHELQRYLQFRPLSISSYLYSKRYLYGPEGLTMVQLLSQIENIQHESGPETENS O60120 YH76_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPBC16G5.06; CHAIN 23..230; /note="Uncharacterized protein C16G5.06"; /id="PRO_0000304063" MNIRSFLLISIFTAISYLVVDGATPRTFAPSASVSINYGTLSTVFPSLYRRASTSSSSSSSSISTSHDSQPSTSSSSPSSTSTSSSSGTSVITASDVSASNEIISSSTNNSIHQQVSVVTEYVTIQPTTYVTTIFQYTSLASTIAAQSGIASLVPQTYTPYGGVKALIGILVGVVVGSVFLLAIVMVIARIWGPRLLANKDQNNNNEDLDSNLVSKDSEGTPQITYASNF O60121 YH77_SCHPO SPBC16G5.07c; CHAIN 1..354; /note="Uncharacterized protein C16G5.07c"; /id="PRO_0000316209" MLKLFLSTPRTLPNSRFLLLRRLQPLGLRYRSDASSLHLFTPTWRDHATNTIIKFVPQQVAYVVERMGRFSRILTPGVAFLAPIIDKIAYIHSLKERALEIPTQSAITLDNVSLGLDGVLYIQVYDPYKASYGVEDADYAISQLAQTTMRSEIGRLTLDHVLRERQSLNIHITDAINKAAESWGIRCLRHEIRDIRPPESVVMAMHQQVSAERQKRAEILESEGKRQAAINVAEGDKQAEILDSEGQKIKTINSALAEAQAIREKASATASGIAVLADSIKKQEHGLEAVSLYIAQQYITNFGKLAKASNSMIVPASTSDVSGMVAQALSIFKQVSKTTAPDKSTPKELHTDEK O60122 TRPD_SCHPO CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; SPBC16G5.08; CHAIN 1..354; /note="Anthranilate phosphoribosyltransferase"; /id="PRO_0000154527" MINTFNPEVRLAIHDLDKVGPAIPLENYEAALRAILTGKASPVETASFLASLHLTKAEEVPDILMQTVQILKSYSTPIANIEMVSPRFVDIVGTGGDGHNTFNVSTASAIVAAGAGLWVCKHGNKASTSASGSADLLMSFGCDLLNVTPKNIVSITEQCKFSFLFAPMCHPTLKNVAPIRKQLGLPTIFNLVGPLLNPIPTYARIIGVSKLSLGEVVAKTLLKLGAGRSLVVCGEEGLDEISPAGPTHTWLVRDGTITHEVYTPESFHLQSHPLSSVASGTPSANAILLEELLSNMLHANHPILDYVLMNTAALLHVAGMAESLREGVKIAQQSISSGAALRELSNFSTISQQP O60131 YH7H_SCHPO SPBC16G5.17; CHAIN 1..560; /note="Uncharacterized transcriptional regulatory protein C16G5.17"; /id="PRO_0000310384" MVGKSKNRAHKNIRARSCLRCRRRKVKCDRQYPCSRCKESEESCTYGVNEQAVQLLEEPLSRPITRETDSSAHQETRTRLEENNLPKTQKFGFVDWKTILKSSAEFQGIVQRDPESRLREALETDPKLKKRLECILETIPPWDVCESLLKVYANTFNVTNYILDFEQADKLLSDLKNSNHVFATSIILIVTAIAVALSLESFPSNIERYFSAVNHSAIELSDALNSKIDDFLNEEVIFRLWRNIDRIRLHAIRAQLCMRNQFRSMNTDLCYAIHYACFVNPIFQNTDTEYEANMEVWLSICEIDALECVLRSCQPWVQHDIYGKLLSQRKMGSDVISYEFHSLLGQLLTCGLEIYKAIHTSTVNEFVNSIQFYESQLSLVLMEIESKFSNIDGSDIHFRYLFLKTVFWTVRKNLYQGFITVSRTLVPNYPDIVQKLGQTSIQLSRLISNSMDCFEKYGWLKAMLILVTHTFLIIHVCSERGYDVPKDFWNVTASVQATLEEKKYPGIVWERIHYVLNIYTTINSVEPELSEDHGDLDDQNLFQVFTDIFDFNFNFPLPNL O60136 YNS5_SCHPO SPBC18H10.05; CHAIN 1..586; /note="Uncharacterized WD repeat-containing protein C18H10.05"; /id="PRO_0000316568" MRVLVAETGREDNVSVHSREVSVNGSDSGTGNDAYKLETDDEHPPATPVRGLSTRSQKRPFRPLTIQQDEDVENDTGMNTEYNDDNSSLVNTPRDSTTYAETNSPNTEKLAGRDDDRSLLNLIDRGEIDSKRQRHYVPVHCKRMPKKEITLNQKLYVSQVIGPADAPKSKTIFGKRIMQWEPSQFKESVWASEISKSGKYLATAGKDAIIRVWKVIETPERRETLLKEGPQSCGRFFTPSSIFEPEPVLECVGHNAEVLSISWSKNDFLLTSSADRTVRLWHPKSTKSLAVFRHNEIVTCVAFHPIDDRYFVSGSLDCKIQLWSILRHKILHWTELEYVVSTICFYPDGESIVVGMFYGLCAIYETKNLQYVSSWLIHHSPSRNKKCRVTGLQCASIIPNDSKSDNVVLVSTNDNAIRLYNTVTHALVLKLSDAHRVNGRVLSRLSEDNSYIISGSDTNEVVLWHIPNKVLINASRKRSVILHLPTETFKVCSERLTSTIIAPARTAVEAKESEHDRSLIAEGYNLVKPHSHRSYGTPPVHPIDIIIATNMAGMTIVLCVDYDLGNSHHGFRNSKFGHFVKRLLRT O60138 YNS7_SCHPO SPBC18H10.07; CHAIN 1..224; /note="Uncharacterized protein C18H10.07"; /id="PRO_0000342265" MADYWKSIPKYYCKYCQIFVKDTPFARRSHEQTYKHQDAIKKVMDDIHRSNLLRQELEKNLSIPKSATATTASAVSSELASYEKPKKEHPKLRPSKKKATLDDWDIPTSSTETDTISTTHTSYIPTLLAKQEENEETKETTTNKNESLPGTSLKRNREIIEKEERSSFHFRVKPKNLDKVPKLAENEGNKSLESKESNENKVVFKKKKSGKLRTKSSLKEYDQS O60140 YNS9_SCHPO BINDING 396; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 398; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 410; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 411; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 417; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 420; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 421; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 427; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 437; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 440; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 452; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"; BINDING 455; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" SPBC18H10.09; CHAIN 1..495; /note="Uncharacterized protein C18H10.09"; /id="PRO_0000310739" MVSIEAMKDSNWDLQIQVFRRRLNPEVIEARNEIFLSLPSDHGLITLVINKDKPFQISVLLEKNQEFMQTAMNKYVETAFQNQKTTLTSLFNYLLQNWKSFETCNTKERELMVQQVDSKKPETPTDLEPLANKLEGPLSERVHLNTTLDYEVLRGQNHCQKQNTTQTKTTISGSEQLFNDEKPKKIIYSKGGNDGKEDDLQNVNEPQDAYSNDHDIQSKDTELLGNEYCLEWKNPHLTNVGTLKAPILRLVIKCVRCHYGSEISIATKFSLVCNKCSNTLRLVWVPGVIHPNNARLGILHTLGCVPVDVMPIDCQVSCMECVDEQITSFKGISSMQPMLQFCKVCKNRILVEHQDTEFHLLKQRQSSMGGKVSAKKKQKQNLNITKGLPLPNNGACEHYKKSFRWFRFSCCDRVYPCDECHDADQNHTFEHANRIICGYCAMESFYKKDATCPHCGNMTVKKQTSAYWEGGKGMRDRVRMSRKDPRKYKRKHHGN O60147 MHR1_SCHPO SPBC18H10.17c; CHAIN 1..175; /note="Large ribosomal subunit protein mL67"; /id="PRO_0000116860" MLEKNKYLYIFRHIQTNQVLLSQGNVLKKTALFQLPYPLQKPVAPNGMRPAKLRKDHWVPLLKVEFPNESMFQSVFMQLLNYRKYRSVQPLTSDLLKLPIPVRRRKIMRQEVPNTIADLADILNKEKFPENSVRLQLSDKSDSEYADWPPSVQIDSEEIKLSRGFREKTTVDEAR O60148 YNSI_SCHPO SPBC18H10.18c; CHAIN 1..242; /note="Uncharacterized membrane protein C18H10.18c"; /id="PRO_0000304060" MPDEKLPQYNEVWNDLEKGCLHSCPSYSVNNHVNNPIVKQNSTLTQPSLRKKNTMAAPARLRKRSENVRLTQARYAIFHIFLPFILTLLLYHNFYNYFDQALADLNSVVKYVIETIVLIFTYVMTVIIVYFSFSLIKLAFEEAYVYAPSVAKANEGLAKHVAKTIAGLVKYVAKAIQGLAHIILSLLLFILGLEVIEQDEETGDVEMSSMRGQAITTEPASDNTMAEGTDCNTSKDVESGSS O60153 YHY4_SCHPO SPBC19C7.04c; CHAIN 1..124; /note="Uncharacterized protein C19C7.04c"; /id="PRO_0000116783" MTEVTKINPSTAITELEPYEMAQTNKEVPTTSLLSKDYYGHSIEEPDENNPTRWRYERPLDTVRAWQYLIDCDENFKTKPHREQNQYRPTADSFRPLSFASMESKLTQRLSRHLSKTSSRHSRL O60154 YHY5_SCHPO SPBC19C7.05; CHAIN 1..150; /note="Uncharacterized protein C19C7.05"; /id="PRO_0000116784" MNDDSSSSSSGDSSDGSSGTTIVQTNSYPWSAYGRWVVVIICIAALIFFFFIIGIINRRRTKKGQATIPFTNFYPLTAPPPYTAEPEARYNSTIHNPMPPMSQAYRPPPTEPPTVPAYETSSEFPPPAYPEAAATSDAAFRKYDGYAKLG O60166 NUDC_SCHPO SPBC19F8.02; CHAIN 1..166; /note="Nuclear movement protein nudc"; /id="PRO_0000310342" MHQVKLEEAEYEWDQTIADVDIVIHVPKGTRAKSLQVDMSNHDLKIQINVPERKVLLSGPLEKQINLDESTWTVEEQERLVIHLEKSNKMEWWSCVIKGHPSIDIGSIEPENSKLSDLDEETRATVEKMMLEQSQKRTDEQKRKDVLQNFMKQHPELDFSNVRDQI O60169 RTPT_SCHPO SPBC19F8.05; CHAIN 1..218; /note="Small ribosomal subunit protein mS26"; /id="PRO_0000304119" MISRCIKRCYRSGYMIFPPNRLQSTIRSKEEINSSRHKFNIADTSVRKQYNEELVFTKDAKENAEAKKVSSKVKKDRKNHSAAMEGVNINVPGIYRDVYPLPNEDVEMHEAKKKENICKKENLSKTVLVRQLAEIYFANSNKYVVDENGLDDLIQQAFKNPNDVFQPLPSKRDGDNMRLFIETEEEADMTSIKQHAIEVVLQDFQEEQPLEDKRDTIE O60170 MEU22_SCHPO SPBC19F8.06c; CHAIN 1..574; /note="Probable amino-acid permease meu22"; /id="PRO_0000054168" MLSKFYEDIDSKLENAMLSQIESSTITCDGKSLNTLPTPKQEDVEFGVPLQPEDTQDLQRKLKPRHMQMIAIGGCVGTGLFVGSGNALADGGPASILIAFAVIGTYVLFTTSALAELSAIYPVSGSFYTYFSKFIDPAWGFAVGIQYWLSFAVTVPLELTVAPLIINFWNASGPVSIWISVFYVIIIAINIWGTEGYGEVEFFLSIMKVISVIGFVILSIIIAAGGVPTDDRGVIGVSYWKQPLVFNNGFKGLCAVSVIAIFSLSGTELVGLAASEAKNPQKTVPAAVKQIFWRIFLFYIVALFMLTLVVPSDLPGLRTSDNSNVLISPFVIAIQLANIRALPSIMNVVILLSTLSVGNSASYAASRALFALAKNGYAPKIFNKTNKRGHPIYAIAVTLLFGSIAYFTEAGVGGALFGWLLSICGLSTTFIWGSICLAHIQFRRAWKIQNRKLEDLPYRSIFGVYGSIYGVAMTILALIAQFYVAVFPIGKKPNPVDFFQAYMAAPILIISFVAWKFFRRTSFVRIEKIDLSEGAHGEQKQNLEPVINIPVEEIDFPMKVATKESMKNVEKNAL O60175 OPI10_SCHPO SPBC21H7.06c; CHAIN 1..200; /note="Protein OPI10 homolog"; /id="PRO_0000343430" MFGAICAGRLVQTNLQQVADNQFVFQLDSAESLNHIVVFLLPNSPFPVGMGAKVYFQWPGKPFQFLGYLTNEKPSAIFRLKNTIQTLSENENCVGITAMLGISVEPLTNFTETPAVSTSASNVIAKPLPPVTSVAQKILTNLYNFLASFATSQLPPNSIGLGDLRPNDTFIPLRVFQDWHAKFLNKLSNNPNFLDSEDQI O60176 YG41_SCHPO MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC23E6.01c; CHAIN 1..473; /note="Uncharacterized RNA-binding protein C23E6.01c"; /id="PRO_0000082025" MSSSPTESEILPKESHNSIDEQSQQPANTDTLVKDNSFNEQDDQEVDNDYKSNDEPVQSQDPISPNMASNESGNSENTSNYGSSRDENVYQKTTLWMGELEPWVTEAFIQQVWNTLGKAVKVKLIRNRYTGMNAGYCFVEFASPHEASSAMSMNNKPIPGTNHLFKLNWASGGGLREKSISKASEYSIFVGDLSPNVNEFDVYSLFASRYNSCKSAKIMTDPQTNVSRGYGFVRFTDENDQKSALAEMQGQICGDRPIRVGLATPKSKAHVFSPVNVVPVSMPPVGFYSAAQPVPQFADTANSTVFVGGLSKFVSEEELKYLFQNFGEIVYVKIPPGKGCGFVQFVNRQSAEIAINQLQGYPLGNSRIRLSWGRNQNPIAAPALNYQSQVSQTTIPATSLFPAMSLPPQAQFSPYPAVAPSPLALQTRGAPIGMEISIGSPALVPDQMHIPENGNSDTMPVPNTQGKHLSAEE O60183 SAT1_SCHPO SPBC23E6.08; CHAIN 1..550; /note="Protein sat1"; /id="PRO_0000097599" MTECDVQMYMPVNVVQSGTDFECIVKFTNLRSSEDVNLLLCYASIHGEMYLDYVLVRVTEFDEVQRQGLLNKRTMSGLVHIPKVSSSYSVINTLNGMIGNLFGVKQASTLTEASEQKQENAIPVLLTRPDILGVDITLSPGEEKCFRLKRRIPLRTAPTYKGLAFRFQHALVIGVQSATNNACVEHEFEITIVPNVQQQPELPLGKNSGNRQSSKLFADLSKPIIETDAAEIEEVSAEKARRQFGKNGIRLSQDAQEEEKQKKKYEQHIKKLLDGESNEEGGGEFQDHGMRSEINEEVLEEEDEEKIALLKKLESKQPMATRFEITSKQKVLCRLLLSKSRYRTGEMMMIELEGLDAMVRQVHMQLESVERIVPDIRIRNSVGTERATRKVWCRITRGVFELENMSASMVVPEECPETFETQQFGVEHFLRVELLRAVNKKREMQGPAHPRYSEEVQSPSRSRYSEEVQRVSEGRLSEEVSKEEEKKGGRESGQHKRMASLTNSREMQIQHAPTTFAAETIQCVLPIRIEKRVVWMEDGMEGGMEGMQPV O60186 RT10_SCHPO TRANSIT 1..17; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC211.01; CHAIN 18..228; /note="Small ribosomal subunit protein uS10m"; /id="PRO_0000352848" MKRYMFGTLPRVQPKRCFQTAIGKESPKGNSEKDQLFENPFFQQLPSNVAAVYLNPVKFNPSENDVLCASLKIKSFETPKLDTFTDFICRTAYYMKIPIKGPRPLPNKVESWTLLRSPFIHKSSQENFERITHSRLIQLYSVNPVTLETFFSYLRKCNMWDLKLQAKAYEYESIDDALKNFESQSKSTDNFKELLNGPSKKDIITQNAEKLLRNDPIYKDLLKNSSRK O74178 KES1_SCHPO SPBC1271.12; CHAIN 1..388; /note="Protein kes1"; /id="PRO_0000232937" MSKTTSSDDSRDGEGDKRLRSTTKSTWLSFLKSIATFSGDLSSLTAPSFILSSTSLIEYSAYWAEHPELFISLPRGETPLERQLLVTKWFASTLKNQYAARNERYGSEKKPLNPILGELFTGKWNTDIGEDTELTSEQVSHHPPITAYHIYNKKAGVRLEGYNGHKSGFSGPQIHVKQIGHARLILEPHNEVYYITFPLVTLEGLWYGSPYIELGKKSYIISTSGYLTTIEYSGKGYFTGKKNTFKATIVNAKTKSEPIYRIEGSWTGMLKYCTFEDQKRSAWEDFLDCGNYKPVNISVAPIEEQGEYESRRVWKNFAVALDAGDYAAASQEKSKIEEGQRELRRQEEEHNEVWHRKYFEWKDKDEGFEEATKCLRQPVKEGFWYYLR O74316 YOGB_SCHPO SPBC15D4.11c; CHAIN 1..263; /note="Uncharacterized protein C15D4.11c"; /id="PRO_0000304023" MLRKAISTARNFKYPLFNCERRFSYFDMFRSKRKFTSGILTEQLALKLDSELGYVKQVLDETLPKKGYEKALHSFIIHEDPSLNYISALKETAKERIRVTVPVYSSRKSYVQTKPITHSAENENGNETSDELVFFQHSIPAYVQLTNNHGTILCALILCKGMLHFDSISFQSPQNSQAFSSDLRLILQKSQKYTGRKTKHVPASIKSSLLEFLDEQGITVKFMKALISRSWRKENVSYKHWIHNIIGFILPSESSTTKKSDSQ O74317 MUG98_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC15D4.12c; CHAIN ?..113; /note="Meiotically up-regulated gene 98 protein, mitochondrial"; /id="PRO_0000116870" MSIPVMQLKHELALKAREEYLRKELPLKVRANTSRMNPGAKTWIPQINHRKSRNHYNRKETCQFPPLYNVEAKINHSYSAFYRPFTKRENGLWYANPYYMQHGPNGNYHHVYY O74324 YH04_SCHPO SPBC1685.04; CHAIN 1..325; /note="Uncharacterized protein C1685.04"; /id="PRO_0000304013" MKQEYIPLDEFPNKSNEGMLNDEGTSSSGLSTRTRSLELFDNMEESGSFPKVERKIQSLLDELAEVLFQSKQPNDLTRIRKAIAEQLQLWCQACQENADLYRSQQRKLKSRWDSQTDILSQIESTKASLAEVHKAEEISNLKTSITHLDEEIQILQEKLAIVTNQRNTLVKRLQTYDNLEKKKALSMEDRLLTLQEQYDAHANVSSLEKRMEVLKKREDLLRLMVGQALPGMQFFQRLIHQIQAVETKLISILGPTSLSEAALPPLTDVQRTSVLSLLTSTLHSLESARQIADSNTWKPIIVCLELEIVYFENMLTAITSTPVSS O74325 YH05_SCHPO SPBC1685.05; CHAIN 1..997; /note="PDZ domain-containing protein C1685.05"; /id="PRO_0000310847" MTPVSSDYRPNHIFLPKFRPDKITSECNTPQQQNVIAEGLYNVSEPFPIRNTDEERYLDTKEIHHTWDNTIKNVVRSIVSIKGSALRSFDTESAGSFCATGFVVNKTLGLILSNRHVVSPGPISARASFINYEEIDIYPIYRDPVHDFGFFRYDPSSIRFHDVTEISLSPESAKVGIDIRIIGNDAGEKLSILSSTLARLDRPAPNYGIDNYNDFNTFYYQAASGTSGGSSGSPVLDISGAAVALNSGGSNSSASSFYLPLDRVVRALRCIENNTPITRGTLLTEFLHWSYDELSRIGLPREFEYDCRTRVPSSTGLLVVSRVLRNSEVSKALEPGDILIAFKTDSHKSTYIVDFVSLFEVLDEMVGKTIELHVYRPKRGFLTFQLTVQDLHNVTPSRFLEVGGAVLHDLSYQLARSYQFSLNSGTYVASSGMLNWSSGTRDFLVTRLANKPTPTLDAFIDVLVQLTDNARVPMHFRVLGKYEEEFTIVTVDRHFFLASIFSRNDEKGTWDRQSLPPPQPSISRRPSVIPRPQEGSKSMEAIQNALVLVHCRMPYSINGFSSTKLYSGTGVIVSVVPPLIVVDRSVIPVDICDIRLTFQSMSAMGHLTFLDNRIAVVSCDYLPSNSVQLNFVADFLRTGDECTLAALDEDLQLLTKKTTVRSVSVVETERSSPPRFRYVNCEVISLMDSLASTGGLVFREVGDDREIVALWISVVHQDVGGKDYTTKYGLSMSYILPVLERLKLPPSARAQHVPTTAGVEWSHITLAGASTLGLSQTRSSEFYMKSRENGTIPRPLYVISHLRPLLHKTSLGVGDILLEVNGKMITRLSDLHEFETESEIKAVILRDGIEMEITIPLYPEYPTFSSRAICWMGAIIHPTHSSVFEQVEPDVDLPGPEGVYVGSILYGSPALNMLRAAHWIVAVDGHDINTFDDFYHMLLEKPTDTFVQVKQMNRRGATSIVSVRPDPLFWPTCIIERDSNGRWCTKHLQRKTKEVCS O74347 COXM1_SCHPO SPBC21D10.07; CHAIN 1..104; /note="COX assembly mitochondrial protein 1"; /id="PRO_0000192946" DISULFID 13..44; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 23..34; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MHPHLDVNNQKQCADLIRALEECHKSFGKFFGECNTIKYELKACLTKDRNDKARLNRENARMRKKVIEENRKKEEIEERILTDRILQQERKKSHANEGAGDNNN O74348 YO88_SCHPO SPBC21D10.08c; CHAIN 1..277; /note="Uncharacterized protein C21D10.08c"; /id="PRO_0000304067" MSNVEQPFMQGIDDGWNLKNYLNIQSTSLCLDKLCNIYTQGQDENEDAKELQAIKIKIEWCKDTSVLLSSICVMLLDSIHDFLVQQGKITKESISKRDYSHEITIFNFKYAQQEMQNEKLYHFAKLLEPALESLKVTNNHITHATIVGQVSGSEHNLSTAIEQVDVIVNYFYDSSEKFLELGNKVQTLGKAKNKKHWLGVYQSFGKASVDQIQKQLECYNVRMMELNKTDENNESAICESQASSKEDERSDKTTSSSKKKSFTKLISNSRLNLWNKQ O74361 YNU4_SCHPO SPBC28E12.04; CHAIN 1..356; /note="Uncharacterized protein C28E12.04"; /id="PRO_0000116861" MADVIKRCILGPTEAGWFVAKSQIKKPVDQRPVILTHCKLHSKMLEPKAIVYKKNSSAIPKRVDNILLRSQKPKHIECLLVDSKITKTRSLLKRFGSCLDETSTIVLLNQSVSLWEDCYSLFPKTETRPRIYLGRFQTLFKSFPFNLISDSFSYRLNLSKLPRTPLEKCTVARACKQFPLNQRSPLLDLMGSFERDYVNFSNFSQMLSAQLCDSMAFLIQIFPTPLLRQKAANAWIEVLSKLPYFHILDKSFFSPHLLLQSSENQACKFFNIGPQVYFDPRERLLHVKELLKFALKHIDSNDSLFTFLKQTCYTCDSPYAKVFQPDKQSFHSIISRKRLAHLEKEYFDKDVSKLVL O74363 YND2_SCHPO SPBC30B4.02c; CHAIN 1..695; /note="G-patch and R3H domain-containing protein C30B4.02c"; /id="PRO_0000303957" MSNFDDLQILDQLQTSARFRGDTRIRRFKGSNNSKSPFGLNPSSRISQWPRITFIRAKDNYNPAEELCQLIDEQNAHNEAKHQSKEIMLPKETNVKSCEDLSKTGEIKALDIVLFKAITSKGDTLKVKKIPEYAEAFDTTKNVEVSSFPEKSMNENVLIQHSLNLAPSDKEISSTEESEQLCYKEQESEKELYSKDNDDSLDILNVPNLVNDDIANNNAAPPPPLAQAQEQLSTENEDEFDIDDTTDKMTTFTMNKFADLSVLEEDDDDEDEDEELEGEKEEEEEEKEKPEISNYDETEGKVNFSLEDSESLEFDEGSDDYDYAKLTTELVGNTDSLAEDEDDILEEDEDEDEEELLAIFDASDDSEIEAYLSIGDTLQNDFTIYDYDSEDEEYNNPSTQKTEKVSQSKKGAKVKEEKGLKKDRKLPKKMRKAQKKLERKAGKAVAARMGDAFSNSLDDESMNLYAELQEQWLKDKSKKARRRAEREKLRSEGLLGKKSKKKLLRESQKPSSSDSDNASLTRIDKIFINDVYQRMQQFKHSAIEEISLPPCRKYVRRLVHALANDLNLKSRSYGSGNKRYTMLSKTHKFDASSVDLVSLTRIMERLQTRVEYQSFSKSGRKSRMTVSSVRSSKATRVYDGQIVGEDAPEISKENPGRRLLEKLGWYAGKGLGHPENEGSKDSLRAIVKVSRSGLG O74371 YG87_SCHPO BINDING 14; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 17; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 37; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 39; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 44; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 47; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 60; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"; BINDING 63; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00623" SPBC32F12.07c; CHAIN 1..340; /note="Uncharacterized RING finger protein C32F12.07c"; /id="PRO_0000310480" MTDTAKYEKSSARCWICYEEYDKKLCSLSNDSWRRPCRCSLIAHESCLISYITRSGSTRCPQCLTAYRIAKPPKEKSWAVNVLGIGHSLEAGLAQVTFGVGSCLGITKFIYSIFKQTGIWICKQVADESSLIEMLKKPVFSSVVLPLLPCMLVRFYEAPPYDIAFSLYTHFSIYSCAEKISNTSLLLCTLPWVRSLYKELMTRIFDGIVIGADGEFEDSETDWFRQFEAQVEHRNQVEDVNEREDTESEFWILLSVAHVFLDAFTTKILRIVRPILLFPLAGKFLGRFIPGNFTKLEKSIIGAFAALVFKDIFVYGFIAWRKRKPWSIRILDNPRRVSDS O74375 TVP18_SCHPO SPBC32F12.12c; CHAIN 1..164; /note="Golgi apparatus membrane protein tvp18"; /id="PRO_0000343030" CARBOHYD 22; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFESIIVDRAKTTFLGELKSYNFSIYAQWLGILSIFLCIILGIVNLFHVTLVVLFSALTIIEGVLLIFIELPFLSRICPVSDKFQAFTNAFASNYYRGLVYFIFSVVTFLSCIFMATSLIATGIVLALTGLCYTFAGIKGQAFTSSSTLGGTGITTETPPSTMV O74380 YNV5_SCHPO SPBC3H7.05c; CHAIN 1..357; /note="Uncharacterized membrane protein C3H7.05c"; /id="PRO_0000304076" MYPFSFDPSSKLPVTGIYNILLFNLFPLATYLVETFCFFRRWKIACTLLCSITVILAYRMCAVYHHVGYKDVSTFGLAYGFLIMMSLRTCFLSWRDMVPSRNDPVQISAVKRRRPFIRNARWNFVDYALSLRKYGWTDDVVPPYCRKVLTYKSLGIRTAVYVGAFCFVNCFKTRLSNWMLLPISANPWYIQVAFCVTSGFFSYLFINALYYLFAIIFVPLGIWDIAEYPLMMGNVSKTTSVNDFWSRDWHVCTKPYFRVIAWDPTIALTGSKFLASCSCFFLSALFHDFAYWSISGRCSPAFFFQLLIQPFLINLEKRIPLLRKYHYWVLIIEMLINGTYGMGVVLLKFKWKTCSQI O74383 YNV8_SCHPO SPBC3H7.08c; CHAIN 1..120; /note="Uncharacterized protein C3H7.08c"; /id="PRO_0000116862" MSIMRSIMSNRLVRWSREYPELFITWCVMTYTFGVAGYMLGQRGLLVQHEDQVRIPSKNAHPWEDTKSSSGKSDESLDYSYKYYPRGDRSKEPRKAPSAIQYSTFPVKGVSEEVLERFSK O74394 RM39_SCHPO SPBC4F6.08c; CHAIN 1..55; /note="Large ribosomal subunit protein bL33m"; /id="PRO_0000350999" MAKKNKARLLVKLLSTAGTGFFYVRSRPKAAPKLAFIKYDPKIHKRVLFEESKMK O74397 ASND1_SCHPO ACT_SITE 2; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" SPBC4F6.11c; CHAIN 2..548; /note="Asparagine synthetase domain-containing protein C4F6.11c"; /id="PRO_0000314119" MCGILFALAEDRDNLLESPSFSALRKRIRARGPDFFGKHKLNSGPWNLHFESSVLHLRGPSDHLTPQPHVDSFGNVLCWNGEIWQINHSDHHKFTLNRNENDGAKLFELLNNNPGDIEKILGSIQGPFAFVYYQVRTNTLWWGRDRLGRRSLLYSLRDSNFVLSSVGNSSDFREVEPGFHSVQVDLIPKINFSKSLMQLEKTNPLPPVDESFLMGSISSDTVDTLHTYLIKALQDRVLTIPKLCSSNLDCSHYSRVCVLYSGGVDCGVLARLMHDIVPNNESIDLINVAFENPRFTETYRDRETGLLPDNFDAYDVCPDRQTGLQGWQELISVCPARKWNFVAINVPYTEVCEAQEIVKTLIYPNDSVMDLSIGLAFYFASQGRGVLLQNVDDIKLKHQLPSYTIKAKVLISGLGADEQLGGYMRHLRAFERKGMAGLEEELQLDIDRIPHRNLGRDDRVMSNQGKEVRYPFLDERLMALFSKMKTTDKMRLDLVGGDKLILRELGRRLGCPLASQEKKRAIQFGSKAAKMTPGTGRTSGRKKLEVCI O74400 YOCE_SCHPO MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 225; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 247; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC4F6.14; CHAIN 1..674; /note="Uncharacterized RNA-binding protein C4F6.14"; /id="PRO_0000310817" MNSNSTLFVRNLAFQTKQDDLTNFFSDVGPIKHAVVVTNPETGENRGYGFVTFSMLEDAQRAAKELKNKKLHGRILRLDFATPRKRSEVDTDQNKAVKKTIRQDNRPRLIIRNLPWSIKKPQHLEPHFSKFGKVREIKIPTKGGGRMCGFAFVWMKDRKAAEEAMNSLNGTEIDGRPIAVDWAVSKDAFEATTLKDASSEEENKEFVSDEGHSIVTEDASADSESEEEVDGHSEGKELAGESEEEGSNVDDVEDSGDSSSDKNSINHEIRDNEGLEDTVFVRNLLFECTEQELYNHFRQFGPLAYAKLVKDPATDRSLGRGFIKFRYEKDCQNCLEMASQLPTQEPTEAEKRFLPSVLVDEGIDTDSVSSRFLLHGRLLKVTSAVTRKEASDINQKSLQERKQKMGKGVDRRHLFLLNEGKIAADHPLFNSLSETDKTLRSQSIAQRKKLLEKNPTLHLSLNRLSIRNISRHIDPKILAMLGRQAIRGFMDDVSKGLRANITEEEENLDKGHRLKRGKSGGVLKQAKVETEKAGAGRSKGFGFMQFISHKYALMALRWLNGREITVKKIIDAEIEWARKHKIPEPQLPNIDYNDRPRRLIVEFAIENIQVVKRRQEKEKSFRQKAKQLKQQEDEDNLKRKRSESDVEDNEAKEKQAKVARIIQRKRMKRRSRKN O74415 YJL2_SCHPO SPCC14G10.02; CHAIN 1..1568; /note="Uncharacterized protein C14G10.02"; /id="PRO_0000116815" MESGSIDLDKEIDELSRVLLEHPAHVEKVLKTVEFDKSALRYIDAILDHHLKQIYRNLTSNSPLHTLSLLQKMASWNNGLACVRVFQAIDWNSKIFIKMLQLPNQIQNSRKGNKRLKITISKKRSSLLLLFITFLRLGTPEIRLEILNSRKLTTPLFKGIYNDEPSVLKELLQCWLTYVLLDHDVSRATKLSYFNEWSLSCLASLYSRDDEIDGISLCNLVHKFFVDACTVPGEGLCFVSNGWHLQKKVDGQSKTIFNRVLQSFVFSLHVHTSTLQRELVLKILKACPDITASFIERNSLTSEPVLSYQWISFVSLLQAILGMGIPFPFYDAETRTVPPTNIIIENILPSSFSKPVVLKALNGNDKFVCFLTVNTLLASFKRLESVLDEIKRSELSEDNKVELVSKISDAILLRLPDSQTFVQLYSSTESDLLKEGLSRILLYFFTYFPENILKLKIDTSIFLRLDLSPGMLDRPFSRLHVENIIQILRYLPEVKWFDVVRSPFVFLCLMYLQTSHSKLRDAIISTLNDVFSQTIIFCPSLAVPPILTILASLQHTSPTQHKAVLEFLNSCINRCISRVFAYLDVCVDCFKKHSVNSQKKTAPEVSPISVTLIEQIPFFLQKRDISDDSKDAVLSWLSDLFSNLVCTGEDANCLFHLLENVNVTAFDSDYTLKPFNQLMSFIESLAVQKLPDYVNQIGSLSQYLLYSTNDELSNSGIQKFGMNLDFLPLYVVIITKRIAIMLQSGDMRVKKFLELIRELVEFSKEETMATSQSPIRTLLSACINLRPFLLQEQYISFNMDFAEFLIDTNASIKGSVVNTCVLDFLYKSFSDKVQENYNLIRIAAKFMLLWTQEEFIGFSKALDSFLSENDDLIYKNLDYVAPLLFECMQFTSTTNANMFSNNSISVLLKAAILKPTKLTHGMFDALNTMKPIISDFTVFEPALHTVENFDLTDCADEQILLLSSFVNFVPLFRKVIWNLLLNNKEALIQKYELLAILCCDLAKQYVAEQSQYDLERIRSFCSEVVENNLDLVLQKSHLIELLFPLMKLSDPKIQYYVKVSNALSEKYLPQGVLELLVLLQKRIDIPSSLRVQTIMRIFAILTRVLSDSPQIGLSLEKFLTNFEALIKMNVDILRDEIDKSTLNSFLESAIVHVTSFSNLRLCLTLAFTMTAEQCDSSRFLQMILAHEKNPLAGEDSSDEIKATMSAIICKLTIIGKNYTLSVLDQILKLFKGRYTLHDSLLCELLAYFETLDDISVASRYKGWVITDEYDMMLLARKDGSGVLEPKIAANTVNQYPSEWEKIDLKVFDDLETTEGLLSSYCSNEWNREVYHPLYALGITASLLHSNQQVSNIQVIVQQNFLGMIVMGLSLFKEEARFACLNFLRNFIPILDEQKFREKHLIKLVLASIIVNVPSSENRLSTLMANFYAFSLTVMMKPTHPLFVGINRYYLQRQHVDVTDIPMYYELLYPSTDYTKSVYWLLTLLHAGLQTNQDLKIYLRRHVFEMICTLYNSCVVNSEIRTLIEKILLKVVALGGGPMLVKYNAIYPMLQMVIPSFQETKENTVVSTT O74416 UMP1_SCHPO SPCC14G10.03c; CHAIN 1..129; /note="Probable proteasome maturation factor ump1"; /id="PRO_0000065719" MKIVPDVEPAAEVSGNFKVSVLEPSIPAVHRVENKHPLESRLKNWEAQQQQIRLDSMRRIYGLHEPVRREMEQKLASQSSRPLALGGSANFHLDILANREAVLDETDIYAAPIPLEMTYQNEMAIRYGL O74419 YQ52_SCHPO MOD_RES 571; /note="O-(pantetheine 4'-phosphoryl)serine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" SPCC162.02c; CHAIN 1..981; /note="Uncharacterized protein C162.02c"; /id="PRO_0000193219" MLCDSSESVSFSSISKEEDTPIARLLKNAKETPDHRFISVYNERGIVAKYTYTELLRRVNTIAKFCDDLGLGKTVGIHMGHELDFLCSIFALWATGRTCVIFNQIWSQQVVRVLVKRLNISDLLYHEYKPKFEVDTLNATSLASLPLDIDAPCIRAGLEPEVALINHSSGSTGVPKSMPFLMKKYALGYDYGTPEFMNHLSTPMVMATSFALTTLSWINALYCNGNLLYPSSSISATCTSEAERLAWNVYYALRAGCERLIILPNLLVLTLQIMPDKEECFPACKLVAAGGEMVPANMYHTCKRVLPNATIYPQYGTTESGLVSFLAYNGKDTLHNKELVYFPGKTVKKLMLVTEDNEAVPEKIGCEGFVCVVTDVQSEPYVGDDAETIQSRNSTFINYDGQPAVRFADLAVWNSYKGKLGITIKGRLGRRVKRNGVFFDLKYFDQVVVGLKEVKDAFSFFIFNRFVLVYVPAYNGVDPVTLKQKLNKELRDHHLFSSCFPLADIPRNAAGKVDLKSIETYASKCLSVEDQRLPVLLNPVAIEISKIASKILQNPSLEGKDAPLYSCGLDSIHSVRFFHAIQSHFHLEGPIRYNMNSNCTPNSIASIIQKKSYNVSSITYELLNEDACALSRTIPKLSILPTNGQYFLLTGATGYFGRRFLEYLVKLNISVVCLVRESSDEAAKERLISLVPSLRISSENIIVWAAHVEEIRFGLDDAKWEFLVENVSRIYHMAAEVHWMKSYQELRPANVLGTKTVLELSVMGPKALYFISGGGQQEVELDDDTQSAKASGYALSKYVAELLCRKISDLGHPLIYVIRPGFIIANDGEILSRDFFWRFVATALRMGIWPQSDESQSLVFHISTTDALCMTLTQILEKEADAYAPLLAYDKFDGDEFACICESMKNVKLDFVTLEDWLKALEKDVDEKGEDHPLFALQHATKFALKSSMTPSNGLRNIYPLSETFLTKEAIANGLENLYIE O74422 YQ56_SCHPO SPCC162.06c; CHAIN 1..210; /note="Uncharacterized protein C162.06c"; /id="PRO_0000303921" MHRLFGRKPPTQPTASLTDAIDSLDKRSDSVEVKIAKLDAQLSVFQQKIANTRPGPGQTALKQRAMNVLRQKKIYESQLQQLQQQSFNMEQAAMTTESLKNTMATVQTMQETARQLKSQSKNVSIEKIEKLQDEIQDYMDAAGELNEVLGQNMTDINVDEEELDAELEALQQESSWLGDQSTAEKPSYLMPSNELPNFVDEEVAEPSTAQ O74432 GET4_SCHPO SPCC1672.12c; CHAIN 1..303; /note="Golgi to ER traffic protein 4"; /id="PRO_0000228106" MDAKIKRAEGRLREDPYEGHQMLRTLVNRQVKAKKHDDAVALLYSGAKTLFEIEQTGSAADLAIYMLDVYEKASYAASLDNKARALTLLGLFPAEEGARKQYVKRLLEWSKSAGPQGDKDVHFAVATMFVKWKEPASAEKHFVLGNEKSARAYGETMYYWFTSDSSISPDTFAGRPVLNYLLAENLISAWNSLETFTKHFTKSNAPDVENMSFDGKDFPVFKEYPQMNFLHLLIFTAYRKDKETYLSLVQKYPKKQDWEAALAKIEEIYFGIRPVSNQPNILANLMSSLFSGPPAATNQLDLE O74438 MCP2_SCHPO SPCC1682.08c; CHAIN 1..703; /note="Meiotic coiled-coil protein 2"; /id="PRO_0000234662" MQSIDLRLPSTSANHSISESLEHSKSELNELSNVSESESYFDITKKLHALSTVVQRQQREIDNQKRDLCTKTKHIEELQTLLSNANIMSDGASSQNDAFAHNPSTSVSVELVRPVVGTKKHAVYATSAPKSMSLQDSLSVPSATALADVSSSLNYSRKLSSNSIKSTNAPVFGTAVKNVTGENILSASSSEENLNSNRNGDPKFRFSVSPWISSSNFNPYEASLANFQSDNCKLKSHNSLPSIRTNVRYSNSKPSTPLSPEDVDLGTYTVKNRDSWSNEVNLSASTNNLSTNTSGTLKPYSLSSSRSSSYSKGVNSAASLQSIWETMNNSNPSVIPESTSSREPAARYRKISERNAVYDWNVIIDKIIVSNDQQSSIFLQQKLKISSYDMKQNIVDSIISQIHPLMLNRFGNFLVQRCFEHGTAPQIRQMGSAMLGNMLKLATDPFGCHVVQKAIDNVTEDIKLAMMDELFLTIDVTIMHHYACHVWQKLFETQWYEYPVNVMNRVNNALRGKWHEVAVGENGSLVVQNMFENCVEKDKRECIEEIIFHLDGIARGQWGNWVVQHMVENGQGEDLKRVIDALLNRAVEFSIDQFASKVIEKAIKSGPKNFISLYLKQITNARVDRTRQPLIDIASDQYGNYLIQQIIQLGQPAEKNLVITHIKKHMVSLRGSKYGQKVAYLVEKWNSQKQVSSVINYNCNTDL O74439 YJE9_SCHPO SPCC1682.09c; CHAIN 1..300; /note="Uncharacterized mitochondrial carrier C1682.09c"; /id="PRO_0000310800" MAPVQLKNKESQTARIVGSASAGILELSLFHPVDTISKRLMSNHGKITSLTQLNTVIFRDAASAPLLQKATSLFPGLGYAACYKIVQRIYKYSGQPIVKDFLNENYRHTFDKTFGKGSGKAIMHATAGSIVGIGEIFLLPLDVLKIKRQTNPAAFKGRGVFRILADEKFALYRGWGWTAARNAPGSFALFGGNAFAKEYIFKLKDYSQATFFQNFFTSIAGASASLIVSAPLDVIKTRIQNKNFDNPQSGFTILKNMLKFEGPTSFFKGLTPKLLTTGPKLVFSFTMAQTLIPFFDKLLK O74447 YCG2_SCHPO MOD_RES 19; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 25; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 47; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16C4.02c; CHAIN 1..548; /note="Uncharacterized protein C16C4.02c"; /id="PRO_0000116544" MHIPHFHLHKGPKGVRTISYEQLLSEDDSYASEKLSEDHVTEVHFVTDKDEDSNASGESRGSMELLENCFSLLHAQDDTSKFVSLTMLAKLLNDHPNLIFKCWERMDMKFLDRLLLSTHYEYVDLGVSILLAFCSEEAILRSYEVKKRVSTLLQCCLKHYDLCIPVICTLSSNPKSAKYLLYYTSFIINEFPFEQAFEILSNALYALDNVQTYMRPIFQGIDKRRGWKLDCTFSFFSDLFSRFPVQSWYSEAIRANLQPLMDAVVERFITDKNLSSATVILSNLLKAAGPASIMPNDGFMILVIGRCSAEIRGSLGMLVKAVGQKGKHGTVSYTVCECYEVLGLLIRYLCENCDVLAQRIEPDKFFQLQRSLTELFSDTMDFLRDAWDNNKNRDNLASHVTVISAVATLCLWLTEDDSQYAQASGLMDIFVYLWRHSWSNGIDYAKWISVALPSMLSNKVFFKAFKDFDAWKVVYDDFIKCNDDLKGDKSFNDYILSTNEEDGEDERLAQAIQDFHILIQLNSLVPQSIWNDDIWQEPYWKNLLESNF O74455 6PGL_SCHPO CATALYTIC ACTIVITY: Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31; SPCC16C4.10; CHAIN 1..257; /note="Probable 6-phosphogluconolactonase"; /id="PRO_0000090086" MSVYSFSDVSLVAKALGAFVKEKSEASIKRHGVFTLALSGGSLPKVLAEGLAQQRGIEFSKWEVFFADERIVPLDDENSNYALCKKLIFDKFEGFDPKKIHTINPELLKENPIDPQNVADEYEKQLVHVFANSSTVKVPVFDLLLLGCGPDGHTCSLFPDHEVLQEDVAWVAPVTDSPKPPKDRITLTLPVVTHAQAIAFVTTGAGKKDILPIVIEDFTSKLPSALITRNNLTRTSWFVDDEASANLERSSLKVFPQ O74460 YCGG_SCHPO SPCC16C4.16c; CHAIN 1..206; /note="Uncharacterized protein C16C4.16c"; /id="PRO_0000116546" MDIVAETQIEEESLIPDATSTPLETEVVADTTLRKTALHLAGVDNLSEEQVKGFISAYAPESQCTIEWINDNECNVVYADDDVSRNALFHLIMESPTEFSEELEYQTKPHPTVPTCQFKIRYARYGDKKVKSAHLYSRYYLFHGDPREEKAQKSKSKSRNQDERGSPLDERLGPKVSDLTLMERIFQVRRKPRKSRRDRRSRVSKR O74466 YQC4_SCHPO SPCC1739.04c; CHAIN 1..274; /note="Uncharacterized protein C1739.04c"; /id="PRO_0000116889" MNSVPNELTKSQELFGQISKISHSKISISELITLLDIHYSELFTKNPWMKKEVRKLASEFVENDPNHLLSKQDACHLIEAFVNVSITSPTLLTSVDPVLYQQLEASSTNDISTVFEDESSSLPIILHPKFSSMQVRTVTSPKDAFVSAFEENKFHFAATESFFEMAFSKIDSCLTSVQSTKKDSIKSRLVERYIQNEESVKRPDKSPFDTMTEATLQSSSDKSENFTKTLLSNVLSTILSVQVIFATVIALIAISVFCFLHTSSKTTSSKTRPS O74468 SUMT_SCHPO CATALYTIC ACTIVITY: Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856, ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107; SPCC1739.06c; CHAIN 1..496; /note="Probable uroporphyrinogen-III C-methyltransferase"; /id="PRO_0000150386" MIVSWSLKDAVVVVVGSGKNAYRRVNLCLSENSSKIFWFCRSSADGGFDVGHLQLDAKKSDAIEILPISEFDPVRSLTTLGKEETDFLVDAVFVSESNHHEKEILHRTCKRYRIPLNIIDNPSLCSFTLPATWSEPPLQISLSTSSNGCRLAQRLLRHVVSSLPSGMPEAIERFGRVRAITKTPEKKQWINHVSDFWPLEKLVRMTEDDLLAIVSDNFSLPLSSSQSSSLANSYESLSTTLDKPSLTLDPEAFPTHKRGSIALIGSGPGSPDLLTVAARKAIMKADYVLADKLVPEAVLQLIPRHTPLFIARKFPGNADKAQDELHQVAFDALSRGDYVVRLKQGDPYIYGRGGEEYLFFTQHGYVPTVIPGISSALMAPISAGIPVTHRGVADQFLVCTGTGQKGSMPKIPSFVPTQTTVFLMALHRLEILVQALIESGWPRVLPVCIAERVSCPDQRFIFSTLEDVVEEYNKYESLPPGLLITGYSCNTLRNTA O74470 YQC8_SCHPO ACT_SITE 157; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 172; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 176; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 33; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 60; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 78; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 105; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 172; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 176; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 206; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPCC1739.08c; CHAIN 1..261; /note="Uncharacterized oxidoreductase C1739.08c"; /id="PRO_0000374035" MSTPPANVTTAHVLDLFSLKGKNCVVFGAAKGIGFSIATAFAQAGGNVIITYLTTDPTEKAKKLAEETGVQVHTLKIDISRSDTVEAGVEEIQKIFKEIHVVVANAGMPFRRSVLDSPPHEFEKVMNINTNSVYRVAYYMGKIFKKQGFGNLIATASMSATIVNAPQHIAAYCASKAAVRQLCKALAVEWAEFARINSVSPGYFATDMPGYEFLKQWEPYVPFKRLGLTPELRGTYLYLASNASSFVTGLDLIVDGGYTCL O74480 YQJ7_SCHPO SIGNAL 1..26; /evidence="ECO:0000255" SPCC1840.07c; CHAIN 27..332; /note="Uncharacterized protein C1840.07c"; /id="PRO_0000310853" MSSLGKLLKLTLLGILLSFSCKFVFGYFNVNQLFDHEFIKVFPNFKGNVEAKIKYPTVVYAIGDIHGDFPNALDVLSAAGVVSPVFPHEWTAGNATLVQTGDVVDRGPDTRKLFRWFNDLHKQAEKHGGRVVRLLGNHEFMNAKGDWRYVHPGDKASYPEPSEENRIIDWGHSGEIGNLLLSEYNVTYKDNTTGSHFMHAGLSPEWAYREETVNELGKELLSHFMSREKIPEYLEDFWAIEGPMWYRGLAQLSEEEACEVALNVTKTLNVNRLVMGHTPQFHGIVSRCEGRILLIDTGLCSAYAGERAVLRISQNDTDSIVEAVYRGKIVKL O74481 YQJ8_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPCC1840.08c; CHAIN 25..561; /note="Uncharacterized protein C1840.08c"; /id="PRO_0000350970" MELGAWRSILYIAFLFAITRHAFCKAVNLVHSPEGEEFENILSSVSATVEKKEVNNKLIMPTANRDNQGVREELLVSSFKERKLLNTNSANLRLNSIGSYEMIDFKQINSEFFLSHRQHGFVLFIDSKKKPRQSFYTDSATSIVQLSKKYRNKIKFKSVDCASSLEKCEEIGINSFPSLVYYNNAGQKKVFTAHTPYEVLSKHADLITELDETDGKVYPQSIIRLEEFKNLKANEPVFFLYLHDYGSTPEDFDSLRIFARYLVGFAPLYRTDDEKVIKTLNVTRLPHLVAIRHGVAFSYSERSVSAMRNTFQLIKWASLLKYPLVPELTPAVVENLDSDSYLAIALINPTSQVKASKAISTVQEIGLKWTLKLREVERKQLLTAREKWWDHLRMLKQKGYDDVAFLAAEYSLPLPKNKKVTFVWVNSLQWKTWISHTFHIDPMGPSRFVLMDPSRMFYWDSSAKGLPLTLDDSSLILDTTFRVLAITGEGLPHEFSIPRGYVYLSEIKQYSSLILISLWISLILFVSFLNRRLILHYSFESVHQLKTLTRKFIYSSLLKQD O74482 YQJ9_SCHPO SPCC1840.09; CHAIN 1..276; /note="Uncharacterized protein C1840.09"; /id="PRO_0000318145" MKIVVLGGSGFLGHNICKLAIAKGYEVVSVSRRGAGGLHNKEPWMDDVEWETLDAQKDPNSLLPVLRDASAVVNSVGILMENNYKKILQNPRGPVSHLINSLSSNMFKTGQNPLAPKPEEAKQSKNKVTFEAINRDLAIETAKIAAKANVPVYCYVSAHAAAPGLDPRYIKTKREAEREISKISNLRSIFLRPGFMYNFNDRPFTGALASLFTVSSSINRATSGALNFLGTASAEPLPSEEVALAALEAISDPSVKGPVEISELKSMAHKFKQKSL O74487 WTF20_SCHPO SPCC1906.04; CHAIN 1..258; /note="Meiotic drive suppressor wtf20"; /id="PRO_0000193232" MKNNYTSLKSPLDEEDELKTDHEIDLEKGLLPEYNSEEEGALPPYSDISKLANPVPEDSSTGPTEIANPNVERRQEFKDSHPNIYFLLRLLISVLAVSVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPILFIAIFYFYETWTKACGKGIKHFLKKWRNMFFTFCKSPIFCLVLLKAENKLSSHLGDQQWGWKCSASAFTFMAVSSILIFIAETVEPGSCSTDLVKRVQAYCDYEARQYASSNTAIPLREMNPENEA O74493 NUP_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPCC285.05; CHAIN 22..348; /note="Probable purine nucleoside permease C285.05"; /id="PRO_0000372355" MLFLKLVASVLALMTIVPAQAGLIGKRSVFKPKVMIINMFSLEANAWLSQMDDLYANNITVVGLNRLYPQVHCNTQQTICQMTTGEGKSNAASSIMALTLSPKFDLTETFFLISGIAGINPYAASLGSVGVARFAVDIDLINSVDLRELPSYFQSSGWEIDTDPYENGSSNEIVYPESMPYQTNLYELNNTLITAAMEIIKDVVLEDNEKAASYRKLYNESAARRPPFITQCDTATGDNYWAGTYMGDFVSNITNVLTNSTGHYCTTQQEDNASLTALTRASFDGLVNINRVVIMRSGSDFDRGAGNITALANLLNSTGHVSSLACDNLYHAGAPLIDHIVNHWSYWT O74497 YCRA_SCHPO SPCC285.10c; CHAIN 1..382; /note="SPRY domain-containing protein C285.10c"; /id="PRO_0000314094" MHPDQIRQLRLQESSNTHPNLAILFIFIALAAVIVLLICLLSVILLLRYTRHGRILLKNTNPGELDDEALENEHIDEEGFSLLDDMGKERYLQAREFELNSMKSNVNTDAKLLDFLQVQEKGVLAWHFIPNQEYNCYVKNKTELSFLGNEECCMQTNLPLQRINEVYYFEVKLLDVPIDTLVSIGLATKPYPPFRLPGWNFWSTAYVSDGTRRSNSPFTGKPYSSFYQQGDVIGVGYKPKCNRIFFTRNGRRCAELPCTYRNLYPTVGAIGPCTLHVNLGQAGYVFIEANIKKWRLAPAVGSLAPPPSYSTSQPTISWDAASESSAGTTTQGDTNRPDKSKNRSPPINFDGTSYDAAGNVFSPSSSNNQAYQMHSMPATDEV O74501 YCRE_SCHPO SPCC285.14; CHAIN 1..1150; /note="Uncharacterized protein CC285.14"; /id="PRO_0000193511" MSKKKPIVQYYDPFDLWPSIATDIESKIPLRNLQWVESYQYKKHTITSLDLEFLPWLEEFSSQDTSKDPTLLNIPLVNMLFLPEQDGEIYKTQHKPLATKWFQKVSKNENQSWMIVLVAEAQQAKRSNSLRRTHSRSSSYFAVKSTIDRVRGDFNTGNINHCVRLDYVRFGTPDAEGWNEFLKCLEWAVLSSLDSRFLQLSEQIRSIKLFDSSIFSDYLLFFLQKERLAASFFDLVLYRESLEQCEDMFSTLSKIISAIDGKKENISKYLGEGSDAQPDLKDFNSSFLILGSRYNTLHNLLADGDFTLFHFTLFLLSKIILLNLKISDYEKAFSTLQQALLFLTSSFFNEFVQNNLEIIAAFNYDCYTLLFKKITEAIHNNDTPIPLCCAKILLYARRQLTRMARWNNLIDDSSPLLWREPSFPLIEHHDNSLLDNRFQKLSETISSTSSFLSEYYRLSSEALSIFKAYKNRYSFVNTACDTGLAQYLLEDYENAYASLKNVDVQTAWSNDPLEEKWSKFYVDLLEKLEKFDEALEFASAISKGKVSIYNKNKILELSKKTAKSKVWNLDDFFTIEIPHMMAVVPHDDGINLSFMCESKVFDLESVDSVTCNYVLSSSKNPMNLLFTLHNSITDGKLNVHCNDIIPGRYHLKTIVFKLKDSVLSFQKDCLHSNKQIEVLNPTKHSNHLYILQSKISQQFQNDGIFACIPIMFGERFYKASCSEIKLSYIENSGFTNLEKSFLSEESHCGLESKTDSLVIKNIQKVPGVAKLYIPLTNTPVEGNEFLINLSYILESGQTVRFGKVLHIENAGIVEANCEKTNNMRDPLTSTIFLHIQPKEPIIFCSWNCMRKTKQGTYDNVFDIPYNIPVLSPMDCFTSCHFDSDMSIDLKFSMNCLRLADVVFMKLCVNIWERFDFIDIEHIMPLLDHACQQISLSNITQGTVVLPEEIRKLNGKKILNSFFDNEELRNEFSEFIQHLESEVSFNSLRSFVQEFEKKERLKNLPFYFSLHQTIGPLPFKDEMQSTTIEYIWKIPQKVLLNKPTEITLTFLRSLTHSKKEKQGQSFEIFYNFPAYTTTILFAGPTQRKIVWEKNQTTAQEQVTAVFLTAGRVMLPEVVVHSKDDDISILKNTKYTLVGRPLNDQPDLDYAP O74504 YJD1_SCHPO MOD_RES 374; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 376; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 477; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 493; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 574; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC594.01; CHAIN 1..791; /note="UPF0590 protein C594.01"; /id="PRO_0000116812" MKLKVSIGCDAQHTQIAWVNYEGRPTEVDGPLWVGRILVRVRDFDGFTPDGSPPKRDSEYFRGRSRKFQIQAEGRFKKEYNGDQVIYGTQFDHMISTFPESAFRAGMRIAKYIDPAVYYDKYARSPYIMSPFVACVNTLSAWPAPSRLEDAVISLVEADSQESDTESLPEINDSSDVSLSDLPSTNVTPKKTTTQIDVQTNIVTPPITVTAVPDSPNPPAATPATVADNDDLSIVSSDSGNTTAPRKNRHRYWSFAGFSDSTRFSHLNVPAAIPDAPSVKTETSQNVSQLSVKSAATSLAPVEDDEDDELLLHRHITNKHKDFNLHVKQLGLLHKPSLDLEEGYIMDENYGKDVYKHGISNVPDDENEDDLQRYFTALEMQQDQKEQHKKSKNKDPFRKITHPSLHLGKFSTPKLIKRMSLRSKKSLRNDSKSDDVGNSTHRFSTASAASTSAVKTEKEKKMSAPRRSLDKLIRIGSLHRHHHHHHKTDLIESDSGIEASESNRRKSDIFSFSGRNSFSVSRPSSSHSTLSYANDSASSAVNVAGETGSLPPLREQTSITSGVPPSNRLKKHVSTPEKIVEERSIDEVSQSNTPSSKQLPQSVDGKTVTANANSTTVAKQPTSNVALTRPKPVRTATSQSKIPKPVKHIPSDSNNLDPQLGPWRFANPKVDPIEDNSFIFGEHKSVKERRKYFSSSKFCRENFFYDKDVVYCMSFFSPHMDFNTFNLNIGPIRLNVYKHLNSDGHQPIRYMMRETDDEDAVMFVVEFDLLEDDDETVLAEQAKERERRKQT O74505 YJD2_SCHPO MOD_RES 26; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 27; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 263; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC594.02c; CHAIN 1..489; /note="Uncharacterized protein C594.02c"; /id="PRO_0000372345" MAPAVFTSDYWKKYFSNKKKPTVKNTSDIDLLHINRGRQPFDEGLSINEDSFFYRHNIHVPRIVYLIIVACGSFIITGGIEFAIAYGMYKKTETSVRLWRLPDTLSGDAAVTNFVQAIVTYWVESILVQGDLRSGLVKPIYFGWWPENFLLREVLRAKPRYHFKFIVFRWMEWLVFVGLRGLVWSVPLWFLFWPATVGILCAPGRHEGNDYYFNNYPAPQVFKLIFGGGEGFVLTPWIAFLHMYMYGHYLHVAKNQKSLPKTSDLEQQRGTSSSQPSENDANITALPKPEPKMYENSDLTPARTPVTPAPLEKPVNLAPEVVEPTNAAASPLQLNAPKLTDVDDSALAYDPTKVQDGEDRFVHNDVPLENAENPSRFVHSDAPIDMTHTTTVISEAQNLPSTLLPQDGNAVHHDTDAPSLSNVRKSVDSPRVPPSFSDDAVSSFSLVTAPSINNVGGSTAPSVNNQEREYDYDDTSSRSSTLTERPVVH O74507 YJD4_SCHPO SPCC594.04c; CHAIN 1..344; /note="Uncharacterized protein C594.04c"; /id="PRO_0000372629" MTLASTMPIIYSASDAAKWKVAVSPYLYQLSNLKLLFTGKLNFADFYYNTNPFVVGLLLSFILGNVLWGVSVWTKNTSQVDRLWPILPTAFSLHFLFYGLGYNIASRRLMIMAFLQTLWSARLTYNYYRKGGYNRGAEDYRWVRVRQIMPKWIYPLFHYFYIHIFQVLHLYLLASPTYIAMLAGNERAFGAWDWIALELFMFMFVLEMLADQQQWDYYEARNHYNVDKTVPPRFKYDLLSLGRGFNATGLFRWSRHPNFLAEQLIWLSFYLFGAIASESLLNWTIFAWLGLVGVFQGSTRLTEKMSCEKYPLYRVYQDKVGRFFPRLDGSHWDIVDDDASLKED O74516 TRM44_SCHPO CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43100, Rhea:RHEA-COMP:10339, Rhea:RHEA-COMP:10340, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.211; SPCC663.10; CHAIN 1..502; /note="tRNA (uracil-O(2)-)-methyltransferase"; /id="PRO_0000249909" MKVPAYWKPREPKNALTCDPPVPYDLQSSYQWQSILEHDTCYAAEVFDKMMIELVYHPERTSSVIMRTDIILDSQEDDSILNKQKSVFENLDERYQISRWIDRRIIPRNTNLDATMDQTVVVLHEKLENDRILMYLPHLDKSLEQPYNHLPYYHPAVAGIAFHYKGSSVEVLYLVEKDFQRELSSRLLRTAHMLLLVLHKHCKGAVEGYQKRMLHDTVVERNKFQDTYVILKDKYAKQLVDNWVEKTDPGKHVFEDLAIAAFLIELWKQTYSSNKEFSFVDVGCGNGLLVYLLLMEGYNGYGFDARKRKSWETYPLWVQVKLYEKVLVPYFLHDFETKIPFPQLPAGFTMSAANIHDGRFSENSFLIGNHADELTPYLPILARLNQKCYFMSIPCCVHDLTGAKISWALPKPRNPKHGGRYAMYIEWLMQLSEEVGWNIEVEPLRIPSTRNYALIGRKLLSNDLLHSSLSTDALYDIVEKNHGSQGFFVHAMQVAAANSRSH O74519 YCPD_SCHPO SPCC663.13c; CHAIN 1..144; /note="Uncharacterized N-acetyltransferase C663.13c"; /id="PRO_0000310294" MIELDAINPNNLKILEVINEKCFDPEIIIFPTSFYKDTISVGPLAQYAYFNQVCVGAVRCKKETHNKSHKIQILSLAVLPAYRNRSIGTKLLEYACETAAEGKAKEIYIKLSPKLDVSEWFIHRGFIIDESSKTEDSVLLSKKL O74521 YCPF_SCHPO SPCC663.15c; CHAIN 1..678; /note="Uncharacterized protein C663.15c"; /id="PRO_0000372340" MDSLTSILLLLELQHEFSGLKVPGRLAKFGPPFRPSEEFADAEDSPVMKMIAQSYIFTPTLPGVNKAPPEFWSDKLQPLLETIGKHNLSDSYDHGRVSKRKMVGFAVVVVLHVLSKGLLGKATPLSEDRKPTSNNEEEDDADEAKSSNADSSTDSVQKSLANVNMDDANGPERLHYPSVKRLREAYSLLVYGDGLQQALDRISVSEDVDSWDEPLRSVIENIRYTIAVILHFSFVTVDAIPESPHLVSNRKGPEGVVERLYNRIPWFLTRQVLRVGNAGLLMSGLTRLFLMKPLSWFGESRNLLQTMLAGIFNADLEHSESTMVETDAEFEDDAKWETMRKALQWFTQLSRTEQDDVRSQSINKELNITIAILEAYEAQQTETTETEGVDKEDSDKASSVQGNEDEVPDTASETEHSEIEDFHFDPYSEKGVHIAMRYFDAALTHRDRECLIHDLCDNDQLNDVVREFMNAFYNIIYEAHQAADFSQAIYDFQYFLWDVIQLSKAGAPLVKFINLVERYQSCFVRFIHRLVVNAPDLCGEWCDWYRHCLKQFSVEVKTPDAVDVAHKALNTLDEETKHQVLEEIGDYVKELDEESKKAIENKDSTSEWLLHLYNFFGSAIITPTTAHGVPQPQLPNCGMKLNRTKEKLLTPFRNLLMEQLNELQAKNQETPSEMTSTE O74523 ATIF_SCHPO TRANSIT 1..?; /note="Mitochondrion" SPCC70.02c; CHAIN ?..90; /note="Putative ATPase inhibitor, mitochondrial"; /id="PRO_0000002553" MYKYCFRKPACISYRGIRFMSKASDTDPTLANASSAKRSAFESREKAKEDFFVHQHEIEQLRKLKESLKLHREELDELESRVDKKMKSNE O74525 YJ44_SCHPO SPCC70.04c; CHAIN 1..244; /note="Uncharacterized membrane protein C70.04c"; /id="PRO_0000304043" MKQNNKKPLPSKTKEISLETDWIDVIETMRETNESPKSQNPSEEATTVNELSCEAKPKLLFTPTKSSLSIGNFPYKEFDPVLKFPGIHYTYSRERLWGTCVILSTLFWSYYVLSNSELLEFEASEYSLLFILIIALDALLTVSLFGLFHHLMFLTTNYSYTINSTLDISKGFFINVLSTMVQALVTVTIAFTKFVTIDFPIYVFSSLFLYHPLSRSRQLPTKMQLDGSGERKTDSSLVHQNPPN O74529 YJ48_SCHPO SPCC70.08c; CHAIN 1..260; /note="Uncharacterized methyltransferase C70.08c"; /id="PRO_0000339149" MPEDYWSAKDYQRNASFVPKLTKDIVKRINLSSSDELLDLGCGDGVLTNELVSQCRRVVGIDASPDMIKAARELGLNAYVIPGEKLLDASEIPSESFDVVFSNAALHWIMRQPKNRPIVMKGVSRVLRTKGRFVAECGAFGNVSEVVGSIYSILLALGATKEQIDQANPWFFGSEDDYTRMLEEAGFHVEYVENISRPTLLNKDVREWLDTFAQHFYHAFPQWKDIIRETVYNALLVTDCRSDGKWFLQYRRLRFVAHKE O74533 QCR7_SCHPO SPCC737.02c; CHAIN 1..137; /note="Cytochrome b-c1 complex subunit 7"; /id="PRO_0000193537" MKPVSLAKYIQKSPFLTKLLLPISNAYVHLSGYRKYGLRYDDLMLEENDDTQKALSRLPKMESYDRVYRIRRAMQLSIENKILPKSEWTKPEEDYHYLRPVLAEVIAERKEREAFDALIVKKPETQAHATSSPAHAH O74534 SLY1_SCHPO SPCC74.01; CHAIN 1..639; /note="Protein sly1"; /id="PRO_0000316617" MSIASVKTPSSLREAQIQSLEKLLNLNQDVNELESSPQHASNFPIWKVLIFDKAGSETISSVLRISDLRKHGVTVHMNITSFRQPIADVPAIYFVQPTQENIELIIEDLSKGLYESAYVCFSSTISRALLEQFAELASKTNTSHMIHQVYDQYLNYVVLESDFFSLQLPKIFHTFHNPSSDEALINSRVQDIVNGLFSVIVTLGTIPIIRCPQGSAAEMVAQKLNQRLKDHLMNTKDAFVSVNPKPRPILILLDRTVDLIPMINHSWTYQALIHDTLNMQLNRITVESVDDGKMTKRFYDLDGNDFFWESNASKPFPKVAENIDEELTRYKNDASEITRKSGVSSLEEVNVDAFADSTYLKSAVSLLPELTARKQILDMHMNIATALLKAIQERHLDDFFQLEDNITGLNRSAILACINNKEQGTPEDKLRFFIIWYLSVDSVPASDLQAYEEALVNNGCTLEALNFVKRVREITKMTMLASSTTRPATGQTGDNLFRGFSSLSTRFTDRFKEAGIGGLENIISGVRNLIPFRKDGTITSIVQSLMDPGSSPASKQTESYLLLDPKSARAITVNNDPRAMNKRQTFSEAIVCVLGGGNYLEYGNLADWAREQNPKKRIIYGSTDILSPSEFMEEMASLS O74537 YCQ4_SCHPO SPCC74.04; CHAIN 1..557; /note="Uncharacterized amino-acid permease C74.04"; /id="PRO_0000054174" MAIPILDALTSSSGKKNSAEFSIHSTSNPTNPEEPNITSEADNAEDLAALGYKQEFQRGLSLFSVFSVSFSLLGLLPSVATTLPYSIGYTGTPGLLWGWLIAMVFIICIALSMAELCSAMPTSGGLYYAAAVLAPEGWGPLAAWFTGWSNYIAQLVGGPSINYSTAAMLLGAVNIGNPNYEVQNYQLFLVSIAIQFIHFILASMPTKYIAKLNSVGTYLNTLFLFISMIVILAMSSKNHGFNETSKVWSHIENYTDWPDGFAILMSFCGVIWTMSGYDAPFHMSEETANASVNAPRGIILTAAIGGIMGWVMQIVIAYTVVDQTAVVTGSDSMWATYLSQCLPKRAALGILSLTIVSSFLMGQSNLIASSRIAYSYARDGVLPYSEWVATVNPITKTPIRAVFVNFVIGVLILFLAFAGAITIGAVFSVTAIAAFTAFVAPVAMRVFFVKDADFRTGPFNLGKFSKPIGFCSVSFVALMIPILCFPSVKNPTPAEMNWTCLVFGAPMLAVLIWYAISGRKWFKGPRINLASEGDNSTLEGVELYTGSEELPQKKEKE O74541 YCV2_SCHPO SPCC777.02; CHAIN 1..612; /note="Uncharacterized transcriptional regulatory protein C777.02"; /id="PRO_0000310379" MNKLSCLYCRRRKIKCDKNRPCHNCFVAKRECIIAGDNRKKRHTKTYVEALESQLANMESTLAKIKVAPVEKIPSLLAGISFKDHLSASLPNKTSYEQADTNATSKSLVDLPVSLEVRGRNTVTFYGPTSIFGTSFTSSPRPPPSASIEDTYPIIHCLQLFFKWQYAQFLFIHRESFLFEYFHRSNDNMYCSEHLIYALCAIGCRSSEDSLLVNQADAFYKMAWDALESYGLENSHITSAQCLLCLGFYKIAMGNTSHGWLLCGMAFRMGQDLGFHLDPRDWHINNVPVVSEEQAALRSRIYWGCYVADVFVSFILGRPTTLSKSDTSVPTSDDLPDFSGIEDFMLERGGAHASSITISQLLNLIVSLSNITDAILLNVFAPYSTKYGIDLRLQNVGKYNLELMKWHFELPPNLSWKKTELRDFGQSPELCFLCLYFFLIRLCLNRPFLSKKGLYVNDMTPRNICIDSIEDVKVLIRAYRENLGLHHTPLIIVYACIVSCSTVFMLFDGATPSEIVALEQDIKFFLHVLTKISKNWDLASKSINLIQKKSTMYDTNARANDTDVDFSNDKQNTHDFQISHDENLIQLFNDESNFFNLNDLGDFQSIFGGPQF O74542 YCV3_SCHPO COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 219; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPCC777.03c; CHAIN 1..396; /note="Uncharacterized aminotransferase C777.03c"; /id="PRO_0000310317" MTVSEGIARIQAFRKQVPLVEKNENITFFNLSFQPPMNSIVANTINEYVDWGLYNPNPKPLWQQKAEETRELVAKYLNASSSDSIAFTRDTTEGLNLFQRSMHFQPGDNVVLLDGEHPNHGFGWISLQEAGLEVRLIPSKDIYYADASTFEPYVDEKTKAIGISSVMFHSGQLNNVKDICNKFRPENIHVLVDMTQQVGLSSIDVQELNVSACAFACHKGLSCPTGLGVLYVAPDVLPQLKNVPPIVGAGAIENLDANLLVNLNPIYFSTARRFEHLNKSLITTLCLNNYLSFLMDIGFENIEQYLRELGKSLVDELSKLGVTIIGSKDPKKRSTHSYVAKILNPEWDAFLKNEGVYASQYRDGIRLSLGLYNNAADISRLANTIKKGVLNKIPFN O74543 YCV4_SCHPO SPCC777.04; CHAIN 1..521; /note="Uncharacterized amino-acid permease C777.04"; /id="PRO_0000054176" MSSIKSKTIIEPSENDIEKGEVDFVSSSISNFEEAYEEGPSLKREFKSRHVNMISVAGAIGTGLVIGSGSALLKGGPGSLFIAYLMTGINLYVVLISLGEMAAFSSDDKGFSGFSSRYVDKALGFATGWNYFFKYAIVYPTNLTAVGIVIHYWRPDLNVGIWVAVFLVVILAINLLHVKYFGEVEFWLSAVKILVLVTLIITCIVITSGGTPVHHKIGFHYWRDPGAFAPYLVEGSTGRFLGFWACLVQSCFAYVGSEVVGIAFGEAPNPEKTIRKSSFQSLFRIATFYVIGVFVLGLCVPYDSDILSSNASKGNAAASPFVVAIKLAQIKVMPDVINACLLVFIISSANSDIYIGSRTLYALAKEGYAPKILMLQTKQGIPWVGCLVTSSFGLLAFMNTKSSSATIFGYFSSAVTVFGTINWINILLSYICYHRATIVQQIPTERIPFRSWGQPYIAYASLIFTGLITFFNGYNAFIHGFKYRSFITSYIGIAAYVIMILGWKFTFKAKRVTSSTVDFRK O74545 YCV6_SCHPO SPCC777.06c; CHAIN 1..301; /note="Putative hydrolase C777.06c"; /id="PRO_0000337691" MTKGTSKLLFMGTGCSSGIPNVCCLTLEKPTCRTCLASLTPEGRKNNRFNTSVLLQVDDGSGDRPKNILIDCGKHFYVSALKHFVEHKIRYLDAVILTHDHADAINGMDDLREWTLGFLQPSVKIYLTERTYKVIERSFPYMVNAKNATGGGSVPTFDFHVFSPDKPFKLDDIDISVTPLPVHHGVYFIEGKESQTYFCMGFRVGDMSYISDCNYVPPTTKKLMEGSNVVVVDALKHEPYPSHFSFKQAEEFIASLEHVPSRVLYTGFSHKVEHNETVKELSVLKVPTEPAYDGQIVEFHV O74550 YCVB_SCHPO SPCC777.11; CHAIN 1..128; /note="Uncharacterized protein C777.11"; /id="PRO_0000303996" MPFLKPSKVSLKRILQGNPPKPIGLTEYGHLLRLVGLREADSKEENERTILKLNEGIIQMHAIERLDTSFIKEPFRTLNHAINAESLPSLPDQEPWNVFQNAKKRDGQYFAVYSKLKDDSSNESPNKQ O74551 YCVC_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPCC777.12c; CHAIN 20..238; /note="Uncharacterized protein C777.12c"; /id="PRO_0000303997" MKINLFFVFLFELLHFVAAYSCEGDESAAIEAMNVLQVPYEKYNTDPVCAFDNSTVVELSDKTWDHVIESGKWFVQLTAEGCANCTLGELLFNDLSHAFHEKYPDVHFARVYLSSSLELSVRLLISRIPSYYFIDNQNFYRVSPQVLPKNKAIALYEKDGFKSMKKEQGFFSVNGPLKSFYWVFGKALALYGHLSQKYTPLGMNVAIFGISAYIMYRSSKKAKQKQAAAAAAAAAKKK O74556 YCZ2_SCHPO CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.; EC=3.2.1.101; SIGNAL 1..19; /evidence="ECO:0000255" SPCC970.02; CHAIN 20..442; /note="Putative mannan endo-1,6-alpha-mannosidase C970.02"; /id="PRO_0000012131" CARBOHYD 25; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 82; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 107; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 131; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 201; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 236; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 261; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 264; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 277; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 361; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MSLTIFISLATILFSFAEAISVDLNDTSSVDLATSLVADGLLNYYAGQHKGGTIGMFLPPAYWWEAGAAWNGLLNRYIATGNSTYNELVKTSMLYQSGEDSDYMPSNYTTSEGNDDQAFWGLTVISAAEANFSNPAADEPQWLELAQAVFNQQVTRWDTDHCNGGLRWQITEFNSGYNYKNTVSNGAFFQLAARLARFTDNDTYAEWANVAYDWSQRIGFIQEDYTVFDGSSIKDNCSSIEITQWTYNIGLYMAGAAYMYNYTNSTVWKTRVEGFANKTAKTFFFKDIMFEPVCEIALSCNYDQTSFKGFLTRFMVYTAQMAPFTAPLLEPLLISTAKAAAGACCGGYDGVTCGVQWWWNNDTWDGLYGLGEQMSALEAIQAPLLLKSLQVFKASNGGSSTGDPNAGLYTAPVSFANKNFENLRKHWMLLGFFLLVPTLVLY O74559 SURF4_SCHPO SPCC970.06; CHAIN 1..302; /note="Surfeit locus protein 4 homolog"; /id="PRO_0000127670" MTSRSPFSTIPLSMNQDSYQTRTTVGIRKKTFSERACQFMEQAETFMAPFTPYMPLLGRFLIVATYFEDAIRIVTQWPEQVSYMRDYRRFRFGTAPLLLFVCVVLMLVGSTLVVFKKRQAYAIGSLLFVTLLQAFAYGLITSGEMFFRNMSVIGGLCLVASDTFIHRRINRFAGLPAVSEHNKRTYFQLAGRVLLIFMFLGLLAKEGSGISWTRILVHILSVTACAMVVIGFKAKFFAAVLVLILSVANFIINSFWSVPRESPYRDFYRYDFFQTLSIVGGLLYLVNTGPGKFSVDEKKKIY O74564 WTF9_SCHPO SPCC970.11c; CHAIN 1..333; /note="Meiotic drive suppressor wtf9"; /id="PRO_0000193224" MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPPNTHRENHSSGTTDNSSPLLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAVEWTLFGFWCFVCTLALIFLTYFYETWTKAVKVTVISLAQCVKVTAVFLAKCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRAKFGNLNLDKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVQKGLMHLFDKHIDGTGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLGGIANAIGGANDNNDIPLEETEAESEV O74628 YQ53_SCHPO ACT_SITE 134; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 148; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 152; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 17; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 55; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 82; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 115; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 148; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 152; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 184; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPCC162.03; CHAIN 1..292; /note="Uncharacterized oxidoreductase C162.03"; /id="PRO_0000374034" MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRELDPNWNIAITIVQPGGMQTEWASSNMQWAKPHPAYENDRSWRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQKLVLGHDSLELIRKQHQDIGEELESNVALSTSVAKDDFDPASVETLRQNLQSM O74648 IAH1_SCHPO ACT_SITE 46; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:P41734"; ACT_SITE 201; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P41734"; ACT_SITE 204; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P41734" CATALYTIC ACTIVITY: Reaction=3-methylbutyl acetate + H2O = 3-methylbutanol + acetate + H(+); Xref=Rhea:RHEA:60436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15837, ChEBI:CHEBI:30089, ChEBI:CHEBI:31725; EC=3.1.1.112; Evidence={ECO:0000250|UniProtKB:P41734}; SPCC126.10; CHAIN 1..246; /note="Isoamyl acetate-hydrolyzing esterase"; /id="PRO_0000314106" MSDSQDKNYISFEKTEIGQIVSEAPAEKYVSFQKKYFNRLTIIGDSITQKGFTPGGYCAELMNFYQRRLRVDVWGFSGYTSRHVLRYLPEIPLEIDSTKLLIVFLGTNDCQLTETGYMCPVDEFKNNLLALTRPFPHSKIIIVSPGICTKDICFKREQEPYVIAASETVNTLNKSKANSAGLINLYEITKSYPTPELLFTDGLHFSSLGYSLLFNEIVATISKAWPELLPNNLPLQFPHWSEILFT O74728 YH93_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPBC1709.03; CHAIN 20..428; /note="Uncharacterized endoplasmic reticulum membrane protein C1709.03"; /id="PRO_0000116770" MSLLRYFIFFIGGCTLALASGVSYTEASVYMSGLSGNENEVPSISPSDSRLVFAHKLGVSRFHKLKSHSGARKIINEMLHSHSELSSFFYAEKSNTFLTIAGLAESELFDTLNPAFRISSCPSSNAFASLMCRYERQLDSLDNGKTTDIYLNDIGGVISIHDSTGVYSQITTTPYKSLEDYEQLFGEDKASMFDISVKQDRVFLSEIYALKILVEFLSSKSQQERSDTSIVIGQLVGLEALYEKYGKDSKIYQVARENMMTLLSMIKQVSSTYTFILLPPIDSSETSTRYHKRQVDMEAFGEEIEEVVASYEKNYNGRCYISEEACSKATNDCSGHGRCSKYGQLDSCYVCQCSNSVVSNAAGQNKTIRWAGESCSKQDISVEFQFFFWFTIIGFGLLIFSIMLLFSIGQEELANVLTSTATVIKKTT O74737 RID1_SCHPO SPBC1709.12; CHAIN 1..400; /note="GTPase-binding protein rid1"; /id="PRO_0000372376" MNSLRSVKRLLGARSLSSDGLSESVNSSDREDSLSFQTPSTPSEDEMPQCFEDLIKPQVLSSEASKSLLSLNEGIKMEIVSSLQQKDQKKRNKLIAWMRKKPCYEQPDDFISYIVNTKIDSIDESIIHKLALLLRNEQVIWVEKFIHNGGFGVVFCTIDKISRLEWREELHDSILEQLLLCVKAMCTVQRGLECLSQSTYNVERLISLLLSKKQPCDFVVREVLVQIVHSFYKAHLDKEEGAMQVFSLFSIKDDKDEEVEFLKNVRVDRPFRRWIIELEDVSRNVFWVWNHDSNVIDLEKQYNQVYEAPLGFIGGIETEATSYVAAHIHLINELLEGLPLEKRQRKRLELQLSGLERIMGLRFRKSSQKFHKKLHEALREWIVAAKIDDWPYKLVQTGST O74743 IF4E2_SCHPO SPBC1709.18; CHAIN 1..243; /note="Eukaryotic translation initiation factor 4E-2"; /id="PRO_0000193652" MADAEDSRHSKNEGFPNTSLITEKLDLLDLFGSPKVKTEREGRPARLLEGLSAVNAETAFVKTHPLQHEWTLWFLKPPTQGLEWSDLLKEIISFKTVEEFWGIFKTISKASMLPAKSDYSYFLKGIRPEWEDPQNMNGGKWAYQSKHKGSNLDELWLYMVLAAIGETLDPTGKEVTGVVCNMRKGFYRIAVWTRNCNDKDVLEKIGLRFKEVLGISDKETIEYSAHEDSSKAGSMRAKTRMSL O74746 SPF31_SCHPO SPBC1734.05c; CHAIN 1..209; /note="J domain-containing protein spf31"; /id="PRO_0000071132" MADVAKFLDRVEGSLNRGREIDRILSSFKLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLDSAYTAARNQLLKEKKLSPNSEDVHSDQFLFDLKVRWREILIADEVARRRARQLDLANQQREQARQDEIARERKRRVESEKVWEETRDNRVGNWQDFLHKTKKNNLKKKNKKPRVLG O74751 YHFA_SCHPO SPBC1734.10c; CHAIN 1..332; /note="Uncharacterized protein C1734.10c"; /id="PRO_0000116772" MLAEYLVHVGRVNVFLDPETKDIPKCVADLKFPLPLTLSRSTPINPIIRSDTIQLVISCPPVTYSDEIQVPWKAIDLNKDDAVKSTIKCKQCQSFLTSISSWKDLPSANWMEMLDCWSCHTDYPTVLSKRGGPSMFQPTDDCAYLGTSYVLIRLQSLEGKVAYGPNFKLHCSFCNAELGLPNNKDSSNGVRLDKSSICIDDQKIHPSFIVASEILTLRDMYATHKFVIVDGERSIWTWCFVPHLPISFQKSPFSSIEFANSPISTIKLLYQLEVPPDFTKSSEDWMDIPVSSHAFDEISHVLEKGNLSFPVSAQKFGPWKVGLLPKFHKQMI O74758 PXP2_SCHPO SPBC17D11.03c; CHAIN 1..213; /note="Peroxisomal protein 2"; /id="PRO_0000317091" MTHNTMLQRFNGLLEPTHLYIVSVVAYSACNRPDKISGIAKEAMEHVGPSIYPKLREALVKSSPLVGFPRTINSLREMTTNIPPPFPDEFARAADADIDTGKRGKIYFEKTYGKVTQRVLRSMQSSSLDLANIALDYAYGKVLSFNEVVSPLETSLMIIAALVPQDVNPQLRGHLKGALNHGATKEQVMSARNIALEISKECGIQFKGDIETL O74763 YBE8_SCHPO MOD_RES 266; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 388; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC17D11.08; CHAIN 1..435; /note="Uncharacterized WD repeat-containing protein C17D11.08"; /id="PRO_0000316548" MTDLRRNRYSISAGVGKSVLDSLGKFYGSPKRQLPNKFEAGKEYTGYNAPWIPFALDWLKQGKYSSEWIAMGSLNEEPNNMIQLLKLITGDDGNSHLEKAQAATDLEYPVTKLLWNPSSVGSNTDSQLLASTDQQLRLWKTDFEAGIDSPLLCQASLSTHVKTHNNAPLTSFDWCKTDPSYIVVSSLDTTCTVWDIVAQQSKTQLIAHDKEVYDVAFLKDSINVFVSVGADGSVRMFDLRSLDHSTIIYEGDSTFWKRNGDYTNASPPVSAPLLRLSACDSDVNLMATFHHNSSDVQMIDIRVPGTAYATLRGHKGDVNAVKWMPGSKSKLATCGDDCVVSLWDLDQPVNPSPAPTLSVSGTTPGMTGSTSEYVTPVSSVNSMRETASPLNADNQYSPLLSWKLEHEVNNLSWSVKNDGLAVVYGKSLEILKVPQ O74770 PHK_SCHPO COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000305}; SPBC24C6.09c; CHAIN 1..825; /note="Probable phosphoketolase"; /id="PRO_0000193895" MATQNDIPNSTPEDLAKQVEIAEKHPDPPAMPSRLPDSLKTLEAKIDTSKITDEEVANVHRFQRACDYLAASLIFLSNGLYTGGDLEEKDIKTRLLGHWGTCPGLSIVYSHCNRIINKYDLNMLFVVGPGHGAPAILSALFLEDSLGPFYPRYQFTKEGLNNLINTFSLPGGFPSHVNAEVPGAIHEGGELGYALSVSYGAVLDRPDLIVTCVVGDGEAETGPTATSWHAHKFLDPAESGAVIPVLELNGYKISERTIYGCMDDSELLSLFSGFGYEVAIVNDTPDQNRVMAATMDWAVERIHDIQHRARVNREEIKPRWPMIILRTPKGKGCPKYLNGKFLEGTFRAHQVPLKLARTDTNQRNLLKDWLNSYNCQDFLDEHGLPTKGITEHLPPREKRMGQRHETYNSYLPLKVPDWKKYGVKKGETTSATSVVGQYLDELLVTNDSTLRIFSPDELESNKLDGALKHSYRTMQTDPELMAKRGRVTEVLSEHLCQGFMQGYTLTGRTAIFPSYEAFMTIVVSMLVQYSKFLKMGLETGWHGKFGSLNYVTSSTWARQEHNGFSHQSPRFITTMLSLKPGVSRVYFPPDANCFLATVARCMKSENTINLMVSSKNPQPAYLSVEEAEHHCKAGASVWKFASTDNGENPDVVIAGVGNEIMFEVVKAAEMLQNDIPELRVRVINVTDLMVLSSLHPHGMNPAEFDSLFTKDRHVHFNYHGYVMDLKALLFDRIQGTRVTMEGYREEGTTTTPFNMMMCNNTSRYHVARMALQHALHNPTVAVNCNMLCAKYAWKLEEIENYIMENKDDPPEIYAAPVFKNKTSTL O74793 YOUB_SCHPO SPBC26H8.11c; CHAIN 1..175; /note="Uncharacterized protein C26H8.11c"; /id="PRO_0000315974" MPETKLVALPEFQELKSNDEYISMQPYKGEDNKSYIANLVRHNALTFCPYYFIEKSGKGSVVYFHPTSDLCGYKNIVHGGFITTMLDEALAFGVFPNFPSKMGVTVQLDTTYVAPALCSHLYKIVTKTTKVEGRKCWTSGELLRLNGSEPPVLCAKASGFFVEPSKLNLEHHVKK O74797 YGN3_SCHPO BINDING 34; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9NWV4"; BINDING 37; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9NWV4"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9NWV4"; BINDING 71; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000250|UniProtKB:Q9NWV4" SPBC2D10.03c; CHAIN 1..157; /note="UPF0587 protein C2D10.03c"; /id="PRO_0000338391" MGKFALNLNAELTGVKNLAPKDEESFYYAFKVQCSGCREIHDNAIEISRSETHSIPGSKGEANLIWTCKNCRKTCSFVIEGPFSPYNDSQETKKVLVLECRGCELVEFIPQGEWIANGAESNTLFDEIVLEDDWYDYDENASSEVSITNLEWSISKA O74800 IMP1_SCHPO ACT_SITE 35; /evidence="ECO:0000250"; ACT_SITE 80; /evidence="ECO:0000250" SPBC2D10.07c; CHAIN 1..157; /note="Mitochondrial inner membrane protease subunit 1"; /id="PRO_0000314116" MAGMFRIPIAVVQIAAFVHQIHEYLFQVQMTSGPSMMPTLNSGGEFVLLDKLHGRFARSCSVGDVVVSAKPSDSKQHVCKRIIGMPGDTIYVDPTSSNKKITIPLGHVWLAGDNIAHSLDSRNYGPVPMGLIKAKVIARVWPHPHWMSNILNDIDVE O74801 RL4P_SCHPO TRANSIT 1..35; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC2D10.08c; CHAIN 36..261; /note="Large ribosomal subunit protein uL4m"; /id="PRO_0000314628" MTAKMLHLVRYKFPSLEPASLFLIPGSFLQERFRRDILHRAVIYEADNDRQGTASSKRRNEITCSGRKLYRQKGTGHARVGDASSPIRRGGAKSHGPKPRDFSTKLQTQVYNLAMRIALSTRFINNELTILENPINLSQPKTRILLEVLKQHKLGHEYGKALFVLNDNYFEDESLKNNNLLLASRQLGYHCSFIPVGEFQVRDALKFGKLFIDSEAMSLIVEKFAQRNTLSDMDQPASLTAYVDANSSSFTKSKPEPSLSL O74806 PTH_SCHPO CATALYTIC ACTIVITY: Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; EC=3.1.1.29; SPBC2D10.15c; CHAIN 1..206; /note="Probable peptidyl-tRNA hydrolase"; /id="PRO_0000187866" MAIKHLPKILIARKNKAEVNHCDLKRRVSIKIIYGLGNPGSAFVKSRHSLGKLMVSMYADSMAFPKNWPSTKENLTLVLSTSYMNDSGKQLKKISNDFVRKVSPLDKIVYVVVHDELELDLGKVKLRLPGGSHRGHNGIRSCQEFLGKESFYRIGLGIGRCESRNREDVSDYVLSKFNSNEMKLIETDIFHKFCNILQQLQLSIET O74809 YGNJ_SCHPO SPBC2D10.19c; CHAIN 1..105; /note="Uncharacterized protein C2D10.19c"; /id="PRO_0000304055" MPHRNDRRKSASKAPNAIIHGRVASKKTIKKQLRNGKYSLKRLAEKGIHLDDIAMEIDNASKKNISKDKSLNENLFGKTEAGKQKDFMNIEPTCKGTILGAPPAL O74822 YBJB_SCHPO SPBC337.11; CHAIN 1..325; /note="Zinc-type alcohol dehydrogenase-like protein C337.11"; /id="PRO_0000339116" MQYYQMMKALRMLKKPKPGCLGIEIQSVPIPQPKNGELLVKIEAAAINPSDLMNATGGFPYTVYPRIVGRDYAGTVISGASHLVGTRVFGTSGSELSFTKDGTHAEYCIIPEKAAVRMPSNLSFTEAASVGVPFTTAYLALSRGETKGSDIVLVVGALGAVGSAVCQIAEDWGCKVITVSRSGSTDINTVVDPELKRVHELVEKVDVVIDTVGDPLLMKSALNQLGIGGRLSYISAPKQGSIEFSYDMKQIYRKNLKIIGCNSLLLSLVESNSLLKNMVAKFEAGKYKVLNKKIAETSLTDECINSYRKLMNECSTKFVITMSTN O74830 YC12_SCHPO CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; SPCC1183.02; CHAIN 1..220; /note="Putative glutathione S-transferase C1183.02"; /id="PRO_0000316037" MFLGTLYSFKTNTRTVCLLELAKLLDLQVDLVETYPHKFSADLAAKFPLQKLPVFIGADGFELSEVIAIVKYFYEKGKHNDKEGLGPVNEVEEAEMLKWMCFINFDIVTPQNVRPWVGMFRGNIPYEEKPFKESATRAIDSLKIPNELVKDRTYLVGDRFTLADLFFGSLLRIFFNSIIDEKTRKELPHLTRYYITMFHQAKLETYFPLELPLTVTVAKK O74838 WTF10_SCHPO SPCC1183.10; CHAIN 1..258; /note="Meiotic drive suppressor wtf10"; /id="PRO_0000193225" MKNNCTSLKSSIDEEDELKTDHEIDLEKGLLPEYDSKEEGALPLYSDHARLSNSPNTHRENNPSRSTDNSSPLLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWTKAVKVTVIFLAQCVKACGKGIKHFLKKWENMPMAFSEVFLFNIFGGALRIISRHFFGKRWGLKCSLADHIIFAILSILVFIAETVKPGSIRVNLIRKMGHEAKQQVNEYTAIPLHEMNPESEA O74840 YCY3_SCHPO SPCC1235.03; CHAIN 1..502; /note="Smr domain-containing protein C1235.03"; /id="PRO_0000116560" MQDWRAALEEYYSRYLDSALVLAIVNDSDDSNTAREILEALSIESQCDSHEEHWDNLRRDEQELLNLKTLDEEINKIDEEDFTWELKDSSLELDPDVYNFLRSMFSDLSAARVQLVQAKCQNDLVRSSDELLNHRAIQESEQIETAADALITSNIGHRSRQRKKKTKKATNSRKPLSKFQSNTEEVNEDPILKPSLSVWENNRLLIEKLTSILNIPSSQINHEFYKNSSAWPITIRNLIHRHQPLSNITNNELMKYQEEATQLAKDTGLSLKICTDVLICSNDYKNALWILCLIKETQHNEMGNIKLSSQTAKSNSSTQTKTCLNDQSSKLVEDDEALSAEDCNRLAEEYLELRNMQYSNSAKEYRRSKSNHLFGGSAMYHAQLGREYHEKALKYRSLAMRSLAHSGTSHSLDLHGATVREAKTIVRERVAAWWAKEADTSPNSIRPFVIVTGRGNHSIGLEARLLPAIVRLLQQDHWRFDAEHGQITVYGINRHSKLNSNA O74847 MPC1_SCHPO SPCC1235.11; CHAIN 1..141; /note="Probable mitochondrial pyruvate carrier 1"; /id="PRO_0000318135" MNASEKLSQKAAQSVTRRFITWLKSPDFRKYLCSTHFWGPLSNFGIPIAAILDLKKDPRLISGRMTGALILYSSVFMRYAWMVSPRNYLLLGCHAFNTTVQTAQGIRFVNFWYGKEGASKQSVFENIMQAAKHPESGTRQK O74848 MU146_SCHPO SPCC1235.12c; CHAIN 1..311; /note="Meiotically up-regulated gene 146 protein"; /id="PRO_0000278629" MICKNTFVDYPTTQVRKERVHTYRTLTSATPSLEFFSNENTNRLSEVQCKLTHFLSSSENSSSVRNTRTHKFKQLLHYIFFSNRSSSVLGKQNVHNSQTLGSVSFCEKHAIDINYSENVNKQLNFESHLDDQTCSKRFYFNEQSGSDRYSLKCDSDTDSSTYFGDSASETCSSASNSLYKQTDLTSLCMFNQNKIQTDWSSIDPMDNDKIVCADFEKNFNILKELLNNTKDNGIDQQIVHKEHISHLEKIWKNINEESSEDPSLLLLRLEFLLTDLQTAIRKYSDTVSTNSVNEAFFDKIKIELQAFGVLV O74851 ADG3_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPCC18.01c; CHAIN 24..1131; /note="Probable secreted beta-glucosidase adg3"; /id="PRO_0000033462" CARBOHYD 58; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 123; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 252; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 551; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 593; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 631; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 689; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 766; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 806; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 857; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 920; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MPSKIEKICLLLLGFTAASNVNAYSHRRAGDTLHHRHKHEKHNDLTDSSYEPLTLSYNDTQIQQLQRRDTVQCAFPYGDKMVAVTPDEGNAGWAMSPDQYCTAGTWCPYACEPGYLMGQWDPNATSYTYPESMYGGLYCNSDGVAVKPFPSKDYCYPGVGDLSVVDQTGDGIAFCQTVLPGNEAMLIPTWVAPDSEQVLAVPDISYWDETAAHYYVNPPGVSTTDGCVWGTSANPYGNWAPYVAGANMDENNITYVKLGANPIYLDDSYWSTVKPTYGLALECEGDTCSGLPCYVDPRENGVQGCPEGSPIGAGGACFCVVGFQQGTTAKIVVVDYSEEMASSSSSASATATSSAESSIATSPITSSSNVVSSISTSSMDSSAVSSYSVVQSSLASIISNAYIATSKSGLNSGVSTLLASPTSSSTFVTSLLRRSSIDGSASSSSASLAVPTVSSSTTGSLHYKTTTTVWVTEVFTRYLGDDSTPVTSSSIFSTATEATDTSVQTSSAIYDSSSTSNIQSSSSVYASSTGALSSNSLSSSTSSVSTSYIPNASSSVYASSTEALSSNSLSSSTSSASTSYIPSASSSYEVASNSSDYYSQTVSSITASGTTSSTSEIVSTPASNSNTGSLNGTSSFNVNSVGPSSSQTTPTSSSSITGSQSLKETSSPAYVSSTVSYTSSSVDSSSTYNSTGSSSSDSQSFSGTTYSDPTTTITSEVSSILSSPTSMQSSVSRPQSSGDASGFNTIFTSISQSSDGETSGYTISSNSSQNSASEPQTAFTSSSSSATPTITQSSISTSVSSQSSMNSSYSSPISSNSVTSSTSIISSIASSSYTSIPSISSIASSFFDASGFTSIYNGTKAGFSSSFALASNSESGASDVLSSTIAKPTFKFSTSNSGSTSYSIPSSSSRNEGTTSYSSNITVTSSTLKPSLTSSVSTASSYIASSASSNTLSTEPKTFSSSSTLSESISSINTNSLTVKPESSLSSSTTSGLTSSSSTIPSSTRSESNSESASTSSASKRSSSSTSLVQSNPVKTVVSLESYKFTTSKISLVKNPTKTYTVTDVETNVVVQTHTVSYVEHSTSYTWVHTTLYEYADVEASTKSTSEPSAKSKRNAVSTFETVFLKSKSSA O74852 YQ92_SCHPO SPCC18.02; CHAIN 1..448; /note="Uncharacterized MFS-type transporter C18.02"; /id="PRO_0000372718" MGLKLWVKQRRSLPFIIGTIAIALFTDLFLYGIITPILPFSLVDRVGISPDRVQSVISTLLAVYAVANIAASSPIGFLADKFLTRKVPMLIGLIFLTSATALLTFGNSVPMLIVARVLQGLSAAVVWTVGLALLVDVVGADNVGSTMGGIFGFISLGEIIAPVFGGIVYESLGYYASFGVCFIILLLDIALRFLMIEPREMKNDSTLQDVERTSILQRQDTQDHELKPKRSGLFSSLCLPIYSLLHHKQIFGPFWTSFVNSCLFSAFDATIPLELKTLFDFNSLQCGLMFGVLSTPYFFCGAWAGAMVDRRGSRTIGKRAYAILGCTLFLLCIPRTNTSLNIYLFSAFLAINGVVLAFTSSPGFVQSSHYVAEYELEHPTFFGHNGPYTQLFSAYNIVYSLGMIIGPLVAGFLRDQFNFITSIACLSLLCFSASLMANSCFTDRLDSE O74855 NLE1_SCHPO SPCC18.05c; CHAIN 1..502; /note="Ribosome assembly protein 4"; /id="PRO_0000316570" MATLLPPKSKRQKKESLNPTTIEIPEKFPLVNVQFRASDDSNELASLLVPGNSSVRQLEALLNQLLENSDDPVPYNFALHHEDETIEIQDNLYTSVFHNGLMKTEDHLTLLYTPQAVFRVRAVTRCTASMNGHDGTIISAQFSPSTSSRLVTGSGDFTARLWDCDTQTPIATMKGHTNWVSCVAWAPDASIIATGSMDNTIRFWDPKKGSPIGDALRRHTKPIMALCWQPLHLAPDSGPYLLASGSKDNTVRIWNVKLRTLLFTLSGHTAPITCVRWGGQNWIYSSSYDKTIRIWDAKDGKCLHILKGHAARVNHLSLSTEHVLRSGAYDHTDFKPKSFSDERRKAKERYEACLKQSGERLVSASDDLQLILWDPQKSTKPITKMHGHQKVVNHASFSPDGRCIATASFDSSVRLWDGKTGKFLATLRGHVAAVYQCAWSTDSRLLVSSSQDTTLKVWDVRSKKMKFDLPGHEDQVFAVDWSPDGQRVASGGADKAVRIWSH O74867 YQ9H_SCHPO SPCC18.17c; CHAIN 1..488; /note="Uncharacterized protein C18.17c"; /id="PRO_0000304092" MDSIELIPGLPGPGRRLLQLLKDLPSNPSVIVREIPDAIDAFRESITPATRPSCLGLLDTILSCFELPIPTEPIMKALGKLLEPMSWADLKKFGIESYLVTGLEHPSTDVEIFCLHLIRRANWEKKEIGEPLFEAIMACINSRSIAVSEEATVLLFDMADFPYYFNLIIKRFTFVDYEIMNSTLRVRWLTLFAKLSTKSPEYLEELIKDDKLVINGDNKDILLQINFVDVLGIMLEAPFTYEYISSEKTKYLDTIAQDYKGSADSYTDHIGLKFLPRLCELHPDAINSLDEKHQLFDAVRERMKTNDATSILLYGVFLSNTVVTQALIKKYGIEDEANRYVPRWLTRRFLMDEPGMSSFAHALLQPDHNLWMQLWRILPPNTLSTLVNTASSPIPRSRQLAYQCLLHIAQNSPIQIASEGFAIRHLLEAEGDHETCLLRFQVLKTMMESPHGGPKLPFGRYREDILKRLQQGPIVSGASTLKVAAETA O74870 MUG73_SCHPO SPCC31H12.02c; CHAIN 1..306; /note="Meiotically up-regulated gene 73 protein"; /id="PRO_0000278563" MNAKLSSSGMVLKELPEVALQKISSNYYWAVFAVFLLCAIVFPLVSIFSLPQKQTYHRFFSILSLVSCLAYFTMACNYGLKNVFSSASFFREVSVRMVYYVRYIQWLINFPLIIVMLHWTVGVSILEIAYVVCYVLFAIVCLLAAALTSSPYKWAYYGFSFVGYFIALAHSVVLHKKYASRLETSARLGFLWSIVYLHVIWFLYYACWILSEGLNVISPIGEAIFYSILDLFEFGFFGAAFSWMLDLVGIENFKSPQSIPLGACSPADDKFSMCPDMEAQNQADDLAVETRIQISNLPSSPTKNNC O74871 YCW3_SCHPO MOD_RES 139; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC31H12.03c; CHAIN 1..245; /note="Protein mlo1"; /id="PRO_0000116557" MSDYKSLKVAELREKLAEKGLSTAGNKAELVSRLTAATESNDENTSNNNATDLGDLAPPEDDIDWGDMENDTISTDVNKPAEPESKETSAPAAAVEIEKENESIISKETSQAPETSTGAEEHQETTEESKQSVSNEVSSPDVAKEQEKLIQRAKRFGIPVDDEQIKKAARAARFGIQQPLASSNNKNHNQSKNPQNRSNSRSKQRNKNAPPKSAPSKRKSNILDDPIEAEKARKRAERFGVAAKN O74872 MU111_SCHPO SPCC31H12.06; CHAIN 1..468; /note="Meiotically up-regulated gene 111 protein"; /id="PRO_0000278505" MLSKKMKICRPSLVLIYLWYLVDCTSFSMNSVTCLRLMQLLLAKYYQIPIDLVGEKLSIVSASSCLLQYLVALVVVPFYSTIIKKLTPWFTVFTTWVGEEYFFFASTLSILYMDDFPTCAYFVIFSISFLLGISGTGPSLNASYKSLCKLYSYENSFIVVLNSIFVVSSCIGPFLGSILLLRVSLLQLYLISWTIHFINFVFHSLLAVFFSSKYTSYAQKEGQPILNATENLEVEYNALNTTPSSFEEQPLLNGLNDSPRNPVSRTNAEGFKALNASFDGSYKFPIPIVLLCFFLYSLLTPFFDIHLQFQLIVMHMSIVQVGFINSVKTFGSLLTCSVCLFLTYVGGFSVHMMKTTMLIGLTATTLIIFILYFATAQTLPCLALFYGITSSIGPSIHGLVAAYVPNDKPHRYWKFTALLEASATFISYPFQSLAFIVCLKYCSFYFFIGPICICLLGSISSYLLLGYH O74876 MU135_SCHPO SPCC330.04c; CHAIN 1..357; /note="Meiotically up-regulated gene 135 protein"; /id="PRO_0000278626" MSEEDNRLNELFANDLGVQPPCERSLKEGRRFLNDFEIAAKKKLLELERKALEDKEKNLNFVVESERTLFNSKKRAFDNDECYNDRCKLFRGIVNEWGRSERTLDSLDEPPAWFRREMGEWKKAREEDKAEWKKAREEDKAEWKKAREEDKAEWKKAREEDKAEWKKAREEDKAEWKKAREEDKEWRNSMDEWRKSMDEWRKSMDEWRKSMDEWRKSTDEWRKSTDERLENLLNIVREILDVQRDMRNDLSNLTRKVDRMDMRLSRNNNMIMRSFAQPITEVPFFNGDIPDPNLPRITRIEDIDSLSEENCTRYLKGYGVSYDENDQSLWKRQLAKAVGLTAAYDESYTFSPFSSSE O74901 YCS1_SCHPO MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC613.01; CHAIN 1..497; /note="Uncharacterized protein CC613.01"; /id="PRO_0000116554" MSTTTETVTWSQYKPQETQRRLSRSSTITPSVSEYRSGFSKTAFGNIELEEIPDKQGNITRATSNLESNSYPKALDPDACPPKRSIALVLLNNLMSEMSLTIALPISAAYTEILGGTDAFSGLVIGIPTMISLVCLYPMLRFANPKSANGYTLYFRPLIVSCISQIIGHLLYSLAYRAQWLYLILIGRMCSGVGFTMFLYHKTYLTDKNFVGQNRSTFLATLNILAQILGSMAGAFLGGILAKASMHLTDPIWNQYTAGSWFMLFIWIVYSIFLSIFFKEVRVGNTATNVRKPESFTGKTAPLSFKQKFMLCFLSMAAFISIFNVAGYQTSVPIYAKALYHYNPFQSGNFLSLSSLVIAPFVFFSTFLSKWLEDRQIMLYGFMMGIVALIVHLVLDAVHKIPVQPYFVLYSIMQFGFSVGSAPLVSLATKQLHPKYHMITGVVVQVGISIGETVGSICGGAIFDITTVGFIAMNLGIALLVFIQLLYLWTFIKTKTG O74902 YCS2_SCHPO SPCC613.02; CHAIN 1..497; /note="Uncharacterized MFS-type transporter C613.02"; /id="PRO_0000372710" MSISIETITKRNQYRVDQPQRQPSRLSTVASISEYQSDYSKTVFEEIELEVIPNKQNISTRSFRNDGNDSDPQTLDPDAYPPKRSIAFVLLNSILSDMSMSTALPISAAYTEILGGTDAFSGLVIGIPTMISLVCLYPMLRFANPKSANGYTLYFRPLIVSCISQIIGHLLYSLAYRAQWLYLILIGRMCNGVGFTMFLYHKKYLTDKHFVGQNRSTFLATLNILAQTVGFMAGSFLGGLLAKACMHLTNPIWNQYTVGSWFMLFAWCIYGILLSIFFKEIRADGNDSSARKPENFNGQAVKLSYTHKFMLVFLSMVAFISYFNIAGYQASVPIYAKELYHYNAFQSGNFLSLSALVIAPLVFLSTFLSKWAEDRDMMLYGFILGILALVVHLVLDVLHKVRVQPYFVLYSAMQFGFSIGSAPLISLATKQLHPKYHILVGIIVQIGISAADTVGAICGGAIFDITTVGFIALNLGIAVLVFIQLLFLWNSIKTKTG O74903 YCS3_SCHPO BINDING 87; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 89; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 91; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 93; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"; BINDING 98; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SIGNAL 1..20; /evidence="ECO:0000255" SPCC613.03; CHAIN 21..189; /note="Uncharacterized calcium-binding protein C613.03"; /id="PRO_0000372333" MKFSTVGFLFSTILFKSAFAGWMDTHMKDEHHIDKYTDESFFRLHDLGKKGYWSDQDILSLYGLFENDEVPFVKKNEVLVDVLKKCDPSGNRRITLDEFLAFRKNGGELTDFGFPGHHGDEEEEFEMHHVEKYHPAGLDEPDENWNHPEDIEHFQKHDEIFHGDKKPEERRKHFVKYNNIPDKYRRVSI O74907 BCP1_SCHPO SPCC613.08; CHAIN 1..282; /note="Protein bcp1"; /id="PRO_0000249705" MAKRHAEENEDTVMSESLKVVDTDFINVDFEFFDPQPIDFHAFKNLLKQLLGYDHTNVNLSALADLILSQPLLGSTVKVDGNNSDPYAMLSVINLNTRRDEPVIKQLTSYIISRLAKSNSRLENELQKLLEPNSGSQVGLIVNERLINMPVQVIPPMYNMLLEEMQWAINENEPYNFTHYLLLSRTYTEIESKLMDDERPSKKGKKSKKTSGEEVMFFHPEDEQFREVAIDIADYPFANQDFNPDANRVFQDAGIKPQGELLLMTNEDFKNLVPKLMEIYSA O74908 SEN54_SCHPO SPCC613.09; CHAIN 1..384; /note="Probable tRNA-splicing endonuclease subunit sen54"; /id="PRO_0000194033" MDAQDEDNPFTNLETTVDVTEEIQDWRFLSNVEKDQGTYTIPKRGQKDFEPDGTNKQHSALDLSRKAMFDALSVERLISAKHAIIATWNAQNGMSCVEKAHGPLFKTMGTADSQNRMWLLPEETLYLVERGSMECWSEEGLPMSLQAVYSASIPLCGSLENYLVYAHLRRCGFSVIRSNLVPVKEDEYRCDSKIMNFKDLLFLGLGKASQILQTFNFRKLAFPFSKRRRQSILLHDTFYTYEEVYHDLQIVRGYVPIACNLITSSDSLFQITFHAYKPSASFKKSALSEPDFRICVVSSQDTLLPTIFEIDALFSSTPLRQNMPQHMFQRLKEGYRNIIIAIVDYGVISYIRLSDVCFEEKVYTDFSKKGSKRKRVSKKFQQLV O74909 MEU23_SCHPO SPCC613.11c; CHAIN 1..254; /note="Meiotic expression up-regulated protein 23"; /id="PRO_0000076256" MPNTESELNEEFSNEFNIPPPTESSSKEGNRFLNDFRVEFEKRRIEARNRILESEGRALENKTHLNEEEIRTNERVKRFQRRVDEWTALEIERESQVQPPLWYQRDREEQNRTLNFLMSGMADLQRTINTMQGTMNTMQGTMNTMQENMINFTNKVNTLDMRSVRAENRDLRKGAYVISPVPFINGNNPDPDLPPITSVQDVDRLSRSQCSRYLQGYGVTFHVNETIGMKKKLASAVGLSAEYDREYPFSGFPN O74915 YJ74_SCHPO SPCC757.04; CHAIN 1..636; /note="Uncharacterized transcriptional regulatory protein C757.04"; /id="PRO_0000310387" MSHRIRHLSCLACRRKKVKCNRQYPCTRCLKYGEACTYDERDNRKKRHSLSYLHSLESQLARLESFIMTLKNSDPEGRDEMLKSVVFSDHLTEPNDQEVKSEGPIEYPVFLNVQDSKTVSFYGPTSAYDLSLPDITKDNKTTWNFQASYSPMVSECLKLFFRYQYSQFLFVYRESFLSDYYYNFHDGFYCTEHLIYAICAIGASMSDDENISRHSKSYYDASWQKLLEFGLDRSHLTSVQCLLCLGYYDIGMGNTSLGWLLSGLAFRMGQDLGFQLNPENWYIDNSPAISSADSDIRRRVFWGSYVADKFIGFIMGRPTMLKRSDASIPGSNQLPEFAGLEEFKLNVTDYMSLTDFSVCDAVALFVDLSDIADSILLNMFSPTSKNRATNINCVLSNLGKYNLELMNWHYKLPDTISWRTIDLKKDRIPNLCAVSLYYHLIRICLNRPFLSRKEVTANDLTPKTICTDSINEIVTVIRAHRTANGLRYSTLYIVYAAIVSCSVILLLRDMCTDSELLTLNNDMMFFIEVLKECSQTWKLAQRSIVLIENTLKGKTNSQSTSEFVSPISDTENGSSSQQVSEAKDIVEPSDVLDELQKFDLLPENDDNFQTFQAFYGGPPIILSPNLYEKKLNEKTL O74916 YJ75_SCHPO ACT_SITE 186; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 152; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 152; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 187; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250" COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; SIGNAL 1..25; /evidence="ECO:0000255" SPCC757.05c; CHAIN 26..400; /note="Peptidase M20 domain-containing protein C757.05c"; /id="PRO_0000359400" CARBOHYD 80; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MTMKISVWSLLIVIGYHLWMSPVLAGPLNFGYLSWGQHSILEQDSVQLISHQSLLPAGDNLISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSSNPTVRDNVYAYLGSQRNTKVVLTSHIDTVNPFLPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTVANKLNADWEVAIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPKSKLLGPSTINIGTIEGGAAANILAAEAKAEVFIRVAEDIETIRDIAEDLFDTEHSEIKVIQYSPPQYLDYDIPGMDTVVLAYATDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMVMYNLR O74920 VPH2_SCHPO SPCC757.10; CHAIN 1..213; /note="Vacuolar ATPase assembly integral membrane protein vph2"; /id="PRO_0000065873" MLYRLSEKQQTDLRCNKLTVDGFELVKMLKELRLHNRNINFLEFLRGVQIVPSDSVFLGEIDENSHTQDNTTTSILKEKELYDGIPLLPSMAGVSMDPEREKKSELRLMKNQISAIINILFTVVGTVTAVWYCTSSLSIEKKIALCAFSAILVLVADTFLYVRYLSAQPVRTSKNHTRQIIYTWTTNDPVLQSNEQLAIELGAIPSLKEKKNQ O74921 YJ7B_SCHPO SPCC757.11c; CHAIN 1..471; /note="Uncharacterized MFS-type transporter C757.11c"; /id="PRO_0000372715" MEQQSNLEKDLSVSSFLDEKEKSGYKQSVRLVSNDPSASPAATHKPPFISAALMLLNNTILCISFTIVVPTSERFVQHLGGGNGLSGVIIGLPTITALVLLYPMLRFSTPKAAKGYTIYRRPYTMSCISCIIGHIMYALADKAKSVALILVSRIFTGVACTMFLYHKRYFTDKALISIKYRTSMGVVNSVMATLGLTAGPFIGGLMAKSSMKSQSDIWNEYTSGNWLMAFIWVGLFLFGFACFREVLSPQTDVKEEVVEEKHVINDVKQDTNSKLGFVGCLVIFVVAFSGFSAYFLLNAYQASVPIYTSMLYNYSSFQAGNFLSLAGIINVPLLLIFSYLTRYLTDRDIILLGCCLNIVCMVIHITIHYTGKEFVQPYFIIYTLVFFGSSIANSPSVSLLTKVLHPKYHLIGNVAVQISISLSDTVGAIFGGAFRSFSPVVFFAVCLILNVMSVLALLIIWKKLKVKLRLA O74923 YJ7D_SCHPO SPCC757.13; CHAIN 1..522; /note="Uncharacterized transporter C757.13"; /id="PRO_0000372785" MSSITSRVSSRSSHELTEKKSGVTNDFKNSFEVGEVKRLPDAEGTADAVAQELLADDDFTYTAKEARRVLWKIDLVMMPVMCITYMIQYLDKTALSYAALYGMKTDTHIDGHTYSSMTTLFYAGYLVAQYPAAILMQKCRLSYFIFCNVFLWSAMVCLMAACRNGPSLLGLRFLAGIFEASITPAFINITAMWYRREEQPMRTLCWYAFNGIAQIIGSILSYGLGHIHGKVASWRYVFIVIGLMSLGWGVVFVFIPSNPSKARFLSSREKRIALERVRDNRTGLENKQFKWKHAYEAFLDPQVIMITLFTGVCMITNGIGVFSTLIIKGLGYNELHSAVLNMPLGAIEVAAMFISGVLCKVFKNGRLLIGVFMNCLTLAGCLMIWKIPDSNPYGRLVGVWFTMWVPASSALLLSLISSNVAGYTKKTVTSATVFVFYSVGNIVSPQLFKSGQTPEYIEGIQAMIVSLCIIIAIAFVLTGYYIYENKRRDRLLAEDPSLGESIKNEEFMDLTDRQQPKFRYRW O74939 YJB1_SCHPO SPCC553.01c; CHAIN 1..715; /note="Uncharacterized protein C553.01c"; /id="PRO_0000116810" MDTSSNVFHYQVLWTSDKAKKVKVWKDGTMRFHSFNNRGILYDSDNRVVDDFFLNNKRIVLDSEIEFNRTIVYVENLQTTTEANIPPIPRKSKLSETGKRPAYLLKPFQPPFHSANSDVSNNSNGALSSNMLKTHAHHTNSTKSTIFRNANLQSYGVDDSDIGSLRCSSKHQLSVTPEIQPKAKFRPNSYLASSVEESNRANNTSPYPPSNSSVTALPKPSKIAYIPVLSKPKSFNGTLVEDPVEEFGEDDIASDFFSSPSADLEADDFTTLNNSNAGHLLQNLSNDNVSVSVKALENGNEEVSNNHARSPHSSRACNTIPSNKNDGLNDDHQRQDSSVAEPSPTSKRLRLTRLPLPLLRKPTGKRQNFINITVTDPSKNLYERSVKTAAELASLQNVTETTDNEIPNSPDFLDAASEEDEHIPSLDSSSLLTPLALPNKKAFQPVKFRVPSFSSPLVKPASSSSFGRSHSHLGTSLRSNELNGSSASSSIFLQSNNAVNPNVSPSTVLEHAKHPSLAKHSGVSLRTGLLIYPKYANGSKRKDGFGATSIISSGEHSSLPKNSKSRNVSVFSSPFNVPSFTVSSSDQVQKKKGNVPNAIETDSSPSDTISSSPTVRAVNLSPSKNQKPPKILTKIPDIFSKAGKKSPILPTFQESCSLPIEPFSSNITDLPFVNTVTLASTSSKIKRAKLKMLKFKHAMTTQGRDLDSDEDGDFI O74943 YJB6_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPCC553.06; CHAIN 19..271; /note="Uncharacterized protein C553.06"; /id="PRO_0000372342" MKGFFLIAGFLLFARALCASWNVEEGTLQLSSQDLESENAYDLKFSQIQSSTVYELTGDETLNLKFTCILNGTGAIPHQAHLLLSDTEHPTLAVIYPASVSQGGVASLELRLFDIPTSLLRSDSTLTAKLLVASFGETIPFSLPLGQLSINVPPSLYHKAEFSPLDELSPKEVILHTFSPPPKRANYFLSICFSVSVVVSLIGLLGVWQKLLPKSNVYSVSSSSFARTFGFASLAVAEILLFIYWTSLSIFQFGAYAAGVAIMCGIAAKSL O74947 YJBA_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPCC553.10; CHAIN 17..349; /note="Uncharacterized protein C553.10"; /id="PRO_0000372343" MLFKISFLALIASALAMSINSPTNGDTWQTNGEEQITWNVVSTDEPSAALYLTNFAVYPTVTQYLDTVDTSTGSYTTNTTNWPTGQGFQINMAYPGRPEQIYAQSQQFNIVEGAASSSSSSSSSSSSLVSSTTSSSSSATPSTTSSSSSSSSSSSSSSSKSSSSSSKSSSRSSSRTTSHRTTSHKSSSYRPTVFPYTTISHYNITNATNGTYCNGTNGTNFTCIVNASNATNSTFWLNGTNSTNGTNSTNSTSTTSHSLTKLPTSSKSLTTSKTTASGHITKGVMEALSTNDTTNTTDDATNTTSDSSSSSSASASSSSSSSSAASLVSQPVGISAVIAFFAVALSLTL O74953 YJC7_SCHPO SPCC736.07c; CHAIN 1..699; /note="Uncharacterized protein C736.07c"; /id="PRO_0000372344" MNDERLVAINFEQQIFSKISEISESVGRAIRYCKEDGKVEGCETASHVDFLNHIHLLLGNYNNDLASSIEKKKSELIVRNSEGLPVMDIHEEVDKDGNIISASVAPQRISSVIDYADVFRSLPGFKNIENGGNRDTSSRIEELSEEEINDSTKNINYKAPEMGSLPSNTEFTSTPTLGVSEFPSKHGDHSDSKTYESPISNSQAASLSDSDMVQQIKNGSKTSLFKKGFLFKKNNAMQNRTTSNIKSNASAIEKNKETILNALNNSTLNENGHQDTQNEVLRDIVLEHPTAKAQDTGESNKDNNTSTSKHKKRPKRLSKFKQAKLETKKSGNKDHATSSEKLSLGNESIHSINETRSSSIEEPDNADNKIVEEEPMLLPVPTTAQGQNVLEAVQYDGLDSLEDMEALIQEMEEEGELDDNSESEEDEHGMTIGFSKELKAPPDPQYFTEKTGATTYVNGNDESLNVSDFPQIVEQEELSSKNPRKVHFSDTLEIKHVSRSGKANIEVIPAPTEEYDNLFGPDDFQSRISAFRKARSKLRAKENEEGNHSNATCTIKNDDLSNTLNNRAANTKLNPKEEDKSTVESELKAPPKEKSSETSKEYLNEPSVVKDFVVERTPSDKISESKEAFDAKVEEISDQRAISQRYYELRKKMIDNTGEYIKDEEEQAVIPLDENGNEKPKMSRFMTARLRGRVPIYEH O74956 RT08_SCHPO SPCC736.10c; CHAIN 1..152; /note="Small ribosomal subunit protein uS8m"; /id="PRO_0000315961" MQLHYVFSHLQNSFRARKSLASVPNCNSVLELCAVLYHQGFLSSIQRGDIHGPDALPTITTRQNVATRRLWLGLKYFEGKPVLHYIRAVSKPSRKVNLTPSELLQFAKGRKVSFVNGLEPAEVGIVETKHGIMSIDDAIKNNLGGNVICRVK O74959 YJCD_SCHPO ACT_SITE 213; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 217; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 54; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 78; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 101; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 128; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 213; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 217; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868" SPCC736.13; CHAIN 1..339; /note="Uncharacterized oxidoreductase C736.13"; /id="PRO_0000374031" MSYSFQGLLNRVNESAIVNTLKEYTGLNTPKWTFNDIPDLTGKVALVTGSSGGIGYVTALELARKGAKVYLAGRNEEKYQKVMKQIHDEVRHSKIRFLRLDLLDFESVYQAAESFIAKEEKLHILVNNAGIMNPPFELTKDGYELQIQTNYLSHYLFTELLLPTLRRTAEECRPGDVRIVHVASIAYLQAPYSGIYFPDLNLPHVLLGTFARYGQSKYAQILYSIALAKRLEKYGIYSVSLHPGVIRTELTRYSPTFALKLLEKSVFQYLLLDPIRGAMTSLYAATSPEISKEHLNGAYFTAIAQRGILHRAHDDAFVEELYRYTHKIFEDLKYLAPSP O74963 NCA2_SCHPO SPBC4B4.02c; CHAIN 1..573; /note="Nuclear control of ATPase protein 2"; /id="PRO_0000374014" MELYQKHLKDVYANFNKLAAVHGETTSNSVTFHVFQQLDSTNLTNYQLENVITQVKELDKGPKDYLYWVILGRCSAHLHVKMLDQLLEEAMIMSDNLHYWESIDKNWYSRVLFLIQSFPTRLYHICRNSIKSILQFQNFSNIFAKKNLFPKVSKSDVLLFPRDAFISQASLLSLIRHEYRGNAKRLRQLRDEHACKIGCLTRAIMSEGVSDAASSSGDKNGISAKADLKQVVSQWIQRLSQLQGQKIDNSESLPDILSITLDNLSHPTDEYFEAKAYFRPSAIERNWPKIFVTLLSAWLSTQIITKNRTSIRLWIDYLYSTAVDFYTNWIQKPILGIFDTIRSNRADSQITLLQTKSLESDMESLQRMVIDFVSDTSPAGINLDLVKQEVQQGDLTYVLQAYEHDLKTPIRTAVSGNLVRTLLIQLQKTKVDVEVALSGIDRLLKSQELVFATVGITPSLIFCYVIIRYVKANIFNNDTLSRAERRQRFRQSLRAAERILVRSQKMNSLDDMSYGLLVFQVNLMAIMSMDMGLSKDVAEDLLQDLEDIQSSSYGVQAQLRAVDRIYRLFKNSI O74965 EIF2A_SCHPO SPBC4B4.04; STRAND 6..13; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 15..19; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 37..42; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 46..55; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 57..61; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 67..71; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 75..81; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 85..92; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 106..113; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 116..120; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 138..143; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 146..152; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 160..162; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 170..173; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 176..178; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 180..185; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 193..201; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 203..214; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 220..222; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 228..233; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 242..247; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 267..269; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 271..276; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 283..297; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 299..301; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 303..311; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 314..317; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 321..327; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 330..333; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 335..340; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 345..352; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 358..361; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 365..372; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 382..390; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 392..397; /evidence="ECO:0007829|PDB:3WJ9"; STRAND 399..406; /evidence="ECO:0007829|PDB:3WJ9" HELIX 20..22; /evidence="ECO:0007829|PDB:3WJ9" TURN 62..64; /evidence="ECO:0007829|PDB:3WJ9"; TURN 341..344; /evidence="ECO:0007829|PDB:3WJ9"; TURN 374..376; /evidence="ECO:0007829|PDB:3WJ9" CHAIN 1..576; /note="Eukaryotic translation initiation factor 2A"; /id="PRO_0000286083" MSQKSQFAYRSSKSIGLVNASENYASPPKFEAISEPARNACYSPNGKLFAYATATQVVINDTESGAKLTQLPAANTYELGFSPLGKYLSTWERPGKEADGTPKQNMKVWNTETGQLVFSFVQRNQTGWNLQYTCDESLAARLVTNEVHFYETGNMSKGPIAKLRVEGISDFALSPGQNHAVAVFIPEKKGAPASVRTYSIPNFNSPLSQKTFFKADKVQFKWNALGTSLLVLTQTEVDKSNKNYYGETNLYLLGITGQFDCRVDLDREGPIHDVCWNADSKEFGIVYGYMPAKTAIFDNRANVVSIIPPAPRNTLIFSPNSRYILLAGFGNLQGSIDIFDAANNMKKITTVEAANCTYCEFSPDSQFLLTAVTSPRLRVDNSIKIWHITGAPMFYEEFNELYQAFWRPRPLNPTLLQNALTSASLPSPPTPHASASKLAAKPSVKPAGAYRPPGARGQNSTFSYRREEIDVMSSGSANKHVNSSRQRVVPGATPVIDGNKKNNKKTKPAVKQVAQPTAEVSDEKKIRSLCKKLRAIDDLKSRLNNNEKLEATQVKKIESEGKVLAELKALGWTPDA O74970 PRP39_SCHPO SPBC4B4.09; CHAIN 1..612; /note="Pre-mRNA-processing factor 39"; /id="PRO_0000205757" MDYGDIYIAEETEWDKYNRQINKNPDDFDAWEGLVRASEHLEGGVGRNSSKQAINTLRSVYDRFLGKYPLLFGYWKKYADFEFFVAGAEASEHIYERGIAGIPHSVDLWTNYCAFKMETNGDANEVRELFMQGANMVGLDFLSHPFWDKYLEFEERQERPDNVFQLLERLIHIPLHQYARYFERFVQVSQSQPIQQLLPPDVLASIRADVTREPAKVVSAGSKQITVERGELEIEREMRARIYNIHLQIFQKVQLETAKRWTFESEIKRPYFHVKELDEAQLVNWRKYLDFEEVEGDFQRICHLYERCLITCALYDEFWFRYARWMSAQPDHLNDVSIIYERASCIFASISRPGIRVQYALFEESQGNIASAKAIYQSILTQLPGNLEAVLGWVGLERRNAPNYDLTNAHAVLRSIINEGKCNTGITEVLITEDIKLVWKIEGDIELARNMFLQNAPALLDCRHFWISFLRFELEQPLNSKNYTEHHARVSNVMEMIRNKTRLPPRTIMDLTKLYMEYLCHQSNDPSVLQEYLLIDRDVFGPFSVRESHWKKLDEGQDLKQVSTRLLSTNGHPGISVNEAKIKSGESPYEKYYRLQGVVETVTSGVAANGSS O74972 FYV4_SCHPO TRANSIT 1..22; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC4B4.11; CHAIN 23..113; /note="Small ribosomal subunit protein mS41"; /id="PRO_0000292474" MLILKRIFIIRNFIFPFSNCRYASTVPSPRSGISNTNDFFKRIGRDTAEKVNGKFESWDGLFRKSTKTMKKEGIDVRTRKYIASQRNRFKEGFIVKPYPVMVKKNGGERRKRK O74978 YQL5_SCHPO SPCC1827.05c; STRAND 106..111; /evidence="ECO:0007829|PDB:8EUY"; STRAND 131..134; /evidence="ECO:0007829|PDB:8EUY"; STRAND 149..155; /evidence="ECO:0007829|PDB:8EUY"; STRAND 169..171; /evidence="ECO:0007829|PDB:8EUY"; STRAND 174..181; /evidence="ECO:0007829|PDB:8EUY" HELIX 118..128; /evidence="ECO:0007829|PDB:8EUY"; HELIX 156..166; /evidence="ECO:0007829|PDB:8EUY"; HELIX 189..191; /evidence="ECO:0007829|PDB:8EUY"; HELIX 203..210; /evidence="ECO:0007829|PDB:8EUY"; HELIX 221..237; /evidence="ECO:0007829|PDB:8EUY" TURN 140..142; /evidence="ECO:0007829|PDB:8EUY"; TURN 183..185; /evidence="ECO:0007829|PDB:8EUY"; TURN 192..195; /evidence="ECO:0007829|PDB:8EUP" CHAIN 1..276; /note="Uncharacterized RNA-binding protein C1827.05c"; /id="PRO_0000310821" MSKAKSPIKSSKKSVNQPKSVLREKKVKDAEKAEHISLQGHVDNSDEEGQDKEFFPGFGSSDDDEEDSPNALVNTSRQIMDLGEDAEKTIKKKVSENKNLQKKKGVLYVGRLPHGFYEKQMRMYFSQFGPVLRLRMSRNRKTGSSKHYAFIEFESLDVANVVAETMHNYLLYGKLLQCKVIPEDQVHENMFKGADVPFKRIPHATIARLQHEKPLSKEKADKLITRHNRKLKLKKRKLKELGITLESDVSHPKAASPVASKKSSKKKNKKVLAAHK O74981 MU112_SCHPO SPCC338.02; CHAIN 1..125; /note="Meiotically up-regulated gene 112 protein"; /id="PRO_0000116822" MEVQKIWKSFLNAISKVFSKGKKLRCTCFPKRKKEASERSCFPFLDTETISSCDLSDDVLSPKLFAKNSYRCSLKETKCIDVIVSHNSLAPQFTEIRYTDGISAKAENTDEMTMHIALAPLTENQ O74982 CID2_SCHPO SPCC338.04; CHAIN 1..167; /note="Protein MIX23"; /id="PRO_0000089748" MNEEKRGLCMNIRYLKNVLRKARKIDDTIQLSLNSAKWEYPEGKVHETQEERCQNVKKKLFEGWLSRDQFLKECQTIVRSQLDQDRNTSKSPLKSQQQLPSSSTTQVSERLDPYAKEVQVQLSPPEEVQIVLQSELSVEQIIRDQTWEVLTNACPGMFKDWRDTYKD O74984 HSP15_SCHPO SPCC338.06c; CHAIN 1..139; /note="Heat shock protein homolog C338.06c"; /id="PRO_0000310435" MLFDAFTNGFMNDIFEFGDRSKFNRSAWLSCWGPALELRETEDTIEVDVEVPGIDKQNLKVDLHGSKLTISGERKKPEEEKAGPLIRWSERCVGAFSRTITLPQPVDEKLIHASLNNGILSIVMKKKNPEFTTRIVEIQ O74989 YJZC_SCHPO SPCC338.12; CHAIN 1..77; /note="Uncharacterized protein C338.12"; /id="PRO_0000372632" MSQKSYIVQLKDSVDPASMDKIKSDLEASGAKIGHTYDTVFKGFSVSLPENAVDALSAHPEIQHFEPDQEMHTMKKD O94243 MUG9_SCHPO SPCC70.09c; CHAIN 1..208; /note="Meiotically up-regulated gene 9 protein"; /id="PRO_0000278486" MRKQAGGPCEKLNFPLVELEPYARVNRETTKLNKAHVRRDYSGRSICQPDTNNPTRWKYERPLETIRAWQDVAEGKVPASNEKAARVSNLKTVPSLKRENKEVNANSKPPVKQQEVIESTVISKSQSPSVKQLKLTESTLLAPSSSLKPSVSLKKDISSNLLCAAASNGYFRRPAAMRAQTLVPITQPDSKKNELKQKFKHLVHHVLT O94254 MUG45_SCHPO SPBP8B7.04; CHAIN 1..819; /note="Meiotically up-regulated gene 45 protein"; /id="PRO_0000278500" MKNLANIKLYWNENDFLIADMLLILKLSPRSSSDCLLDLRDRKWELVCCKELNIGNERNPLNVPLFELPVNSLELQNSVSNDMFKHVYSQNVELNHKTQVDFTEQLIPKKSLNKLNGTLRETMSRMPSFESISLSETSNALDDSCFNDDWITIESEFSPPIDRGMTLEAMDSQNDTLFTSKQLNNGPNFPVEKATFFLESNMGLSQRAAATSTTPVCNISSVTSAINSVGEISNASHSSSTSELPCTYGNTSSIFQVKNEMSNIKSAISEGYIAHDQQSKKVSVQNIKKEFLIPFEFSLEGGFLNYNKTFSNLYKVLSETEKTRDSKVWFTFRLVLKTKPLYASESEFYETKLNFFTFPLECAINFHIDCSCFDDWRLFSLKESSSVAVPIPKIKKESGRSMFQSLLFQFNHCIPFRLSWINYKQSQLNIILTETTIRPRICAAYQKLEYNILVLLNEKPSSGSQLILSASPTCTIENIYIENTRLHFSKSQTPEQTVISFIDVQCVKVTEATKTLELSVILSERLVYETALKLPVIKYVKGDNRFCFKQLLEYYDIYLKFKLLADWRLLTNPVLQIQEISDYCHFKLLKKVNRNLQIKTNYPTQEFHLLRPTIKILQISKHEYFLHFSSSYIFNDARERDVYGVKLSKNMWISWAYVDNCEANFFCKDGTYFFRTTSRKQILLLEIGILIKPERYNLFKYRVYLPQFLPPTDSRTLVEFQTIVYTNSTLLFDGSFYFSQNGGFDFEPRQNYTYFDFKSEFIILQNSYSIYGPAKNIIKLLLELIEVILNVNVSTTAMCLLTLLIGIYLILQVVFIYTN O94257 LCMT1_SCHPO BINDING 50; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 75; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 100; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 145..146; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 169; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA-COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=2.1.1.233; SPBP8B7.08c; CHAIN 1..310; /note="Leucine carboxyl methyltransferase 1"; /id="PRO_0000226132" MDITETDLDALKCRSSATKSGYIHDPFIKFFSPSRNSHKPPIINRGTYVRTWSIDHILQKFIESFDGKKQIISLGAGTDTRVFRYISEYGPENLKFIEFDFYPNCIRKIRTIEKHEALKQNIGDYVVDISGGSLVSGSLDIYSYDIREIVHKGFPGFVDFSLPTIVLSECCLCYLEPEEASSLCRWFQNMFATSGIVVYEPIQGMDNFGKMMKANLSARGVILKTLDCYETTEQQRMRFLDYGYSEVIAEDFLTIEETWIPIEEKKRTMSIEMLDELEEWQLLAKHYCLTFAATENLWNQIILQLPHLKT O94264 YORF_SCHPO SPBP8B7.15c; CHAIN 1..482; /note="Uncharacterized RING finger protein P8B7.15c"; /id="PRO_0000310491" MSGVIYYKFKSQKDPSRITFDGTIGMSVFDVKREIIMQKKLGNGLDFDLLLYNANSNEEYDDDTFIIPRSTSVIVRRVPAQKSGKGTAARYVSGAPKTTGARSDSVKRPVPMLQKKAPITSGESNINKSPSSSEDAAIQQMFQVSSDQWRETQDKMASATPIYKPNQRRIAASVPDKPPPPGYICYRCGQKGHWIQACPTNADPNYDGKPRVKRTTGIPRSFLKNVERPAEGDAANIMINAEGDYVVVQPDVASWETYQSRKAALTANDVYKMQPPNISLACTLCKKLARNACRTPCCDKLFCEECIQTALLDSDFECPNCHRKDVLLDTLNPDYQKQREIEAVVKSVLGSNSKNSDKVGTSDDNNTPMSEKRKREDDDANGPNKFAARSSAVFSKATAEPAFKSAMAIPDMPSMPHVQGFPAPFPPFMMPGLPQMPPMMMNAIAGQVYHNNRNPPRTNSRPSNASVPPPSSLHKNPPTKTN O94271 YORN_SCHPO SPBP8B7.23; CHAIN 1..673; /note="Uncharacterized RING finger protein P8B7.23"; /id="PRO_0000310492" MLNGEKSALGEMPSNSNSSSKLNAKSPNFIPSSSNIPRSSAKTKEHSADRKPHRNSEKKTQGMPRKNQQLASSERKTKNKKRLEKQSSAIADSIGESLDDPQTVYDEHLFDILSARTNKRGQINLNHLLNFQFTPRTNSNAFSAPPRRSRGYNTYGQGSGHHPMDKSRYVNANYRFVVSPIGDYQSQKLDPDSPVKWEDVWQVLCSSDFQLAACPFCLEEKPVAARMSRCGHVYCFSCLLRFVETPTAAEVKAAETSGTKIVKCGHRSCPICWDSIRLRDVHPIRWVEDKEFQKLEEGKSVCLRLYQRNNGSILAFPRSCRSFALDGSFHSDEIPNFTMSGAAYARIIIGSHDYMVQQHLLEIEQLQQIAAEDISLYGSADTYYERITQILLDRISSLSESVNEQNIKSLQTDIDNLCLQSNSLKQLSEVDDLNDVSGSEIADAYLFYQPFAHSHIYLSPLDIRILKSAFGSYENFPDELVPRVERISSGHLVNSELRQRFKYMAHLPEGCEVAFIECDWSKIIPKEVLLTFKSEISKRRKQRKAQEMREERYRQRAERDTEEQIYSELNMQRPVPKTVVHEDPAEAFPTLGSHHQFESTDEVNTDESTLSTAKTVWGTRALANIQNDTDDQDDLDGWKVDWDKVAQLSAPSKNSKNKKKKKLVLLSTGAAHR O94274 YORQ_SCHPO SPBP8B7.26; CHAIN 1..262; /note="Uncharacterized protein P8B7.26"; /id="PRO_0000304061" MFDSTKKSLHSMSDSANRFQNKITSKLPGEHGEDAMYDIRSVHGTGPRLSIKYVDVTKLPPPPKHASQLRAGGSSTGSTPRTASPAVGNQDYSKPSYSQPSYSQPSQPPKEPALPSRGTPSLPSRPGSRPSVLNQEQVPPPPVRPNVMSQMPPPPSYSSSGSYSQTYQSNANYTASSPLPTASANAPLPVPPPRRVSQNSSYASGSVPAATAASTASPVKKPPPPAPPKPRRLAARTSSNSSGVSSPTSVPPPVQRNTRPNL O94280 YGX1_SCHPO SPBC2G5.01; CHAIN 1..374; /note="UPF0674 endoplasmic reticulum membrane protein C2G5.01"; /id="PRO_0000353797" CARBOHYD 287; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MINKKLLFLVFALAKGVLADEEDEYEEDYNMNPELENPGMFKHVDWRDFRLEFVILACFFLYVFSFITQKKKNQKIASRWYGSLQSSFRQQFAQYGPGPNSSPIIYDSPTEFSSYLTGRLNVKNVYTTLQLFPRQDLLAYSLNQIVEILLGNVMSSVLPVADRFQFDLTLADQNLKAERFVFAIVHKDCMRILREIRYDLSFTRISSSPYLPETHVLMSENNECSQAIFEIPEFMSSINECIENLEYFIVTDQPSVPPATEKDYVTKPRIEASIRIKKITSLSGLSNATGSALFNSLLLVADSCPKFQWRPEVSKKLTSARKLAFEQVVHASAAKAAKKKVKSSGDISKLSESDQKKRMERERQRKMRRRAKKM O94287 YOO2_SCHPO SPBC887.02; CHAIN 1..696; /note="Uncharacterized chloride channel protein C887.02"; /id="PRO_0000314105" MKDDQLIDWIHERYEEQKSANRLAGRFRFLGLETKYSIISIISGIFIGLTAALLNALASLLNSFREGYCTVNILFDKQTCCSTLTEDYECQEFFFWRNNHSVFVSCLIYVSVSVGFAFIATTLGYVVAPAARASGIPTIKAILSGYKYPDMNVFFSIKTLCSKSLAVCFSVASGLWVGKEGPFVHIATNIIYLVERIAPSLADSEIFTRQLLAAAMASGIAASFNAPVGGVIFALEQLASSSFPSLFTGSIWYEFLCSASSVVALQLIRSWHTDVGYLSYVSLDRRWSYKDTLPFIFISILCGCLGSVLIYLNMKFASKTKGFSKISNVFFVIFLSLITSLTAYAILGESELLFNPMELFPQVINSCSPSSSTVLCETTFWVTAIVLFTSALLGLLLTSATFGAAIPTGIIVPSLAIGACIGRAVGTLLKSRFPSLAGTSIYGVIGSIAFLSSTTRLVVALVVILFELTGALNIALPLMLATLISKWVSDSIIETSIYDAWIQFRNIPYFPSSNSLKFSIPLNFPVRSPEQLVRLPIRSCSIEELERAMHDSSQSFFVVLKNDTEFFEGFISRNKVSELLNRRPMSSNMQTTDNTGLDPLRSASAPVDSTFDLFDYIHPTTFTLNYDTPPVLMLKLFKDAGITNLALLNHGKLHGVLTKIDIIEYAKKCKTHTGNTYSELPTGVTYETDIFNRADD O94292 RM38_SCHPO SPBC887.07; CHAIN 1..136; /note="Large ribosomal subunit protein uL14m"; /id="PRO_0000310370" MYGQVLESLAMIGLKGILKVIDNSGATLAECIRVVRAGKFASLGDEVVVVVKKARSGSSVTAANKVKRGDIHHAIIVRTKSPVRRPDGRYVRFDDNACVLVNKECEPLGTRILSVVANELRTKHHTKIASLAPRTI O94301 HFI1_SCHPO SPBC887.18c; CHAIN 1..339; /note="Transcriptional coactivator hfi1"; /id="PRO_0000372427" MTEGVTVQKVQSASSNGHKPNTVISQIISEMQSLLGSSFEVYTKTMTDFLIGQLSRKEMKSMLLTFAGKSNFDKLHNSIIFHILKLMQKNNDTFSALHHLPWFKRKKVDNSLFLHKKISSQNAQVRLIKRIVMSLSYKDRARIKTALKEKPVTPSLISGLLLETRIAKLPKIPVSRDKLNSVFVNDIKAGYVAPLACETLELPDSESLKERITAISLENGLLGGVQKGVSDIILAGLESHLKNILSRCFSILNKNIRQKNTENDAAGFTINDLNLAWTIEPHAFVEQYPQKLRMPFLLHDSYTEDEISICAESPSYMLASNDAQSDRNSVASLLDEVLS O94302 RFT1_SCHPO SPBC887.19; CHAIN 1..527; /note="Man(5)GlcNAc(2)-PP-dolichol translocation protein RFT1"; /id="PRO_0000212418" MDKSDSLLQSSSKGLRSSIFFQGSSRILTFFLNQLTIRLTSPSAYAFSSIHFEILQSTILFLSRESVRLAMQRIPSENAIITSTSTESNKSKKLSDQLQLIKNTSLISVYIGIVISLLVSLFYFYSLPNFPYSKTCIFIYTVSSFIELLSEPYYEVLQWRQKFSKTASAEGLGTIICSLLSFAISVLGRNKAPSSLPFALGNLSEKVTIFFTLRYFAKQPFSIFLHKVGENERYIFWDSSTLRIICSHTYQVLLKHLITKGDKIMVAWYASPSAQGPYALASNYGSLLARIVFRPVEDHSHIVFAQLTHYKNKKDEKKALNLLAWILKLYSYMSLFILFGSNYSDIVLLFGAGSKWASPDSSSILSWYAMYIPFMAANGVLEAFYVSAANSSQLYDQGKCYLASAVFYFITGKFLLSWFNLGSHGLILANILNLSLRICFALRFILHNYKDFSLPRSLPRPFLLALSILLSIISSFLVKHWRESKVPFLVYFLSAPSLAILYSCFIILVDKDVRGYAKILLSKYYIK O94306 YCGJ_SCHPO SPCC16C4.19; CHAIN 1..184; /note="Uncharacterized protein C16C4.19"; /id="PRO_0000116547" MDQERKLQFLLSIAAETYAISPSLSSHYLRRMFSLLEEWNLETDPKTLLHGCSKCGSLFIFGRNIKLRTISSERKARTDLKKGEVSRLGTNLEINCLVCSYVHEIPLGVPLRLHQSKQALRAKAIAESSSTKLESRKSAHNAKVKQRQRLRASGLNGILDRKKKKDEVAKSTSSLSLQDFMSPI O94312 PDP2_SCHPO SPBC215.07c; STRAND 128..133; /evidence="ECO:0007829|PDB:1H3Z"; STRAND 136..143; /evidence="ECO:0007829|PDB:1H3Z"; STRAND 160..162; /evidence="ECO:0007829|PDB:1H3Z"; STRAND 165..169; /evidence="ECO:0007829|PDB:1H3Z"; STRAND 176..178; /evidence="ECO:0007829|PDB:1H3Z"; STRAND 183..185; /evidence="ECO:0007829|PDB:1H3Z" HELIX 146..148; /evidence="ECO:0007829|PDB:1H3Z"; HELIX 151..155; /evidence="ECO:0007829|PDB:1H3Z"; HELIX 180..182; /evidence="ECO:0007829|PDB:1H3Z"; HELIX 188..196; /evidence="ECO:0007829|PDB:1H3Z"; HELIX 203..214; /evidence="ECO:0007829|PDB:1H3Z"; HELIX 218..220; /evidence="ECO:0007829|PDB:1H3Z" TURN 170..173; /evidence="ECO:0007829|PDB:1H3Z" CHAIN 1..568; /note="PWWP domain-containing protein2"; /id="PRO_0000116768" MTEIKDSSVKDENPGKQEESSIAVESREMSTATNNSKNIETTSSNGAEDIKIQRDVGDDKDLDDKEANDKSSKGLEEESDSKDRKTIETDQPSNNIGDIKSQKSEKSNGNARKETKQSERVNYKPGMRVLTKMSGFPWWPSMVVTESKMTSVARKSKPKRAGTFYPVIFFPNKEYLWTGSDSLTPLTSEAISQFLEKPKPKTASLIKAYKMAQSTPDLDSLSVPSSESEVSEEESDQEMSEPSPIEEDYNDTKARRITRKGTKKKTVTFDPSLESVPQKRLNASSNVSSNPAKKTRVSPRRSTAASKKKSPSSKRASSDEIEKDKEEEEGSVANEEDVAKRTFHSREQSLLFLRHKLQSSLLSPKQDLSQVDYKLVHNYLDKLANFQGIDVPLIQKTKIAVVVRKIFSLAGLPKENEDEVKSICGDILENRWKSLLQEISSQKQLSTDASQTQDASIANENETEIASLDEGSESKPTPSPPAEQLTDQKQNEDNEDKVKADSNGPTQNENETADASKDMISEEKSSKDADNSLEVAGKDFAEDGTEQTPNLAEPEDGVAAVDLSTGQK O94314 YH5A_SCHPO SPBC215.10; CHAIN 1..302; /note="Uncharacterized hydrolase C215.10"; /id="PRO_0000343147" MPSKEIDINQKKNVLPKPEDIQLIICDVDGTLLGPDHKPHPRNLRALKYLRENYPQLPFVLATGRQRTSVGNIREALGLHVFPCVHLNGCVVYDKGEIVACAALKNSLAIDIIDKLKDIQTCALFGYDEDYVYQIKQESDKKQHGIKFLRLCGETVKDDANEMLPQLKGPKDIFNKMVVFDDDTNGLEEAKKRLAGIPSDEVALTQALPQTFEIIPPNDNKGVALKNILSKIYPSISLENVLAFGDGANDVCMFELAGYSVAIRSGMPVALKAAKAISDVSSAEGAVGEVLERIYNIPPDFN O94315 YH5B_SCHPO SPBC215.11c; CHAIN 1..306; /note="Uncharacterized oxidoreductase C215.11c"; /id="PRO_0000310312" MSKTAASSAVDASQAGTVKVGDMVVNRMGFGAMRVTGDGIWDEPKDKEACIATLKRLPELNINFIDTADSYGPEVSENLLREALYPYKGLIIATKGGLVRTGPNEWHPCGAPKFLRQEVLMSMRRLGVKQIDLWQLHRIDPKVPRKDQFSEIAAMKKEGLIRHVGLSEVTVDDIKEAEQYFPVVSVQNLFNLVNRKNEKVLEYCEQKGIAFIPWYPLASGALAKPGTILDAVSKDLDRSTSQIALSWVLQRSPVMLPIPGTSKVDHLEENVKAAGIQLSSEVFAKLDEEGKSEDAKRQEEEKKKSS O94317 YH5D_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPBC215.13; PROPEP ?..534; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000373872" CHAIN 23..?; /note="Uncharacterized serine-rich protein C215.13"; /id="PRO_0000374070" CARBOHYD 31; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 426; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MGLRLLFSLICVFCISNIFTQAFLVHQIYGNSSFTKISLNQLEGRDSQEELQRRQEIRYYGRAAETGGTPTYYGYATPTSSSEPSIFSESATPSETNSYSSPVSSYSDPATSQLPSSTSFFSPTSSEYTPSSTESSSLLDPSSVSSAILPSSTSVEVSISSSSLSSSDPLTSSTFSSLSSSTSSSQPSVSSTSSSTFSSAAPTSTSSSYLSSSSVVSSSSSPSSSSSSTLTSSSLSTSSIPSTSSSSSSTSSSLSSSSSSSTASSSSSSSSIISSSSSSSSSPTSTSSTISSSSSSSSSPTSTSSTISSSSSSSSSFSSTLSSSSMSSSSSFSSSPTSSSSTISSSSSSPSSSSFSSTTSSSKSSSSFSSTVSSSSSTSSSTLTSSSSSSSRPASSSSHSSSLSSHKSSSSSKSSSAPVSSAFYHNSTSSRSSSHSSSHSLSSLSSKPILTASSSSLLTSSSHTYERSTVYVVTVETVSSGSSTYASQSTQTSILLVIVGDSSSTDSSGASSTHSKTSIFFSLFVVLAAAIVII O94322 YGK3_SCHPO SPBC725.03; CHAIN 1..257; /note="Uncharacterized protein C725.03"; /id="PRO_0000116760" MSLAWKNELLKLLKENVDSSGVIHPEYFQLATLPTGNEIYPRNRTVAIRGFVGTGWHKPRPDDVLATDLLVFSTDIASHKAAEIAEQQKNTFPSGPIPNAFEMCGWLPKTMQQIRISGQIWLYTPELADRNEFPADKLIQDHLINSNGRIPEEWSWEEERRRIWELHSPELRASFSTPPSYSKYQGDVKVSPLPSTLTGKEDPGVIEAWKTAWGRFSLVVCEANEVEFLNLTPPPGKRVLHNRDLNTKQWSSTRVNV O94323 YGK5_SCHPO ACT_SITE 118; /note="Nucleophile"; /evidence="ECO:0000250" SPBC725.05c; CHAIN 1..485; /note="Uncharacterized pyrophosphatase/phosphodiesterase C725.05c"; /id="PRO_0000317129" CARBOHYD 67; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 306; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 338; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 453; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 467; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFSWANIGSNEYLPLKNDRKAYLNQWAKRSGLAIAAICILGILILAIVKLFCFKAIIFPIVGGSFNNGTNVFQSTVIVISLDGFRADYLYRGFTPNLLSLAERNVHVPFLIPSFPSITFPNHYTIVTGLYPESHGIVSNNFFDPVTGKQFVNSMPECNKDPTWWDKGEPIWVNAERNNVRSAVHMWPGNEVENHGYRPTYSDGFNFDTTLREKKDRILEWLDLPDKDRPQLLLAYAPHVDMVGHAFGPDSPELNIIIQEVDIVIGELIEGLKKRNIDKHVNIIFLSDHGMAPTSDNRLIWLDNMFNLSAVAHRDAWPLGGFRGESDLDDEYIYESLVNYSRSSLPSAENWNVYSKKDIPSRWHYSNNERIAPVWMIPDVGWSLVSMLDHSPELEYEPLGVHGYDNLSPVMRALFIASGSSFKNFKGKKLAPFQNTEIYGILSHILDLPAQPNNGTYEGALPLRRNRNSTKEWLLKDIEQAYSKLI O94327 TSPO_SCHPO SPBC725.10; CHAIN 1..164; /note="Translocator protein homolog"; /id="PRO_0000315635" MDLNYQVFTSISKNWWSASLVPVACGWFIGNSYKPRKDYENKKQPKFHPPASAFGPAWTLLYLTMGYASHLAYKADPLMITNASRNGSILYIAQLAANFAWMPLFYGLAKPKLALADLGILTGLVGWLAKTWWPLAPTASKWLIPYLAWLGYAGYLNLGYCLLN O94336 YHM3_SCHPO SPBC1271.03c; CHAIN 1..244; /note="Uncharacterized FCP1 homology domain-containing protein C1271.03c"; /id="PRO_0000116776" MAPEPSLTYLSQASSCNGATDNRKLVILDLNGTLLCRALAVRSEKSVYEASRNPIPRPGLHNFLKYIFANFSVMVFSSSKPHNVQAMLSAIMNEEQKKALIACWTRVDMKLTKHQFDRKVQTYKNLDTVWEKIHHDSTGKPVSWSQYNTIIVDDSKTKCAAHPYNHIAVSDFVAKSHSNIPKDIELACVIRYLKHLKSVPNVSYYIYKFPFKILADKSLEDNLKYLDELDENYKKECQVDNPQP O94338 YHM5_SCHPO BINDING 150; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 155; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 166; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 169; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 174; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 177; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 183; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"; BINDING 185; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" SPBC1271.05c; CHAIN 1..215; /note="AN1-type zinc finger protein C1271.05c"; /id="PRO_0000310726" MVLLQIIASQSYSIEVDEHSSLGNIFDLLSDQGILPKNAKSLHAFYYHGTRLNMNMTCADYGIIHDSAVHIAPLPSSCDIDFKDYSTSAFHLHFSPLTPNHASTEAVSNFKQSSTIPSISKSNLTNPPLESEKSSDKALLTRPATSRRRCCHPTCTRITLRLAGNCLHCNGRFCAAHRLMEDHDCVALFSLRKEEHERNRIKLEKEHGDTLISKV O94339 MUG96_SCHPO SPBC1271.06c; CHAIN 1..146; /note="Meiotically up-regulated gene 96 protein"; /id="PRO_0000278617" MVIFSSYFSKQMNRFSTPFVFFFKKLNNTLKKSLQFIMRFHSYHPMFICLLRDSSRNENRKKKVSIGLRTIMRAFSFLMQVATCLIRYSLILTCLVAILLSVLWRIQFAALRMHDLIEEELKMFVLQHNCTLADLWSGKCPSSEDE O94340 YHM7_SCHPO SPBC1271.07c; CHAIN 1..163; /note="Uncharacterized N-acetyltransferase C1271.07c"; /id="PRO_0000310298" MMKPSNISISAVKLPQDLDDFKMLVQEYLQEFGMDLTFQNVDDELANPMRKYGPPHGIMLVARDEHGTALGCVAVHPFGGPGCCEMKRLYVRPESRGLKLGVLLVKEIIQYSEKLGYSSMVLDTLDTLLPAVRLYKSFGFKTTEPYYHNPIPNVVYMRLEMSK O94342 YHM9_SCHPO SPBC1271.09; CHAIN 1..543; /note="Probable metabolite transport protein C1271.09"; /id="PRO_0000310745" MSGGWDESKYVDNGEDEVVRQVSEPSVEEPIEASVTRYRSDEEKLDDKSSGAHVTEKEAEFDIEGGSRETSQWKHFLNVAVAGVALMSDGYCSNSIGTVITILRKLYPEETTHNKSLQDIGMIAYVGTIVGQLSFGWYSDRFGRKNGMITATIILIVSTALCTGAYGYKGSINGMLSALIAYRFFLGIGIGAEYPCGSVAASESSNELKSGLRHAAFIVVTDGAIDFGFVVGALVPYILVCIFGEHHLRIVWRLSIGLGLVIPCVLLPFRIAMKDPKTYVKHKVPLTKIPWLLVLKMYGFRLFILCLIWFVYDLSAFAFGLYSSTIVDGVLPADASTARSFGWNVLINTFYLPGALLGGVFSDLLGPKYCLITGLVLQSIFGFFMSGFYNQLVHKIAGFCVIYGIFLTLGEFGPGGNIGLLASKTSPTAIRGVYYGIAAAIGKCGAIAGVYAFGGDQVRNYFYAASAMAIFVAVLALLFVPKLKQTCIEDEDKRFIQACIDAGYGNPYNYEKNEPEQLEEPDRPPAFNPFLSATFSFHHIILC O94343 YHMA_SCHPO MOD_RES 28; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1271.10c; CHAIN 1..581; /note="Uncharacterized MFS-type transporter C1271.10c"; /id="PRO_0000372713" MEPDGYVEELPGTILIYKENQYAASEHSVLKKDGDIVLQPQPSDDPNDPLNWNKFRKNWHLVLICLVSLVTGAIANDAGSAQDQMNAELGISYDAMDNAAGVLFICVGYFTYLAMPATFLYGRRCVYLVCLLFGMLGSMWFALVKTTSNSIGNQAFIGISEACAEALTQFSVSEVFFEHERGIKIGIYILSTSVGTYLGPLAAGYIASSQGWRWIGWWGLIISGITFVLFLFTFEETTFDRAAAIDRKQIQISNDQLTVKEDFDLKDMQSDIKPDVEKSDAMDDSKMKVDYTVNEISNAVQPIYSKPSYWKRIALITPANSLSGIGFRQYIMRLFQTLRIFLFPAVLYSGLQWGAQDAWLSFYLTTEEEDWMEAPYNYGDNAVAIMNVPCIIGATIGCIYGGYFGDYFTLWAAKRNNGIKEAESRLWLMILPCIINPIGLFMFGIGTARHWHWGPTYVGLGFIGFGWGCAGDISMAYLMDAYPGMVLEAMVGVSVINNTFGYVFTFACQSWIDSLGTERTYISIGVLCFIFIATSFPMILCGKRLRKWTAKQYYTFLNVRNRLDEKIPDQDRRGQDGVESR O94344 YHMB_SCHPO SPBC1271.11; CHAIN 1..258; /note="Uncharacterized mitochondrial carrier C1271.11"; /id="PRO_0000310797" MTDDEVQWKPILVGGLSGLVAETLVFPLSTIITRVQSSLSFQQAGGFQHLYRGLSSVLVSTLPSASSFFFVYEYAKARQKPGVRNHLVSASVAEVVSCGILAPAEVVRQRAQISKTSVSQIFQSMIHNYRDLWHSFKGMCGRNVPATAFQFVLYEQFKKKFSATDHVFGAPKGAALSGAITAAVLTPLDVIKTQINLRPESYRKVVRRIYKENGIFGFEKGLGLRVFASSLGLSIYLGTYEHVKSHLHIRKAGEVSVA O94345 RM08_SCHPO SPBC1271.13; CHAIN 1..207; /note="Large ribosomal subunit protein bL17m"; /id="PRO_0000317228" MTKTLYYRKLGRTSAHRQALLRNLVTSLVKHESIQTTWAKAKEAQRFAEKLITMAKRANPQNNRKGLAEGMVFEKETTLKKVFDVLVPRYNGRRCGYTRLLKLPPRSTDNAPMGVLEFVDGPKDIRFHMTAKTVGICLAQQKALTPITRKNIHKVLLFRKNGKAEFDQLVQKEKESEHARLKEDHEDEKTVKKDWKRGDPIPRPTYI O94356 MEU6_SCHPO SPBC428.07; CHAIN 1..651; /note="Meiotic expression up-regulated protein 6"; /id="PRO_0000096455" MSYEGREERPEQIAEPTFENVSEHNEHDSGSAEAQVETLEVPLSNETDNDDATENAVPAEVQAPEEPKEPETVDNIDPADDDPNSVAAPKVEEKKSKKKAKDEKPLTYTTGGYLYCRSNGLIPHVMKRYFYMLEGPMSMDLLDHYYKKHFHGTLQGNPTEPSLASEQMHDSDADSLFQSANDHLNRIAKATQDCRGLLFYSKSQSTSVPSGIINLTDAVSIEPGTGNKFTINFNNGKSETLEALDPESKNTWITDLKNAIAKKKETKDKIKELRAYNDTLKRLGKLAARSGPSASETFRYFLPMLSNGRDAKKSSSKSHGGKQNNSVAKDGLFDFFQNMIKGKTPQNDTASPIDNETSADPVDTTVEAQSVEVPENETNQIPTTEEHFPATTEEVAPASEEKPATGPAEESTSTQNVEQASTQNDNGTPIGQIADAIEEDVKGTAQSVEQAFIEETDIALPDIALPDVATPTADDQDPSTAATNEESVVSNEDRTSKKAGKKHHRHHKKKKGGNKRVFGFKLHKYAKPTKSVKTLQADPSLEFAKAGFEIFPSNLSKKLSGLVQKKVHKKFDKDGRLKEISQFSKTTIKPETPLTPTTTPTPRTAAQEDPAEETTDALASAEGENNQMPQVLETEAAPSIASEGRSITVNA O94358 YHOA_SCHPO MOD_RES 567; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC428.10; CHAIN 1..845; /note="Uncharacterized protein C428.10"; /id="PRO_0000304015" MKRKSSHYNDAHASHINEDIEESYKDLYNNLSPSSTILLLLYARWFPATLIHFLDKYYTSTPILIDMIHKQCIYNPPKGSLHVQLEYYLAFLNRMALIFDRFPDLFPTEISKVKFFTKDFSKKDKLTALDTYRSFPGSTWKTIVTFATQEVFYLPEGLEPLKRDFSSMDKLKLIGKITYKLRLKGDTALKFAYLHAPSDVRDKVFDDAFWQEIITPKASLEQQSNNIPTGIQDSSKYTVNGPTERDNKSMKSFVRSFFTSTDSSVADTTIIPSMTQQFDKDPSTLVQSSIDKEIQVKEDGTTSSVAVNAETAVQNVNGTIKESQGTESISFASKNNSAPSADANNGNMTKLVSKEKAFLNTVTTPNADLIISEEDELTEMTLRTANGSEPTKKSNRSEQSKTVANTNVGSKNGTTPRSFAQKSSKRIKPTEGSANLNTVTELTGIGSRIAMNGSSVKASNISTEKSKTIAKPKPAKELSPQATLNSPIQSAEAGNVELKLHPQTPDRIVKVERKVHSLNMTLRSPKAGSAGKENSWRSKYLSEGKNSKAKYTAKQPSYDRAGSSLASPTKSSASPLVKAPKETPERLCTENQSTENEDQANLKESELPKEKSDIQPKNSRSTIEYIETSTRVYEMPKDTIPSRFKTSISTEVHDGRLKKYPYYHVKTPEKGTTVVSRTVTSPKSGAYASPSKASYNQDSSPNASLEQCFVQRSPSKMLTTLRNNSSTFPSLRKNAMIARKSTADSLSSPKRQSVPSTPKASLSPRVHKSMTYSPSEASPLYANKSPKSSTMVPLMKYKSGLNEGMRTSSIYSSTSSPYIRDQYFLNRMLTNGSHNGSPSWRDGLL O94359 YHOC_SCHPO SPBC428.12c; CHAIN 1..116; /note="Uncharacterized RNA-binding protein C428.12c"; /id="PRO_0000310813" MERRKATVHVGNLAPSVTESLLYNAFIPFGEIISVALHRKEKAVDRSYAFVEFDEPEDAKEAMENMNYSILCDRCIRVSPANFALSAEETAVPDIAMLHPESADFQTFKSTSTPTS O94361 YHOE_SCHPO SPBC428.14; CHAIN 1..350; /note="Uncharacterized acyltransferase C428.14"; /id="PRO_0000317311" MTCRIAIRKYSFILCLAVGSVTIYTSEVIGTPLYFVNKELYNKYIAFTKSFAGILFTALVQLFSPTPVTLTYDPELRNLFYLDRNGCLETIAAERNIVIANHQLYSDWMYVWWLSYTAKQHGHVYIMLKNSLKWLPVIGWGMQLFRFIFLSRKWDKDYETMSRHFKFIRNVRDSVSLILFPEGTNLVESTYQRSRVYADKIGVKMPKHLMLPRVRGLFYSISQLRDSMTYLYDYTFYFSDPSPKKYAADAFSLPKLFFEGVPIKRLHIHVRRFPISEIPTEEDQFTDWLYQRWYEKDKLIDTLLETGNFPGPKKLHTTVRLKHRLEILSLFSVLFTCIVAGLFLKLFISH O94362 YHOF_SCHPO BINDING 11..18; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 83..87; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" SPBC428.15; CHAIN 1..409; /note="Uncharacterized GTP-binding protein C428.15"; /id="PRO_0000339164" MGRDILIGFVGKPSSGKSTMLNALTDATAKTGNFPFTTIEPNRAIGYAQIECACSRFGLQDKCKPIYGGCKNGVRSIPIQLLDVAGLIPGAHAGKGLGNKFLDDLRHADALVHVVDVSGTTDAEGKVCRGYDPSVDIAWLYKEITAWIGNNLREKWPNIVRRHIATKANPVNTLQSQFSGYGSTPAVTAKVLDSLHLDTPLEKWDDDTIEKVVNRFVDIKFPTVIALNKIDHPDADANISKIARKEDPNRLVLASAISEVFLRRLAKQGFVKYEEGSEFVDTLDDFPDSGLKPLSENLKTRIADLQDMVLFRHGSTGVCNVLAKAMELLNLIPVFPVKNVHNFANSPNEGVFRDCILVKQGTTAGQVSQMVLGGEAMSIVGVNGNVGESDVIVPGKTDILHFRLRKAEA O94370 YG04_SCHPO SPBC1604.04; CHAIN 1..283; /note="Uncharacterized mitochondrial carrier C1604.04"; /id="PRO_0000311181" MGLAKQKDSQEFAQPVWHYTLAGGISSVICRFMIAPFDVIKIRMQITQSSLRPVFKETVQKEGVRALWRGNVVAELLYLVYGAAEFVAFSKLKHLTENLAMNDHAVNFLCGTSAGIFATLTSYPLDTMRTKFASYAKTPHMLPATKKIYAEAGIKGFFPGLKFSVIQIGPYAGCFFMFYRASEAVLSPLGLALSSTLSGVIAGAGSKAIMFPVDTVVKTLQTFPSNYKSFKDCFLSIYRNSGIKGLYRGLSVSMLKVAPGRAITMLIYEQTLQGLRTLSSPEA O94372 YG06_SCHPO SPBC1604.06c; CHAIN 1..485; /note="Uncharacterized protein C1604.06c"; /id="PRO_0000310338" MIKDLENEIYKSRKNLNNILVLFDYIDLSNHSIDEVNDAAAALCRVYCYLSRNGLLKRPKEDDSSANAQVKNWVCDNYINYTEKLTEIFSMANVEALQVSFLTMTMRLCKAESQMDENGTFRNQFYIRFCLELLSSSQLSDICIKDFVTSYLVPYDDVRFFFYKNSKKVISSLIESSKTDDPMANLDIVAFNTIRILSAIPSPLPSSSTSSWADEPSPSSTETSSIKRAFQESWLSALSLPLSVNLYKQVLNVIHKRVIPFLQKPNLLMDFLTDAYNSHHAVSLLALNGLFTLMISHNLDYPLFYPKLYALLDRNLLYLKTRSRFFRLLDLFLSSTHLPATLIASFIKRLARLALTAPPGAIAIVIPFIYNCLQRHPTCMQMLHRSSAESGDSFDFDQPDPLLTGAIESSLWELSTLQNHYYSNIASLASIMSQKFTKPRYELEDFLDHGYATMCDAELRRPLKNEPPIEFEKRTLASGLEKSWI O94373 ATPF_SCHPO TRANSIT 1..36; /note="Mitochondrion"; /evidence="ECO:0000250" SPBC1604.07; CHAIN 37..244; /note="ATP synthase subunit 4, mitochondrial"; /id="PRO_0000002523" MSSKLFCLRSFPSVQRTAWQRLVLPSTRKFSLTPTTFDKTPSGRIPPDQKAANIISSVPSTSLLTKSGVLTVTAAALATAISKGIYVVNDESIVVASFLGLVGVFGTLGRKAYNEWSDKTIAKIGGIMQAARNDHTSAIRERIDQVASLQEVESVTQALFHTSKETARMEAEIFELEQRVALAKEAKSVLDSWVHHEANVRAEQQERLVEDVLARVNSKVSTQKFQQDALNESLGEIEKVLASA O94378 YG0C_SCHPO MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 70; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 309; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 555; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 597; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 603; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 649; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 655; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 657; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1604.12; CHAIN 1..860; /note="Uncharacterized protein C1604.12"; /id="PRO_0000304121" MERIQENDPIIKSADESKESPAETLSSIFKRPKIKSSSLNKAYLGKAGSVNGASNTSTNQISSLKVDVSSPPSTAPGSAGSTPKTTPVSLNAGVPPSNTGANITTNSNNNAQTISSSSQSVGHIDNPSGLGTHGKVRLSIKLSTGGSGGSSVTGKRTAPGNPWAIRSAERLASNPTSIGTSSPESIDNNSNNKKSAPSLYAAAAASAARHSMSAAYASFTGTVYDSNGNVIKGLDTSSSLSSSSHPSHEALSTIDTKNLQALAASAAPSSCRQQPVDEERQDRVSKISKHFQDSGTPVSEEVSPTRLPSPTSARRASHLSEGKWDEIDDEDDDDWGSTIEFEDGTTVVIDAKTRRYEPVKRQDTLASNHVPSAPSNESVSSAAPSKIPVPEEASINEHSNITDEAVSLPEPVYPNAPTSAVSVHNPTISDEAEPTERAFLKKEKPQISKEKKNPNVTHEEFVEKSTALPRHINKVEIVSDSSESFAHKNNEKRFDKEASGRINDLRAEQQQIMLEARQKAIERRRNEEEELARSRERARKKAEEIKISSSKMNSSPTITNERSSNVESSKKVEAIYTKEPQSITNSPEGLHSNQETTEIDPSSPRDDSTPLSWRSHSHPIPPVQVSPLFTSDKNDPLQLNPQSDDSTSSPKHGKSRSIDEVILSIKDVIFDNNLYKQRSYQSGVAANAHLPHRVPNEHGGVSRIGNSNALGQPVSSSSSYSHSKGRDTRSSSYVVSSETSSLKSSRLILSHANSVRIQRSKGDVILNLHLPKVNPERFLPTKSLKLEEMKPLEEKVPIYRSSSKQPLRIHPTHPLRVTVCLPGSKTIQVARRSFRNSMNANRYDPQRRERIDSGLWRAKN O94384 ELY5_SCHPO SPBC29A10.06c; CHAIN 1..298; /note="Uncharacterized protein ely5"; /id="PRO_0000116764" MLKMEDDQFERFVGLFSMKDEDFPYNSQVTNEIQTFRKQQVDSQLFFDVLLSFIEGIEDPSSLYPPKSIDDLQSLFMIIENSNIDELKQQCFYYYLLKDWEKSETYSEQVSLPKNYQHLMDGYYYLDRLKFEEAINHLLLPDVLPNFPDKIIETLYSNEKYKFLIRFVSFVGPPLDTFRKEECYALSLVRYSFLASYHYMKKCTKPLVLWEEMIQLILESNDTQSCKLIVSLPLSQEECEVLFSLLRSKKEPLYLNTLLALLVESNNIQEALELSSNSTHLQKSAVNTYLHKLNSLSS O94390 ATP7_SCHPO MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000250" SPBC29A10.13; CHAIN 2..175; /note="ATP synthase subunit d, mitochondrial"; /id="PRO_0000071680" MSKVASAAGKAIDWASVASKLKLDAATASAIANFRSRHAQAVAKLGTLREQATTVDFATYRSVLANKEIVNRIESSMKSFKPVKIDLNSQLKAINAFEAKASEGAKKNVELVKAELQNLSATLKNIEQARPTEEITIEDMKQAVPEIEKIVETMVTKGKWVIPGYREKFGDLSIM O94392 YLV1_SCHPO SPAC2H10.01; CHAIN 1..480; /note="Uncharacterized transcriptional regulatory protein C2H10.01"; /id="PRO_0000310390" MTQKNTGPRRRTAVACDRCRRRKIRCTGSDIPGQPCLACQKAHADCHFSTTSWRACRKKSAPLHCPSTNGKTNVLPSYASTPSLSPMTSSHFPYASDGTLISATNHCDDCSYNPHYLPVNSNGSSPSHTSSLDSIPGYASGSGPFKTPYRPVAVSESSSRSSFSMGSSEFASSTWSQSPMQSSLYVSPSSQPLDRFSPASFPSKETLTSSSLSSSVPRSVSLSNFADSNTSNYPESSLLPAAKVGNNGFVGSNVLGSMSYSNVEDSVRFQTDSVSQMSSKSLEHLPMLSEMTLSSSASFGASVSPKSTPGSNSTGAAVDTNSVHSNGGSDLDYSSYLTDSSAVDSPSLDADEVLRSFNLANDPIGAVDPLTLEIDQGSGSQLLGQQSFANDSLNAKQSSGKLGPLPPQSFNSSDYISFDEPSRYLSDDASLWPDQYVDKVQPLATMKTCNPAVFSSNTSLDDMFFFIRDFDEDHPIQTAY O94393 PSMD9_SCHPO SPAC2H10.02c; CHAIN 1..213; /note="Probable 26S proteasome regulatory subunit p27"; /id="PRO_0000343145" MDEFKQLDLKKREIENRLNELEGVLLKERVTMDTPLLTEDGFPRSDIDVPSIRTARHEIITLRNDHRELEDQIKKVLEKVFSGFSKESLAANDETKLAQEADPLNFNAANYNMNDIISRSKILGRVKPFCVVDSVAVESPAQEAGLCIGDELVHVQNVTSLSELPTFISNNVNKTLDVLLIRGYSADGSTNLVELKLTPHKWQGPGLLGCHLR O94394 YQF1_SCHPO SPCC126.01c; CHAIN 1..369; /note="Uncharacterized WD repeat-containing protein C126.01c"; /id="PRO_0000051500" MQTNNPSYFFRSESALQDEKRKEEKSHNPNGNPRNLKAKILNIELDRTTPKKKQFPRLFVCEASHICKLYDLEINKTCKTYKGHSGPVTCCQIESLRKDGKVRHIYTGSWDHTIKKWNVSTGECVETLIGHTDYVKCLLLLEEEGLLLSGSTDASLIVWDVSSQPSRLLYKLTGHSRGIECITRQPNTDIFWTCGSESSIRCWHITKVGGSQLEEEGFWGHQSNVYCLLFDPQDSEALWTASADKTVREWSLYQGIHEETRMEHPDVCTDVLTLADGNIATACRDEEIRVWDTTTGNVKDIYSGHYESVTKILQWKSYLISSSLDQTIRVWDLEYSADNNEADDHPSLGPPSTKLTAEELAELEELMND O94398 RM17_SCHPO TRANSIT 1..25; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC126.05c; CHAIN 26..268; /note="Large ribosomal subunit protein mL46"; /id="PRO_0000343146" MYLKRNIINMQRSFSRQFHISVRNSIQSSKPLSNSTPLKGCSVGTILIRSPILTRQPSEFEKSIYKYNAELWNELSDPLPAEFYFKKGSVGEKDWQERQKTLKGKESPFETIFGKERKEMESNKLLDSATHLQSRVTEADTKNDERSTLRSLDKSLYLLVKKSKSSGWQFPNTPVTSSEKALHLLCQDLLKNILDENSLTWLVARHPLALLKTEQEKTFLLRARLLNGLDVPNLQNVYDWVWCTYDELKNKLSPSSWDSVKNILSDRL O94400 YQF7_SCHPO SPCC126.07c; CHAIN 1..571; /note="PHD and RING finger domain-containing protein C126.07c"; /id="PRO_0000303919" MNAEEDPKPADSDSSEECIICLSNLPNCPLDQWDSSSVPASISSTLDGLRIAKIPCGHYFHNHCLESWCRVANTCPLCRTEFLKVDVLEFVKGPWYRAYPVEEKTQSVANAGEPFEDEGSETCRCVICGRSDHAEVLLLCDGCDDAYHTYCLNMDAVPIEEFYCPNCVLLNYQENETLSSRISLSRRGQTRRRRVGAAARASRVSQQQQRAWTRAWNAIRNRAWDALNSDLSYYGMQQERLPARDVSSELLRRRIESARLRSNQLNEPVEQPRVVQTPVTNASEQQAWNDFDEILHANSSVHSVATEATISNPRPSSGRFQQTPIEEHHQQDTRFVNDPNSTSHDRRQKRPTRRHIPCSNKSSGSSTVLGNNSSSKSENSFLASLISNINQPSTSRIDTSFMLSLQHEIKNSHSEASDGTSDVHLTPLFSNLSPRPSHVPLSPREISNDNLDDHLIELSEPGEIVDNHLVNDTSMHQRRTSGRHDLVHSSKKVSYETKYRIERLVNAALKPYYREAKISKDQFALFNKNICRSVYTALSDGTLSLEGPQQHKISKTIREKVVNCIQSLSND O94403 YQFB_SCHPO SPCC126.11c; CHAIN 1..183; /note="Uncharacterized RNA-binding protein C126.11c"; /id="PRO_0000310820" MAKRGNKKKQEAPLSLGKHTVGGRVGKPTNAKTGSALTSDKSLFDKRIVKQLKNNELFNRLTLPSQELRDGIVRENQTKPSNSNSQSNGAISIRGIAGPTNVVIENLAPGTSSDDVAATLLNFGEILNCQVNDSQGKVRASVRFSTLASAQQVVQKLDGVTADGFKLSCYIKKNSKKRRTQKK O94404 NIF3_SCHPO SPCC126.12; CHAIN 1..278; /note="Protein NIF3 homolog"; /id="PRO_0000147355" MSKANISSKLKKVVESIYNPKLADSWDNTGLLLEAPFPRTNASSVLLTIDLTEKVAEEAISNKLVSSIVAYHPIIFRGLKAITMEDPQQRSLLKLAAEGIHVYSPHTAVDAAVDGVNDWLAQGIAGGRNNIKSVVPTQQNSVMAEAEGYGRICELKIPTTLRELVQRAKELTGLQYVQVCAPNGLDSHISKVSLCAGSGGSVVMNTDADLYFTGELSHHQVLAAMAKGISVILCGHSNTERGYLKDVMCQKLASSFHKEGVDANVIVSSMDADPLTTM O94405 YQFD_SCHPO SPCC126.13c; CHAIN 1..145; /note="Uncharacterized protein C126.13c"; /id="PRO_0000343535" MDIRESRSQSPELSQSEDAVGPCPFLISVYHQFQTKNHVLDIFEDVIPSIQVYGWLTMTLYELGVLIADQLLLNNEETRHSEWSLQIRTIFYDKYKDRPIARDLGTVCLHNPKLFQGNKLLKRTGIKCGDKIDVTIKEDKIRIKK O94406 PRP18_SCHPO SPCC126.14; CHAIN 1..343; /note="Pre-mRNA-splicing factor 18"; /id="PRO_0000058585" MDFLKEEIERKRRQLEGTSELPVKKAFRRGDWEKEREKKYLQEKQQKDEQRELKKRKLEEERLKYEEKKLRISRLANKESSRNEELLTETTTPSPAVKASPASTKLSVSENDRLSIPEITKDNLTLTEIIAKLREMKEPIRLFGESEEATIQRYYSLLKYKKLEEIENELLTKGVETIDFEHATTTKPKVSKQVVAFLQHGIRIWDNFLSSKSINSFESSESQMQLKIFRQAKQDLDVLIQLIVDEALNDDIFKSIAEICYRCQKHEFVKANDMYLRLTIGNAPWPIGVTMVGIHERSAHQRLQANPSSNILKDEKKRKCLQALKRFITFQERESSNLPEYTD O94410 MU163_SCHPO SPCC1620.03; CHAIN 1..186; /note="Meiotically up-regulated gene 163 protein"; /id="PRO_0000278513" MPFMNFRNFNFMPLLRPLNPVYKGAEHLCRKNIHNQVYNVETGKTIQILQDLVPLVLYRALPDAILDHHVELVIFPNSLNFPRIEGLTIYKFIFKTARLLLSSTYGSSAKRPIDIIHQLHSSMENKNVRYSMKCNWIASPNDEYTWVFHFDIDKKGIIYRHIIDNLERNRSRQCEKISALKPDPIE O94420 YQGD_SCHPO ACT_SITE 61; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250|UniProtKB:P62707"; ACT_SITE 135; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P62707" SPCC1620.13; CHAIN 1..282; /note="Probable phosphatase C1620.13"; /id="PRO_0000318492" MPLNVTVEEETLQIVEEEPQQEITNTILEEDFNLLDNSFQTDISSTSSQNDSKFTCLLVRHAESEHNVRGIRAGARIDSELTVHGYNQAKKLAKSIRNLDIVCVYSSPQKRAKRTAEEITKVANCPLYISDFLMEKDLGSLEGTSFRYTANYRPREPPMKVTNLESRDSLLTRARGFTDILFNEAIGFEGESGKTIVVVSHGIFLPFLLRAILARARTPLPSMIIPWNNASYCLITIDLGGNSIVKMNCNSHLRGIKRTRKLGSSTYDSKQKPITEFCSKLN O94428 MU168_SCHPO SPBC660.09; CHAIN 1..115; /note="Meiotically up-regulated gene 168 protein"; /id="PRO_0000116775" MRMDGSDFEDRKVSKPSPVLPFDVSNIGDLSQGVHSPLGISHFDSKNPTPFGRSTKNSVYEYETVTPYSRFKVDKKFGSATSVSPVHTKAEEPGLGLTPMNSADFSNKIASRYRS O94432 YHKF_SCHPO SPBC660.15; CHAIN 1..474; /note="Uncharacterized RNA-binding protein C660.15"; /id="PRO_0000310812" MGGSDFEDDELFKDLYGEENEKKVESASGNQETSNVTPTKENEGYEELEKSGEAGAERTKENPFREEPGADFDRSGSDQQYSAEAEANQEDDLNETSQQAPDPSSYDIRGQALSSATWDNAEDGENSKNDNYNENQSALTGSGAMESNEDNAEETSPFNREDGKMFIGGLNWETTDDSLRDYFEQFGEVLDCTVMRDSTTGRSRGFGFLTFKNPKCVNEVMSKEHHLDGKIIDPKRAIPREEQEKTAKMFVGGVPGDCTEEEFRNFFNQFGRVLDATLMMDKDTGRPRGFGFVTYENESAVEATMSQPYITIHGKPVEVKRATPKASLRDSHDRHQHGYHGNANPYYAQNMNMYGGMTPAMMAQYYRQMQQYMEAMRNMPAAAGAVPYPQPVMPAGMADWQQQQQQGAAYFDPSKMNQGTGDGVPFSPSMPSGSSRGGYHGRNPGGPNRQRYRGRRDGRGGNTGGGHSFHPYRR O94435 MUG35_SCHPO MOD_RES 127; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 132; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22H12.01c; CHAIN 1..234; /note="Meiotically up-regulated gene 35 protein"; /id="PRO_0000116743" MTNERHDELACLGIFPLKNPKQLDGVVTPILQLRVKFLAPTDRWWEGLVINKDLSKEESEELWKFLQSFDPRSAKFVGRGTPEDHVISYLFEAGKYEFEVFFYQKDHSLKLMGLYDKTQKQLLRRDSSGDLTSTDKERDVSPVSHSEKPYWDRYDLDQPSNQDVEESRNLVQEPKHRSKKYDRLGLDELVMEQTASLWKICSRNGMSVDEFLRFIRMGLESNFQHSNQVIPTHF O94437 YFI3_SCHPO ACT_SITE 95; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q6DRD9"; ACT_SITE 190; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q6DRD9"; ACT_SITE 250; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q6DRD9" SPAC22H12.03; CHAIN 1..270; /note="Abhydrolase domain-containing protein C22H12.03"; /id="PRO_0000312657" MSLKPVKLAFEKYSATVAKHPPVLIFHGLLGSKRNWRSLAKKFSCKLDRDIYAIDQRCHGDSPCVAPLSYSAMALDAFQFMKDHKLDKASIIGHSMGAKTAMVTALKWPDKVEKLVVVDNSPWYQDLPRDYGAYFRKMIQIDEANITKYSEADKMMSTVEKDILVRSFLLSNLKKDSNNSNTFKFRVPIELISKSLKTIEGFPASLNDLVYDSPTLVIRALKAPFIPDSALPVFKKFFPKYELVSLDCGHWVHFEKPKEFSESIINFLNN O94455 YFFE_SCHPO SPAC1687.14c; CHAIN 1..76; /note="Uncharacterized calcium-binding protein C1687.14c"; /id="PRO_0000310331" MSVSTKRLEMDEEAEEAFDLFDVTHKGYIDFEDLRRSCAQLGENLTKEQLQLMLDLAGTNGKVSREEFAELWIHIS O94458 YFFH_SCHPO SPAC1687.17c; CHAIN 1..190; /note="Uncharacterized derlin-like protein C1687.17c"; /id="PRO_0000351083" MAILPEFISQTPPVTRYIVLGTLFTTLAVNFGYVSDLKIFFNWKLFLAKGEYWRAITTFLYVGPFGLELILYLSFLLRFMSMLERSSPPPQTQSFLKTVLIVWFSLLVTSYFSYMPFAASYFSFTMLYIWSWKHPLYRISILGLFDVKAPYVPWVMVLLRWLRTGIFPLLDLISALIGHVYFFVTDFSTV O94465 CMS1_SCHPO SPBC23G7.07c; CHAIN 1..277; /note="Protein cms1"; /id="PRO_0000350819" MSYTTTDADALDDQLDYQVDLVSEISVSDEESAQPTTITENFTASQNNDSAKREKRKKQRQKQKERKRAKLLELQDTNASIIQSPDTLSDLLNNYIKSIYSDLTDVELSDKVIKASYIEDTISFSKPKTVDNYPEYIQHLPGFTKKVVQNSNPEILVLCISALRAIDVLKPTKSLQNKNFKVAKLFGKHIRLEEHINYCKANKIGVGIGTTPRIAQLTNECFTCENLKYIILDYSFRDIKNNSILTSKESRKAVIDFLTSKTILENMAERKTKICFY O94469 DUR31_SCHPO SPBC23G7.13c; CHAIN 1..664; /note="Probable urea active transporter 1"; /id="PRO_0000314766" MVQPELTQSVGYGIVVGLGLGFAALMIFVSWSLKKFNNENQTSEHFNTASHSVRTGLVASAVVSSWTWASTLLTSAQKTYQYGVSGAFWYASGACVQILLFTVLAIELKRKAPNAHTFLEVVRARCGPIAHGVFLVFAYITNILVMAMLLCGGSATISSVTGMNTVAVCFLLPVGVIIYTMFGGIKATFLTDYIHTVIILVILIMFSLATYSADKKIGSPGKLYDMLKEAGDAHPVAGNAQGSYLTMRSQEGAIFFIINLAGNFGTVFVDNGYWQKAIAANPASALPGYILGGLAWFAIPWLAATTMGLVALGLENKPYFPTYPNRMSDLEVSEGLVLPYAAIALMGRAGANATLLLVFMAVTSAASAELIAVSSIFTYDIYKQYVRPRATGKELLYTGHASLIVFGFAMSGFATGLYYGQVSMGYLYLLMGVLVCPAVVPATCVMLFSRVSTIAVTVSPVLGIISSIITWLVVARAEGGKTLTIETTGANNPMLAGNVVGLLSPALYILILSIIFPEKYDFNRLLATFAMHFSSEEDEIQQTKKLNRASVISKVAALIITAAFIILWPWPMYGTGYIFSKRFFTGWVVVGLIWIFFTVFAVGIFPLWEGRNDIYQVVSNMAASIFGRKVNDIVEDEGVVVETISIGSGSKEKVNFEKKDIESV O94472 PBN1_SCHPO SPCC1919.02; CHAIN 1..332; /note="Protein pbn1"; /id="PRO_0000246308" CARBOHYD 36; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 56; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 112; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 206; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MDLQRTNQDTGTTTLFKVVISNTVNYLPKGVWILRNNTIDSLSIAKQFREIKNNINISHLSRENYWVETPFGKVFHSEVVSEEFMQIFIDKGNKALNNEEMIFACMSEKGWNVSLETVPNLDIPVGSYETQLGLPVGLHPKLHVHLKNLHKPEDECSLQGFMYIPPTLFIDRYELSNIAEMHADNLGHVLGIWGETDLEAPSYKLNGTGSFFWFDIYTDDGLLQKDYIDTIIPLHTRYQSPLKGQTYLKTSLTNPKFFWNCDTEDKVNDFRFLFSSKNKYTLQNDPTTLSISIPIADLSYKHVVEWVTNGVAIFSFFYLLLYLWKRFRYAKD O94474 SKI3_SCHPO SPCC1919.05; CHAIN 1..1389; /note="Superkiller protein 3"; /id="PRO_0000311765" MAKPALKAAKEALVVKNYELAIEQSKKALSFDANNYNANVFLGVAYFSTKQLSESKEAYLDAIKIDEKAVLAWQGLWNLYESTHDISELHKITPILASKFLELEEQNKCLNTVNKYMEVVKKYGNKADEFKALKLLTPEEGEIYEYLEGRVLPLQTVYMQMVDIQESMDRCYFESEVNKRKTRLGARLEQVMRDVELEIYKDSPLETLYNQIINYAETDEIRRLTESKLLHMYNKLLILSEIKEKSHWRERIWDLIQGMVTLHIPEQAAWTIYFEWQDHSDISFFQSAELQEYIELFPGSPLAQALFAFRNSDLWHKEHPIQLEDSNNSAELAKETKEEDDSENSVDKKENEEDIISSTMMPQDEVLANLTEAYENAPQSTIISECLAKYYIHLKEYEYAIGLSKAALEVLKRLQQDTGVKLDKLTRIFQLCLAIGYSHYEVPRYLFQAMHYYDILLAADPRNYHALLGKGLVQIENEQYSDAVKTLGLLLDDHENDPSLSELSWCYFKTGNLPKAISTVEKCLDVLLSMDVERFKIAEAYYRYGIYILNRKSENYLEDSFSAFVSSLRKDPNYAPAYTSLGLYYRDIHDMVRATKCFQKAFELDASQVEAAEALAKTFAEANEWELVEVISRRVLNTSENDLKRKKKFNWHHTSLGVLELNAKNFHKAIVHFQSALRISPKDTNAWSGLGEAYARSGRYVSALKAFNRASILDPDDWYVKYFIATLEKDMGEYEVAVSTLSEILAVRSKELCVQVSLAETYVRLAKLYHARGFYSRAADSLEKSIQICCNVLKEDITSIFSWEILGDACLSFCQLKNYHNRFPNSLISDILFTTEAMKCANNGRQFENMIYLPDLETSSGAIFIAAVAITCFTIHLSLVADDKLLLPVSWYNLGSSYYRFYECDTTKDATLQVAINCIKQAIKLEAKNYVFWNMLGVLFSQTKAVRSAQHCYIQSLLLNERSSGVWANYGALCIQNHDVECANAAFTRSISIDPDNSQAWLGKAYCSIAVGSIRKAVQIIHHAFEISSGKMPDVNYWYADTMLHAVNTEDFVTTDGDIWSATYAIKRYLGENPTDTFAYYIKASLLEHLGETTDSVPSAIRLCELLEQEYDVSESPVILKRFIDAKALLGRLYLAKKSFENSVEQAGIALDLLEGEEDEDIKRTTLGLNLTCGTASFFLNKLEKSLDCFEKALLVSDSNADVVVLVSKVLWALGSENGKQAAREQLFEALEQSPSHIGSLLCLGAIAIYDEDDAVCSAIEDSIAHLKKDEVLRSGALKQVQIMEVLLTKKIDESMIKSLLQRFLHVYPFAASSWTLLTNRYASKSLANAFATTLYTHPSRPDDLAQSYRLQNSIDRAQVAIHLVPWDSANWKALHGVTHEALVSSDAS O94475 YC67_SCHPO SPCC1919.07; CHAIN 1..206; /note="Uncharacterized protein C1919.07"; /id="PRO_0000304002" MVVQDKWKRKATLAYKKKHDIHDAPVKPRKKNLGNNEWRFKNAGEYFDEDNNEEEYPSLESLKTVGNGDTIQDEEEDFEYSKLQARPLTGLGISNQKPKSKVRTIQREEVADMLESVEHEKSIQEFRKRYNVQKPKVNISHAEAEEDIDSFLESMDQSAPPSITEDKGENYISSNHSSMHISRNDSRNYMSEKPNKDQSWLDELLR O94490 YC79_SCHPO SPCC417.09c; CHAIN 1..767; /note="Uncharacterized transcriptional regulatory protein C417.09c"; /id="PRO_0000310376" MHARMQPHEDRSRSGMSRSEAMELEDQLEEEERGGNVVVGSSSANANASTAETGKKSAGGSKPKRRRGERIPPSKRIRKAIAYVNKYASGCFGRVERRLVCTRSISRHSNQKLLDFCVECKKHKIKCVGNFPCGRCLKKGLECVIETPPRLLMNKDEISLNLQRLSHMETILSKLMPSMSLDLPSLEAKIAELSESLQTYPDKVLTDIELGSYQQVTLNETQTYYEDAGSNESFVARVHEIICQGREFQVQHKLTNKGNKTFEDILDPADNTVASLIHALPPKDITFYLLMTFWQFSSDNNHFYYNTKLFAAKVHHLFDDPTSFQSKDGGFVCMLLLSMAMGSLFSYIRHPEFLSDENHDRWTYPGSQFYQNAKLLFPKVISESSLETVQSFFLAGMYLSPTLAHEVVYMYFGIAMRAAVANGMHKKSANAQFSGDVAELRKRLFWSVYCMERKIGISLGRPESLVRSEIDIHFPEYRESLDSQNFIASFRTFTLAIKISLLTNKVYDMWYSSLHGKANLKAATIKEIVNEIEAWRQQLSPDLEIQNIGPDSRSYRGIVHLHLAYHIVRIAMGRPFLLHRLRERTMNSKTDEGARLLTDKLISYCYSSALHIVDLLVLLRMHKFLSVYSFMDYHSCHAASFIILVHLLINPSEQTIEQLNTAIDILNFVTDRFPLLKGSTDVITNLRAFAEQSEVYQSRLNATEPAYSTQVPFFPRDADYHNQINLQNLWNDENINASLEALFNDAKGFGFLLPADNFIFPSDDGDM O94492 YC7B_SCHPO COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305}; MOD_RES 273; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPCC417.11c; CHAIN 1..438; /note="Uncharacterized aminotransferase C417.11c"; /id="PRO_0000358866" MRNMVSEISDLSLAKEKSEAQFIARNPKSNDFHCKACDSLPGGNTRTVLHGAPFPIFIEAGYGSKLRDVDGHEYTDFLNELTAGIYGHSNPVIKKALMQGFDEIGISLGGTTTCELNYAEALKSRFLSIEKIRFCNSGTEANITAIIAARKFTGKRAVIAMHGGYHGGPLSFAHGISPYNMDSQDFILCEYNNSTQFKELVNSSQDIAAVIVEAMQGAGGAIPADKEFMQTIQLECEKNDIVFILDEVMTSRLSPGGLQQIYCLKPDLTTLGKYLGGGLPFGAFGGRADIMSCFDPRLPGSLSHSGTFNNDTLTLTAGYVGLTELYTPEAVKRLNALGDGLRKDIESYCHNTKMSITGLGSIMNIHFTESGRVNSYNDTAGEVIELKDLLWMDLLKEGFWIARRGMITLSLVLTESELEAFKLTIKAWIHRRMSLIRI O94493 YC7C_SCHPO ACT_SITE 216; /note="Acyl-ester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10039" SPCC417.12; CHAIN 1..539; /note="Uncharacterized esterase/lipase C417.12"; /id="PRO_0000310361" MYESPIILGSKPCTLNIPGMGVLHGLTVLDENGKEKCHRFTGIRYAKPPVGKLRWRRPVTLEDGYDYSGDYNQFKTICPQPFYNNRKNQVRNPDFKYDEDCLFLNIWVPAGEKPAEGWPVLYFIHGGWLQVGNPLHYRQCDPQDLQADGSPAKFILVSPGHRLNLFGFLAGKELLEEDPKSSNFGFWDQRLGLEWTYKHIESFGGNKENIAVGGISAGSYSALFQLIYETYHPEANQIIKRALLLSNGLSVQPKSVEESQIQFNELAQKFGIPLELSSAEKLEKLRAIPFQDLADNILNLRLHTFRAVTDGDFVNPNTFKDIYDGTFGKRIRDSGRELIIGEVNNEHSIYANTNPPKSKEDLFNQVNNYYPEKVTKALLELYPKVPDMEDEKEYLAAIKALFGSIVSDMQVYASTRVLINGLVKGGVPLEKIYRYRIAFRGKFFDKYEPPESLVPHAGDLGLWFYNVVDGILPEEIPIYKAWLKSYGEWMSTGKTDWGTTKTEEYRLLDADGTIKVVDDEKWDWGLKVGRTVAGVFGLN O94497 YBS7_SCHPO MOD_RES 149; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 152; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 275; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 276; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 297; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 514; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 516; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC18E5.07; CHAIN 1..615; /note="Uncharacterized serine-rich protein C18E5.07"; /id="PRO_0000116521" MSETSSNSPASGSKEAVPKSLAGSTSNIPNELFVGPDGRPLSQNAQGASKSSSKVVPQALVPEDDIRAVEGILNYGGSNDNRPVSHTHTFVELQKSHQNHLTENDRNFGTSRLDDVAPNADGVRRLRTSGSSTGLSNAPPSANVSKASSNLSLASLAKTQPERATPEVCVPLNPDTGSVPLIHPEQTDRGLPYAPDEKFHNSGSLKLPKGASLEDLSRSPSRAVLNEDGNVDECAPPEPWENEYNEVLDDVENAVVGTSPLEYTSKPLAANRQRSTADLTESDNICGLTAGKSDPVTDVDESQTIDEQSIPEAEKGFYTKDGEGTAGLPFDIVSNLDIPNENAHESSRSKKKHTGPSLSSASQPSAASSSSSSEPSNLDKINDVKKNIEVSANEPQPRPVKEDVPKSQVGGETDTTDVINNSTPKEETEESPSTELPETGKEQPPNKAEPAVPTEASSTKPSEAAEESTPRFSVRPNKFTGSRAGFVAALESRLQKGPLMRSFVPNKSKSPSGTKSPASGETSEAGVKETETTTSSESALPDARKSRARGPVRRPPTSVNTKPSFSVSGIDVFLNLPQSSVMKKKGVETRKEVEPKEEAVIPEEDVEVEVETEEQ O94498 YBS8_SCHPO SPBC18E5.08; CHAIN 1..186; /note="Uncharacterized N-acetyltransferase C18E5.08"; /id="PRO_0000310293" MSKIILKTSRFLLKSPVEEDDFDQITKIKSDPLVSNTQLYGKVESRELCRFMFQHYITDARITKTRRKRWVFGIYPLEVSSTFPSICYIGNVGLSKKNVKSDTANLFFEIGPLYWGMGIATECVGRVIEFGSENNIQNFIIDPIIGNEASKKVALKLGFEDSGTFVTAYNGLQQHIYKLSKQIRTG O94500 NDUV1_SCHPO BINDING 80..89; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000255"; BINDING 198..245; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255"; BINDING 377; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255"; BINDING 380; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255"; BINDING 383; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255"; BINDING 424; /ligand="[4Fe-4S] cluster"; /ligand_id="ChEBI:CHEBI:49883"; /evidence="ECO:0000255" COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255}; Note=Binds 1 FMN. {ECO:0000255}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255}; TRANSIT 1..25; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC18E5.10; CHAIN 26..452; /note="NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial"; /id="PRO_0000317309" MLSRGHCCKLKHSFNGLRNVALKRLVGSKAGYRMFPNLIEKRIRRIDDALADGEYENLSEILKYDPLNIIELVQESELRGRGRYGFPTGEKMLSLYKATSSERGRKEKPVVIVNAAENDIGSFKDRLLLRHEPHKIIEGAIIAARAVEASACYLFIRKDYYEETVMMQKCIIQAYAKKLLGKNLLGTSIGLELLIHPGAGSYITGEESALIQSLQGEFPVPDIPINNTITSGLFGLPTLVLNVETVSNLPAIIKKGPKFFISMGRPNNRGTKLFSISGEVNEPNVIEACMSIPLKDLIENYAGGVRGGWNKLVGIFPGGPCSGILNKNQCEQVTMDFDSLKALDSSLGTGSVIVLNDHDQIFESLLNFAKFYSTNTCHTCPVCRDGVEDVIETLKGLKDGHAHLSQLKDMFSKFNMPSSSKVFCGFGDSMRHQIHSIQRNFPDQITFRTKVT O94502 YBT5_SCHPO SPBC12D12.05c; CHAIN 1..426; /note="Uncharacterized mitochondrial carrier C12D12.05c"; /id="PRO_0000310791" MPTELSDITIQSVLPCDYSLFKNNLRVSRLPESRFVFSPKEEINCQSLLQGPELKTALDNLNFIHKQKFEHQFRHGYWKLHPHPHHQHDSIIPASWIHDTPHMKLVFHRLQNLPDGDLLLENDPKNNVGYFISGGIAGIVSRTCTAPLDRLKVMLISDTGSKPSPKYPFATLLHTTKVLWNRNGIRSFFVGNGINVLKVMPESSIKFGTYEAMKRVLGISSSSENHSPLYSYLAGGMAGSVAQMFIYPVDTLKFRIQCSDLSRGQHGKSIILSNAKELYKSVGIRGYYRGVLVGILGMFPYSATDLGTFEGLKRTWIGILASRDNVDPQDVKLPNGLVMAFGALSGSTGATIVFPLNVIRTRLQTQGTSAHPATYDGFIDCFYKTTKNEGFRGLYKGLSPNLLKVAPSVAISYLVYENCKKWLGLE O94516 PEX16_SCHPO MOD_RES 200; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC646.15c; CHAIN 1..364; /note="Peroxisomal membrane protein PEX16"; /id="PRO_0000374020" MKPLAYYEDQLLKDEKSFLKVTEIERLLSYAAYLLPAEFRDDQLKSQTITSILLLLHQFHTGLLFRKIAELPKTEQAILKSERTQYLEYFRKKNPSFEKVSELLYFLNISTFPIELVISKYNPSRQYDSVLFLESVKFLLRVHIMWTTGGDLPLSNPVLQRDFNVKTFIHLHKKYSNSGSAVVLKNSKKVVPRLNTVNSSLDFLQNRTPRLSSILPDEIFTKRLPNLRIFSNFIKVCRPLIYMLFMWHWKRKQKSSSLKVRPWGPWIVAFVFEVISQLIDRRCESATSSRQGFGLERRTNQSQFQHFVVWAFTQGRFYDEFTKHWINRSLSWVNSIPVFGKYLLLSVEERQKSLENYISSVRNY O94517 PSA1_SCHPO SPBC646.16; CHAIN 1..244; /note="Probable proteasome subunit alpha type-1"; /id="PRO_0000124140" MSQARGFDRTITVFSPEGRLYQVEYAFKAFNNAGITSVGVTGKNCACVISQKKVPDKLIDASTVKHVFPITKGIGCVMTGSIADARAQVSRARSEAAEFEYKNGYPMPCDVLAKRMANIAQVSTQRAAMRPLGVAMTLVAVDDEIGPSLFKLDPAGFYIGYKATSAGPKQTETINWLEKRFKKDGIPSNLTDTVETGIQALMSSLSTDFKSTELQIGVVEDDKPFRVLSVEEIEAHLQSIAEKD O94520 YQ13_SCHPO SPCC1281.03c; CHAIN 1..193; /note="ER membrane protein complex subunit 4"; /id="PRO_0000340089" MHINEETDWIDLVKPALAKKPKKIVDNSDKFPTPRGFQQKSLVSKNIHSGNSASSTSIFAKREEELQKDLLLKKAWELAYSPLKQIPMNAILAYMSGNSLQIFSIMTTLMLLVNPLKAITSTGSAFTPFKGTHPGTLWPAMGAYILFQLLLMGIGVYKLQRMGLLPTTTSDWLAWEVSKVFMDRSYGPSKTVL O94521 PLR2_SCHPO ACT_SITE 52; /note="Proton donor"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal; Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65; SPCC1281.04; CHAIN 1..333; /note="Probable pyridoxal reductase 2"; /id="PRO_0000310315" MPIVNGFKVGPIGLGLMGLTWRPKQTPIKQAFELMNYALSQGSNYWNAGEFYGINPPTANLDLLADYFEKYPKNADKVFLSVKGGTDFKTLAPHGDPESVTKSVKNALTRLRGKKKLDLFQCARVDHKVPIETTMKALKAFVDSGEISCVGLSEASAESIKRALAIVPIAAVETEYSLFSRDIEKNGILDTCTQLSIPIIAYAPFCHGLLTGRVKTAEDLKDFIKAFPFLRNMDKFNPKVFEKNIPFLKAVEQLAQKFGMSMPEFALNFIIANGKGMIIPIPGSTTVQRAESNLSALKKSLSSEQLEEAKKVLDKHQIFGLRYNKQLESTLSI O94525 YBU1_SCHPO SPBC609.01; CHAIN 1..1157; /note="Uncharacterized ribonuclease C609.01"; /id="PRO_0000314758" MDPHWKRHDSSNIPTQPSPSASPKSNKPSSAQRFGNLPWVAPDVIQSQIEYLQALQMQQSLSESENYLQPNFFPFQSGPFSKSRRENTLLPRLNPLAPIGARQPNPSIPQQFSKPINESGTGTMGPAVGELTSPVMKNRAESIFSPVTESFEAFTQGMQTTPQRAGAGVSTATSHTRRRSSAGTDPFSPVSPSNPNFLTPLKPIDGNQEWQQSPLESPLSMHSLQESLHSVEPESPIFQQAPQIPLSNASQQSYINHSSDGASLPQSSFLNFNSSGKRVSVSAAAQQHKNLFLPYLPQASLPKFIGTGKLLVGTLHINRKNRSDAYVITDVLDEPIFICGSKDRNRTLEGDLVAVELLDVNEIMQTKREKEEKKIRRNLSLSGSSKYSVNSKAKMMSISTPMALGMNRGVLSFERSIEKRKNDYEVTGQSLSFVDDVSLTPDSAPKYAGHVVAVLNRPSGETCSGTLALYRPNSLALKNQSSHRRNSSTSSGETGKGPKIVWFKPSDKRIPLIAISSDQVPPTFFTNNDDFKDKVFLAGIKRWPTTSLHPFGTLYESIGTIGDPKVEYKAILHDFSCHTYDFPESLSHCVKRLPTPIPAEELQKRYNLRDKLTFMIGTRDYALHIDTGSIDGVITLGIHVADVAYYVKQDMPLDDEAANRVSEVQLLQGSVPFLPKKVSEEISLIEGHDCLTISIVVQLDLKSGAVLQCSLGPSVIHPSSFISLESAQANLQTNEALQLVDASAHVLTKLRLKTDKKLDLQSLYCFEFCDGQIPNIQNINMSIFEAFPIACSLQQIEHWVNEKVASHLMSVFPSKVILRKNQRPSDFASLVAVSELTGVNLSASSTPSEIMTEIATTKDKRTKMLLQLTLRRMCNESEYTIGTSNAKDVSHFVFSCPYYTHFCHPTRRYIDICVQRQLREAFDGRPDFSKDYRSLLSITQSCNTLSNFYRNAQEKSLHAYLCQLLHSINLRSGLVKHKAFVLAVDQEYIDIVIYEFGLERRISLDLLPLSNCDFNEQKHELYLSWRTNASFFYASSSLEIDTPCFNDFKKKFLDSNGMCKQICDMMDAQVRDLANAAESQESFYSKARGNDSTSKTAKSSSGNQDISGDGKLHSLRMKEPEVVQTIRPGQEVSVLIFADTSATYSLSLITLQSPLSS O94528 CAF5_SCHPO SPBC609.04; CHAIN 1..531; /note="Caffeine resistance protein 5"; /id="PRO_0000173432" MGFLRETVFGELVEYVSHNSNDNDLEKLRVWKDISKVDSNDSCSSESGDLKIHEVNSEGHIIVRWDDANDPENPLNWPLWAKLVVTFDICFLTFAVYVGSAIFTPGISEMQETMHVGTVPVVLGLTLFVLGYAIGPLILSPLSEIPQVGRQKIYVLSLLVFVCLQIPTALGSSLGVLLPMRFLAGFFGSPALATGGATLADIWQPWLLPYFMCFWAIGAIGGPVLGPLLGGAMVVAESWRWQFWLLMMISGFALIVIFFFMPETSEWHILYKRAKRFRKITGNENYRTEAELASSHLSVAQLAKETIIRPIILSISEPIVLSLNIYIGLIYSILYLWFEAFPILFTSVYHFTIIENGLVYLGILVGALITLACYFVFLYKVMIPAFMASGGDFAPEGVLVISFPATFFIPICLFWFGWSGRESVHWIVPIVSTLFYASGAFLMFQSMFQYLAASYPKYVASVFAGNDLFRSAMAASFPLFARAMFNNTGPSYAPVAWGSTILGIVACLMIPIPFVLHKWGLKLRSRSKYAS O94535 YCA8_SCHPO SPCC895.08c; CHAIN 1..490; /note="Uncharacterized protein C895.08c"; /id="PRO_0000343154" MDNSRDKIHILGAVSDTFQEVQHPCSILKYKVYFVTTDTFYCKYLTASFTGLKKFPTERQLPLECHFNHIDWDLGNNFKVKEGVFYTFDIIAPLPRCTPRTIVTQEGSISYKLTVKLYTEDDCRMPKSANVPVVVPFTLNPDRIPESQHIRYGAPLNDACFTSLSMKSSKYSFLTAFFKYPQQCYKGPGCVCPLLIDLESEDADVLSSTPGSAGTDDPHIDPIAINSQDSQFIFQDRLPRLSNDCDMKGRSSLSRTSSPVVEKKLKRYYIRVLLVQSITFFLFNDAFRNSITVLFEDGKWSPPIVPGLHSRVEFTIPVNDLIHGSCTENPHLLVRHSIYVSIHSREPSSLSRKLAPPFLRTHKAKSNSLFSMKRPSSSSSSLSGSWHGDTENSVKQSLASPSEASLPNLSKYSRKNAKKLNEWLDSLDFKLPIYLFHRKLESELSHLPPYSPYRDSYFYLEDDDGDADTPSTASLDYFSNISPPDFLNKA O94539 PAM17_SCHPO TRANSIT 1..26; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC167.04; CHAIN 27..209; /note="Presequence translocated-associated motor subunit pam17, mitochondrial"; /id="PRO_0000043159" MKYTFSNKQGFVMIPIIRPGLVVKRLQSPKIFLTLWKTCYNVKTYSTESIKQKKPQDLNWPTFLKLRKSRRIFETLTSIPTALTGLGLGSAYFLTRTVDPTMTIMGLDLFTLYVIGTIASGGLGWLLGPSIGRKIWTLLHKSQARQIAAREQEFYRHLVKNRVTPQMESYSNPIPDYYGEKIYSLSDYRRWLRDQKAYIQRAFWRTSNR O94546 MU150_SCHPO SPCC1322.07c; CHAIN 1..104; /note="Meiotically up-regulated gene 150 protein"; /id="PRO_0000278508" MASLFIIMDKRFAVFASSDKPNNCSRKNMFFLKNIIVLSNYLYLLYKAWIVCTTISLCCDFPLFNFLFIAIPYFTEILYNDSSLLWFLFVSLCFITLSFQSLEI O94548 MTC1_SCHPO SPCC1322.09; CHAIN 1..455; /note="Maintenance of telomere capping protein 1"; /id="PRO_0000343155" MAETKEQTDDVETLMASLDQLGMEADPTSKEFNNDDSKIGAPSEVQDEKELLEFLDQLENDEEKNEKNPIEEANEENESVAATSNERQQHDASNQPSQAAQTTINKNTESATPKTVNEINKSQEFQEHVETPKQSNWLGGFWSTASAAVRSAEQRVRSIKGFEENANWDINVRNMVDLNKLGDLSNGIRSKALPTLSNTIHNVLNVVAPPIHDHEVLQVTVFHDLAGFAHLDRIVYESFEKVMFQVEGGELTVLLDKEAKVRPRTNDVYEDFGLCNGYLEAKKLAKANLAEPITEAKKMNKENKQENVGAGDDEDASESPMVRVTHLLLVIQAFTIKNKEVSDDEQLCFLIHLNDTNHNLEFSTTSQPLPLEWQRWAVDPRYIKLFGSNAILPNEWVTEWVEQSISVAAGIVAQMYTSKRMALGDPSLFAGLPEEDVNTGSSETPVPYYDGAMYA O94549 YCDA_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPCC1322.10; PROPEP 243..262; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000343215" CHAIN 21..242; /note="UPF0619 GPI-anchored membrane protein C1322.10"; /id="PRO_0000343214" CARBOHYD 207; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 227; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" LIPID 242; /note="GPI-like-anchor amidated asparagine"; /evidence="ECO:0000255" MLARVGTTLFFLANALAAYAVSVTSPTRDTTWQSGQVNTVTWSSVSTDPEEMVIMLVNNAHYPNQNFNLGTVQSSAGSLDTDISISSDLPTDGWQIYFNGATSQNQGSLAQSEQFDFEGSDSTLAASTISGGIYSSTSASSTSSSTATPSSSSTTSSSSSSSSSTPISSSITSSISSSASSSVSSSSASSSGSISSADAKTVSASSNSTISGFSTSTTSASSSAAGNSSSSSYTSYSGAVSNGVAQLSVAACMGIAALMLIA O94550 PHB2_SCHPO SPCC1322.16; CHAIN 1..288; /note="Prohibitin-2"; /id="PRO_0000316249" MNRQRPFQQMNDLMKRGLPKGKYAFTGTGLLLALGLAGFAVQTSLFNVDGGHRAIKYSRIGGIKNLIYPEGTHFLIPWIETAIDYDVRAKPRNISSLTGTKDLQMVNINCRVLSRPDVHALPKIYRTLGGDYDERVLPSIVNEVLKSVVAQFNASQLITQRERVSRLVRENLMKRAARFNILLDDVSLTHVQFSPEFTAAVEAKQIAQQDAQRATFYVDRARMEKQGFIVRAQGEGRAAQLIGEAIKNKPGFIELRKLETAREIANILSKSNNKVMLNASTLLLDDIK O94562 YGD3_SCHPO MOD_RES 285; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000255" SPBC1773.03c; CHAIN 1..459; /note="Uncharacterized aminotransferase C1771.03c"; /id="PRO_0000358868" MTETVTTTSSDKSEKKNYLFYTSPNHRPPTVVRAEGVYLYLEDGTRIMDATGGAAVACLGHGNKEVIDAMHKQSEKVCYIHSMGFSNEPADKLANLLVSEHPDVFARAYFANSGSEAVETCLKLILQYWQLVGEKQRCHIIARKQGYHGNTLFALSVGGMKPRKQPYEGVFSHTTSHVSPCFEYRYKENGETTEEYVARLAKELEDEILRVGPEKVAAFVAETVSGACTGCATPVPGYFKAMRKVCDKYGVIFYLDEVMSGIGRTGTMHAWEQEGVTPDIQSIAKCLGGGYQPISGALVGHRIMNVFEQKDAAMAGFFTYQAHPIACSAALAVQTILRRDHLVERAAEMGKYLSEKLHETFDSHPNVGNIRGRGLFWGLEIVKDKATKECFPPEYKVGSLANKIGCEHGVFVYPGMGTIDGTRGDHVLLAPPYIITREQIDELVEALSKTITSTVAALP O94563 YGD4_SCHPO BINDING 38; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:A0A059TC02"; BINDING 167; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:A0A059TC02" SIGNAL 1..21; /evidence="ECO:0000255" MOD_RES 153; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1773.04; CHAIN 22..336; /note="Putative uncharacterized oxidoreductase C1773.04"; /id="PRO_0000316222" MSELVLITGITGFVASHSAEALLSQGYRVRGTYRFQEKLDGLLKNRPEWEKKVEFVQVPDCRAPNAYVEAAKGVDYVIHAATEVHSNLEPPRKDPHELLHIAIQGCENALIAAAQEPKVKRFVYISSEAALKGPVNYFGDGHVFTEKDWNPKTLREAEESDDELLNYTVCKKLGERAMHAFVARNTPRFQAIALNPPLILGPVFHLQSVDNLNFSTWFFWQLIKGRYEVAPESKFFNYVDVRDLAEAQVKALTAKTDKDRFVISGGAFKNDDIVNVALKYFPQFKDKIAKPNGETSPCNYEVDASLSIKELGLTYRPAEETFKDATESLYKLAGLL O94564 YGD6_SCHPO SPBC1773.06c; CHAIN 1..346; /note="Zinc-type alcohol dehydrogenase-like protein C1773.06c"; /id="PRO_0000339117" MALRYVVHDEISGFDQLKPEEYEVPQKLNPGEVLVKLKAASLNYRDLIITKGLYPLPLQLPVVPGSDGAGIIEKVGEDVEGFEKGDSVVCNFFTNYLDGTPTDFATHSALGGTRDGCFQKYAVLPAHALVHAPKNLSFEEIATLPCAAVTAWNGLFGSKEHQVKPGNNVLVLGTGGVSTFALQFALAAGANVTVTSSSDEKLEFAKKLGATHTINYKKTPQWASPALKMTNGVGYHHVIEVGGEKTLPQSIACLAKDGMISMIGFVASEGTTPNLTSIIGQILNRNANIRGIFVGSVSMFRDMVACIEAKDIHPVVDKVFPFDQLKEAYEYQWSQAHIGKVVLKID O94572 YGDF_SCHPO SPBC1773.15; CHAIN 1..497; /note="Uncharacterized transporter C1773.15"; /id="PRO_0000372784" MEKTEEENYSIKELGEKGSDSQEDVAVIFAEKHPIIDKSLNRKLKLKTDLWVMPLLCLISAFQYMDKSTSNYSSIMGIRTDLNMVGNQYNWVGTSFYLGFMVFSLPLSTLLQKFPLSKVTSAFIVAWGILMTLTCLVHSYASYIATRTLLGILESVITPAFVLFIAQWYRKEEQFFRMAFLVAWNGLGGLIGGSMSYGLYKRELENNLTMSPWRILFIITGLITIINGVFIFIHIPDEPSKAWFLSEKEKDLVLKRLDTDHAGLGSKKFKKYQILEACRDVRMYLYFFLQIAVAIPNGGLSNFSSIMLKNLGYVKGKALLMNMPTSSISFAALTLFGLIPEFTNRRMDIALVGLAINLTSGSLIAFAKPTHAQLAGYWLFGISPIPYICILSCISSNSAGHTKKVFMSAVSMIGYCVGNMVGPQTFRSTQAPKYQGAKVSFVVCYCVAIFIIIAIYAVNVRENRRRDEKNEYLSNELSEEDKKDLTDFENPEFRYSI O94573 YGDG_SCHPO SPBC1773.16c; CHAIN 1..595; /note="Uncharacterized transcriptional regulatory protein C1773.16c"; /id="PRO_0000310382" MKRIRNACELCRRKKLRCNGELTCQNCMVYGEECRYVKRVKHDNRAAVQENERYPILYTPLSTSDHDNDEENEINELKNAVKALDKRFDNFELKLEALFSLLRSQQDSERKVKPGGFPSLVSQILSAGALVDSKLQAYTMRTNFFSNGFSSNDLFPHSFPTWKSAFRDVPDKDWAKTCLDWYFRFINCNWPIFYKKQYMESFEKLYIDKNLVKGAWIVSFYAILALAVSRDKRVDNSKLAESFFATSWFLIQRPGFFLTPQLEKIQALVIMIQFASHLSLYNLCKKLCGQVCLMVKDLNLHKESTDKDLDQDMAELHRRIFWVCYIFETTTSLIFGTPPVLGDLEIECKYPDINYAHCFAENVQGDLIFTCEISLTVLKHEIRTKLYNSNNVFLDKGQKGVISNIQTKILNFERAIPSEMKHYFEILKAGNGLPEELDIIKQHFFTACVEIYLSYCNTLIYLYLADDSIEGSKICLSTARAAIDVIKGFLVVLDPISKNICYLWLFLYCPFTPFLTVFSHLLEDDDLDADICVKDVDRLYSIHAFFLKMKDISGEFAERLSVITENFIQSAEQYLALQNTSVFGTFDALSESFSI O94574 YGDH_SCHPO ACT_SITE 251; /evidence="ECO:0000250"; ACT_SITE 280; /evidence="ECO:0000250"; ACT_SITE 298; /note="Proton donor"; /evidence="ECO:0000250" BINDING 169..170; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 249..251; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 275; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 298..301; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" SPBC1773.17c; CHAIN 1..340; /note="Putative 2-hydroxyacid dehydrogenase C1773.17c"; /id="PRO_0000076039" MKQSRTKRVLAIGELKFATNTLKRLSEKYHFEFIVPDPHDRSKTIEKIHEAASKSTFDACFWLFRNAAISPFTEEMLGPLLPTCKLFVTGAAGYNNVDVDWATRNGVYVANTPNGPTEGTANMNLMLFMCTLRGAREAEQSLRLGKWRQNLSLTDDPYGKRVGIIGMGAIGKSFAQKILPLGCEIVYHNRNRLEAEEEKRLGASFVSFDELLSSSDVISINCPLTPATHDLISTKEFEKMKDGVYIINTARGAIINEDAFIKAIKSGKVARAGLDVFLNEPTPNKFWLECDKVTIQPHCGVYTNFTVAKTEECVLASIETFLDTGIPTNPVNGPFGMNGC O94577 RMR1_SCHPO MOD_RES 328; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 330; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 331; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1442.04c; CHAIN 1..502; /note="Reduced meiotic recombination protein C1442.04c"; /id="PRO_0000350756" MAGVSPVVNHPYTTNSGDFIELGMEPAQKVQVDLDEAFNQMLHDGKVEEVVEAINGSPDLLSESDVENAKNNEHTYDIDNKNFNFEPKNSVNKTETIREELDQAASKILIETLDLHQKEGFEETIVTEEATDAVDLEAKGTTHGENDLDEVPTELNELANEVVDVDDVVSPSSELNAQSVNNILPISDDPKDSTSEAETRDFNWLSKGIVIFPNSSECAFYGNNNDEGMYLYSNGDDLNENTIEDFFGLVRARLESLNLLDSDSELLCEFPDLSLKINEDNVYASQIHLVDILEILTVHCDLEESFSIVFSTQPRFIARYNELVQAVSSSSNSEIDEVEDAETIDSKILEKRNDLNNEEPNSVVAEDGSEIITLDENDQSPNEATEKLRDNDLEESLIKDENLEDVEDENVKLDNYNIDGSLNNADLSQEPITNDGENVDWEATSEDVLERGYESAFPESEGTINSSKRRLSVTTDTENIELSDELASAGTPKKSKLMPSDD O94579 PSA2_SCHPO SPCC1442.06; CHAIN 1..245; /note="Probable proteasome subunit alpha type-2"; /id="PRO_0000124089" MTDKYAFSLTTFSPNGKLVQIEYALNAVNAGVTSVGIKATDGVVLATEKKPTSELAIGASLEKVCAITPDIGMVYSGMGPDFRVLVDKSRKVAQTTYKKIYNEYPPTKILVQEIASVMQESTQSGGVRPFGVSLLVAGMDEKGPSLYQVDPSGTYFAWKATAIGKSSTAAKTFLEKRYNDELELDDAVHTAILALKETFEGELTEDNIEIAVVSTKPTDSGIVGVPGGHFCRLSQSEIRDYLDQV O94589 YC93_SCHPO MOD_RES 441; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC584.03c; CHAIN 1..551; /note="RanBD1 domain-containing protein C584.03c"; /id="PRO_0000303895" MDELLNVASHAATFATNFALKHSISFAGKLAVQQVSSYIKRASADDQSELESVKTQLLEMIRVVTPAIELIEIMSVGENENFKSTKQLVDSLHADIEQFTKHVLSAAHSEFPPSSEKETLQKNVDTSILREMKTLLLKINDAVPLLNLSITTSGASISSSLPKSTSFSQLLRANSYIYRANVAFTGNEPLQVGPTFFLRTYKIIDNHAKSGYISNDLVMWKEEMPVCIAKMFRMPPQRLKSKDTVLAYALSLKQSFDDDRYHDEDETPVTKTISLNDVRTLFFSLSGKLLRLDDVQTPVLLLKYADDETEYSSNTAPSNWIALEALPLVSIPNESLDESDELAESLSDSEAARLQLLGIKKQESVAKKKSSFPSTIKDQPNLTLLEYLIRLCALESTTQESVLQLPDEQIALYLKDYQGRERPRDPASYNALENRSELSASPGSVSSSRHSGIFATPTFLSPWNIKNIPLVTPEVSTRQTKNVDEEDSALLMASPSVRKSNLLPQEDLISKDSVIKLKENPSVIPHSEPESSSKVINCQAKLNVEKEKKNP O94591 YC81_SCHPO MOD_RES 21; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC622.01c; CHAIN 1..149; /note="Uncharacterized membrane protein C622.01c"; /id="PRO_0000304003" MTVDNVFIHAVPREQIRRRYSYFEAFEKNCHIQGILSKRALYMLIPCFMEFAVGSIVYSFGVPGWVLGMNTVLAAGFLVMFLFLVWPCFQLVDERQIEEPGEDEMALNAGGYYPYAEEVPPPSYPSLEEENEGNEEIEESEEMNTLLSK O94597 YC87_SCHPO SPCC622.07; CHAIN 1..128; /note="Putative uncharacterized membrane protein C622.07"; /id="PRO_0000303967" MASLDIHLYVKKDLTYGECVRVAKEKYKIIHRLLYISIIFLFLNYVVDIVCYVKNYNGFSFFCWVFLNLGVIGIIITVIIYYISIPKPDAESEFLNKPDSLNQNVGESQSNEPPKYTSTFMDELDKQD O94599 YC8B_SCHPO SPCC622.11; CHAIN 1..562; /note="LIMR family protein C622.11"; /id="PRO_0000339412" MSSWFNVGILCLLRFKNVQDNKIIFEAIFEVFLHFLKIPVYMTHLGFPITPTVCLIEMLGLLLLLLIPALFTLIWIYKYIEPHSLISIPGIFVFLGLYVPFVVTLLIPIDVTWDVSLSIWRFLYWLTFVLSWIILPFVQGYMESKFSTPRSRLSDSFYKNLRYYLLLTFLTCVVIAYLRFALRTMSFSNFKELVISLTYFWGLLFVIFLLGNGFVYVPVSMWKKAFITKRAALLERQAVGVYSKLQARLESYSLPSSSISLNNGRNQSSSDFFTSSLTDHAFNPHSSPNGMSNVIALQTTWNQMVKEYNRIMLIKTAKASGSYRLYLPDSYIPIHPVVAYAFYVWILPAFRILFSIFMASMSVIIVVSEVFLHTQYSLVGIILQKFTNSSATSIFVSFLFVYYMRYCTYKSLMRTQFAPHYYYALVPFRATNTASLIYFASQLCRLTLPLCYNFVSLQPYPTQFHQFYGESIDLLPLGNLISKRYPTFILLPIIFSMISLKYRLRQFIYSITLRKSSSASSSDDFDDSSLNSENDDDLFNETSAAYLAEGRALLLGTNNAHV O94601 YC8E_SCHPO SPCC622.14; CHAIN 1..321; /note="Uncharacterized protein C622.14"; /id="PRO_0000318102" MSYKLDQLTRLPENKKCFDCDAPNPQWASCNLGIFICLDCSGQHRGLGVEKSFVRSITMDNWSERQVKMMEVGGNSNAKTFLSTDPMFSAAGSIREKYNTDIAEDLRQKIRAEVDGVEWVKVDRPKSVSSHASVTSSSTVPTIPSVSKEANDKYFAKLGSINSQRPDDLPPSQGGRYQGFGSSNSVNPNSSARNNGGSFLDQLSSNPVSALSHGWNMFSRSVSQQIQDVNKSYIQPGITKVQDPETRKDYMNAINNFSSNVQEGAKQSFTQLKSFLDENVYSENPQNTRGTYDAEIDSPYSALAASPPPEDYSKKNFDKHD O94602 YC8F_SCHPO SPCC622.15c; CHAIN 1..557; /note="Uncharacterized protein C622.15c"; /id="PRO_0000352821" MNEDETSILNKKMEKIEVEMAEFERLGAEREKEAVERIVQEENQNPEVPSNDDASTDIKSRKEGNMKVTAEEIGLETENFDELPVSNGFGVSRRETHYGNNRTYYKNSQGYRRKPKRDDYNNNRKNFYPPIQNSTYFINATGGIDSMPYFGLNNAPGNIYPFSMYKPLEADPQYLSVPSSMPSRREAGMAYGYQNYKRGGYTPNTQYFEEPLNNTSFPNSQGKEGKNSGYRKSSRILDIRVKFGNSSMKAINFQPKKKIVHVVHNPRLHQNKVLRVSIPGSQPALVTPKHKMNVPPMGMYPLPFSPLPSAAPPIPFSPNVSSHPHMAFLPATVPTHSAPPGFVPYDFPITNDKMYPSPSFQEEFPSTSKSPSATPGSSNAPVVDMHPSADSATYPTSIYPSNVRARDDSQQAYISANMTTGEMPSMTNVPAGNAPAAPGTMYTTPLPTANSPIAYQSYSVMPTYWSFPQNYDSTVPAVYPYMPPPFSGSDMNVMSNPAADTLRSYSPASQVSTPPFGFVYYYDPNQYYVPVSNESANATSQPLSNLDTGGSAPYDHI O94611 MUG65_SCHPO SPAC1296.04; CHAIN 1..248; /note="Meiotically up-regulated gene 65 protein"; /id="PRO_0000116746" MTESERTSHLDILYENQRGIMLCGVPYFSEKSLLNFDPAPWVDQHFVASPVSTKTATCPDPSWEWAWQRWYIDMSGDVDESGWQYGFSFTMNNWHGKPVSLHSFVRRRRWIRKRKKKELRRDELPLVPESFTISSSYPIQRSSTQTRSSFEDDSSDFDLSEVTTIPALLRALQDSRIDREKLEALATFLASASIDEKVYVKNCKKDLLKNFVFEHSCRKANELLNASLTAAEASTSQVALRESPTPQD O94624 TIM54_SCHPO SPBC1347.04; CHAIN 1..347; /note="Mitochondrial import inner membrane translocase subunit tim54"; /id="PRO_0000228018" MLKTIKSYMPGRNMSIFLGFVAGISGAIYYDRRQKNLIIEKYCSQVRHLADQPMAPLELPRKLKVYLHGPPGDGIYVAREEFEEYIRPIFNAAAIEFETVESKGEGNLLEQVARTVYNKRHNISEVSEPEKNLLSVLKPSVDPPAIVLLGRHALKEFLYGVRYGFSDDIMKRKLETEKLEANNKEEKEEKEGKDDKDDKEDSNDTKNDKKISKNEVDSSLIEASPLTGQVPPKFLDTIAIFPLPNLLGFSNTPKRLSRFFKRRELADELGAIAVNVALSRDVTKFPKQDGTLLLAEEETDWPKQFFTRSDLENRIWTAPFLQDSDEIRFFENIDIFDSTKAKQDKYE O94628 YGE9_SCHPO SPBC1347.09; CHAIN 1..284; /note="Uncharacterized methyltransferase C1347.09"; /id="PRO_0000339155" MSDIVYANVSHYNKIEASKYDNPSTLAISKVISSKILQFEDNSETSLRHDLPKYDQDRLLLTSDDDLTNVNNFWKKSGMSILDFACGTGLISQHLFPYCKQIVGIDVSQDMVDVYNEKFRKMNIPKERACAYVLSLDDLDGNGDEPFSTEFDAVVCSMAYHHIKDLQEVTNKLSKLLKPNGRLFVADLIKGGDTFHGNLHPDEIAKLGVAHHGGFTPQSILNLFKNASLSNAEVIGKAQANVWVDEAKYQRSTQSKDAKTLDLANGEKLYEVKLQLMVISGIKT O94644 RTC5_SCHPO SPBC21.02; CHAIN 1..511; /note="Restriction of telomere capping protein 5"; /id="PRO_0000116524" MGQKESQFKVLWQLQTHEEYMKQTSSFLRDFNALERYNLKENFEALSSFDNGEKIWVEDAFTTFFGIPDVIQLSPFFYRSACSFGRDLNINRQRLTFSALARFLASYTGRHKDVWSDFESNLMIIASWCDSFPKFRVEVLKNSKQISRLIHSDVQNISNFFDQNFGIRRSNIYQLCLLLLCISKLKPGESVGCHINSFLDSMFVKEQKAAFYVLQGISPDISSNIIKPSYLLHFLESNPYFLKSLGSLFELALFPHSAHNQKVQDDVSPLNDFAILSPLIHAQICFFLPKSVWQVNGLTSLFRASFHGYSMYALERKMCNYHNPSILLIKAKKINANHKSSSRPISLDATIPRKYPPHCIGTDKAVPQKFGADFHNENILLGAYISTRWRQSHMGFFGDHSTLLFQLQPIHQVYYASNLDKNYCMFDKNVGLGFGLSRHKVTNKVQYDVPGVCMYIDDGLEYGLFRHAGDGAFKPATNYENFEYEERFLIQDLEVIGVDTTKPVEPIHIGL O94654 YGF3_SCHPO SPBC405.03c; CHAIN 1..341; /note="Uncharacterized transporter C405.03c"; /id="PRO_0000343213" MVLQAIGKHALGVVLLLFVVFLWLISSFLTSSLLDDDNFFSPFLITYINTGTFVFYLIPWYFSEKKTRKHRLMSELSMYESVHDSSFNLGTRPNSPLGFRQTAYLSLGFCIIWFAANYFSNSSLGFTNVASFTIISSMSGFFTLGLGTIVNVERFTLSKLLALMASVGGVIIVVTQDAKQADLNDSPPSRPALGNAYALLAALLYGCYSVMVKFHITEESCVSTRLFFGLVGLFDLILLWPFLIILHLYGVERFSLPSTTAGLIVLIINASITFVSDYLWVIAMLMTSPLLVTVGMSLSIPLALFFDILLKGHYLNFSLILGSLLVFAGFIVVNYNQQNII O94674 YG76_SCHPO SPBC776.06c; CHAIN 1..623; /note="AFI1-like protein C776.06c"; /id="PRO_0000374002" MMQIDYLLTAIFDPDRGPVLQYQCPENGEASDLHFLAELMLPDRVHERREDWSLFFIHFSKKSNVFSLFSNVDDINFEPSDSNMYYVLNTIRAKRVEGTRRGGSVFAMAICTTFPHVHALKPLLDTAWEIFDSSPSLKTLSMLHKSFNLHNFQSFYQKLSLDSSLILALNNFWSFFNLYLTNSPHIMNDIINKDIDNIPKPGSELIELSRDSYNSQATFCLSAESQERYVTCVIPSIHIPECVGEVSISNLINTFIDGPSPFMNTDISADINPINVLITALLISKKVLFLTKTSSASVLADFVLSSCALVSGATGLLQGLTRITFPYIDLSNVESLVKLPGYLAGVMNPAFTHHADWWDVLCDIDNQTIQVSSNLFSDATTTMDTKSLFNNTSPFTPISKDNQDDEIFIKDLRKFLKADDKETLVRWRVRLYIQSFIRKATSYEALFLESSPLNPYYKDYKFKGFGWSWDNDDEKVNELLYLAPKFEAWRQASTYKDYCYRLHCASTPVLRCMDIQFHLDRLRNSSLSTTDAAEIFLALESHIRTEEDVNYLLSNCPLHSGGLSVIAFGLYHISDKVRKAVSKLLNRIETHKYGKLFYMALNKVDISTHVYINSQHKKKKDSF O94675 MAM33_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC776.07; CHAIN ?..269; /note="Mitochondrial acidic protein mam33"; /id="PRO_0000316240" MNSLRVLKIFRSVSRSIRIPASNGCINLGRNAYRVQLAKAPFSFSSIRRSSHTAGNPRSKLINALSSEIDYEKNQVLSEISLPPVNYDIEDVQGSAVVVLKAKHGDENIRITMNVSQDVTDAVPEEQDFTEFEDEQELQNQGESAEDEFPNEDLGRFQPCTIEISKPGNGALVFEATALDDGFDIENIYFSKDIDMLTSDSLEAEWKRRKQYLGPSFKELDPELQDLFHSYLEERKIDESLSSFIVSFGLTKELKEYINWLESVRQFLK O94683 RRP7_SCHPO SPBC776.17; CHAIN 1..238; /note="Ribosomal RNA-processing protein 7"; /id="PRO_0000374040" MDKLKEKGFVKLEIYLENKKRLHSIFLKEDTEDVEKKSLYLINVPITTTEKILKRAISQLGGRIVNIYPNISGLLKSGTHLRVKLVEPAEVKQVIKAASKKTTSLPWKFTQHTGLKRYVESYDRQFVNPRVLAESVDSYMKRVTKKEIAEKRRLFAMKNQPDEDGFVTVVRSGRAPVGRPQDAERQLEKKKDTGIHKDFYRFQLREKKKKALLDLAHKFEFDKQRIQQLKEKRQFKPY O94689 YME2_SCHPO TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC83.05; CHAIN 30..773; /note="Mitochondrial escape protein 2"; /id="PRO_0000343131" MNLFLSRFTGLRNTSFLGHARPFMFPRRYAHSLVAHNIGHIKLDPNEGLFFVDNLVNTPTYFYIQRYTALLFQNNLKKQLSAAFPSSDTMQLEDIIFRWQDGGAFLKVRYKEFPQDTEAVSEHVRESFRKRPVRTILHPFSTPIPHMVHGIPWLQDLYIFPSRTVDVNFEGPPLSQERLYSIFRTYGKLRSVTINSPTSATLSFSSLRSATSALNCMHGFVYGKTEFHMRYRHMNRFVAFKDWLFSHPRFTIPLVAAAITVLTASLFDPIRKFFVETNIVHGQKLRNINVVGWVKKKTRDIVLSPFHENGTNIKAPIWTTREKDCEQLKEWLDEALHSFIVVQGPRGSGKRDLVDRVVKERKNVLFFDCDRLFSTTNTEMFVSTLASQTGYFPLFSFLNNISSLIDMAAQGLIGQKTGIVSSSEGQVRQILNTTQTVLRSLALREHKEADTSVLDESEFLEVHADRLPVVILDNFQLRKLSNPMQRVVAEWAGNLVKEGIAHVLMLTPDVGGTKSLEQYVNGWENRTLLLGDADPVLAQRYVIESLPEEMQTEELRKELRVQLPKIGGRLRDLDYVARRLRVNSSSVSEAIGGIVSQNASDILQTFLRPASLTSEEKPTFTPEESWTLITYLSQHEYIPYHMLMLDPLFKGHDDAVRALEESELITITTVNARPDKVYAGKPVYVTAFRQLVNDPVLSANMQLVRCNALIGMANNAIKNDEQELQMLKDLGNLESGVKDRAHYLTTRIQKNQGVITDNEKSIERLTEALKKID O94690 RTC6_SCHPO TRANSIT 1..54; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC83.06c; CHAIN 55..92; /note="Large ribosomal subunit protein bL36m"; /id="PRO_0000337686" MASLGRKFFAVGVLSRVFPSAFNAQKGLLKNASMFLTPAFRLSPSLLPWNFSRGFKVKASVKKRCSSCYFVRRKGRLYVLCKKHPRHKTRQG O94693 LIN1_SCHPO SPBC83.09c; CHAIN 1..408; /note="LIN1-like protein"; /id="PRO_0000195037" MKRTLRNPGNSSTVGDVHDVFFEYDVSNVGRKRPRTKEEGYYESESEEDEDQILNKEKKEGQSEDMFSDTSEDEKRTLPNDEAQKRRDFIENGDAERLAHKGLRNKEVLNDDSDDEDDNGKYSKLRYEDIEGQEDTNQANDLDADEEGSEISVPSSPKRMSFNLKEDMEEGDFDENGNFIRKNYDPESQYDAWLNGSVSNKKSIAAAREAEQKRKEMENRRRNQELEEFSKLPFSTVPEALSFFIARMERDESILEFLQRQSGNKKSYKKKKNNTAEGISPERKSADAFRKKLIELITAGLTFLEDKIGKEDIYSETRESLQRIYQKLTSNSWSSPVSYDDSNSSQYNFKWEFDDKTYGPYTASQIQAWSNEGYFTDAKHAAFIQLANMDEWMYPNNICFCDVVSLKK O94694 YG1A_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPBC83.10; CHAIN 24..189; /note="UPF0620 protein C83.10"; /id="PRO_0000343218" MKLHTFLLLSVLCFAGCIQQSLQAEVYGKVLTNTILPKINLLSYDTRARLISSNKTFETVVERDGSFTFPNVPDEIYFLRLESIDYEFSEFHIIINESIVYPYYTSPAEKRPASSTAKNTSYPIKVRAVLKRDYLKEPRKFSLIRLLKSPMMLLSLASVVLVFILPKLNIEAKALEQARLAEAAEKKTA O94699 IML2_SCHPO SPBC83.16c; CHAIN 1..563; /note="Inclusion body clearance protein IML2"; /id="PRO_0000373873" MSKSQEQRLQNFVTVIQGLNDILDDKMDEATEKFKSGNSSFHLSGQAVVAFIQAVLTFEPSRFKDSQNRIDIAIKALSADKDDASKNNTFLSTFDPGVEYRVSIGLMLLLSALIGFCSESIVTSVKSVYKLRKAHSIFSKINKRHFDHFSAAFHSTGRSDVDLANEYVQTGTLLCTGLFTLLISLLPPKMITILNVFGYKGDRDWALQCMWMPALQRPTSFFAAVAFAALIQYYSGAVQLCSIYKKTPEEPDGWPDKRCFEILEKVEKAHPDGPMWPLHRAKLLSMVKKQDEAIVVLEELMAKPPPRLKQLEVLIVFEHALDCAFSHRYVDGANSFLKLSSLNDSSTALYSYFAAACFLQDVHVNANVEALEKASKLLEPLHDLVANKTAPLDVHIRRKVGKLIKRRASAGNQGGLAEYVGFSPLYELVYVWNGFRRMTDDELSKFDVERMEPWQDQDDDICQALIKATVLRNLGRTDEVFPILQKICAVTRTTETWAVAFAHYEMAVAFFESNGSKKEGLKHCDAYLRKARDFGGDNEFESRLIIRVQLARHVVRKCLQSMS O94706 TAF8_SCHPO SPCC1259.06; CHAIN 1..222; /note="Transcription initiation factor TFIID subunit 8"; /id="PRO_0000343160" MEAVIANILQQLGFDSMTKAAEASFVEAVDKYLRNSFRELALHTQLSKHTIPTTKDVALWLNLLNIPMSSLQTELEKYLKPLPPAINDELDRLANESQDIPSKFKSSLDSKMVSQLLGSLAVSQNRPAYVVNHLPPFPASHTYMATPVYPVRPTSPKQIRELATQESRLAEHALRKILNVNQPRSADSPRHASFEKACSELNLDVSSFHLVNWESQKWSSQR O94708 YC58_SCHPO MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 121; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 379; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1259.08; CHAIN 1..394; /note="Uncharacterized protein C1259.08"; /id="PRO_0000353135" MTGLLSILLHYKGNGDLATTDIPSHEKIPSAKRTAVQFCIGPTHEQSPRMSTVSQGRVTFAVLPTKPKDEVTSMKANGSRQSSCIVSNARKRQSVHCLSRSPIPSTRLKENDSRLCSPLASPTGGLKRPAKVSFALANTPSRKGNLVPQSPRRTIATTCKGVLEDVLKKDNELKFNDSDEEDEVDDEEIESFNSFSRKMQTISNSRYRGSPKPNIEKQSCSSESDRVSQISDDEEDEEGSADEEDEEDSDVELSESSLSDDEDSPLRCPSTPVQTAAAPNESQIPDDTDFVPGTFDEDQPACLAFACSLTHANSKRSIMLPQDIDPTFPDSEPEDDGHASSTVGSLSKEEARFKAKAKWNYKSSFSAHVSSEVLRNSKSPPLDIARKAVGAHRV O94711 GYP2_SCHPO SPCC1259.11c; CHAIN 1..720; /note="GTPase-activating protein gyp2"; /id="PRO_0000312836" MNLLKHIFLEDDYDAYEGTLDPASFFRINKQEEIIASTVCEIGWEYSKSFGNAYICTSFLCFHSDDFKTRFTFPLAAVRKLERENSDNDTFTFDLSNFHSQIIHLRFKGTRQQSEFFCDRLVRQLHASLEDASSVGLFLLSLASERVCFSESANSQEIESIDLGLGSQFGYPIASSNTNGLINENNSKSWIQYLKKNGANFNLIQTPNFQKLVQSGIPNNLRADIWETCSGSLFPRWKSKGFYAKNIDSVINNRCEYSEEIEKDLTRSLPDYPAYQSPTGINTLRRILLFYSETNKEVGYCQAMNIVLAALLVYCTEEQAYFLFSQLCEFYIPGYYAKIIHGLLLDLTVFEYVLEHTLPHLYQKIIELDMDLKLITINWFFSLFIKDFRLDYAFRILDCLFVNGPRVLFQVALALFKVNAQGILNATDDSSVMKVFRQCFDHINQGTAADEKMAALGSRSSMCTLPQLFAVAFEYFDFITDSFVSAKRKEFKSSVLYSLRCFTKRSHLRSVYQTTLLSNTDLDLVYDAFINAIGENNICHGDVLEQKIDFNGFERLVDCAAPPLSVIREPLHYQRSKRKLFTRLYIWMKDGDSTETSLTFKRIIHGLERLKADIALHSEILCFQLYDLKRDGTLRTEEVVELSESLILLCCYEGDEKDEERLTVISEFLKSCFSGCQDRRSFQITMEDFQAIVDTTGLHATLEFFLKKLIDGLLGKLNAS O94712 YC5C_SCHPO SPCC1259.12c; CHAIN 1..491; /note="Uncharacterized protein C1259.12c"; /id="PRO_0000303960" MLPRAYLRMTSTPKNLEKQPINFDNLPLYLQGTNYGENVLRSDPRWLKWEKYLREFDMTREGNVTNTPKAIPSSWNPNDKSDSLELMNNNMGVYFFGPEAGTEHDAASVKADHAIPSNTSIYYYEIQILSRGKEGKMGVGFCRKSMQTNRLPGCTAESWGYHGNSGEKFNCSKTGEAYGPEFTTGDIIGCGVNFINRTIFYTKNGAYLGVAFKKVSDVLYPVIGLKSHGEHVEVNFGQNPFLYDIDYAIQMEKNKLFEQATKSPKQEELKQRQEFLNELISSFLLNNGFVETAKKFCPENTEVSDASIRKEISSMLANGQLDLAMTKIDCQYPVAIQECPDLIMSLRFLRFLQLVKVTHDQRLTKSKGTKQISQEEDLRILQPLMNYAQELSNDYEHTKSSNLQAMIKLSMGLLAYFDPFSSPLSFFMSSDFHKYMAEQINCLLLELTGHSPDSELRRFLQHTVCLNDLLCRNGCRSNTLFNVQSDFLSPY O94718 IPI1_SCHPO SPCC1393.06c; CHAIN 1..413; /note="Pre-rRNA-processing protein ipi1"; /id="PRO_0000308729" MGKSKKAKAKRADFNKQKLKVGKSKNAPNNFTDTSFRTKTLVLPTQAALEKEDFNTTAKDQAYFAHLLGMLKHHNANQRQETLEKLTQYVLSHTSILTTSTALLLKLTSPLILDESSSVRDCLYRFLEKFIYIMGPELLEPNIGMIFLYTHSGMTHITPSIRNDSTKFLSLLINACKDRLSSSAISLQWKKTLECFTNLLGWNSESASVKRTTSFSKKSSANMIRHLTVCNDFLQLGLNPKLQAKNQQSSVHLKYPYLQQCIVIHPKYEAFRSPCSFAYLSLFNPNKHDLVDNPTFRWQTIYPLIPGIIEFIRNSWSDACPVVKDGSNSPSASKVCRTVLSMLGLFTEQVFSVADEPNNHRKKISQVLRKINRDIELININYGTDSEWRGVLKGYDKLRERAVELDALENPGK O94719 MUG4_SCHPO SPCC1393.07c; CHAIN 1..845; /note="Meiotically up-regulated gene 4 protein"; /id="PRO_0000278485" MTPPSSSSHFPSPSSANNDFHSLSLEAHGSLSDKFISQFRLNYTIIPIAQKSNISLPFLTLSPCSFTICSLRARLHSLHGPSTVFLKRETSQISARVNDENGFTASPSFFSVDCFDELFPTLSTTDEQPKEPSIISISSSSSDPSSSPPPSSSLLKTPDNDFCARPETFVKSDTADIKLQIHQNNLVLTFLDTTTVSKVNIVLEIHIPVLRDFVTFEQYIPLMFLPSPFETILSFDNLKSDSPSSDLHLGWDHTVSKESMSQSIAEVLNPYNKGVSRSLNDATNMETYHWSPFPPQFSTFNDNALRLRIYYKPKSWLPKNSSCSLSVDVKATLLETTPPSCEVSYNLLLTCRSSNRFRLFPASTPNSNGLCRNDSKCRFLMILPETIIKSPSSFIGDSYNIANIDPPSSMNVQSSEFRVGEVQSFTTNTSSFAFTFKEIVQLGSKASVPMILFPAPSNYKLTIEKPPFPCDLTIPHTAINDSWLPMKLKETNAISYYRKTCSSCKYPFQFFINKLPFYQSPSLPLSATYVWIASALLSVQPGNGSFNIMLSLKFVSSMKPGTELLTIKQPKSSLLNWGLVNGYPKTEGRIVLLPRNDIVLIQADQPTSVFDLCWTIKPTYEKSSNFSCLQLPIPVLNTPILTPVTINIQSTTYYLIGYANQNSKKTLDQPTSLLVLGCKAKNVSELILSYLPEKPIPDGAPIVTNVVETNKTNEAPSSFRKCLQQFLVFLTFTGMTLFILYQLTFPYGVAKDNSSFIDTPLPHSCEMEKSLNVLQHKVLQLQAVNMKLHDYYEKEPTEIYKTVSVTSTQIMPAVTKMSSFELEREQFHKAFGFLRLNRKKDDNAN O94721 YCF9_SCHPO SPCC1393.09c; CHAIN 1..215; /note="RWD domain-containing protein C1393.09c"; /id="PRO_0000372421" MTSAIEEEREILESIYPEEFKCINDSTFEITQPIDREESNCDNPPSLIFTCQLSEAYPDEVPDVKITFSEPHPWLGEEEIERLKQVVAQNAEECLGMAMIFSLCSVAKEETNAILIEQSQRETQAIEERHRKEAEQENKKFHGTPVTVESFTEWKKGFDAWRNEQLKLEQESKLKEALSAASSSNARKAILEKRMTGRELFENNLVKLDDVEGEA O94723 RM20_SCHPO TRANSIT 1..20; /note="Mitochondrion" SPCC1393.11; CHAIN 21..197; /note="Large ribosomal subunit protein mL58"; /id="PRO_0000374038" MLFTIKPSFLKPVGFIQTRNLNRLYPKQRIPKRPKIPMGSKIAEVTETTSAYYNPPASSPDVRITPPVFRYDAPPIHQRDTSLSKESMFLPPAVSRKSKSKGKLRFSTHQLSSEDIKSIQDLRTKDPNAWTTGTLSKKFNTTRLLISRVCEAPKERIQKVEENFEAEKLAWGSKKREIRRQRASRQAFRTLERVAQV O94724 YCFC_SCHPO MOD_RES 56; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1393.12; CHAIN 1..108; /note="Uncharacterized protein C1393.12"; /id="PRO_0000303938" MNRRVTLGALAAAVGVGYYMTRHNRQASSRLEQKNAEIVRAVENEGQRFDKAVGETTEKAKSYLQSGKERVVDELDKPRENVKNVLSEAQAKGTEQAEALKKGTSKWF O94728 YG0G_SCHPO SPBC1604.16c; CHAIN 1..199; /note="Uncharacterized protein C1604.16c"; /id="PRO_0000116752" MENKGNMELSNSYGFYKNGRRVSFVKATSEQSLDEATFIEKGSAQAFYHSLFENDRDNSHTMNSKRDEAGFACEVCQIYIPNSKKINHFKSMTHLLSSQHISNKFQPHLLKPKSLGYRVLSQYGWSPQGDTAGLGLENQGRRAPVRAFRVKNDTIGLGTKIDLEKVAVNKCRKGKRQCQIQHSKDVRLKEALIKHFSSN O94733 YQ61_SCHPO SPCC191.01; CHAIN 1..178; /note="Uncharacterized protein C191.01"; /id="PRO_0000304114" MVTRRLSTNVHIDLQPIRQGILLPFHDRPAEMRDLAKCNDQFFRNVRDTISEPKFTQLMELWLEKSRAEVPDADFLMTTRNIMLSFPSNEEQGHQRSASHGSTSSATSTPKRLSISSMDPARIHLWRQFCNVVGYDMPTPGEQKEAPPSPAQEAIPESPVEEAIASDSDEEEEEEIKA P05511 YMC6_SCHPO SPMIT.06; CHAIN 1..807; /note="Uncharacterized 91 kDa protein in cob intron"; /id="PRO_0000196883" MRRCGIYVYPHRERDILCVKIWTIHLGSWGNPMPNRACVQKVLPVTKQISSDGSVQIDTVRAVLPEFQFPSHPQIGDCLSWIETFFSRSLVGFYDQGYTPGEESCTNSTIKGMSGKPTSIISNIYTTTGPAKVSNDYAVRDPGVAVDHFDQYGPLKEGRSLNSAKISTQWSGSATLKSSNRSIFNIGLGYINTFLGVSNVRGFSTGSGRSKNVLNKLDDLSKRSKNYPNLVIDRNLYKDFLLNRDMFLIAYNKLKSNPGMMTHGLKPDTLDGMSIDVIDKIIQSLKSEEFNFTPGRRILIDKASGGKRPLTIGSPRDKLVQEILRIVLEAIYEPLFNTASHGFRPGRSCHSALRSIFTNFKGCTWWIEGDIKACFDSIPHDKLIALLSSKIKDQRFIQLIRKALNAGYLTENRYKYDIVGTPQGSIVSPILANIYLHQLDEFIENLKSEFDYKGPIARKRTSESRHLHYLMAKAKRENADSKTIRKIAIEMRNVPNKIHGIQSNKLMYVRYADDWIVAVNGSYTQTKEILAKITCFCSSIGLTVSPTKTKITNSYTDKILFLGTNISHSKNVTFSRHFGILQRNSGFILLSAPMDRIAKKLRETGLMLNHKGRSVIRWLPLDVRQIIGLANSIIRGYDNYYSFVHNRGRFATYVYFIIKDCVLRTLAHKLSLGTRMKVIKKFGPDLSIYDYNSRDENNKPKLITQLFKPSWKVNVWGFKSDKVKLNIRTLYASHLSMANLENLQCAACQSTYKVEMHHVRQMKNLKPIKGTLDYLMAKANRKQIPLCRSCHMKLHANKLTLNEDKKV P0CS86 YI41_SCHPO SPBC1348.01; CHAIN 1..269; /note="UPF0494 membrane protein C1348.01"; /id="PRO_0000306279" MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDLFTEFSKFHNSYYPDGRISTRSNFRWPLLIIWSIIIVFAVDKKFEVQKFLSIWINENRFYSEIWVPIAIYVCLLVLMLLSLIFFAEFAVLALRVTGVIIAVLGMIIAVLGMIIAALGATITGLLYFGHWALYKLVILSLGFKIVTPGDVCVSNTLPTHNGETALHSETTVGSDIEQIELQNMPTPVKK P0CT59 RS22B_SCHPO SPAC5D6.01; CHAIN 1..130; /note="Small ribosomal subunit protein uS8B"; /id="PRO_0000433422" MVRQSVLADCLNNIVNAERRGRRQVLIRPSSKVIVKFLTVMQKHGYIDEFTEIDDHRSGKIVIQLNGRINKCGVISPRFNVKLKDIEKWVNQLLPSRQVGVIVLTTSRGIMSHNEARAKDAGGKILGFFY P0CT61 RL23B_SCHPO SPCC1322.11; CHAIN 1..139; /note="Large ribosomal subunit protein uL14B"; /id="PRO_0000433421" MSRGRGAASGTKYRMTLGLPVQAIMNCADNSGAKNLYIVSVFGTGARLNRLPAASCGDMVLATVKKGKPDLRKKIMPAIVVRQRKAWRRKDGVYLYFEDNAGVIVNPKGEMKGSAITGPVAKECADLWPRIASNAGTVV P0CT64 RS16A_SCHPO SPBC18H10.14; CHAIN 1..140; /note="Small ribosomal subunit protein uS9A"; /id="PRO_0000111501" MQSVQCFGKKGNATAVAHCKVGKGLIKVNGAPLSLVQPEILRMKVYEPILVAGADKFAGVDIRVRVSGGGHVSQIYAIRQAISKAIVAYYQKFVDEHSKAELKKALITYDRTLLVADPRRMEPKKFGGHGARARQQKSYR P0CT74 RS11B_SCHPO SPAC144.11; CHAIN 1..152; /note="Small ribosomal subunit protein uS17B"; /id="PRO_0000433414" MATELVVQSERAFQKQPHIFQNAKKGAGRRWYKDVGLGFKTPAEAIYGEYVDKKCPFVGQVSIRGRILTGTVVSTKMHRTIIIRREYLHFIPKYNRYEKRHKNLAAHVSPAFRINEGDVVTVGQCRPLSKTVRFNVLRVVKHTEGPKQFGKF P0CT94 YHJ4_SCHPO SPBPB10D8.04c; CHAIN 1..379; /note="Uncharacterized transporter SPBPB10D8.04c"; /id="PRO_0000319983" MSWFYRFFIRDYQNCWMVSIMGTGLSANVLHNFPFAARWLRICSYIMFGFALVCLFTNTIVFFFKHTIYRGTLIQKEEFIDVPNTLFLGCYTMGFQSCINMLCFLSSQSSPQGWINFLYILWIFSVAMSFFTAWVIFSTILTKRAKIEFSTFLPTILLPIVPLTVAASTGSVVIETFSTRLNKKIILNTIVTSFICWSNAIALGFCIIACILWRMIFFKVPARALIFTQFVPIGVLGQGAFGIIMQAINAKTFALSYYQQIPMIEFYSNCVLVQSLILSLFLISFGYFFTFFAVFSVINYGFRHKFTVAWWAMTFPLGTMSISNTQLSKVTNIIFFRVIGAIYGTALILITIVCIVGNTIMAIQKLKSETSSKNLVGII P0CT95 YHJ5_SCHPO SPBPB10D8.05c; CHAIN 1..379; /note="Uncharacterized transporter SPBPB10D8.05c"; /id="PRO_0000437223" MSWFYRFFIRDYQNCWMVSIMGTGLSANVLHNFPFAARWLRICSYIMFGFALVCLFTNTIVFFFKHTIYRGTLIQKEEFIDVPNTLFLGCYTMGFQSCINMLCFLSSQSSPQGWINFLYILWIFSVAMSFFTAWVIFSTILTKRAKIEFSTFLPTILLPIVPLTVAASTGSVVIETFSTRLNKKIILNTIVTSFICWSNAIALGFCIIACILWRMIFFKVPARALIFTQFVPIGVLGQGAFGIIMQAINAKTFALSYYQQIPMIEFYSNCVLVQSLILSLFLISFGYFFTFFAVFSVINYGFRHKFTVAWWAMTFPLGTMSISNTQLSKVTNIIFFRVIGAIYGTALILITIVCIVGNTIMAIQKLKSETSSKNLVGII P0CT96 YHJ6_SCHPO SPBPB10D8.06c; CHAIN 1..379; /note="Uncharacterized transporter SPBPB10D8.06c"; /id="PRO_0000437224" MSWFYRFFIRDYQNCWMVSIMGTGLSANVLHNFPFAARWLRICSYIMFGFALVCLFTNTIVFFFKHTIYRGTLIQKEEFIDVPNTLFLGCYTMGFQSCINMLCFLSSQSSPQGWINFLYILWIFSVAMSFFTAWVIFSTILTKRAKIEFSTFLPTILLPIVPLTVAASTGSVVIETFSTRLNKKIILNTIVTSFICWSNAIALGFCIIACILWRMIFFKVPARALIFTQFVPIGVLGQGAFGIIMQAINAKTFALSYYQQIPMIEFYSNCVLVQSLILSLFLISFGYFFTFFAVFSVINYGFRHKFTVAWWAMTFPLGTMSISNTQLSKVTNIIFFRVIGAIYGTALILITIVCIVGNTIMAIQKLKSETSSKNLVGII P0CT97 YHJ7_SCHPO SPBPB10D8.07c; CHAIN 1..379; /note="Uncharacterized transporter SPBPB10D8.07c"; /id="PRO_0000437225" MSWFYRFFIRDYQNCWMVSIMGTGLSANVLHNFPFAARWLRICSYIMFGFALVCLFTNTIVFFFKHTIYRGTLIQKEEFIDVPNTLFLGCYTMGFQSCINMLCFLSSQSSPQGWINFLYILWIFSVAMSFFTAWVIFSTILTKRAKIEFSTFLPTILLPIVPLTVAASTGSVVIETFSTRLNKKIILNTIVTSFICWSNAIALGFCIIACILWRMIFFKVPARALIFTQFVPIGVLGQGAFGIIMQAINAKTFALSYYQQIPMIEFYSNCVLVQSLILSLFLISFGYFFTFFAVFSVINYGFRHKFTVAWWAMTFPLGTMSISNTQLSKVTNIIFFRVIGAIYGTALILITIVCIVGNTIMAIQKLKSETSSKNLVGII P0CU00 YI78_SCHPO ACT_SITE 100; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 114; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 118; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 22; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 49; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 82; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 114; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 118; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868" SPAC977.08; CHAIN 1..236; /note="Uncharacterized oxidoreductase SPAC977.08"; /id="PRO_0000437227" MREPKNAKVLSRLENVLVTQLDVNNFSSIKKSVEKAISHFGRIDVLLNNAGYSVYSPLESTTEEQIHNIFNTNVFGALEVIKAITPIFRSQHNGMIINVSSIGGKMTFPLGCLYYGTKYAIEGISEALTWEMQSIGVKVKIIEPGFTATEFRVEEGAGKHYAEYDNLKQKLYEDLLPKLKTATPPQKIAEVILQAATDESDELRYPTGDYVVEWMALRSKVDDATFLATHRKQMGL P0CU01 YI49_SCHPO ACT_SITE 100; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 114; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 118; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 22; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 49; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 82; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 114; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 118; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868" SPBC1348.09; CHAIN 1..236; /note="Uncharacterized oxidoreductase SPBC1348.09"; /id="PRO_0000374030" MREPKNAKVLSRLENVLVTQLDVNNFSSIKKSVEKAISHFGRIDVLLNNAGYSVYSPLESTTEEQIHNIFNTNVFGALEVIKAITPIFRSQHNGMIINVSSIGGKMTFPLGCLYYGTKYAIEGISEALTWEMQSIGVKVKIIEPGFTATEFRVEEGAGKHYAEYDNLKQKLYEDLLPKLKTATPPQKIAEVILQAATDESDELRYPTGDYVVEWMALRSKVDDATFLATHRKQMGL P0CU04 YI48_SCHPO SIGNAL 1..27; /evidence="ECO:0000255" SPBC1348.08c; CHAIN 28..416; /note="Putative cell agglutination protein SPAC1348.08c"; /id="PRO_0000353813" CARBOHYD 19; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 344; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MNFFLYFRTIFLIQLYFFNYSTFGCSASSTSVQSDTTNQVSVSCPKYTTIYTSGTSPDTKTIYPESTSTKSITTSTQSHSSPVIVVSTVGTVTETTISGSTEYTTTIPAEGITSGTVEIVEPTAGTVTETITSGTLPFTTTLAQASGTVSGTVEIVSPKNNPTTVYSGTVATTETFSSSTVVVIPTAICDGVRGLEYAVYDYTISSSMNEFCYPKNGQTDVFAFNEPAYFGSSDLDQSSPLFTGVFSSTDDIPEWASSWYLPPYPPQASDMASTYCACKVIVYQFFLRIPETDTYTLVVNNVDDVFFGWFGDKAISGWSNNNFDAYSYWHESPNMGLGTVGMGNFTVGNYPEGYFLPVRFVVANGAYIGGFDFYFTSDSTGPLATTSYSYTKTCTQQFLPFGQGNGGVNGPTEKLS P0CU07 YI72_SCHPO SPAC977.02; CHAIN 1..146; /note="UPF0742 protein SPAC977.02"; /id="PRO_0000437230" MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVYHNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR P0CU10 YLZ2_SCHPO SPAC750.02c; CHAIN 1..485; /note="Uncharacterized transporter SPAC750.02c"; /id="PRO_0000372790" MKEESILKKCDSSSIKHVPSTPLETNCPDKYNPKTWPIRLKVRNVIVISSMTFLNQYGDSVFAPSISNIAEQFHASRTLVTLGATLYTLGILFGNLIFAPLSEQFGRRPIYLIGYSVFALLQIPIALSVNLAMFLVFRFFSGLFGSVGLSNGSGSLADLFEKKDRGKYMVIYFTVLSIGPGIAPIISGFISQSSIGWQWEFWILLILSGFNLFWAFLLLKETYPPVLNRKKFEKYGEIGENEPVALRLTGKQLLIKLLILLSMKKPISILLSQPILICVACTIGSIYGMINLVLIAFSEVWKSSYDFSPGISGLMYISITLGLFSAVFIAMPINQKFYSYLVKRNGGEGEPEFRLPMGFIGITLFEIGILLFGWTARYKIFWFVPTIGSAIMGGGYIMTSNPLNMYVVDSYGIYSASASAGVKIFQLLLGAIFPLFAESLFRRLNYGWGCTLLAFILLACGCSLPILFKYGKQIRNLRPFDPSKY P0CU11 YHEG_SCHPO SPBPB2B2.16c; CHAIN 1..485; /note="Uncharacterized transporter SPBPB2B2.16c"; /id="PRO_0000437232" MKEESILKKCDSSSIKHVPSTPLETNCPDKYNPKTWPIRLKVRNVIVISSMTFLNQYGDSVFAPSISNIAEQFHASRTLVTLGATLYTLGILFGNLIFAPLSEQFGRRPIYLIGYSVFALLQIPIALSVNLAMFLVFRFFSGLFGSVGLSNGSGSLADLFEKKDRGKYMVIYFTVLSIGPGIAPIISGFISQSSIGWQWEFWILLILSGFNLFWAFLLLKETYPPVLNRKKFEKYGEIGENEPVALRLTGKQLLIKLLILLSMKKPISILLSQPILICVACTIGSIYGMINLVLIAFSEVWKSSYDFSPGISGLMYISITLGLFSAVFIAMPINQKFYSYLVKRNGGEGEPEFRLPMGFIGITLFEIGILLFGWTARYKIFWFVPTIGSAIMGGGYIMTSNPLNMYVVDSYGIYSASASAGVKIFQLLLGAIFPLFAESLFRRLNYGWGCTLLAFILLACGCSLPILFKYGKQIRNLRPFDPSKY P0CU14 YI42_SCHPO SPBC1348.02; CHAIN 1..344; /note="Uncharacterized membrane protein SPBC1348.02"; /id="PRO_0000371803" MIDFVKSRDTVIQKSFFEEFNSQNREMGSFAYSGNSESVWTGENITSIWKTILINETGSYCVAARPMTMDGAEFNLDLMGYSVSEDQINNDEIGIWNYISVAEMGGVLLFLSYWIWTCLHFSKIIFPAQKVICLYIFLFALNQTLQECIEEYVFSSECIKYRQFYSVYEIIDFLRTNFYRLFVIYCALGFGITRTVPKYLMIKGISIVIALCSVYWISLYKDVYVVSEIFDMIQYEVSPAIWVYSICHLLKQCTSVTTYENASKARFFRRMLNAFIFIFCASPMLHYLSNIIFGNFDYRLSVIIGDLFTFMEKIAFPCYIMFPTHNEALAYNRNVAEEAQEKMI P0CU15 YHEJ_SCHPO SPBPB2B2.19c; CHAIN 1..344; /note="Uncharacterized membrane protein SPBPB2B2.19c"; /id="PRO_0000437234" MIDFVKSRDTVIQKSFFEEFNSQNREMGSFAYSGNSESVWTGENITSIWKTILINETGSYCVAARPMTMDGAEFNLDLMGYSVSEDQINNDEIGIWNYISVAEMGGVLLFLSYWIWTCLHFSKIIFPAQKVICLYIFLFALNQTLQECIEEYVFSSECIKYRQFYSVYEIIDFLRTNFYRLFVIYCALGFGITRTVPKYLMIKGISIVIALCSVYWISLYKDVYVVSEIFDMIQYEVSPAIWVYSICHLLKQCTSVTTYENASKARFFRRMLNAFIFIFCASPMLHYLSNIIFGNFDYRLSVIIGDLFTFMEKIAFPCYIMFPTHNEALAYNRNVAEEAQEKMI P0CU16 YI71_SCHPO SPAC977.01; CHAIN <1..316; /note="Uncharacterized membrane protein SPAC977.01"; /id="PRO_0000437235" SFAYSGNSESVWTGENITSIWKTILINETGSYCVAARPMTMDGAEFNLDLMGYSVSEDQINNDEIGIWNYISVAEMGGVLLFLSYWIWTCLHFSKIIFPAQKVICLYIFLFALNQTLQECIEEYVFSSECIKYRQFYSVYEIIDFLRTNFYRLFVIYCALGFGITRTVPKYLMIKGISIVIALCSVYWISLYKDVYVVSEIFDMIQYEVSPAIWVYSICHLLKQCTSVTTYENASKARFFRRMLNAFIFIFCASPMLHYLSNIIFGNFDYRLSVIIGDLFTFMEKIAFPCYIMFPTHNEALAYNRNVAEEAQEKMI P0CU22 YKBH_SCHPO SPAC823.17; CHAIN 1..48; /note="Uncharacterized protein SPAC823.17"; /id="PRO_0000437262" MDRISAQKDIFKKVVNKENSSIFVSLGVFAVSVAILKSRLGNFLVPQL P0CU26 INA17_SCHPO TRANSIT 1..24; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC3B8.10; CHAIN 25..112; /note="Inner membrane assembly complex subunit 17"; /evidence="ECO:0000255"; /id="PRO_0000437260" MLRKLPINFAKWTVKKVPVQQKRFNSQQKEISPHIMFYKNYARPLGKVTLFALATYYGLEIVWWKLDASEQEAIKNSKLLICESSFSLLTFRRITEFRECEIKTRDLYDPEI P0CY14 MTMI3_SCHPO SPBC1711.01c; CHAIN 1..42; /note="Silenced mating-type M-specific polypeptide Mi"; /id="PRO_0000096247" MSAEDLFTIQILCDQIELKLASIVINSNIKLQLKRKKKTQQL P0CY16 MTMC3_SCHPO SPBC1711.02; CHAIN 1..181; /note="Silenced mating-type M-specific polypeptide Mc"; /id="PRO_0000048585" MDSHQELSAGSPISYDFLDPDWCFKRYLTKDALHSIETGKGAAYFVPDGFTPILIPNSQSYLLDGNSAQLPRPQPISFTLDQCKVPGYILKSLRKDTTSTERTPRPPNAFILYRKEKHATLLKSNPSINNSQVSKLVGEMWRNESKEVRMRYFKMSEFYKAQHQKMYPGYKYQPRKNKVKR P21536 ATP8_SCHPO SPMIT.09; CHAIN 1..48; /note="ATP synthase protein 8"; /id="PRO_0000195604" MPQLVPFYFINILSFGFLIFTVLLYISSVYVLPRYNELFISRSIISSL P21547 RMAR_SCHPO SPMIT.08; CHAIN 1..227; /note="Small ribosomal subunit protein uS3m"; /id="PRO_0000130333" MQKNNLKNLITTIVTNAFFNQKANFSIPLKGVIGEKRPSILIGNININFKSDSLIEVSFPYYPLLNKNYPNPSIISNIIQKALSNHLLYSSKNYSFIVNIRALPISTPYGSSLIFSKYIAIIIGSNPKIASTLWIDPKRFINLPKLQSDSIFKILGLNVPKGWKGIHISLNLIKWNSLSSRGRITNIIKGSVPLTNNSNGYDESSLAIYSKMGTIQIKVRLSYSSNL P22190 YMC2_SCHPO SPMIT.03; CHAIN 1..323; /note="Uncharacterized cox1 intron-2 37.2 kDa protein"; /id="PRO_0000196885" NLIGLLTLLYAGTTWKILDKSFCFKYSKKNTRLVFIFIVKMLKQLSISAGNLLNKGTSETLRNEITTKKVSIHLPKHLKPANDSQFGHYLAGLIDGDGHFSSKQQLIIAFHSLDIQLAYYIKKQIGYGIVRKIKDKNAILFIIANSKGIERVITLINNKFRTTSKYNQIINNIFAHPRFKEFSKTITLGLNSNNNLNNHWLAGFSDADASFQIKILNRDKKIEVRLNYQIDQKKEYLLSLIKDNLGGNIGYRKSQDTYYYGSTSFGSAKKVINYFDNYHLLSSKYISYLKWRKAYLIIQENKHLTESGLSQIKKPHPYRKNIN P22191 YMC1_SCHPO SPMIT.02; CHAIN 1..384; /note="Uncharacterized cox1 intron-1 45.6 kDa protein"; /id="PRO_0000196884" MKPQTKLSENSSRCEKVLYSEVITQLIYFLTSKKITNLGKIRLVKSIRDSFLSQLENILCFFLVYRTTYSFGVCLMKRFLFNKFFNRHPFTRVKSCFSSSSPSKFSFTQWLVGFTDGDGCFSISKQKIKNGKNKWSLTFKLTQNLYNYRILYFIKRNLGIGSLYKESSTNTVIYRLRRREHLKKIIDIFDQFPLLTKKYWDYYLFKKAFLILEDANLNSFEKNSKLEEIRIEKKSLKQYSPVNLEKYLTKSWLIGFIEAEGSFYLLQKSPVRIIHGFEITQNYEQPLLAQISEFLFNSQISPKIKSKKNSLITNYSLSTSSKERMLFLSSYFENCFKGVKSLEFKIWSRSLRKNYNFEQLLRARDLIRKLKNKYSRGSQHPKDK P32235 GTP1_SCHPO BINDING 69..76; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 115..119; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 246..249; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" SPBC354.01; CHAIN 1..363; /note="GTP-binding protein 1"; /id="PRO_0000205431" MGVLEKIQEIEAEMRRTQKNKATEYHLGLLKGKLAKLRAQLLEPTSKSGPKGEGFDVLKSGDARVAFIGFPSVGKSTLLSAITKTKSATASYEFTTLTAIPGVLEYDGAEIQMLDLPGIIEGASQGRGGRQAVSAARTADLILMVLDATKAADQREKIEYELEQVGIRLNRQPPNVTLTIKKNGGIKFNHTVPLTHMDYKMAYNILHEYRIHNADILIREDITVDDFIDLVMGNRRYINCLYCYSKIDAVSLEEVDRLARLPKSVVISCNMKLNLDFLKERIWEELNLYRIYTKRKGEMPDFSEALIVRKGSTIEQVCNRIHRTLAEQLKYALVWGTSAKHSPQVVGLNHRVEEGDVVTIVTK P36625 REC7_SCHPO SPCC1753.03c; CHAIN 1..339; /note="Meiotic recombination protein rec7"; /id="PRO_0000097226" MNIFPIVKYSVAEDSYTTDSSHINWSHYSDGGFTLSLTSGLLQIRQHEELIQSINLLDLWHQLIPGTKEKCLTLLSRAPCMNIRAFTNNVMKRFQVKFPSDVHYMKAKVEFEKLGLVFKDAKSSSEKKQFNNSQSQSNNSQELSLMNNAYNKSSAQQPNLLLQPSYIPMTQTATTAVNNSTNYVNPAPLQHVMPNAEIFSNTPPLKRFRGDAGMTQMPLRSDTSIESITASQQPTWDENVVITSSPFNPNRNAYSYGANSQYPIIAATPLNSQTQASWVAQPENQAYANLIPSPPTTSQILPTELTEEEKQLRSKVLFYLKQDSFIQLCQSLERVWNKM P40373 HIS1_SCHPO CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17; SPAC25G10.05c; CHAIN 1..310; /note="ATP phosphoribosyltransferase"; /id="PRO_0000151956" MDLVNHLEDRLLFAVPKKGRLYESCVNVLKGSDIKFRRNPRLDIALVQNLPIALVFLPAADIPRFVGTGRVHLGITGQDQIAEARLRIGDKLKIEELVDLQFGGCKLQVQVPESGDITSVDQLVGRRIVTSFEYLVAEYFDKVEKKAKSEGKVDSGIKTEISFVSGSVEASCALGIADAVVDLVESGETMRASGLKPIETVMSTSAVLVRSSNCSSELEPLLQTIITRIRGYIIAQQYVLVNYNVNREHLPVVLKITPGKRAPTITTLDEPGWVAVSSMVVKKEVAQVMDKLSQNHAHDILVLSIDNSRP P40901 ISP5_SCHPO SPAC1039.09; CHAIN 1..580; /note="Sexual differentiation process putative amino-acid permease isp5"; /id="PRO_0000054167" MNNYGVSSIGTSLTPSPTGSIDEYTSKEVKHPEDVKVDASYEKEEVGYGELEVVPERGNLFQRWYRSFLPPEDGKPQKLKRTLTARHIQMIGIGGAIGTGVWVGSKNTLREGGAASVLICYSLVGSMVLMTVYSLGELAVAFPINGSFHTYGTRFIHPSWGFTLGWNYLASFLATYPLELITASICLQFWININSGIWITVFIALLCFVNMFGVRGYGEVEFFVSSLKVMAMVGFIICGIVIDCGGVRTDHRGYIGATIFRKNAFIHGFHGFCSVFSTAAFSYAGTEYIGIAASETKNPAKAFPKAVKQVFIRVSLFYILALFVVSLLISGRDERLTTLSATAASPFILALMDAKIRGLPHVLNAVILISVLTAANGITYTGSRTLHSMAEQGHAPKWFKYVDREGRPLLAMAFVLCFGALGYICESAQSDTVFDWLLSISNLATLFVWLSINVSYIIYRLAFKKQGKSYDEVGYHSPFGIYGACYGAFIIILVFITEFYVSIFPIGASPDAGAFFQSYLCFPVVVIVFIAHALITRQKFRKLSEIDLDTGFSKYDRLEESDKGPMTAKSLAKSVLSFCV P40902 ISP7_SCHPO SPAC25B8.13c; CHAIN 1..397; /note="Sexual differentiation process protein isp7"; /id="PRO_0000067298" MLSQLIERSTQYVREASLEEQNRIMPLIDFGPYVNQEPGAHERIIQQLRAACESTGFFQIVNSPISPDVVKNAFRASKQFFELPFDEKLTLSKDMFSNRGYELMEDFVLEGEEDSSSPLEISGIDFEAGSYPGEAPLPPSSIGYVLPPSSLANGEGSSMFDADMTTSNAVAHGDESISNEFRESFYFGNDNLSKDRLLRPFQGPNKWPSTAGSSFRKALVKYHDQMLAFANHVMSLLAESLELSPDAFDEFCSDPTTSIRLLRYPSSPNRLGVQEHTDADALTLMSQDNVKGLEILDPVSNCFLSVSPAPGALIANLGDIMAILTNNRYKSSMHRVCNNSGSDRYTIPFFLQGNIDYVVAPLPGLGPSTAEPIAVEDLLRDHFQNSYTSHTTSLEVA P41890 SCN1_SCHPO SPAC688.13; CHAIN 1..335; /note="Cut9-interacting protein scn1"; /id="PRO_0000097629" MESIIDAHCHPTDAPQELHLVANLSVGKLIVMGTRPTDQKYVEQLAKEYPGKVIPSFGIHPWFSYYLYDDLDKDLQSSETRKKKHYEKILTPIPDEDFINALPNPVPISEFLEDARRHLKQYPNALIGEIGLDKPFRLPVGPYDARSSLPQGPLSPFYVKMEHQCKVFEAQVRLAAEFQRAVSVHCVQTYALLYSSLAKFWDGRWIPSKTKIRKMKKEEYENSLAEERKHYPPKICLHSYSGSIEQISQFSAHKVPTEFYYSFSIGINSRYKNFIQTLKGVPDDKLLAESDHHSASQIDELVRQSLNVMSEAKSWTFEDTITKISSNSKAFLKVT P53693 RDS1_SCHPO SPAC343.12; CHAIN 1..402; /note="Protein rds1"; /id="PRO_0000097212" MVQALTASLMAGALLARGIIGAKADPVNFAGIGGAAYEYNYTATGSFNQSIMPANFTPAGGIDTNDSSPTYHPFSDFDYQSLSLALYHEYIEYDLFNYGLTKFSDAEFDEAGIDAEYRHLIRFMAQQEIGHIELVTNMLGPNAPKACSYQYNFDTVGSFIDFAQTLTKWSESGVYGFLPHLDSRAAAALLLQSITTEARQQMSLRQLQGLFPYPVWFETGIPQSFAWSLIAPFIVGCPAENEKLVWQNFPALHLVSPPVHTNFTNGSFPQYPNGTYMYPAAVSTNRTFPLSLPGQSVELAWDAPGMAVGPNSSYITSTSAGTPRYAAWISQLNVTYAPLNITGNNSGVTYQPSSHLYNDSTQQVINGTNFLVLVDEAIPVTPFNITAINEHVVAGPLVYESG P54069 BEM46_SCHPO SPBC32H8.03; CHAIN 1..299; /note="Protein bem46"; /id="PRO_0000064909" MAGSLSSAIFNVLKYSGMASLAVTLIALGFLYKYQKTLVYPSAFPQGSRENVPTPKEFNMEYERIELRTRDKVTLDSYLMLQSESPESRPTLLYFHANAGNMGHRLPIARVFYSALNMNVFIISYRGYGKSTGSPSEAGLKIDSQTALEYLMEHPICSKTKIVVYGQSIGGAVAIALTAKNQDRISALILENTFTSIKDMIPTVFPYGGSIISRFCTEIWSSQDEIRKIKKLPVLFLSGEKDEIVPPPQMVLLFGLCGSAKKKFHSFPKCTHNDTCLGDGYFQVIADFLAENDINTPAS P62506 RM44_SCHPO SPBC56F2.14; CHAIN 1..100; /note="Large ribosomal subunit protein mL53"; /id="PRO_0000087695" MIFGYINKLSILNVNPFSKASQSAKLLLAVASKETSNSLYGLNLITSLASKDTNSKPSVEVVYKDGKKLTVDPTKMNIGRLTELIDDYSKTLKFKEMMQK P78750 UTP18_SCHPO SPBC29A3.06; CHAIN 1..519; /note="Probable U3 small nucleolar RNA-associated protein 18"; /id="PRO_0000051329" MEKDTEELELENAVFGNINNFSSFLDKENETFDVMMNEAPELSEDNDAQEDELEKLEDAELFMFDTGSADGAKDSVPLDIIAGDNTVKEDEEASNEIPSIWEDSDDERLMISLQDHSRLRKLRQYEDEDMVNGLQYARRLRTQFERVYPVPEWAKKQDVTEEEDEFNALSEKSVIPKSLKSLFKSSVSYINQSSKLLAPGTINIKRLKDANFQAPSHSGIRCMSIHPYFPLLLTCGFDRTLRIYQLDGKVNPLVTSLHLRSSALQTALFHPDGKRVIAAGRRKYMYIWDLESAQVQKVSRMYGQENFQPSMERFHVDPTGKYIALEGRSGHINLLHALTGQFATSFKIEGVLSDVLFTSDGSEMLVLSYGAEVWHFNVEQRSVVRRWQVQDGVSTTHFCLDPSNKYLAIGSKSGIVNIYDLQTSNADAAPKPVTTLDNITFSINSMSFSQDSQVLAIASRGKKDTLRLVHVPSFSVFRNWPTSATPLGRVTCLAFGKGGELCVGNEAGRVGLWKLAHYD P78763 YG1D_SCHPO SPBC83.13; CHAIN 1..293; /note="Uncharacterized mitochondrial carrier C83.13"; /id="PRO_0000310795" MSKIEKKQASASNLLLGAGLNLFETSSLGQPLEVTKVQMAANRTQTMAQAIKAIMSRGGILGFYQGLIPWAWIEASTKGAVLLFTSAELEYWGRRLGLGATSAGAIAGMGGGVAQAYATMGFCTCMKTAEVTRAKQAATGQEVKGTFRVFADLYKEKGIRGINRGVNAVALRQMTNWGSRLALSRFLEKPIRYFTGRTEAEPLTTGQRFVASVSAGALSCWNQPLEVARVEMQSLTKGIQHSSPGIMQTIMSIYKNNGIKGLYRGAVPRMGLGAYQTFVMVFLADCVRGYLAK P78817 YFE6_SCHPO SPAC637.06; CHAIN 1..347; /note="Uncharacterized alpha-1,2-galactosyltransferase C637.06"; /id="PRO_0000339341" MWNPKKKSEALAKFKSFPYPKPGTSNVLDSKEGDTRRKYFTKTHLHRLFVFVVLLLCSGYFLKHTLLTRPKESNVVMIFVNNIGGGVLDVKSPRQWELEKISTENKKKYAERHGYHFFVKSTGLKRRYAHEWRESWEKADYIMEAMKKYPHAEWFWWVDLTTFIMEPQYSLEKLIINRLDHIATRNITDSMEFNPKNFHEIPFVDYSEDINFILGQDCNGFSLGSFLVRRSDWTSRLMDFLWDPVVYGQKHMDWPHDEQNAIEYFYENNAWLRSGMGFVPLRLFNSYPPGACAGEGENPRFFYNQKEGDFLVNLAGCNYGRDCLDEINHYKGLAQRKRGWRKLVPFL P78890 YEPF_SCHPO SPAC23H3.15c; CHAIN 1..325; /note="Uncharacterized protein C23H3.15c"; /id="PRO_0000116729" MSYQQRANDSMNSAKQYSSSAGAVHNSDEPFSSSGAPQNRNFDTSYTSEIPSNSSRAANDMGTDIGSGDPYAGMTSDTKKGFNSVESRKKEQSDVRGGDTSYSRRHDDSSYSSNKYSTGGNDSYSSGGRNEDYSTSGGSYTTDPSRTDDTASYGQSQYNQSRKTTQGGDYGEDYSQSYPTDTYGSRQKATPSDTVGGGAYDYSSSGSHTHGGSHGTEHRGGSYGNDNTANKTRGAVSSAGYSGEGYGKGTYATDTTAEANRRAATGTRNARTTAQRNAQLAEDEHVSMGDKMKGNMEKMAGKLTRDPELVQKGEDLKTGHHSERY P78920 YGNB_SCHPO SPBC2D10.11c; CHAIN 1..379; /note="Putative nucleosome assembly protein C2D10.11C"; /id="PRO_0000185660" MSKGPGDFKKSWNGFAAQTPQNTPSSDVHLSKAALEKARQTLQSQLEDKSAHDEVSGLLRNNPAMLSMIEGRLSSLVGKSSGYIESLAPAVQNRITALKGLQKDCDAIQYEFRQKMLDLETKYEKKYQPIFSRRAEIIKGVSEPVDDELDHEEEIFQNNLPDPKGIPEFWLTCLHNVFLVGEMITPEDENVLRSLSDIRFTNLSGDVHGYKLEFEFDSNDYFTNKILTKTYYYKDDLSPSGEFLYDHAEGDKINWIKPEKNLTVRVETKKQRNRKTNQTRLVRTTVPNDSFFNFFSPPQLDDDESDDGLDDKTELLELDYQLGEVFKDQIIPLAIDCFLEEGDLSDFNQMDEEDSEDAYTDEEDLSSDDEEILSSEISD P78962 ATF21_SCHPO SPBC2F12.09c; CHAIN 1..355; /note="Transcription factor atf21"; /id="PRO_0000076534" MDFANVYLGLDTLGNEGYGASVSNGTHHDFHFNFNTFRDGGNHEVGEKRAESSDIGVYECRGPVQGPKDQTSFPSNSHNNYASIVGDASIGHYLKGPERTSEVSLPQTVNLSEISNNNDKGQPTNTPPVRSTIVAPSLYSEGSTLNHYNNGSHQVLHPQFQNGTNAPYVVQSNLMQNNVNLTGAEQEKGLDLYKNSATANNDEIFYNLESLRREGYLNSNKKQSQSPNGDYNSSDESCSNKTVASSQRRGTPGSNNVHTASNNETPDMKRRRFLERNRIAASKCRQKKKLWTQNLEKTAHIACEQSKALRILVSQLREEVICLKNQLLAHQDCNCEGIRQYLSSEAQGIMSFQKH P79060 SUI1_SCHPO SPBC23G7.05; CHAIN 1..109; /note="Protein translation factor sui1"; /id="PRO_0000130565" MSAIQNFNTVDPFADTGDDDAQPLNNIHIRIQQRNGRKTLTTVQGLPREFDQKRILRALKKDFACNGTIVKDDDLGEVIQLQGDQRIKVMEFLTQQLGLQKKNIKIHGF P79082 MGR2_SCHPO SPBC27.06c; CHAIN 1..120; /note="Protein mgr2"; /id="PRO_0000343158" MQSMQPSTVDKLKMGAIMGSAAGLGIGFLFGGVAVLRYGPGPRGFLRTLGQYMLTSAATFGFFMSIGSVIRNEDIPLIQQSGSHWNQRLLNENANSSRIFALAMQQAKSSPRKSNEVAEC P87054 MUG15_SCHPO SPAC57A10.06; CHAIN 1..133; /note="Meiotically up-regulated gene 15 protein"; /id="PRO_0000116634" MNVGDLKSANDLYESVRSIEGVTGVHLFRIRDAGILKSTMIPELDALTTISLDELNKSPTVFTKNLLQGCGGTDLDVPAELKRLVIFVCNILESCNEFTDLGSARLLRLTFDSCQLVIMYDSLFVVAITKDET P87055 YDJ7_SCHPO SPAC57A10.07; CHAIN 1..311; /note="Uncharacterized protein C57A10.07"; /id="PRO_0000116635" MLNKRLTIQLPFYATQTASSSRFWRVLSPKSRTGIALYASLILLCIFFTIFSTMSHPSLQCFSPTSLVGAQPLKNLTHLIIVAGHAVWLGGSTNGEDDSEWILEPYQKGEGKVFAQHVRSGLDLLSQDDSSLLVFSGGQTRNGAGPSSEAQSYYSLSMQINSDEGLAARRTTEEFARDSLENVLFSVARFYEVTSRYPQKITVVSFDFKRDRFLNLHRKAIKFPEHKFHFVGIDPEGGVSDATREAERKNAIIPFTEDPYACSNPLLVKKRMERNPFRRQHSYLITCPELIPLLQYCPSDPSKFFNGKLPW P87118 IPYR2_SCHPO BINDING 85; /ligand="diphosphate"; /ligand_id="ChEBI:CHEBI:33019"; /evidence="ECO:0000250"; BINDING 122; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 127; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 127; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 159; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; SPAC3A12.02; CHAIN 1..286; /note="Putative inorganic pyrophosphatase C3A12.02"; /id="PRO_0000137590" MASLAKNILQFRSKITGKLNTPDFRVYCYKNNKPISFFHDVPLTSDKDTFNMVTEIPRWTQAKCEISLTSPFHPIKQDLKNGKLRYVANSFPYHGFIWNYGALPQTWEDPNVIDSRTKMKGDGDPLDVCEIGGSIGYIGQIKQVKVLGALGLIDQGETDWKILAIDINDPRAKLLNDISDVQNLMPRLLPCTRDWFAIYKIPDGKPKNRFFFDGNYLPKSDALDIIAQCHQHWKVSRDRKQYIKNFHNESVNNVDLINKINSLKEEVSQNVSNYPSFPYFHTIPNL P87122 YDL6_SCHPO SPAC3A12.06c; CHAIN 1..743; /note="Putative cation exchanger C3A12.06c"; /id="PRO_0000317130" MSKTSCFLKKYRLILLWCILGIAYILFWTHRISKAFASVSSTSDSTVHLFERGNTLNDSNDQILLTCNDIKNITPANQCRFAKAYCKGEASGFFDYVEFYFCTINSLRFPVLSIIVGWLIFLFITIGISASDFFSTNLVTISWLLQLPDSVVGVTFLALGNGSPDILSTFAAVRVNSGGMAIGELLGSAFFIVAIVAGSVCLIKPFKIPRRHFLRDVAFLTGTILLVIMFVLHDGSLSIWQSLVMILYYLLYVLFVFFSGSSGVSVVITDENYLPVSLPVYSPVLNSFDDSDSYSSTDSELSEEAFLLPAQASRKTQKIHYINDNDPSNSYSSYQHSHVHDFIHKNNTHSNRVLSQSSGPIVRPSLLAALDFRSSNEEQHPGLRSLDPLNIQDGDLTMHPMHIRHSQSDFYPSGINTPVSGINYPNLGFSANNSVQSLVSEIFRHPTHTDEDFPLPSPSLSSLLFPTLRNFAKKSWYEKLMDVLAVPSVLIFTLALPVYQCPRLAVDPIYHMDVSNCNPSKPTWSRKLRLLQCVFVPFAFVTFSITGGNRLYIYAASSVFSILCITALYYYTDEEKPPKFLPWVSFIGFVLGIIWISTIANEVVGILRALGVIFNLNESILGLTVFAAGNSLSDLIADIMIARSGFPEMAMGGVFGGPTLNILIGIGISSFYSSISNHGNDSVIEIPHSLSITAYFLLACLLLLLIYVPLNRFRVNRVLGLLLFILYIVGTSTNIVVELLKDK P87124 YDL8_SCHPO SPAC3A12.08; CHAIN 1..214; /note="Uncharacterized protein C3A12.08"; /id="PRO_0000116637" MSSKLFQNKLLLAGIGGFMVGGLASWVVSSDAYTAYHRLPASAKHISEISKSPEAVQMIDNIYRERQRSMKMEEHPSLLQSKYPSNFLSFKDGLIPVFKTFYDPEHEEWISIGLMGKALTGYQKLAHGGAIATLLIESLETVRNLRSSQANSQSTQPRDPIPTENFDVRTPSYSINYKKPVPAGDWVIVRVKDDVARLYNSKSQLLAEALDLQS P87125 URED_SCHPO SPAC3A12.09c; CHAIN 1..290; /note="Uncharacterized urease accessory protein ureD-like"; /id="PRO_0000316577" MEDKEGRFRVECIENVHYVTDMFCKYPLKLIAPKTKLDFSILYIMSYGGGLVSGDRVALDIIVGKNATLCIQSQGNTKLYKQIPGKPATQQKLDVEVGTNALCLLLQDPVQPFGDSNYIQTQNFVLEDETSSLALLDWTLHGRSHINEQWSMRSYVSKNCIQMKIPASNQRKTLLRDVLKIFDEPNLHIGLKAERMHHFECIGNLYLIGPKFLKTKEAVLNQYRNKEKRISKTTDSSQMKKIIWTACEIRSVTIIKFAAYNTETARNFLLKLFSDYASFLDHETLRAFWY P87127 ATP11_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC3A12.12; CHAIN ?..286; /note="Protein atp11, mitochondrial"; /id="PRO_0000002534" MLPIWKLPVNHLLCHSFKSIPRTSAYAVRFAHHTSNNDDLEVKKNTVYERYERKLKSKAEELHMPVTNLLKKGQTKEREHVIPKKSFSAKKSLVGQNAKKSDLSGLNRYIDVEKIKELPTSTIEKLWRARNIGDDILSACIPKEIYEKMLSRARMYPYFVLPLPRGDKGIESHFLQWNFPNKNEAHLLVTSLLEYKLKGSYAAPHTIMLHFADLLNLKGITLMRCQFEPKKLSANDVQLLVLAIQKFYNASENTPLGKERLALLAAFSKGADFDLHKVATHMDMLE P87132 YFK5_SCHPO MOD_RES 247; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 281; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 335; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC167.05; CHAIN 1..601; /note="Uncharacterized protein C167.05"; /id="PRO_0000116744" MTSALYSGGGKSAGSLESALDEERLEVLRWMKEREEKKHRQLALQYDPIVRDYCLVKHGDSGYRMDSSLMTSLPHSRNPPIFEAIQGEQPSDIDTLNLKKVKSGPTSPSSIDRLSSPNAKAGDILASSLFSSGSPPDTTRRNSTSNLSSVSTNSDKSRTIGSNYNMLQSTKSTASQRRMSDSSTPSTTKSKEKIFSPKALSSPTQGASSNVTPESPPEKPIPSFVLSPPPVSATNEANKLSDIQTSSPSQDIPAKHLEPLHLNRSLSSSPSSEDSDLSLSSDSDDDEKKQPSKSEKTSSMSVSIKPPKIIRKGSKEQNRIAKEKASGAPLTKSKSHNDTSTEYDSNSLRRSRSNPAFANDDTVHPNTSFVSSNINNWYGSDLEELEQDVKTAKSMKVDIGPTRWIPTANRTIRCIRRGDFQTAASSSKRNCTYFLTLDLSSESLHAAEWAVGILLRNGDTLIIVDVIECDDPSARAVKDRMESEQLETLEKITKYILKLLSKTVLEVEVNIEVIHHEKAKHLIIEMIDYIEPSLVVMGSRGRSHLKGVLLGSFSNYLVNKSSVPVMVARKKLKKNKQRLGNQSRLANNLSDAIVDEVGRTP P87133 MU143_SCHPO SPAC167.06c; CHAIN 1..121; /note="Meiotically up-regulated gene 143 protein"; /id="PRO_0000116745" MIRYSLNGIRLFGSLNLFNATRILPISLGRASYAHARLFTSKVEKSGTAEESALPSVDEEEDKLNSLLGNIKVRTAQEDGVSVEEVLMHHPELLRNAPHALQQSVKEILASKEVGDAFKKN P87136 YDM5_SCHPO SPAC57A7.05; CHAIN 1..1337; /note="Uncharacterized protein C57A7.05"; /id="PRO_0000116640" MPTSGAPSNLDRANAQLSNTSSTESSSSNNSSTASGSRHVKIESNRVSLPPLKIQKGSFPAIRQPTESSTHFQSSHSVSNAHNQSPLNQSQSSANPVTFEIADEPSPSFNHSFFEKDNARDIPQQPSHSQNPSSSSSSSSSQSSQHSTHLQFQIPSNEKKSLDDPSPRRKPSFFSKSNLKRKYRYLKNPDAWNLPPSLQFIPKNLNRKGLKPVIRAAINSWIAFLLVLARHTNRVLGMSSFFVVITSILVPAMEPIAPMLWKTLFQFLLLFSAYAWTVLAAKLATVARGSPSREASLAQAVSEGFVCPDPSQGFNYCIREAVFQGYFVRPLPSIIWALFEFSAVALFIRLKMKYPPLNFPCVFSIICTAVSANMGPMYPYFYPRIGLFFIVPNCVQTGITIGCTLFILPETCNHAYNTMLCKLTEDTSSFLKRQTEMLSHSPASSHWASFSSLENEIANLKNLLSKMKSTELFLDMEFSYGRLKGEDLVSIQRIFKKTILRLSAFSYFQRLIDHNMQIYDDETIQKAGEATVSSWLNTPALSAASARTSSGRNSSESDRVSYFGLAPVNATTQDSERNGEEIRRLASKQLNVPVNNNFRTVGYASPSNASTASFNDIVQRGRSHVRTGSNNSEAPLAAKTSTTKRNGDLLEPQSPSLRSHKSRLHLPSSLGKFYKKRKKSYKPVGVLEAQQYLALESRLPFNKPQFLDSLLSILKNSSGDLFDQAIYSLDALNAWLVELNHDRIKKIFSKRDQKAAGRDRLKLIKLHYDHLSQALHEYEREKCFDVRKPYESLFQNQDVQQFYMHSLRSLFVVYYYESHLMQAVRGILQILETVIDLEERRPIRRLWWPLRSIRRSLLSQLTGHQGDYDENIHNDVDKDMNQSSTQPRDPDADHPSSLYHICGYRLTKFFKSIFRPMNVFVLKVGTLAVICTIPAFCRSSAGWYYRNRGLWAVILAIMSLQRFTADTVYGYLMRIFGTFFGAILGMVIWYTGSGHGLGNAYGLAAVWGAAIPFIQFIRVHFVILTPMPAVIFCVTAALTVTYSWKSNHEPGVVTLGIGWDVAYRRFLTVAAGITVAFIFSFLPQPRTAKYAVRKNIGNTLIDIGSIHCEISNFARRPVHNHIDPDIQSKVLNLSNTIQSLIGRLNMVNFEPSFKGRWPMEKYQLLCKTQLELVDLLNSLMTTITTLEDRWLFALLYRVGWLDHKFVADQLAVLYMSSNALQTGNPLPQVVPSPLVDRFFTTSGDVFLPPGLNDAPVPIPKAMEYELLNNMQYLNFAVGCTIAYAVVNHIDRIMFITKSLCGEIFEIDKWPFHFDDEYLYTCHPTNSPDQRKSPHDLV P87137 YDM6_SCHPO MOD_RES 251; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 555; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 557; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 758; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 760; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 764; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC57A7.06; CHAIN 1..929; /note="Uncharacterized protein C57A7.06"; /id="PRO_0000116641" MARKGKVNTLPQPQGKHQRKGKKQLENKILHSYEEESAGFDSEELEDNDEQGYSFGVNSEDDEEIDSDEAFDEEDEKRFADWSFNASKSGKSNKDHKNLNNTKEISLNEEDDSDDSVNSDKLENEGSVGSSIDENELVDLDTLLDNDQPEKNESNTASTIRPPWIGNNDHATDKENLLESDASSSNDSESELTDSADNMNESDSESEIESSDSDHDDGENSDSKLDNLRNYIVSLNQKRKKDEADAESVLSSDDNDSIEEISIKKVKYDPHETNKESEYNLIGSSEKTIDITDLLDSIPMNEQLKVSLKPLVSESSSISSKKLDAPLAKSIQDRLERQAAYEQTKNDLEKWKPIVADNRKSDQLIFPMNETARPVPSNNGLASSFEPRTESERKMHQALLDAGLENESALKKQEELALNKLSVEEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNRKEKEMALIPKSEEDLENERIKSEEARALERMTQRHKNTSSWTRKMLERASHGEGTREAVNEQIRKGDELMQRIHGKEISEMDGEDVSEFSDSDYDTNEQVSTAFEKIRNEEEPKLKGVLGMKFMRDASNRQKALVQDEMQAFEDELAGVPNEDDTSQKGEDGVPGVLIGNNTGRRSFKPSEEAAKLSLPSRKNPFVSDSAVLKVNKPEMKEGQKKAEARKKKESPLEATEETNPWLQVPDQRTSSAKKLDKNSSKADKKNHKLKMDKVASLQELVEEPKVQPDLIFEEKAFESASEAESDVDVSVPMLKPTKGRLSIKQRELVAKAFAGDDVVAEFEKDKEDWVQEDAPKEEDHSLPGWGSWGGVGVKQRKTKPKVKKIAGLDPSKRKDSKLKHVIINEKRNKKAAKLTADSVPFPFESREQYERSLNLPMGPEWTTRASHHKAVAPRVVTKRGKVINPIKAPN P87138 YDM7_SCHPO SPAC57A7.07c; CHAIN 1..308; /note="Uncharacterized protein C57A7.07c"; /id="PRO_0000114625" MLMLDGGSTAILPKLPESISESRLWTSEALVRYPEIVVKHHEEFLKVCDIISTFTYQLDASIYDEKVEGVPLKQVYANSIGLPVYAREHLGLPNKYIALCLGSHAATIPGCMEYKMIYDKPTDFEMLYNFHKNRIEAIQASNPKAFEKIDFIAFESLPHVTEAEVVCQLIQDMKGWSKRCWITCTCPERSTIERVSSIISKILSINHDSIWGIGVNCFHLSLLEPIAKMLSSLLPSNITAILYPDGRGLYQNPDGTFSPGSTDHPAPSPEEWSTITAKYSNLHNGNLILGGCCETNYNHLSLLREKTK P87143 YDMD_SCHPO SPAC57A7.13; CHAIN 1..565; /note="Uncharacterized RNA-binding protein C57A7.13"; /id="PRO_0000303889" MKDYYSENGFEEIFEEKGSTSSNISDNCASRDYDVNISSDNPRLLDSYRPKGNYGRDRNSPLSRHIGVPNQEIILQGLTPEILEEHIELALYATGAKVSTVTLIREKETQKSRCFAFAKFVSLQDSKDWMEANFPTLVIDGIDVSVRFSRAAREQIEGWCCQNCDILNYSYRESCFKCRVPRNQASIAIGNHKISKRNGDMDVSDVPSVYLILRNLDRSLSEETLWKGLSKLEIDVQRVFMIRYKFNDAFCGYAILEFKDVDESAKALMKARTYPGKGFTLASRKVSVDYIHDGVLIPAYTESARWQFPTKTGYLVYWDPELYCSIYVPEGIDTDQFKPIEVNKKPKKEKRARSSNYIDVPASKKVATSLQRWNDAQKELKDNIPDLSEEEEKLLLHFVWKSALICVLCERKFQSWGHVVKHITQSIMHNNNLKNHELVSSAELLMHRVRQTESVDYRDRATERRIVPAASSDTIVEAKKSSQGSSFHSTSNVSMKMLNSMGWNKGSGLGTNENGIKEAIQPTMYLPGVGLGNKGSKIQINMTPVDRVKDRARSLYFQNDKNNNL P87144 SYTC_SCHPO CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; SPBC25H2.02; CHAIN 1..703; /note="Threonine--tRNA ligase, cytoplasmic"; /id="PRO_0000101124" MSAAAVKGVQASLDNLSLEIPFIQHRLDLFDKLQKEYKESLATKPREEIDITLPDGKVIKGTSWETTPISIAASISKGLADRVTVAIVNGEPWDLTRPLEASCTLKLCDFNDPEGKRVFWHSSAHILGEATELSFHCHLCIGPPTDEGFFYEMGIDNGRVITNDDYSSIESYAKQAIKQKQPFERLVISKEGLLEMFRYNKYKQYIIQTKIPDGASTTVYRCGPLIDLCTGPHVPHTGRIKSFAVTKNSSSYFLGDAKNDSLQRVYGISFPDNKQMQEYKTFLAEAAKRDHRKIGRDQELFFFNEISPGSCFFLPHGARIYNTLLKYMRYQYSKRGYQEVITPNMYNVNLWKTSGHWNNYSENMFSFDIEKEKYALKPMNCPGHCVMFKSRDRSYRDLPWRVADFGVLHRNEFSGALSGLTRVRRFQQDDAHIFCTPDQVRSEIEGCFDFLKEVYGTFGFTFHLELSTRPEEKYLGDLATWDKAEAQLKAALDASGYKWELNAGDGAFYGPKIDITVFDALKRQHQCATIQLDFQLPERFQLEFHAPASAEEAKESGNNNKYTRPVMVHRAILGSLERMIAILTEHYAGKWPFWMSPRQVCIIPVSAAAYNYADKVHNILSEADIFVDTDKSDNTLPKKIRNAQLAQYNFIFVVGAEEESTNSVNVRNRDDPKKQSKGSTVAVEEVVKKLLKLKESKSLINDL P87145 VAC14_SCHPO SPBC25H2.03; CHAIN 1..811; /note="Protein VAC14 homolog"; /id="PRO_0000116490" MDNLLVRGLTHKLYDKRKATAYELERVVKGYLENDETEKIRAVISQLANDFVYSPARGPNATFGGLIGLAAVAIALGPKIDSYMESILLPVLYCFNDSDSKIRYYACESMYNIGKVAKGEVFRYFNLIFDVLCKLFADTEITVKNGAELLDRLIKDIVMQQAATYMSSAEDIKNFKEGPVSSSIQDVPVMSTEQPRMHTFSLSELVPLLSERLYVINPNTRMFLVSWIRLLDSIPDLEFISYLPFLLDGLMNYLSDPNESIRIVTSNCLYDFLREIQKIAKVKYHILQRDEESEPDFFDSMVRRNMSDAELKEISDYVESSLRDGSFILEAHIQIDYKRILEIIIDHLGSSVPLIQEKALKWLFEFIYIAPKDVLLQIPKVLENLLPLMSNDENMRQSAKDLSQNLVILVSKIMDIEFSGSETNNKDNSLSVDFRSLIEVLQKLLSNDNEETRLCALEWVLLLQRRTGGKLINMHDPIFQTLLLQLSDPSDLVVSRTLELLAHIAISHKSVNLVPFLKSLLQMFAEDRKFLNSRGNLIIRQLCNYIEGERVYTSFAGILETEENLELASIMVEVLNNNLFTAPELYDLRKKLKQSAPKLQNIFTTLYTAWCHNSIAVFSLCLLSQNYEHAANLLSVFAEIEFNIDMLIQLDKLVQLIESPVFTYMRLQLLEPEKYPYLHKALYGILMLLPQSSAFRTLRDRLQCSSTPRTNTILANERLPRSRRDDPYWTDLLERLKAVQLSHQNNYREPIRATRLALAGALPSTPTATTISTTTSASGITTTASNSRDSFITRLPPTAALSTGARKKPKQ P87149 MRS2_SCHPO TRANSIT 1..49; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC25H2.08c; CHAIN 50..422; /note="Mitochondrial inner membrane magnesium transporter mrs2"; /id="PRO_0000043248" MVLIVGFNLRTSIASFSPICRSLFLFPKYRSRIIRPVVLLEKPFDKHFYATDSNPLITGFPETSKNCPPSVAATKNRLLMNCTEFDDHGNVRVISGDFKKMDLCKQNGLLPRDLRKLNTSINSIVPVILVREGSILINLLHIRALIKANSVLLFDVYGSQHSHSQSQFIYELEGRLKQKSSDFGWLPYEMRALETILVSVVNTLDSELHVLHNLVSDLLADFELDINQERLRTLLIFSKRLSGFLKKATLIRDVLDELLEQDQDLAGMYLTERLKTGKPRDLDKHDEVELLLETYCKQVDEIVQQTDNLVGNIRSTEEICNIMLDANRNSLMLLGLKLSAMTLGLGFGAVVASLYGMNLQNGLENHPYAFYITTGSIFAFAAFLSSLGILKIRRLKRIQMALYHRCNLPISLDPRSLRPPYL P87150 MIC19_SCHPO SPBC25H2.09; CHAIN 1..162; /note="MICOS complex subunit mic19"; /id="PRO_0000116491" MGNQQSQPEFVLRAPTEFSEKFVRHLQESTETDTSRYMDMENYIQKRVQDELKQLQLRQKKAIDAIQEEEWKSNAKTIKDSQGSLDSNLLSAEFRSFQEKLEKQSSINDKELKIKLKEVESIRSDLLKCMSEHPDKSLICHPLAEKFAILASKLHNPKVGSV P87151 YB0A_SCHPO SPBC25H2.10c; CHAIN 1..287; /note="Uncharacterized protein C25H2.10c"; /id="PRO_0000116492" MSALSEILSYLIISFETSFTFHLEFKYKRTGIEKNESGVLVTVPRGKERQSSSEILDVFTQHIATLWPETQSSDQENEEEGEELEDAVAKEINSLQKKNKKELLTPIMLDMPCVYFVKTRPPIDPVRLVEFTCEVGKTKKMTRYTQRLIPIVRTTGVSLDDLEELAKSLIDPLFHEGQEGIKEFAVQANIRNHTVLKKDDIYRTVARIVGKQHMVDLKNFKLLILVQVIKNIIGISIVQNFEELRRFNLNEVYKQPENTKSIPNDSKLDNFDRDKNQIINDKAEHAE P87156 TSR4_SCHPO SPBC25H2.15; CHAIN 1..396; /note="Probable 20S rRNA accumulation protein 4"; /id="PRO_0000116493" MSQKWVQTQAWLGFPDVPISQEDKPDEYSTFLGGFPVFFDGCSLNPNIIKCGNCKNLCRLLLQCYAPLEGDNLKERALYVWGCHNPSCRRVPNSIVCVRGVRLPLKSDIEAVKSPKAISHLEEKKSSPKEKKVNPFAITSESSRGLNPFSDATSANNPFSLSTDVNPSKPSSNVFSKPSFAAKAQQSITDQQKTQAKTKTKHIALTTSGMSVHPPVTETYTYPVTEAFQGMFLGLDLEYVPQNKVNSKKDDFSTFKNYTPYLNDSSEAWEKESYEKSPSVYEKTFRLFSEKISHNPTQCLRYERGGTPLLASGRDKLGQQLKSVTNFGKSPVPLCPLCKSPRLFEMQLMPHAISILNDEIAEWSTILVATCSMDCNPPINKDRVGYAVEWVGIQWD P87167 BUT2_SCHPO SPBC3D6.02; CHAIN 1..390; /note="Uba3-binding protein but2"; /id="PRO_0000065026" MQLLNSFLGFAASIAVLASSADAAPTLYKRKSKSNTNTAKSVAILDGVGVNNTFGVISYREKFPMDYHIWHTAPSTGKTYLQPWNDAVEPSTYYIDEGTFLRTGLKFAYIGDNMDLAFTNHTDWKASKHDDGTHRVDLSQRKPANNFMATQRCGKLDPFGYQLKRSKKVFQACGTQVFVGSGRSIDCQWMDSVALNLSRYYGNTEALSSLPLPRNLSADIPAKSSRLFPHGIYNFNFSAPNKRMQRFTASEATTVNGQNQSVYLTYDVPYGRSLYYYTSCALEFRFTNEFFPMDVTPNDGSAQFVVYNMSGNPKKQTTSSKGPTRLYEVARFNCTTRGCEYTQNIPCPRAGHSHTYELAPASPNTSISWIQSYSPRIGVTLQVYSNANFD P87172 GPI3_SCHPO CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705, ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198; SPBC3D6.07; CHAIN 1..456; /note="Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit"; /id="PRO_0000339138" MVSDFFFPQPGGIESHIFQLSQRLIDLGHKVIVITHAYKDRVGVRYLTNGLTVYYVPLHTVYRETTFPSFFSFFPIFRNIVIRENIEIVHGHGSLSFLCHDAILHARTMGLKTCFTDHSLFGFADAGSIVTNKLLKFTMSDVNHVICVSHTCRENTVLRAVLNPKRVSVIPNALVAENFQPDPSKASKDFLTIVVISRLYYNKGIDLLIAVIPRICAQHPKVRFVIAGDGPKSIDLEQMREKYMLQDRVEMLGSVRHDQVRDVMVRGHIYLHPSLTEAFGTVLVEAASCGLYVISTKVGGVPEVLPSHMTRFARPEEDDLADTLSSVITDYLDHKIKTETFHEEVKQMYSWIDVAERTEKVYDSICSENNLRLIDRLKLYYGCGQWAGKLFCLLIAIDYLVMVLLEWIWPASDIDPAVDRVSSTFKISKQNFDESLVLTDPKKKTKIKTACLKDAQ P87216 VIPI_SCHPO MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 177; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 230; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 232; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 235; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC10F6.06; CHAIN 1..257; /note="Protein vip1"; /id="PRO_0000082004" MSNQVIVTNISPEVTEKQISDFFSFCGKVSNISTEKSGETQTAKIQFERPSATKTALLLQDALLGQNKIQITSEDGGAASTTDQGGAGGDQAARQEDKPRSAIISELLSRGYHLSDVTLEKSIQLDQSYGVSSKFKGILESALSGVRSVNERYHVTEKANEVDNKFAISDKLNRTSSLVSTYFHKALETAAGTSAGQKVQNAYEDGKNQLLGIHNEARRLADAKNQAEGTASPASSTPTAPAEKEPTAPTTESKTTE P87229 YC03_SCHPO SPCC4G3.03; CHAIN 1..347; /note="Uncharacterized protein C4G3.03"; /id="PRO_0000343217" MTVDNRCSNSSLCLRNVTPKQHPARVCSNHWQLKNLISTQNTGEESNPIYYTNSVFVWKIYPNSEKVVQVGQGLSFKPLSLLGKCGYIAAGGQLGEFDYWSPTSKQTHMKLCDQHNNGIEIHRRNCDSHAEALISSNDHTIKVVDLEHGLLRKQLHFPVNMNHASVSNDGRFMVCVGDSPQVFFYEIDRSGEYHLRHTTVADTTDSSFCTSISQRNELFAVASQDSSLSVFDVRYLRTPMLTKTSSRPDPNGSIRSCHFTPPNGGPLDLLLYSEGFSYSHLLDLRTGKDVELVLPSEDRFFSPASQDIFGSCFADDGSSVYVASATHLYEWNIDKRSRICFPSYQLL P87232 RM04_SCHPO TRANSIT 1..68; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC4G3.06c; CHAIN 69..144; /note="Large ribosomal subunit protein uL29m"; /id="PRO_0000372411" MRSTLASAQKAAVRIPKGFVFPVPKVKSAPKVSDTHPLWNFFRDKQALPPPSEEAKFGRAWAAEELRWKSFNDLHGLWYNCLREKNLLFTQRAEMKRLQLTIPKASNERVLAVNKTMAAIKFVLWERQRAYTSAKQLEKQKGSS P87237 YC0C_SCHPO SPCC4G3.12c; CHAIN 1..821; /note="Uncharacterized RING finger protein C4G3.12c"; /id="PRO_0000310481" MGQTNSRHSLIETDEPTTSSRVSMLVDRVKLLWKRYTTPLSTEDGSREAHFAVPSENYADTPSRNTPNSSNGFPSETLVTSSAHCSTQPHKDEAYSHHGYSSTMALDDSSLAQTYHEYEEGTSGNSPLRRAIGSYDFLHPRPSGNSSRLDRNSSRPFTSSFHSAPFLSSYGSSNDPSQERVNEYSLPSNSNSTYTTPLQSINNEHPLPTVLENNALLNNSGNSPSLINHLRQYLNQDFSRLHQSPSPIPNSNDNDSQTRRSSWSSIASAFNDFPEEFPNASNPEAHSNFTPLNGNDESTVNMLSRLLSAAAIETVASIMNSEARNMDSQNMANGEPSRFRSVDGSFEQFLTDLRSGNLTNVLQNSSQNGNDQISSDPESNSSDLQYLRMFRFPSFHQSHNQPASNNEASDTNGPALVPVLIVCMRSISETSEDHAPTMTQENQSLHNESRENISINDITERMAQSTEFSTDLPPTFERSNSTFSHPEPTRSDFSQAFTPVSDFPANLFPGSRNLFPTSNSGNQSTSSFSRYNQPTVSVDLRNSSILRRAQEPVNGSTGENHIGDDYISSLLDSSNSNSQRPFSTVPSESNVFSRNASGNFSMSQTHQPTTDNTSSFSTQPGRLSTGLHHFPSDRDLLSNQTRRSSLARSYRFEEQLSVDDNTSDFSTLASNGAADMVTQTHSEGTFSNSTHGDWLIYVFGGLFPEHHPVLSTVSLFSDNPMYEDLLALTTYLGPAKKPVASHEDVKRSGGLFAYFDDASLSSADSCLICLETYTNGDICRKLQACKHFFHQACIDQWLTTGNNSCPLCRAHGVTTQAEEEN P87238 CUE4_SCHPO TRANSIT 1..29; /note="Mitochondrion"; /evidence="ECO:0000255" SPCC4G3.13c; HELIX 181..212; /evidence="ECO:0007829|PDB:6OP8" CHAIN 30..215; /note="CUE domain-containing protein 4, mitochondrial"; /id="PRO_0000310344" MQPEQLAGCAVVLTVTVLTLRWMFRVDKGGEVSESRTSSSGVDNEPPVNSEHVHLVKTVFPHLESSAIAYDLQKTKNVDATIENALRGQPLPLPPRNSSLYARFPLSAGAGASSHSEETTPSHEVTSNVSSGSSASSLASNEHRSLIETYNLSSRISSSDNSSSSTGNEEVRNRSKLPSSKKEREELFRKRKEEMILAARKRMEGKIKGEKQDKN P87293 YDN1_SCHPO SPAC16A10.01; CHAIN 1..830; /note="Uncharacterized protein C16A10.01"; /id="PRO_0000116642" MGVQLKLDPNSKNWLRQPDQQPIQDSICTLPGPGSLLKKKIRKTEFRIDNGLLGNTSPIINVESKIPFHRRANSTPEESRKRVSFSLTSNDGAKSDRSSQKSSNSRKSIRSQSRSRSSSVGSDSQASIQSGTNSEVVSDDEEDGNFASIPELHEDNEYHSNLATSSNPFSDGSSSKSASLTASSAAASPTVSFSPASTSENLTPTSSKSLASNTSLVQSFNSASRSSSISGNQYTYNLLGKSTDESPKITISAGTSMSHFPSASSKLIQMRRHAHMNSEKCDPELLSHNEYFPMMKRGFISRFLCLFVSRDANVYIGPLESSHAKPYRPFGSFVSRFTNRVASDLESQIPDALEAVLTQNNDYDFNSFLHNMGYSRCYVDENYHITIHVSSYERRVEFMLAVCEAMMLYGSPSHKIQQSLRIASRILQLPATFLYLPDCMFVYFKKLEQYSPDVFVVRVTSQTDLNRMVLVNEIFRRVMRDKLSAEDGTEVLRNITSFRPLYRDWLVAFMHGVASASILPVVYGGGWRDMLIGFVLGLLLGIFRVYINPRFFLFDSLFEVIISIILSFLGRAFGSISRYDKPVFCFAALVEGAITLILPGYVVFCGVLELQSKNIVAGGVRMLYAVIFSLFLSFGITIGSALYGWMDKDATDADTCMSIIAVSPYWYILLIPIFTLSLLIVTQSHPRQWPIQMFVACCGYVVYYFSSLHFGASQISSAIGSFAVGCLGNMYSHFIKSSSFAVVLPAIFVLVPSGFAAQGGVSAGLDTASQITSKNTTTNTTTVTTENSQNSSLEFGFTMVEIAIGIAIGFLASSLTVYPFFGYRRKNMML P87299 MUG74_SCHPO SPAC16A10.08c; CHAIN 1..285; /note="Meiotically up-regulated gene 74 protein"; /id="PRO_0000116643" MKKHKSSIKCFKIDQISQQPETDLVFTKRSECKVKDELFSDKENSILCKQLKELDLVVSSNKEFLNEKTSDQISFLKPRETVVEKKLANGSIWPNETSHLDKSRDLSSHSNGLDALAMTPYIVKENNKTHLSPRGNYPSEAEKSCDFYGQPLHFYRENTSPCLYGSSLSNVFTEKSSDYRHGLGSPTSLVSSNTASKLHLGRKDIVKLSELRNCINSSKDSNQIQELENLLRKEKQRNTEHEKIIRRMKKELKELHSQFNFAKKLFISALSANQDILDKMNDEFN P87304 YB22_SCHPO SPBC31F10.02; CHAIN 1..161; /note="Putative esterase C31F10.02"; /id="PRO_0000156700" MAINSSGTKVLSFVRSVWQDFVNTNGFDAHVVSDIQIISAVPGFVECSLKLQKHHLNRMGNLHGGCIAALTDLGGSLALASRGLFISGVSIDMNQTFLQSGGTLGSSILLHAKCDRLGSNIAFTSVDFLTSSNEVFAKGRHTKFVRNALGDPRNCLDLAED P87307 MUG37_SCHPO SPBC31F10.05; CHAIN 1..217; /note="Meiotically up-regulated gene 37 protein"; /id="PRO_0000278498" MKRHANRIGEEFSQTVQFIKSETTLKQKKTKIDVQNVYGLDRNTKNLEKRDIQFLENDKLDLNSHENEGEKTKTETVPTRKQFPKVGEFNSAIHGLSSESVLRTCFRVGEVLAVFRMKRRDVCIIVEFFAKVRSAKKVGNVILYYFEDAFRGQKSPAIFAKYYSCCEISPLLTKPATMIRVVGIVSHAEKILKVIHIASSDLDELWDTYNMVLYETL P87313 TMA20_SCHPO SPBC31F10.12; CHAIN 1..181; /note="Translation machinery-associated protein 20"; /id="PRO_0000316591" MFKRFNSREDIKGTTPIKSSIQRGIKAKLVQAYPNLKQVIDELIPKKSQLTQIKCEDRLFLYTLNGEIILFQHFDGPIIPSLRLVHKCPDAFTQVRVDRGAIKFLLSGANIMIPGLVSKGGNLPDDIEKDQYVIVTAEGKEAPAAIGLTKMSAKEMKETNKGIGIENVHYLGDNLWKTILE P87316 ATP5E_SCHPO SPBC31F10.15c; CHAIN 1..67; /note="Putative ATP synthase subunit epsilon, mitochondrial"; /id="PRO_0000071666" MAFAWKKNFSYSKYASICSQTVRQALKPEIKNEVKTHGDAEFLYTRWKNGAQEKTESYNSAKSADKE Q09189 AZR1_SCHPO SPAC1556.03; CHAIN 1..299; /note="5-azacytidine resistance protein azr1"; /id="PRO_0000064784" MNVTRLYFRVAGTKQFARYVHKYAAYSSTSFQKKKSHFPSPATLDHPDAGEDAFINLRNENYILNAVFDGVGGWANVGIDPSIFSWGLVREIKKVFNNSDEFQPSPLTLLSKAYAALKKSNTVEAGSSTACLTLFNCGNGKLHSLNLGDSGFLILRNGAIHYASPAQVLQFNMPYQLAIYPRNYRSAENIGPKMGQATVHDLKDNDLVILATDGIFDNIEEKSILDIAGVVDFSSLSNVQKCLDDLAMRICRQAVLNSLDTKWESPFAKTAKSFGFKFQGGKVDDTTITCLLIKSKNYE Q09329 MLO2_SCHPO SPBC4.05; CHAIN 1..329; /note="Protein mlo2"; /id="PRO_0000096500" MEETAHELTVKQYVEQQRELEREAREVLPYSFDTCTYSMGYLKQPLYACLTCQKASGSLNAVCYSCSISCHADHDLVDLFNKRHFRCDCGTTRTHSIPCNLRKSVDECGSENDYNHNFEGRFCICDTVYNPETEEGTMFQCILCEDWFHEKCLQKTNKGIAIPDAETFEWLVCSECSEKYRDHLLNQKHESIAGTERAPLFLSENFRENLCPCESCISLRNLEMPMLVAEEPIYEPPEDSEDGISEMNEDPSESGEMIEQVISSTMNDVLRILDRLPRVQANESVYAYNRLKSELTDFLTPFARENRVVTKEDISNFFLERSRISKNLR Q09672 PANB_SCHPO CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453; EC=2.1.2.11; SPAC5H10.09c; CHAIN 1..267; /note="Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase"; /id="PRO_0000184926" MSLKQITISTLRQWKLANKKFACITAYDASFSRLFAEQGMPVMLVGDSLGMTAQGHSTTLPVSVEDIAYHTKSVRRGAPNRLLMADLPFMSYSTWEDACKNAATVMRAGANIVKIEGGGNWIFEIVQRLTERSVPVAGHLGLTPQSVNIFGGYKIQGREQSAAARLIENAQQLEKFGAQLLVLECIPESLAEQITKTISIPTIGIGAGKHTDGQILVMHDALGITGGRPPKFAKNFLSGAGDIRTAIQRYIYEVEQGLYPAEEHSFQ Q09674 YA01_SCHPO SPAC5H10.01; CHAIN 1..301; /note="Putative hydro-lyase C5H10.01"; /id="PRO_0000217174" MTTTSIDPPVYATVDVIREPKAYDGMPKKDECRLPSYSERAITKPVEARKLIRNRLMTKSTTGWCEGYIQANLLVLPAKYRDDFVNLCVRNPVPCPLLGETEIGKPTEFKPEALAKQSNVATDIPFYCEYINGKFSRELENISKEWTEDYVGFLIGCSFSFEAALVAENFIPRHLPTGDAPPMFITNIPLCASGVFTGTFVVSMRPYPEKDLERIRKITSAYTNCHGEPVAWGWDGAKKIGVKDCGKPDFGVPVEFKEGEIPIFWGCGVTPQNVVMMSKLPEPVYSHKPGYMYLTDLTHNC Q09676 YA03_SCHPO ACT_SITE 14; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250"; ACT_SITE 167; /evidence="ECO:0000250" SPAC5H10.03; CHAIN 1..219; /note="Probable phosphatase SPAC5H10.03"; /id="PRO_0000116378" MTNNLKKTVYLIRHGQAQHNVGPDEDHNIRDPVLTSEGIEQCEALAKELESKQIPIDGIVCSPMRRTLQTMEIALKKYLAEGGPDKVPVYISPFFQEVGHLPCDIGLELDKLNKLYPKYNFQSCQDGIYPEKRDIYASDVTISAIRSKEALEYLAALPQQQIAVITHSAFIRFLLKKMVKAADIDFLPPQLSFKNCEFRIYDLVQTTTGELKLVESSSA Q09677 YA05_SCHPO BINDING 15..22; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P0AEY7"; BINDING 68..71; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P0AEY7"; BINDING 107; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P0AEY7"; BINDING 123..126; /ligand="FAD"; /ligand_id="ChEBI:CHEBI:57692"; /evidence="ECO:0000250|UniProtKB:P0AEY7" COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P0AEY5}; SPAC5H10.05c; CHAIN 1..196; /note="Uncharacterized protein C5H10.05c"; /id="PRO_0000116379" MKILLINGAQEFAHSQGKFNKTLHNVAKDTLIQLGHTVQETVVDEGYDENTEVEKILWANVIIYQWPGWWMGTPWKLKRYMDEVFTAGYGQLYANDGRSSKNPTQNYGKGGLLHEHRYMISCTWNAPAAAFEEVGNFFDGRGVDGTLLTFHKANQFLGMKPLPTFMVNDVIKNPKVDIAVCAYKDHLNDVFGSANA Q09680 YA0C_SCHPO SPAC5H10.12c; CHAIN 1..371; /note="Uncharacterized protein C5H10.12c"; /id="PRO_0000116381" MSRISLSNFLSLPRYKFLLFSVVLIIVMTTLVFNGHDYKQTLNDRLTSLKNNFVEENDNAVLKEEPGKYTYMSLFTMPSTEEDYYFNATRVLIHRLKYHPTTKSKYPIHILALRGVDEWKIERFRKDGASVIVIDPIASSDIVYDTSSFSQEISARYEQMFSKLRIFEQIQFDKICVIDSDILIMKNIDDIFDTPYMYQQINTLNYTRLPSYTKPDDDTVYHFNEDFKEYGASRSEFYPYLLAAVSDRGEHHSIPPEDTPYFNAGLMLIRPSELHFNRILKIGRFPYMYENAKMMEQSLLNLAFSLDGWFPWTRLDPYYNGVWPSIDERPLLKTAHGKFWNIGSSEFAPVYLADWYAAYGEMLSFHKYETH Q09681 GMH2_SCHPO SPAC5H10.13c; CHAIN 1..346; /note="Probable alpha-1,2-galactosyltransferase gmh2"; /id="PRO_0000215167" CARBOHYD 64; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 142; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 224; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MALMLSRIPRRFFFLFLTVGLIAGAFLYSLIYFVDVDLVSKVNQLYDQQIAPMLSDAIGTPSVNHSFELAPLDSHLVATSTTFHEASYESEPQQNPASQNIVLLLVSDGHTSYNNGANTFEEAIQNRVDYSTKQNYNFEYVNVTGLPIPAVWSKMPAVLQTMKKYPKAEWIWLLDQDAIITNTHLSLQDSFLKPENLQKTLITNTILTKRPINANGDLRYTPSNYSLKDIENLMVIISQDHNGLNAGSILFRNSPATALFLDIWTDPVVAECAKANNEQDMLGYLISKHSQLASLVGLIPQRKINAFHEGPENMEWQKGDLVIHFAGCWVENRCDELWQKFYALID Q09682 PSA3_SCHPO SPAC13C5.01c; CHAIN 1..248; /note="Probable proteasome subunit alpha type-3"; /id="PRO_0000124115" MSRSYDSRTTIFSPEGRLYQVEYALEAINHAGVALGIVAKDGIVLAAEKKVTSKLLEQEESAEKLYHIGDNMLCAVAGLTADANILINYARRVGQQYLQTFNEEMPCEQLVRRVCDLKQGYTQYGGLRPFGVSFLYAGWDHIRGYQLFQSNPSGNYGSWQANSIGGNSTSVQSLMRQEYKDDINLDEASAMAVKFLSKTLDSNSLTHEKIEFATITKDTTKNKMVCKIWKSDEINEVLNKYQETQRQS Q09686 YA14_SCHPO SPAC13C5.04; CHAIN 1..248; /note="Putative glutamine amidotransferase-like protein C13C5.04"; /id="PRO_0000116382" MDYHIAILNADTPMVEITSAYGDYADMVKSLLQSGSEYYSTEWNLVTKTYEVYKNPNDYPQKEDFPNINAIIITGSKASATSDAPWIKKLISFVKDVLFKYPHIKIVGLCFGHQIVAKAAGVPIIQNPKGWEVSSTVVQLTENGEKFFGRKVININQMHQDMAVDVPEGFELLGSTEDCEFQIFYKPRQALTFQGHPEFSTEVVNTMVKVLRGTEVFTEQQKEEALKRSENPADNDFLAVSIVKFLLE Q09688 MU121_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPAC13C5.06c; CHAIN 24..177; /note="Meiotically up-regulated gene 121 protein"; /id="PRO_0000014189" CARBOHYD 121; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKGFVVISRFILTLFILITPGLAGVVNYAENSEWNVPKYGNVLDSNCQGQKPVTFFGSVTEHVSNSWWIKLYDYMMTFISGEKLCMQNVAYEFEDISLCMDVVGSKCIPTLQSTDIEKVVNSTSAYLENSESDLTLGCFQIQRFQEESTLYIRALKSSEPVSCDTVRCIHFNHIPYV Q09695 YA22_SCHPO MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC2F7.02c; CHAIN 1..325; /note="Uncharacterized protein C2F7.02c"; /id="PRO_0000212578" MKSTKTQPSPEREREPSFFQKLFGNLCSCFQDASIDEKPTYTPAKPVKKAPSVVQPRRVSRTLRSSESVHTNHGPERVFESPTPARTSISLESAISPNGTTNEQDIAQQGDMIDSHVHFGEQPTEPIDFADPPLPEVKRYGEGNWLLPPIAKEDEGKKCLILDLDETLVHSSFKYIEPADFVVSIEIDGLQHDVRVVKRPGVDEFLKKMGDMFEIVVFTASLAKYADPVLDMLDHSHVIRHRLFREACCNYEGNFVKDLSQLGRNLEDSIIIDNSPSSYIFHPSHAVPISSWFNDMHDMELIDLIPFLEHLARVPDVSTVLNLQL Q09705 RT24_SCHPO TRANSIT 1..39; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC2F7.15; CHAIN 40..258; /note="Small ribosomal subunit protein mS35"; /id="PRO_0000116385" MAFNPLLSLLKADAIFLGQLSKSSFCATSRAFSVFYFTRFKRSAYVSAPFGIEPHDEKELKTIDDNVHSNNLSWQKIQEHEVIRELYRKAAYELPGLTPYTQSFKKPADSQIFRFESDVQMSSFEKMNPKVVVTFKVTNIPLLEEKQRHVLRLLVGPRYNPEEDLVRISSDKYSSALQNKYHLIKILTSLIEESKRNAEKFSHVPLNTGHWKYKKCDKRMPQEWLADATTLTSKKKTTIGKQSHNTVLERESIATTDE Q09707 YA39_SCHPO SPAC18B11.09c; CHAIN 1..207; /note="Putative acetyltransferase C18B11.09c"; /id="PRO_0000068744" MTRTRVQKMIPKTIEYQKMISGQPYKAYDEELTQARCNAKKLMRRFNDTMGDLENVGPAELIKRRAELLAEVFVFDESSAPEIEPPMAFDYGFNVHFGKKFFANYNCTFLDVAIITIGNNVMLGPNVQLCTATHPLDFKARNSGIEFGLPINIQDNVWIGMGVIVLPGVTIGEGSVIGAGAVVTKDIPPNTLAVGSPAKPIRKIENE Q09708 YAGG_SCHPO BINDING 36; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 81; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 300; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 302; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000250"; BINDING 321; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 323; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250"; BINDING 375; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000250" COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000250}; SPAC12G12.16c; CHAIN 1..496; /note="Uncharacterized protein C12G12.16c"; /id="PRO_0000154047" MGVHGLLPIIRKVASEGIRWLQPEFFSKYYPVLAVDGNLLLYRFFRSPNTPLHTNYQHVLWALKLSRYCRKLKTSPIVVFDNLKPNDFKAEEHEKRSLISSQIVNQRQVVQEQMYFLCNLKNCLIDNNFPTGNFYYEIGPLLSQIGKLLFDLRSLNERDNPFHAQNNAENLENATFVRLIVDKLNDREKTLMIQEKKNHLIHSLRQLLAFSEINDFPSEIRSYLEFILSNLDLECLTLCLKIIKGILTLDELQKAIKLKQTELDKLERRLYRPSPQNIFEIFEILKILGIPASFSPIGVEAEAFASAISQNNLAYAVATQDTDVLLLGSSMISNFLDLNDNFHLPLQIMDPRKIAQELNLTFDGFQDYCLMCGTDFTSRIPKIGPVRALKLIRYYGNAFDVLKALNVEEKYIIPTDYIKKFLTAKKLFTDLPSNNELFSFIHNIPKEFLHLSDSTYLDLEKQVLRIFNVQIEELDAKTPWYYHYELEKDVKSTYEY Q09709 YA32_SCHPO ACT_SITE 156; /evidence="ECO:0000250|UniProtKB:P0AA37" CATALYTIC ACTIVITY: Reaction=a uridine in RNA = a pseudouridine in RNA; Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q8IZ73}; SPAC18B11.02c; CHAIN 1..394; /note="Pseudouridylate synthase C18B11.02c"; /id="PRO_0000162755" MLKRPKRDPLKDCEYVFKGDGLRRVPPYYYEYITFAKLRWYGKTLLEVFNTEFRDRESGYYEKAIRNGQVKVNNQIGNVDTLIENGYIVSHHAHRHEPPVSDQPVGIVHEDESYVVIDKPAGVPVHPTGRYNHNTVLHILMKENKCSLLYPCNRLDRLTSGLMFFSKSPKAAEEMRVHMISKSLKKEYVARVIGEFPNSGEVICDAPLLTVAPTLGLNRIHPDGKEASTVFKRIAFDGHTSLVLCKPLTGRTHQLRVHLQYLGYPIANDPIYANKRVWGPSLGKNGEGSNESVIMRLSEIGKTETASPLLQYEWYTNETEAEAKARRDKRLGELLTGKHCSECGTPLYSDPSPEELGIWLHALKYESKDWSYKTQLPKWALDVCCRDPNALPIE Q09710 YA33_SCHPO SPAC18B11.03c; CHAIN 1..447; /note="Uncharacterized protein C18B11.03c"; /id="PRO_0000116386" MDTYMEEREAGRLEIYSVKRNVLNMFSIVIVSATYSISLDSTVLYPAVYHAIVNQPMLGARIHNCHSKIPIVKKLKTIDLDKVVKYADDQKVDSFCNNALQNFKLCYDDETLPLWMVYVLNDKSELVFIYDHSLFDGGSGPLFHKYVLEGLQMSKTNFSSSTVPVSELPLPKNLEKLIDVHPSWFCLMKALWTNSGLPFSKGFRSPSYKGHAPVRPFSSHTIFFSISNAVVKNIKQLSKNIDASFTSIFYSVFMLSIYYAIAKNGKVNLDMLIDVNARRFLPVAKQTMGNYVFSYVHHLNGFQPSQRQEDYKHTMVDLATEFSHRLKAALSNPREMSQQIGLLSYIDIEDYLLKSCEKTRGNTAEISNLGYFSFPADSSVKIKNMAFAQPCSSLSAPFVLNVITVADGPCSFSLSIFDDGNTEQTHELAIKIRDKFLSILEKVSMNS Q09713 YA36_SCHPO MOD_RES 153; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 154; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 309; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC18B11.06; CHAIN 1..327; /note="Uncharacterized protein C18B11.06"; /id="PRO_0000116388" MDVLNKSIQTALEALPKTSSSSSDGVSLVSLKCQLLLSYVQKLAFLMLVKLDDESFLQHQDVVEKLVQLRIEIEKIRPLENRIQYSVDKLLRAAGRKEEIGSIKEPENNGNDKDSQDSLKLHYKPNLSEFADDSDGPASENNVVKEDDKSSISSEDEEEELRSAKDGIYRPPRIRAVTMDSEKRTRHRPNHLVDEFVSSDMSSVPQSMPSVGSNLEKRGRVIHADERELQKMRERIEYEESNYTRLPKLSKKDLKKSKRVKKHDYGGEDWSLLDRKFHDDDFSNRKLDLTSRAKRRANFEDVNDGSLASPVQIGQSYRKRKKNLKRR Q09714 YA38_SCHPO SPAC18B11.08c; CHAIN 1..95; /note="Uncharacterized protein C18B11.08c"; /id="PRO_0000116389" MAPAELKRPDLIVPYKARVKANEEVGLSLVSTATCMAALFLRFKLIAWVAFILTFSNLLNANTSPSSSPTSMAFMGIAALVSTYLPQFLNTPNKT Q09716 YA3B_SCHPO SPAC18B11.11; CHAIN 1..1294; /note="Uncharacterized protein C18B11.11"; /id="PRO_0000116390" MKALDIDTILTQISNQQSLDKRYKRIKRLINNEQFCKNVILQKLVDSTKDIIENKVHGNILAATISLWTHAAEKHKEMSSDDRALLFNELSKVPNSEYYPATVDALIVITSQGERTESFSNDILKVLSEWLTDLFTIIDDMRAQSRKSFKGSAELRNYTRCFRQIILLLTNMFRVGFNLFDEMEVSSMLANCVWVSKSTTDEEDIALVFSLLNCIISYGRISSAVLYSIVEVVCRAKFGLVASSQSAQQIVEKLLKTATKYEALNSLKRIMEETDEGSYIAIMGGIQIVSALFTDIPRSVYCTRGMLLGFLQRSLKNKSSRIALETTRSLYNALERRSFVEVLYADEWISLLDLLVEISSSLPKSLNYRPGTWQHIEPNIIESIASYQLQHLLLFNEILKPDSNHFVLEKFHEFLKINFSYLTPTLSQKLFTVLDLRSQLPYSEGWLEDQTILLKSYFDTSFSLDFHVYLIGLFRKVLFACPVELRPEVYARMLCPLVKSLDKSSSEVIIDEVISLVCDLSWIYPSNVFHEVKDSLCFYAHNSSNGDLQLRSIQAIVSLTFYYVLLPEFKSVLYDGLVEISCDFKIRRTFRIPVLKLLLQLRINTNDYCFVNLSPAQLELISVYSTQWHNPFISEEAQRCRDNKVKDRDLSFSPVFQKFPLKVNTSATLSKDLMSLPINEWVKNVMYIVTHETDWKVVQYILINFTNQLRNTKMFTKTVEALQLLLNSLRDIINGKQSLNINFSDFFRIEDLLVSLSKILSVLMVYKDVLPPTAHEQFFQLLNRFAEKGDKTMESCIDTLITNCCAMQSFSIMHLPKFFSITMSSNLSERSLVNFLRLLHVVSDNWELNEGLEKETIQSICLFCLKVIRTKKEELDGHKKLVNPNTKVFCLYLVSFSYSIISNLFLGCETTERAQLASFLLKEFLNLKNGSHFEGYERVFYELLLRYTYSDERIESYPSDSRFHFNSSSKSWLYRGCVITINAEYETGDYQMILRRMSGTTIYRFWRNMRDRGAFEKSLMMEQSMVSSELKQKYLQEIAASHVFMETVLSPLDSPDEEPILIKPDARTEELIQSLDATHTKPVINIAVALQAGDVSDINTTVGWQLFYRLLESFGHEKKLDNGETIYVWQSKTIEMIFRYVSDPAEALESSLYSSLIIIGSDDLVGPDSLNWDSVDVPVIIKISLDSHLDALKMFDTLFHVKLEIITTGTDISHQSFWKLDQIISTNSIAPLLHSYLADIGLYQMIFENFAYVHPWLLRQQYIDTLYTIHQVPTTQRESSALPSDKTFDFTLFL Q09727 MRP20_SCHPO TRANSIT 1..34; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC31A2.08; CHAIN 35..161; /note="Large ribosomal subunit protein uL23m"; /id="PRO_0000129492" MSKIAGKRLVYFPNITFTLCRGLNLQPKFAVFRVPLHVNKFDVRDYLQHVYNLKVVSVKSRIYQGKLFRNQLGQVKRPQSEKRVIVEMEEPFVYPNAPNDLKDWQEGELLPDGSNVKTLSRYPKVLEQVDMKRVNEELSKLQDKQILESQQKIARLLKKKY Q09744 YB63_SCHPO COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; SPBC12C2.03c; CHAIN 1..571; /note="Uncharacterized FAD-binding protein C12C2.03c"; /id="PRO_0000167630" MAPSVATSLKAEILPSPRTSSPSSNFKTCVSNENGCINCRCSPSEPHESANVDESVNKLSKTFSKLSLNPTFQALNMDLGLLHENITLDRIPKVPENHVSLIDIDEARAKEDPNFQIHSTPSRMPPHYVQPHPPFSVFPAPILDVRELTKPGAVKRVFHFELDVSNYPLPEGEEWMVGGSFGVMAPNNEEDVDELLQLLHINPDQADAPVLLKTDGGRWPTIWAEDTPRELVTTRRELLKWTVEFMSVAPKKQLIRLLAEYAKDDTERQVLLFLVSRLGQRAFCDLRDHNVTLITLLKAFPSVQLPLDHLLTVLPQLMPRWYSLSNDPKVSNNVLEFAVTVVEINKVEGGTRSGIGSGFLKRLALRFLNGERDLVLPMYRGLHKNAFATHFASDGPMCLIGAGVGVAPFRGFVQRRLTNATCAGKVWVFHGCRDQELDELYHGEWENPLQKSSDDDASSTVSQQTETEMDSFEVKKDGTSGPNHLVVESRSHQHAYVQDEIRHRGDIVWSVLSHPHGKVYLCGGKKGFLDGVENALIDVCVQYGKMSRLEATQQLALWQSPLNLKYIKEIW Q09749 ADRL_SCHPO SPBC12C2.09c; CHAIN 1..324; /note="ADIPOR-like receptor SPBC12C2.09c"; /id="PRO_0000218833" MSESEQLLEKQQDHKWDAATHADKGITIKTGKIAVSSSDIPLRNRKGLLTWDQLEPWQQDNQYIISGYRPPSFSFYLCVKSIFHVHNESVNIWTHLFGAIVFLFFIFKSELILKRDTTTAEDVYVITVFLFSAFTMLGCSTFYHTISNHSDDVSKFGNKLDYLGIVVMIVGSFIPCLHYAFACHANFRTLYIGTIIGIGVIVASTCLLDRFRQPEWRPYRALIFVLMGLFGIFPVIHALKIFSFSEILVRMGLVWLLLQGLFYIVGAVIYALRIPEKWSPGKYDVFGSSHQWFHVCVIIAAFCHFHGVCIAYDYFHERRGCGEM Q09759 YA72_SCHPO BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"; BINDING 85; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"; BINDING 107; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"; BINDING 110; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00834" SPAC24H6.02c; CHAIN 1..175; /note="Uncharacterized protein C24H6.02c"; /id="PRO_0000116395" MWSFARYTQKFCLRNLQLKNFSNKVKVSSLLFCSPNVRNISNWQCKRFTQSDAKDLASGVPSVKSDADQLQPKPTYNVSFTCTVCNTRSNHNFSKQAYHNGTVLVQCPKCKNRHLMADHLKIFSEERVTIEDILAKKGETFKKGYGQVINGNVVEFKPPQFKIRPAKSSSSNSSK Q09771 ATF31_SCHPO SPAC22F3.02; CHAIN 1..209; /note="Transcription factor atf31"; /id="PRO_0000076539" MTYETNTPTEESIIPKHEDGEEYNSIYLSRFEKDISISQTLDFSQFMQTQILLTAKRKALELGDDRSPINNDPYNIRRSDFDELSEYTASKSPSIISEASHNSPSRELDDSGDENTSKLTGTKQSMLKARNRQAAQKCRIKKKKYLQTLQDQVNYYTSENKELLQSANDLREEIIKLRTLVFAHRDCPVSKACSKALFLMGKEKPLTPP Q09774 ATPN_SCHPO SPAC22F3.07c; CHAIN 1..118; /note="ATP synthase subunit g, mitochondrial"; /id="PRO_0000116400" MFSTSRIISRINYNFLRKSHYSTKTVAEQAKGRFTPLIQKLSAVQQPIMYWANVSKELVQQVYHSQKIAPPSNTHSPFLFWKSQSSEAWGRNFFIAVEIVGIFCAGQMVGRRKITPYH Q09786 YA98_SCHPO SPAC13G6.08; CHAIN 1..535; /note="Uncharacterized WD repeat-containing protein C13G6.08"; /id="PRO_0000051488" MSTLYQVNKIKEILIRFLETIIINGMNSFSSTVYGQNAERSNTPTLIDPSNKETANVCPISKNLFQSYPKGSYRNSQRLTSRNGLDRFIPMTSNKDTISLGRHSSLSRNLVNKTKNASETYQQLLEYALEVERDDNVFTYAKLQKSDMTQKCPTMVASEKDNKGKLNEKKNRSPENLLPFRILDAPELRDDFYTSLLSWSPKGDLAIGLAENIYLWSKELGPTRVLEESIYDVSSVAYSYNGDILAVGRVDGTLQFWQDNERVPRISIHHPGDIGVLAWKPVLETNRLLVGKGNGNIFVYDIIWSESTSKAVLVATITNAHDEQVCGLTWNHDGSQFASGGNDNRVCLFKGSDLRQPLYVWQQNAAVKALSFCPWQRSLLATGAGSHDKHIRFYNCFNGKKIDELYCGAQITSIHWSPKYREFSVTFGYSLETVQHRFAVYSWPQLECLVSVLPSVPDIRCVHSVLTSQLNETTGRCEMTDSIIIASSNETIKFFDLSEESSWHNSRVLTWHGIFDSQILEMLEGIDGKIDSHLR Q09791 YA9F_SCHPO SPAC13G6.15c; CHAIN 1..163; /note="Uncharacterized protein C13G6.15c"; /id="PRO_0000211425" MLVFTTSPDHVDELNEFVQQLNPVAFTRVLRGLGKVLASYNDKAVEEDTLKKSSTGSLPSGQQVHCQYVLDDPNHVEGISVDQSLQVPKFEKNWLISPPGSPPVGWEPIVEESPNSQHLAHDIQLKLDELGNALLNDHSAGPQIVISEHNNTKETSPSRQFEH Q09795 YAA1_SCHPO BINDING 397; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 408; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 408; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 506; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 520; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 520; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255" COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; Note=Binds 2 manganese ions per subunit. {ECO:0000305}; SPAC22G7.01c; CHAIN 1..598; /note="Uncharacterized peptidase C22G7.01c"; /id="PRO_0000185095" MVVHTGNRLNKLRELMKERGYTLYVVPSEDAHSSEYTCDADARRAFISGFDGSAGCAVIGETSAALFTDGRYFNQASQQLDENWTLMKQGFTGVPTWEEYCTQMTKCNEKVGIDSSLITFPAAKALRESLFLKSGAVLVGDHDNLVDIVWGASRPKEPLEKLIVQEIKYAGLGVDEKLHNLREAMKEQKIEAFVVSMLDEVAWLYNLRGADVPYNPVFFAYSLVTLDEAFLYVDERKVTPEVSKHLDGFVKILPYDRVFSDAKNSNLTRIGISSKTSWCIATSFGETKVMPILSPISQAKGIKNDAELKGMKECHIRDGCALVEYFAWLDEYLNSGNKINEFDAATKLEQFRRKNNLFMGLSFETISSTGPNGAVIHYSPPATGSAIIDPTKIYLCDSGAQYKDGTTDVTRTWHFGEPSEFERQTATLALKGHIALANIVFPKGTTGYMIDVLARQYLWKYGLDYLHGTGHGVGSFLNVHELPVGIGSREVFNSAPLQAGMVTSNEPGFYEDGHFGYRVENCVYITEVNTENRFAGRTYLGLKDLTLAPHCQKLIDPSLLSPEEVKYLNEYHSEVYTTLSPMLSVSAKKWLSKHTSPI Q09800 YAA7_SCHPO SPAC22G7.07c; CHAIN 1..419; /note="Uncharacterized protein C22G7.07c"; /id="PRO_0000207636" MPCILYMDDTSCLIDLPTSLQFNKHILPTRTKPVVKPYLLPEKSTSDYENSGKGTVGQVLQSLQRVRRALQLRSLDDNQSTDKSHHVQFQDIVYRSNTSASEIHFQAENAPLVQWYSDIFKVLVKAPVIQFEDQCLQWLKMLNTIPPSYSFITIKSKDTVELGLEEIYQQCVQNDGASAIKLKLKGSKVITESSETNCRDSIYYIPARSSFIMGDVEKTAQILLEAIDGHLEKPKCIIIDPPWPNKSVARSSVYKVNRNLGYLKALPIQESLSKTGVVAVWCTNKEKYVNFVKKVLFKKWNLTLVSTWTWLKITAFGEPLFDVYSNMRKPWEQLLIGVTSEYTSVYSDKIPPTFTIIGIPDYHSRKPSLKPFISRWFNCSANESLPVLEIFGRSLTPNWITWGREPLLFMHELYWSSDN Q09802 YAAB_SCHPO SPAC22G7.11c; CHAIN 1..140; /note="UPF0654 protein C22G7.11c"; /id="PRO_0000116408" MPDPNRVLAGKKATLHNPNVSQQAKERAEDYIESHSSGQETGDYSAQAGGRDLDYEDLGDYDEDADFDNEEGLNVLGDESGFVDDPMKTGDLVEEDQLEGKNIENVRGGYKATMHNPNVSKQAKTRAQRALEEIDDETQA Q09804 URB2_SCHPO SPAC2G11.02; CHAIN 1..1318; /note="Probable nucleolar pre-ribosomal-associated protein 2"; /id="PRO_0000116409" MSLQTLTKRIRDKNGSREDQIDLANKLFRGEVDVYFPNKEEFIINFLLDRLKENSNLTCVNIGYWQLFLNIWKSDKLSGSFRVSAIRRQSLYPIILNAFEYLIKEFKKDVFLKISDVFVCVYSNLNILYISRSFPDQISLLFSRYCYLIASKIDDLLDSHPNEVFKETLICVIQSAVHSQASSTKAQTQFLHQTLGSILALLCKTQKGDPYFSFLNAVLMKCVLTQHTLDVLLLTKKDSSMTLCSLLNAISFEPINLKAIPLFFIICADSINFHLSSVEKSISQQKASELMYKLFSEHIAFLLSLKNLPEEATLDCMLSICQVFENDNLHRGHSDEYTFAMLEQLLELSVKTLRQNTCWSTSWEMLSSLLAIDFDVLLPHSKILWECIKSVSHQDDIHALKFLKRWVRASAKARILDSFCIDWHLNVQTMSERSILTNRDFITSFSAVAEVSLSQISIKKLVTWLMSSESIMSENSNRFVVYYSLCKSLKRESYPAHLVPNFELFTRSIFNASLKNFNILDERSQALLCMCQISHVQFFSSDMSISASVGMKTLFEDLMAEKSRGLSSTVWSLQLLLCYLEQCLRLNTLHEDTTFPMRVVNYALEYSSKALDKFAENSHLILLDMVDVGKPDLVLTLLCRWLHMVHLYSSRTSITSWIYSIASKFYFIDSLNLETKDSVLESNWERFISSTETYELDSIRDSLIDCLIRLLCYSSNNAIDPVSAPGNLDFDNSAELCSSLTRFTPKNIDFVLKSLIHIPIHSITKNQRTRLLNLLIIHEKLLSDKDNSAHISLRKIIYTLMKTPCSSGFYRDPKIIIDLMQFGKTDLSFHKVHVLIMRSWIQHLDEGNKSEVILKLLQLILADFRELPLETITLIFNALVDSLPTSKHIKNSNDILSSVFTINDMLIDEMTAYLSKKESLCSGTFSCLLACCNSVLRTQNLTSESLNKLHILKVGIEEKAISLKLNELPFLENWILFQCLLSFGGDDFLKVVAYMVYYRRTVGEMSFRVSDFELALSRLSTNDADYAILNILNLLTSNECDEFDYSVLMKVVGVFANYSDCFQRNRHLVHMVLLCCTHVFYNQTLKPATLIDSALDVFLCFVQKTSKFISLDSFNTILTALSTILNLKELECEPKDHANLILKIIQILNGLLFNHRSYMSGRFHVFYSILKSLLYSMVQHDSEMKKIKGIALMNFYKPKKVPIHVVQSFCRLLTTWMNPNLMHDSNKKNSSLTDAERLFVKATTKHFVFLLTDFMSAQTVYQIDIQVKELLTNCFYNVYENLSNHEKQMALVAMNAPSKSLYQKFVNDYLIFAKWNEA Q09806 YAB4_SCHPO SPAC2G11.04; CHAIN 1..301; /note="Uncharacterized protein C2G11.04"; /id="PRO_0000116410" MGFMLYEGIDSKSIEEITEESEKTKTDLQKANTPNKTEAVHSLNNTCSEQNSGTKDYLNSLQFLPSNFRPKTHKKKKSVSSYLSSTIQKNANENIPHVQCRNDSQSTVTTRNPTPFKIEVGIYPSKPNNLNKEPPASTVHSDNLGDAVEHEWVELYDPLFPTSYSVFKESDYANLCETNWSHYVNQVPSLSIEAKLSNIVNASKSGIGPPPSLLSHATLARPSESMVLSNNIAAEDLDFFKKSPPVPAISKKENVALKMLQRCGWKEGQGLGQHNQGIINPLHVEISGFVTETKHSKINDK Q09807 PALA_SCHPO SPAC2G11.05c; CHAIN 1..701; /note="pH-response regulator protein palA/rim20"; /id="PRO_0000218883" MEFLNIPTKNTFHWSCDPLFNELKRLSCFKSFTYENDLKTFKALRSQLCLSHPSINSLSSFQTYHQLLCVLEQKHLSECVAPFVWTLSSSSNERESFENLIFEHACLIYRLACTYHTTAISLCNEKPPNLVQACQYFQLSAGCFRYINDFYIYTKSLDFNENLLKAWEIYCLAEAQTCIFSKANSNDTTSESIIVKILAKVFLLYEDAYKLFKNATGAPSIFVHWTYIQKLFYQTITYQIISRTSYSLNKYGENISYLRLSLLHCKEALKTRFDFGFNVKVYEKLEKLESSLQFELKRNERDNDFIHLQPEIPVGSFPLLDTVTMVQSITPDVLTDKTAAYPYFSTCLDKEFMDLIEEHEKNILDAAVKSIDCLTKEGTEKLFALMEEIKSVNDNRYITETSNKVMENFTEIKNLGGLEFLRSEASSLDCLIDKVNGTYRHCCQALDEIINSVKSSQNMKEKGFYSDVIKLHEEVSLLKVNVENSQNAKDTIQKDISAFGKDIFELSAQSERILSNLAEKKNPNTDQLLLQANSYLAQWDLLKDERNMLKKLGSNDYFNISMYSNHTDIHSLLKCFREAVDAKWNFRRQRERQEIIIQNVEKLKSYLNSFKVQAECSEISKILSFSQETEKKYKFLLQTVRNETEIARELYNIICRAEERYSQYENRYENENRLNKIKLQHSSSNAFNPEIHKIKFKSSKK Q09809 CSC1_SCHPO SPAC2G11.09; CHAIN 1..793; /note="Calcium permeable stress-gated cation channel 1"; /id="PRO_0000116411" MAFNGYGIFDSDPRKNPSSDLRTQFWLAFLLGASACVFFCFFRKRWKVLYAPRTTIEGLNLPTLSSSYYKWLMDLVNIPDDVVQNCAGLDGYVFLLFFKMGIKFLSFASLLGVLIIMPVNKHFRGDAFGNITLSMPAKSEYFFSSPLVKKSIVQSPIIANGSELNVGVLGPSLFNPIGNLSDIPGLPQPGDGFLYLYVLFTYFISIFLLYVLFSSTKSIADIRQSYLARQNRLTDRTVFISGLPNELCSTENLKAYFDKLDVGSIDSLSICRNYSYMDILLSKKSKYVKKLEKYWSIYLSNCKKLGISTLPPSNYLSPNRAELESTPEQLLEVPWQHHQCHPLIKTHFFGIFGQKIDAIDFYSAKLYKISQQIENARSFDYPTTGQAFITFESMATAQIVAQTHIDSKSLMGLHIELAPAANDIQWHNTYIGRWHKFFQGWFITLVTFMIILLWTVPVGAIAVFINLDTIRRLWPELGRMIEDLPFLNSLLRTFLPTLVYSLFISISPFLFRWLSSMQGLSSRAEEEIYAVGKNYAYLFVNFFLVYVIAGSTSIWELAKDTTSFAHFLANRLPHQAQFFIDLIVLQGIGMFPLKLIQLGKLSSYFVRRSFVPYSIASKKFETPDSFSVGIFLPQPMFIMLICLCYSIISPLILVFGLIYFIIGFLVYKYELIYQMEHPQHSTGELWSTIFLRMIFGCVIMQLTMMGLMSLRKAYWLSTVIFPLLCFTVISAYNFSTMIRSSMQFVSLYYIRTHQSNTLSSESESRNSESSGSYVHPGFDLSNEELPLIDLNTA Q09817 NMD3_SCHPO SPAC16C9.03; CHAIN 1..498; /note="60S ribosomal export protein nmd3"; /id="PRO_0000116414" MDMDSGSMGVAFQPSEPIASTILCCECGVPTPPNAAAMCMDCIKMTTDITSGIPRESTVNHCRECERYMQPPNNWMIAPLESRELMAICLKKLRGLNQVRLVDANFIWTEPHSRRIKVKLTVQKEAFTNTILQQSFQVEFYVNNTQCPDCARTYTPHIWKAVCQVRQKVLHKRTFLYLEQIILKHKAHMNTVNIKETKDGIDFYFGQRAHAIKMVEFLSAVVPIRYKGSEELISEDFKSNTANYKFTYSIEIVPICKDDLVCLPKTVAKAHGNIAQLVVCTKVGPTIRFLDPLTLQTCDMLPSIYWRTPFPALADIPELTEFIVADVDLLGPTNGKYALADVELIKSSDGSTHLTRTHLGGILNAGNTVLAYHLAVTNFNNEVYDTLREDSIPEVVIVKKTYPQTKKKNRNWRLKTIGMQKAEDVKKQDIERQERDYELFLQNLEEDPELRQGVNLYKAPVKAIAVADTDMDEEDEVDEDIPQISVDELLDDVEAMHI Q09829 YAD3_SCHPO SPAC4G8.03c; CHAIN 1..780; /note="Pumilio domain-containing protein C4G8.03c"; /id="PRO_0000075935" MVNRDAYNELNLNKKSQETNRKPSPLSSYTSISRELDYANQSPFSSNSFSPTELKARTSATFDVRSASTSPINASDFHKYSHDPFQRLFKAKGNASFSKTKSFPSSVTYSPSEETFPLTSGMNKSVHEYPFTLSESAISSSHKSSIPERRNFDSSVSVSNPLLHWNNVDTLLRDGSLENVNNSRQDQFLPYKTFSSTISNSDFLHRESSFSSLIDEESKLASLRNLNINDRPPLPVLKNSERNLLHRQLLSNHPFFSQNNVSLSTNSKNYSTDFTKIQSDSSLLQNRQQNHRIETDQLSHFPDHLDPSRIPSPYQPSSLQPLESRKLHSKVDVHSKKLNALSQLNPILRSENVLQNDNHHSSLSMDNDPTNVSTKNRNNQTVGEHPYVDDNKKKKKGPAKPKEKATLGKTVNSFFGSHSTSNYSKVPLSAKLTGEKSDDLSNLLKNKGKKKSQDNQIPHLVGFLGHLSTICKDQYGCRYLQKLLDENPKVNASLFFPEIRQSVVQLMIDPFGNYMCQKLFVYASREQKLSMLNGIGEGIVDICSNLYGTRSMQNIIDKLTSNEQISLLLKIIIPSLTTLACDNNGTHVLQKCIAKFPPEKLEPLFLSMEENLITLATNRHGCCILQRCLDRTNGDIQERLVNSIIKSCLLLVQNAYGNYLVQHVLELNIQPYTERIIEKFFGNICKLSLQKFSSNAIEQCIRTASPSTREQMLQEFLSFPNIEQLLDDCYANYVMQRFLNVADESQKFLILRSISHVIPKIQNTRHGRHILAKLTSSTSS Q09830 YAD4_SCHPO MOD_RES 395; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4G8.04; CHAIN 1..772; /note="TBC domain-containing protein C4G8.04"; /id="PRO_0000208059" MQPSVSDSSVYLSSAPTKPIASGSVATGIDSMPSKVDITPCDLLENSKSSAPLFVECNQESLHSIPGSLHLVPDASIERLIEKHGAVNLLRQLAKDVAERDSFISDLKFHFESREYVFRELLREHGLDPVLANTKLSQRHSASFFPSSQEPSIPENPSSLTGEKPHLYARIDSAINEPFTPSDRLSPSSLVPLLKLPALDHAVSSSSSSDLPSDPNSASYIASSKQKASSLKLTSSLKKFYSWTSSSSLQHTRENLHDSTSSLRDHDPSLLSSSKFFRSSPRCSTPSVSSTFVSATSEPEVETYSVSTKNSSSNKNLRSSLSKLLSTSNLNNKPLSLSSTAPSMPSIGSVELGNMIPKETQPPSMRNDWKDYLDNNSKEILDQFGFLQKRPSHDTPLCPEDIKLNQKQTLSFYESNYGLVDDFFGNELDGLNDSPLLLNKKDILLDMKESTRQKNWSLFFQRLYKKYKITDEDTIGLLGISSIGVKGRHGKKRWHKFRELVKNGVPLCYKAKVWLECSGAYQLHSPGYYEELLSRTDEVESASVAQIDMDINRTMAKNVFFGGKGPGIPKLRRILVAYSRHNPHIGYCQGMNVIGAFLLLLYASEEDAFYMLMSIIENVLPPKYFTPDLMTSRADQLVLKSFVKESLPEIYSHLELLGVDLDAISFHWFLSVYTDTLPTNISFRIFDMLFCDGYVCLFRVALTILKSLKQQILACNSSSAIYSFLSDLVQYSFQPDSFIKEAADRWSKLVTEKSIERKRNLAISSLNLAVNY Q09834 YAD8_SCHPO SPAC4G8.08; CHAIN 1..271; /note="Uncharacterized mitochondrial carrier C4G8.08"; /id="PRO_0000090700" MDVQTLMAASAGAVASRLLCHPIDTITVHKQTIGKFSFKTMPLKAYYRGLPISLTLITPATCLYLSTYVEAKRRFKPSVGEGAILYSICGMTAEVVSSFVWTPLEVIKARTQISQKGSVINTISTLARSEGLKGFYRGYWMGVAIYLPTTVSWWVCYEESKKYLQKQSNWDISVIAPICSALGTVVATTISTPLDIVKTRYQVATSSAMRKAEYGLQAEKELGILEIAKLLFSKHGVKGFTRGLFTRMCYIMPSGMISMSVFESFKSKDID Q09836 ATP10_SCHPO SPAC4G8.11c; CHAIN 1..267; /note="Probable mitochondrial ATPase complex subunit atp10"; /id="PRO_0000071726" MAYNYLKNLVIPRLIVKHQFKLRSFSTKSLNDTKEKAPSALIPVGLLVKPTMLSEVQKPTLWEKLTKPASTSSPEQRQKELLNEMKRSTIQDFNEVRRFNGKLFYSPPRLFKEKSALWMYNFHGKSLRNQYKELYKDWQGSPFFFALFSNAFGENQCRNWIQHLAPFDYLPVRYANVQSNLIKYWLQKIFIGKVKRSIPEKCWNEYITAYDNKFSFPEIGWNNKLVGNVYLIDDSCKIRWLGTGDPTNVEIENLKTAIKFLVNKNVG Q09854 MOK11_SCHPO CATALYTIC ACTIVITY: Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378, ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.183; SPAC1527.01; CHAIN 1..2397; /note="Cell wall alpha-1,3-glucan synthase mok11"; /id="PRO_0000080329" MAYPLVVSFFLYIVILDKHAWCAPFNNLLTDWNLNTNVSALDPSDYWGEWENHEFFPSPEHWRFPIYTIAIDKWVDGDPTNNDFSGTRFEYDIYETEFRNGGDIIGVRQSLDYLQGMGVKAVYFAGTPFVNMPWGADQYSPLDFTLLDPHLGTINDWRGTIEEMHSKGMYVIVDLTVATLADLIGFEGFTNTTTPFTFIEHNALWKGEDRYADWNFTNSWDPDCELPRFWGESGEPVVVEWTGCYNSDFDQYGDTEAFGSHPDWQRQLSKFASVQDRLREWKPSVASKLKRLSCLVISMLDVDGFRIDKATQMTVDFLVDWAKSVRLCANRFNKSNFFIPGEVTGPSSFGAIYYNRGRQPNQRPANLIDALNATSSDNVYFLREEGENALDASAFHYSVYRIILRFLRMDGLMEIPYDLPVDLAEAWHQIVINEDSFNPKTEKYDPRHLYGVSNYDVFRWASVADGSRRLILGTMMTFFLFPGAPLIYYGDEQGLYVLDNSANNYLYGRQSMAAAPAWYIHGCYSGSSSTYPAIDLSPAKIGCLDIWNSLDHFDPSRIERQLFIEFQDIRSRYSALTHGWKSELLGNWTNIEYLPNSGINPSNVGTFSMVRGAINSLQNISSEYNFPGVKTSSSDVWILFTNSNVSVNLKSNCFSKEAIVSPFISGTKIKNLVYPYDEYQLEASSHFSQISNTEPMGCLPELGLDGYGYKLFVPINEYIPRRPFITKFSPSHDSRLVIPLEKLRIIVEFSEEMDCKSISKSLLITSKTLNGDSPVLDESSVTCQKINDKDRVRFSGQSSSLFRWSATFSNIADGIHRISFNNASTADGKDFTHSVDHFLLRVGSLNNPIVFSSANYSYDLLQKENNSVYIKHAAIGADMFRYSLDFGSTWTEWQTYDGNNTYCNLSGWSQSSRYGWKGHHIMVQYWSELTGSSNYMQESDLEYPYKRWFPHVFMDSDYTQWTHDSDIRNRMLPLENGSFLGYHIADVYPSALQFNVWGLNKDGKADKSFIYGSLQNNSFLSRVSPSSLEENVFYIQHPPPKSYLSWSVTFDPQRRRYYINPSGCVFVSLGIYLSSLIVPLLTGVLAVYIFKKKFYHVKFNAFGTSKQNLHFRQHDVLGMKNLFNFSCSNKIKGEEVLNDGDKGKRRTVLLATLEYDIPSLNICIKIGGLGVMAQLMARHLEHEDIIWVIPCVGDVSYSNVEEDDPIEVVIIDQTYFINVYKYVIGNIIYILLDAPIFRRQTSGKPYPSRADDLSSAIFYSAWNQCIASVISRNNIDLYHMNDYHGSLAPLYLLPKIIPVALSLHNAEFQGLWPLRNSSEKEEVCSVFNISKSVCSKYVQFGNVFNLLHAGASYIRIHQKGYGVVGVSSKYGKRSWARYPIFWGLRKIGKLPNPDPADNGTNFKDLDANSMNEFENIKAKHKRSAQEWANLNIDPEADLLIFVGRWTLQKGIDLIADITPTLLENFNSQIVVVGPVIDLYGKFAAEKFTALMKKYPGRIYSRPLFTQLPSYIFSGADFALIPSRDEPFGLVAVEFGRKGTLGIGAKVGGLGQMPGWWYTIESNTTAHLLCQFEEACRQALTSSKSVRTKLRAISTIQRFPVSEWVSKLDTHVRNCIKFSHKQNLEEDFIHEPVIDVDEFAISSSKDIDADEDLEIIGSSDNKAIDSNGEGFLIEKDNIGTGSYSNQQSFDFKSSESDSFPQKSPSVESFSIIDNDNPFHEGQNSSTGYKDIVQGLLAENGVSEAGVDVMTSIVSSTIPIVSNHQTEGSQMFNEISSVSSIHVYHDESQPPVEMPAESDTPLQNKLYHPGMWSSSDIRIPNNSSQLSIDSVRSGMRPFSLSKVPHQFDDEEGKALQIFREKLKDLNCKNSMNEMCIENFLMKCTRKYFDEVRKLRLGTLKPENLQFVKDPSSLALETNLLPASDTIEEKNDVGNKQVNSHILDPGFLKEEECVYEFEQLHGLRKALQVEIYGWPLYTILLAIGQVLAATSFQLNLFSDTPDQPEYQSYIVCSVYISASLFWYILHSLVPNIYALSTPFIIYATAFALAGLTTFSSLGDSRLWISRVATWIYSIASGSQALFFSLNFGNEGRYDILYWIVRACFIQGSQQVWSAALWYWGSYSTDKPNRMGVSGKLNPQPWMAAITWPIALVLLAIAFVVYRGLPNFYRQCPSKIPAFYRSLFRRRLIMWFFISVFLQNYWMSSVYGRSWAFMWSAHNVHKWAMFLLVILFYVAIWIALVALLASLSRYHSWILPILGLGFGAPRWLQTLWGTSNIGIYVPFLGKGAPYLSRMLWLYLGLLDTVQTVGIGIILLQTLTREHITVVLITGQIVGAIASMVGKASSPSKFGPGDVFIDFTHWSVKDGPQILASIPFWVCLICQLSVIIGYFLFFRRENLSRP Q09865 RM06_SCHPO TRANSIT 1..32; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC12G12.08; CHAIN 33..213; /note="Large ribosomal subunit protein uL6m"; /id="PRO_0000030547" MFSIDSCLKTRPLTFRIARLGMNFTTCSAARSYVGKKEIIVPKNIQFDLEGEQLQITGPHGTLNMRFPNYLNLSKTNDILKVGMDANIEKQATKKQRAMWGTTRAILANNVKGVTMYWQSIIKLVGIGYRTSLNDGNIHLKIGYANDILVSIPTDVQVENPTPTSLVLRGIDRQKVTQFAAKIRSFKKPEPYKGKGIYVDGEKPQLKAKRSIS Q09867 EFG1P_SCHPO SPAC12G12.02; CHAIN 1..183; /note="rRNA-processing protein efg1"; /id="PRO_0000116426" MPKFKGPGLSVLKKKIRDNERLLKKENLPANIRVEHERALLGLQEQLSMAQLEHKKQKIFERYKKVRFFERKKAERRIKQLEKSLKDETMDDEKRKQCEKSMRKCQIDLMYIKEYPPLTKYVSLYAEGTSEQTEETRNRIWAEMEERFNSGRKHKIPSSGSNRVPVQEKSSTGGDLEDEFLQR Q09870 RCL1_SCHPO SPAC12G12.06c; CHAIN 1..363; /note="Probable RNA 3'-terminal phosphate cyclase-like protein"; /id="PRO_0000156443" MSTGQLKRFKGCEYLTHRLVLATLSGTPIRVEGIYPDEADPGVKDYQVSFLRLLEKLTNGSVIEISYTGTSFIYRPGNIIGGRVVHDCPTTKGIGYFLEPILILCLFAKTPTSLTLTGVTSSNEDIGVDVLRTSVLPSLQKRFQVGDELELRILKRGSAPGGGGEVNFLCPVIKESLPPIRLSEFGRVFRIRGIASSTRVSPAFANRLVESARGVLNPFIPDVFIYTDVRRGDECGNSPGYSITLVAETNKGCSYAAEHCGEAGETPEDVGSFCAKKLLEVIESGGCVDPYTQPSTLTGMLLSSEDVNTIVVGQLGITSQLVVFLRDVKALFNCEYRFKELESGQVEMSCLGKGYLNVNRRIQ Q09872 YAG9_SCHPO MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC12G12.09; CHAIN 1..977; /note="Uncharacterized protein C12G12.09"; /id="PRO_0000116428" MSFYKEKSINETNLGSFVDESNELFFSALSESSMNHGTPDDSILLDLVSRSDNKDLYQDSLDVRDNFSNLSSDEIPQSSSYEQTRKPFFHHFNPFEFLEATSPLQQNGKSRDTEKPPSMKEKDLSSNSSSQHDKAFHERVDQGKNKSSTTKYQEFRTVADYREFSPGQSVNSLKPNSGDEVPSTKSSTSSEMHTQLLKDEQKKILTPAPDVPHDVYCIEPSLGRVFSFPASFVASPLLLEDCNKIASCDLPYSTFYANSQVIDKFSEYFAYVDQDPCHIRVLNANTDQSLILYTQSDVKNLHFGKNKHTKPHLLVMDALSNLYVWKILQKRSEISVSLLFTIRRANYGICDWIPNSSNMFSMIVKNSLYIVDISNIRSNNISPKVYAKDFNGLQAAKVDLPGPINSYTISSDRSVVAILVNSQIFFYSFPVSNLFSTNPSHRGNWAAIATMSLQLPSTANSISFLSSPPNNNDIIDKVICVSYANNTILGLFDFGLCAFTQEIEFSNEKEKSPIQQLLTFNNSNMIVAKRNQLLDIFIYSPSDLSNVGVLSNTAALISAVSKGKRFGDSGYINKVISNEVVDHSIVFVTLIGCDSSKLELILALSSGYFQFCIESDSKFDEGTSLEYPNSDKRILARASLTSGLKSNNTLRALSQDLKNCAKSKDDSTTQNLTESLGSVCYPSMPFFNQYVPQNPNEVRENISSVMKSRIHAKFESLHSRVELVVKNSYMKLLEQTISEAATDEISDLFKLIHSKPFLLEVGFLETGFLANDLENLTSTYRSSNRQLCDFSNRIGNINQKLEKLLMIERLETSDQSPTSSSNFEESESFAVSKKVLELVRISKNKEALICFTKDPSIEAFRSLQDVPDYSLDDCSSIHLLAFIHVLSKLIIKEEQLSFSRLQLLSRATSRLRTMTLSVFNNSGTLTPELFSSVVRIVLKNVREFVLIGNSSIQKSKHEFLITTLQALLREVDIFLNT Q09874 YAGB_SCHPO SPAC12G12.11c; CHAIN 1..365; /note="Uncharacterized protein C12G12.11c"; /id="PRO_0000116430" MDNVQEHDPDTQEHNNETQNHKQEDHSNSYQTRTIPFIEPLSREYQKRIILCQTVNGPCPIIALSNALILKSNVDRPFELPKKRYITPDELTEYLVEFAKAYGLCKNQQSLQDKLTSMHFGQQLNPCLYDIEKFEYGHEIFCTFGVRLVHGWILSDDMGLSDEDLSYLRKLEYYEKVADTFAERRSLLEMQEPLTEQQQDFLNNSTCVDKVMENRYTMQFLTNAGLKKILELVGPGEIVVVFRSSHFSTMYSNPDSFAQFTLVTDSGYARTGEDVVWETFDSQTVETGNGELCAANFIPAVYVLNQRKEEKKKRAKDDEQYAKRLAKEEEERGKKETPKKASNTPRRNKSNTQKSRKQSENCLIS Q09875 YAGC_SCHPO SPAC12G12.12; CHAIN 1..324; /note="Uncharacterized protein C12G12.12"; /id="PRO_0000116431" MLLPIIMLTSGVANTVLSKYQDSIAEESEPIKSMAVLQSLNIFLGEACLWFYVLYKRHSQGPGYESLDHLPLKHKVFMALPAIMDICGSTLMNVGLLYTSASIYQMTRGSLIIFVALFATTLLKRTIGQLQWLSLSFVVLGVAIVGYSGSSSSIGSNPILGITAVLIGQFFLATQFTIEEYILSFIQVDPSELVAYEGTYGVFFVLLGMIISYYFIGSTTAGYHGWFDYSHVISRFNEVPALYVISGVILVSIAFFNVSGLAITKLHSATTRSLLDIARTFGIWIIAMAMGMESFHLLQFLGFVLLIYGIFTYHSIIKFPLAES Q09886 MUG42_SCHPO SPCC584.12; CHAIN 1..115; /note="Meiotically up-regulated gene 42 protein"; /id="PRO_0000116539" MGILIGTFPPRRRPTLHETENHVKKKNWRCGKGIKCFFKPSDQVYLVGQVDCRFLLHHNAKNKQFPLIFVTNFITSLPNFQFPLFFFVSLLHLYRRPRNQISTRKYTPHTQSGRR Q09887 YC9D_SCHPO SPCC584.13; CHAIN 1..544; /note="Uncharacterized amino-acid permease C584.13"; /id="PRO_0000054175" MSIFKKSSNTAPSQHEDVEALASDEADLAALGYKQEFKREFSAWTSFCVSFSVLGLLPSFASTMYYTTGYAGTPAMVWGWLIAMVFVQCVANGMAELCSSMPTSGGLYYAAAVLAPKGWGPFAAWLTGWSNYLVQVTGPPSVAYSFAGMILTLVQLHNPNFETQNYQIFLLAVAAMIAQGFISSMPTKVLAVFNTWGTVLNMLFLAIVMITVLAVAGTKTPRGFNSNHKVWNEFDNQTDWSNGMAMLMSFAGVIWTMSGYDSPFHLSEECSNASVAAPRAIVMTSAFGGIVGWLLNLCIAYTIVDVNAAMNDDLGQPFVVYLRQVCNYKTTVALTSLTVICSFMMGQGCMVAASRVTYSYARDGVFPFSKYLAIVDKRTKTPNVCVWMNVVVGILCCLLIFAGEAAINAIFSVGAIAAFVAFTTPIFLRVFFVKEDEFKRGPWHLGKFSKINGYAACAFVLLMVPILCFPQFRGKDNTPDAMNWTCVVFGGPMLMVLIWWFVSARKWFKGPRLTIGVDDAVSEINVLEGVTKSDDDSISTLKKK Q09888 ATX10_SCHPO SPCC584.14; CHAIN 1..434; /note="Ataxin-10 homolog"; /id="PRO_0000116540" MEKMESTEEWEALLSSSSNGDELTMKLIRNGLAKGFKSQKAAGDAGLYSRFLPYHFTESVSNDSFSSLPWQIFANSVAGNSPLQNEAWAFLMDNEDFFLPVPMNPAQCTALEIALWSLIRVDDQRLFELCHSKSGIRLLSIIFDFDSHPDWLREDVMFNIAERILKSNFPNVLVNVASKIGPKSIYFLIDCMSHKIKLKETATGFYVILDVLSCVGRQFASVLEECFTKEISSAGLDHINHFSEIVMLGVDLLYRDYVSYDTTISLKNDDSSSLGDMEFETSQPSSSISEIIHLLAVLDKRIPKKTLVEKTYASSMELQELYNAVVGVKRECVRFIAFICSKFSTAPDLVRHFNGVALIISQANYDDWNPYIREISVLCTRLLLQNNIENQKIIGGLTPITTTHSDALEEAGFTSYINDKGKVVLQPKTAKNSH Q09893 YAI5_SCHPO SPAC24B11.05; CHAIN 1..226; /note="Uncharacterized protein C24B11.05"; /id="PRO_0000116432" MTVEQKIIFFDLDNCLYPKSYKIHNMMAARITAFFSDKLGIPTEEAERLREVYYRHYGIAIRGLVLHHEIDAVDYDQRVDQSLPLEKVIKKDEVLREMLLELRKKYKCWIFTNAYIVHANRVLKYLGIEDCFDGITYCDYNAKDLIAKPMPEMYERVMREAGVTDKDKCIFVDDSYGNILGAREFGWKYTVQLVEHGDPLPQPQAGSHVIRDIHKFKHLLDEIDGE Q09894 YAI7_SCHPO MOD_RES 383; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC24B11.07c; CHAIN 1..561; /note="Uncharacterized protein C24B11.07c"; /id="PRO_0000116433" MTDAGKKERVSILCVGSPSITTLLGWRLQQSSVVTCQETIMFFNAPEPSTNVFTIQSKKFGTRKYRPTYRLSKLEEVTSDSEPFDYVFVSIKPNSRNFQLSNILEPVITAKHTCIVYNSTGAIGVEEALQRQYPENPIFSLITHTPVSQRSVDEFFFGDCAPFYLAPAGSNLEIDQLSRLVEILEGGEISSEILDTLLPLEIEDLALPLSLYPLTVLTQNPNLPKLLERPDINDLHQGILQELDSLCNCLGSSLDVKKLSKQRETLLSHMQVNPAFREYRSNRPVEIVQYLHYCIDLATKQSLQVPRLRTISALISSIQHLPLVQPHHMNDMHGPTDNSPKKNKVLVNMRPINPSSFVSDRHSPLHPYSVPENGKPNMGRIPSAPSLSKGRAMTADNMDMLSLTTRRSRRSLYSPSLMQMQQSLKSDYEGLGRTFDPRFAPRGSPPVRGGKNVLSPEAKEHTHKNISPESSRFGTPSDPNSSSQSLGNEVLSRPNSNSNSAESRNGETDDSGESETYFTLMNNNKGVEPRASVASETSSMTVIPNAMRRFPLARGTSRMKS Q09895 YAI8_SCHPO SPAC24B11.08c; CHAIN 1..390; /note="Uncharacterized protein C24B11.08c"; /id="PRO_0000116434" MQFRSPLRRFDAFQKTVEDARIKTASGGLITLVSGLIVIFIVLMEWINYRRVIAVHEIIVNPSHGDRMEINFNITFPRIPCQILTVDVLDVSGEFQRDIHHTVSKTRLSPSGEIISVDDLDIGNQQSISDDGAAECGDCYGAADFAPEDTPGCCNTCDAVRDAYGKAHWRIGDVDAFKQCKDENFKELYEAQKVEGCNLAGQLSVNRMAGNFHIAPGRSTQNGNQHVHDTRDYINELDLHDMSHSIHHLSFGPPLDASVHYSNPLDGTVKKVSTADYRYEYFIKCVSYQFMPLSKSTLPIDTNKYAVTQHERSIRGGREEKVPTHVNFHGGIPGVWFQFDISPMRVIERQVRGNTFGGFLSNVLALLGGCVTLASFVDRGYYEVQKLKKN Q09896 MPC2_SCHPO SPAC24B11.09; CHAIN 1..118; /note="Probable mitochondrial pyruvate carrier 2"; /id="PRO_0000212802" MFRAGFKRFWNHPAGPKTVHFWAPAMKWTLVLSGIGDYARSPEYLSIRQYAALCATGAIWTRWSLIVRPKNYFNATVNFFLAIVGAVQVSRILVYQRQQKRITAQSEQRTELARSLAA Q09901 YAJ1_SCHPO ACT_SITE 504; /evidence="ECO:0000250"; ACT_SITE 672; /note="Proton donor"; /evidence="ECO:0000250" SIGNAL 1..24; /evidence="ECO:0000255" SPAC30D11.01c; CHAIN 25..993; /note="Uncharacterized family 31 glucosidase C30D11.01c"; /id="PRO_0000018587" CARBOHYD 7; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 44; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 89; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 121; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 138; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 161; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 169; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 232; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 361; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 386; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 393; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 423; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 447; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 480; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 488; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 545; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 548; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 614; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 673; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 814; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 826; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 835; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 846; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 910; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 940; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 987; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLLFKFNFTTAFLFTILAFAQARSHSSSSSSTSKSSASHHSSINSTSATSVYDFSSLTTPIVPTNGVAQEPTLYESSRGLSCPGYQARNISEYSYGVLAILELAGDACYAYGTDYPYLLLNVSYDTEERVHISISDLNQTQFQLSNRRDVWDAPLFYRSSNFSGNLQYNFSFNTDPFEFWITRIADDQVLFDTRGNPLIFEDQYIELTTNMVEDYNVYGLSGSQQSFRLGNNLTKTFWATGYSDSPEANMYGSHPFYMEQRYIPIGTTNTYTSASHGVLMLSSNGMEVLLRSTYIKYRMIGGIIDLFVYSGSTVSPKYTIQQYVQSIGTPTMQPYWSLGFQMSRWGYKTLSDLINMRSYLNASNIPTEGFWNDIDYMSEFRTFTVNSTAFPPNQTLDFFRSLDESHQHYVPVLDPAIYAANPNKSADRTYYPYYSGFEDNIFIKNPNGSAYVGMAWPGFVVYPDFTNPAVLQYWKQGILNLSTAFGSNYSYDLPFSGLCLDMNEPTSFCIGSCGSDLLKLNPVHPPFSLPGDVDNKVYSYPEDFNATNTTEYKSVSRASQSQYKATATSEKSHETPSSESLINGKPEFSINYPPYALDTDTETHDLAQFGVSPNATMHGNTLRYNLFNTYGYSESKISFEALNSIQPNIRPFLLSRSTFVGSGRYAAHWLGDNKSQWSDMVSSISSILTFNLLGIPMVGADVCGYNGNTDEELCARWMALGAFLPFYRNHNSLGSIPQEPFRWASVAEASRSAIEIRYSLLPYWYTLMHTASVDGTPMVRPLFFEFPKQISLASVDKQFMIGTALLISPALEPNTTYIQGIIPGDNDTIWYDWYNHSVINHDYDENITMSAPLGYVNIAVRGGNIIPLQQPGYTTYESRNNPYSLLIAMDNNGFASGSLYIDDGISMQTNSSLSVKLNSNSNTITCVVSGTMVSSPSLANITILGLSNPPNTILFNGQQLSDYQYSDQTLSLTNLLDLTVDGAFSKNWTVTWS Q09902 MU144_SCHPO SPAC30D11.02c; CHAIN 1..85; /note="Meiotically up-regulated gene 144 protein"; /id="PRO_0000116436" MGKLVKHCHTSLHSELVILFYAKNRFCISIDHLRPLKSHRTHGHYCLLNFSLRENKNYLIIVYLPIEGFSANHMCISHGTSFNIK Q09910 YAJB_SCHPO SPAC30D11.11; CHAIN 1..442; /note="Uncharacterized protein C30D11.11"; /id="PRO_0000116438" MSTVKTFSSTETEGFKKRLLSRRHSSYQVRDEEDDVLEEFIVLKLDLFLTRLNHRMKRLEELGLPNRKDAAAATYQFLANLQASFLGTTILGKTQVSFILRRIEETYNDVLSACDTFPAKAQKALTFLEHHLRDLEDYAEKSKNNVETLMTDIKDVVEHAAKLGAQRLITLEELPVQWHNNPYIIRGYRFYTSKRKCFRSILSWHNETFNIWTHLSAFIVFFAVLAYFYPSSSSWVSSNVSNRIVRIFFLLSAMKCLGCSVIWHTFSSLSNYKHMRCAACMDYVGISALIAASIISVEYHAFVCQGPLRFIFIAFTGTLGLIGIYTPWKKWFNEYKYRSVKIFFFVGLACSGLIPMITMFYIKGTRRTVKYLDPVFKSIFSYIIGVLFYGLHIPERFLPGKFDIIGNSHQIWHIAIIVGVAFHYTGVKRFETDYEAFSCGVL Q09911 YAJE_SCHPO SPAC30D11.14c; CHAIN 1..534; /note="Uncharacterized protein C30D11.14c"; /id="PRO_0000116439" MSDSRQNSQREDNYSRDRRSRFTEDSYSRRDSQRSGNEAPRESRYYRKEEHLQERSRSRSPARDSRWKSSSSGFAPAHPPIEEPTNNGAEAAAAAARRIAESLQSTKATSSRTSYDHSEGITSTTSASPPSAPAPPLPPSSEGPAVDIPPSMADITSKVIEGDGVFMQDVEINNVRNRYILVRASTLSEIENKSGVQLFSKGRYYPNKALATDKDPPLYLHIVSHNRKDLTVALQEIESWINKDMGPLIDERRFRRREDNERNNSNSPRNFSTHGNGNGENGQPRRKWLEEKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAFIEPSTNRESDEPIHLCIMSHDPNAIQRAKVLCEDLIASVHQQYKAWKSQPKDRDQNQGNRAYNPPNRNQAFSARDSRQEKTQPTNASPAPLVTPSLPVPSIPAVPGMEAMAMPPGVTSSIAVPTTSSMPLQGMPTMFGAPGVSAPGTEAPGTGTPGLTTPGVDPYAAYGGYNAYVQYYQQQIYAQMHGVSGDQSHPQ Q09922 YAKB_SCHPO SPAC1F7.11c; CHAIN 1..782; /note="Uncharacterized transcriptional regulatory protein C1F7.11c"; /id="PRO_0000115007" MSASGKKPGTKGTKRHRKITSCRECHRLKLKCDRVWPCENCKKRGIPNLCPNGILVSVSDKLIKLLLSRIDTLQNCVKSVSPNHESLIVSSDDQKIIDDIYEKFGEKPAEDTKDENRSQPIHDPDHPTLEDVAQMLGKLKVGSHGYFNYYGASSSRSCIPQQDPNSEEEDTFMQRPFLYPASSYNSALHWSHRIPNILNPSTLCDMLPVPQFAVRLMGLYFDNVGWSSHIIHRPSFEEACLNLYSAAPDRTNPQPQFLSLTYMVFCLGTLFTSPVLVRNRYSLAHEFFLRAQLCFDISVSGFTPSLDSVVAVMLMAQYSYFCDRLERTNFAWNCIGLAIRLAVAMGLHRDGEVFELSAFQLHMRRLIWSELLFFDRMLSMSLGRPFAISNDQTNVHEPSNVCDIQISSQSNCIPDPSYERTEASFTIFKAKLSKVIASVLDRAFRFTPPSYSEVEALTEQFKVLENELPDYMRISRDTPNLPPMVIIEQYSAKFLIQQALLYLHRPWFVRAATRKEEREHYKSSFNLCTSVSHELIHNLYSLMCLVPVEPLRWWVFRFHSLNAGIIQAAYALCFPNTDYALTAYNDLQYICRIFEHLKGGFMFSNKDYDFLIQLKSKVFNRFQLSSQGLTPEDLTEDVPFLHFNVPSSRPNSKSPDDSSMRAEKAAQLDGLGLSSDDLNTAQSENLPIYEQENPLLFDSLSWHVPKDDTRNDKSPLVPTWNADMMFEEEQKPIVPIDLSSMQDDQVSSLTTNEEFDPLSSFQASHSGSNFWTNMMNEMGIPK Q09929 CAF17_SCHPO TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC21E11.07; CHAIN 22..325; /note="Putative transferase caf17, mitochondrial"; /id="PRO_0000116442" MNRFTVRSKFIKFSFQLFRNYSVCLNSSKSLIRVEGVDAVKFLQGLTTNKITLDNPVYTGFLNTQGRVLFDSFIYPKVSNNGTENERSDELYVEIDKVAESDFLKHLKKYNLRSRCSIAKIPSEELSIKVIWDVKEESRLKDTVAYAKDPRFSKQRLLRMIVPTSTCTSSSSGSLDDYKVFRYRNGIPEGPQEIIPSISFPLESNMDWMKGIDFHKGCYLGQELTVRTYYTGVTRKRIFPFIIPNYEDNPSQVIEPSAPLSIVAKQGEPVSRRSPGKIIAILGKVGLALVRLQYLKSDLACNGIPIQLNTSIWLDELSSTPSENS Q10058 YAM3_SCHPO SPAC1F5.03c; CHAIN 1..382; /note="Putative oxidoreductase C1F5.03c"; /id="PRO_0000116443" MSNSRNIVIVGGGITGVSCLYFLAHHPSFNRDRDTITLFESAGIASAASGKASGFLSLEWHGPSTSSLAALSYNLHKELSDQYDGVNKWGYRALDTWSIKADENCQQPDKLPEGIEWIAPSIVENVTRLGNKKNSGQVHPYKFCHAIYEEASKVANVTLVKGHVLSVDENEVEYRLIGDDYAPDEEEEITSAEELHTIHSMEATHIIVAAGPWTPQLIPNLRISGARIHSITIDLPIKLNGNAVFSEITYKDGTIAAPEFYAREDELYVCGEFDDEPLPELSSDTKVDQDKCALIKQCANHFHQIIRDSPVKVRQACYLPISNATGAPVIGKIGSSIYVAAAHGCWGITLGPGTGKVLSELILDGAVTSANIDLLDPEGSLE Q10060 YAM5_SCHPO SPAC1F5.05c; CHAIN 1..151; /note="Uncharacterized protein C1F5.05c"; /id="PRO_0000116444" MWSKLSISSKINRIRDPESDNTIEDTHVARVMRKYYMDKIGTLPEWLRPPGWQPPVNTGPTSPVSINASNAAPSNLKASYIPANPRRLSSSTSSASSPPLRRLPSVQHSTFDDLFEGVGSLQKSPSTTKPLSSTPSGSLLRSKFDHTRKKF Q10068 YAN2_SCHPO SPAC3H1.02c; CHAIN 1..1036; /note="Uncharacterized protein C3H1.02c"; /id="PRO_0000178014" MLSDDTSFRQISSERILNYTVNKWINDATGFSVASVKTPTSRLQGSFVVATEAHDNLGCPHTLEHLCFMGSKKYPMNGILTKFAGRACGDINACTDVDYTSYELSAAEEDGFLRLLPVFADHILSPILSDEAFCTEVYHINGMGEESGVVYSEMQNTQSSETDVMFDCMRTSQYPVTSGYYYETGGHPSELRKLSIEKIREYHKEMYVPSNICLIVTGCINESRLLSCASGIVKEILANGIITPPTWTRPWCSTNVDYTIPEPILKTVKFSSEDEYTGSVSLAWNGPSALDAYTVFAIETLCEFLSESAVSPFGQTFVEIEDPFCSFVYFYVSLRVPCSIQLFFDSVPLEKINGLEQRALRLLAETKQIDMNRMKDYLKTRRDQYLTNLEAFPSSLFMKILTLDHVYGSREGKDLPNLLKMLEYNRLLEEWEEKDWLKLLKKWFVENNSVTVIALPSFEMAENIKKENAEQLNKRRCLLGASGLEKLAEKLKKSKEKNEQKLSVNLISSFRISDPESIRFYSSTTARTRSAGQPFDNEVQTYIDTDVSSENPFIQFDHIDSSFVQLATYIDTSMIPSSLKPYLSVFAKYIEAAPALLSGTIPTPYHEVVKQLERDTVSLNVSLSFDTSSCGYAYYETKRELLSIEIKVTRENYEKGVYWIRNLLAKTVWDRERMLSVINQQLADIPFQKRDAEFILPSYFDIRLYNDCSLKYSLNTLSQEKILRELRDKLQNDHSSIFDAFQKMRNYMLQHQAIRIHVIGDILKLPQPISTWNKLLDSECHRNPNMEFLSTFSKNYLKPQEFGSSSSLTVIPMPSNESSDLVFSIPGITSWLDPSLPVIVLIANYLGLMDGPFWNTIRGSGLAYGFNMSIDVDGGVLYYCINTSPDVYKAWASSRDLVKSLISGEVQVSSFDLESAKCVSYSIVSELENNAIYSSKNSFTLLSIKGLNKDEDHKFLEKVKQVTLQQFLEGLKIYCLPFFSSSNNLAVITSSLAKIEQTVEQFTEEGFNVNVESLHEIQGIESESEDDLSVGGNDDN Q10069 MU151_SCHPO SPAC3H1.03; CHAIN 1..146; /note="Meiotically up-regulated gene 151 protein"; /id="PRO_0000116446" MSLVAYDSEEEEQTSLVNENNDIKGRSEEPHWKIPNSPKAEVDTELEKKIKQFIKLKAKGIHFHTRLSENENFRNPKLLDNLQDFLDIKEPRGTMISKDMWDPTDFHKNVYASALSKSQDEMIARRENYQKHDRTEIKFQTSQHPK Q10070 MDM31_SCHPO TRANSIT 1..66; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC3H1.04c; CHAIN 67..601; /note="Mitochondrial distribution and morphology protein 31"; /id="PRO_0000116447" MLESRLAKNIARIVQARKPYLISYHVRASTQNALLKQTVLQSSSFKSFPTLPRLAARNISNSGILSRTTPVIIKQISMVRSYSSGDVENPEILNKNESNQSSGVKRAMPFRVLKKMKSFLFKQNKPLTVDNVTAFFSWWLVSHIVWIVVGTTTFFSLLLYTLNTVSAQELLGRWIGQLMTKNTGFQFVFESAIVPNWRKGLITFNKISVIRRPDTLNGIGAQNPNNKSDYEKEYMALRKRYDSNEEPDTEALSQGNYTQFELSIDKADVSFSFARFLNGKGIVKELQLKGVRGVVDRRFIEWDPSSDPRDYRRKHNWGDFEIEKFKLEDLRVTLLQPKGFRKFPVSVFFCELPRLRKQWLFYDLMNAKTLTGSFDNSMFTIHRLQLRPYSPYLKVGKQLDDMRHSRLRIDNVAIDHLNRGVSGAFGWINDGSVDFLVNISFPSEPSENSFQKAWISLMDKLKKKEKDEDVYKDVHFDVNVQLHNPKAVIPIFTNQVSYINNALIRPIIAYINSTRTFIPILCHVSKPLSDFDGSWTFYDSGVLQEISAQVYESFARDVLNQEIRRKRIQKVGYWSLRRFLHLVLVSLQELAPTTSSISNFE Q10072 YAN6_SCHPO SPAC3H1.06c; CHAIN 1..589; /note="Uncharacterized transporter C3H1.06c"; /id="PRO_0000173430" MNPSSSPNRSLNPTRGLNLYSTGNEVTWFSSTVDEVNELKPAKSKAFSISAQDQIYGTSSLKSRFSTHEASSEKDDSSDFTLVLPSNRMYIVIPGLMLSIFLSALDQTVITTAIPTIVANLDGGSSYSWIGTAYTLAQTSILPFCGIMSEVVGRKIVLYTSIVLFLFGSAMCGAAQNMLWLVLCRAVQGIGGGGITSLVTIVIADITPLQTRPYYTGCMGVTWGLASVMGPLIGGAISQKASWRWIFFINLPTGGLSLALLIFFLNLVPKPTVSFRVFLRDFDFVGIITITTGVVLFLVGLNIGSTTGHWAHANVLCYLIFGILCIAGFVVNEFYTTRTRIITPSAFKTLSLTSVMVTSFLHYYIVSTITYYIPVYFQNIKGDGPLMSGVHTLSLAVVSSLLSAVSGMGIGKLKNYRYPMIGGWIVLLAGTGSMIAIYYNTDISRTMGFLALTAVGTGNLFQPNLIAVQASVPPALIATSCSAFMLLRNMGASVGISMGAVIYDQQLTTLLKGTKYSAGLSYSQIASIPNVSEKNFVFNAYANAIRMIWIVNCPVAGVGMLLSFFTKQEKLSQSVTEYKEKDKGFKDAP Q10073 YAN8_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC3H1.08c; CHAIN ?..211; /note="Uncharacterized CCDC90 family protein C3H1.08c, mitochondrial"; /id="PRO_0000116448" MIIRKQIFPFLSQNRPWTIINRIQSERYSASYEPSPELLKQSSRRLEQAGYSVKNAETITNLMRTITGEALTELEKNIGFKAKQESVSFQQKRTFLQIRKYLETIEENEFDKVRKSSDKLINEIEKTKSSLREDVKTALSEVRLNLNLEKGRMKDAATSRNTNIHENETKILNEVDILHKEINDMKIQTNQWFTGFVGVVSSVVLIILFYF Q10079 YANE_SCHPO SPAC3H1.14; CHAIN 1..195; /note="Uncharacterized protein C3H1.14"; /id="PRO_0000116450" MKGCSFLRNGAKFQGKQKGVSSSTLEVHVTILHVNLAKSMLCGFIHVSYTSPNNTSLTTYFEAEIIGNRFTFETKWPEWGASEEIDNRHWKRLGALKSNGKDIPLRLIQPYDPLSRETVYMRWKELAMLDKTVDYQNHNQSFPFGISYEGFYYISFSQSTGKIKGYYYHHSEPEKVLFLELNPIIDRTFPVIEFQ Q10080 YAO1_SCHPO SPAC11D3.01c; CHAIN 1..79; /note="UPF0654 protein C11D3.01c"; /id="PRO_0000116451" MPNPGNVIGGHKAALHNPNVSEETKQREKEYLEEHEGEVGEEHQKNTGNVRGGYKAAMHNPNVSGEAKQRAQEELENLE Q10081 YAO2_SCHPO SPAC11D3.02c; CHAIN 1..150; /note="UPF0039 protein C11D3.02c"; /id="PRO_0000201930" MSNLEFVYKYFNSLDVKELYDIYLLRTNVFVVEQKCAYPEVDEIDLKCGHLMLRNANGKLVAYARLIPEQQQTVRIGRVVVDPDERKNGYGRKLMLQALETSKQEFSSSKTFVLSSQEYAQPLYRSVGFKKCSDAYLEDGIPHVEMRLEL Q10084 MFS2_SCHPO SPAC11D3.05; CHAIN 1..546; /note="Uncharacterized transporter mfs2"; /id="PRO_0000173444" MDLLSLITGKKFEKHYSKVGSRFSDESLNGLEKQLSNGADAAIDTTADDRGSVVSLGASLPLSQGRPAKSKNILNDTLLAEDQYLVTWDGPDDPLNPRNWSHSYKWWIVIQVSVITIVVTFASSVYSSGIIDIASELHSSIPVSTLGSCTFLVGFGVGSLPFAPLSDIYGRFIIYFVTLLIFTIFQVGGGCAHNVWTLAIVRFFQGVFGSTPLANAGGTISDLFTPVQRTYVLPGFCTFPYLGPIIGPIIGDFITQSYLEWRWTFWINMIWAAAVIVFVFIFFPETHEDTILDYKAKYLRKTTGNTAYYTIHERERDPKNAMIQAATQAVSLIFTEPIVVCFTLYLTVVYIINYINFEGYPIVFAKYGFNKGEQGLSFIGVGVGIVCAGLCTPFIYWHYLKVNKKRNGVICPEDRLYPLFIGCFLLPISMFWFAWTCYPHHIHWIVPIIASAFFGFSLLIVFFVSYNYIIDSYQHMAPSALAAATLVRYSASGGISMVARPMYLNLGDHWATSVLGFISVAMVPIPFIFYRFGKSIRAWSKNAYKL Q10085 YAO6_SCHPO SPAC11D3.06; CHAIN 1..455; /note="Uncharacterized transporter C11D3.06"; /id="PRO_0000164257" MGRPLTEVKYLLINSAPVILGYALQNSLQTSSVIVTGRLGPSELSVAAFAYMFAMSTGWLIALGGTTAFDTLGSNLWGAGKKQELGILLQTGFIVLSILYLPICLVWWYSKPILIFLHQTPELAEASQKFLRYLIPGGLGYVCFELLKKFLQTQEITRAGSYILLVTSPLNVALNFLLVHYYGLGLKGAPLATGLSYWLSFILLTQYAKYVKGAEAWNGWNKRCLENFGPFVKLSLLGIVMVGTEWWAFEIVALVAGKLGAVPLAAQSVIMTTDQLLNTIPFGLGIITSNRVAYYLGAGLPDNASLTAKVAAIVGVAVGSVIMITMIAVRNIYGRIFTNDPDVIQLVALVMPLVAAFQISDSLNGTMGGALRGTGRQKVGAIVNITAYYLFALPLGIYLAFHGKGLVGLWIGQVIALSIVGILELKIVMATDWISQSRKAISRFGDSSELTALLN Q10086 YAO7_SCHPO SPAC11D3.07c; CHAIN 1..637; /note="Uncharacterized transcriptional regulatory protein C11D3.07c"; /id="PRO_0000115008" MSQNKACDLCRLKKIKCSRGQPRCQTCTLFQADCHYSNRARRKRLVQRSKETFGGITLPVFDYAAGINGNEPEPSDHSIPNQENFALTTNGTISKNIEKPEDGEESVQRRLKLLEEKIDLLLDIATETSEFKRENKAIELPSLVTQIKDAESIVIKHRQGSPVDNTPTRILNVESLFPPQLPDWEKAFHDIPKKEVAHELVTSYFQHVNWWWPTFVYNDFMYEFERLYAFGFHSNNAWLISFYSILALSSIRKRLGNSKTLAESLFSTAWVFVQKSDFFLTPSIDKVQALIVMTQYAAYLSSSSLCRTLCGQACLMAQQLNLHRKQSTDVEPEKAESWKRIFWMCYILDKNISLIFGTPSVFNDKDIDCNLPDSKYELLFGVQSGGDLIFVPTVSLTIIQSEIRNRLYSVKSPTQMAAREKIIIPIHQKLKAWEENLPSEIKMYHEMLLNNTFSPTISLSDRFEFLTFAGMEVYFSYLNTLIILHRPSSSTENRRICINAAREAVQLLKNRLNIDLRVNVKADPLWIFLYCPFTPFLIIFNNLVHETDTETDSETLLNDLDLLHVIYDFFMEMEPVSDVALELVKIADKLLRVAKEVCSAKNNDVTDSTFKDIVEGFELNDLNSWDFDRVTNVMRNL Q10087 YAO8_SCHPO SPAC11D3.08c; CHAIN 1..550; /note="Uncharacterized amino-acid permease C11D3.08c"; /id="PRO_0000054170" MSDIDKESLKQNQKQWENEVELGESREANQDDELLMSLGYKPEFTREFSYVSIFGQSFGSMGLCPAMAGSLIFSMNCGGGGMVWSWIIGCICLIPVSISLGELASSMPTSGGLYFWIFTLASPSSRAFLCWVCGYVSVLGYATIYASTVYSASSMVQALAVIGSPSYSPTKYEQYGIYAALLFVISAMTAIPSRVIAKVNIINITFQFLVSIILIIALAAGSDSTTRNSGSFIFGDFTNYSGWSNMGWAFILSFTTPVWVVSGFESSAAVAEESTNAAKAAPFAMISSLGVATILGWCIVITVVATMGHDFNAILGSSLGQPVAQVLVNNVGNKGALGIFSLLVIALCLNCISLLIAASREVFAFCRDGGIPGSRYLRLLTKQKVPLNAILLVLLYSLLVGLLILVNVTAISSVFNLAIIALYIAYSGPLMCRFVYNKFQPGVFYVGKWSKPAALWSLVWMWFMILMLLFPQYQKPNQDEMNWAIVVLGFVMVFCVVYYYLPKIGGKTFFTGPIPTVQQENEYISGVPLNELSLSSLPLPKDFDQKQITE Q10088 SPEB1_SCHPO BINDING 186; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 209; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 209; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 211; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 213; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 307; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 307; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 309; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" CATALYTIC ACTIVITY: Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145, ChEBI:CHEBI:326268; EC=3.5.3.11; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; SIGNAL 1..20; /evidence="ECO:0000255" SPAC11D3.09; CHAIN 21..394; /note="Putative agmatinase 1"; /id="PRO_0000002091" MALQSLFLILLAGAAQLAQAHPKIFEQSRANAVETFDDAFPGDGETQADSVFSGIATFGRLPYWKCLNDKSQSFDIAFLGAPFDTGTSYRPGARFGPSGIREGSRRLNLYGGYNVPMETNPFNNWAKIVDCGDIPLTSYDNAVAIKQIENGHFELLTRKPTSYSEKDGYALDGSVLPRVITLGGDHTIVLPILRSVSRAYGPVSIIHFDSHLDSWKPKVFGGGKSSVGSINHGTYFYHASQEGLVSNDSNIHAGIRTTLSGLSDYDNDADCGFEIIEAREIDTIGIDAIIKRIRDRVGDGIAYLSIDIDVLDPAYAPATGTPESAGWTTRELRTILRGLDGIKLVGADIVEVAPAYDFAEVTTLAAADILFEVMSIMVKTPVYKEQAKQQSRFY Q10093 YAOE_SCHPO SPAC11D3.14c; CHAIN 1..1260; /note="Uncharacterized protein C11D3.14c"; /id="PRO_0000208583" MKQDVRIAIDRGGTFTDVYYKISGWREQEGIFKLLSVNPKLYDDAPTEGIRRVLCYASGEEIPRKVPLDLTRVSSIRMGTTVATNALLERKGEKTAFIITEGFRNLVEIGNQARPDLFDLTVSRPSPLYQRVIEAKERVVLENQFSKTAGIVQGITGEFLRVEKKLDEEALYQDLKELYNEGFRSISVSLMHSYTYPLHEEVVEKIAKRIGFTDISLSSKLTPMVKIVPRAVSAIIDAYLSSTLRYYLDSFKKNFYNVKPNTIQFMKSDGGLVDIDNFTAISAIMSGPAAGTVGFAKTSSLHADDKTPAIGFDMGGTSTDVSRYDGKFEHIYEANIFGLYIQSPQLDIQTVAAGGGSRLFWRNQLFSVGPESAGAFPGPACYLNGGPLTVTDANVLLGRIIPDFFPKIFGPKENESMNKDIVIEKFSELRDIINIDIEKEKTIEEIAMGFIQVANETMCRPIRKLTESRGLDLSAHHLAVFGGAGGQHACAIASLLNIEKIIIHKYSSVLSAYGLALAHVTHEEQMPCLSVLDEDNLPLIQSKFDVLDKKAVSFLENEGYLESQISTELFANLRYEGNDTTMMIAKPKDSWDFKTLFEESYKNQFGFSLIDRKIMVEDIRIRAIARASNQSEVDTVFASETENENTVFIRDNKPTMYTPVYFAEVGKVNCHVYQLSSLPVHSLITGPAVIVDTTQTLLIEPSFTAKIFARHVLLEKTKSTLVVKKNVDLDPITMTIFANRFMSISEQMGQVLQKTAVSVNVKERLDYSCALFSPDGGLVANAPHVPAMLGSMQTAVKWQHNYWKGKLVPGDVLLSNHPIAGGVHLPDLTVVTPVFDNNKDIIFYCAARGHMVDVGGITPGSMPSNSKAIYEEGAAIKTFKVVKAGTFDEKGLTQLLFDEPAKYPDCSGSRTLRDNISDVKAMLSACHRGRSMVEKLVVEYGLDIVQRSMYGIQAAAEKAVRDVLKAFSVQNSQKPLKAIDYMDDGTPLQLEVKIDPETGDAVFDFEGTGPEVYGNWNAPIAITYSSVIYCLRSIINQDIPLNEGCLKPIEIRIPPSCFLNPSETAAVVGGNVLTSQRITDVILKAFSICAASQGCMNNLTFGYDGENGEEGFAMYETIAGGAGAGPTWNGTSGVHTHMTNTRITDPEVVERRAPVILRRFCLRENSGGKGEYHGGDGVIRHFEFRRSMHCSILSERRSRAPYGMNGGEDGAMGVNTWIDCSNPDFPRYVNLGGKNHVLMGKGDHIVIETPGGGGYGAVSI Q10094 YAOF_SCHPO SPAC11D3.15; CHAIN 1..1317; /note="Uncharacterized protein C11D3.15"; /id="PRO_0000208584" MSVKIHIDRGGTFTDAIATFADESRPPIVIKLLSEDPSNYKDASIEAVRRILEIVQGKSIPRTEKLDTSCINHLRCGTTVATNALLERKGERCAFITTKGFKDGLLIGNQSRPNIFELGIRRPEVLYSKVIEVDERVTLEDYVEDPMKVKTTIDGSDPSLVVGRSGEVVRIMKKVDCDALRKDLQALYDEGFTSIAVCLAHSFTFPDHELLVGKIAEEVGFSNISLSTKLMPMIKYVPRATSATADAYLSPVVRRYLAGFQSGFLHGLKTKDNSKGVRCEFMQSDGGLVDVNKFSGLHAILSGPAGGVVGFALTSYDEDVKIPVIGFDMGGTSTDVSRYGGSYEHVFETTTAGVTIQSPQLDINTVAAGGGSRLFWKNGLFVVGPESAGAHPGPVCYRKGGYLTVTDANLLLGRLLPESFPKIFGPNEDESLDVESTRKEFEKLTAEINSGLEKERQMTADEVAFGFIKIANETMARPIRALTEAKGHDISIHRLTSFGGAGGQHCAAIAKSLGITQVLVHKYSSILSAYGMALADVVSEVQEPSSFTLDDSNTESIKKRFDSLKEEAKANLEEQGFTESQISYELFLNCRYQGTDSTLMISKPLESWDFKQSFFDKHKQEFGFIFENKDIIIDDIRIRASGKSFQSKEPSVDAQLKELKFEPVQKSLATCVKDIYFEGGRVPSEVYSLDNLPVGTIVNGPSLIVDKTQTIVVPPKAVARILHTHVVIDISHGNEYTANDSLAKASTIDPIYLSVFGSRFMAVAEQMGRALQKTSVSTNVKERLDYSCALFDAKGNLVANAPHMPVHLGSMSTCVRTQAKIHEGKLKPGDVLVTNHPSYGGTHLPDITTITPHFEGDEIMFYVAARAHHADIGGILPGSMPSSSKELSEEGATIKSEKLVVDGVFQEERMIDLLYNEPAKVEGGSGSRCLRDNLNDLKAQVSANQKGINLITSLIKEYGKNSVLRYMKAIQENAESAVRQLLLGVRERFLGEDLYAEDHMDDGSKICLRITIDEENGDAIFDFTGTTEEIYGNINAPEAVTYSAIIYCLRVLISENIPLNQGCLLPIKVIIPDNCFLKPSETAAVVGGNVLTSQRITDTILKAFQACAASQGDTNNLTFGIGGKDPETGEVKPGFGYYETICGGSGAIDGLDGTSGVHTHMTNTRITDLEVLERRYPVILRKFIIRENSGGAGKYKGGDGVIRDIEFRIPVTLSILSERRAYHPYGMKGGKDAECGKNIWIRKDILPSGEQRVRQINVGGKNTCHMQAGDHIVIMTPGGGGYGPPSERVDTVKKANGVQHFRANGTISQLQEIQHTN Q10096 YAOH_SCHPO MOD_RES 553; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC11D3.17; CHAIN 1..585; /note="Zinc finger protein C11D3.17"; /id="PRO_0000046866" MVDHVSENSTNVLSAKRKLTEPSLIDSKRVFPCDQCAKRFTRHENLTRHKACHSKAEPIPCPYCEIKCKRKDLLKRHIQRFHNDKSVIEEGSKDVLDVKAAASQQEDNMKIVLPSFDAIDVPKAYHPSLRPYFTILPLIPSDFLEHYIEGYFEWFHPVFPFIHQASFNSENVAASFLRSLVVIACLCTGIESDFSMALLFWDSGFHVLQLYLQGDPERVKKAWVFQSRLLFCTASLFEKTACFSGIGHVLLKDLVHESRTFGWTKLNWSVEGDTDISNLIDLECIRRSVFCLYILEWFLALIFNKPPSLSVLELQMPLPISSALWSSKELLSKDYWRPNPLNPRDALSILVNGPLLLEETNISGFVLLFAIFEFIRDEAKLSMIGLPRQPNRSYEIMLQHLKVSMELSNPCAKTSSIFLCLWHLVLTYYYLPDPLFLRSITLTDLESATSYFKDDSWMDDDYISPCMTTYNLTMGWENVIWGLRYAETELTKFKFDLPVPHLTLFRIFLQGLYALRDFDQISTSSLQTFTMLWKKLSTSLNMKEDAQNTAPSTCVKEFSAFVASALDVEGGWGIGPLLTKAFRPT Q10097 YAOI_SCHPO SPAC11D3.18c; CHAIN 1..498; /note="Uncharacterized transporter C11D3.18C"; /id="PRO_0000121374" MSDQSEYKISKDDEHSIYASEINKEKLQNTASPDVDYGDTASLKIDPKVEKKLLLKMDLVISPIIGFLYLMAFLDRSNIGNAAVAGMTEALSLYGERLNVAVSIFYVLYILVETPSVVLVKRIKASRMLAFISFAWSMTVLFSGFMSSYGGLIATRLILGLLEGCLFPALNLYLTTHYTRKEQCQRLSYLFASAGLAGAFGGLFAYALEQVHAGNKEGWQWIYIVEGLVSFIGVPLCLFALPDKMENAWFLTREEREVAIIRRDINARYHGEQHFEWSEVRKAFKDPKVYVSATSQFCADMVLYGFSSFLPVIIKGLGFVGLQTNYMTIPVYIAGVISFLFVAWLSDRTQLRAVYLISASTVVAVGYIIMLASDSNAAKYTATYIIAIGCYIGPGLNLGWLNNNVAGHYKRATAIGIQQTLANSSGIVAGQIYRSKNAPKYILGNAFTLGCVIVGGLAYVVMFFSLRYVNKKRDERCARGEFDPSAIGDFADDFRYYL Q10100 NTF2_SCHPO SPAC15F9.03c; CHAIN 1..123; /note="Nuclear transport factor 2"; /id="PRO_0000194790" MADYNALATQFTQFYYQTFDSDRSQLSSLYREESMLSFEGAQLQGTKAIVEKLVSLPFQRVQHRISTLDAQPTGTTGSVIVMVTGELLLDEEQMAQRYSQVFHLVNNNGNYYVLNDLFRLNYG Q10108 YAQ9_SCHPO SPAC18G6.09c; STRAND 156..159; /evidence="ECO:0007829|PDB:5J3T" HELIX 169..171; /evidence="ECO:0007829|PDB:5J3T"; HELIX 176..178; /evidence="ECO:0007829|PDB:5J3T" CHAIN 1..312; /note="Uncharacterized protein C18G6.09c"; /id="PRO_0000116459" MQKDIGRRFQRNKKKINSKPGGAMVASSDVEFSLDGMSIMPQRDGNLQIPNFVKPKSTFATSNIGESNGKRNGDKVRGNRRSKSGHSSYAGSRISGGNSNSHLPSGVASAPAGLGIDKVAVGEVDSHLKSVSSYVSNSSGADRSFSSNSSSDTNSILYAGPTFTHSPAASNLPIPTFLHSPVSEKAEWQPPTGSVNSNMPFQFHQSSSVPSTPSEVAMGHNFCPMSRNDPSLQSIQQTNGFYSGHNSPHTNYSASTPSFNHFNAAGHPTGNITPTLNSPNNGIHCHSTSALDLLFHRDREQRLFRMLRQGSA Q10138 YAS2_SCHPO MOD_RES 40; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 43; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 418; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3H8.02; CHAIN 1..444; /note="CRAL-TRIO domain-containing protein C3H8.02"; /id="PRO_0000210748" MPEGAGRPWNLTELEEEKLKTMWSYLFKLFGITLLERTESWYTVKTHLSDDSSSSSSHRLSSVSYAKSRTRLELTSSSHGSDTRSFNDKTKNVHLERVEKIASEWDPEGLRVCFWDAVNCDDPDGLLLRFLRARKWNVEAALEMFMKTVHWRSREMNVGEIVCNADHLDKDDDFVRQLRIGKCFIFGEDKHNRPVCYIRARLHKVGDVSPESVERLTVWVMETARLILKPPIETATVVFDMTDFSMSNMDYGPLKFMIKCFEAHYPECLGECIVHKAPWLFQGVWSIIKSWLDPVVVSKVKFTRNYRDLQQYINPDNILKEFGGPNPWRYTYPEPCQNEAEALKNVEARKSLRAKKDAIAKQYEEVTMDWILNNGDMAEVKQKRRKLASQLIDAYWNLDKYIRARSVYDRMGLIAPQTSHTLLLSQPTNGDVKESMVEVTSSAT Q10139 IMG2_SCHPO TRANSIT 1..15; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC3H8.03; CHAIN 16..105; /note="Large ribosomal subunit protein mL49"; /id="PRO_0000116464" MRSSLKPVLSNLRFNSTIASESLRFHVSRTPSKNLPVYLDYKQRGTKILTLIRKIHGDSNALRLRLISTLKMSPKDVYVNKLTNQVVLKGNHIVTVREWLQDQGF Q10141 YAS5_SCHPO BINDING 392..399; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SIGNAL 1..36; /evidence="ECO:0000255" SPAC3H8.05c; CHAIN 37..1073; /note="Uncharacterized protein C3H8.05c"; /id="PRO_0000014191" CARBOHYD 132; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 544; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 632; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 703; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 732; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 953; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MAEIIHHSNVFTWAFHVSEYDGAPLLLLGSFSSVASVSLKRSGDLLLFERFTLPARTRSVALLSSHFLQSESGRHSIANILIATENGKCYLLQLVKTPEKAFPTIRIRDEFVLDTRMYNHEQLGKSIDLCPNASLWATNSFAGDIVFFFSHHPSLSKQVFAQLSIDGIILHTIFVPPKRSSSSCVTYVCLFLDSNSNPRINVYRWSKTETFSDASSYITFSIPVPSEFSLASHIIPCSNIPDHFLVLLETKICLLSVPQIECGDLKFLQTDLPCSGSHNYPLSIANDNETPNCCYLTYENGDLYRIRYSILSIDINLIGKTGSSLGNLILPCYPYIVFCGDCSDTLVYDVSVSPMSFFGSLIACAPMWDFVYSSSRHNTLLDEDINCNTVYATAGIGKSGCLVTMRYGCSSTTLLEAILTEGAVLSGIINSNHNSEFYAWLTYPWQTQILRLHLDGVVEDVTESLFLDDIKALYVINYQNTFIIITGKSIYAVTPSCTKYNLLEVSGDEEFVLAAYNELIFIVKKDLMNFKSQLLTLKLNTLSNGTLELQSLPDSFDLHDVPTCITSFSLERKLLVILVHPSPYFECVFYDETSHSSVYKVPLTGFQFGYLPHSISYLRKSNRAVYVLISSNSTLLTVYVTLTLEGVPDFKVYSNPISTDLPLTLQSPSDEFSTIYAWSDYLYIVGIDMETEQPTLNQILEVNDSFTCVSGIYDIPNKFQNSESRIIVYYSNNTLYLSELWLPQRTFSSKLNLAATPKRLLVDKYTNTLIIGCCHVLVNEITTSGLAFYDLTNSRLFPVNWPSMDIKGKPIFKPEELLYSMSFWIVADDQKRKYRYLCIGTGVRKNGLTTGRLLILTMNKDHDSNAIELRNVITINMKDPIYSVCSIGKHGLCYATGRKIGVKMLDLDSKKFCNSDCELPVRSPIVSMSTYKDYVYTSSLRDSVAVFQYDSENNSLNLVCSDTSSRLGIDCFYISQKKLLFSCDKDRLLTCFKVEGEVCTSTREQMLQPILTTVSQTKTNALTNHLKYSVIRVDKDNHNIVWGLMGCTLDGNIFKILMPNDPTSSDTIIYSDT Q10143 PFD3_SCHPO SPAC3H8.07c; CHAIN 1..169; /note="Probable prefoldin subunit 3"; /id="PRO_0000153658" MSSSNPRGIPPAQFFEFKELSMEEAQGHLEKFQEAIAKYKFMETSVVRRVASLDDKIPDIRKTLQSVQFLKERQGDSFTVTYELNDTLNAKAEVEAKDNVYLWLGANVMLEYTVEEAEALLTQKLNSAEETLKACKEDLEFLRAQVTTMEVNTARVYNYTVLLRKKTKM Q10144 YAS8_SCHPO SPAC3H8.08c; CHAIN 1..563; /note="Uncharacterized transcriptional regulatory protein C3H8.08c"; /id="PRO_0000115009" MSSSPPALKKFRKRSPKSCLICRRRKVKCDRQQPCSRCKERNEVCTYADDTIDKMNVGPHPSHSENASDSETTLEVSPDINPKKNEKFDFYGWRSLFELIKYRKDSDMCSSRPSFSIQAYSSYKDNVVVESLANLLPPFCISQKIVNLFFKTLNVVCPIYDQETVEKSLNNIESPESFSYEDAFTLLPIIAATIQLSDLPDVILNFYNSAGITPLESSRLINLKLNEISEQEYKHLCLPDKEIIQMLLLRAYATKFRTRIRGVNTDLCRSIHVSTLVTPLFQVTEKIGKNTSDLWFALCEIDGLECVLKYRPPFIQHDTYGRLKPLRCFFNDDISYNFHLLLGRLLDCGVSIYKSVHSLTVSKFIDKLESYESQLSLILVDIEAKFYDPSNEDIQFRYIFLKMVFWTARVNLYQCFITLDSGILEDEETIIGNLGESCIQCVRLLISQITILEKRGWLLVALLEIIHALMLAAFCRDKGFEVPSDLGDITLYVQERMVDIVTFDDGMAVRFGYVLRFINSMLHPNEPPMQDAEPETTEDPSKLFADIFDFTSNYFIPSALLDQ Q10145 YAS9_SCHPO SPAC3H8.09c; CHAIN 1..738; /note="Uncharacterized RNA-binding protein C3H8.09c"; /id="PRO_0000082019" MSSSSKDSSFQVETPVQNILETSTNSELQDQVSSPYEPDYNSPVKQAAASISALQTQDDTLFNNVDERTLENKDGNKSDDANFDQVSGIPSGSLEIPILNSATSNIRLTPSDTYNNIPVSDTNNEEISKNIYGAPILESTSSDFQSKDSLSTTQPSVSGGNGSTSQSPPSLDVEQNKPFSISNEPVEQETENSSTKDLQVYDFQTASEHLPEQSLQNTTYYDPSKTYSSVNFEEIEYGKSHEKLDLPYRTTDFIPYSKDLSTSPEAHRTSIYSYSANLPNYYNEHNELHEHHNPQTPSSPESAYSPENLQLNHEAQNVEYLGNNAAEKSLQMNLEDEQRFQQFLKDEESIMSNWYPGQFPSASRLFLGHLNTKSLSKRNLWKVFKIYGPLAQIVLKANYGFVQFFTNEDCARALNAEQGNFVRGQKLHLEISKIQKKYQNQIENMKKGSHVTKSNQYSEMIGNLPYPTSSRKRTRSPLMSKGKSYDRKGSISMSKNFSPDCEILVTEDCPKEFVWGVEKVFQERRLNIHTTCLYRDSNLQVIIKSCIINSVKSIILINAGLAHLGKVSVQVFKDGSSDSEVRCDEYAAVDVMVAASIVHHAKTSLMHSAASSTPSYNGERIVPDVPSPCISTNPNLPALVGSLDSVNLHHLLGFIQNTYSTTSYIPTRVSFNPNDTGGSFGTITSQSQFVVNEMPKNYARDNYEALHSQESRQRSSVAGNKQLQKILEQLAELKQPDF Q10149 YAT2_SCHPO SPAC1D4.02c; CHAIN 1..345; /note="Uncharacterized protein C1D4.02c"; /id="PRO_0000116467" MFGGLKNFIKEKSEALAGIHRESDESCGFRVLKVENDSKAYNARIESYYDFITAVNGILLNGDPSMFMALLRDSSPEVTLEVFSLKGQITRKVNIKINSDEKIGMVLQWASIAPAVDAIWHILNVIDDSPVARASLVPYEDYIVGTPEGMMTGEKALSDLIESHLNRPLRLYIYNHYRDSTRQVTIVPNRHWGGNGAIGCGVGHGVLHRLPAPLSGPPPQPGDIVFSNPMLGGPDHKVSQPSETENFLPTPEPPKIASANAGSSNEISIPHYQRHKKSHKGAIQDSSIQSYLDEEEKLSRELDHKTKDASSTNDSQTTPLPPPPPVAVNSTNDESAPQNEELVKN Q10151 ERD12_SCHPO SPAC1D4.05c; CHAIN 1..387; /note="Protein ERD1 homolog 2"; /id="PRO_0000116469" MDLEVVEFPLHHKLALPFRIGLLVIVGTWLWSVCYHLIYILNRYQPISPNPRGSLNSKWYHLLQIPLSNRHTDLEENTEFKANLVSPVDFHAGYCFAAILSISWATGFILFLKKTQGDIGGLYSHPIYPLLWVITAFILIVFPFPWRYRSSQRGLRKSIIRVFLFFQADFRSPYKDFIVSEIFTSYAKALGDFYIFGCVLQGHISKFTLRPDLKCDGTFFVPLAMAYPFIVAILQCLHYGLSRRKHTFKINLLSALKHATALPVIYLSAIIHAKQTKFTLTSGHGYLFWLWILSALLSSAYTFLWDVFIDWRIRFPFHKSINHKRFPMFIYAIGCFINFILRVTWSMKLHPRLHQFHEYEMGIFSFEMLEILRRFLWLFFHLDAISS Q10166 YAUB_SCHPO ACT_SITE 83; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 154; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"; ACT_SITE 195; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" SPAC26A3.11; CHAIN 1..322; /note="Hydrolase C26A3.11"; /id="PRO_0000213254" MNSKFFGLVQKGTRSFFPSLNFCYTRNIMSVSASSLVPKDFRAFRIGLVQLANTKDKSENLQLARLKVLEAAKNGSNVIVLPEIFNSPYGTGYFNQYAEPIEESSPSYQALSSMAKDTKTYLFGGSIPERKDGKLYNTAMVFDPSGKLIAVHRKIHLFDIDIPGGVSFRESDSLSPGDAMTMVDTEYGKFGLGICYDIRFPELAMIAARNGCSVMIYPGAFNLSTGPLHWELLARARAVDNEMFVACCAPARDMNADYHSWGHSTVVDPFGKVIATTDEKPSIVYADIDPSVMSTARNSVPIYTQRRFDVYSEVLPALKKEE Q10174 YAV5_SCHPO COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305}; MOD_RES 305; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC27F1.05c; CHAIN 1..484; /note="Uncharacterized aminotransferase C27F1.05c"; /id="PRO_0000120542" MIDSTSTATATSKTVELNTNGSKTDASSENGTASNYPEGLWCFDEAMKMDPETTVKLQLDHLNKLRTVHGHARNFVKADNSRFVDEKGTEHLDLIGGVGVVTVGNNNQYVWDCLQKCFDAKLYMMGAISYRNLAAAFGRNMALLSPGQKLTRTWTATGGAEANEGVIKLIRLATRYKPNKKKFLSTLNSFHGKTTGAVFLGGKEKWQKYQSPAPFDVDYVPYGDAEALQVALSSGMYRSFIVEPIQGEGGVIVPPPGYLAKARELCTKYDTYLVLDEIQTGCGRTGKFWACEYENIIPDCIAFAKGFSGGLIPFAGYIATEELWNAAYNSLETAFLHTATYQENTLGLAAGVATIDYIVQNDLLSRCRKLGGIMFDRLNKLQTKFPHVMKDVRGRGMIVGIEFYPIPESVQEEFGEYYATPIVNDLADTYHVQVYCSLNNPSVFRFLPPLTIPEADLDEGLSAVESAVAKFDAKVKEAVAAKST Q10180 MU113_SCHPO SPAC3F10.05c; CHAIN 1..326; /note="Meiotically up-regulated gene 113 protein"; /id="PRO_0000116477" MKMPNTLHSVSISTDFPSPNVESEAADVNEYSSTSKFETLGNQSSTNLGFSNSLQDKWDCWKRDLWSIWWSLSRKATRFYRWLSRSLKWRPVTYETVYPQTYETQMSEPREVTTIVKDLNNGDSFVLNVTEPVDPEFLRANIPPVHRKHLPPRLSLVASPGTIPTRGVVVLEDWINPLLSERCKLLLQSELCNQDSYDCPGYICVYRFEQKNNPSVVLGDSTLIQISRVSDLQRHLREYPKNCAFSRSVLEIFPDPGKTSKPCQVSFKVERLVHKELNEYLSWMQPFTCDSCGSLHENWLQIDSKQWDQIRGVILRWVEYSRVIYA Q10181 YAW6_SCHPO SPAC3F10.06c; CHAIN 1..453; /note="Uncharacterized protein C3F10.06c"; /id="PRO_0000116478" MDEFDPLDAVQQIHVQARHPKNRLLSIAHDAKFVDSVIASYPTFKPVVNERCGTWYVNRRHAPISVYFKSTDGHTGQWSFSCRRLNLHLLNEITTCDGLIIVDSTRRGKRMPDALSKTIPIWIATLNKCVFERLRPHSFPNARLAFLPPFLPDTEKSSILQRLDGFVDSLMQSGIDLDALAAKLTKPIRPLWVTPASRLTSAQFEEYFTVVLVTASAQVQNGYSREHGFLYVQGAADDEEEWSHGLTPEVFWQNTESILTCPEEQLEQKISLLLSSTRNSPTMSNSSLTHLLPTPIFVGDVTGFYPPPENTSYFVLNLSNTTLNVKNELCFPIPSGKKGAPVFRKHFPSILQELNSLDPPFYERDAIFIVDEGNAKEAASCLALMILCLYYDLHMHLLAHPISLSASQSHLTKQTVRQFLVKITELHSKTNPSRAFLLAVNSLLLSANTIATS Q10183 YAW8_SCHPO MOD_RES 127; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC3F10.08c; CHAIN 1..259; /note="Uncharacterized protein C3F10.08c"; /id="PRO_0000116479" MSENALLALQRHFEDQFGHIEGLQPVSAKPSETAFNSDASEKEQSPTTSNEEEDAISDMEDKEDVSFGSKILRVSHQEVEKPTLSATVGRVSFLKKMPKLEDEEEILAKKREEQKLRKRSRQNDDGSDDDEVENLKNDLELQKLLRESHLLHEATSRTGQVQLVAEGKIRHKVVQQHIAQLGGKKETEKMPMAARRGMKKKQKHIEKVIENEARESGTVLAKKRKERKQFKKGFRPVTFSAPGKLVGGTLLLPKSMIPK Q10184 HIS4_SCHPO CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469, ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16; SPAC3F10.09; CHAIN 1..264; /note="1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase"; /id="PRO_0000141961" MEKSQHTLFRPCIDIHQGQVKQIVGGTLGNDADVKTNYVSLKPSSYYAELYKLNHLEGAHVIMLGPNCEEAAKTALHTWPGALQIGGGINISNAQNWLQEGASKVIVTSWLFPDAQFDLDRLKAISSKIGKDRLVVDVSCRRKDNRWFAAINKWQVMTAFELNEENLDLLSQYCSEFLIHAADVEGLCKGIDEDLVIKLGEWVKIPTTYAGGGRSIEDLDLVDKLSKGKVDLTIGSALDIFGGVLEFTRVVAWNRRFTPLPLQD Q10186 YAWC_SCHPO SPAC3F10.12c; CHAIN 1..201; /note="Uncharacterized bHLH domain-containing protein C3F10.12c"; /id="PRO_0000127507" MQRDMSINHLLPPLSGPGQVEQLTGFTNDIVYNDFYAHAVSYNPYPSEKIDFPKKNTAHKNSTTSTVASSGNTTMEKPCVGSEEWYKAKRLSHKEVERRRREAISEGIKELANIVPGCEKNKGSILQRTAQYIRSLKEMEEMCREKSNLEKLVADHTIQELARENARLKSECERAWRSVELWKQAARSFDSELDVEENSES Q10189 SPO12_SCHPO SPAC3F10.15c; CHAIN 1..90; /note="Mitosis-specific protein spo12"; /id="PRO_0000072132" MSETQADSIAKSSVETTIQPLHQESATLRQQVLQKHELPKHALNVASPTDSLMSPCTAKLQAHKKKYYMKRKPPVMSLQNTLQSVQTEKE Q10195 YBY6_SCHPO SPBC11C11.06c; CHAIN 1..178; /note="Uncharacterized protein C11C11.06c"; /id="PRO_0000116534" MSAKEGSSHPSYAEIVREHAPEQTAAEKAAPQPPEVEEVLSEEPYQKNEKVVVLDEEDADAFLHPEEAEAKKESEKPSDGEKKGKTEKLEKEAKSVYSKACNFVNAHKVPASAAISINLLSLGAISAYLLKSRQSGTLNNRTLCTCTAIAGIVFTISAVFSKTPKTACCASKKSNKST Q10196 YBY5_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPBC11C11.05; CHAIN 22..284; /note="Uncharacterized protein C11C11.05"; /id="PRO_0000014193" MKTTMLMLVLLVCSYIHYVCAQIRFVTPATTDSMDFTAISFSWEESNTGIPLEDITNTVFYICSGSMDAPQPCAVLYTSPSPSSISQAGPFAISQVFGPAGRLYFLWAQSTYAGGIVNDYTDFFTVNGLTGTFDNYEIYASLMALGVYPYVPTLTGFSTFLGVWPTGTMRDWYLSQTTGVLRTGPIQNRPDSTFTAATTDIQPLWETSSYSVFTTFAGPPIATSTVFASPTYMYTLYANYASTASKPTIIATPTAGLRRRDSWAQAAPKRGMRLGEHKRGLLYS Q10200 YBY1_SCHPO MOD_RES 40; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 42; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 371; /note="Phosphoserine"; /evidence="ECO:0000250" SPBC11C11.01; CHAIN 1..466; /note="Uncharacterized protein C11C11.01"; /id="PRO_0000116532" MKKNNERVNTNPSLISKSYNMKKRPVIGTRRHFARKEIESDSDDEDDIFLAGERKKYLQNQSYERRKQKNEHGNNLTLQEELLRHEAYEKNEEIANENDVDQVNLMKYFVHMDNISPVTTNGSLKESLRKYSSIIAVNIFSETGDLKKGIAIFQDLSDAEQAVQYLSNCKIDGRLISATITNHPKRLPNAEHLESSTKTKDESQDKDKLTKLDRAKLEWLIQGLNCEKGSIGNLLCFAVEHVNNHVEITDAFLKEFFNDQPTDDTKVYDDDYINERGEKKLSLIYLMNDILFNGISGTSLVWRYRFSFEPHVERLLDDLYLFSKRLGGRIKEDIFCKKVVKVIEVWKTWIAFQEETLERAWRNFSGNTPQSPQINSAALKVETKNSWTAISEETEGLQDDEEYNGIPVDVNELLNVEFISQIPMSTETSSSSSPQPTEERKAKFKPSFTQGTFVSKRMRMHAEDLF Q10209 YAY1_SCHPO MOD_RES 108; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC4H3.01; CHAIN 1..392; /note="Uncharacterized J domain-containing protein C4H3.01"; /id="PRO_0000071156" MATPVDTEYYDLLGISTDATAVDIKKAYRKLAVKYHPDKNPDDPQGASEKFQKISEAYQVLGDEKLRSQYDQFGKEKAVPEQGFTDAYDFFTNLFGGAPFREWVGELSFVKEMFREEDSAVEQGQMNDKQQLLLESSEPTPTIKQQFNDRKKNAQIREREALAKREQEMIEDRRQRIKEVTENLEKRLDDWIAKATTEEGLNALREKYTQEANTLRIESFGVEILHAIGEVYTQKGRTVLKSSKFGIGGFWSRMKEKGKIARATWDTVSAAMDAKLSIDQMQKLEDKGEDQASAEERAKLELDITGKILRASWCGARYDIQGVLREACSNLLKKRVPTELRLKRAHALLEIGTIFSNVEADPDDPNRIFENLILENKKKRKKGSEAKPPKAT Q10211 YAY3_SCHPO SPAC4H3.03c; CHAIN 1..649; /note="Uncharacterized protein C4H3.03c"; /id="PRO_0000116482" MPPNARVSYGAEKYLPREIDNHGIVGNMHTSAMISLDGSVEMMCWPNFDSPSIFARILDARAGHFSITPIEQTSCKQMYEPSTNILHTKFYSERGVLRLLDFFHRPWEDYEPLYPWLIRRVSCIRGTSRIKLECFPALDYARQSHETRVSKITENYYQAEFVPASGDPKYILDCVPSGDQLKIDLELIYPAEHLIEGGGVISYLELEEGQEITFIFRQEGLGPNVDYVTPNLVDKLEDSTKRYWRAWIQQCVYTGRYREFVQRNALTLKLLIYEPTGAVIASPTFSLPEDLGGVRNWDYRFTWIRDSAFTIYALAQLGFRAEAVEYMSFIYHVLKKKNKDGGINIVYSIHGDSQNLEEVELTHLRGYYNSHPVRIGNAAVHHLQLDIYGELMDSIYIYDKKCQPIAYDLWLEVRQICDYVCANWKRPDKSIWEVRGQERNFLYSKIMLWVALDRALRIAFTRSLPCPKHMVWMDTRDEIYEAIMDSGYNMEKGFFAQSFENNDILDASVLVMPLVSFISPTDPRFLSTMDNIMKPLEKDGLMSNGLIFRYNNFVYEDGVGGDEGAFTMVCFWLVEALAMAGCSGYPKLLSTAVSMFEDLVRYSSHLQYYSEECSLSSESLGNSPQAFSSIAAIAAAHILDKALSIFNEI Q10214 YAY6_SCHPO SPAC4H3.06; HELIX 6..36; /evidence="ECO:0007829|PDB:8J0H"; HELIX 42..65; /evidence="ECO:0007829|PDB:8J0H"; HELIX 72..101; /evidence="ECO:0007829|PDB:8J0H"; HELIX 106..134; /evidence="ECO:0007829|PDB:8J0H" TURN 66..69; /evidence="ECO:0007829|PDB:8J0H" CHAIN 1..137; /note="Uncharacterized protein C4H3.06"; /id="PRO_0000116483" MYHLPDMEETVNKILRAQETRAQLYKELEDALNANQEKKIGLEQMGIIVQLVTEGLNEVSSDIRNYQASLTKELKLLVDSLQEKERSKLQATVKLEQLKVVSTNSPVENTQISELEARLSSLSKEINDILQNMKDEI Q10215 RDL_SCHPO ACT_SITE 104; /note="Cysteine persulfide intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00173" CATALYTIC ACTIVITY: Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407, ChEBI:CHEBI:33542; EC=2.8.1.1; TRANSIT 1..25; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC4H3.07c; CHAIN 26..142; /note="Putative thiosulfate sulfurtransferase, mitochondrial"; /id="PRO_0000116484" MFSKTLSVSRLLMTRSFYSSTVVKNVSIFDFEKVYNLSKRPTGDKSTVLIDVREPDEFKQGAIETSYNLPVGKIEEAMKLSDEEFSKTYGFSKPVFEDNVVVYCRSGRRSTTASDILTKLGYKNIGNYTGSWLEWSDKIKSK Q10216 YAY8_SCHPO ACT_SITE 178; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 192; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"; ACT_SITE 196; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 54; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 128; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 162; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 192; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 196; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 225; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 227; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPAC4H3.08; CHAIN 1..286; /note="Uncharacterized oxidoreductase C4H3.08"; /id="PRO_0000054875" MDPVPSTQTQKWPGKHADLDPEPSLLRYCDGRVHVGSGKLAEKKTLLTGGDSGIGKAAAVMFAREGSDLVISCLPEERDDAEVTRDLIEREGRNCWIWEGKLDKSDNCRDLVDFALKKLGWIDVLVNNIAYQQVAQSIEDIDDEQWDLTFKTNIFSFFWVTKAAISHMKSGSSIVNCSSINAYVGRPDLLDYTSTKGAITAFTRGLSNQYAQHGIRVNAVAPGPIYTPLVSSTFPKEKIELSDQVPLGRMGQPVEVASCYLFLACSDGGYMTGQTLHPNGGTVINN Q10227 YD03_SCHPO SPAC2E12.03c; CHAIN 1..283; /note="Uncharacterized protein C2E12.03c"; /id="PRO_0000116563" CARBOHYD 15; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 228; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MPSSTTTAPPGTHPNATASTVFAILGTVCWCVQLIPQIIKNYRAKSTEGLDTLFILSWVVASIPLSVYNQVQELNIALKVQPELFQALAFTTFFQCLYYGSKWPLRKALFVVISFMLFSGGLQAMLILTIKLGIRRHVEWPVVFMGVLATVLVNIGFLPQYISIFRARAVTGISYLFLAIDSSGSLFSFLSLPFDRWDVLAAVDYGLLFIIEMGVFVLAFIFNVLLKNKSTPTDEDVTFTEEDGDEKDEEYSDIFSIKGKFNTRPNAWQNAYDSDTKSAIQIP Q10238 MPF1_SCHPO SPAC4G9.05; CHAIN 1..581; /note="Meiotic PUF family protein 1"; /id="PRO_0000075936" MQRDEERPIDFGMSLELPKTPNDVNYVKKLITQILYLQTLVSEQQKKIESSTLEVQKKKDQIRELERIYEMNPKSFLTLRRTPALKLLPETLSVELSNEVNLTSSTTSSCVKPSPYLTNCNLKNKDTFPVSKNNCSLSSGIFTNSNGTNNCFSTHPKSLDDAKDNVVPKKLNDTDQFPLWSKNETIDPIDLGYSFISPFSMSFASKGNEILDPGESTNKNLFYEFPNGTTEPFEKNSVHSGKETLQYSATISKWKAMIEQIIFQNDQAASLSLQQQLKNEDIEDNINLINTILPFSVTLMKNKFGNFLIQKCFEYSTEAQLQSFSYFLKKHVKELSIDAFGSHVLQKSLEIYPERFTNNLIEELIECLPATLMQRHSCHVWQKFFETRRKSLVDGIFDHFNKKMQGKWLQVSVSEMGSLVVQTIFENCKEKDKRTCLDEIINNMDQIICGQWGNWVIQHIIEHGSEPDKQRILNSLLKEVESYSTNRYASKVVERALRVCHVTFFDRYVKEITTPQNELPTIFLQEIASNQYGNYIVQYLLQVATPSQINLMAEHLKKHMVSLRGHKYGQRIAALVEKSKS Q10240 MU133_SCHPO SPAC4G9.07; CHAIN 1..513; /note="Meiotically up-regulated gene 133 protein"; /id="PRO_0000118857" MEECKLDINKGKDAEILYEEYKYHEIKEMSFSSCARTSPELLKKFGCDAHVITSVEGAPKKENKKIWEFFKGSNKIKNLFTMFTCCFANDEEEIWGEETNESVVYKEYTYNSRWKIEIPSYPVREIPYVVADTPYNKLLCPLSSLEWVSKLILMDNANSIGMKNNRYSTNPFIYGMCYIIRNNANRILLESCYCENSTGMSTCPRILEFMPYEPLLKYNSYRLLSTYENSYKELSEMLTNNNAPLEVLIHHVMLYHYYPSFLQSALWTAVSSYLEERCNNGLYSKLLVKAAKQHFGDIRLYFVTPDDIYTFDHCNNWIAIVTRNFMAYIETKRKLEFDSIPFNCPLITQLFPLISSPKEMAWLLLIVCTDSNESWFPVHAYINTKTRILRPRSPKLDFFLKESDLLYFQDKQSISEFDIIRKDLLEDLIQCDSYVNTREQLRRRRETLNRKRITIAKLQNNHSQITFPYKRHNIHKSVDSIQFCKPASNLLTLKDNSYTQIPLEPLLLAEISV Q10244 YD1E_SCHPO SPAC4G9.14; CHAIN 1..221; /note="Uncharacterized protein C4G9.14"; /id="PRO_0000218936" MFIAKSIVIGLLICVLFFFFFVSRFNDKYELQPLLTLGLLNASLTALSDLLAQALDSYKLLKFRNKRDVSLEKYGNTILLPASTSKLDVHRTIRYAAYGLCLTPIQFRWFVALSNVIQTENPFIAIVLRVALDQFIFAPLGIVFFFLFMGITECKSYERLKSYFRKHYWPTLKANYILWPAVQLFNFTFVPLVLQVIFANAVSMVWTAYLSLKNSSPNADV Q10247 YD1J_SCHPO SPAC4G9.19; CHAIN 1..270; /note="Uncharacterized J domain-containing protein C4G9.19"; /id="PRO_0000071157" MSKIFFRLNLVRNSLWRRAASFTSYSELKSLTPYEILELPRTCTANDIKRKYIELVKKHHPDKMKNASQLAPTESPPEINKHNEEYFRLLLAANALLSDKRRREEYDRFGIHWNQPSHPTHPSPQNWSQARYPTYSRSRRSAGMGSWEEYYYNSYDYMNDQNASNKNRKFDDEGMLVFAGILSILVIINIYSNYRNGKFYREARSAAIGRAEDNFDYYSTGMADLSKDDRISRFLILREQSKQIPTQQKPSSLPPPERALPAPTMPTPSS Q10248 YD1K_SCHPO SPAC4G9.20c; CHAIN 1..298; /note="Uncharacterized mitochondrial carrier C4G9.20c"; /id="PRO_0000090701" MEPVIPEGALSQSTKDFLAGVSGGVAQVLVGQPFDCVKVRLQSQSNVSPIYNNALDCVKKISKNEGLAAFYKGTVLPLLGIGFCVSIQFTTFEYCKRFFSRDGTPVTMPQYYVSGAISGLANSFLVGPVEHVRIRLQIQTGKNVLYHGPWDCIKKISSQYGLSGIMKGYNPTAAREAHGLGMYFLAYEALVKNTMAKHHLTDRSQTPGWKLCVFGAGAGYAMWLAAYPFDIVKSKIQTDGFLSKATYKNSWQCAKGIYTKAGLRGFYRGFVPVLVRAAPANAVTFYVYETVSQHIRHL Q10250 YD22_SCHPO SPAC56F8.02; CHAIN 1..1517; /note="Uncharacterized protein C56F8.02"; /id="PRO_0000116566" CARBOHYD 35; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 40; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 76; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 917; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1178; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 1321; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNQFPNQPGNFGQNYYKPVQGSIPANSEATNFQQNNSRENKSECELRQNSIAASMSAYPNGMYAGAENHNVENHENYTMVGHDHMEEVYGDDLVNEPRIAYSSDIVATFDGKDFGSNLHVDDTLDQQWAHFAGKQQHPLEPREIPFPVTDPLNSKIEMKQFTNIAAVLRYRGVHSAKKTAFIILDNKGKEFTSITWEKLASRAEKVAQVIRDKSGLFRSDRVVLMYRDCEAIDFVVSLFGCFIAGVVAVPINRFDDYNELSSILTTTSARLALTTDANLKAFQRDLNAKKLHWPKNVEWWKTNEFGGFHLKKKAEMPPLQVPDLAYIEFSRSPIGELHGVVISHRTILHQMNCLAAIHATAPAYESDKLDYLSIDREYTEGLSKSGLFLTYLDLRQAIGLILGVLHTVFSGYTTVWCPQNAVFVPGLWANLATRYRASFMLTDYAGLKTIAYNYQNDPKATLGFSKKHSVDLSSLRMCMVDCLNVDCEFQEIVSDRWLKPLGNQNPRATFVPLLCLPEHGGMVISMKDWIGGEEFMSPKGFKSPRTPENEISEVLLEKEALKLNEVVVLAEDDKARRQSKHPNTIRVGAFWYPFVDATLAIVDPETQVLCLPNIVGEIWVDSPSLSGGFFALPKQTEAIFHARTSFISSDTFQPIPSNQEFLRTGLLGFIRKGKVYVLGLYEDRLQQKVEWVDNGKQDTIFFHHYTSHLVNTIMRKVSKVFDCSAFDIFVNSEHLPVVLLESPAANIPTEANGNQVVINYGLLDLITTECVECLLEDHQVRVYCVLICAPFTLPRVTKNGRQEIGNMMCRRAFEHGTLPFLYVKFAVERAVLNLPVGEDAIDGIWSSYASGIRQNLLSDQELQYSGFIDRSLRYDAKTSVDISSCHTMLQLLQLRVAKNAEDIAYITIDGRGREGKNITWRKFDQRVATIIRYLQKKKYIKPGRVVVLMYTHSEDFVYALYACFYLGLIPIPVPPLDHMRLSEDVPAFLFLIKHYYVSAVLVNSEADTALRAKTTSQHLKQSAMAAKVVLPSFIVTSKISKQTKSIKELNVKLDPICLDPAFPALVWAFWSPDHRLTLTAYNHQTLLSICQIHKETCQMTHKRPLLGHVRSMSGIGFFHTCLMGVFLGTTTYLLSPVDFANNPLLLFQIISKYKIKDTYATFQTLNYIQNQQPTKWPNLSCLENLMIPHDGRISAFYIASLQKYFVKHGLSPYAFSTVYSNCLNPFISTRSYMGAIPTPQLLDLRALRHGLIQPCESADKPYALPLLDSGMVPVSTQLAIVNPDTRELCRVGEYGEIWMRSSANAISFFQSTDPVDMMRFNATNSDGFLGNGYVRTGDLGFLQITSHSMGPNAPVVDMQLLYVLGPIGETFEVNGLSHFPSDIEDTIERSHPRIARGGTAVFQSAGRVVVVIEALGQDFLAAIVPVVINSILDEHQIIADVVAFTSRGNFPRSRLREKQRGKILASWVTGRLRTTQVFYIRGSGEGEFQSSYVPDYNPSLRSTPSVSSRSTLPQRVF Q10253 MUG64_SCHPO SPAC56F8.05c; CHAIN 1..286; /note="Meiotically up-regulated gene 64 protein"; /id="PRO_0000116567" METFKTHITGQFNATVSSITPFAKKTTHYLRTKIGSRVEELSLPEDYVELEQQVDSLKEAYNLVLPIVETVEVDGYDYPTNFRDSITDFGKTVSGKVRNLGNLTPLEQTPLASVGKNLEEKEAAAKPSRTLYNAISRAASEATTKMGAGNPLSSAFGQISVLEEKVGNLQGERDSAISKNFCEQVRAVLYPRFAEAHRVKADVQDKRLQLEMAKLDVESAKPENLEHCKSAVRSAEDELNGAIEHAKILYEQILNKDYNTDLLRSIIKNQLKFHQDAAAALSDITI Q10255 EMA19_SCHPO SPAC56F8.07; CHAIN 1..183; /note="Efficient mitochondria targeting-associated protein 19"; /id="PRO_0000116568" MKVVSLRRIYSSEIYKLPTTRLHMDTLYYYYFVSHLAAALFVDLPITEWLGGSLSCLSGLRRFYLSTYEDPILLIPAPWKTALFSSELFFQVPFFIWVSLRLRKKARDPVLWVAILIYGVHAFTTTWCCMFELFAEKKWMIMSFYFPYLAIPLWMAIDMGGRLVKSCHAAKSGPSSTITSKSD Q10260 YD2C_SCHPO SPAC56F8.12; CHAIN 1..394; /note="Uncharacterized protein C56F8.12"; /id="PRO_0000116570" CARBOHYD 3; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 14; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 20; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 25; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 283; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 286; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 344; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MMNDSQVQLFQLYNYSVYSNGTISNFTNCYLINDEHTPIIESDGMIYNGQSCDSPVKSLASHGAVGIVTACFCFFLIPLLLVNIAKYWKGKPPLLKRRMEFIWITLLILALAVGGFAYIDVDRNLVQGAAMKIFSFTFQTALPISIAIIWHVISTYGFALYRQRIVVGKHAAHFSLDHWIFVVEYYAPIVFYVFNLMGFFLAALHPWTKVVRGDGNAATDGRFKASSVLLAIAWVFACAMFIVYSFVYKLDRRGRWVGMVIMMISILPRIVYQFLETWSFTLNASNVSVNAGLVFGLGFCPPLILAYTVCIYGWAVPSIAELEKEAIHEECRQRKRRTTISRDNSTRSTWGIGSEHDMQCLPPSYETMGPCEKEMKEETNEVEIASIESGEVRE Q10262 MU115_SCHPO SPAC56F8.14c; CHAIN 1..131; /note="Meiotically up-regulated gene 115 protein"; /id="PRO_0000116572" MRKPCYAVYHPALRLKCLVRKGLGKIKGDTDMCDKQQLKKKEKEKQRAQKVACGPRDPPCTFSRSYTDQKRKEIHLGSTEWGLKESFTLTRGPNRRGNVGKGVKRPMVNKKLGQLELTSLDLRWQKEGKGN Q10267 UPF3_SCHPO SPAC13G7.03; CHAIN 1..278; /note="Nonsense-mediated mRNA decay protein 3"; /id="PRO_0000116574" MAPDISKKRLPCKVLVFNLPPTLPEQVFLQSINSFLPHVEWHRFSKGKATVGTRSELLSFAYLKFQSATAVQEFFRVYQGHTFIDKKNNTYRAIVTIAPYQKIPPSKVKADSLEGSLEQDPKFQEFKVQRESYSQTASNDDVIEKLQTSTPLLQYLAEKKNAVVEKGKSKPSKKSVKAKKKLRLAEKPASNNSKAGKSSQESKKSSKAPAESAAAVIKEDKVSDRKKSKKKPKKTPVSNSTASQASENASDKKTKEKKSSGKQKIASKKKDQLTTDNV Q10275 YD3B_SCHPO SPAC13G7.11; CHAIN 1..269; /note="Uncharacterized protein C13G7.11"; /id="PRO_0000116577" MNVLRTQKYWVNQFAINFACRNTYVNPMFLRYFHCAVPRAISQRALKPMDIPFLQCYIEPIDNTSFFLHPFKKIRFWWRYLFYGWWNLKKNQFLIKRTFPDRDFSIAEIIQNALKLHSGVNKALANHDLQQLEELCTLRTAQILKQQALNQPKCIWKLEKHISKPKLLNLSRAQADLKGEEFFVQAVVRLHTLQSLRTDKGSPKIEKPDIENVVIQQRSWTSPIRWQLWGSVPSTPVNTVRKTLPDGQVTFVAKPSKKSFLKQLFSGKE Q10296 YD42_SCHPO MOD_RES 110; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22H10.02; CHAIN 1..138; /note="Uncharacterized protein C22H10.02"; /id="PRO_0000116578" MAFYYKNNLGYQNIPYGYQLNDFRASFEKARTFDMEDDLEFCPSLSDEELVSIYQSTGLSPTSSSPSLSPMTPNLYPNVLPNVHPGVSNYTHHPLSGLHQNVGSRTRKSSGIPIIDPVTRAPAVLAGAVSSSRAKQMW Q10301 YD48_SCHPO SPAC22H10.08; CHAIN 1..492; /note="UPF0652 protein C22H10.08"; /id="PRO_0000116581" MDAEALRNLYLSSILPNESKTGNESPEKKFSSPVLLQRAKVIPLRLEYEERKLLHLLTAALDVSDYTDSVDTLSFSSPAKRLAQQLKGITAVLSGIMVAYDYKVGQELLEHKNFEQHAEFFKKIFEIGRRYKVLNPNRLGSTYGKLMYFVQDSMRPEIQDALGFNLFKPILTVYEFLNERDALNALEDPYAEIATMEIVAENRSRSAIQKDIKAKERAVEHIAKKYYSSKITKEKVRWCLYSIADSNSYLRYNRDPIAKLIGLVEAYFSPDTVDDEFTLAIDAINGSRLKHSHYKQYHYVVQSLHLWLLIMGEIFSLWALSDLELTNPDMEYKLIDNNQGIHRMQPCPNIRIAMERILRTAQEQSETWIGSSTIHLGDTAVPNALLFIDKYMQVPRILTPLVLLFKELDSLNDHSLLNYIDTAFGGREYLKKTILTDFMRFGFDGSGADNWFDAGSCIDGRLTSAWNWANNIHTKDYYRVLLMSGFLSFNGE Q10305 GDI1_SCHPO SPAC22H10.12c; CHAIN 1..440; /note="Probable secretory pathway GDP dissociation inhibitor 1"; /id="PRO_0000056685" MDEEYDVIVLGTGLTECVLSGLLSVDGKKVLHIDRNDYYGADSASLNLTQLYALFRPGEQRPESLGRDRDWCVDLVPKFLMANGDLTNILIYTDVTRYIEFKQIAGSYVYRDGRIAKVPGNEMEALKSPLMSLFEKRRAKKFLEWVNNYREDDPSTYKDINIDRDSMESVFKKFGLQSGTQDFIGHAMALYLDDAYLKKPARETRERILLYASSIAKFGKSPYIYPLYGLGELPQGFARLSAIYGGTYMLNQPVDEIVYGDDGVAIGVRSGDQVAKAKQIIGDPSYFREKVRSVGRLVRAICILNHPIPNTDNLDSVQIIIPQNQVKRKHDIYIAGISSVHNVCPKGYYLAIISTIVETANPLSEIAPGLKLLGPVVESFSRVQEIYEPVTDGTKDQCYISKSVDATSHFETLTCDVRDIYKRMTGTDLVLKQRPKMEDQ Q10307 YD52_SCHPO SPAC6C3.02c; CHAIN 1..172; /note="Uncharacterized protein C6C3.02c"; /id="PRO_0000116584" MPRRRSAAPPPRRAAPARSASTAAALPPRTMAPPPAPSRVQQAPPPTAVQGGSSPGFFGNLVSTAAGVGIGSAIGHTVGSVITGGFSGSGSNNAPADTSVPQSSYSNSVPEAAYGSAPPSTFASSAISEEAKNACKGDAKMFADCINEHEFSQCSYYLEQLKACQAMWSNQQ Q10308 MUG43_SCHPO SPAC6C3.05; CHAIN 1..269; /note="Meiotically up-regulated gene 43 protein"; /id="PRO_0000116586" MNNITRDIYTKGQPADLKRLLMKRNSFRRPLLNMRCNSVLQYSLEKRKLTVQDLKDTRMELNNMIRILTEAMAAHEWTVDNVNIADIQSLQSTIHSTLKNFQKINVLQLNINASDNSLAYLSKPEESYNFLTIYFSTLLSYEKVENLIKKSLTVIDSLYGLLNYQINAQHSLGCIPLNQDSFKQLKLLICILEEDIKLDDCGLEISASKNEYLEKIKTHYKTWLRIHTFLTLFPVPSVLSSNLKKQMYGWFEDLRDESLKSIILASLSE Q10310 MUG68_SCHPO SPAC6C3.07; CHAIN 1..515; /note="Meiotically up-regulated gene 68 protein"; /id="PRO_0000116587" MNTRNMFDILRKGIFKDEITQIEKILLKMEDNTYEYVDVFLEKYESQQKLLLKLTKAITEYLSNLKPQLSKQENIYVKHIKSSNEAKTELEIFNCYKEISISKEKKINSLLKLVRESAQDYTINEENDILYHSEISAKKNASPMEFGDASFDLEKQRLHFANSNLHSIESERNESSLSLDSGESEKKSEEDNGNGEQNYIPEQYERLDSPVKEKIINTCCKGKAEPPNYERIKPKAKKGNQMQKIKISKLGTAETQTEDVMNKSSQKENNDILRKHKTSVKFPTNLDALNSCTMENHEINELTATNKMNDGPITKCARETINIKNLKTSNLERNQNSPKNKRTVSYERLANSFSFNALNDYNLKKGGEKLRKKAIKRALKDRGSQDKAYGGVVQSNSRQPKVGFHVNNSSSGHNDNEGNHSLILSSKTKSPQLFNNEKKDESYSGFSNTNSYAIEETSRALMGTSKTRKPENKSKYLIKNGWFEDSLNSEIWSDANPLDWRKTDILEESTSIVYK Q10311 YD58_SCHPO SPAC6C3.08; CHAIN 1..234; /note="Ankyrin repeat-containing protein C6C3.08"; /id="PRO_0000067249" MVYASLGKAIEENCPEEYVEQAIQNDPNSLNAVDDDKRTPLHWACSVGKVNTIYFLLKQPNIKPDEKDEAGWTPLMISINNRSVPDNVIEELINRSDVDPTITTRGGQTCLHYAAGKGRLSIVQLLCDKAPELIRKKDLQGQTPLHRAAAVGKIQVVKYLISQRAPLNTSDSYGFTPLHFALAEGHPDVGVELVRAGADTLRKDSENHTALEVCPDRIVCNEFLEACKEQNLEI Q10312 YD59_SCHPO SPAC6C3.09; CHAIN 1..335; /note="Uncharacterized protein C6C3.09"; /id="PRO_0000116588" MNCAFTKELKDEIYQKNYTEHEILQNAYNGKLDILLPVEDASEEAIRSITKIVQDLSFYEFSGSPALLLHPDLYSTFIHTGIATIVSSSDNDNKICISQGILSVTLDKDSYLVSGIDAKPSSSEPKDTLWVANIDLKSAFLRPQWKGFERLKAALGRLPGKWSFYLTFPTEKVDQSYQNNLSHSLPVPMISREINLKKGKLDQAKIPPPLVSTLNRNELFPSNGPLEVLEILSFLRCNAKCVQNSFVPDPYISRYKPSCAVTDVLYLSIKGLFSSSTCLELYELIRNISWNFIGVESFNSFRDVDNSSQLHSGDSSLLSFYDSRTERIRWTWRLS Q10314 YD62_SCHPO ACT_SITE 257; /evidence="ECO:0000250" SPAC17G8.02; CHAIN 1..330; /note="Uncharacterized protein C17G8.02"; /id="PRO_0000206841" MTNTIDSFQKGSALENYNIWIDCDPGHDDVVALTLAACAGHCKILGVSTVHGNTTLEFTTKNALAVMELLNQDVDVHAGAAKPLMRESAFATHIHGTNGLAGISLLPDYPKKKATPDAVFAMYTTISNYPEPVTLVATGPLTNIALLLATYPSVTDNIERFIFMGGSTGIGNITSQAEFNVYADPEAARLVLETKSLIGKLFMVPLDVTHKVLLDANIIQLLRQHSNPFSSTLVELMTVFQQTYENVYGIRNGVPVHDVCAVALALWPSLWTSRSMYVTVSLDSLTLGRTVCDVWSQQNQYPANVHVVLEADVSLFWETFIGVIDRLNYL Q10326 MUG8_SCHPO SPAC32A11.01; CHAIN 1..720; /note="Meiotically up-regulated gene 8 protein"; /id="PRO_0000116593" MSRSICTLTCILPTFSMDYWNQECVELSQVENLFTELASRLELLEMNSKNVLYRLTIGTNPDRNWEAIAFIREFFDSAKHGYVIPKHEIRNRIRLLSEASLISCLRWLLHRIPGGVITWSTYKLFDEAETRANYPVRGFDIFMKHATKHSCHFNILKCFLKLLMSLSAKLAVSSNSSTVSSLELVSQIASIWAFDWPMMNLQETFIYWDRCTNACLRLLLCYIRYTNKSSETGFSCLPSALQSQLQSFNYPPSLKKLNDAKAHVFTFSMNYYMTRDPLEMIQIVTKMNIPDHLTATLPRSSDDIQNDCLFALRQVSKRSSYHSVFSAQESAWTDFIKNGFDHPILPTCTQETVYSLLTGNDTACVYPFPNKPYRLPDVDFEIFSHCSFESLTTVTTNTNIWWVWAESRCTEIPESKRTVFPNCTMLIDKTGRLIILQQTVPQKPVALTASSNKRKNRIFGKIRRSFKRILKPRKINKTVKIMSNSQRRSCQSVLSEGNRTILLHLADQMNACSLQTKSRESIKTLKLIEEKDEYWEPETAGYFNTIVGWADQRKSLYDEAVIKINHSNMLNTLPPTSQGATSTTVSSASSNFLSSSCTPIDDTNSVTGSTLSCSFDEMKLSDKIDDANSLKDDDFIQGSKKDFFEMNLNHSSYQNKDELKPFQLLVKHAFKPPSYRLIRPPLRDWQSSDTLSSEMSKSISSSRSSPFSLEQTISKIQNKL Q10333 PEX11_SCHPO SPBC582.09; CHAIN 1..238; /note="Peroxisomal biogenesis factor 11"; /id="PRO_0000116518" MAVIFENPQYVHVLRMLNSMPARDKTFRALQFVAKLLSWHLFYGGSSLSTVNKWKKLESNISFSRKLFSIGKVLDYICKVYFDSLKLQNPLSGNKSALPTISFTKDVAFAGYATAELIGWFNKTELMPCSHSKQISTIGKQCLAVALLSSCLAGCYELQQNSKKIKSATQEASEKDSTSLQTLQKERKEILFFALQNALDATIPLAELDILKVNDGFVAAAGITTSLMSVYKTWIGSY Q10335 RPN7_SCHPO SPBC582.07c; CHAIN 1..409; /note="Probable 26S proteasome regulatory subunit rpn7"; /id="PRO_0000173844" MCSPSATLTHRTMTEKARTVSDLTISQAIFELSSPFLENKSQKALDTLFSAIRDHDLAPLYKYLSENPKTSASIDFDSNFLNSMIKKNEEKLAEFDKAIEDAQELNGEHEILEAMKNKADYYTNICDRERGVQLCDETFERATLTGMKIDVLFSKIRLAYVYADMRVVGQLLEKLKPLIEKGGDWERKNRLKAYQGIYLMSIRNFSGAADLLLDCMSTFSSTELLPYYDVVRYAVISGAISLDRVDVKTKIVDSPEVLAVLPQNESMSSLEACINSLYLCDYSGFFRTLADVEVNHLKCDQFLVAHYRYYVREMRRRAYAQLLESYRALSIDSMAASFGVSVDYIDRDLASFIPDNKLNCVIDRVNGVVFTNRPDEKNRQYQEVVKQGDVLLNKLQKYQATVMRGAFKV Q10338 YBM4_SCHPO SPBC582.04c; CHAIN 1..583; /note="Uncharacterized protein C582.04c"; /id="PRO_0000116517" MAENKKFSIRKKRECSYPTFRTLYEFNKFFLRYKTEISKIQRRTSSLIQYEEHSSAIFIYYETPQMFDLATKALQTLYNSHTREGETKAASKWYRNPRKDFPSQEAALVRKKKRDALILKKYLLNVDPSLSFRAEGLFTLPSDDLDVYEFFGGENLTLFNQVRVDCQCYIHYLPKLAAFYVRCDSVKNLKVALKRVKHIFYEQVSLIRLERTQPILHLMNFDDYSTSYELFYDRNFPLAKKYKPNSIYLHRLPESIPTPVDSVKINLIRERSFNLLKNFVSASLFNVFLFSGTVFMRVKVGIPLFERLKVGTNKVKNNSVNIAQSFLEPQTRSTFLRYLFSDEVSVKVCHVLKELRSPTGEKLFESFSDDPITAVHFEVMNCKGVQDTLTAIWNTNSGKPSGWYLESTMYKALDVTYYNLNTLSWNLYIEYGHPTQNSTFYKEFISNISMSDDGRIYFMNTRDIKVRSLVVKLKHKYWHLSSGFHLHITRFEAHDMGKVKDIDTDFEPGLQCYQVGSDTSVLRYGLSFWDPKWDYLLADNQHKQQWQAPSYKPLISEFFPMGIEHFIETAQSIVMAVNRSTID Q10340 YBLJ_SCHPO SPBC106.19; CHAIN 1..515; /note="Uncharacterized protein C106.19"; /id="PRO_0000116516" MFLRPWSRNFLCSCRGFSVCTPYASIKSASELALKNISELQALQKIQNHTEKLKFFSSKLHNKGEPFTLQLGDLITEHTSVPELNEILDKFSQSNELFTMRFLEKASIIAHKNRSAELARRLRTYAANAMIDLSRVAFVNIFWTLLKTRDKEGIVETIEGQPIAFKVARRIFRRLLVYTSEAGENIEICFFLTNSLFKRLLNNREALSKDEKSELQNLYYDLLLCFSYSYYVPGVKLLLPMLYNGSFKEINRTAIDRSLLALLSTGELEAALELLVYLKNNNIPINDAYLRMMVINFCLANKPTLAVRFCQAWFKQSKMLSSTENLLLIAESLSRASNDFAAISKQMQPFSIESSSFYLPSHRLLMLVALMMKNSSGILHSYAVLKKANAITNKELRIMMQHAMDLRSTEFAEAVLKESEFTLQSNRSQLLMDFVAILFLNKEYTKAFATLEKTFASKIKPSHNIISFSLSLVKRFGTKNDLFFLRRSFKNMGIETLDEIEKNLPPKVVYRCFNY Q10342 SDA1_SCHPO SPBC106.14c; CHAIN 1..719; /note="Protein sda1"; /id="PRO_0000116515" MVKRRTAAVLPNNLPHLQHLVKKDPKSYREEFLQQWNHYETAREIFLVNPSSDISEFCSLIDFISQTCNYYHDVTADFPSELIELLQKNHTIFPFELCEKIVLCLVLLKNKTVISPITLLQCFFPLFRENPTRGVRELLYQQVSLTIRNANKQAKNDKLNKAVQSALFTLVDGSGSGSATHTDYSGQKREYSASELSGVWAVKMVRDLWKRNVWSGDARAVNIMKSAALSSNPKVMLAGIYFFLGADNQEEEEESDDEGPDVSKLLHQANVNKKTKSREAALLRARAVVKKKERGKQNVPTNVNFPALQLLHDPQGFAEELFEKHLASSKSRLSMDQKLVVLRLLTRLVGSHKLTVLGLYSFLMKYLTPHQRDVTQFLACLAQASHEFVPPDALEPLVRKIADEFVTSGVANEVVCAGINAIREVCARAPLAMTPDLLQDLTEYKSSKDKGVMMASRSLITLYREVAPDMLKRKDRGKLASIEMKDRTPLKYGEELNVTHGIQGLELLAQYKAEHGEEGENGDDWDNWEVSEDGQNSDDSGGWIDVDSDDNIELSDSDEEEEKATARKESDEKGSSSQKELVDRMTELASQSILTPNDLKKLEELREQAGVDRLVNGPKRSLKRPDDAVEADEIEGPRKKAKNDREARIASVMEGREGRDKFSSKKAGFNPTSLSNKRKQRNKNFMMIKHKLKGKAGRSLVQKQKVLREHVAREKRKIK Q10347 YDA5_SCHPO SPAC1F12.05; CHAIN 1..377; /note="Uncharacterized protein C1F12.05"; /id="PRO_0000116602" MPSLVRRFQHASTEEQPFELNIQMESPPLVMYGNPDVSSGALASGLAKLTVFPADLKCESIVMEFVRIISTKRPLRDSCPDCKAQVEAFEKWEFSKEPTVYTHGTHTWPFTFIIPGHFPQTTNSPFINVTYILKTRVKIPSQPDFVFEYPLNLKRSIVTNADKIAQRLFPPTSLIALLELPPVIHPLSCVPVEFQLTGVKPENSKVGWRLTKISWRIEEQIKAQINGCSTHTGTKKPYIFKETRLLGNNEHKSGWKEDGDRIIFEIPISTSLLSKPICDVSFDGQFSLYIAHQLILETIVVEVMNSHPINSNARILRMKVNLPLTERGGLGVSWDEECPPMFNSVGPSPPAYEQVARSSPTDIPLPPPSCPTNVQRD Q10350 YDA8_SCHPO SPAC1F12.08; CHAIN 1..316; /note="Uncharacterized protein C1F12.08"; /id="PRO_0000116603" MGKTLIFIKLSSLNECIKYSTIISKIARELSIHKGNELYIWVSCSEMCQKRTKHLFRELQNALCELYLSSATTNDSSLLSVVPTIVLFEYWSNIQLGSITDSWNSVYYSENAKDQILNIPAKSFQSIGPDVLNEIHNIEHLPKKDESEDSGKEINNMVSAVGGTFDHLHVGHKVLLTLTAWFGVKEVIVGVSGDELLKKKVQKEFLENIQKRKEEVSNFLHSIKEDINCRVVTIHDPFGPTITDAEIDSLIVSEETKTGATAVQEERVKRGLPELSIYCIDLLYPAQELNLKDNNSLKVSSTAIREELAKLAYKNK Q10352 YDAA_SCHPO BINDING 106; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"; BINDING 129; /ligand="heme"; /ligand_id="ChEBI:CHEBI:30413"; /ligand_part="Fe"; /ligand_part_id="ChEBI:CHEBI:18248"; /note="axial binding residue"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" SPAC1F12.10c; CHAIN 1..147; /note="Uncharacterized protein C1F12.10c"; /id="PRO_0000166038" MVALFKSSLGRPEQHQTPQIRISPASSNVEHSEKQPRRDFRVKKYVAPGFSQLNWSKLVASGQNLSGVEKPIPVTKEELAKHKTKEDCWIAIRGKVYNVSAYLPYHPAGQKRILDYAGRDATVIFMKFHAWVNEEALLKTSFVGFLV Q10354 YDB1_SCHPO SPAC22E12.01; CHAIN 1..374; /note="Uncharacterized transporter C22E12.01"; /id="PRO_0000213401" METDPILKVEREPEFTPSPAPEAIVKDIEQGVAPVSQNEPDRPQHWITRVVIIVLIVLAWYFFSLLLSMMNKWIFSESKMDFQFPLFLSSCQMLVQMGFAKLTILAFPRYQPNKKDNFSWLEYFYRAGICALVTGLDIGLSNASLETITLSFYTMCRSSILIFVFFFSVIFRIEMFDWILLCITLVISAGVVLMVATETQFVLSGFLLVMASSVLSGLRWALTQKLLLDHPWTSNPFTSLFALTPLMFLFLLVAGLIFEGPVRFIESPAWKEFGPFMSVVILVPGTLAFFMVASEFGLIQKTSIVTLSVCGILKEIITIIASTLFYHDILLPINIVGLVITLCGIGVYNYYRITKGNKKEAEKEVEYIVLNENA Q10355 YDB2_SCHPO SPAC22E12.02; CHAIN 1..219; /note="Uncharacterized RNA-binding protein C22E12.02"; /id="PRO_0000082022" MSRVKTTVVRKAGGQVWEDPTLLEWDPNHFRLFVGNLGNDVNDESLYQAFSEYPSLVKTKVVRDREGKTRGFGFVSFKDSDQFLKAWREKNGKYIGSRPVKLSRATSDVKPNEVNEKTIDSKIRNSLYSRTIHHGNRVQKKIKNKHGKNSSKSSRAAQSAAAELISSSSITGARPANSTSVPNAVNTEISAARATESEASRNQTKASRDYSRASSFRRV Q10368 YDBI_SCHPO MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC22E12.18; CHAIN 1..336; /note="Uncharacterized protein C22E12.18"; /id="PRO_0000116607" MSDTMVKNQAEEDEIVKSLNNVLKIVVTARKCLDDMKPIELPSELVESPLSMLKDVATLIHQYTTKLSVAAKPPITRDALEKYANDMATTITPLIAAVQVFNAEKYGEIIQNRLKMYAERVLFGIEALLRSVSPKPLGYISEDWKTRGRLIDTGILWESCEKIEKLGSEGIVGYMLEEWDNFVSMLEDARSDLEDYKEGDDSNWDDFGSESEDDSKEAHSEEVFRSEEQIQLANSLLQKLNACKILFLSIKKRRIKNEYPNTFLGELFNAAKQTSDSIDDIVAQIQEDDENFENELDNFHRSARNLCKICISSAQEDSFTPWFSKWLENWEIVSQK Q10422 YDC1_SCHPO MOD_RES 184; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC25G10.01; CHAIN 1..297; /note="Uncharacterized RNA-binding protein C25G10.01"; /id="PRO_0000082023" MDTLPPATSEESFEIPNADVAGSAVLETETSQDIHQLEIEKDAGETDSDAGSIAMNVHQLDTAGEPLQSMNEDEVDPNNESTALDKKEPQSAPEGSENLGNDLFVSGIASRMQEDELQQIFSKFGTVTHVRIMREPVTKASRGFGFLSFSTVEEATSAIDNLNSQEFYGRVLNVQKAKRSRPHSPTPGKYMGYDRRRNSRDFPSNNKDGGYRRNNYRDRDSNRYRNSYRPSRPQREHSPGNYRKERYNVDSRPRRERHFHGRSFAHAEHHSVPNMRNDTPGNEALPSHSSVPPNEDQ Q10436 YDE2_SCHPO SPAC12B10.02c; CHAIN 1..235; /note="Uncharacterized protein C12B10.02c"; /id="PRO_0000116610" MSNVQRKRIDIRRPTLAELSSIRSIAMNALNGQSRNLSQKIFWHPLYLAVFGLVFMGIYRLTNMVEGNTKLRTFVLLILVSAVFLTLIEFPCRNVYAKISTEDNQPDGCLAEENLKHFYMARIDKERVIGIIGILPANAPGAYQNTPTIVHWTVIPKFYQYAFDLLDSALREAKEMGADVVSARVYSTDPMLKAFERKDFTPVVDEAFDYLSFFGLRRLVLQKNLSEQPGFENRR Q10440 SDHF2_SCHPO TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000255|HAMAP-Rule:MF_03057" SPAC12B10.06c; CHAIN 29..139; /note="Succinate dehydrogenase assembly factor 2, mitochondrial"; /id="PRO_0000116611" MLRKTNLSNITTLLRSARCMNRMPQLRFEHTKGDLKRVNRSYETRDAMLARLKYQSRKRGILETDLLLSNFAKDQIDKYPVSLLREYDQLLDEPDWDILYWCSGEREAPEKWKSSQVFKELSKYCRSQRNHTLRMPELF Q10442 YDE9_SCHPO SPAC12B10.09; CHAIN 1..345; /note="Uncharacterized mitochondrial carrier C12B10.09"; /id="PRO_0000090702" MIFNYVFSNSFSFLYLMVNVQCRIKEIMYWNICLYWDVFSKLIIYNKVCQFGRIHIFHGKNRHQLLRTCHFTPSKRHSAMSFFEALGAGICAGLAVDLSLFPIDTLKTRLQAKGGFVKNGGFHGVYRGLGSILVGSAPGASLFFTTYENMKSRLSQSGLGLSDPQIHMCSASLGEIAACIVRVPTEVIKQRAQASGGTLSSRNILQTILKSNNVWRDFYAGYGITIAREIPFTLIQFPIWEHLKLKWRIKHSRNKNLAHEAAISGSIAGGIAAALTTPFDVVKTRIMTSQQRLSYVFTIKSIVAHEGFLALYKGIVPRVLWLSGGGAIFLGCYDVILNFMKAEGL Q10443 YDEA_SCHPO SPAC12B10.10; CHAIN 1..419; /note="Uncharacterized protein C12B10.10"; /id="PRO_0000116612" MEKPLPNPPIQESLRKQSPQDAVYDDLVFGLKRYEAAFSIKDSIEDVLANFSKDEEKEMVCLSTSIAENPYQSLSLESVPSKILFGSFLFYVKDRIPEKAGYIIEEQFCKRLQQIDYDAYSFSPKECNEKLKNIFSEFSQMKLKMLSVFFSIVQILLPKLSGDYQEHVQFFASISAVVAPRGYVFEIYHAVEHLSLEAREVFQLHHPPSPKQTRRVVSEGPLNGVNYKQNTTNNRVSSFQNSQYSTLNNFQNNSNQSPNSNDLQPLQAEAFHSAHNGYSSSTLNLNSELNVMKDHDLQAPIPRALKQHKLPPIPVPEVQTTNIGYQTDLPLQNPNDNLVSLAIYEALYEKFLKACKDLEEVSKSYEESREEIEALHETFTEEVTSFQSTKRLKEEKIIQEKSRVDKMIDEYRQKLSEST Q10446 YDED_SCHPO SPAC12B10.13; CHAIN 1..240; /note="Uncharacterized protein C12B10.13"; /id="PRO_0000116613" MVGTSSLDISMSGSSSSDAEQWEKQTKSVHIDNSDVNSLILDYLVIQGDEEAAKTFAEEAQITDYYIPPYVKERLEICELIKSGSINSAICKLNELEPEILDTNSELLFELLRLRLLELIREVVEEKDTSDLAVERCLNFAHENLAPLAPSNQKFLNSLELTMSLLCFPPSSYSPALKNVLNYSQRERVANLANVSILKSQGLSNESRLLSLVNFERWCEKEAQRNSIEVQKFVPKASIK Q10448 YDEF_SCHPO SPAC12B10.15c; CHAIN 1..147; /note="Uncharacterized protein C12B10.15c"; /id="PRO_0000116614" MDSVKPIVKLEQAGSSNLEKASLLPCHISYDGPAPVFEYFHDKIQISNNTHSKTTVCLRGRELNGEELDLPENYTGQVVLCDDGLENDETSEKEIPESTWCINSTFEKVMLWNRDNMRSSEKDQWKRGVLEWIQFASKVKFNCSLYN Q10449 MU157_SCHPO SPAC12B10.16c; CHAIN 1..509; /note="Meiotically up-regulated gene 157 protein"; /id="PRO_0000116615" MKYWQAILFFLFGIAFANNLNIPWKACPNYKTYSGRRHYPATGPLRLPFQRPATSCRTFHSKSVEQTIEDVKEQLEDEDLARLFENCMPNTLDTTIRWHAADSHNPQTLVITGDIPAEWIRDSANQLLPYLPLAKSDSPLATLILGAIQTQAEMLIQFPYCNAFQPPKQSFLSGNDNGQSDRVTPAYDPAVVFECKYELDSLASFLKLSYTYWLYTKDQSIFTVKWLAAVERIIQVLEEQSSPSFDEKTGLPKDPVYTFLRNTDSGTETLGLAGRGFPLNANASLIRSAFRPSDDACVLQYFIPANAMMVVELSHLNQMLQASGHADIARTALVWANKIQKGIDQHGIVDHPKFGKVYAYEVDGYGSILFMDDANVPSLLSLPYLGFVERDDPVYVNTRKMILSSEGNPYYLKGKVISGIGGPHIGLRNVWPMSLIVQALTSDDDDEIMSLLDVLKHSTAGLGLMHESVDVSSFKSFTRPWFSWANSLFAELILDLLERKPHLLKKNAS Q10478 SAM50_SCHPO SPAC17C9.06; CHAIN 1..475; /note="SAM50-like protein SPAC17C9.06"; /id="PRO_0000215942" MTEQFESTSFPSDIPAVNEESKLSAEETFKSLSEILAENSTLPVGISSIRVTGAHHTRPSFIRKVLKTCLDTSKPAKSRSLLETLNAIQETTGNLMAFNVYETANIKIDRASSSVSGDDDLDVTIQVKEKPRLYVETGTDVGNVEGNVHANVLARNVFGGAELLSGNVSYGTRNRSTMSVNFETPVNADPKTRLRFNGHSNLRDNKSISSHDLLTKGITLSLQHQDLWSGEHLLSQNLLWRQVTHLTEYASPSVRLEAGDSLKQSLSYTYTRDTRDHLMIPTKGDYVRQTLELAGFGFLPGDASFLKSEFWGQKAVALNSSRSVSLSLSARIGALHSLNKKQVSLCDRFMLGGSTSLRGFSEDRIGPKDGRDSLGGTAYMAFSMSLLFPLPKVDASKPFRLQLFANAGGLSNLTSPNPCGTYKSILSKPCISTGLGLVYATPAARFELNFTLPIATTEKDIGRKGLQFGAGIDFM Q10481 TIM13_SCHPO SPAC17C9.09c; CHAIN 1..95; /note="Mitochondrial import inner membrane translocase subunit tim13"; /id="PRO_0000193631" DISULFID 45..68; /evidence="ECO:0000250"; DISULFID 49..64; /evidence="ECO:0000250" MGIFGGNSGNAPSSEDKKSIFMKQIRQELAVAQAGELISKINENCFDKCIPEPGSTFDPNEKSCVSKCMERYMDAWNIVSRTYISRMQREQKNLN Q10483 YDFB_SCHPO SPAC17C9.11c; CHAIN 1..240; /note="Uncharacterized protein C17C9.11c"; /id="PRO_0000116617" MVLKCLECDKLLSSIEMAEFHSTKTSHDQFEETEEEIKKRSPEELKQAIEALREKAKEKKEKERILALEEKKTNYKILQKSNDETAQAMRKMQDQARLRDLQKIRQQKAEDAEQRKKILAEIERDKKRRAAERENKNSSVKETAAPIKQPKNANSSSTCTRTPPTSGRFSIRHDGQVCNITIAAEETLRQLAQQVAEKMNVSPPTKFTTTFPRASYGTDVFDKPVNQLDLFPSAVLIPQW Q10485 YDFE_SCHPO SPAC17C9.14; CHAIN 1..232; /note="Uncharacterized protein C17C9.14"; /id="PRO_0000116618" MSNPTIEGDENRKENTKSNTKPNFDDLDDLDDILDDLDVPSAFKNEEKKNIDEHKQTGNTSKENERIKNDDNLNSLIQEMMSKFEDLGGPSGLDGSQLSSSFQNDQLLNVILEDQFATEKDSDNGAVNYGALEAALNSLMSQVTSKEILYEPLKDLEANYPKFLKNAKETEKQGFEEQYQKIQKCIQIFESPEYDARKDADIISKLVEEIQEKPLPAPLIDNSMETAGCPTQ Q10487 MFS1_SCHPO SPAC17C9.16c; CHAIN 1..531; /note="Transporter mfs1"; /id="PRO_0000173445" CARBOHYD 486; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MWFLRETIFGELVEYFSGGTRQVDVEKLGVCTDNSNVELSSCPDSSFDDEKTNQVNSEGLIIVTWDGEDDPENPKNWPLWAKLVVTFDVCFLTFAVYMGSAIFTPGIQEIRETMHVGTVPVILGLTLFVEGYAVGPLIFSPLSEVPQIGRQKIYVLSLIVFICLQIPTALGSSLGVLLPMRFLAGVFGSPALSTGGASLADIWQPWLYPYFMCFWSLGAVGGPVLGPLLGAAMVVAKSWRWQFWLLMMISALVLVIITFFMPETSEWHLLYKRAKRLRELTGNPNYKTEAEIASSQLSKGQFAKQILVRPIILCVSEPIVLSLTIYIGLVYSILYLWFEAFPILFTTVYHFTTIENGLVYMGILVGSVLTVAFYFIYLRKVMIPKFVENKGKFPAEEILIISFPAAFFIPISLFWFGWTGRESVHWIVPIVGTLFYASGSFLLFQSMFQYLAAAYPKYVASVFAGNALFRSSMAAASPLYARAMFNNTGPSYAPVGWGSTILGVISCIMIPIPFLIYKWGLKLRSRSKYAT Q10492 PNN1_SCHPO SPAC26F1.02; CHAIN 1..197; /note="Pinin homolog 1"; /id="PRO_0000116620" MKILAMDERREELSAKSTVQNVKISEAPILDGKVNNEDSHMEIDQPEGSMEEDDHRQVKEKNTSENSVEQKRGRRMFGALLGTLGKFQQESEREQKSARKVKRAELEEKLAKRREQELQELEKQEKIEAEILESRLQEQRKVALDELELDRNDLKKVLDNKKSYYLRTKTQPSLFYRPYYLLPSQRTQLEQMKSEAP Q10493 MU106_SCHPO SIGNAL 1..34; /evidence="ECO:0000255" SPAC26F1.05; CHAIN 35..115; /note="Meiotically up-regulated gene 106 protein"; /id="PRO_0000116621" MSIKVEWIKFTRLKKCATLLVQLSLLRYRYMVLAYNHKFDCIVVTIYCGCLFWFSNGALFTEGKARDRGRWAKATMKKNYGVKLKIFLFTILLAFETNTFTPYTSTFSHFARGCL Q10495 YDG8_SCHPO SPAC26F1.08c; CHAIN 1..977; /note="Uncharacterized protein C26F1.08c"; /id="PRO_0000116622" CARBOHYD 210; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 262; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 265; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 300; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 346; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 364; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 496; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 773; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 926; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 969; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNFHHGWTFHKLRKNEHFLKYSAIFYSLLKPVVALFACQCLVLIRPLARKIGSFPFLILTFHTLFYPIQNTVGAQFEVIGQSLMGTAVGVTWGIITKLFATAANRNHGDGSPILATSLALASFISAYIRSRYGYRFFCIIWIFIDCFLLTRDPFEKTIAKSFYISLVYPSLIAAGVVSLVTILVPPMRMASDLVGQSGLDHLNKIMQSLNFSVENFFPSDESVSFSSSSSVIKRMFKEHESVLRNSMDDFHTAISSSEIELNYSNVSVSTLKLLEPKFERITLAMSAQLAASFTLYETYNFSIYKNQDKEVEGDIRVSELRFSLPESTEVQQKRNIFTPQYQLHINGSLRAKVRPKDSKDRIVNLSNLYFSNVDHMSSLILGSLKLAHAIMKWLVSDVEHIPDERLRECIESLQEIDSKEENLMTEIFCTAFKETKKVNDFGGFEEIEDEEEVLVIAYYLFNLFEVAREVKNLLLLLEGLKAQRHNKPKLFFRKFNLSLFDKQKYANYAISALLTHFTAGDADKCDDEAPDDASGEEDDSPKVLNDQSFFDSVRYPLKFFLRKMRRKCWRVYHFTARSKDVRYGLKMAIGIGLLSIVAFQKSTAARYTLWNGQWSLISTLFVLEVTVSTTLRVGLFRTLGTLSGAVYAYAAWEVSQGWSYAIATLTFAISWVSCYVKYNTEYSGIATVFNITFPPILYGSYLKTSTISPFHLACIRFIVVNVGIGMAIVVNIVVFPYLARRVLKYKLGQASLLSLKQYTTLSDYLLSRNLYTNLTICEGYKKQISSLLVTARKLLQLVNMEFNLKGPFPVGIYNDLIIKLENLGIRLVVLNRVRSRFGLYLYYDVVKNMIDYRKDLIVSMTLTFYILYNSIMSKAPIPYFVPSCRQALWNLRLAIEEEGKRRFVTNGGILAQGAGSDGVAKDVPENHSWLPAQKNFFLYYVECQVIGDIVTDLEYSISLVRRINGEKENETIGKKMA Q10498 HGH1_SCHPO SPAC26F1.12c; CHAIN 1..356; /note="Protein HGH1 homolog"; /id="PRO_0000116624" MSELIELVGFLHDQNPQVRMLAVQHLLPYTARNHPQFSIWFHNDFEPVKDLKALLKDKPQIASQAVTALVNVSQNEKVRKVLMDDEFLQLIFSIVTNPLHGLADLSCMLLCNLAKEEDFARILDMQVPLREFSLSKNIIDQLMDLFVKGTDHGINEYANFDFLANVFADMTRFERGRKYFTTLQEYDHVIPASKLVVFTEHKSLLRRTGVAAIIKNISFDIPFQKVLMDEEGINVLPYLLLPLAGPEELSEEDMDGMFDELQLLPDDKKREPDHFIMKTLVETLVLLTATREGREHMRRRKVYPIIRELHLNVDDEEIREVCDQLVQMLVRDEAPEELEHIQDNPPDEDDVIVEVD Q1K9B6 YFS2_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPAC19D5.02c; CHAIN 18..223; /note="Uncharacterized protein C19D5.02c"; /id="PRO_0000371802" CARBOHYD 58; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLGQGLIFISLAFVAHALEIPISCAVSHNEQTEIFPHGTIDIPEMTFRPSDSQIDWSNLSHSDFVQCGVYEDSTNTWLAGASKYKIDEIKTLPKVPRDHYIILCDSSESNEIAKFTQVVHSFDFSSDSESAVVEQLHPSSPIPILTTAVRKKGSRPSKPQKEKQGNKQGSKTEESPNVDEDELESEPEEKTFFQKYGLYLIPILFLIIMSGNNANQQAANTAK Q1MTN8 ACL4_SCHPO SPBC16D10.01c; CHAIN 1..336; /note="Probable assembly chaperone of rpl4"; /id="PRO_0000351428" MSVTDAELLEIREKLVKDETSEALILAKKAADKSPKEDGRAFELLGEVYAELADVKKARSAFKEAVSRSKNLTNDQGYEKYLWLAQINDNGSKALKLYQKGVTILERLLIDKGEDADLKKKIQGAYCSIAELFMTDLCMQPDAEENCELYTKLALQIDATNAEALQTLASMRISQQKIEEAKDALSKCLQSISRAATEDSVDLPTYAVRTSIVRLLIEVEMHEEAHQLLVYLQKEDDQILDIWYLLGWNCYVEAQNLQEQGNGSEEEIKELLMNAKFYFISALGVYQKIGWDDEGIKSHIQELLEILNGLGVPNMDEENEEAEWETSENEEEMDED Q1MTP1 THP3_SCHPO SPBC2A9.11c; CHAIN 1..395; /note="THP3 homolog C2A9.11c"; /id="PRO_0000352828" MKKEHHSPWPDSLKEFIGRCIQDAEENSQPELEDEVKLLISRQYEMGNIWNVDWSSMNLESLRKLTNAQNTIIEDKKRKVEKPVSGNQFSLLSEEDEVDKKEKRRRRFENGSRSQNNAKSEELKVNPENGAIIGRSTELEKRYLRLTSAPDPDTVRPLPVLKQTLELLKKKWKEEKNYAYICDQFKSLRQDLTVQRIQNEFSVLVYEIHARIALEKGDVGEYNQCQTQLFHLYSFGIPGNTKEFLAYRILYMLFTKNRSEMNSLLANLKEEDKTNAAVTHALEVRSAMATGDYYKFFHLYLVAPNMGGYLMDLFIERERVQAMIMMCKAYRPSLTMEFLANTLAFEEMEDCVNFFRSCNAVYDSKDPNRILMKESTDRFEKCMKKHAVVDIKGQI Q1MTR0 ATP23_SCHPO ACT_SITE 87; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" BINDING 86; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 90; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /ligand_note="catalytic"; /evidence="ECO:0000250" SPCC320.12; CHAIN 1..185; /note="Mitochondrial inner membrane protease atp23"; /id="PRO_0000330073" MSEDPQSWSKERKNCERVKRALMSQSPVIIFLKTALDRLNCNIEAKDISCQPCDAQSTGGYIPGKGIVLCENRLYTKKMAENTIAHEMIHMFDDHRFEVDWNNLRHQACSEIRASSMSGECRWTKELRFGNIKTFRKHHQECVKRRATISVQGNPNCKSKEQAEAIVEEVFNSCFNDFRPFEKIY Q1MTR1 IRC3_SCHPO BINDING 53..60; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SPBC11C11.11c; CHAIN 1..606; /note="Putative mitochondrial ATP-dependent helicase irc3"; /id="PRO_0000353817" MLLNACCKKNLWPRNGSTIFRRFALKLRPYQEECLSACLNAFDEGKRRIAVSLATGSGKTALFPHFIKYAPTLRPNSEQCLILVHRKELALQALKHCRESLPNKSIEIDMGNQCASGLADVTVASVFSLKNERLLKYNPLNFKLLIFDEVHHMASPSYLRILEHFGAESEKSKVNVIGLTATLFRADGKGLACGLDEIVYHRHFVDMIKDNWLVEPKVINIKWSTDLVLADSSSFLDQEKLKKEAQSEKAIFEIPRAWLEHASNRSSTLVFCINVEHSLKVCNAFRKLGIDARALFGETNDSERETLIQDFRKKKFPVLVNCMVLTEGTDIPNIDCLMIARPTSSPNLLTQMIGRGLRLHEGKRDCLILDFCDSLRRVSLHVDPTLAGLSPDEVENFYNKSKNSLANPDYDPKIYGLQSVLWYSKLRKLIEMMDNIKNKDRSIFNLSTNAWVAVGMGRYVLSFLQKVLIIDTNFEDGTHKISEYTKEKLGTRVYNRKRIVSDRIPSLKFAIRAAETYISNLKTPRSLISRKAVWRMRPASVRQINFLKKSNLKLDEKLLTAGVAADMITKVIYGGKGRQVRTDKLQSYLKHDANLKRITTLKELKG Q1MTR7 YBPE_SCHPO ACT_SITE 166; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 178; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 182; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 47; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 67; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 178; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 182; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 213; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 215; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPBC16H5.14c; CHAIN 1..286; /note="Uncharacterized oxidoreductase C16H5.14c"; /id="PRO_0000352847" MLNHILLLVISLVCAALTLSWFPLLFRKQSYSCAKGLIVITGGSGILGHAIIQEALDRGFSVASLDSTEPASFLQYNSKFSALKCNITKDKDVEGCVHSLKKMNRTPFALINAAAIAPKNHLLSISRQELQKCFETNVIGQLAITSALFPLLLQDPNPHVVNIASSLAYFSAMGVGAYSSSKAALVSLHETLEEEVLSQHPNFKFSLYVLGQIKSTMFEKDTPNRVLAPLLEPQNLAKIIIQNLYTNKSGRFYYPFYARFMPLLRFFPLPIQKLARLFSGMDKIYS Q1MTR8 SVP26_SCHPO SPCC1795.10c; CHAIN 1..227; /note="Protein svp26"; /id="PRO_0000247437" MIVLNALSYLGIVLGFIGMTVSIASALYYISEFVEEHSRLAKAFLCRLVYFIMAVMVFLVIFDGFPFWLSAFSIFSHYIYKINFDTFPFFSFKRMRFLLACFLIVANHILWVRFFQVHEFPIKPRGLTYDFVGQRLLTSRASFSQVASFMGVCVWSVPIGIFVSFTAADNTLPTITTPSSSSPDAYSSGSSRRTSNVLRQAYKKLGIFVERSLTSLGLSDRSSERYV Q5WRL1 RM27_SCHPO TRANSIT 1..13; /note="Mitochondrion" SPAC3A12.19; CHAIN 14..93; /note="Large ribosomal subunit protein mL41"; /id="PRO_0000343157" MHQSLLCFGARRLPMTTKLGHQYYKGTRTGKMGQKTRHGGFLVQWSRVRTFVPPSGDCELLPFVSRRIQATKGTYPEGANGLDGAVYFDLAHS Q6LA56 YF4B_SCHPO SPAC3H5.11; CHAIN 1..393; /note="Uncharacterized kinase C3H5.11"; /id="PRO_0000316601" MAEFDDSCLPTNPTTENDYHGSFPYCSVHAQLYPYVSDCMVMHRKAPINEQEALRDVVWETRTINKKLHVTPIKPNITSILLVSKPGDEEVEEKLKEFVYWLISLDNITVFIQKSMEDLFEKTEKIQYWTTLLCTKHSQLFDLVLTLGGDGTVLYTSRLFQRTVPPIMPFAMGTLGFLTHFDVKKYKTSILEICNEMYVHLRTRFECRVMKKKNRTQWINIDEHLSQSLHATDTETHTFTDSLVVLNEVVIDRGPNTAMSDIMLYVDSKYLTTVKADGLCISTPTGSTAYSLAAGGSLCHPDISVMIVSPICAHSLSLRPIHVPDSMALHVVIPQDAQQSSWISFDGRNRTELLPGDYLTVRISRYPFPTVHSTEEDADWFESIKRTLMWNQN Q76PC3 YQ73_SCHPO SPCC1442.03; CHAIN 1..338; /note="Uncharacterized mitochondrial carrier C1442.03"; /id="PRO_0000343156" MEPGIPPMIDKAPAYSHVLIAGGIGGATADFLMHSLDTVKTRQQAALYTNKYNGMVKCYSTILCEEGVFHGLYSGVCPMLIGSLPATALFFSSYEYTKRHLMSNYNLPETLCFLLAGFVGDLFASVVYVPSEVLKTRLQLQGRYNNPHFQSNYNYPSFRGAVKQIAKQEGMKTFFYGYRATILRDIPFSGFQLLFYEKLRQVAQKECGQKDIGVFRELITGSLAGAGAGFLTTPLDVAKTRLQTMIRTTDKVSDDINSGRYFFAKDENSKSKSAASLVKPKIGIRHVLGGLYKSEGLLGLFRGFGPRIFWTSSQSSLMFVFYEGIIRLFNKNNVLERD Q7LKV1 YK98_SCHPO SPAC20H4.08; CHAIN 1..270; /note="Uncharacterized protein C20H4.08"; /id="PRO_0000353826" MSVPIDRINTVDTLANTLESNLKFFPEKIHFNIRGKLIVIDRVELPILPTTVLALLFPNGFHLLLKHEGGDVSSCFKCHKIDPSICKWILDTYLPLFKKSNNAYPSKIAFNPISNTTLVLFLTECCNIYLFSENKKPVDQKIRSDLLEQTFKNNDVFESADKKKIRKGLSDGPLVDALQHCGFRYNDKWAKRVKEPKLMSLMSYIITTVESSSLSEEFLSKILKLWGQPGNKCWWINEVIKVNGSLINVWRRKQWLLEVTIMGNRENSQD Q7LKV3 SEN15_SCHPO SPAC959.10; CHAIN 1..143; /note="Probable tRNA-splicing endonuclease subunit sen15"; /id="PRO_0000194027" MQHNTFLPNDAVEEQKQNPYYGILRAVETDLRLGQRWCELKVHVLDIDLKTKRPLLSGIPVNGQLKDKLQYVLPLYLQETISIEFLSSVFDSMKKLSLPLVKDARGLSGDEFFLYLGIMCSDSTIVYYKITDGLIKPRQNDEE Q7LKZ5 FAM50_SCHPO SPCC1020.12c; CHAIN 1..288; /note="FAM50 family protein C1020.12c"; /id="PRO_0000352811" MSGHTDADEIHEILRNSTTGLVHLKDYQRVKQNIVEKREKHALSTTSTKIKKRKDALSKKVKQGIKVNKGKLSFGEDEELENDDLPLKKVEKKMFMGKDPSADTSFLPDAEREIRENAKRAEYRKQWLKEQEQIREKEILIPFIYYDGTSTTYHVRTRLKDSVGHFLADMKQQIPFLKRILDMDKFLLVQSDLIIPHHHELYYFYINKVQGRDGLLFDFDKLSCSSPEMVATTQLPSQCIPHLVQKSYYLQNRHVFPCVHWEVFDSRKDYSLEKHATDPNAALFYRPS Q7LL00 YQJC_SCHPO SPCC1840.12; CHAIN 1..791; /note="Uncharacterized oligopeptide transporter C1840.12"; /id="PRO_0000353819" CARBOHYD 265; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 621; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 759; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKTPKFITYVTRGFKGLESKSVENNKDHIVENSSPIASKFHEFDEQKKSFEIINYAGHEKFVDDITERESSVPGNAVYDITVRDIDAIVPVTDDVDIPASTFRMWILAFGLATVIAGVDAFFLMRYPSVSIAAIVALLVAYPLGQLWYYIIPQWEIKLPRGIRVSLNPGRFNRKEHACLYIFVNICVSAKLVNTLIIEQIKFFGVNIGIGRAILFNLCSYLSSFGWSGLALPILVYPPTLIWPSVLSSCALFKIFHDNDNTKACNWTISRLRYFFIVFVASFIWYWFPDLIFPALSSLGAWISWCKPSSAVLSQIFGVKTGLGLFPLTLDWAQISSLSNPLITPWWATCCIFTSFVFWIWIVLPGLYYQNYWQVAHFPIMTNSIYTVSGKSYDAQKVVDSKWELVTQKYQEYSPVMLPIAFIINIALSLGAFSSMMISFFLRFPTDVIQPICHVFKYSDIHTKLLKKYKRVHWGFYLASIIVSLGLGFAFTEGWHDIQIRSYGFVVSMVIGAALYIPLSLIESRSSFTISMQAFFEIVAAFWFNGQPMALLYFYSFGFGTLQHAMHMTQSAKIGHYMKVPPRLVAALLFTSGIWSSLVNSAVTGWIMYHVRDVCTSNAENNMTCRSPKTQFNSHLIWGLVGNHIFSSDGRYSFVMWFFLVGAVVSVVVYLLQISFPKSSWKHVNPALLLGGAAQIPSVTGINYSTWAAVAFCFNYLIRRGYYSWWKKYNLITAAAMDCGVAIAGLFIYFCVVYTGGSSNFSWWGTTVSSAGCDKKGCAHLSVSDISKPSGW Q7LL04 YQK1_SCHPO SPCC1494.01; CHAIN 1..321; /note="UPF0676 protein C1494.01"; /id="PRO_0000353799" MGSLEVPCIDLSENDTSIVVKELLDACKNWGFVSLKNHGIPLDEIDRTFKLADKFFDIPVEEKQKYLFKGGRLHSGYTGHFGEKLDMEHQSRGDLKESYDLAGFPDPKLENLCPFIAEHMDEFLQFQRHCYKLTLRLLDFFAIGFGIPPDFFSKSHSSEEDVLRLLKYSIPEGVERREDDEDAGAHSDYGSITLLFQRDAAGLEIRPPNFVKDMDWIKVNVQPDVVLVNIADMLQFWTSGKLRSTVHRVRIDPGVKTRQTIAYFVTPDPETPLSPLFEEKTGKDIETVTAGEWIDGRINFTYGYSAPPKGYLGSQNDGIVA Q7Z995 YGMI_SCHPO SPBC19G7.18c; CHAIN 1..252; /note="Uncharacterized protein C19G7.18c"; /id="PRO_0000304093" MDFFWERMLNDPQNHFSDDQKEFLNHAKYRVKRNTIFGMLVGFSLPLYLARNKKVTPIRLYATSIIGGLAGNGVAQITTLAYNLSAIRQRDDGFEILRKIQDSLIRQRTTMRQGRFPSSSSEFPPKNSKYQLPGSMPNTGASSSQDPFTNSQSTEKEDAMYSKDNGFEDRSKPASAWEAIRNRNRNTGNNSFPFYEEDSSVKSTDSAFSGQENSEAFPSRTSNLGSEQLDEPISHEQEAFDQLIWNDSSSSK Q7Z9I0 YHA8_SCHPO SPBC409.08; CHAIN 1..552; /note="Uncharacterized MFS-type transporter SPBC409.08"; /id="PRO_0000372711" MPLEKTNTHDSTATVEDQEATDNPMHLTQSRMLDLAGNPNRTTSRQSETLFPNGVDLNYPFTTTRGPPDVAEYNLETAEGVYRDPTINEGEEELVTWELNDPENPHNWSRLWKWYITIVNSLLVVCSAFGSSVIAGDLEDVSRDLKVGPEVANLSCSLMVVGFGIGPLVISPLSEMIGRRIVYLVTLMIYIVLQIPCALAPNIACLLIVRFFCGCFGCTPLTLAGGVISDVWETRERGLAIAFFAAGPYAGPTLGPLVGGWIGVGTGDFRWIFWVNMIYMFVMYLTLLPVPETYAPVLLRWRAQRIRKETGRQVFTAQEKQMLSFKEIVQVNLTRPLTLLLTEPILVCISGYIALIYALLYGYFFAYPNVFVKGKGYNEGITGLMFIPILVGVVGALSTTPFLEKQYMAKLDANNGKSVPEWRLVGMCIASPFIPTGLLIFAWTSFPRLIWIGPAFSGAPFGYGMVLFYFSANNYLIDVYQNYCASALAAKTMVRSAGGAAFPLFIDYMMDGMTRQWAFFLLGMVAVAAIPIPFTFYLFGDKIRARSKAAIV Q7Z9I3 YCP8_SCHPO ACT_SITE 158; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 162; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 17; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 36; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 62; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 89; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 158; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 162; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 191; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 193; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPCC663.08c; CHAIN 1..253; /note="Uncharacterized oxidoreductase C663.08c"; /id="PRO_0000374028" MSTTNKIYFIAGGNRGIGLSLVKELSNRKGTVVFASARKPGAATKLQEWSKSHSNVHIIKLDVSSLESANEAAQEVTKVVDAVDVLWVNSAVFHSFGPVVNTPDDVWNSHYKTNVLGPIHVYQAFYPLIKKGRSKIIVFTSSLAGSMGAFFPSSQSAYGQSKAALNYTMKEISFELQDEGFIVISIHPGAVRTDSAQEIVNQHAEKKPEILDLFAKQALTPEKSASDMLKVVDNLKPENNGLFYNYDGTIIPF Q7Z9I4 YCP6_SCHPO ACT_SITE 158; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 162; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 17; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 36; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 62; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 89; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 158; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 162; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 191; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 193; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPCC663.06c; CHAIN 1..253; /note="Uncharacterized oxidoreductase C663.06c"; /id="PRO_0000374027" MSTTNKIYFIAGGNRGIGLSLVKELSNREGTVVFASARKPEAATELQEWSKSHSNVHIIKLDISSLESANEAAQEVAKAVGKVDVLWVNSGIFHSFNTVLNTPDDVWNSHYKTNVLGPIHVYQAFYPLVKKGESKIIVFTSSLVGSMGAFFPFNQSGYGQSKAALNFTMKEISFELQDEGFIVISIHPGMVRTDSAQEAVNQHAEAKPEILDIFAKQALAPDQSASDMLKVVDNLKPENNGFFFNYDGTTIPY Q8NIP8 WTF12_SCHPO SPCC622.21; CHAIN 1..197; /note="Uncharacterized protein wtf12"; /id="PRO_0000193226" MKNNYTSLKSSVDEEDELKTGHEIDLEKGPLPEHNSEGESTLPPYSDISKLANLVPEDSSTGPTETANPNVERRQEFKDLHPNIYSLLRLLIAVLAVSVVFFTAWGCVNPLEKSTFGKIAFFVLIGLTCLILLITMILEPGLIGISIMKRLIGDNGNDERDYFVENRLLSSPDCDARQHANSDTAIPLREMNPESEA Q8NIQ1 RNK_SCHPO SPAC2F3.18c; CHAIN 1..85; /note="V-type proton ATPase subunit f"; /id="PRO_0000304124" MKPLVSPGLAKACTGLSLIGIVFLLVLSYLFSIEAETLMHDLVGSGLTGKQVAKTCLGAVVIYAVFFLFCGSQVIVSRYQKPVRI Q8NKC1 COMT2_SCHPO BINDING 78; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 100; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 108; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 127; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 128; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 156; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 183; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 183; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"; BINDING 186; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 211; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 212; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000250"; BINDING 212; /ligand="substrate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; SPBPB21E7.04c; CHAIN 1..281; /note="Probable catechol O-methyltransferase 2"; /id="PRO_0000318149" MFAQALHWLTTSKLRYALALPFLFFILYTKTKKSKEQELENYIFSLPREKLDQIRGKPDEVINVIDEYVEQGHFLMNIGKLKGKIISEKIQQVKPKVMIELGGYVGYSAILFGKQLTDPSAHYYSLEVNPKFAKIASKIIDLAGLSNKVTIIVGKATDSLVELRRSLPNVIPSFEYLDFVFIDHWKDLYVPDLRVMETLDLIGQGSIIAADNILRPGVPEYVKYVQGSLDYRKEYDSTVSNVNGPQFIGKWNIIYKSKTIKVDDGKREKDAVEITEYIEAK Q8TF80 WTF5_SCHPO SPCC794.02; CHAIN 1..269; /note="Meiotic drive suppressor wtf5"; /id="PRO_0000193222" MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEESTLPPYSDHALVNNPPNTHRENHSYGTTDNSSPLLIILLISFTSIILFNAPEVCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWTKAVKVTVISLAKCVKVTAIFLAQCVKACGKGIKHFLKKWENMPMAFSEVFLFNILVGSPRMNLRYIFGDRWGLKCSLADHIIFVVLSILVFIAETVKPGSIRVNLIRKMGYEAKQQVNEYTAVPLREMNSESEA Q8TFF9 YP23_SCHPO ACT_SITE 134; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 209; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 233; /note="Acyl-ester intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4; SPBPB8B6.03; CHAIN 1..547; /note="Putative amidase PB8B6.03"; /id="PRO_0000316203" MDTPTWEVVAALKRNQVLNSIPKEWRKPNIRKEMISSGYVNTYEYLNLILPPEENAITNLSMLELATNIAKGNYTSYNVTKAFCHRAALAHQILNCCIEIFFDEALKKAKELDDVFQKTSKVVGPFHGIPISLKDQVDLPGKDSSIGYVSLVGKPKTEIALLAKILQDKGAIFYVKTTVPMAMMAPQTVSNLHGYTYNALNINLSSGGSSGGEGALLGSGASCCGIGTDIGGSIRIPSCFQGLYALKPSTGRISYLNVTNSYSGQELIPSVIGPMARSLKDIEFFTETVIASEAWKIDSKLLPIPWKNQSHLKSKKLIFGVLKTDGIVKPHPPIIRALNEVVAVLEKSGYEVIEISIPFQKDMLDTVVKVFSADARFEINNESQKTGEPVVSVVKRFVSDKIFKKPITVNEWWDLGNQVYKIRQMFLELWNNTAIQTLSGNSIDAIIAPIWASTSFLPESKADHLYTSLFNICDCPCVVFPFTKVDANIDLSDVSYKPLNEEDKENNDMYDPVLFDNMPVCLQVVTKKLEEEKCLAAASSIMDCLTN Q8TFG1 GHT7_SCHPO SPBC1348.14c; CHAIN 1..518; /note="Probable high-affinity hexose transporter ght7"; /id="PRO_0000050415" MRDFQSRFADRYNQITNSYSYSSSRQGLITGMVNVGSFFGCLLSSPVADKIGKRLSIIVWTTVYLIGIIIQVTTVPSWVQILVAKIWTGLSIGALSVITPGYQSEVAPAIMRGAIVTTYQLFITLGIFIAACINMGTHKYSHGTTAQWRISIGINLLWGIITLVGIIFLPESPRYLIAIGKDDEALKIMCYNNDLPLEHEIIQTEYHTIKSDCDAELAGGPARWPEIFNANIRYRTFLGMAVMMFQQLTGANYYFYYGTQVFRGTGMDSPYLAALIPDAVNCGCTFGAIFVLEFFGRRSPLIVGGIWQYICFFIYAAVGDRALYHKNGTSNHRAGAVMIVFSCLFIFSFSQTWAPAAYVIVGESYPVRYRSKCAAVATSANWFWNFLISFFTPFITNSIGFKYGYIFASCNLTGAAIIFLFVHETKGRTLEEINTMYASNLKPWMPHPEGYREFGREQNNATLKSHIGLNGETTELIENTDNQGDSGSFQTSTPDDSRPEQNQASATYIRPDKREPRL Q8TFH0 YIKE_SCHPO ACT_SITE 281; /evidence="ECO:0000255"; ACT_SITE 312; /evidence="ECO:0000255"; ACT_SITE 540; /evidence="ECO:0000255"; ACT_SITE 608; /note="Proton donor"; /evidence="ECO:0000250" BINDING 197..204; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255"; BINDING 346; /ligand="beta-D-fructose 6-phosphate"; /ligand_id="ChEBI:CHEBI:57634"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579, ChEBI:CHEBI:456216; EC=2.7.1.105; SPAPB17E12.14c; CHAIN 1..668; /note="Probable 6-phosphofructo-2-kinase PB17E12.14c"; /id="PRO_0000318494" MSNNNNKDDSELQSRTHYYNPDRTAIPVKDDVDQLDKFGSPKLSANDHSFTNTDSVTSEDRPFSSPVSTLTSNSANFSDSSLQNSPVHPIPSPALSPTLNLGSRPDVKRVSSGGYFALPKQLTSIRQTHRPMSQQHRVPSFHPASDTAPPSPIPFHHHLRKKGSSMSIPGQTSIVSSNNGSEATNPPEEKLAIIMVGLPARGKSYIVNKLVRYYNWLQYNCKAFNVGNFRRKHASHSHDDASFFDPSNEEASKLRESFAMDTLDALLQWFEEEDGVVGIFDATNSTSKRRKAIVDHLSKVPYVTTLFIESICNDEQLIAANMRMKLVGPDYKDLNPEQSLRDFQERVRMYERKYEPLGKSEEDLNLRYIKVINVGKKVVAFNIRGFLAGQAVFFLLNFNLSPRQIWVTRHGESVDNVRGRIGGNAELTPLGRQFSEDLALFIDEKRDEFQERLYNDYSKESHLLQHGSHSFNGKQFETSFNCLTPSENTVNDPQVLDPEDEERLEKPYSVWTSMMQRSIQTAAYFDEEQYDIKAMRMLNEICSGICDGLTYEEIKSIYPKEYEARKLDKLNYRYPGSGGESYLDVIYRLQSVIVEIERMKHHVLVIGHRVITRIIIAYFLGCRREDIAYLNVPLHTVYCIEPQPYGTDFYQYNYDPNTRKFSRVPFSL Q8TFH2 YIKC_SCHPO SPAPB17E12.12c; CHAIN 1..317; /note="Uncharacterized mitochondrial carrier PB17E12.12c"; /id="PRO_0000310799" MQKDKFGPCAPSRIPLLSNDLISMLSGGVAATVSRTAVSPLERMKIIFQVQNNKEYTSLTSTLVKIWNREGLIGFFRGNGTNCLRAFPYGAVQFATFNMLKQRALKNRSHQNLENHERLLFGAIAGAASCATTYPLDIARTRLSIETAGLTSRSLAINNVANNSLKVKPLTLWSTLLYIVQHEGGYPALYNGLPATLLNVVPYVSICFFTFEFCKQKFFSNADLTAFQKLFLGGFTGIIGQTLTFPADVLRRRFQVNRIPGIGHNYKNIKSAIFHIYKTEGINGFFRGYSSNMLKIIPVMSITWYTYETVSKMLHDL Q8TFH4 YIKA_SCHPO ACT_SITE 247; /note="Proton acceptor"; /evidence="ECO:0000250" BINDING 87; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 89; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 107; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250"; BINDING 186; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a uridine in rRNA + S-adenosyl-L-methionine = a 2'-O-methyluridine in rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54152, Rhea:RHEA-COMP:13812, Rhea:RHEA-COMP:13814, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; SPAPB17E12.10c; CHAIN 1..301; /note="Putative ribosomal RNA methyltransferase PB17E12.10c"; /id="PRO_0000317209" MSMRIWSRSSSAYSAIARSSSWFNNSLFSSCLLRFYSNPPKKTKKNTLISLRKSAETANEKFIEKINKEHQLFKPGQIVVDLGCAPGIWSTIAARHVGLFGRVIACDIIPCRLPENSSMIQGNILSMEIQLEIAKAAIRSRNSFFRNQQDHNSASIPYLQSVFEEERDTKEKAKIEDLSADVIMSDLGPPFPMVQGFEFWISKLPYLAMQTNEHLAVKDELDSLYLAQAALLFAIKALKPDGIFLCKVLESSHLRSFAEDLSMCFKCVKKIQFKTKIKDELYAVYFCSGKQLSCHSKLLNI Q8TFH5 YIK9_SCHPO SPAPB17E12.09; CHAIN 1..203; /note="Meiotically up-regulated protein PB17E12.09"; /id="PRO_0000304028" MQDRFLKENTEIINLSSSIHPNRDSYLDSQSDPLNQNLYNIETENVKDLNIEDVDYYEKLQNFKIVDENIDPGLRTYSKRSVGVNNTFQNPCNRKIEGYIKEIERLSNSNKNLQAAVLQMAVSDTDDPRLKEEYKQTEKELLREISGNHKSKILKLEEELNDLKHSMKEMQLYMTKIIDKAMNNASLENLFSLDENNTKIHDK Q8TFH6 EOS1_SCHPO SPAPB17E12.08; CHAIN 1..209; /note="N-glycosylation protein eos1"; /id="PRO_0000350749" MKQYLNTVISNPRPAQALGINQPFVVFCFITSRALSFVPAIYWCFKCLHLAFVADKFKWLPLTSALWTLVSAYLSFVLANGFLLKWLIHYSIGPTIIRLFSLNVINFSFLSLSVSFITHGDNAYLLPAWIAISCFQTAAYIVQDWITSPIIRTLPFRSSSSSSSNYRHNLDFLEITVFAVVPVGIASFFTMVMLIWQLYKYPDSFLVSA Q8WZK1 RT21_SCHPO TRANSIT 1..14; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC839.09c; CHAIN 15..121; /note="Small ribosomal subunit protein bS21m"; /id="PRO_0000350750" MNSSYFPGVLGVRWVHTNRKLQKRKEEHGAFQDSLHFMIPAAETKDLGASVTVGNSLTRAFRQVDRICQRNNVPRLFRSQRFYEKPSEKRSRVRSERHRARFRAGIVRLVNLAKNMRRWGY Q8WZK4 DCN1_SCHPO SPBC839.03c; CHAIN 1..251; /note="Defective in cullin neddylation protein 1"; /id="PRO_0000129515" MKPDTVSLTRAFSKATSTSSKAALSWLKKYNFDYDVAYTKWIQQKSREEAEKQLNNVFSQFSSKEDKDLIELDGSVQLFTALDISLEDPETLLVSYFLKSPRMGEFHRESFVEGALNLSTTSLDQLKLAIKEKVQVWRSDASLQKAIYIYTYPLACDKGKKTLSTSIAIEFFQILLKDTFPLLDDWIAFLKVSPIIEKSLPKDTWNELWDFSVFVKSDPNCSNYDFEGAWPTLIDEFVSYYREHGYKNSSS Q8WZK5 ALY1_SCHPO SPBC839.02; CHAIN 1..504; /note="Putative arrestin-related trafficking adapter SPBC839.02"; /id="PRO_0000353798" MYIPNLRNYHDKVFPYGPSSNGYNPVIRLTDRTTQPDPSQHIYQEEKISKCEGLSYRAREWLLLSSNSNARVAIALAEPVLYLPGATSSEIQSEHSAVLRGSLCIQIYKPVKLKKIQLSFKGKSRTEWPEGIPPKLFDTYEENSIMNHCWVFFHSEQKVDENSHGAVWYKVLPHYADTAHYPRSMECFYPGEYVYNFELPISCTYPESIQTDMGRVYYFLETLVDRSSTFSGKSTGRIPIELIRSPCSTSVATSEPILVSKSWEDRLHYEVQVGEKCVVMGQVVPVNFKFTLLGEVKFHKLRLFLMERRYYYCRQRSVRRKEKTRQLLLYERSAPKNQCLLSDWKQVRPDVYELSDQVRIPGCHDMAANIVHFDTTYPNIKITHTVRTVLRFSCENSPELMGSAKYLEIYIDSPVRLLSCRCSDGSTMLPAYCPIIPSSEVNFCSIDNRIIAGMNRDLALDSDIIGNSPPSFDSWTAVPYQAPPPKYDDIFQSGSSHDENHDDN Q92338 ABCI_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC2D10.18; CHAIN ?..610; /note="Protein ABC1 homolog, mitochondrial"; /id="PRO_0000000261" MANSGLWELITIGSAVRNVAKSYLKAEASSITAKQLYDASKITSSKRSTSDLHVQLLEKYRNGKVKHASQIKELGLSSKDTKRTLLGNSLDVQKDASGVKHLQEQSSKEIKNPISQPILPNKKDEISPAKPSAIDSSIKDVTKSHPATNANFTADFESSIEESYSTENKSPVILSSSKVPSSQWSRLWHYGGLATSLSVGAIGEKMKRMWGISKDDGALLLNERNVEILVNKLTQMRGAALKMGQMLSFQDSKLIDPRVSQILERVRDGAHSMPEKQLEQVMVKNLGKNWMTHYSEFDRKPMAAASIGQVHRARLASNHMEVVVKVQYPGVMSSIDSDLNNLAYLLKASRILPKGLFLENSLAAARKELKWECDYEREAAFAERFGSLLKNDSDFKVPMVFREASGPSVITLEYLHGIALGKQKYSQATRNHIGYLLTKQCLREISEYHFMQTDPNWSNFLYNGKTKKIELLDFGASIEYDEKFIKKYCRLLLAAAHRNREKCKKLSVELGYLNNHESAQMIDAHINSIFTLAEPFAFDAPDVYDFGDQTITARVKQQIPVMLDLRLQPPPEETYSLHRRLSGHFLLCAKLGAKVRCKELFSGMLKHYAD Q92342 YDI4_SCHPO BINDING 66; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255"; BINDING 68; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255"; BINDING 230; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255"; BINDING 319; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255" SPAC1F8.04c; CHAIN 1..463; /note="Uncharacterized protein C1F8.04c"; /id="PRO_0000122307" MLYTHANIITVNPTRDILIDGAILVKDGSNTIDDIGKTDRLVSIYPNEKHKSLEGHIVMPGLISLHVHLAQSLLRSAADDLPLISWLCDTVWKMQGNFTQEDGYVASQLTIAEMLKSGTTTFVEALFAQRYGIEGAVKAVIESGIRGCIGKVVMDQPRYATQTGVSMHEGLIENSNSLNQAVESHSKFHGKGNGRVEIWFGARTPGGVSEELYRKMVKIARANNIGITMHCAEVKADREFFASKEHTPMTYCKDLGLLGPKTVLAHMVHLDTQDLEILEKHGNGTSVAHCPVSNSKLGSGIAPLKEMLEKSIIVGIGCDGCPCNNTMDLLQEMKMASLLPKALHGDPSIVPAEKIVEMATINGAKALGRDDLGSLEVGKKADFISLDLSNKLYAQPLRDLVSAVVYIATGADVATVVIDGKLIVEDHVLLTIDEPKLIDKAKKHGKKLQERAKVDVKGRWKEI Q92359 YDHE_SCHPO SPAC6G9.14; CHAIN 1..681; /note="Pumilio domain-containing protein C6G9.14"; /id="PRO_0000075938" MTEQSSKSHPSFMSTEYSLPVFSSQYSDIENKDVLKSNSWDPYAANAPIALSEIPSSSKSGKTNGSKAAVESGLASGAFGNRTGNMNRNTSMSGYTFGSSNFVPYNLLSNTPSFTTSHSSSTTFVPPATMGGGLNNLSSPSSSLYLPGSASYQRSNSKNSSASILQMNTTLDDIPILLRRPGLSSYTPGPSTSRRSISSSSNLGGNPGLIANNPSASKNFAFTSGSSSTNNSTTSSSSMANGLQSISKHSAAFPLLSNATSFFGENLTPSLAASTASTGSTDSSGSNIANTLIAPTPTISPPSANTVGNPSPADTPGFNVPSLISDDPSVSSSLSSSVASLSLQNSNILSFCKDQHGCRYLQRLLEKKNQSHIDAVFAETHPYLAVLMVDAFGNYLCQKLFEHASEAQRSTFIQIIAPKLVPISFNMHGTRALQKIIDLVSSPDQISCIVNALRPNVVLLTKDLNGNHVIQKCLNKFSQEDCQFIFDAICEDPLDVSTHRHGCCVVQRCFDHASPAQIEQLVEHIVPHALTLVQDAFGNYVLQYVLELNNPNHTEAIISYFLYKVRALSTQKFSSNVMEKCIFFAPAAIKEKLISELMDEKHLPKLLRDSFANYVIQTALDNASVKQRAELVERIKPLIPSIKNTPCGRRILSKLERRHPSSKEKPIVYSNSERVNTSSSA Q92360 YDHF_SCHPO SPAC6G9.15c; CHAIN 1..498; /note="Uncharacterized protein C6G9.15c"; /id="PRO_0000116630" MSNDSSDNQIRRRHHPVLPKGSFQKKDDSIVLEQELSTPKQVNQARPKFPSPITPTLPEMHLPVGNSKFQAVLPSLISPTLPPGFGMASDDSEASLAENDLHPLDNDSTRTSKTLKNSSEVLTASKLTDEGNSKPLLEEGEVAVSSPILLDSKDVIMGVTKSSKNLVEDAHKSKKASTNSSINNMVSTVNSENSNVNNGSSLNGNTSSNLKRKANVTLGDYKRLKVKNKNPSSQELITADVDKTSGSLSEKSEVNHASLKKTYMRLLNSGKMQKKECDKKGKFFEAYAVDAVLCYTVAFHLQNLSNLSRNHPATTSNWRTLPAYIQFLIKEEDKLDPCIQGLFFLLLGIAFREIFHIEVMRIRHSQLNLMRDIKESSSGLTSAKSLGDAQNLCENAVRLYSSYKHYITSMKKGSSLLTIEYISSTAPNTFNEFFVQKKANIPLPLDIDAPIGVTIRFSHNLLNEWIKKQGDVFESKLLKEDIENLQSLEESYPIAQYL Q96VG1 YBAI_SCHPO SPBC119.18; CHAIN 1..69; /note="Uncharacterized protein C119.18"; /id="PRO_0000220525" DISULFID 9..48; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"; DISULFID 19..38; /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" MSSSVSEECTPAKKKYDACFNDWYANKFLKGDLHNRDCDELFAEYKSCLLKALKTKKIDPLLEAARKED Q96VG2 OST4_SCHPO SPAC7D4.15c; CHAIN 1..32; /note="Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase 4 kDa subunit"; /id="PRO_0000058097" MTDVQLQNIVTTFGISMMLLIILYHYLSRPQA Q96WV4 YHU5_SCHPO SPBPJ4664.05; CHAIN 1..223; /note="UPF0641 membrane protein PJ4664.05"; /id="PRO_0000350751" MSSAISRSRFNSFILHTVATANLIWAFNWINHNSDVAIRRSYGSHFQHLTVLSLAVTLLSMVVGLFSDISGSLTLVKLKNILLYIVCPLETIVSILYWSIVSYDRSLLIPKDRPVPLPLNFDISVHLMPTVYTLIDYLFFSPPFSLSIGPSLLVYLSIAVSYMLWVEKCYQMNKFYAYPILAILDPIKKTIFYTVASIISFSCYIVLKMVHPYALPSGAPPRS Q96WW3 YNH5_SCHPO SPBC32H8.05; HELIX 89..100; /evidence="ECO:0007829|PDB:8ETC"; HELIX 105..116; /evidence="ECO:0007829|PDB:8ETC" TURN 102..104; /evidence="ECO:0007829|PDB:8ETC" CHAIN 1..117; /note="UPF0642 protein C32H8.05"; /id="PRO_0000350752" MAKSARSKSIRRNKKVLRENVFQPVIDERTKRLSAHLRDQVNDLTKSSSSKEEGIADNSLKEVSSSEVSDNVGMEVDQPKVSTSGPRDNNRNKWAKKHLKKGKRAKNSNFSKFLKKK Q96WW5 COG8_SCHPO SPBC11B10.03; CHAIN 1..378; /note="Conserved oligomeric Golgi complex subunit 8"; /id="PRO_0000356246" MDSIGDNVTEMDAFVRDLTMKPYAELEKRKAELHAQKLKLVQKRQQLLRDNYNVLVDYARNQDAFYQLLENSRHDFKELVLHTNQLYEPVKRSQNFLTSISEHYRDAKLMHQVQPQLSSILELPELMNACIERNYFSETLEFQALAYRLKDRFGTNSIIQELITQVETLVVKLTEKLILQLQKPLKLYSLIKVVTYLRVTAKLSEAQLKYVFLYFSWKQLQTSLRNLVPLLDYNNPELYLRRYIQVIRDRAFSLLFQYQSVFGESSNDRLNAAGTVDIPNSTSTSASPFEMDPEGFNNFGQNILSSFVRKLQLEICYVLQKFMPNVKDSTSKFSLLLQLYYCNQSLTKVGTDISIPLSKILGSEWLEMIHSQSSEKQA Q9C0U3 MU153_SCHPO SPACUNK4.19; CHAIN 1..109; /note="Meiotically up-regulated gene 153 protein"; /id="PRO_0000116715" MGSPSLTKTINASLSLHSITQPITLLKTMHYVLQLTILPSAMQHYATLRNFTHPACSVNKQAEQGKEQQQYAMKSQFQFRSGICSKVRSDELGFKGNSLQLNDLPKNPY Q9C0V0 YQD2_SCHPO SPCPB1C11.02; CHAIN 1..505; /note="Probable amino-acid permease PB1C11.02"; /id="PRO_0000054180" MDASVSLLPEGESLHRSLSASQIQMLAFGGIIGTGLFLGIGSSLAESGPASLLISFSVLGVSVYCTMLALGEMSVYMPVAGSFCTYVGRYVDEALSFSLTWNYWLNDTIALASHVLATRLVVDFWLIPTEGDPVSASLSLPPWKEAVRIITPITSLSANIILNMLPVGGFGEIEYWLSSIKVFTVAAFIVNGILCNLGVNNEKKFIGFRYWKDPGAFNNGIIGVISSFVNAAFAYAGTESIALTAGEAKSPITTLPKAIRFTAHRVLLLYIISVLVVGINLPYNTPGLDGDSVRMSPFTFVFKKFGVPGAASIMNLVILSSALSAGNHSLYAGTRLLYSLAKSGHAPKVFSKCNKHGIPWLSVLATSATAILCLMSSQAGKTWGFLLNVIAVSNQISWIFIAVSSLRFRKALRVQGKTHRLYFPNWTYPVGPYIIILLNGVFLFLQGYKSLYPFRLSLFVSYYMEIPIVLGLYLIWKIYKKTKLVSSSEADLETDWKSLEDTDSA Q9C0V5 YOM1_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPBPB7E8.01; CHAIN 23..569; /note="Uncharacterized protein PB7E8.01"; /id="PRO_0000304044" MSLLVKAALILKCASMLQGVSAQYFCRDTTFDKRTLESVRFESECIPTVNKRDLDPNAEGVYKRSFDGNMNPSDFQLLPLAPRDGAIVNVDKESFSKRSTTNMFDFNFSCYFGSDGHSNDTLCQQYIDVADSVGEQFSRVLNLNTPIVIDVTVVGACTGESVCSQGQGMVAGSIGGEASPSREIPMACSDGLTRYYPQAVVKQLGLSDPPSYADSDITIALNADANFYFGSGDMGYEAVDLAYVLFHEITHGLGFSTGWGVFGYENLTDPYMNALLPTVSYVIGEMNGETMYAFHDVIENAFDRNIFYSIDPNEGLPTIAEFFHSVGAAFTLKADSIAGVVAQMNDTTTQFHIQANEAYRKAINPGRLVIYPDAGIDTYSPFIYLDSSYVPFSSGSSLSHVALHHYDCEPNFLMRAFYTAGATLESYIECAYGSDQADVAYGPIGPAMRTVFRRMGYSVNNLTGVTNEYSESLAKRSLSEKPKTAPTGKQLALHPLRRETSILDSTNTTSTNATNTTTTTSSSSTASSSASASSSTSATSGAAGDLFSVSKNLMMTLTAGLCLITASLF Q9C0V7 YHJ2_SCHPO BINDING 327; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250"; BINDING 328; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000250" COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; SPBPB10D8.02c; CHAIN 1..554; /note="Uncharacterized sulfatase PB10D8.02c"; /id="PRO_0000316607" MAFNKQAESKKPNFLVIVADDLGWSDVSPFGSEIHTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHIAGLGQMAETVRRFSKVWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFALLPGGGNHFAYEPGTRENPAVPFLPPLYTHNHDPVDHKSLKNFYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGRYSEGPDVLRKNRLQAQKDLGLIPENVIPAPVDGMGTKSWDELTTEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNGAEGSVLEAIPVLSTKPPVKYFDNSLENLGNYNSFIWYGPRWAQAATAPSRLSKGFITEGGIRCPAIIRYPPLIKPDIISDEFVTVMDILPTILELAEVPHPGHKFQGRDVVIPRGKPWIDHFVHGKPVHKDTDFSGWELFGQRAIRKGNYKAIYVPKEGIKTEWELYDLSQDKGELENLAKVHPDILNELIEYWLVYEAETGVVTAPDDFVAENVGLFKPAKHNL Q9C0V8 YHJ1_SCHPO SPBPB10D8.01; CHAIN 1..552; /note="Uncharacterized transporter PB10D8.01"; /id="PRO_0000121376" MPQPSYADQINVEDSSDYEKDPKEYVDKEKGYFPHVITSHISKSSSQSHPDVSNAVLDETFSFMQEAKDLEPLTPKQDKRLRWKLYFTVLVMLMILDMMLYIDKATLSYSSILGLFEDTHINSNQYNDINTLFYVGFVIGQIPGHMLLQRFPVSKFVAASTALWTIIIFLHCAAYNFSGLMALRFFLGLVESSLLPTMEATIGMFFPHSEQALLQPFFYISCYGCNIPAGFIAYGVQYAKNTISPWKLFMIIVGGITFFLTIGLFFYYPDNTSTARFLTKKERLYTVDRVRRSNHSGIESKTFKKYQVIEALKDPVTWLFTFHVFCNQLSNNLAYQQNLLFTSLNVSDLNSTLVGVASAGYNCVSAIIATYMMSVIKNQSAFHGAIWYIPSIAGGIACVAMSWDHKIGELAAIIIASNFGIPFIISLGWTTASCAGYTKKLTRGVMFMIGYAIANIIGPQMWQSRDAPRYYPAWIVQIVIAWSVSPFVLLIIRWILVRRNKKRLALLEQNKEQYEKTWIETIDSSGNHVSGFYENSMLDLTDQENLSFIYPL Q9C0V9 YNH1_SCHPO SPBC32H8.01c; CHAIN 1..187; /note="UPF0589 protein C32H8.01c"; /id="PRO_0000339160" MLKKMPMSNKFENFYTLRQVSEVDKKPCFICYKPTKWVLITKTKLDFFYVCYNHLQDRGFATPISVIKSVTNKIDTNKLEAKDESKNVEKDATGNPQESKQEPNLEVQQTEKEKDVDSASAENESINSSSSSSKECSTQTQSKHYNLHRDIFQMRIRYHANRAAAEKTARLLQSGQGLPSPPSKPLP Q9C0W3 YHI4_SCHPO SPBP22H7.04; CHAIN 1..255; /note="Uncharacterized membrane protein P22H7.04"; /id="PRO_0000304031" MSMLIFNIRVARHKALLSRIVSTNMFNPMFRSLRPIQKSFSEISILRVFNKPPIKKFHNSNILKDITSKRNATPAKIAWQAMTTREPFLVYQAKADKKISLIYLLTVGMLINVCVITSFASVDIYRAKDEIFANWVDMDYYEKLSYIGSAFITPALYFTLTLILFLPRRNIYSISTLPSQRFEIVTGFLSPFNKLYFSKSLIVPRKDVSIVTYSLQKNPITLKIRDRPFYYLLNANGKYAGNSKDVLFCVIGNRY Q9C0X2 YB7J_SCHPO SPBC16E9.19; CHAIN 1..143; /note="Uncharacterized protein C16E9.19"; /id="PRO_0000116507" MFPKIKQTSKNYNGKEIQAISMRFSNQITILVTISGKIGQMYMMTYEKSVMSPVSITGDMSTLPEIGVRTLLGGGGEDDIKSHWAQITAGQVGSLLARQQMLVRPDVRIPRVCLGLHVPWTDDNEKNGDLTVVILELVKEICF Q9C0X9 NPC2_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPAPB8E5.04c; PROPEP 20..40; /evidence="ECO:0000250"; /id="PRO_0000019891" CHAIN 41..188; /note="Phosphatidylglycerol/phosphatidylinositol transfer protein"; /id="PRO_0000019892" MRLTTFIYAITCLPIFISASSWFSSFSFGESKSTDLVSSTSEKIPGANPASYCADWDRGDDHVVVDYINLIPNPPAAGKNLTIETEINVGTTVLNGSYVDIQVKYGFVRIVNERLDICDKAYELAAVECPVEPGIITKQATISLPWAIPPGRYHVLATAYNADGEQLTCVSASVSFSHFGFQLINQDH Q9C0Y2 YKL1_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAPB2C8.01; CHAIN 22..1220; /note="Putative cell agglutination protein SPAPB2C8.01"; /id="PRO_0000353809" CARBOHYD 44; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 72; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 131; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 160; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 232; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 304; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 376; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 448; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 520; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"; CARBOHYD 592; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" MAVSRLLILICLYSFVTFAYPKVTQDYRNHLPIKFAKRSEVTPNTSLAQCPKYVTVYSSGSSHYISTIYPVNKTHHTEYTTLTDGSIDTYTITAKTDTGTDVVVVETSANTITTTLYSGSLEFTTTLDSANGTTPATIEVVEPAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVVDTAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVVDTAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVVDTAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVVDTAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVVDTAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVVDTAAGTVTTTIYSGTTPFNTTLASATDTVPGTVEVVEPEAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVIEPAAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVIEPAAGTVTSTVYSGTQEYTTTLATASGTVSGTVEVIEPAAGTVTTTVYSGTQEYTTTLATASGTVSGTVEVIEPAAGTVTTTVYSGSEVYTTTLASASESVPGTVEVVDPEAGSVTTTIYSGSVEYTTVLADASGSVTGTVEVVEPAAGTVTTTVYSGSEVYTTTLASASESVPGTVEVVDPEAGSVTTTIYSGSVEYTTVLADASGSVTGTVEVVEPAAGTVTGTLTSGSQFFTTTIAQASGSVSGNVEVIEPSGSTVTSTIYSGSESFTTTLAVGSGTIPGTVEVILPAPTTIYTGTVATTITYSSSSTPVSTVVVIPTAVCSGVRGLQYAVYNYDISASKSKFCVSSGNTDVAAFTQPAYFGSSSLDQSSPLFTGVLSSTAALPEWTSSYYLPDYPPDATAMESTRCNCKAIVYQFFFRVPYTDTYELNVYNVDDVFYGWFGDKAISGWSNTNYDAYAYWHVTTGQTGMGSFSMGTLTQGSFLPIRLIVANGGGKGGFNFDFSSSTDTYAATSYAYTATCTQSFLPFGLGNGGIDN Q9C0Y6 YKM8_SCHPO SPAPB24D3.08c; CHAIN 1..349; /note="Zinc-type alcohol dehydrogenase-like protein PB24D3.08c"; /id="PRO_0000339118" MVSNNAVIIKKYLDSTAGYPVIGEHLAFEKREFDLENAQVDEETPVLLKNIYTSVDPYLRMRMQSPKHASYIPPLELGKPFYNSTVAKVVKSTLDQYKPGMDVVFVSGWEEYTFVSKQALGFLQPINNPYKLPLIDFVGSLGMPSQTAYCGLKHIGKPKAGETIYISAASGAVGQMAGQLAKAMGLHVVGSVGSDEKFKICLDSGYDSVFNYKKESPFKALPRLCPKGIDIYFENVGGETMDAVLENMNLQGRIIFCGAISQYNNPNPYRVKNLGMVLVKSLTIQGFIVANILPQYQEQYFEEMPKLIAEGKIKYKCDVYDGLESAPEAFIGMLQGKNSGKTIVKIADE Q9C0Y8 YKM6_SCHPO SPAPB24D3.06c; CHAIN 1..316; /note="UPF0613 protein PB24D3.06c"; /id="PRO_0000343142" MSASHPGILHEYTERLVAFELVGKSNVTLTSNVTRSLLLFVGGLGDGLLTVPYVQELVNPLDEIGWSIVQVQTQSSYIGWGTGSLKRDDEDLHKAVDYFLHIGGADFSTRKIVLMGHSTGSQNVLYYLTQSILPNYLIAGIAQAPVSDREAAYQFNGKEKTKELVDWVKAEYLDKGLGNDVLPRSKVENFFGEVPTSANRCIDLTDVRGNDDFFSSDLSADDFAKTFGNLKEISGSTAHSQLILLMSERDEFVSPSTDKAQLLNRFRESIRPTTSNSSLSGIIPGATHNVGPKSSPEALKWLINQLITALRSFIDQ Q9C0Y9 SPEB3_SCHPO BINDING 198; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 222; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 222; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 224; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 226; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 319; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 319; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"; BINDING 321; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" CATALYTIC ACTIVITY: Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145, ChEBI:CHEBI:326268; EC=3.5.3.11; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; SIGNAL 1..21; /evidence="ECO:0000255" SPAPB24D3.03; CHAIN 22..408; /note="Putative agmatinase 3"; /id="PRO_0000311760" MKSVEWFTWGVFLLLSGFGEAGRMGLGFQEKNPVFVKEKQSPFYAVPSNYEEVEFSSIVEPMYSGIATFGRLENVECLSKRSEDFDIAFIGMPFDTGTSYRPGARFGPSSLREGSRRINTKYGAVNVPLEINPFKSWAKLVDCGDIPVTTYDILKAMDQLESAYFQLIARKPSSFTDHDGFAKNDTVLPRVLSLGGDHTIVLPILRALHRVYGQPISVIHFDSHLDTWAPGLIGDGDEADGINHGSYFYFASQEGIMSKDANIHAGIRTPISSFSDYDDDVDCGFKIIEAREIDDLGIDGIVKKIRDRVGDNLVYLSIDIDVLDPAFAPATGTPETGGWSSREMRAILRGLQGLKFVGADLVEVAPAYDVAEITSLAGAQLLFDIVSMMVKYPLVKEADLSRYMPIHK Q9C0Z0 YKM2_SCHPO SPAPB24D3.02c; CHAIN 1..543; /note="Uncharacterized amino-acid permease PB24D3.02c"; /id="PRO_0000310829" CARBOHYD 275; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 406; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 519; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MDETIGMKKEFHDISVGDIEVGESAPVTEDDKMLLNLGYKQEFKREFSLLAVFGQSFGSMGLCPSLVGSMAFSMNCGAGGMVWSWFVGATCLLPIAFALSELASSMPTSGSLYFWTAYLSPPKYRAFLSWFLGYVLALAYSTGFASTIYAAAGLVQATASVANPSYAPTKYEEYGIYVALSFACSALIVLPTKFLARFSSFNVVFQICTILIFIISLAASSTSETRNTGSYIFGNFENYSGWTNMGWSFILCFTTPVWVLSGFESCATIVEEAKNASKAAPIAIISSLTVSLFMGFCIMITIAGTMGHDFSSILNTPYGEPVSQVLYNNLGKRGAVGVSAVLIIALCFNCSALCLASSREIFAFARDKGLPGSWIFRKLTPGGIPLNAILLVNLYTIIVGLLMLVNVTAISSIFNLAIIAFFISYSLPLVCRLLFNRLNPGKFYCGKFSKPISIVAVAWLWFMALMLLFPSYQNPNKVEMNWAIVVLGFTVFFCVGYYYLPKYGGKTFFKGPVKTVDENVTEGVTVDFQADHVSKEDDGKSYN Q9C0Z3 SLX9_SCHPO SPAPB21F2.03; CHAIN 1..172; /note="Ribosome biogenesis protein slx9"; /id="PRO_0000350771" MPKAKKRVSLASKASSRLPSSGKPSQQASIPNVELSSTVTSNSQVLNNDPLKETKKDKRKDRHFNWQQKFSNPKISASARKRRNRKARENLKVNVSSIGEVLPEIDLDISVANSRLKPVIKDSLSSKQTKSSMKRNTVEEIERFQAILKHPSFVSNPLETVREHLGNSLDSR Q9C0Z8 YKTB_SCHPO SPAPB1E7.11c; CHAIN 1..319; /note="Uncharacterized protein PB1E7.11c"; /id="PRO_0000304018" MTAVPKFYRAALSDKYKRIVLDAMSRGYRPSEGIWFRVRTYFPVSYPADIKSEALPSRYFQLKAFPYYNAEERLKEWIVLAKVRPEIPLPPAAPIPMKKASNTEPVEKEISSFFSEEGATKENEDFINEKEEEEDLSFSINAAHTFSNIGTWYLARANEVAEFKHQQKKIVAINKGRFPKSLLLQYVPSNISSERLFKTLKRHGLVQGVMEMNTKPLKTSKTTPTKKMLSTTDTKDWLVITPVPNKLTRLLHKSQWDLIEKLSFPLRLSDYKKITKKENIGLSSRDEMGDPLLFAHSYFELTPENKTSAPKINVKSEGK Q9C101 YKT8_SCHPO MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB1E7.08c; CHAIN 1..554; /note="Uncharacterized MFS-type transporter PB1E7.08c"; /id="PRO_0000372717" MSSSIPPRLYDMSPTESKKQEDVSETELVYPVELADATIQPSKSDDDLFDSNDFSKTYLAKSRILSNAMNEIGFGRYQWYLFFVAGFGWMSDNIWPVCTSLILMRLDEVDGPHPPAEGRAPYLTLSQNLGLLVGAMVWSLSADTIGRRWAFNLTFLFTGVFAVIAGASPNFASICVFDALWSFGVGGNLPVDSAIFLEALPSSHQWLLTVMSFWWAIGQVIANLVSWGLISNFSCPDDESVCHRADNKGWRYFLFTMGGMTLLMFAARFLVSVYESPKFYLAKGDDYKAVETIHKIARINGKTCTLTVEELYAIDRQEQEESDLDDSKSSDAKSVTQGTTNLIVEKLRKYNFEHIRQCFGSRKLAISSILVILSWAVIGLAFPLYNAFLPYYLETRGNANEPLSVAKTYRNSLIVSAIGVPGSLIAGVLVEFRIGRKGTLCLSLILTGVFLFASTTAKTSNAYLGWNCTFSFFSDIMYGVLYAYTPEVFPSKVRGTAVGLAASANRILGIFSPVIAMRANLTTSAPIFVSGALFIFAGILVVFFPYEPRGKSSF Q9C108 YKT1_SCHPO MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 127; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB1E7.01c; CHAIN 1..163; /note="Uncharacterized protein PB1E7.01c"; /id="PRO_0000373870" MEQKVSADVLLNKYQTSISITKNLINSWLGNENTSVSSDEKNDDPPLQARPPRLGLGASRKDQSENSWVTSKNEKLKSLPPALKKKIERQLQKKKEAEKIEGGKNHDNLKRKLNKVGDELNEQQSDTDDDDDDSKARITSRSKRANAQSSGFDIYKKLGKKKR Q9C110 MU177_SCHPO SPAC630.15; CHAIN 1..105; /note="Meiotically up-regulated gene 177 protein"; /id="PRO_0000116828" MYPKIVARCMIVITKNRESERNVLICYRNVTNVYFSLRILLNRQNEGNNCKYKLVFSLYRVSFRRMRLNDRQLSCVESVTNGIGLLCLKQADQVCLFTPTVDSHL Q9C112 YAVA_SCHPO SIGNAL 1..27; /evidence="ECO:0000255" SPAC27F1.10; CHAIN 28..101; /note="Uncharacterized membrane protein C27F1.10"; /id="PRO_0000303926" MQLTGSIYPWFTAYALLKSTLMELINSFIPYKSQTGKAPKCLVPYWLSIRLSLLYFKLTEAISFTEKCEKYNISLFDSTFVFGYIVNCFFIIHLNTFLTSQ Q9C117 YDRC_SCHPO SPAC16E8.12c; CHAIN 1..211; /note="Uncharacterized protein C16E8.12c"; /id="PRO_0000304005" MAKPKKENDLDLLIQLADALEAIPGDLSKNFTEVRFLEAELKDVYSQALSSIDDLLNRDTSVERRNLVARNLSLLLKSDDVQTRKKSHIAMYAEAITHSNVLRLEHCYQKMEMKLPNFFIPFTPEVIKEQKTSRPIRASRRRANLRNRRAKELLAAENASEEGDKKQIITDSGKLPETEELTETTNEDLDIKQFSPYSSESSANVSSYNKS Q9C1W4 PMP3_SCHPO SPBC713.11c; CHAIN 1..57; /note="Plasma membrane proteolipid 3"; /id="PRO_0000247914" MALTGSDIFKVIFAIILPPLGVFLERGCGADVIINILLCCLGYVPGIIHALYIILKY Q9C1W6 YN59_SCHPO SPBC713.09; CHAIN 1..395; /note="Uncharacterized protein C713.09"; /id="PRO_0000304009" MSDREEKLAAAKQRLLEVKKKKRQAKSKNSVAEDNVDRESNDGNNQVNEPTGNDNTQVVENTEDISASNVVSAEGAEASTGDASTQSPETSENVVKNSVDESVAEKPEKEDLAVIESEDKAAKPDGEIKKNVETEVTSRSTSSQEKDELEKQVKTLHDLNEQKDKKIKELKERINDLTYDYETLKANADDSEGKQTLVSKREAALEEFQSKLLIRENEINKRELKMNGKEDDLKKREKDLENRLLKVEEHEKSLNERATKLSEANENFNNRFKEFEEREKSAIKQNKEQSSEGSKTANQTHEQKELINSLEKKVSDIALEKQLLEEAVERYKLAMVEFAECQRRLKELEAMHFEQPGSVTEKLFPDPTNFEVIDNVSIDLTLTGFPGAHGIPFSV Q9C1X4 YKW3_SCHPO SPAP32A8.03c; CHAIN 1..513; /note="Uncharacterized RING finger protein P32A8.03c"; /id="PRO_0000310487" MESQPVIWYCHSCSNEFQRPGNCPRCNSDFVEMVEPNTAPEDDPRAANFVNATEFNDPNAMLQNILQSLGQGVVPNVNPTDANRTANPNTNSNPNPNATNAQPNPTMFSTGQFSTEQGLPNVFFGAAAAQPGSGTPFVMPGIVNAAQIRNFFQNIMGGNAPQPEANSEQARNANTETSNPPFASAQTQGQEHRPSSPNPAEHMTGAYVNTPLNQPPSYAASTQPEFQQTTSPIFSSSSTPPPPPPRPSQPTSGESQNTNPRFPFSAQSFVFSVGPNGALHQVNTSTENPQNAQAGAIPITDLGSILERIFGSLNQPGAQQGEGEPFNPANMFSNIFNLSGNPGDYAWGARGLDDIISQLMEQAQGHNAPAPAPEDVIAKMKVQKPPKELIDEEGECTICMEMFKINDDVIQLPCKHYFHENCIKPWLRVNGTCAICRAPVDPNSQQRNNTSTDSANGHNPSNHANPSTSTTNDQGATLRNESFNAASQSNLSSEHGHSSRTPMDDFVDEEPLE Q9HDU0 YHEH_SCHPO SPBPB2B2.17c; CHAIN 1..146; /note="UPF0742 protein PB2B2.17c"; /id="PRO_0000373864" MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSVSSKFRSFTFGCVVVYHNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR Q9HDU4 YHEB_SCHPO SPBPB2B2.11; CHAIN 1..365; /note="Uncharacterized protein PB2B2.11"; /id="PRO_0000318144" MTGDYKEYKGYALITGGAGFIGSNFLDYAVDKYPDFHFTCIDKLSYVSNYTTVFLSKVLNQPNFRFLEMDLATNYKFLYQFMVEDSEINKITHIINFAAESSVDRSFIDPLYFTKNNILSTQNLLECVRILLGKKEELRNRLNFVHVSTDEVYGEQDENASVDEKSKLNPTSPYAASKAAVDLIIQSYRYSYKISVTVIRANNVYGPRQYEEKLIPMTLGKLKKFINQKSQKIMQDKITLHGDGLHKRKYLHIYDFINAIDLVWMKQGSEVYHSTLESKMSGQIFNIGSDDEIDNLSLVKFICDYFLYRKLSLKNLDYSKYITFVQDRNYNDSRYSLNYEKIKSLGWRPQIPLETGLRKLIDEYY Q9HDU7 YHE8_SCHPO SPBPB2B2.08; CHAIN 1..220; /note="UPF0643 protein PB2B2.08"; /id="PRO_0000350753" MIVQHKTAKIEEDHGLFQPILRPSDISKTTDTKFIQSSPYIEKEHWLDLGTLSVGHYFLSLALQTFVPKDSVRYAHLPYAQAFDIAEIVNLIREYSHKYHKHIPAFSAYIVAFRSVLQPEVQVSPEARHKLAEIDKGSHLEANVSGGLLKYWYGIPDDVFGQNLATCWWTSKESARLGGAGKIHREGLKAVRGWYKNWKIEEYELEVIEGGSSYIFKGLS Q9HDU8 YHE7_SCHPO SPBPB2B2.07c; CHAIN 1..250; /note="UPF0494 membrane protein PB2B2.07c"; /id="PRO_0000306277" MSNPESAKKQVDPPGYNELFMVRDTRNVDLERGLELCKPEKVNKQNLFTNIIKPQKDKINIKTDKIKFFLNNLFTEFSKFHDSCYPDGRISTRSKLRWPLLIIWCILIVFAIDKNFEVKDFLSIWINESFINENRFYSEIWGPIAIYICLFILLLLGLICMFPLHLCRVCVLALRETGMIIAVLGAALGMIIAALGATITGLLYFSHWALYKVVILALDLKIEPFKDEIAFLTLPTHNGETLSIRDNNQS Q9HDU9 YHE6_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPBPB2B2.06c; CHAIN 25..601; /note="Uncharacterized protein PB2B2.06c"; /id="PRO_0000310848" MKTASIHFWSTLVLLFSCIGSVIAYSSTDLTTMYDWNQIIKPLEWGQMNFIHTTDTHGWLNGHLRDARYKADFGEFKSFVLRMKELADFKDVDLLLVDTGDLHDGNGLSDASDPEGIYTNNIFTYLPYDILTIGNHELYQASVSNNTHEYFVPHWNGTYLASNVQIFNSSNELEQFAAESAYFTTKHGVRVLAVGFLYDFTGNANNTVVTPVETAVNSRWYQQQINRTDVDLFLLLGHIPVRDWDEWKSLHASIRKVHPDTPIQIFGGHSHIRDFAVYDESSVSLEGGRYCETVGWLSIDGLAASNATRQYVGRPVTNETRQSYPNLPIPNTPLYYTRRYIDFNRQNFRFHTQQSEDSFDTPEGIELSKIIKQYRDDLNLSYVFGCVPKNYYMTEVSPQSDDSIFKLMTDRVLPEIITNRNRSTVPRIIISNGGGIRGSMYQGKFGPDEMFQLNPFLTNYYMYLADVPYKYAKKLYSTLNGGSNLRNINENLAALNPGYVTSDDFGEDGDDTVHTSVPSYATPNILQAQAGFNATSSPETIDVVFLNFLQSIVLKALNNMANDTLYTSSNVTQYWVRDDGYDSSPYSFAYFVQQEWSDNCD Q9HDV0 YHE5_SCHPO ACT_SITE 100; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 200; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"; ACT_SITE 202; /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" SPBPB2B2.05; CHAIN 1..253; /note="Putative glutamine amidotransferase PB2B2.05"; /id="PRO_0000363384" MECPIIALSVGFSNNSQPYVEAIIKAGGCPIVIYPGLQRNSIPPNIDGIILAGGESVHPNRYGEDFDPNAPKSVDVIRDSTEWGMIDFALKKKIPILGICRGCQVLNVYFGGSLYQNVSSCGFRDIHRPSKPRHYLAHKVMAKPGKLKNILGSNVIDVNSIHDQGIKTLGMGLQSTVISDDGLCEGIESKDGLIIGVQWHPEAIIDKQPHSLKLFQYFINRSKWHMKQSNIFSNVPHESSFYRNSIISIPIAP Q9HDV2 YHE1_SCHPO SPBPB2B2.01; CHAIN 1..585; /note="Uncharacterized amino-acid permease PB2B2.01"; /id="PRO_0000310827" MNAYVRDSESVYSESYPPENFISNEPEKSKDKDNFNGEEVISYVGEVETVPAKEENVFRRFINGFKIEKNQQDSAGQGLKRRLKSRHIQMIGIGGAIGTGVWVGSSKSLYRGGAASVLIDYCIVGTMVFCTVYALGELAVAFPTRGSFVTHATRFIDESWGFALSWNYVFSFIVTIPLELTTGTMMIKYWTNLNSGIWVTVFIVFLFFINIFGVKGYGEMEFIMSTIKVVAMCGFIILGIIIDCGGVPTDHRGYMGTHIFRENAFRHKFKGFCAVFTSAAFSFSGTEYVGVAAAETENPAKAFPVAVRQTLFRIAIFYILSLFIVSLLISGADPRLTSYHGVDASPFVLAIKDANIKALPSILNAIILISVISSANAQLYAGSRAIHSLGCNGFAPKCFTLVDREGRPLVALLILFLFMFLGYLVETGQYDTVFDWMLSISGLGTLFCWGSICLAHIRYRAAMKHQNRSLKEVGFVSPFNVYASYYAFILVCLVLAAEFYVSIFPVGGKPDASAFFENYLSAPVILVFFICHKLYYKTKRITLSNMDLETDFAYKTPVEEEEEEEKSAGSLSIKQRMKKLSDMMC Q9HDV3 YOE7_SCHPO SPBP19A11.07c; CHAIN 1..688; /note="Hid-1 family protein P19A11.07c"; /id="PRO_0000116869" MGSAESKISFRHAILASLNTKPEREIYEFLFTCNLTENDVFSFILAQDIRICRDSNKFDNLAILLQVCVLNIVSIQNKFSEQYPLKKNALLNSFLILTRLLPYLYESTNSSNWVRTYFQKDFSQTVDDLKPLLSELGLNYEIELPNSFSNLTSLLSSTFQLCFQHEFTVSKYASSEESIWSAGIAIPEIAHPPSYDHRLHQSLLSCFLVVLLSNTLYDSIDELDFSVLNSIVSLDAKDIYIRVICSFVNTGFIDSTNWFLNSFNQRRNSLQLYSSWFIILILSDARIKENTHLYANGEGQHIKNHLLELFKKLHRTQDFLIIAESINKFLSNPLKKERQIITFMGDFKRCVVESLCFLFLLLTNQPRFTDELVNFKSSNEMMMNLLFIHVKYSGDTENSYMSSLAGYCLQQLVSHEKLVKAACHIDKSLISPSPSSQFPVFDTSVAIYVIQVLCTLENPSSIEYNIISNILFSIPTIPLKNASPIVELISYVMKPEFFMKSQQNASDCKKLLSSFLYFLINNFNDNLHIIELLQKDKRKFEPIIAWSETEFSEFFVTSNISQSALDNGLVDQAGLDEQKWYEKWFHDLNIPLLRKCLTLRTDKNPFIEQPDEPNVTKKIYRVTYTDALQRWNLVNIWRHIFKETVTLNSGISCPWYGTNVKLFTVREVRQPTILQSRSLGEFQGRLFS Q9HDV5 RM02_SCHPO TRANSIT 1..37; /note="Mitochondrion"; /evidence="ECO:0000255" SPAP19A11.05c; CHAIN 38..153; /note="Large ribosomal subunit protein bL27m"; /id="PRO_0000030501" MINQGLFIRVNNFQLLKASLAYKKASNILTFPPIRTSTKHGGGSSKNTGDSAGRRLGIKRSENQFVRAGEILIRQRGTKFHPGDNTGLGKDHTIYSLVSGYVKFFQMDVSLRKRRKYVGVVFDKETTLPRPKDEPTIRRVNKYITSANSAQVS Q9HDV8 YOE2_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPBP19A11.02c; CHAIN 19..244; /note="Uncharacterized protein P19A11.02c"; /id="PRO_0000304094" MQFSVLCKFLLLVTAVMAQTEYTPGFTTDVATTVTPTPLPSANVTTTSFSSASTETSTHSVTSTNITSIVPPPSTSHNSTTTTVPPTTSMNTTTTVPPTTSLNTTTTTAPPTTHVNSTTTVVPPTTHVNTTTVVPPTTHVNTTTVVPPTTHANTTSFVPTTTESSIHPITTGFYNTTFTTGYFNTSVTSVAVHNSTTVFPTSVPIVNTTSFNVTTIPSSAVHYASPSGLLALVVMLISAFAFLA Q9HDW5 YFW6_SCHPO SPAPB2B4.06; CHAIN 1..256; /note="UPF0644 protein PB2B4.06"; /id="PRO_0000350754" MGIASSLRLFGKAPASYLFNGFRRQMKNPLMKKGVVYAGVSGTCAAAGYMFGNFVMEKHIYQVKYTEEQEKEVLEVENRLQNLKIVKDLRQNPSFRELRMPFNRSNHSLTNNLLSGPGRITVPPVIFYDKSTRQVYAIAHVGKDVGLDDDTIHPGLIATCMDEVLAICSFLSLPNKIAVTANLKLSNPTKAYTNHFYILRSHLEWTKGRKAQTHGTAYMLDNEDPSKSTCVAIADGLFVEPRFAKYLKHVIPVSLP Q9HDX1 YKN4_SCHPO SPAPB1A11.04c; CHAIN 1..697; /note="Uncharacterized transcriptional regulatory protein PB1A11.04c"; /id="PRO_0000310388" MIAAVEKDAVPRKRRVISQVSQACIRCRQKKIKCSGEKPSCQACSNNKVECIWPDRPNMRGKKPSSAARTLSPLTGIVQPYLGSHPFSPTILSPSSPNMDFTYSINSFGDYQKQLRLPTSRKLLQLWDIFLKTSYTELFGIFNKAQITSQIASDTAPPVLVLCICAHAARFSQEEVNRFKSSTAASDYYANQAFSLLPCRFQDISLTNITCLLLLCLIELGSCRGAKAWLLLGMALRMVDSLDLGNEINDNPLTMGSNTVSWTEAEQKRRVYWACFFVERLLSTGYMAPSKLRSLSLSLQKTSIQLPCPEPNFLFNQPILTELFDGSLPENTQSDTTSMAPYQRSLQLEFMTGSLIRLSNLWSEISRWALCGGYTKDITPPWLNQSQFHRSFELLKAWHENLPPRAVWSYTNYSAYSSPGESAGACYTFMHLLYHTTLTYLLRNVLDLFPEKSRQKSKLFSSVSQRFGQQPPTVWMDMILDQVITSADFITKLSKDPLNYIMSPFVGFSILTAATIHMLLKFCVVNIDQNYISSSRLVHVDHQILQDRSKYWKINQAMLVTLQRLYNFYRFQYLEEQSLYNFKIPGFPLCILEYGIVEDQSMKSNPDLNSFSKELFSRGTNELLNNGDDTQSGNSTPAMGVSEIRTDTILDEEVPVDPLITSILDDGRWWEEMFGSERKAGFKETVFEDMNGRSIRL Q9HDX2 YKN3_SCHPO ACT_SITE 301; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" BINDING 54; /ligand="a 2-oxocarboxylate"; /ligand_id="ChEBI:CHEBI:35179"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 136; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 158; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 160; /ligand="a 2-oxocarboxylate"; /ligand_id="ChEBI:CHEBI:35179"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 188; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 197; /ligand="a 2-oxocarboxylate"; /ligand_id="ChEBI:CHEBI:35179"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 277; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 304; /ligand="a 2-oxocarboxylate"; /ligand_id="ChEBI:CHEBI:35179"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 332..336; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"; BINDING 355..356; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|PROSITE-ProRule:PRU00683}; SPAPB1A11.03; CHAIN 1..407; /note="FMN-dependent alpha-hydroxy acid dehydrogenase PB1A11.03"; /id="PRO_0000316582" MFRNYNWFDAKEPISYESEIYAKGLKFQRPQITVDGRHWEQLAVERMTKDAAGYVYGCAGKRETYDKNMESFKKWSIIPNRLIKSGFPDLSTTVFGQKYPFPIALAPVGVQKIFNPEGESGSCAAATREHIPYIISTASATSFEDIEKASGPGERWYQLYWPSNDHQDITISLLNRAKKTGCRVLIVTLDTFILGWRPSDMDNGYDPFLNPDSIGVEHGFSDPVFRKQFKEKHGVEVEENMLEAAKEFAGIVFPGISHDWEDLKFLRKHWDGPIVLKGIMNVPDAKKAVEYGMQGIVVSNHGGRQQDGGVASLTMLPKIVDAVGDKLDVLFDSGVRSGADIAKALALGAKMVLIGRPYVYGLALEGSSGVSHVIRCLLGDLELTLHLSGIVSVKPKDLNRDVLYKEE Q9HDX5 ARV1_SCHPO SPAPB1A10.15; CHAIN 1..266; /note="Protein arv1"; /id="PRO_0000310327" MKCVECGAEVDSLYTYYGRGTSNIRLAQCKNCKQFADKYIELDVVLISMDVILMKPQVYRHLLFNSLSARTFRNVVNFCILISLFNVFLVWSRLEKRAALFPYFTPAQAFLSQPIIRQYLTLLLICLVETTVYQISVVLLLCLTMGWKSWTSASGAVILSSSTRMLPVFMVIWDYDLSIAATVVEWVVLFSNVDALCILTGSRRYFKIGLIVLFASLVRSIVVYIFLHLTGLSQIQPSTPCDGFQHFVNLLCVYFRSITLTAQTAV Q9HDX6 POF15_SCHPO SPAPB1A10.14; CHAIN 1..243; /note="F-box protein pof15"; /id="PRO_0000116823" MSCVTRAPMSVPQTALQPNSYVNFDAQQTSSTLLPVEVIDSVMQYLPAHDVIQSSFASYPLTLIANKIIRARLSFLDEYSLRVFAKDVYTDSPICNLSARRGLYSLQYDGYSVFHLDPNNCSSIFQISFEDDEDLASFERYPGEFLAPHINVRIHVTLSRSSCDRHQADIFSCFQDPIRVRRDWLDSIKPGQPETLWFDQNTQHVIGLIVTRVDAAPGKYDLSVTSVIVQTEYLLSCLEKRVH Q9HDX7 YK1D_SCHPO MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 217; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB1A10.13; CHAIN 1..529; /note="Uncharacterized protein PB1A10.13"; /id="PRO_0000304080" MSSSKIKELREGLMSSSKWSMAPGMMMQQNQPRPATTTPPISRGNEDADEGLNTARSFSSFQDLKGMSGDAKEQESATLVHLTKGRAHPRSRRPPRQISIDSAKKEETKNTGSTKAADTKSSVEATISPLKDTKSPSNASVFPIKPTESKTSTTKDSETAKEEDDASSSTTKAVEATTSKASSAHTDTLATSASNSDRGASTPEMVVKAEKREGSTSPIPYSSLSIAERIKQAQNTPFLESKVLPQNNETSDEENVDVKPAAGTVKNVMQAFLQPATPAKDTASKEPSKSSQQPVRTKPRIAQSPFLAQDAKENGGNVEVSSPLSFSASKSPAAVDSSTKTPTEQVNVVSKQAPTTSSTSVISPDPLQTAAPSANVNEVIASLESKVVTRRTGSGNNYRVGLRNVSGSERTKSLSKESPVEPEKPALPDATSSSTPTTENKESWTNQGIKSSQQRSANASPATSPSNQASIHASFTKESSTHSSPSFTLESLFSGAPRVVELTRFSQPSPACSRALLARWKEEYRTSIH Q9HDY2 YK18_SCHPO SPAPB1A10.08; CHAIN 1..416; /note="Meiotically up-regulated protein PB1A10.08"; /id="PRO_0000371804" MMTRMELRPLEIGFSKALTEVAPVTCQCECWDHNLCSSQASEMDLIYQSQDTHSCASKQDAVFQLLSETKIPVPNRYRKISHRLSTLSNKKTLKSQLDRFLSSSKKLHNDDVNRGDYCFLLSTPVECSASTNSHSYDCLWNFSCNSFPEYSSYSASETSSVASYSYYSGPNPATPSSSSCNLVNANSLDIYLNINNLKKSKSVPRLRGQFMEPVEHNHPLSKSLEEQSSFLEQSKDASSNLTACNRSGSSLSSNFYSSRLSKKTSLASLNKSRASLQHKIMSLSRNIIRRVFHKPEVHLDPSASILNLSSSHGESNLTNGLLCQNFKLFQDDWLMEDCAPDANFTLYTPLQPWEKRSVKPEIRRPRLNPNFFRVFVLEAQMRRAGKLSANTAGRAQLIYLPKPAVTFSTSPLHVEL Q9HDY3 YK17_SCHPO SPAPB1A10.07c; CHAIN 1..441; /note="Membrane protein PB1A10.07c"; /id="PRO_0000218973" MGAVLSIPLALASSLSGVVGIASSFLVTSVLSLTNSIQSNVGAVISYAVLYFVNSLLSWCMLSSWFNSKLSKLSAGYLQFDCQNDGKCYSVIAVHRLSFTLVMFHLFLAFILSLCNTRSRVAIKIQNGLWPFKIVLWFVLGIFSFFIPTKFLSFWGNIISVMGSALFIVYGLMLLVDFAHTWAERCVDRVLTSDSSSSKFYLIGSTVGMYVVGLVLTILTYVFFCASSCSFNQAINTINLLLCIAVSCLSVHPTIQEYNPRSGLAQSSMVMCYTCYLILSALANRPDEGQCNPWGNSASGTREFSKVIGAAFTFFTILYSAVRAASSRESDDSYSYLYADSHDMGVSTPLEDGSSEEDKHQSDYNFIWFHIVFVLAAFYTASLLTNWNTTSVYENQKNDVFVRIGFSYAAVWVKIITSWVCHGLYVWSCLAPVFFPYRFMI Q9HDZ5 YKP9_SCHPO TRANSIT 1..28; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC589.09; CHAIN 29..388; /note="CRAL-TRIO domain-containing protein C589.09, mitochondrial"; /id="PRO_0000310746" MFSRLWVRCRCSTALSAAAAGTFFFRRSQKQPEPETVDEKVSFESYSPLKLMIQKTWPRFQEHKEYRESFIRLAKCDSPDAILVRFLASCNNDSHEASQKLINTLQWRVDTGVERIVERGELYAKETNDDQFLEQLRTGKVTMLGRDLSDRPICYIQVHLHQPSKLTQNSLREMTVWVMETMRLFLRPQKTLKDSMDSPQNVNVLFDLSNFSLHNMDYSFVKYLASCLEYYYPQSLGVCILHKSPWIFRSVWNIIKGWIKPEIAAKIVFTQSANDLEKYIDYSVIPTSLGGGNKKIFQYIEPVEHENDAVIEDSAEKTAALARYYAYFSEWEQHSLNWAKLDDDDAQNEKVRLCCDAAGTNFANCYWNVDKYIRARTVYDRLKWIGNV Q9HE00 MTX1_SCHPO SPAC589.04; CHAIN 1..271; /note="Metaxin-1"; /id="PRO_0000350818" MGGLTKFSSYFHSIFSRFPLITFSNPYPGENEDYKTKTVMYLTMWNSDLNSEALDVNSLQWQTWAKLNDPSIVFLNVSNHASPDEKVPFIQIESRKLVLNPSLLQYFLKDESTLQQISPWMSLLINQVETAILLTMYLDNENFSEIQKKWLPNMSWPLNIIKSIGLPSQIKRKICLQLNESTLDFDAILEDASKAFSALSELLGSDKWFFNNESPSFLDVSLFAHAEIINHLPLKNDQLKVVLGTHKNLTDLTTRVRTLAGYTSAGPIALR Q9HE01 YKP3_SCHPO SPAC589.03c; CHAIN 1..168; /note="Uncharacterized protein C589.03c"; /id="PRO_0000304085" MDLSLFSDIKDVVERDMKKNSKVVENSSARSLKNKTEENKTIDKHKSSVGPKEPKSSLEKPKANRKRKQSYGLLHDIKELGGTEEDLELIEDVESDEELEFEEPNRKQPKKDGTDAFANELNLFAKKLGFSKNSFDARALDTESEDETEIEKSSSENSDSVDVDSDDE Q9HE12 YI31_SCHPO SPAC1399.01c; CHAIN 1..601; /note="Putative purine permease C1399.01c"; /id="PRO_0000316576" MSESIQDQDHEKTTIIEKTRRFVLSIFTKDFWIGDYDYSFLLPAIPFTKQKPKSPPFFSLNAKVPVLLALLLGFQHALAMVGGVTSPPRIIAASANLTTEQTNYLVSAGLISSGIMTLIQIARVHIPKTKYYIGTGMLSVLGISFTSVSVAPKVLSQMYENGYCPKDENGTKLPCPDGYGAFLATACVCSLLEIFMSFIPPRILKRLFPPIVTGPVVLLIGTSLISSGLNDWAGGEGSCTGRPTEAEAPGYSLCPSDTSPHALGWGSAQFIGLGFSVFATIIIIERFGPPLMKTTSVVLGLVVGMIISAATGYWDHSIIDAAPVVTFNWVHTFRLRIYGPAVLPMLALYIVNMMEAIGDIGATSDVSMLEVDGPAFDARVQGGILGDGLASLIASLMTTTPLTTFAQNNGVISLTKCANRRAGFFCAVILFFMGLFAKFAAVFVAIPSPVLGGMTTFLFSSVAVSGIAIISQIPFNRRNRFILTASMTLGMGAILVPDWFTYFFEYSGPNKALVGFLDAITLVMENGFAIGAFISIFLNLILPYEFDPDLTNDSPGLSTTNGVNNGIVEVRGIDPNDSLSNTDTEYANENKKDEVDVDKVV Q9HE13 YI32_SCHPO SPAC1399.02; CHAIN 1..589; /note="Uncharacterized MFS-type transporter C1399.02"; /id="PRO_0000343520" MNPSTSPNRNLASPKSLQLYTTGSEVAWYPTALDEANEIKSINSKAFSFKNQDQIYGAGSLKSRFSTHEISSEKNDSPDFTLVLPSNRLYIVIPGLMLSIFLAALDQTVITTAIPTIVANLDGGSSYSWIGTAYSLAETSILPFCGIMSEVVGRKIVLYTSIVLFLFGSAMCGAAQNMLWLVLCRAVQGIGGGGIMSLVTIVIADITPLQTRPYYTGCMGVTWGVASVMGPLIGGAISQNTTWRWIFFINLPTGGLSLALLIFFLNLVPKPTVSFCVFLRDFDFVGIVTITTGVVLFLLGLNIGSTTGHWAHANVLCYLIFGILCIAGFVVNELYTTRTRIIAPSAFQTLSLSSVMVTSFLHYYIMSTVTYYIPIYFQSIKGDGPLMSGVHTLSLAVVSSVVSAISGMGIGKLKNYRYPMIGGWIVLLAGTGSMIAIYYDTPIPRTMGFLALTAVGIGNLFQPNLIAIQASVPPALMATSCSAFMLLRNMGASVGISIGAVIYDQQLTTLLKGTEYSTGLSYSQIASIPSVSERNFVFNVYANAIRTIWIVNCPVAGVGMLLSFFTKQEKLSQSVTEYKEKDKGFKDAP Q9HFE6 YNW6_SCHPO MOD_RES 207; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 308; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP16F5.06; CHAIN 1..478; /note="Uncharacterized RNA-binding protein P16F5.06"; /id="PRO_0000310816" MELEKRIYVGGLSSSIESSDLESRFSRFGSVSNLEIINKSTPVGTIQRFAYLNFRTDEDKWQKCKSYLSNATFKGSKLRIEEARPYYLVKLQQEKKIADLQSTNNDEKNEDHSSKVDLEDPVFHGEIIVPGKHSKNMQVVTDSDVRKDPPRKGWKKGPYGRAIVVLRMYNKNTKKTRFFYPLGKNCLQKLWGRVETNMDNTTAFYDSDHDEYVSYGGKRASRDKIRMQAKLGIKASTQKDDNDFELLNNTTGEIEVTKELNEEQLDALRKKDKDTAASVLAELFGSENTEEIDTVSKTSGVLELDNDSTNNFQKEGLDEQDNLQKEESVHIDVPAEFEAFDERTAVVNVDNLKEMFSSNAQDTSKFSLFGNENGVGEESEMESEIDDRNYETMEEEADGETPLAIVKASSGTKGWPKMFTLPNPSSLFQPGNEDYTSREALESWWSENRLFLTRDYKRKRKDAVKRQRRAHEKRIRLV Q9HFE7 YNW5_SCHPO SPBP16F5.05c; CHAIN 1..146; /note="Ankyrin repeat-containing protein P16F5.05c"; /id="PRO_0000310322" MDVDDLIYACRAADEELLDEIIEKCPQELSRRDENGNSGLHMASANGHIAVVQKIIPYLNKEVINAQNESGNTAMHWAALNGHAEICKLLLEAGGDPHIKNIYEKSPIYEADIRNQQKVMDLFLDFEIAKGSEENTGDEEKLEDGI Q9HFF0 MIC10_SCHPO SPAPJ691.03; CHAIN 1..86; /note="MICOS complex subunit mic10"; /id="PRO_0000221639" MSTSQSSEQTLNYQWDVCLSNMVVQSGIGLGAGIVSSVLFFRRAAWPVWGGLGFGLGKSYADSNARLRTFHAIPKQLPASSTQKKD Q9HFF2 YL92_SCHPO SPAC683.02c; CHAIN 1..218; /note="Uncharacterized protein C683.02c"; /id="PRO_0000116841" MARITNMGKRKRFLEATPYESKVLEQPKNSSNTNEESSSQDNMKASFGSSKRYDERQKKKRSEYRRLRRINQRNRDKFCFACRQQGHIVQDCPEAKDNVSICFRCGSKEHSLNACSKKGPLKFAKCFICHENGHLSGQCEQNPKGLYPKGGCCKFCSSVHHLAKDCDQVNKDDVSFGHVVGVAGTTGADEDVYHEYAKTVAAPTKKRPVKPVKKLVTF Q9HGL0 YHLC_SCHPO SPBC800.12c; CHAIN 1..137; /note="Uncharacterized ubiquitin-like protein C800.12c"; /id="PRO_0000310775" MSEVQIVKSFLEELSKTPRNHPDSIPIEKIDETAISITIPAPLVEFQGNLALFEEKKVHVVAKTVRPPIQQASTEINVQSTILELKEVLASQLSTQPSSIRLMYKGKPLVNSRLLDDYVDADSVSEVNLQMFLMNIS Q9HGL1 YHLB_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPBC800.11; CHAIN 24..389; /note="Uncharacterized protein C800.11"; /id="PRO_0000316596" MHFAKLGAIGLLGSIICAYAASAASKVIIDNDGLTDLQVLFALQAKQQILGVTAIYGDYTLDDSLFLASDVLSTGNLTYCIPSFAGAAQPLLRTNNTFQIWQELYGSYVWQGYWQPEYETANTNNESYIYNTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIMGGYVDSQIAQVTGGDFLNDMYSDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSLYNGIIARAGGMANIESDSGLSYAKQFVGNGTLPSGSFPFWDEVASAIAAWPEIVNSSYDAYVSVDTAYDSPFYGSLRMVPADLVPKKGVRTAKASMITGINVAMFYQKIYDSLTAEYSSYCMNGTIITPSNITISNTTNTTNTTGFY Q9HGM7 NPRL3_SCHPO SPBC543.04; CHAIN 1..585; /note="Nitrogen permease regulator 3-like protein"; /id="PRO_0000220641" MVRLTPRLVAIFLVEKTTSGANFVFHWPLQPQVRLQATHHNNDSAESAIGMLDLDDSDDDENNRFTEVADDTHVLGYEKGFLANMLSPRIELCNQKFEIWVDGLTFLGCPVHIGPNGEWAKRRKPRTTVESNASSSHLVSKPESSHPSTGSFEVKSSSSKSRSSMSLFHVVFVLNVPTATVYRPTVNTMYDHIVVKLVTGLKYEQAKRNYVENECIHILKLTEKYSSQNVPFDVYAAQIPHHSNLASVLATTYEALINMHTAYLEINQSINLSLLWPMSVSTNTLENYELQVRPSTILASQTIFSEEHPSSIEPFVAPYWTLLLLKDTDTIMKRVPLLQNSLLSSFIAIVKPNLTFTDIANRLGISVSECFILAKHLIHWRKAIAIPPLLIRNTYVTSPTANLFNLEEESKLFKKEFPSLPSLSTFLAILSFKPRPFASIIPSKDHELVYLEMLAWLCRRNWVYEQNIYMYILVPEEIKKKAIALIESDESSKNDMQLRKQLEQDNGKESIIIDPHSASLLEQKWIQIIAYERGPEMAPLFTSIVKYLNGRFALQTIWVAEGLPRKLMRNILNEYNDYILRWHSW Q9HGM9 DNJC7_SCHPO SPBC543.02c; CHAIN 1..476; /note="DnaJ homolog subfamily C member 7 homolog"; /id="PRO_0000363383" MTEVETTHMNAGTESQQEPAELAEKQKAIGNAFYKEKKYAEAIKAYTEAIDLGSDSALAIYYSNRAATYMQIGEFELALCDAKQSDRIKPDVPKTQSRIRQAYEGLSILNEAEVYLKNKQAGLALNALDRLQRRIDSTTQPPMSWMYLKAQVYIFQNDMDRAQKIAHDVLRLNPKNVEALVLRGKVMYYSGENAKAITHFQEALKLDPDCTTAKTLFKQVRKLENTKNQGNDLFRQGNYQDAYEKYSEALQIDPDNKETVAKLYMNRATVLLRLKRPEEALSDSDNALAIDSSYLKGLKVRAKAHEALEKWEEAVRDVQSAIELDASDANLRQELRRLQLELKKSKRKDHYKILGVSKEATDIEIKKAYRKLALVYHPDKNAGNLEAEARFKEVGEAYTILSDPESRRRFDSGVDLEPGMEGGAGMDPFDILRAYQAGGSFPGGGFPGGGFPGGSYNSQGFGMGGGFPGFTSFQFS Q9HGN8 SVF2_SCHPO SPBC36B7.02; CHAIN 1..353; /note="Survival factor 2"; /id="PRO_0000374001" MSSSYSSRAEKYDLISCKDLTWDLSRSHLTTQYKSFYMCFDDGSFGYLQIAYGNLGLLVKVTPLGWTYYPAKTEKNVEPIVNSSTYLYRSMKISKDRYSVDVQKHFMHFNSSTREWHIVIEGVYDLKIKTEDSGFSLVDFGQNDSSSRMEHKIFPINTVEGTVTAHGREKKLTGVAVYVGALFFREKFTNLGHTWQNSILFDKSKKSILTCLHYFPRDPSQPFRSQASLTLDGKLIAVLLDNEYSTKGAAQVDGIRYLLPEQIHRILSGQTFDGKPVRVELSAELEELDSITDVLKIFPKWAKDIVSIWAGLPFVFVWLQHITAEVFIDNEHVATLSGCYYLEQTCVHLPQTC Q9HGP1 YNK4_SCHPO SPBC29B5.04c; CHAIN 1..605; /note="Uncharacterized protein C29B5.04c"; /id="PRO_0000350768" MFRSFGRLFRGSEESPTINDLTSITIYPQCFISTGKEYGSEPKHISVHVRGWVYENPDLNNLGRKDRLMLNLLRRYVGLPPKSKETGTYPEKDDENTNLQVVVDTKAQLNVNVNDGKPNDIELSSTSKTENDPPLSLHTTPDDLQGNGVNVPNPSLSASRSWYQSGYGISGFFNRIMTPSVNSQYISTIGLAKCEEYFEERSLASLQRGLKDEFVLVKIYATDKNFEQKVVAEFNVATNVEGYFIIDEVIPFYTTKNNKFSVEAVLLQSTSEDKVIKAYMSEVPVLDRNGISIISDIDDTVKNTRVIEGPRKVGETTLLAPLNTQTIEGVSDWFRVMTNLNATVHFVSNSPWQLWPTLSKFFTNDNMPYISSIYLRHFNGVLQNIIEPAAARKRSSLLTAIRSLGDRKIVLIGDNGEQDLQIYAEMAACFPERILGIFIRDVMSDFCGVLKKQTTKSNSLPEVVQTKPFATSTPDTPLKEFTTTLKDVDNEQASEFYQLEKEPDTVPSTFILHRYYTYRIFVEDRANKTRKPVVQVEHAASKLENVHILCDYCKHKCSNIMEQDWFVQLARARGVIPLHIPIVIWFNGEEPISFTEDLLKSAFAS Q9HGP7 YM08_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC212.08c; PROPEP 97..278; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000353834" CHAIN 21..96; /note="Uncharacterized GPI-anchored protein C212.08c"; /id="PRO_0000353833" LIPID 96; /note="GPI-anchor amidated glycine"; /evidence="ECO:0000255" MSPLIVGTLIIILLSGLATAFYVTWQGRLICAGVGLILEQAYEGGQMFNTLMAHCFETYNGVEKSGTQCVADWLKVGLLAVTFGAGGPRLVNTLGGTFLTSPTAKRSNLYCDDFTGADYFSCELETLRPYTLMRKSLPYGNIHDVWINTTDTHQMIGVHMTLNGTDMIHYYNKTYVINYSGLKLNSSAINKRSYFYPQDSFLVSHAEWQDGNGIWTDTDYFAAMADCDFLGQNLGFWLASSYPNAYKWETQLWRTVGINLNGNIIYPGQLIMQTFNGS Q9HGP8 YM04_SCHPO SPAC212.04c; CHAIN 1..288; /note="UPF0494 membrane protein C212.04c"; /id="PRO_0000306284" MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDLFTEFSKFHNSYYPNGRISTQDKSRWVLLIIWSIITILTIDKKFKIKESYLEWIGENQSHSEIWGPIVIYVGLFILLLSAFNYCSKLIIKALPLISMVIAWVGVVIAAFSVIITATIAGVIAAFSVIITATIAGVIAAMVGILYFGHWLVYKILILAFGFKIVTSGDVCVSNTLPTHNGETALHSDATVGSDIEQIELQNMPTPVKK Q9P374 YLM7_SCHPO SPAC19B12.07c; CHAIN 1..319; /note="Zinc finger protein C19B12.07c"; /id="PRO_0000351139" MSSDDAIIIRCPFDCEFAGDSISFISHLTTIHNSSVQTLAKNAYLCASEIANELNQNPNLKDQEILLLQIAQENSLKRVLRQQQKERREGKIKSLQCLFCNNEGLLNRQEWFEHSFHVHGLNIGLADNIVYINRLLEKIKNELESFRCLCCHVPCKNKKLLREHMNNKRHFRLDPKSSEYDEFYIINYASVTKSITISHSQFAINEDINETDDTISDINDEDAEPLSVECIFCTNFYEPVFCFEHCKIVHDWDIKKIQKDYSLDVYGAIRVINYSRKTKKKSIPAETDSFWKEPGWLIPVVPDDALIICLSEVIEDPRL Q9P375 YLM6_SCHPO ACT_SITE 188; /evidence="ECO:0000250" SPAC19B12.06c; CHAIN 1..258; /note="Uncharacterized rhomboid protein C19B12.06c"; /id="PRO_0000317207" MAIELGERISTSVGFLAELFLMKIPLFTVIVALLTIILGIVNIFLPIVDFFGLSWHNLINIRLHTLNTYPLVHHGVISFILGLLGIFLLMPRFERRYGTLCTIAMFFGFLEVIPAIAYLIACYVAESDDVYVGIGGWVYSLLAMYLLNLFGDLHPKLLNLPQVVRMALALVAPVLGLPLDFSITIVLHLTAVVISIIFSFAYMDFFLPRGGFLVWVETKFSKIIDAIPNYISVTEAAYYQADGAIPIQDLGSNSSGIV Q9P3A8 CAND1_SCHPO SPAC1565.07c; CHAIN 1..1220; /note="Cullin-associated NEDD8-dissociated protein 1"; /id="PRO_0000374019" MEEGILLKKYVESSDKDIRYMALSDLAARLNDANHLKNLKLESFPDTLDVLLQALSDASPEVQQEAVRCVAIISSKIPQDKLKSTVENLLSGVAGKKSKNYLSALSLLLSNSNVQPFVNKFYTSTVFPSFLQILKQYNVAQEEFFAILCVVCDSLEIYHSNLSTLLPNNFELCIDVFQKCTTQCQRELIIKKACYLLSDVSLYGPRFAYKYIIEVLDRGLGPSTQMSEVNISIKLLNEILLSSKKEKDSSTSFISTAVADYTNKILSLLKKEEAPDELTQKLLEVLGLLLEYQQVNILKIWPELHGLLISKISYDPNLISDTNDEDDIADFLEEMSDYSSIYEDEEDVSWIVRRESLKVVLSVILSRLEYLPIVLQALGTSVVSKLNDREESVCLISIEVLKQAFLHVPRWIEVYATSNDRKRRYEGLPSDRSAISDTSIYLVSVIGKHVSKLSDKTPLSIVSELLNLVTVIFSSRDLGVQSEFSNLSSIIYRFPDFSTLDIKIKLNLVRLISAIISCGCEEIENMESKMSTILSLAVQNNYPQLSYEALITELSFCKYIHKKQPTNVSTDFSTMIDSSLQLLESKISDLKVRLALIDLVSQYVILFYEPDFDSIFLRRVLIILCKKLQEEPTRSAAARALCDIFMSVTDITKIENGTKIYEEILQDCCRHIDKSGNEFTTAYLELLEVLLKVGQKYLAESLLEHILGLLIETLKRNTENTVAILKCLLIIPLSILLKSKNLLIDTIISHLQSSTIHLNEESVCLLSRIIAVISKEEDLELIINSFTCAQKPVEEMVTLALIAAQLICIFQSKAIVTSLNKSFMSPKSEVRIKVFTTLIFGQLDYGKLTLPANEYFDTIASNLNSPNADVMKAAAIALGSLTSQSEKFIKELCALYVSDAYDKELLLISFLTFLKKSKIDYETADKIWDILSKDIENIKDFSTSPFRTLLSECLGLLICNESSSLYYKLELLSSSEASNHMLLSLSVFRFSLTLDCPKLKAYEKQFFEKAYKLFQNPDLEVSQETLQVIISVIKNRRSCIADVYNELLQGLISKSSVDSSNVHVVQMGPFQHVVDNSINQRQLVFETLYSLLDIPESLNHLTHFLQVSVMGLEDEHYIKLVSLSILEKLVDCSPSIIDEQVDTILEALRKIIELRKTEKTLKTDSDNILDLVRSALRVLFTMKLKCDNPVISEFESQVQKGPYSLEYEGIKNEIKTTIKT Q9P3A9 YIL5_SCHPO SPAC1565.05; CHAIN 1..773; /note="Uncharacterized protein C1565.05"; /id="PRO_0000304047" MASFGELSFLSEISNIHKSNKKHEIQSAGTVALDNGVESPYYICVQVENQGIEVYHMKDERLFASCPLPEKTRFSCSPIYIKEGNWHYIWTCTSLKSNGEWKILLWKFNDLEEESEVVYRDISNQQIFALHFISSTGQLVIVFRNGKIAFLDPEDDKVHMSASVNESATLLQSMYVPSQANPIDAVRLASNEASGTNNNPKEIEMNSDTTSSVPKSGSTSFSANVTSSTSMVYLLYSVHVDKIIQYYVDSFSVSERRLVNTRAVVLKEVQAPSHILMSKDSTSIYTISLEGLSIYSLHDESKSYMLIKILHFQSISKIEHIELISDNFLLIQHDSQLSLWDITFGTIQDVYDLKQKPTILTFTCYKSSLKKMNQNSQLTGYIAVLLKKGLAIVPYTLPIKMLLADAVGKRTSKIGKLRGTNELIGEGVLTKSKNGPSMRDQLLKNIQLQDHSLRDELISLRSLAEQKNTIEFDAKFLGVVERYQNQYANNCKILKTSSVLPIPFAHAIESLLFSLDEENELQVSCAASGTLNYLIRHRLFSYSTLVQKGFSGSVFDCLYKFQKDIAFNFLERTSDISAYEIACAIKTAINSSKVKLLRSALARLSLFDSTTSREALLLAFVPEDFDSLFKTLGNLVVDSNLASVKFNLETYIYCLSVVLDAMGVGGVASSSENLEAARILYNDLQEKLTNLTAMSLVLPAISEIVKRKKDVHAERVQFYANPQPKAIVDDMGDLATLLKKDFLSEKRKGKSQRARGKEIDMAIGKYTVERLEI Q9P3B1 YIL2_SCHPO SPAC1565.02c; STRAND 9..14; /evidence="ECO:0007829|PDB:7E0W"; STRAND 20..25; /evidence="ECO:0007829|PDB:7E0W"; STRAND 58..63; /evidence="ECO:0007829|PDB:7E0W"; STRAND 90..97; /evidence="ECO:0007829|PDB:7E0W"; STRAND 122..127; /evidence="ECO:0007829|PDB:7E0W" HELIX 2..8; /evidence="ECO:0007829|PDB:7E0W"; HELIX 26..32; /evidence="ECO:0007829|PDB:7E0W"; HELIX 40..51; /evidence="ECO:0007829|PDB:7E0W"; HELIX 73..81; /evidence="ECO:0007829|PDB:7E0W"; HELIX 85..89; /evidence="ECO:0007829|PDB:7E0W"; HELIX 102..113; /evidence="ECO:0007829|PDB:7E0W"; HELIX 117..120; /evidence="ECO:0007829|PDB:7E0W"; HELIX 128..131; /evidence="ECO:0007829|PDB:7E0W"; HELIX 137..139; /evidence="ECO:0007829|PDB:7E0W"; HELIX 144..146; /evidence="ECO:0007829|PDB:7E0W" TURN 132..134; /evidence="ECO:0007829|PDB:7E0W" CHAIN 1..374; /note="Putative Rho GTPase-activating protein C1565.02c"; /id="PRO_0000314093" MEHDLERLCFIGGYDNDNDKVIVVVTKNLELFKKYDDINLIKEAYNHVHKLIQKDERYTAVFFAHDSTVFSYLGLSLKAYYGMDYYLHKNVKAVYVIHTDWMSKVAIRTLLSIASPKFTRKFRYLNSISDLNKYIPLSHLKLPPIVYEFDRNVEPAIFPSNPSATSNFIFPVQQWTRPPDALVEGMQVVSKSLQTEGLFRKSCSRKHLDIVIELYDNGCMVDLEAFGPIAACSLIKHLFRSLPSPLFSAEFLNGLTDHMDSGIDYAVSLQKLIDASMDKNSQKLARLIFSLLYQITQHEQENMMNAQNLALCIGPSFSKADNIAELMSMKDKEYNPYCYFLEYAILHWNTLFANEENWDSYIPQDPTLLLPKTP Q9P3E4 YLZ7_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC750.07c; PROPEP 97..123; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000353832" CHAIN 21..96; /note="Uncharacterized GPI-anchored protein SPAC750.07c"; /id="PRO_0000353831" LIPID 96; /note="GPI-anchor amidated glycine"; /evidence="ECO:0000255" MSPLIVGTLIIILLSGLATAFYVTWQGRLICAGVGLILEQAYEGGQMFNTLMAHCFETYNGVEKSGTQCVADWLKVGLLAVTFGAGGPRLVNTLGGSSPTTKRVIYIVMILLVLITLAVNLKH Q9P3E5 YLZ6_SCHPO SPAC750.06c; CHAIN 1..280; /note="UPF0494 membrane protein C750.06c"; /id="PRO_0000306282" MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDPFTEFSKFHNSYYPDGRISTRSNFRWPLLIIWSIIIVFAVDKKFEVQKFLSIWINENRFYSEIWVPIAIYVCLLVLMLLSLIFFAEFAVLALRVTGVIIAVLGAVLGMIIAVLGMIIAALGMIIAALGATITGLLYFGHWALYKLVILSLGFKIVTPGDVCVSNTLPTHNGETALHSETTVGSDIEQIELQNMPTPVKK Q9P3E7 YLZ3_SCHPO SPAC750.03c; CHAIN 1..145; /note="Uncharacterized methyltransferase C750.03c"; /id="PRO_0000339150" MNLLQLGKLHENVLDAGCEPNRNARYLASLGYKVVGIDISERAISKAIDKTSSEKSNVNFNQRDFSRLNEFKGHFDTVIDIGCFHSILNSDHEPYTASLSHICHSDSSVFLRAFSETNKSRYRRWQGHKRYSLALKRNNVKKLSL Q9P3T7 ODC_SCHPO SPAC328.09; CHAIN 1..298; /note="Probable mitochondrial 2-oxodicarboxylate carrier"; /id="PRO_0000310803" MPHDNIPFPVTFAAGAVAGISEVLTLYPLDVVKTRMQLSVGKSDYNGTFDCLKKIVKNEGPHRLYRGILPPILMEAPKRALKFASNDTYSKLWRKVFKRKDSSPALSILTGSCAGFTETFVVVPFELMKIRLQDVKNASKYNGTVDCFTKIVKQERILALYNGFEATMWRHVVWNAGYFGVIQKIRNSLTPASSRIGEIRNNLIAGTIGGIFGTFLSTPFDVIKSRIQTVPRIAGQVPKYNWAYPALVTVAREEGFTALYKGFVPKVLRLGPGGGILLVVFNSVIEFYKRCLVHNASA Q9P3T8 TBCC_SCHPO SPAC328.08c; CHAIN 1..259; /note="Tubulin-specific chaperone C"; /id="PRO_0000337255" MSEKFVELRKEFLTKLYKSTPSEQTSRSEKETWLEEKSKYLGEMTRELNEVQDQIAPYDRRVCMEQLVDLTRRLQQIRHDILPRQPFRFQRALHVKSSQKPVKNITVNAEAPEVYFENDTLYLANLKNQNIGDNVIPYPNNKAVKVSAKSLRSCNISISNCSSVNLHNATKCNFTFPTIQGSIHLSDINDSTICVSCHQFRLHHSTNLRVHLRCKTSPVIEESKEISFSYKDEHPILDFTWARSDPSPHFRITSDLFDA Q9P3U8 YJ95_SCHPO SPCC548.05c; CHAIN 1..468; /note="Uncharacterized RING finger protein C548.05c"; /id="PRO_0000310486" MVKRSSHRQVVLDEDDEENYNNNLDDEKMEVLLIPQSNSTTFASSDATQMYKKSRISSNSENKKQIPDTKTLLETFQKIKKTLECPICTEALQRPFTTHCGHTYCYECLLNWLKESKSCPTCRQKLYTQPSPAYLVYEIMNVVAASNSGFPLVGINENPAKKQKEVLFDGMFKQEDSHYPRSILVDSEDGVLRCARCQWELENPYHCDHCGFQISDDQDSGREWFWDGENAESDSSLNGDNTRGGNISTNRAFNNMGHAPITAVPQDWLRFDEGEEFVGSDLESDFSGPGEYDVDDGFIDNRATSQLSPVESDDDFVAPVNGSNGNGITALDSTDSEEIDIMNGFDEERDSGGTNMVSRSETCYNDGQRYDELRRELADIQNESLDSLNSSSNNSPSHNNIHSRQHPFSSDEDEGNIVTNGTGLRSSQSSSQNRGFDLEPYSEVFTASYPRRQARRTRTIQLDSDEES Q9P3V3 YI47_SCHPO SPBC1348.07; CHAIN 1..230; /note="UPF0494 membrane protein C1348.07"; /id="PRO_0000306280" MVRDTRNVDLERGLELCKPEKVNKQNLFTNIVKPQKDKINIKTDKIKFFLNNLFTEFSKFHDSCYPDGRISTRSKLRWPLLIIWCILIVFAIDKNFEVKDFLSIWINESFINENRFYSEIWGPIAIYICLFILLLLGLIYCSKIVVKAIPLISIVIAAVVVIIAVAMVKILYICHWLIYKILILAFGIKVKPLGDTLPTHNGETGSHSKATVGSDIEQIEFQNMPTPVKK Q9P3V5 YI45_SCHPO SPBC1348.05; CHAIN 1..485; /note="Uncharacterized transporter C1348.05"; /id="PRO_0000372789" MKEESILKKCDSSSIKHVPSTPLETNCPDKYNPKTWPIRLKVRNVIVISSMTFLNQYGDSVFAPSISNIAEQFHASRTLVTLGATLYTLGILFGNLIFAPLSEQFGRRPIYLIGYSVFALLQIPIALSVNLAMFLVFRFFSGLFGSVGLSNGSGSLADLFEKKDRGKYMVIYFTVLSIGPGIAPIISGFISQSSIGWQWEFWILLILSGFNLFWAFLLLKETYPPVLNRKKFEKYGEIGENEPVALRLTGKQLLIKLLILLSMKKPISILLSQPILICVACTIGSIYGMINLVLIAFSEVWKSSYDFSPGISGLMYISITLGLFSAVFIAMPINQKFYSYLVKRNGGEGEPEFRLPMGFIGITLFEIGILLFGWTARYKIFWFVPTIGSAIMGGGYIMTSNPLNMYVVDSYGIYSASASAGVKIFQLLFGAIFPLFAESLFRRLNYGWGCTLLAFILLACGCSLPILFKYGKQIRNLRPFDPSKY Q9P3V6 YI44_SCHPO SPBC1348.04; CHAIN 1..145; /note="Uncharacterized methyltransferase C1348.04"; /id="PRO_0000339151" MNLVQLGKLHENVLDAGCEPNRNARYLASLGYKVVGIDISERAISKAIDKTSSEKSNVNFNQRDFSRLNEFKGHFDTVIDIGCFHSILNSDHEPYTASLSHICHSDSSVFLRAFSETNKSRYRRWQGHKRYSLALKRNNVKKLSL Q9P4X3 UTP7_SCHPO SPAC959.03c; CHAIN 1..520; /note="Probable U3 small nucleolar RNA-associated protein 7"; /id="PRO_0000316546" MSAQKLNLEDVNASTKKYSRGRKLNPKKIKDKKLRSNIQKIEERIENVESSLAKTEILHEDNPGLLEAEGLERTYKFRQDQLAPNVALETATKSFSLDLDKFGGYSFDYTRDGRMILLGGRKGHISAFDWRTGKLLTELHLRETVRDVKWFHNHQYFAVAQKKYVYVYDNMGTEIHCLKRHIEVNALDFLPYHLLLTSIGNAGYLKYQDVSTGQLVAEHRTGMGASHVLHQNPHNAVEHVGHANGQVTLWSPSSTTPLVKMLTHRGPVRDLAVNRDGRYMVTAGADSLLKVWDLRTYKELHSYYTPTPAQRLTLSDRGLLAVGWGPHATIWKDALRTKQNFPYMNHLLPSSSVVDLHYCPYEDILGIGHAKGFESIIVPGSGEPNYDSYENDPFASRKQRQETEVRQLLEKLRPEMISLNADFIGNVDRAAPSLRKAEAEEEKPPEEKWVPKAKARGKNSALRRYLRKHARNVVDQRRLKVEKSLEIEKKMRAQRVRREQKLPEEREKWGYALSRFVSKK Q9P5N3 ALR2_SCHPO ACT_SITE 38; /note="Proton acceptor; specific for D-alanine"; /evidence="ECO:0000250"; ACT_SITE 266; /note="Proton acceptor; specific for L-alanine"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; MOD_RES 38; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPBC359.02; CHAIN 1..370; /note="Putative alanine racemase 2"; /id="PRO_0000114605" MRGARAVIDLRAIGYNYNLIRELLDEKNPDAHILCILKANAYGHGAVEVAQFLAKYCSAEGFGVASIEEALELRLSGIQNRILLLEGFFTDEDELSLIDKYNFSITIHCEEQLKSFMNYPFKKPVEVHLKLDSGMNRLGFTPAEYADKYRLLKNHKNVSGIVKATHFAFADIPEKSEYTLKQWRIFEKAAGCLPDPLSAGGGVIVVGWLNTIHMDWLRTGSMLYGLDPYDLDAKAPELPKPLIPAMKLMSTIVCVKHVEKDQPIGYGGAYVTTRDSLIGVVAIGYGDGFPQVRNGCPVIINGKRVPTVGKVCMDMLAIDVTDVPDVKRGDDVVLWGNPELTIEEVSTFSNENPFEIITGLTRRVPLQYTF Q9P5N4 YH81_SCHPO SPBC359.01; CHAIN 1..581; /note="Uncharacterized amino-acid permease C359.01"; /id="PRO_0000054172" MSHSDYNFDIEQNAFEKEAPKVSIERKGDVVEEEVIATGEVENYAEPKSRNFLQRFFDDFKPALTTRGDGVALKRKLTSRHMQMISVGGAIGSGLYVGSGSAFADGGPASVIINYILIGIMMIFVIYALGELAIAYPVAGSFNTYATRFIDPAWGFAVSWNYFLNYFVTCPLELTTCAITFKFWTEINSAAWISIFLAVVIVINLFGVRAYGEVEFILSTIKVIATVGFIILAIIINCGGVPTDHRGYIGGSIIKQKPFRHGFKGFCSVFTTAAFSFSGTEIIGLAAAEVGNPRKSVPSAVKQVFWRIAIFYVVSLILIGLLVSPDDPRLMGNGDVSVSPFVLAIQEANIKGLPSVFNAVIIISVVSVTNSTTYTAARTLQGMATLKQAPKFFSYTDRVGRPLIAMVVVLLFGFFAYINEADKNGSDISDTVFDWLLAISGLSSFFTWGSICLSHIMFRLAFKKQGHSLKELGFVSPMGIWGSVIGLGFNILCLMAEFYVSLFLIGGSPNANDFFQGYLAACIALAFFIGYKIYDRSHIPSLDKLDIDTGLKTYDNQDEEKEEYSSKGPLNILKKAWNAVC Q9P6I4 YHG6_SCHPO CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.; EC=3.2.1.101; SIGNAL 1..20; /evidence="ECO:0000255" SPBC1198.06c; CHAIN 21..466; /note="Putative mannan endo-1,6-alpha-mannosidase C1198.06c"; /id="PRO_0000012129" CARBOHYD 47; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 77; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 131; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 195; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 217; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 232; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 257; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 357; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 396; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 399; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 409; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 412; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNIYSVGLFYFFLVFIGAQAMDLDITDYQSIDNTVNIMMKDLMNYWNASSQAFVASYWWVTGATMGALLYNYELFNNDTYVDLISSSLLYNAGSGFDYQPSFEYFNLGNDDQGMWAAAAMDAAEANFSPPNSTEHSWLELTQAAFNRMSGRWDSSTCGGGLRWQAFAWLNGYSYKASVSNALLFQLSSRLARFTNESVYSDWANKIWDWTTDVGFVNTTTYAVYDGADTSTNCTTLDPSQWSYNIGIFMVGAAYMYNYTGETVWRERLDGLISHATSYFFTDDIAWDPQCEYFDDCNSDQTAFKGIFMQSFGNTIRLAPYTYDTLYPLIQTSAAAAAKQCCGGYSGTSCGIYWFWNNGTWDDNYGVQEQFSALQAVQMLMIEYAPEIATLASSTDNRSNSTYASNVVINDTNTTTTIVVKEKDRGGAGFLTFLSAIFILGASIWALVEDEEGKIPSRGKKGIAISS Q9P6I6 YHG3_SCHPO SPBC1198.03c; CHAIN 1..249; /note="Uncharacterized protein C1198.03c"; /id="PRO_0000304116" MDIKDEKALTIEKACTINVFAPFVRNVTAEDEKAVTNKKHINSSATVHVFHGVVNRTFKTKGNTVGLPKSFSKAVIETLSYKPFAPICIHSRSDEVVNGFPLIYFPEDLASHDISGKDWKSFIHDVNMACSFSDVALMGLDQILNLVSFGLSAYVISYYVEKYVDKAKFPIIKGFIEMWNRKFFNPRKTHVYFINSDEVAEQRAVSIKAYQQGKGTKGLFSKFNAQREWKKQHQDISSTQHSRLLLISL Q9P6J0 YHDC_SCHPO SPBC1683.12; CHAIN 1..482; /note="Uncharacterized transporter C1683.12"; /id="PRO_0000372721" MSTMEEEKVISKSTSVDISEGTFDDITIEKKEEAKLVRKLDWYLMPMFSVLYFLSFLDRANIGNAAVVGLKEDLKLQAYQYSAAVSVFYATYITAETPSVLLVKKFGPHYYLSAMIIGWSLVTIFTCFVRHYWSLVLTRLLLGICEGGFFPCLSLYISMTYKREEQGKRLAYLYVCSCFSGAFGGLIATGLTKIPKSSGLPNWGWLYIIEGLISAISALWILFCLPDDPSTARFLNPREKELMKIRAEQRQKYMGSPNFDWTQFRKAFKDPKMYMSCVIQFCQDLVLYGISTFLPSILKLELGYSSLAAQYMSVPVYALGGISVYVICLLSDRTNIRGWFIIGMNFFGLAGFIILLATTNSAANYVATYLIALPLYPTVALNITWINNNMAPHYRRATALGCNQTIGNLAGVIAGQVYRSSPYKLGHGFALGCTVVGTLTATAMRFYLQRQNKIKQEILNGERVDEKKERDGCDALDFVYVL Q9P6J5 YHD5_SCHPO SPBC1683.05; CHAIN 1..559; /note="Uncharacterized permease C1683.05"; /id="PRO_0000317320" MEDPKSDEKFDIGISEKNLDVGFGESSSVDVPVKGRFASFLKKLELSSGPEKENIDLRPTPPDRRHYSALDIIYLWSCNGISASAFRTGTSYMEMGLSPKQALAALIAGNVFIAMPMTLNGLFGSHYHIPFAVQSRASFGYYFNTLIILLRFIAGLFYYGTNVYTGAECVQTILYAIFKSFRSYKNRLPADAGITSDFLISYFVYWVISFPFHLIRPEYLQRFFLIKSISTYIACFAMLIFLLCNVGSHVVWDQPATVSGRSWSWVFMCALNSSVAGFSTLAVNVNDFTRYVKHPKTPYVQMLILPLVAAVSAPIGIVSGVASKIMYGTAMWDPLQIANNWTSRGGRAAAFFMGLTYLVSMIAQNISDNTVAAANDLLYFFPRYLDIRRAQVIVIIIGAWAIVPWKILQNGTAFLAFLGSLSIFLGPAAGIFVADKFKNHHKYDIDEFYNPSGIYRYNKLGLNWRALIAFLCACVPLIPGMAMSINPSITMPDGVIHLYYIGYFYSFMTAFLIYWGLNLVFPAKETLLEEAVYPPKSNAELVDPSTLSGKDKFWYYIDY Q9P6J7 YHD3_SCHPO SPBC1683.03c; CHAIN 1..519; /note="Uncharacterized MFS-type transporter C1683.03c"; /id="PRO_0000372712" MMNYVKSLGTYNTRNMEKESSKDLVQNEDTPLPVQKISMSLFHEIVFVFIACTAQLMTQAGLGQSIAPNNIIGKSLGTTNPGQLSWFPASYSLTVGTFILIAGRLGDIYGHKKMFVLGYIWFCIWSLISGFSYYAKSVIMFDVCRALTGIAPAFLLPNALALLGRVYPPGKKKNLIFALFGATAPNGFLLGSVFSGIFAQLSWWPWTYWTTAIVCIVFAIIGYFAIPHIEADEVEEKQKFDYLGAFFGVSGLVLINFSWNQGPVVGWQVPYVYILLIIGFLSLVVFVLVEKRVVQPILAPSMMNSEMGCVLICVAAGWACFGIWMYYLWQFLENLRFATPLLVTAQLTPVGISGCAAALTTGYLLKRLKPTKIMVVSMIAFTVGTILIATAPIHQTYWAQTFVSIIVTPWGMDMSFPAATLMLSDFVPKQHQGIAASLVSTVVNYSISIGLGIAGTVETHLNHKGVDLIRGYRSAWYMGTGFGGLGVCVAILTVFASYLKVGQQKSPKFPLIMKNTKAV Q9P6J9 YHD1_SCHPO SPBC1683.01; CHAIN 1..573; /note="Putative inorganic phosphate transporter C1683.01"; /id="PRO_0000050480" MKLNIFKSHGDSNTAEERPVPLEQVEAEDQQHENRFWLGLTAKEFRLMMLAGVGFFLDSYDLFIINLVTPIFEYLYWGGIEKGPNGKGHYPSGIRGLVNAASNIGNIFGQLMFGFMGDFFGRKFVYGKEMIIVIIATILLIAMPKSIHSPLSKMMWVFCWRWLLGVGIGGDYPMSAAITSERSKLNRRGTLISLIFAFQGFGTLAGAIVTIILLGCFEHPLNREGHYRKLEGVWRLQFGLALVPAIGVLIPRLMMEETQKFKNSQQLNSGDNRDPKTSLNFEDDELVKNPSVTKGHPEIHESSENYLSRSNTVENEPENIEKQFESVSAPANRSGFIQYFRQWHHFKHLLGTSVCWFLLDIAFYGVNLNQSVILKNIGFSSGTNEYRTLMKNAIGNLIIAVAGYVPGYWFNVFLVEILGRKWIQLQGFVITGLMFAILAGRWNEISTGGRFACFVIAQLFSNFGPNSTTFIYPAEVFPARVRGTAHGISAALGKCGAILASLLFNFLTSIIGYGNVMWIFCGCMWGGILFTLLLPETKGRDADEIDRVELFYGGDGKVECNSKWKSWYVNGIF Q9P6K0 YLA3_SCHPO MOD_RES 408; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 410; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1527.03; CHAIN 1..475; /note="Uncharacterized HTH La-type RNA-binding protein C1527.03"; /id="PRO_0000339172" MSHKEPSAAETSTVVHSEEDKAFCIGTGAVISEEREKEVLKNLQNSLTGKTAEENLNDEANHTSSDKSKSEDYQPSNVNVWALRKEKMIPKKHSHVKQEKRFSKSLQLQDPNVWPSPEIAEKQVEDRKLSDDSQKPLAPKANGKEKWVTITPNFTHTPISNRKSSRSRNDGSRRNGNGRRRGNYSSHGSNKRQTNYSREKDASRSIDSSNPSAEYRDDINNTFGSQTVSSANGKEVPQTSEDSSSQAPHHSSSSGHAPSQQGGNKHSYKKSDSQQSFHHKGRNTRKGQRHNNGFYRNIANNIQGPFPNYPVVVNGNGVNPYLCDVQAFLTSQLEYYFSIENLCKDMFLRKHMDDEGYVPLAFLASFNRIKSFSTDLNLLHAACKASDIIDVAIDLQSPMSIKVRRKETWSPWILPSESRLKFEMAKYPQINSSSSMSPLASSISNLTISPPFIPSSVDSIIKRDVQTEVEDKLTV Q9P6K1 SFT2_SCHPO SPAC1527.02; CHAIN 1..201; /note="Protein transport protein sft2"; /id="PRO_0000238615" MEGSFQSRLQSIIQRTGETTAESTNSWYNRLRTSMPWSNDYTEIPTNASGGNSYFQSSEFSLSRWERYMLFGICLLGSLACYAIACFMFPVLVLKPRKFVLLWTMGSLLAVLGFAIVQGFVAHFRQLTTMERLPITLSYFVTLLATIIATIKIKSTILSIVFGVLHILSFVAYLIAFFPFGTRTVSLGTRMASRSLSNWLP Q9P6K3 CUB1_SCHPO SPAC30C2.08; CHAIN 1..457; /note="CUB1 family protein C30C2.08"; /id="PRO_0000352784" MMSYEPAEPVPVEEQPILEKLIGIRQRLAVLKRDRTRFIEKNEVFHLKDELVEQMNLLDSRRSTNSTRTIVDSQLEDCLHLLSLFYLAIGRNNDLPAFFVQLGTVRRLLEYNLEGACYTQNDLKPLKERLERIRAAIVEGSKKEDASPVVVKYLNNKLAVCDRNYSEAQHNISKISPELIGIQTRLVSIHRQIDGFAVRPTSDPGFIDRTMEQLKEIEEMKDSNGMFCDADHVPLQGQELCNGILEECFSFLEDAKTKEGLSDEMKSSPKLQQIYHRLDELLNKLKHLTLTHRWTLRETDLYVYRASLAEIDSMRIDGQFLDEQGNAPAGQRILLYLLRRCYAYIYQLLSSSEPVSEELMAVHNQLRTVKRCLLEVQRSGGICSERDLYPYQMKLASLENLRVNGKFLASDHSVPEGQELVNSLLTQCHQLIEELRDEKHQHDIEEREGSENTDGNL Q9P6K5 DML1_SCHPO MOD_RES 446; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC30C2.06c; CHAIN 1..465; /note="Protein dml1"; /id="PRO_0000285341" MHEILTVTFGRKSNFCWTHFWNTQESYFVYDPNDHAKVNVNTNFRVLKKRDPEAIVTVPRECIYDTPIEFGNTRKNWLEELNESSGGKGTAWDGKLTQIMQTPVDVHPYQEALWSRDEIHEGNAIESEYELPSIRPKSVKYWSDFNRLFLDTEYLFPVNCSELNSSDFSFQLGVERFHDFDKQFNVWDEGLRPLVEECDSVQGFQAAIDIDTPWGGFASEYMKVVQDELGECRVPTWVYGIREPIQSDSSATIDNHFGKLNEALSLSQLNGSCSQYFPLCTISQGDDLWASSAKINLAIESFTLPTRVYGSSCYRMKDIESKLQSEGRGFIHNLNFKAKNYSSKEWALVSSASFVNVAQDYSQQNNCLFGVVRSPKDNQGLLEGKNYNASSISKIVNIQNLGLPSLETVPEGLRTLDTVFVEATNDGQINSHIQGLTKSLNRRFVSFVDQDELEEIREILSSYII Q9P6L4 YKQC_SCHPO SPAC688.12c; CHAIN 1..167; /note="Uncharacterized protein C688.12c"; /id="PRO_0000116832" MSEEESPYQLTKTFSNPKNNKIGLAIFLIGAFINLIHIYKPKGPSNNPTKRNYHISFGPPGKIRWFPLGIRKEVRSNVSGREIIIKMIITFILVQTTLITLDLYVFGATGLGLILSWKLFEVACANPEDEALLAERKQRLKEQREKKEQKKEQKKEKKTERRKKKKL Q9P6L7 YKQ9_SCHPO SPAC688.09; CHAIN 1..361; /note="Uncharacterized mitochondrial carrier C688.09"; /id="PRO_0000310802" MTLHCQEPKIRSLDMLSNSEIKPSENSQKTKVLLTKANNASNERAPPPLSHFIAGGVAGMLGAIATAPLDVVKTRLQSDFYKDRFLKQTAKSKSPLTAAYRHFMDTCIILKNVKVHEGTRALFRGLGPNLIGTIPARSINFFSYGNGKRILADLFNNGQENSQIHLMAAAIAGVITSAATNPIWLVKTRLQLDKKSGQAAQYRSSIDCIIKTIRLEGFRGLYKGLSASLLGVGESTLQWVLYEKFKHAVAIRQLRRKELGIQETIYDKVLDWGGKLGGAGIAKFMAAGIAYPHEVVRTRLRQSPSINGTPKYTGLIQCFKLVWMEQGIVGLYGGLTAHLLRVVPNACILFGSYEVIMHFIG Q9P6M7 MUG99_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1610.04; CHAIN ?..526; /note="Meiotically up-regulated gene 99 protein, mitochondrial"; /id="PRO_0000278618" MLRFGIKTWKRSVLAIRRSSTAPHVQIISNLQKKLLNELYSLRRLVDDNSPATIRVGNVSLLLSKSNIRRRIALQALSSSAEDVACVKQITHALLAAPFMPESKELKYAMDHNGLNPLYISFGTNALFERNARYSTSHLFLPSDFLQVNNLEIIHLPPGTVDSDILASCHARYICSTSYLRMTSSDFTTADTLVLDIDPKLHSLLKNEKSIIPVSSSAALKATKALQDDPHNFQNYQNQWEQSGFQQLRTNMTPTSDLEICKRFLNYLCCSFSLTKAEKDLVRATEFSNSMLISIEKWAKYCDVDLQEFEKKLQKFWKNFGTLKLYSNIESLPASLKQLIKDEYLQKSKLELSFILGELSKNGDDKNNFELAMKDFGTFQNSRMSAVDQALQPLRRKTLYTTAFQGLGALGSLYLYFVSHFSLYNAFSVFSVCGVFGLYYLQSSYRSWKKEYWKELLEEGRKFERQLCRNVFGRSSFYVQQKTAAEKKEHISLIMKKLTKTLDLMKEFQLQSSFSDSPTASKKQLL Q9P6M9 RM01_SCHPO TRANSIT 1..81; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1610.02c; CHAIN 82..253; /note="Large ribosomal subunit protein uL1m"; /id="PRO_0000314110" MSSLIALGKRQTLLSHNEFLNFKNQKGFCKRFISQLNKKSNFPALAMTVPEATKYLKSVSISVPYVGSYMLSIALKSNRRAPSARGQIAFPHPFQEPPKICVFAKGAAADEALKLGATYVGAEDLVKKIQTEPLEFSKCFAHPNSAELLPQVAKLLGSKRLMPSIKRGTISDELKPLIESALTAVDYRQNDAGSINLPVGKLGFSDKELQENIEALVSNVRFTLAKLPGKVKVTVKHVHLSASHAIAIPLQYK Q9P6P7 YKCG_SCHPO SPAC644.16; CHAIN 1..422; /note="Uncharacterized RNA-binding protein C644.16"; /id="PRO_0000310814" MNPSCVVYVGNIPYEMAEEQVIDIFKQSGPVKSFQLVIDPESGQPKGYGFCEYHDPATAASAVRNLNNYDAGTRRLRVDFPTADQIRRLDKLLGPSRYGYYPQSYANQSYTYGNNFGSYPPTQPSTQPLPQSYGYPSYPPAGYRGGSARPSGVLANDEVYRVLAQLAPNEIDYMLSAIKALCLEAPEQAAQLFETNPQLSYAVFQAMLMKRYTSESVVADLLIPAGVNLPGAQEPNRGYFSPMHTYSSAVPGPISVPSAPYGRASSTIAEVSPMYGSHAAPYASTPSAAVGSSRGSTPASATVPISPARGFPTTSAYNPAPPAYGMANPAYGSTGIRSSSIPSSGSIRSPSLTTTSAQATTNATNNITTTTAAQDENATKAALIAQLMALTDDQINVLPPDQKERILQIRQALPSSYKTESK Q9P6Q1 PLPHP_SCHPO MOD_RES 31; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000255|HAMAP-Rule:MF_03225" SPAC644.09; CHAIN 1..237; /note="Pyridoxal phosphate homeostasis protein"; /id="PRO_0000316622" MSTIHSCLDLIRSQIQQSANGRNVLLVAVSKFHPVETLMEAYNAGQRHFGENYMQEFLKKVELMPDDVQWHFIGSLQSSKCKKIASVKNLYSIETIDTEKKARLVNSAREALQLPLNVYIQVNTSGEENKGGVTPSKVLELCKQVQDMKYLRLKGLMTIGSISNSQLSDHNPDFQVLSDLRESLQNELGIPLQLSMGMSSDYLLAIKYGSDSVRVGSSIFGSRPTEKPSDVHISASK Q9P6R3 YOH7_SCHPO SPBC13E7.07; CHAIN 1..273; /note="Uncharacterized protein C13E7.07"; /id="PRO_0000304037" MGYEEAFFRWAFLIATVYVAYYFLVSSDKKLATKPQKSKLTKLGKQKQRQKQKNTKKDTLVNRETPSKKSQKLETSDALKSKSKDSSKKEPVVVPKKGTPKIFQENHKVKKVKSPKKEKLVGKNPAEKEDTTDVEDTQKLEQKHSTTPSSLKMKSSISLAAITADDSLHNSFSSNDIDDGFQTVTSSRSYGKKKSTEPLTKRQRQNQQKKLRAKEMQELADEEQRRRLAAHRKELHEANRPRGGLNNSSRSAYSYINNGQAGSSKGNRYDSLW Q9P769 RL10B_SCHPO SPAP7G5.05; CHAIN 1..221; /note="Large ribosomal subunit protein uL16B"; /id="PRO_0000147128" MARRPARCYRYCKNKPYPKSRYNRAVPDSKIRIFDLGRKRAGVDEFPLCIHLVSNEYEQITSEALEAARICANKYLVKIGGKDSFHLRVRAHPFHVVRINKMLSCAGADRLQTGMRHAFGKPNGLVARVNIGQVLMSVRTKDSSRATAIEALRRCQYKFPGQQRIIVSKKWGFSQYARDEYIEKRSRGEIIPDGCYAKFLNKRGSLQEKLDLFPEASFNLA Q9P781 TVP38_SCHPO SPBC1711.09c; CHAIN 1..276; /note="Golgi apparatus membrane protein tvp38"; /id="PRO_0000343074" CARBOHYD 191; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MPAPVSSIKIIALAAIGILIVVFAILLAVFHNDLLAIAMPIAERIAKLPMSFLIALVLIAASSIPPLLGQDPLALLIGAVWGLNVGFWTVVCGIFIGETIAFMAYRYFLEQKAQEFREHHEEHYGTFVKIVEEGSYPLIWLIRLSFLPTHFTTVFFATLPELSYIGWAIAFWLSCFKYLVPVYAGYCIVHNKSSAANIVGIVLSIVVTLGTLAFLIVRYKAIKNSTLEDSTNSTSDVLNHLESQPTDSIDLRHLEQTSEQNETDNSERKHLLSHQH Q9P782 YNY8_SCHPO SPBC1711.08; CHAIN 1..336; /note="Uncharacterized protein C1711.08"; /id="PRO_0000215824" MSATSINPNNWHWTSKDCRVWSHEYFNKELPKIQASEGPTSARITQVNSCEGDVDVSMRKRKVITIFDLKIQMEFKGETKDGVEATGSITCPELSYDLGYSDYVFDIDIYSASKEKEPIKELVREKIIPQIRQLFSGFSQVLLQTHGDDVYLSTEEHNGNAARGLPVHSSFKQNNSSQTSSNKGTTTVAAGSGSDGSRVSAVVNTADISENYTFDAPANELYATFLDPARVAAWSRAPPQLDVRPQGAFSLFHGNVVGKFLVLEENKKIVQTWRLSSWPTGHYAEITFTFDQADSYTTLRMIMKGVPIGEEEVVQGNIQDYYIRPIKTVFGFGAVL Q9P785 YNY5_SCHPO SPBC1711.05; CHAIN 1..451; /note="LisH domain-containing protein C1711.05"; /id="PRO_0000303958" MGEISMKSKVCPLIYHFLQENGYVKTAQTFLKETGDKDLAKGKVKKNLLDLLSQKEFLPYLTTEDVGKHKKTKESLEKSNDDSQKISKKGAPPEKAHSSSEASGSGSSSDESDSSSSESESSSEDNDSSSSSSDSESESSSEDSDSSSSSSDSESESSSEGSDSSSSSSSSESESSSEDNDSSSSSSDSESESSSEDSDSSSSSSDSESESSSEGSDSSSSSSSSESESSSEDNDSSSSSSDSESESSSEDSDSSSSSSDSESESSSKDSDSSSNSSDSEDDSSSDSSDSESESSSEDSDSTSSSSDSDSSSSSEDGNSNTDTTTSGEVSAQSSTNSTSSEESTSVKDEDSSKIHDKSLKRKHEDDESSTSTKSSRTTKTPFTRVGDPSQWDFASPALRDNSFNFEDDYGTLANRDLIVTRGKGFRQEKNKKKRGSYRGGRINTEVRSFKF Q9P787 YNY3_SCHPO SPBC1711.03; CHAIN 1..258; /note="ER membrane protein complex subunit 3"; /id="PRO_0000340103" MQKLLLDPALRNWVLLPIMFVMILIGILRHNATILLQSSPKKLSKEEIREQRLLQRAYALRACSNSLLPESIEARKCFLIESLKSGKYLKPVDPNAPKAANPLMDDKTLEGLMESMKGNMLMVVPQTIIMTWINEFFSGFILLKLPFPLTLRFKSIFQSGVATQDLDVQWVSSISWYFLNLFGLKSVYALLLGENNAASNATNEMGMAGFSSAAATAQLIQPGQDISKMMLSEAENVQILKNESLLVDVEKRLLAQFA Q9P799 YN84_SCHPO SPBP35G2.04c; CHAIN 1..249; /note="Uncharacterized protein P35G2.04c"; /id="PRO_0000304096" MISNSSIEDRINKNEAYIAKFFEIFSKNDKIRFHGVSLDRKALDSFMVRNNFKKRFVSGINLPILIRLHFYKKLFTILWLTVRTVALLSHARNIQCLIQESDGDAKDVARSIYITTAEFRNYLLTEKGFYVTTRSISHFRAILDSIRYPFGKDHASKNMELLPITYDLSFCTVFHGYLTSILEAYEFFRGVFKKYKAPLSSNFIAIGKTTDESNFSQLHHYFQKFDERIRRILHLISQELDGYCRIAKQ Q9P7A1 PITH1_SCHPO SPBP35G2.02; CHAIN 1..207; /note="PITH domain-containing protein P35G2.02"; /id="PRO_0000339879" MSGPHHCSADCDEHPFESGPNDTLYSCIRKESIVTLNEAVPDSGKLVFKPWDLRYDDTDIVESDADDQLLFQVPFAGAATLKSILVRIFPNETAPHSFSLFPNRTDLDFDTIGDVQATETFEFPLTFEGSHIFEFPVKTRLYQNLQNLNIFFTKSDGSDDPTQIAYIGLRGSFVPFKGDPVVTIYEATPRPSDHPKVNQEEVFRSYY Q9P7B7 YK24_SCHPO SPAC140.04; CHAIN 1..295; /note="Uncharacterized protein C140.04"; /id="PRO_0000363356" MNVGKKSEIQVSAKSNLNFLNELIEEKKRYEDEKRKISHQKYTDKLLEANDNETTKRKLLVKQKRKSNKEFQSNIIKKRKDEERKGTLKTEQANEEELLQRSRLELERKAKKYDQYAAGELEIKETEDDGILVDFTRKWAEEAPENETVEITDEFGRTRSVSIYETGNTLLSQKEEYKPEKPIYGDYMPSFEVDEEKVQKLWKEDEQQAVHYDSTKEVRNKGTAFYQFSFDEKEREEQLLSLKEIHAKVTQQQRKNTEDVLTLRDKKLEERRKFLERDYAIKLGERWMSEHFSNN Q9P7C0 YKU5_SCHPO SPAC2E1P5.05; CHAIN 1..524; /note="Uncharacterized WD repeat-containing protein C2E1P5.05"; /id="PRO_0000051499" MSDPFFTRPEHRKRKARSATSKREKENQKLERNGPANEDLASISSESEFNGFEDEIDEENEDTYETAAEKRLRLAREYLDEVKNELVEDGGFDAKEVDRELLASRLKEDVLEKKGQMYLDYTSKINPDVKIETAQLRGRHMRPLVGVVAYENFVYSADKSGLIQKWEALQEKDTENRENDDHEIGKAIKLHFRPIKFSRSRRGENDHVKEITCLAISNDGRWIVTGGLDHRIVIRDSVTLEPQHCWKHHRDAVMGLAMRRGTNEMFSCSADRSIKVWSLDQMSYIETLFGHQDVIFGVDALARERCVSVGGRDRTSRLWKIVEESQLVFRSGGTSMKATAGYMEGSVDCVAMIDEDHFVTGSDNGVIALWSVQRKKPLFTYPLAHGLDPILAPGRHSAETSPDPVTIPPQPRWITSLAAIPYSNLFASGSWDGNIRLWKIAEGLRSFEPLTIATPLSVYGCINSLSLSLQGKGKQSEVRVFAACGRETRVGRWKTLRGIPNSGFVFNIPLTVIPSVTDGDEIDE Q9P7C2 MU109_SCHPO SPAC2E1P5.02c; CHAIN 1..163; /note="Meiotically up-regulated gene 109 protein"; /id="PRO_0000278620" MMKLENKLHRVLCSLHQNSISTHKTYVAVAAQDEYVRMGKVSLPRMYAVKPRIQKNFQDNYRFYGTLLCICWLYFFIWYPFALLALMVGVFLSFVMHGLGSLTINQNIRLDPKYSIPGVCAVTLIVIMFLAPVGRLFWSFCIVSSFAGLHCLLTTYENPAGIL Q9P7D3 YOFG_SCHPO SPBP4H10.16c; CHAIN 1..295; /note="WHI2-like protein P4H10.16c"; /id="PRO_0000363357" MSVITQAQEIPTVAANPDFNYEGDPIIIQLCDRDTVFELSRDQLLGLPESILMCLFPRGLLLDYEIQECQLTQRPLIFQTADFDPSLLQYILNYFQMAENRTANDEIALSPPPPSFPGKCGIILLKEDIEFFILPPISPTTNIAIEVSPNDLLKLKQRVAQRLLQQKKIFDCLHLENSTSEGSAEKNLVRMLCYSGFHEDDEWKRRIQEPHRACITSVTLTNLDFSADQGPVSDPEYFPVYHKLLLFWQKPARKCWWDSSTSITYNGIEFATWVRRVWTLELAVLGANTYETAAV Q9P7D5 YOFE_SCHPO SPBP4H10.14c; CHAIN 1..308; /note="Uncharacterized protein P4H10.14c"; /id="PRO_0000304125" MFSGKVRAFIDEELFHSNRNNSSDGLSLDTPLAIHTPAKGFDADLSPQSLYDLHTVTTPVTPLAPDEWDFSLDQSSGVIPSPSSFLSDHNNNNLFSDDTISRQYSNTDDINPSDFGGQCAILDSQNFTLSNASTKSKWSFTKHGSNTPSDSSSPLCNSSKRVVGMLRRFLPSSRMVRLSKAHQPLRIPTTGVSLDSADLTPLSVSTSHLNHPSTSNSPDPLYSASQPPSIKTDASPVDIKNMDAAEKLKKIDLLLEEILQLDSAYDAAERRMIESGWSSVDEIRDVHNKRLDAWSEWKQKLLPLKKCC Q9P7D6 YOFC_SCHPO SPBP4H10.12; CHAIN 1..179; /note="UPF0303 protein P4H10.12"; /id="PRO_0000208925" MFSILKRTDHLEESFLKNPNDNLKELENIIIEQEEALRFSSLSYADCYSLGVIVRDLYAKAAYTAPIVIDITLNGHQVFHLAYDGSSPDNDAFIKRKYATVQRFRMSSMRMGLMMAQQGTTMPAKYDVPAEEYGAFGGGFPIKLTSGIQIGVFCISGLRQIQDHCLIARSIAEFLTTKQ Q9P7D8 YOFA_SCHPO ACT_SITE 292; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 351; /evidence="ECO:0000250" TRANSIT 1..34; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP4H10.10; CHAIN 35..392; /note="Uncharacterized rhomboid protein P4H10.10, mitochondrial"; /id="PRO_0000317208" MCISSSSLLCGINSLKYASNRVGILIPPFQTASSLNIFRPYVIFSRSHRSLSSVDVSSPSLPLREHLPLKNVYSQVPLLPVWSPIPKGPRRFLLPPKFHYRLSPPPGEFKSSPRVAIMVAVIVCLVNGVVFWHWDLARDEAIRLHDFKRFRFMMTHAQASLFNLYEGRWWTLVVSIFSHQNLAHLLVNCVAIYSFLSIVVYKFGVWKALSVYLGAGVFGNYVALQRMMNEENPFATLPNGPTKVWDLLFPKGPYPPISRPALYLGSNPEYGPIIRTATFVPQSWATGLLGASGAVYATAAIFACLFPYTEFFLFFVYPVKAGIFMPLDFIAEYVLCLLNYEKKFHVAFDAHVSGTFFGVVSSLFLLPAMWKRRSLYCVGIVKKRIWSNKAKA Q9P7E1 YOF7_SCHPO MOD_RES 580; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBP4H10.07; CHAIN 1..583; /note="Uncharacterized RING finger protein P4H10.07"; /id="PRO_0000056334" MGQGESIPSRQIQRDASMQAVSSESENINDSDRQNSGFSRLWNRFPSLQRVLGLRRAKRHRNDEGNSENGNRDRTTERSAFRSRYRGSLLNRNSPSLRSLSPPATPATPRSRIEGESQTSAIPQTDRLILENHQQEFERAARRFRSSIAALRNLNTQNNQSTLASNHEDENVSSSGGQEMQDHGSVNNLESPGTAIGRLPVRSVTSLADSNMEDYTRAVMNYINNSENTQQASVSPEESQLVMLSRFVFSVASGWVSVLMNSSSAHQSNNLEFPSSISGNVESGNVAFDEFLSLLHAGNLVQAMNAETNPRTAELIANAVDLEEESGPINLFRTFRFDNLHRNHEGQEVIPIIIVGIRSLRNSGSDEDDQPSADSPTLMHPSDLISSLVNSQNQTTSVSDNTGPNENVNEAEHISEDEQASTATDVNGISDNNGSSTQQAPETRNNNSQTDHQLPRSWAIYVREAFVPQNHPVLRAPSLFTDSPTYEDMLLLNSIIGIEKPPVASQKDLEKAGGVFPFSGTDERCLVCLSNFELNDECRRLKQCNHFFHRECIDQWLTSSQNSCPLCRTKGVASASTPSSPKP Q9P7E7 ADG1_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAPJ760.03c; CHAIN 23..166; /note="Protein adg1"; /id="PRO_0000303925" MFLRSIFQTLCAVSFLAGSVFADSGVSIVSTPATTTVYLVRTVDCSSSEVTSQPVVTVYNVLKPDTVTFTVTETAGSYAKRSIEIDSDSVSPTSATTTTPVASATDVSVYSASIHVPTGNPPVDTHNPLSYDTEVTATTTFSIALPKFNKGDRVSSANTYSVSFVA Q9P7F1 YKK5_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPAC2E1P3.05c; CHAIN 24..197; /note="Carbohydrate-binding domain-containing protein C2E1P3.05c"; /id="PRO_0000314120" CARBOHYD 182; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 193; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" DISULFID 33..50; /evidence="ECO:0000250"; DISULFID 44..60; /evidence="ECO:0000250"; DISULFID 76..93; /evidence="ECO:0000250"; DISULFID 87..103; /evidence="ECO:0000250" MLTQSLFLTVLTLALSLVSKTSASQCSPRYGTCGGIYYDGPTCCVVGSSCIYSNPWYSQCIPVDYTGPCAKLYQQCGGINYNGPTCCEPGSECIYNGPYYSQCIPVDIDPSSSSSSAASSTTSTTSSSSLVSSTTLTSSSPSAVSSTTSIPSISSTISSSVSTSSFTSLSSSGFSTVLSSTNTTSALPSSGWNVTGY Q9P7F4 YKK1_SCHPO SPAC2E1P3.01; CHAIN 1..348; /note="Zinc-type alcohol dehydrogenase-like protein C2E1P3.01"; /id="PRO_0000339119" MKAVIADGQNGVEVISDAPKPTPEKGEFLGRVIRVAFNPIDWKTLYNASIEKGTVGGTDFVAVVEDVGEGVDRSKYIGATVSGWAPGPLDGSNAAWREYITLDVNLVYFVPKNITPSQAATLPLTFTTASQGLNQYLGLPLPPTDGSKNSAQQKWVLVWSGSSSVGQYVVQLAHHAGYKVIATCSPHNFDWIKKLGADFTVDYHDPNVVEIIKKATDDSVFYGFDAASFPETSTLAVKAFSSKVKDGKLINILSSPPSPRSEVKIIGIIDYSLFNREFNFFGNKIEPIQASYDHAVEVYKKLTGWLQEGVIIPNRVKEFDGGLQAIPKALREFASGKHSAVKFVVRID Q9P7G3 YK45_SCHPO SPAP14E8.05c; CHAIN 1..101; /note="TMEM14 protein homolog P14E8.05c"; /id="PRO_0000317217" MTPDQNALVLSFLLTVGGLIGYLRKKSKVSLIAGTALGANFAWASKLMERGSSQGINYAFYGSLVLLASSGPRFYKSRKPVPMILTVLGVISTWYFYRLWA Q9P7G8 YLKC_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPAC1782.12c; CHAIN 19..118; /note="UPF0382 membrane protein C1782.12c"; /id="PRO_0000316613" MTIWNVAALTGLLSVGLGAYGSHGLQKRVQDPHLLKSWSTACTYLMFHSLATMAVSLHPVYGKSRWTGPLLITGSCLFSGTIYGLCLLPKGHSLRRILGPLTPIGGLVMLTGWATMLV Q9P7H3 PHB1_SCHPO SPAC1782.06c; CHAIN 1..282; /note="Prohibitin-1"; /id="PRO_0000316248" MAVVLERVARYAIPIGIGFTLLQSSIYDVPGGKRAVLFDRLSGVQKQVVQEGTHFLIPWLQKAIVYDVRTRPRNIATTTGSKDLQMVSLTLRVLHRPEVGMLPQIYQNLGLDYDERVLPSIGNEILKSVVAQFDAAELITQREVVSAKIRQELVQRATEFGIRLEDVSITHMTFGKEFTKAVERKQIAQQEAERARFLVEQSEQERQANVIRAEGEAEAADIVSKALDKAGGALIQIRRLETSKEVATALANKGAQVTYLPFGAGSNAQSSSGSGLLLNVNP Q9P7H5 COX24_SCHPO SPAC1782.04; CHAIN 1..175; /note="Small ribosomal subunit protein mS38"; /id="PRO_0000337250" MLRRGALSTILKGLNGLSLRSPIPIWHVSASPEVGSKYNLPTVPTTSHVSYRQIAKANFFAGYRPLSANQICVPKVESKTQVSQSQDEEDQPQEYVLSLEDGYLYAQSFSASGSVTQTQPARISTQVWEQICDKLISITPLDLTSVKRKRKLKMNKHKFKKRLRRQRALRKRLGK Q9P7H6 YLK3_SCHPO SPAC1782.03; CHAIN 1..355; /note="Uncharacterized protein C1782.03"; /id="PRO_0000346779" MPIDTPLIPHKPISRYRSGRLEGLESESSSESDYEEVSDSHDQENSISSSRHVITPVFEKEGISETKTSSNFQNINPVQTIDNSASEYETDASSAEGGSNSAASSSEEEDSSDSEYEMELRRRTLLLPPKFTSKVIKNRAKANEEDTEVLKKVTSQKILEETIKRELLLKETKNNNELLNDIDDTDGIDPQSEYELWKLRHLLRKKRDKEKSLELEREKMAIEERRLMNSEEREAQDLKDAEASRRGKKKSSMQFLQKYYHKGAFYQNEDIVSKRDYSEATEGEVLNKDLLPKPMQIRGDLFAKAGQTRWTHLANEDTTKEGSAWYDPKNPILQKNLHRLGGLHSDSPLSKRKRT Q9P7H7 ILM1_SCHPO SPAC1782.02c; CHAIN 1..161; /note="Protein ilm1"; /id="PRO_0000353192" MLFSFRAIVLFYCCMLTFAGIGFLWNPKFVVESGLVALIGASMEVKPLIVTQDNLSTLALSGLVFLILGMIYTISLLQSNFLFFSGITPIRAIFDFILTGFIYLKKEHIASNSLTFTFAFCDLMWQFWMFAAMSEERAKYLKNQKKAEELAARKAREVEES Q9P7H9 YIT3_SCHPO SPAC105.03c; CHAIN 1..708; /note="Uncharacterized transcriptional regulatory protein C105.03c"; /id="PRO_0000316608" MDQSSSPSQPESQAQPNLCIPCSLGTCLIHFHEFSSSSFMDPVSLFCSSPYPNLPPHSRSSSLESKKPSVASQDVKSDGTLPIGTNNNPLIPSHSQESSHWTIRHESMPSALAGSSAQSMQQFPSITQNEENFRFKKSFTQPQPIVKETTFPKSEPGQEHAKLSDLSYEEFLKKYSSTKVERVSEAAPPPSSLNSSTVLDENDSLISQGSSVDDQTDFLGFDDSLSYAYILNPTSDSDVDLIRQYFIPKEGTYTFSNMHIRYVSANPKTPVMYMVDPAYEPHKQIARYEKLQQIFQVVEATVSPEVGERLIGLYFRYIHRVYPVIHGERFLLAFKKAKHKLSPILLTAMYASSIIYWDADKELRNYPRLDAKKLWDLTEDFLDLSFSLSRLSTLQAAIIFLTGRPWINVAGNWSILTRAIALAQILGFHLDCSEWQIPKEEKILRNRVWWALFVNEKWLSMYIGINASIRQDDYLVPPLTDNQLLAGEQRIADSFNVFVKMAELSILLQNVLQHLFNARAVMTMSKNRRTVAQKISKYLISLEEFSCSCNLRENQPGSLSLFLQIDALELLLRKTALKLKLTDAVYQQEMLNVVQRCVSHFLAINESHFTDFFWPYSQFYFCILSSAIIKMYLDFEFNENFNATTFGLLSSFTKHCVWLKFRNFDLVFMAYKRLNALLIELSSGRPLIGKLLQETFEHRKRNLDETLT Q9P7I1 KHA1_SCHPO SPAC105.01c; CHAIN 1..889; /note="K(+)/H(+) antiporter 1"; /id="PRO_0000317080" MSTQSIFDGDNVVVYSASDPLLLFIVQAIIIIALCRLIHIPLSFLQQPRVIAEIIGGIVLGPTVMGRIPKFLDYIFPTSSMGPLNLVSNLGLVLFLFVIGMEVDLRVLVLNYKVTLLVTVFSIVIPFGAGAGISAGLYKFTTREFEFGKFLLFISTAMSITAFPVLARILSELHLLHKRVGVIVLSAGIGNDVIGWILLALSVTLVNSGSGVRAVYILLLALGWCLFLFIAIKPLVYLLAVKTRSLKDKPSESFICIVLSMVLVSAFFTDIIGIHPIFGGFLVGTIIPHENDLTVKITEKIEDLVNCLFLPLYFASSGLKTNISTLNTGKIWGYTIGTICVAIASKMGSSMLAARILKMPWSDSLVVGSLMSCKGLVELIVLNIGLSTGILNETIFSMFVFMAVITTFVTTPMTKFFLRFTKSEHDDNSIESSEELVQYLPELPTRLSFLINHPLDASAAMIFIQHIYENRDKVSGCLHLPQIIIHSIWTLFVDSRTSNLLRASQVDNKVENEALMGLFETFVKIKKFEYESNALLVSGTGYYNVVLETLKKSSSNILIMPYLKDYKTIENESSSSPLSLSSIRLALGDSFKSLDELIPLIKMARIPVGVFFTRNPHNLSVKKIRPIIRSTEYGSPKNDFEQLEKDKKSFDQVEISVKEKGSTYERSKVVILIYLGTENDLIALELLLKFLYEETSIAYIYTYDEFYKDDYATSLPNVVYTSEVLLSKHNDSAFKVWPKLRKNIRKITKPNGFTTDQHSQTFIPSQTHTKLDLRLSDVTDSVRSRINVVKFGNLNSLLSCLHELIQPATLTPSFETEKSITMFLGCRDKQAVSEKLEVAALSEMKKLGYIESSSEFGMLAGLIPLVLLSNFPLIDFFLGKAPTKMVQGY Q9P7I3 MDV1_SCHPO SPAC664.15; CHAIN 1..651; /note="Mitochondrial division protein 1"; /id="PRO_0000051490" MTDNNSKSKDSSQKIPNDSLTPTISKGLRKDVFYWTKAIAYTTWNFFDSSPVTPQRNPISLFVRGLSHPFLRHRLSKSQFNEWFLSHNGVDPVQAQTLPDPLLFDIPDHQETSYSLLEGYSVTAHDHSDTSPLPITSSNQKEGKKNVSSIDVSMVSDSSEFKPDSLQHEKLVKKCNQLRLQKLINSSELAQIDLELSKLYSRRRQVLERLSKIEEQNLKYTSKLASVEKLMLDSDAQDLYSSYSHDLIPSQIEAGKNGANPDVFDDTHDKYTDNLSARAISPRAPRPSTASEVVSDYFEQNSAFSKAPENTESSVNQNYIVGNLVKQFQAHSEYITSLDFSHPFGTLATASTDKTVKVWDMAGVVYLGSLKGHSDYVSCLAIQDSFIATGSMDTTVRLWNLDNDVLHKDNPVEESLNSPPDQPVDNATNVLTSHTAPVTALALSSDDVLITGADDKTVRQWDIVTGRCIQTLDFVWAETHDTSTSQILVSDTYKQEPFIRALDCLDAAVASGTVDGLIRIWDLRIGLPVRSFIGHTAPISSLQFDSNHLYSGSYDNSVRIWDLRSGSPINIIPMEKKVNSLRLYQGRLAVASDEPNVRIFDTVSNRNWICSIPSHSDSIAAEPNSVPTSVQYKDRFLVDGKSDGSVSVFSA Q9P7I6 YJNK_SCHPO ACT_SITE 159; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 163; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 18; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 37; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 63; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 90; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 159; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 163; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 192; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 194; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPCC24B10.20; CHAIN 1..254; /note="Uncharacterized oxidoreductase C24B10.20"; /id="PRO_0000374032" MSAAGGIVYVIVGGNRGIGLSLVKELSNKEGVTVFASARGPGSASELKDWSKTHSNVHIIKLDVTSLRSAKDAAMQVEKVVKCIDVLWVNSGISKSFQPVLKTSDELWMSHYQTNVLGPIHVYQAFYHLLKEGKLKNIVFTSSMAACMGGVRPNTYSAYGQSKAALNYTMKEISFELEKDGFVVVSIHPGVVNTDMFVNAMQKLASKYPEMVESIKSNAISPEQSASSMLKIVDNLKTEDNGMFYNLDGTKLPF Q9P7I7 YJNJ_SCHPO MOD_RES 328; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC24B10.19c; CHAIN 1..493; /note="Uncharacterized protein C24B10.19c"; /id="PRO_0000304097" MVKSCQKKPDIDEFFSFLQSAFHPLQTEELDTFVRNIFEYDDRGRLYNCLLTLVPYERLPIDAEDLSSRKTYARPVLIRQYRSLRFANKEENICRLTPNSAFVPVRDSAVASISTSKVQDFNSYATLTEAQKKTATPVEEKNFLNQIVIQCLDSLETDVETNTTHATLLAVDPTWLIRVSQHTCDRKAVANLCIQYGSQIFYDPSFRNAYELWSNPSVLLAFLKAQRVLVVSDIFTSSTLRSTQGTPMSFPNLALESADNVENVSKPINPRMERFSSEVKSSSILKQQIAAVVEKINYDIRPQRDQIPEENIVPRISYLTSTTTSTKSSPVPESTTTNTTEVLKELNDIQENKSRKNVEKATAATEEMLRGHHKPVEGTTATSEKESIKEEVDLEVNGDGKVEAEERIELESSDSEKELSELIDFLKREHPPEDTPEKRVKIKRIRTLLDTWQQEWRILNKAISNAESNSGRGQNSKTKTTSVNLSRNKRTRT Q9P7I8 U390_SCHPO SPCC24B10.18; CHAIN 1..93; /note="UPF0390 protein C24B10.18"; /id="PRO_0000255470" MAQGEFKKKKNSSANKGGRVTKHSKNPKKGARYCAPRRAAAIKDHTINANITKTLNVRNEKLIAGIASQQVGKLTITKALGEAGAKELKEGKH Q9P7J0 YJNG_SCHPO SPCC24B10.16c; CHAIN 1..124; /note="Uncharacterized protein C24B10.16c"; /id="PRO_0000116817" MFQVIQKELDFGNAMIPKVWIQVIKLNPSSSIFVWGSNVSTCPAGDLALSMPGKSDVVTTKLTGAGSIDDLSTQMSRILSKKFQAQVYTSINLQGDFPNDPEVQSVFTQVIRAVIEIIESSKSS Q9P7J1 SWT1_SCHPO SPCC24B10.15; CHAIN 1..465; /note="Transcriptional protein swt1"; /id="PRO_0000353139" MDRMEIDDQAGIDFVTESINSERARNRWSTSHIPSLSEINPSSFQSPSPSPFASSTSLASKPARYSKPLGLFVLDTNFLLSHLSLCQNLIEFLTARCPRLVVVLPWTVLQELDGLKSESSSTCGYLARQAHNFLLQCFRSNVSSLRGQKVHEHCSSTEKGDDAILDCCIYYQEEKLIPAVLLSDDKNLSIKAAVHHIQSLSFSKGLEAASIVQTSFPSAFSSNSENLENLSMDIDLTVSQPLATATNHRNQGASTVDIPMDRTHDNSIWASRYAHFPPYDKKKDTTRSAADYIPYTYTALTKEEILHASHPRACKLLDQITKIMVEETAFLLSRHLLKLWGDYDLAMTKLLASPQFPPQNINDVGHELYIHWYTCFDGYLPAQERSNLKSKAELWNEWMLWAERGIGIGPKNQEELQTYVTFWSNIWTLLSRREILGDQASTYIGFREQNIEKWVERSGRERILS Q9P7J3 CG121_SCHPO SPCC24B10.12; CHAIN 1..174; /note="EKC/KEOPS complex subunit cgi121"; /id="PRO_0000279217" MILPLFPETQVHVFVYENVSNCAAIHEQLISQNPIYDYAFLDAATILYKKQVYSAIIRALEDRRDEQMKTKTIHSEVILSLSPKTEISSAFRQFSMTKKSKNIVVVKIDSKLTEEEEFERLDKLVEGNRVEFSDEELQKLIDFKVLKKNYKLDPSTLENPLASILSSIALRGYS Q9P7J5 YJNA_SCHPO BINDING 132..139; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255" SPCC24B10.10c; CHAIN 1..355; /note="Uncharacterized AAA domain-containing protein C24B10.10c"; /id="PRO_0000310284" MNPTTKRAIKEIVVYALAFGCSWYAAHKLLSTLDPYRQKRQDTVSKSRKRLDEWAGEQVKELETLELNEYEQIVASQLVLPSEIDVSFDDIGGMDEHVNQLLQDVLFPLKYPEVFDTHGGLLSCPKGLLLYGPPGCGKTMLAKALAKQSQATFINVSVGLLTDKWFGESNKLVDALFTLARKLEPTIIFIDEIDTFLRQRQRTDHEAMAQIKAEFMSMWDGLLSGQSRVLVLGATNRPADIDEAIRRRMPKVFSIPLPNAEQRRKILELYLKKVPLEANFDWNGVVNATAGLSGSYIKEVCRSALSVPRRELFDKHGNDLEAIKYDIQSGGLRSLKTEDFYHYESLQNVSGIDVE Q9P7J9 YJN6_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPCC24B10.06; PROPEP 130..156; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000373869" CHAIN 23..129; /note="Uncharacterized protein C24B10.06"; /id="PRO_0000373868" LIPID 129; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255" MFGKVSSLLVFASFLIIQGAFATLVAPIGDLEHLSEIELLYTNRVLPSKIPLTPFVKRDDDSSSTQASYSTTVSDVVIVTDKSWSDGVETIFPYSYTEYQPSTTYTSAPAGSIGYAASIPNTGRELMESGSPVRFSKSSLLIVSLLSIAAFAALVL Q9P7K0 TIM9_SCHPO SPCC24B10.05; CHAIN 1..84; /note="Mitochondrial import inner membrane translocase subunit tim9"; /id="PRO_0000193609" DISULFID 35..59; /evidence="ECO:0000250"; DISULFID 39..55; /evidence="ECO:0000250" MDRLNVKEQEHLTQVLEAKQLKEYLNMYSTLTQNCFSDCVQDFTSSKLSNKESECIAKCADKFLKHSERVGQRFAEFNAKYMGQ Q9P7K2 YJN3_SCHPO SPCC24B10.03; CHAIN 1..128; /note="Uncharacterized protein C24B10.03"; /id="PRO_0000304017" MDADDFGKKDLENGNESPKKPIFMKDWKNSQPNEQGRWLHLDARMNRNIEDLEISNYNLRLMNEQLESQLLSLNVKPVVSFAEQGKSSESKTDEEGFILNSASNVLDNFISIVNELVQHAEDVLDDLG Q9P7K6 SDO1L_SCHPO SPBC21C3.19; CHAIN 1..106; /note="SDO1-like protein C21C3.19"; /id="PRO_0000373996" MSSSKANQTRVCYQPEDTTFIIIASNGPDVMRWRKDKTVPLTEIVDSFQVFTTSNNKGNEGQLITASKQELENTFGTSKDVDVVTKILTDGKIIPHREHGKHKEVN Q9P7K7 YOSH_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPBC21C3.17c; CHAIN 22..186; /note="Uncharacterized protein C21C3.17c"; /id="PRO_0000014215" CARBOHYD 62; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 75; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 93; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKFFLGSALFLILTFINLVRAEFEFITPAEDSRWARGFTYAVKWKQPTEQFVEIALQYADSNNTLITSSGVIPSNQTYWMVKIDKKWLMKMDNITARVVAVPQNGTASTVYVGPQVLLANTFYWKMVVDVSPAFSVNPIDKKLAIGLSVGLSCCILIVLFLHFATRRERRILKNEKELEMSSYRKH Q9P7K9 YOSF_SCHPO ACT_SITE 239; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008"; ACT_SITE 273; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008" SPBC21C3.15c; CHAIN 1..522; /note="Putative aldehyde dehydrogenase-like protein C21C3"; /id="PRO_0000310350" MSSTLTCYCPGDGSLLGEVKLFNKSDIDQSIILAEEAQKEWKSTSFAERRNFLKALKENIIRNQDKYAEIACKDTGKTLVDAAFGEILVTLEKINWTLANGEQSLRPTKRPNSLLTSYKGGYVKYEPLGVIAALVSWNYPLHNALGPIISALFAGNAIVVKGSELTAWSTHQYCEMVRSLLQSMGHSPELVQCITCLPDVADHLTSHSGIKHITFIGSQPIAKLVAASAAKQLTPLCLELGGKDPCILTDDHRLEEILSIVMRGVFQSAGQNCIGIERIIALDGVYDTIITKLYNRISTMRLGMYTQNDVDMGAMVSNNRFDHLESLIQDAVSKGARLVYGGHRFQHPKYPKGNYFLPTLLVDATNEMKIAQEECFAPIALVFRAKSPEHALEIANGTEFGLGASVFGRDKQLCQYFTDNLETGMVAVNDFGAFYLLQMPFGGCKKSGYGRFAGYEGLRGICNSKAIAYDRFSAIHTGIPPAVDYPIPDSQKAWQFVRGLMGTVYGAWISLVPNVYQLWRNS Q9P7L0 YOSE_SCHPO SIGNAL 1..31; /evidence="ECO:0000255" SPBC21C3.14c; CHAIN 32..841; /note="Uncharacterized protein C21C3.14c"; /id="PRO_0000304069" MKIERYFKAIARAFIITFLFSLILQDNGVLARKAKKQDKGAALKSIYDYHVRPYGTVVQSQIAKASPIVDAAKQATVNVKSYYDEHAKPKVENIRYEVNEVIDKKVAPCIKAFNEKARKIGSKVLDGDNLRELYTTGKERIHFFIVDVLIPFFQRVVQEVRTISRDIAEKLQYFWEIHAIPAYHHYKPIIQRGAMDGYMQLRYVFFPAAKATITQMIETSIRFLRTFLDMHIKPQLQHIYESVVEEKSEAFASATSSKILSEMSASMASSSAHYTSSPTILSRTKSVETPVPMEAAEEEPATEYSIPSSVTFNSQNDCFSNAMNYLEHEYETLVSTFTLSVSEHWEDLLRKATDSCQKELEAFEEISNLRVLAVENSLGNLIQKAEESNYDQAIMDLFEYVKDSILRVHERAIKLRTLSDSIRADVAENIEMGINSIREQAAASSEVALAACSGIKHNAEQVNKLNALIQKVYSYITAESEKVGNRYGETLDNVIKQHLSRIGSVASSAVQRLTAVKNSHKLKMVDRSSAELPNFDYLVSDQVHKIVEINDEHADCDDVNFSTASFEIYERSIPTHGADSERKILKRDSLLNEDDEIFNDLNSDKTIKTNQATSTSSSNTQEISYTGTLNDNINEGLSTFPSIDIPASEADNVYSILPIDVSTSEAEGAYSILPIDVPKSVAEETYSFLPSDVPKSEAEKVYSILPIDVPQSVAEETYSFKPSDIPESEAEKIYSILPIDVKDPSLEKDGHVIDSSNLQTDSVKDYSEVSRADNLDASSDTIFSVLHAENEASITKEVHSTPLSDVASSEAEKVYTILPIEVPTDPLPNYSSDVESELTSD Q9P7L1 YOSC_SCHPO ACT_SITE 39; /note="Nucleophile"; /evidence="ECO:0000250" SPBC21C3.12c; CHAIN 1..124; /note="Thioredoxin domain-containing protein C21C3.12c"; /id="PRO_0000372630" MLLPLKESLESTLANVAKNETLFVAYLASVDPRTKQPWCPTVRAALPLFNNAFNSSKKLNVVHVYVGNMPQWKTPHNEFRVKFGISAVPTLGKYTRDAQGNLKTSLLVDYDCLDANKFSKFIDI Q9P7M0 YOS3_SCHPO TRANSIT 1..91; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC21C3.03; CHAIN 92..692; /note="ABC1 family protein C21C3.03, mitochondrial"; /id="PRO_0000310292" MISFSHWNSHIRSGLSLSMIPSANSRFAFIIQRNYIPVVNSQNTRWKRLCGTQSVWSPYKKKHVLVNRLKHISLFPKPIFARKFTTRQKSEDQKQWRILRITFLVLPFTVGGLWILYRVKNRKNNIFSFDELELEERSNRPRSIFGKIKQFFNILLRSFNLFIIFSPIIITLPFIALISFLHLRSLSSLTVSIWLRFLVTQLERAGATFIKLGQWAASRTDLFPPAFCKTLSKLHSHVTPHSLAYTQSVICKTYKVESIEEIFVNFNPIPIGVGAIAQVYTATIKKAATQQDNSYFTSMLQSIGFRQKNISDAPVTQDVAIKVLHPNVEKYISLDLQILGFFAKLINLVPSMKWLSLPDEVKVFGAMLNQQLNLHYEALHLNQFRLNFRGNRYVEFPAPYDDYTTNQILLEDYMPGIPLSAFLKHKSGPFNKLLANTGNNALFQMLIVDNFTHADLHPGNVLVKFYKGIPKTIFNQDNEINDSIYKILSTCSTEEWDSAMEELNILGYRPTLVFLDAGLVTKLSTQDQKNFLDLFQAVLTFHGYEAGLLMVERSRQTERVINKDIFALKMEHLLNEIQKSTLSLKSLQIGTILQEVMTMAREHHVRIEANFANTVLSILLVEGAGRQLYPEMDLLSNATPYLRSASSKSNVSLTNPMVQLWIALEARQFLLLSTSKETVEKWVKSDMIAPNI Q9P7M6 YIOC_SCHPO SPAP27G11.12; CHAIN 1..797; /note="Hid-1 family protein P27G11.12"; /id="PRO_0000353194" MGSQQSKLDFRNAVLRLHEERNIPKFDLIWERLWTLPETTEDVFHLMSIDDLTKVKDNAPENLQTIIAVLWDKLEDLQKETLFDDPAAPTTKCALNCMRLLTRLMPIIFEDKSMLEWFDYFAWTVPKDPNINTPRGASFLNTVVDYLFLINFTIPAHNDLTHGVHYCIWETGVVYHPTMLKERSYELHRVEVLRLLLSLFSEEIYRTDGNGSSCCAYVASIANRRLVLCLLSSLINTAMRFNTMFWKPEFLPLDNSVAHMSLIEYCFSVLLILMSEENNNGTPCYNNYRSSKNTLPKNYFSILLSKLQPYSDFQIILDGMSRLLYPPMQSTIPKRSSLIMFDYYPLVLIFCKLFIHYNERFFHYLIDTDRAIDLFIFLLYLSFEYLGDPSTYNHLKLCVILLKRLTAEKYFCKRLNKPFQQQTALPISMPVPFEGGTYADFTIIAISLLVQYTKDYHSEIAQMLCCSLCYLCLYAQNLNSHSSQSLFELFQSASYPGFLISNDVNHKILKYVIGAINNAIQYAQKYNAPLLYFFSMHKDYIEAVSALSFDAIMSVRNSSAEGDSAYWTRNGKTFSSKAFDSILLSRLRYVRSKSPTPYYPIESSEFGFTNLKDVTSKDEITDGFDKALRSNSLRTHRDSRPVQPLLKQRPQLHRALTESATLHGNDRSLEDTDEAKVEPIAHSVDYTFKPTVEWWNKWWPSLNFRTMLDIFTDLSLKISDMKKAGHPASEIMAMIKTQKYPATNQPYIPKYRTKEWRQQLANFARLFAWQVSCDLDSHKREGPGIFEGTDVKIFDSF Q9P7N0 MUG11_SCHPO SPAP27G11.08c; CHAIN 1..392; /note="Meiotically up-regulated gene 11 protein"; /id="PRO_0000116793" MEVYLSEFINWKLYEFKKINELGTSTFRYYFKGKIVNLKNKRVSSNEVCYMFKLMDDTGIVELNYSLSKYSPKFEMLRQLQLGISVFVYSDVVCRVSGIRAWKLQIHSKNLESKIEATISEPEQIPCPGFGSDNIVPLSLVNDFKDGAFVNVLVAIQWKEEFEIFNNETKKSLPKQTIHVHDISGSAMIVLIGESQVKSALSWNNETILLIHNAIAYRTNTGMLELSIKDAIIQTLQSFDGKVLKLLNFSIKRKELIKINAYRLSTLEALEKIASQSGEAFGQVGVLIMQSKIKDLTKEGGLVYGNDLTGLRFADLISIIVDETGSVKNPKFSQKLLEEITNIAPTELSVLNEEQAMHLENVFLYRHYRVCVGFLNKQIYVFSSDEPLKSYI Q9P7N6 YIO2_SCHPO TRANSIT 1..20; /note="Mitochondrion"; /evidence="ECO:0000255" SPAP27G11.02; CHAIN 21..356; /note="TPR repeat-containing protein P27G11.02"; /id="PRO_0000363380" MRMQWIWKSRRSLQNVFIRRSSQYHKPFWRRPLPATLLGCAVLGVAAVYFAKPSPIDENYPRSVAKYLHEALYRQKGENNHDFQDAWKAYQSAIKQAESEKMDMESPPVQGIRLQMANLLASAGALHKAWSMYWDILERTSKLPDFLEQRVLIASKLIELSEPLGLQKDATKAADLIVKALLSKQFNGDDEQKSRLFEQSATLYFQAGTPSYAVPLYHEALNLTMANPSCHGLILMNNLATSLLAQTETVDKKHHETLMKQSQSWSQKAVDSYYFAYPKDRNQECHAGCAAAFYTLGQIAERQGNIDLALKHYKNSEALRKDDPYNDGSMLSHIAIDRLDKDAFIKKLDKSSSPTD Q9P7P8 DDH1_SCHPO ACT_SITE 235; /evidence="ECO:0000250"; ACT_SITE 264; /evidence="ECO:0000250"; ACT_SITE 296; /note="Proton donor"; /evidence="ECO:0000250" BINDING 154..155; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 233..235; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 259; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 296..299; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" SPAC186.07c; CHAIN 1..332; /note="2-hydroxyacid dehydrogenase homolog 1"; /id="PRO_0000316030" MRIAFFSAQPYEKEPFEKVNENYKHEIDYHESILNKKTAVLAEKAPVVCVFVNDKVDADTLKVLAKNGTKLIALRCAGFNNVDLKAAADNGITVVRVPAYSPYAVAEYTIGLLLSLNRKIHRAYVRVREDDFNLNGLLGHDLHGKTIGLLGTGRIGGLVAKCLKLGFGCEVLAHDIKPNKELEKFGIQFVEQQEVLAKADFLCLHCPLTPDTEHLVDEKLLASMKKGVKIINTSRGGLVDTKALVKAIESGQVGGCAMDVYEGERRLFYRDLSNEVIKDTTFQQLANFPNVLVTSHQAFFTAEALSAIAHTTLKNVSDFASQNNDPSVIVKN Q9P7P9 YLY6_SCHPO SPAC186.06; CHAIN 1..184; /note="Uncharacterized isomerase C186.06"; /id="PRO_0000317237" MSIKLGYLFKLPSYKTSSISPEVIVDLEKFLNLCEGSCSQCNTPFCVDVGPRNAIIQLPNGADVLNLNPNFQAIFECCSKNSLTGVQIFGMYNDGTYELRSFCPVHGVNEDPANGSGAGSVGVFFALNNPSIISSDFAHLLFNQGKILGRNALIRVAIKLSANGLYDIHVGGGSKICISGTAEI Q9P7Q1 DDH2_SCHPO ACT_SITE 235; /evidence="ECO:0000250"; ACT_SITE 264; /evidence="ECO:0000250"; ACT_SITE 296; /note="Proton donor"; /evidence="ECO:0000250" BINDING 154..155; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 233..235; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 259; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250"; BINDING 296..299; /ligand="NAD(+)"; /ligand_id="ChEBI:CHEBI:57540"; /evidence="ECO:0000250" SPAC186.02c; CHAIN 1..332; /note="2-hydroxyacid dehydrogenase homolog 2"; /id="PRO_0000316031" MRVVLFSSQSYDRGPFEEANKTFNHEIIYHNFSLNKDTVSLAGKAQVVCVFVNDQVDADTLKALAENGVKLVALRCGGYNNVNLKAASEYKITVVHVPSYSPFAVSEFTVGLLLSLNRKIHRAYVRVREDDFNIVGLLGCDIHGKTVGVIGTGKIGSNVAKCFKMGFGCDVLAYDINPDKKLENYGVQFVEQNEVLKKADFLCLHCPLTPSTTHIVNSDSLALMKKGVTIVNTSRGGLIDTKALVDAIDSGQVGGCAIDVYEGERNLFYKDLSNEVIKDSTFQRLVNFPNVLVTSHQAFFTTEALCSIAHTTLKSASDFYTNSLDESVIANK Q9P7R6 YHV5_SCHPO SPBC211.05; CHAIN 1..85; /note="Uncharacterized protein C211.05"; /id="PRO_0000220762" MADRLRSQAKLEQLQARYVGVGNAFTTKYEWMVNQHRDTLSSVVGHPPLLAYMATALGEPRVQVRKNLLEKMIMPCGPPPPSNQF Q9P7S1 YIFC_SCHPO SPAC23G3.12c; CHAIN 1..996; /note="PDZ domain-containing protein C23G3.12c"; /id="PRO_0000116790" MSIKKRARAGSKSDDIGNKTPKKNGIEHEATKSSETVIEMTPSGPIAESKKWKESIARVVKSVVSIRFSQVAAFDTDESGTGEASAFVVDAKNGYMLTNRHVVCAGPFVGHAVFDNHEEVEVFPVYRDPVHDFGFLRFDPKKIRYMNVEQLELRPDLAKVGTEIRVVGNDAAEKLSILAGWISRIDRNVPDYGELTYCDFNTNYIQAAANASGGSSGSPVVERNGNVVALQAGGHMIAATDYFLPLDRPLRALRCLQNNTPITRGTIQAQFLIKTFDECSRLGLDSAMEEKVRTLFPEATSMLVVETVLPEGPSFKKLKEGDILLYVNSMILINLIELESILDESVGKDVVLTVQRGSELVELTCTAQSTHDIAPDRYVEVCGAKFHNLSYQLARQYALPVKGVFISEPAGSFRLEGPEYGYILDSIAYKPVPDLDTFIEVMRDIPDRSRVAVGYHFIHDKHSLITDVVEIDRHWLKAFRMVTRNDETGLWDFKNLGDPLPAEPSKPCTTSIPKLNVENFGPTANIINCFVKVLYYMPLHLDGSRKSRKKGTALVLDKDKGLAVTSRSTVPYDLGDLTITVADSIQIPAEVVHLHPTQNLAFIKYDPKLLGDTPIQAAKLKDYYVSQGDPVNFFGFNSKSRVVAAKTSVTDVITMVIPSSPMPRFRAINFESITVESNLSTQCGSGVLTDDDGLVVALWLTHYGEQTSRGTDVKYHLGLASPVVLSTLRRLQSGVNVNPRILNVEFRAIQLAQARSLGLPAERIRKIETESGKKHQLFMITHVEAGTPRILTDGDIIISANGKSITRIRDLQVDDVTEVDMEILREGKVQTVKVPTFPSDNCETNRVVICWGATLQAPHRAVRLQIEDLPSNVFVTNRGRGSPADQYDLGAAQFITAVNGVTTLNLEDFVREIRKIDDNSYVRVSTSTFDKVPVVLTIKMNKHYFPTIDLVQDAKAENGWRAVQYDEVGEKKNPSMGFTIDEEVDDNTFDTEGEQQ Q9P7S8 RAX1_SCHPO SPAC23G3.05c; CHAIN 1..343; /note="Protein rax1"; /id="PRO_0000353802" MASAPRVSEVLTKKNLPPLSLYNFYIYIRDEENAIEFLDLFLDIMLHKFLFREHIRGLYKAGVTSTSLNTESSSTLGPHHFTRFRSASLSLEDLSTVYWPNFGPLLLEELSNEQTINSSDLLLSKDRAAYLKNLLTSNIQSLTQESTVISKEQVKMFTQIIIEKYFNPASPHEVMLPPQLVQPILDCKEHQRQDELRLFEDVETYLLNFLLKPAYYRFLNHKFKHNLNPLTCTGRFIIGYVSTFAAYWLGFCGIFLDYSRRKRVWTLLPFAFGFYNLICTWSKHDPVLALLGYSEVKPFHYEKVLQPSIRLSLNRRAIFVLSIIVLIVGANTAIFSCVPSIRL Q9P7T6 YIW4_SCHPO SPAC694.04c; CHAIN 1..324; /note="MYG1 protein C694.04c"; /id="PRO_0000213486" MNNLVKIATHSGTFHADEALAVYMLRRLDRFSGAQIVRSRDPQVLDSCDIIVDVGGKYDGIKYFDHHQREFNDTFSPKYSTRLSSAGLIYKHFGREVIHAVLPQLKINEQDLETLYEKVYQSFVEGLDANDNGISAYPAGLKPSFKAAMSLPEMVSSFLPAWNSEKQDDQTYLECFQKASDLMGTWFVRSVEHYALSWLPAKTLAREAILKAKDSPILIVDQFFPWKGHLFDIEKELGIENQFKYAIYSDGKAWRVQAVSIDPTSFTCRLPLPEPWRGIRDEKLSELTGIPGCIFVHASGFIGGNQTFEGALEMARKALDFPQN Q9P7T9 YI7H_SCHPO SPAC977.17; CHAIN 1..598; /note="Uncharacterized membrane protein C977.17"; /id="PRO_0000310367" MSVPLRFSTPSSSPSASDNESVHDDGPTTELDTFNTTDVPRRVNTTKARQMRPKNTLKVAFSSPNLKGLDNTADSDSQPWLGGYLAGRLEDISGQSRRNYVDPYYEELNAGRRPNKPVWSLNGPLPHVLGNSVVEKISQKNQEARSRANSRVNSRANSRANSSVSLAGMDGSPNWKRKMKSAVFGSRVKLNDEEAQLPRNKSSVSIAEQAASRPKVSFSLQSSRQPSIAEEQPQTQRKSSAITVEHAENAEPETPRNNVSFSRKPSIAEQDSSQDITMPPNEIIAEESLDSGSDTETLYLNYWCKIRHFFREGFAEFLGTLVLVVFGVGSNLQATVTNGAGGSFESLSFAWGFGCMLGVYIAGGISGGHVNPAVTISLAIFRKFPWYKVPIYIFFQIWGAFFGGALAYGYHWSSITEFEGGKDIRTPATGGCLYTNPKPYVTWRNAFFDEFIGTAVLVGCLFAILDDTNSPPTQGMTAFIVGLLIAAIGMALGYQTSFTLNPARDLGPRMFAWWIGYGPHSFHLYHWWWTWGAWGGTIGGGIAGGLIYDLVIFTGPESPLNYPDNGFIDKKVHQITAKFEKEEEVENLEKTDSPIENN Q9P7U1 YI7F_SCHPO SPAC977.15; CHAIN 1..247; /note="Uncharacterized AIM2 family protein C977.15"; /id="PRO_0000351444" MPCCPTKSGAAPTNRNYELQGEMLKDIGGMQTYFTGKRSSKVVLIGFMDVFGLSKQIKEGADQLANHELAIYLPDFLNGETASIEMIDPKTIEQKEARSKFMEKISSPLHWPKLTKVIEDIERIHGQDVKIGAYGFCWGAKVLITYPNKERFLRIGCAHPSLLDPVDAKHVHCPVCFLCSKDEDPEEVDAWKKSFENSPYFSESYFETFGKMHHGWMAARANLSDPENRKYFDLGYQIFLKFFKELF Q9P7U2 YI7E_SCHPO MOD_RES 113; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC977.14c; CHAIN 1..351; /note="Putative aryl-alcohol dehydrogenase C977.14c"; /id="PRO_0000310316" MSSLSPELYGCLGNSGLKVSKLILGCMSYGKKEYWEDWVLEDEEEVFKIMKAAYDAGIRTFDTANCYSAGVSEELVGKFIRKYEIPRSSIVILSKCFFPVRKDLIKIFGDLSSRGVHFLDSPELANQCGLSRKHIFDAVEDSVKRLGTYIDVLQIHRYDPHVSAEEVMRALNDVVESGKVRYIGASTMRCYQFIELQNTAEKHGWHKFISMQNYHNLLYREEEREMIPYCQKTGVGLIPWSPLARGLLTRSIDANEETIRSKTDLYTRALEFGAGYKAILSRVEELAKKYNVSMATLATAWSLHKGDYPIVGISKVERLKDALAAVELKLSEEDIKYLEEPYCPVPIQGEI Q9P7U4 YI75_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPAC977.05c; CHAIN 18..204; /note="VEL1-related protein AC977.05c"; /id="PRO_0000326040" MIFKNLISLFFIGLATAIRFNLTDLECSRLRGPHCGTYLLKVVGTNATYVGEKSFIGLDALTESKGEFFQRMLEQEPRLIPRLFTIAENDTANFTPLTFTTYLKTCNPQSIENAMIPFVNTVTSEISFDAWAYTAQNSSRITGLSNQLMNSTLYNVQVATCTPGFSALLLDSPTINVFNNEEGMPSWCQPIELIPVCPLDEGFN Q9P7U5 YI73_SCHPO SPAC977.03; CHAIN 1..145; /note="Uncharacterized methyltransferase C977.03"; /id="PRO_0000339152" MNLVQLGKLHENVLDAGCEPNRNARYLASLGYKVVGIDISERAISKAIDKTSSEKSNVNFNQRDFSRLNEFKGHFDTVIDIGCFHSILNSDHEPHTASLSHICHSDSSVFLRAFSETNKSRYRRWQGHKRYSLALKRNNVKKLSL Q9P7U7 YP13_SCHPO SPBP4G3.03; CHAIN 1..241; /note="Uncharacterized protein P4G3.03"; /id="PRO_0000350769" MSYNGKDLGELQLKCHQSMLQAGAVFENCTFVNGDVLLEIPSFFIESLQFHYLINQSEKISLKLIFWNELVYLLGLNDTSKASATTSFQQGQIETKPDLTLFINELLTTKKEHKKLDNDNRESEIPFSDTRFHDEFDRESRACLHRSEFPKNPHAFLAQDLPHGLPHRRAALPCEALGFHPNVGDYFDWYPHRPNHFGGKFDGHSRGRGAGRGGFCGRHGRGGFGKRSGLHGCREEFWMQV Q9P7V6 VPS33_SCHPO SPBC1703.15c; CHAIN 1..592; /note="Vacuolar protein sorting-associated protein 33"; /id="PRO_0000206310" MTTDVKEKATFKLLDLIDSVTGKKSLLLERDLSGILGQIVTTNTLQEHGIPQVYWFNENIPNDIEKKTIYLCRPTYENAKLVATHVRQFQRDMLRIESTVIVLPTSNILFETVLQEEGVFGELLVTEWPLHAVPLDKDLLSLELGPEKLEESLLQRSTDALIDFERTHGRFPRVSGRGPYAAKMLELLEKTYQEEATINFGKVEGEISALYDSVLLVDRSLDRITPFLTQLTYFGFLDEILGIQQMNVKLPSSLVNRNEASNTGPMKKFSLSSSSSQITKEIRDINFNCIGPYLSKIARKLSSDFEGRRQAKTVNQIRDFVSKLGSLQSEHTSLNIHTGLAETLVQHTKNNYFQKLLQLQHLLVSHADSFTQFNLLDEIIYAEAPVEEVFRVLCLASITTNGLRRKDIDHYRREITQTYGYYHLLTFQALIDAGLLRLRQSTNISLQKSLSYSTWLNTYPLVKDEVDEQNPEDIAYTYSGYGPLSVHIAYDILKGRDNEEKILKLQNMPGTYVDKWTLDQEKVMPKNLKTNVPGKRRVLVFFIGGCTYTELAAFRLLQEKEDLYEFTFMTTGMVTGSSLIRAFIPNIESLNE Q9P7W0 OPA3_SCHPO SPBC1703.11; CHAIN 1..218; /note="OPA3-like protein"; /id="PRO_0000220766" MSSLALKIGSLLVRTLSKPIANTIKAQAKEHKAFRKACIEFAQWMHRAEFRITGINRAKSGGANVRLRPLNDAKAVDAGATFLSETFIFTVAGGAILFETWRARRKEKNRRDEVAEAILGLQHEIVRINEIMEKQFVLQKKKNELQSSTEEIDSTEKDFDELHKVILKVERELHTLRQNTPSQNEQAEATPSKEIPRETVSEKADHPPSSNTKSVSTG Q9P7W2 FTHC_SCHPO BINDING 5..9; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 57; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 102; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 139..146; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250"; BINDING 140..144; /ligand="substrate"; /evidence="ECO:0000250"; BINDING 188; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455, ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2; SPBC1703.08c; CHAIN 1..204; /note="Probable 5-formyltetrahydrofolate cyclo-ligase"; /id="PRO_0000200279" MSLKKNQLRAILNSSLGKLADHIIDSQSISICKQVVELPEWKRCKNVCLYMNMPKKEVRTRCLIDVAFKEGKNVFIPKCIGSHVMEMYQVFEKTESLTINKWGIAEPNGESRKIMDDETDCELIIVPGVAFDEKLSRLGHGKGYYDNYISKYQSWALQKESRANMFKVGICLKEQILPNREIPMDTRDQKLDALVTPEKVIRNI Q9P7W7 YGQ3_SCHPO SPBC1703.03c; CHAIN 1..664; /note="Uncharacterized ARM-like repeat-containing protein C1703.03c"; /id="PRO_0000310326" MGRANGKRRNHRKNRMNPIQKKGFLEQEIPLNNSEAALPLLSRLDNPEIKERSWACSAISNIIASCTEGRLYLLKNGLVSKLIDRISDDSVEVVVEATGALRNLAIEEGYSICMDMYRKNVLAPLQIWQTKIVQTLDEATEGKNVLETYEDRSTFSCLCAIAENISSLLVNLGETTSQVIKVLNQKNTLVFLSRLLIPEAKIPQSVQEMALQAFFTLTDDNDDGIITWIQNSSDFALKTINQIYLYFSYPSCLVRVYSIGIIYNIYQSGFVNKKMESVVKGISLFDSFIPEALPILSDLLPSEENYRNLVRQVYDKDTYFKTKKDDLTLSSELLVIPATLELISSMTSLLQSLADGTDELEEQEDSLMEDEDLSYMDDMSNVVNEDENLIIDEIPSNTPQKGNFKLVEYMLDHVLPKVITYCVVAFEFSSEEIPSNLSNYFQEVGDRTIECLNNISWSCNSVFVESSEAFTRWKLSAGKILQWIFQTIFLRLGLGVWPFSSEGFTTACSLLWSVSKPFPAEIQVLSVDDISTLILFSSTHGSLEAQSRLLGAFGSLGRCGNIQINQLLGQTLMSCVIASDPNPLLAVEALNAIFDVYGDKSYPYDAPVFKGSGYLSQLSEALPRLKNMVKKIDRRREKHLRFRAEEALENLESFIDYKHAEYAS Q9P7X9 YH66_SCHPO SPBP23A10.06; CHAIN 1..335; /note="Uncharacterized mitochondrial carrier P23A10.06"; /id="PRO_0000310796" MQIGAATEGVEADLSVNAEPDVKPIAKMLSACVGSVITTLTVTPLDVVKTRLQSESISQYSSTQPISSAKILGKGRPAPKPLGGPVSGLYQIARHEGVRSLWRGLVPSLTMLLPANTVQFLGYEQLLPLYSDWGFPAAAAIAGASARTISATIVSPIELFRTRVQAVGGHYPPGHAREIANEVFDGLKLMIHQKGILNLWSGVSVTLWRDVPFSAFYWWSYERIRLFLLGHPSLQAFSSSQSTKDLYINFVSGGISGTLATLLTQPFDVSKTAKQVHGHTLTRGQFMLTLWKRGGPKALWKGTLPRCVKVAPSCAIMISSYHLTKKYFSESVDAY Q9P7Y2 SDHF3_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPBP23A10.03c; CHAIN ?..115; /note="Succinate dehydrogenase assembly factor 3, mitochondrial"; /id="PRO_0000042751" MNNITKLMKQKNILTPPLPLYRRVLRAHRYHLGAEERALGDEYVKAEFRRHRNVTNPLHLVGFLSSWERYADALENESWKQEKYSNTDLLESLNDQQIGQLYELSKALQEQKKSE Q9P7Y3 PKR1_SCHPO SPBP23A10.02; CHAIN 1..132; /note="V-type ATPase assembly factor pkr1"; /id="PRO_0000374007" MSYWVELWESIFTPGVTPVLAKSAHVACGALVAVFLGLYIGTKSIHCLILFFLAICLWLSLTWFLVELAHARVNNDLQMSSQSANKNDDNSNNQNPSNNKEMSDKESDSATTTQTFSVPEELLRARTTANNS Q9P7Y7 P5CR_SCHPO CATALYTIC ACTIVITY: Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2; CATALYTIC ACTIVITY: Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2; SPAPYUG7.05; CHAIN 1..282; /note="Pyrroline-5-carboxylate reductase"; /id="PRO_0000187327" MSGFCVLGCGTMGKALLTGIFDSIAENGNDVSDEIIIPNKFYACVKFPKEKEDVQKLFGDRVKVVMGAKENAEMAAISNVLLLSCKPQAAEDVLNSPKMKEALKGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAEWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQGQHPAMIRNDVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK Q9P7Z6 YJIA_SCHPO SPCC5E4.10c; CHAIN 1..198; /note="Uncharacterized protein C5E4.10c"; /id="PRO_0000304091" MPLNLLKHKSWNVYNEKNIERVRRDEELARLSADKEQAKNDLEESKRRIARLRGTVYEEDSKETEPKVEFANFWAEQEEKERKRQKVYSENRHDLEIMKERHGLGPLPWYMKTDKISIDETSNNMSSKYRAPQDDPMFLVEKLLSNRKTKNPESDRRRQSRKKKSTQIQASDEMKHRRHHVHKVHHYSQKQSSSTTRR Q9P7Z9 YCGK_SCHPO SPCC16C4.20c; CHAIN 1..77; /note="Uncharacterized protein C16C4.20c"; /id="PRO_0000303993" MDPQVVNLLQETEEDVYRRKTARIRRKVSEIEKECEMYAVKIYNVERDIQRYRHEAQLLSKVLEKKGLNKEKEAGET Q9P801 RML9_SCHPO TRANSIT 1..32; /note="Mitochondrion" SPCC777.17c; CHAIN 33..101; /note="Large ribosomal subunit protein bL9m"; /id="PRO_0000315957" MSIMKPTTRFFRFNSLELAVSPFQRIYGQLRFLRKQPKPFLVKLLNNEVSKLGRQGDVVSVTRGYYRNTLFPKKQAIAVDALKSMKAHLLQGSEFSTKTKE Q9UR06 MMF2_SCHPO TRANSIT 1..?; /note="Mitochondrion" SPAC1039.10; CHAIN ?..126; /note="Protein mmf2, mitochondrial"; /id="PRO_0000036211" MSKVPINSSKLSCGGPYNQAVKSGGLIFCSGQAAVKDGNFVPGTIQEQTRLTIENLAEVLRVAGSSLEKLVKVNIFLTDIDDFAAMNEVYKEMLPDPMPARTTVAAGKIPLSSKGGKIEIECIAAE Q9URT2 YJU3_SCHPO MOD_RES 202; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 582; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 707; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 738; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCP25A2.03; CHAIN 1..752; /note="Uncharacterized protein P25A2.03"; /id="PRO_0000116819" MEVQKGLIEAFYNTYPLEKAKELDKSPLCSEYELFIKELWPSIVESFHNSTEFETAIRFCCYETARKSEIGLEERLKCLFAILDLLVIGNEINESFCDHLLPFLILEELMDIHTVNECAKLYEYFETRPSLMKGIVSNRGRGPVLLRISNELLRRLSRQENSSFCGRIDILLSKAFPPEERSGANLRGDYNTVHSFGKVELSPPSTPISDRTDLSYHKKLNTLFTAYWDLQCMCSNPPKLLASDTLPKFIDAAGSAIQAFESILQNTFFNGKSNPTIDPNSSSLLSEKYITLDKGFPSKYIYSRSLFEYQLSDEDFRLQAILQLIIIFDFLLDHSKERIERRTLEKWTNKAVIPIVILSDEDTSKLNELSKEAYSFLHTARCGSVQRTIKEIIHIEGNWKLWKGLGCPSLEKPLVDKAAIDEAVEGLKKLTNTPVKLRFAMGNAALSRLWEQAGENTLDDLKKEERYRIPSPESFLSGVKADKFEIEEAVRDDDKHFHEQSLATKTWRAFRSAINSHLQNFSDTGLGDVELLCNSIEGKPTTSKITPSIPPAFDIHIIEGEELLEEMKKRENVKHNSQNFASPMQTDAEGDIVQNEEEKESVEVEEGKHKNDLPKVSPKPPTEGVDSEVNGESLVQVNKVLKSEDDNTSEASKDPSSHVKSPENIEKLKQNDDHFEVTEEITSTINSKISEKQENNVAETILEVTSSPKSSENSQKQSEITKKRGRDEEDEPSDLHSSPKRPKTGEDGEIVL Q9URV0 YBLC_SCHPO SPBC106.12c; CHAIN 1..274; /note="Uncharacterized RNA-binding protein C106.12c"; /id="PRO_0000082021" MSLEKSLDEIINERTNGFDHKHSRRRGSQNRISKKSRLTYKFKRASKEHNSSPDDGPWQHDLDQEQDAHPRTTHLQKRQHSENRFGVRVENLHYQVLEKDVLSLFENFHPIRVIMNYDRAGRSEGSCDVYFETSQDAEDAQKTLQSTNLKGSEIQISKKSPPSLFDRISDMPHSARKPSRSSRSNRGFNRSSKKDDRSFRSSSKKSSNNSISHEDLDKELDEYAMSFHAASTVSSHSSQDFTPSIANAHEKNEPVAPSKDSNLTEEMDLQMEAV Q9URV3 MUG2_SCHPO SPBC106.08c; CHAIN 1..296; /note="Meiotically up-regulated gene 2 protein"; /id="PRO_0000278484" MKKENWQKIENVYLLGKKIDKAKRMANKGESNTNMLSTEENIVKAKAVSRKKPVDVSYAGLARHESHVDTDYHGQALNTDNQDPKNYQARSFVKENELYESSQDCGHSRLAQILSEENQIKRLPQSDNTTTERIIENNPNYSNKPSKLKRALSGENSVFSIHQRNTLSPSSNLPRIPSDLYDIKQFLENLDARSFKSDMDLKRSQNMRRRATGYPAIVVPFLNGSLPQADLPPLRTIEDIDNLTREQCLTFIQGYGIPIDSSDTVYLKEKLRDAIGMRAFTDMSFEMNSFHLESPR Q9URV6 ATPJ_SCHPO SPBC106.05c; CHAIN 1..92; /note="ATP synthase subunit e, mitochondrial"; /id="PRO_0000116513" MNSINVKTLRWSALVLGLGAGMYEHRSHIQCQKQKEIDENYHRQESLIESAKIAYLNTKNTPPKEDSMLPNLKKDSEDFDMDEFVKELEKNV Q9URV8 YBL3_SCHPO MOD_RES 282; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC106.03; CHAIN 1..357; /note="UPF0744 protein C106.03"; /id="PRO_0000374008" MNPERWAADLVSNVKDYGKRIIDYAHEKTSNPQPVTVHTTNSAKGRLGEFLYQNRVSVGLGSAALFLAGLSYYKRYDYVRKRRAPRAPNHQKTQVVVLSAWNPLASVIAHDLDRRGFIVVVLVRDASEAATVSLQQRPYIQSLIVTHNEAVERFLLSFSNQSGPKEYALRLRGLILVPTGDSLYTPIENIGKDAWISAFQQLSESFSNVSRMIPLLKSQKARIIGLSHGILSAYEPPNYAVPSILSSSIETFLRTLKRETGLQVICIKLGNLSFLNYDHSSSPGKSNYPPSLCTERKVLNKIFDSLLGCWPSPTRHVGCRTFFMVTVSRFLPTCVIDGIFSLFGKFHFFSCSLIKRS Q9URW3 YIPL_SCHPO BINDING 16; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"; BINDING 19; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"; BINDING 72; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"; BINDING 75; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01128" SPAPJ691.02; CHAIN 1..131; /note="Protein yippee-like PJ691.02"; /id="PRO_0000212409" MGRYYPVHLKSRCYVCAKCKTHLAFKGHLLSHDYRGKNGPACLFKRVENVIEMEPKTEQMSTGRFIVRHIHCCRCHTYIGWKYVSSYEPSQKFKDGHYILEMQDAVLQRDDPEPDDCFIHPPITFLSSSFS Q9URX0 YLX6_SCHPO ACT_SITE 145; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 149; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 17; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 53; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 80; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 113; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 145; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 149; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 178; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 180; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" SPAC922.06; CHAIN 1..258; /note="Uncharacterized oxidoreductase C922.06"; /id="PRO_0000374033" MTVEGRVVLITGAAGGIGKVLCKMFTELGDRVAGIDIVDPSKVQDAALALQADVSKADQIETAIEKVIQTLGPIDVLINNAGLADDTPFEQLSHESWDHDVSLVLRGNYLTQRYVIPHMAKQGKGGSIVNIGSVNGHIYLGSPAYSAAKAGLENLTKALAVRYGPLGIRVNVCAPGTIWSPAWDERFKKHPDVGDRMKRWYPVGRLGTPEDVARAVIFLADSKNSFITGTTLYVDGGLLAGNPCLIQDIYSENNNFVF Q9URX1 YLX5_SCHPO SPAC922.05c; CHAIN 1..504; /note="UNC93-like protein C922.05c"; /id="PRO_0000372418" MSSDNLDISMEKKYSADVDVEKAPTPEYGEVETAPLSQSSWIYRRPRIGRFKSLAYGSALTQTIIVSWVCFLCPGMFNALSGLGGGGEVNADVANDANVALYSTFAGLGFFAGSICNLIGVKLTLAIGGTGYSVYTASLLCYKHVYNRGFVIFGGCYLGLTAGMLWAAQGAVIMSYPREENKARYIAIFWGIFNLGAVIGSIVPLAQTMHSSVNSVGDGTYAGFIVLMAVGSALALFMVSPEKTVKEDGKFVHIEKSMGWKKELLGLVQTLYKEYWVLLLFPMFFSSNWFTTYQFNDFNLAYFNIRTRSLNNLLYWFAQIMGSAVAALFLDWQRFNRVIRARVGWGLVFVLICVIWGGGLAFQLKYTRKSVAESDFVVTDFTHRGYTGYAFLYIFYGMLDAIFQSYAYWIIGSLSNDTNKLAVYMGFYKSLQSAGAAITYRMDTLNIPYMNYFASCWALLCGSLIVASPVIWKKIKLTTEGIEDEIPPLANGLAVDGPVVPLKE Q9URX4 YFZB_SCHPO ACT_SITE 502; /evidence="ECO:0000250"; ACT_SITE 669; /note="Proton donor"; /evidence="ECO:0000250" SIGNAL 1..30; /evidence="ECO:0000255" SPAC1039.11c; CHAIN 31..995; /note="Uncharacterized family 31 glucosidase C1039.11c"; /id="PRO_0000018588" CARBOHYD 115; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 162; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 225; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 422; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 478; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 486; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 546; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 611; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 670; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 823; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 843; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 986; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFIHRMKSNLASLFLSFFLLLACEFTFSYADFSTTTSDATHPSATATEDIFSTPAVPSLGLAQNPSVYEPYRGDKCGGYNAIQVSEYEKGVLAILQLNGDPCYAYGTDYPFLALNVSFDSIDRLHVSIQDLYGAQFQFSKRTDVWDAPLYHFQPQFGDRTYNFSFNSQPFEFWVTRVSDGEVLFDTRGHKLIFEDQYIELTTNMVDDYNVYGLAETVHGLRLGNNLTRTFWANGNPTPLDRNAYGTHPFYLEHRYTPSENLNSDGQPSYTSSTHGVLMLTANGMEVLLRPNYLQYRIIGGIVDLYIYVGGTKNPKDTVSQFVQSVGTPAMQQHWTFGFHICRWGYKNVFDLVEVKENFKNFEIPVDTFWSDIDYMYEYRDFTVESNAFPKDKMMEFFNSLQQSNQHYVPIIDAAIYAANPINRSDDVYYPYYEGVRRDIFLRNPDRSLYVGNVWPGFTTFPDFTNPETTNYWTECLMNLSAAFGYNSSFPLPYSGLWIDMNEPTSFCIGSCGTDKLDQNPVHPAFILEGEPNNMVYMYPEGFEHTNASEHASAYQASVSQYYATATSTVESVKATSTPLNVRPKYNINYPPYALNTEQGEGDLSNLGVSVNATYHDGTVRYNLFNTYGYDQSRVTYDSLTSIEPNVRPFILSRSTFVGSGKYAAHWLGDNYSLWSNMIFSIPGALTFNMVGLPMVGADVCGFMGNTDEELCSRWMALGAFLPFYRNHNSLGSISQEPYRWESVAESSRCAMNIRYSLLPYWYTLMYEASSQGLPLIRPLFFEFPNEPSLANADRQFMVGSALLVTPVLEPNVDYVRGVFPGDNSTIWYDWYDHKVIYRQHNENITLSAPLTHINVAIRGGNIIPMQKPSLTTHETKQNPYDLLVALDSDRKACGSLYVDDGVSIQQESTLFVKFVANGDSLSIESYGDLQVHEPLSKITIIGLPCAPIGVYFEGVQVESFSYLEDTKELVLTNLEAFTSTGAFSNNWTISWNLPV Q9URY3 YLOH_SCHPO SPAC1952.17c; CHAIN 1..619; /note="TBC domain-containing protein C1952.17c"; /id="PRO_0000352834" MDYKQRIEKFKDILNSEEPISLPGLCSLCIQGIPDEYSLRAKAWMLMLEFLPTDRSNWQSVLEKHRKTYTSFVQELLIDPWRKLTLHEESGENSDHPLNTSDDSKWKEYFDDNQILEQIDKDIRRTLPDLSFFQGKSEINKKPSVNNVSENISVNTEDDKVEEVGQKLNYTKITSIDQSQETPVHLSTIDFSKFQEECHLVLQGRIYRLENESTSSSTTALSTPRQSMDSKRTINAEAIAGENKLGLHREAAERILFIYAKLNPGIGYVQGMNEILAPLYYVLATDPTYENYYLCECDAFFLFTQMMVQVRDLYEKTLDHDSDHGIHFLMSKFTERLKKYDYELWENLEEKQIHPTYYSFRWFTCLLSQEFPLPDVIRLWDSIIADQMKARLFGKNDDGFNGAYDFLMDFCCSILIELRESILERNFADSIKLLQAHFNVDMPKLLNLTFELQHLRKTSKNDEDMSYVRKNSYNTNALANSLKNRVLSTYNTVKANVPQSSSSYTDNNKQKEPLEEKRSFFPSFRSSLDGVSPTQGRKSGEENIRTIFAKPTAHIGENGWSNLKVKGSSIFQRFGNFVGDTMRYITEEEESSEEEDLTTSRRKIGITSKRKVSVKRNVI Q9URY4 YI01_SCHPO ACT_SITE 141; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 222; /note="Charge relay system"; /evidence="ECO:0000250"; ACT_SITE 246; /note="Acyl-ester intermediate"; /evidence="ECO:0000250" CATALYTIC ACTIVITY: Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4; SIGNAL 1..19; /evidence="ECO:0000255" SPAC869.01; CHAIN 20..583; /note="Putative amidase C869.01"; /id="PRO_0000316204" MKLQLLFLTLAQLAKHGLAIPLLQSSKTTTNSTLVASQEVNFTTYVYPDTNSTNIFPMPKCQNITLEDATIDQLQNYMENGILTSTDIVHCYLDRYLQVNPYVNGILQLNPDVLTIASELDDERANGIIRGPLHGIPFIVKDNFATKDKMDTTAGSYALLGSIVPRDAYVVKQLREAGAVLFGHATLSEWADMRSNDYSEGYSARGGQSRCPFNLTVNPGGSSSGSAISVASNMIAFALGTETDGSIIDPAMRNGVVGLKPTVGLTSRYGVIPESEHQDTTGPIARTVRDAVYVFQSMWGIDENDIYTLNQTGKTPEDGDYMKFLSNKTSLEGARFGLPWKRLWQNAKADEIDRLLEVVKQIEEAGAIVYNNTNFYNLDVISNDGWNWELGSVNESEYTVVKVDFYNNIKSYLSEVKNTEIHSLEDIVEYNNKYMGTEGGKPNIVPAFSSGQDGFLASLEWGGVKNETYWQAVEYVRRTSQDEGIDYALNYTDPKTNDSFILNGLLVPSGTSITYQQAAKAGYPMITLPIGVKTNGRPFGLGIMHSAWQEPQLIKYGSAIEDLLQYKAKPKFYEYVAKNVPVW Q9URY7 FMDA_SCHPO CATALYTIC ACTIVITY: Reaction=formamide + H2O = formate + NH4(+); Xref=Rhea:RHEA:21948, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, ChEBI:CHEBI:16397, ChEBI:CHEBI:28938; EC=3.5.1.49; SPAC869.04; CHAIN 1..410; /note="Putative formamidase C869.04"; /id="PRO_0000316040" MAPRTIVKVDLNKPAWEQPNLHNRWHPDIPFAESIDEGETVKIECLDWTGGQIKNDDSAEDIKNVDLTRIHYLSGPFEIKGAEPGDVLVVEIQDVQPLENQPWGYSGIFAKENGGGFLDEHYPKAAKAVFDFEGIFCSSRHIPGVRFPGLIHPGIIGTAPSKEILAEWNRREGALVAENPHSTHVMAQLPNASYAFAGILADEKLSATVASEGARTIPGRPENGGNCDIKNLSRGSKVFLPVHVPGAKLSIGDLHFSQGDGEISFCGAIEMAGSITIKCKILKNGISDLAMKSPMYLPGPVEPHFSPSRYLTFEGFSVDESGKQHYLCTTTAYRQTCLRVIEYFRRFGYNDYQLYLLLSCAPIQGHVAGIVDIPNSCTTIGVPMDIFEFDVSPNGKAKIIDLGSCAFANS Q9URY9 YI06_SCHPO BINDING 34; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P02244"; BINDING 97; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="1"; /evidence="ECO:0000250|UniProtKB:P02244"; BINDING 97; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P02244"; BINDING 172; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /ligand_label="2"; /evidence="ECO:0000250|UniProtKB:P02244" SPAC869.06c; CHAIN 1..203; /note="Uncharacterized hemerythrin-like protein C869.06c"; /id="PRO_0000317095" MLQYSKKKVSLNFFPVRLLSYKMTRISDAIFKDHRKLQSDYQNIKSANDYDTATRWQNQFVWELARHSVGEEIVVYPKFEKYLGEEGKEMAEKDRHEHQLVKEMLYKFQSMKANQSNFIPALDELMESLQKHIDEEEQHDIPFLEKHLSEEESLHMASSFERTKKFVPTHSHPSAPNKPPFETVAGLFAAPIDKLRDMMEKWP Q9URZ2 YI09_SCHPO SPAC869.09; CHAIN 1..116; /note="UPF0654 protein C869.09"; /id="PRO_0000350766" MPDPAHIIAGHKAALSNPHVSEEAKERARKYLKEHGSESHYTTGTTRGQKADADDAGELREEGFGTKNQFEDNESQAKNLGNVRGGYKAAMHNPKVSQKGRRHAKELLEEVDDESK Q9US02 SDHF1_SCHPO SPAC664.12c; CHAIN 1..79; /note="Succinate dehydrogenase assembly factor 1, mitochondrial"; /id="PRO_0000374046" MALSGLQRQVIHFYRRCLHAAKAKEQPYNERWMAFVHQEFRKNQTISKRDFFYIEHLLRVGQRQYEAYSRPEVKDIHFS Q9US05 BFR2_SCHPO MOD_RES 31; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC664.08c; CHAIN 1..452; /note="Protein bfr2"; /id="PRO_0000056631" MGKVSLKDELAGMLNPQPQERDPEALEDAFSDREDSSEEENDTLGREHYVDVSESKLRSKQAPQLDPKFKGRKTSRQELLNSGSLNSQSSSPSEEEDSEEDENDAVSEDHENFSSSEASSISEENEDDDQSSAIPEKDMDRLKKIINGEKKLSDQIRTSALEDMKKGLALKEQMRFYDNVLDTRIRLQKGCSQLLSSSNQLQGDKVEARDGLVSFIQHTLQLRKNLLIDSGVEILDSRSKRKENPVSLEEIALEMNNLDDSLNEWKNDTLTKWHNRVQAVQGISQSNKFKALNQSIVQQIENSMINKKDLVERTRIDYSDPNNKTFNPEIYNDTDFYQSLLKDFINSRMADSTRDGTVRWMATKKQKQKKENVDTKASKGRKIRYHVHDKLQNFMAPIEVTVWPDEQTEDLFSSLLGQQLDLSETANDTNTSNFVEKDDELISSNDGFSLFG Q9US08 SPO3_SCHPO SPAC607.10; CHAIN 1..1028; /note="Sporulation-specific protein 3"; /id="PRO_0000072138" MGILSVIRIFIYCLIRLFSFNSRKRNSSIDELERGEINAFACDKQNTPSPNSECRPLTPLNSPFRRTVEGDTANLQAPSPTACPSFDSASSIKSSKEDIACRKLSTERFFYSPNGIDEMKKQQQFKKIPTVSITEVEPAFIPSNMEQALFSEEPFVIQDDLSHQINLDDNRKFSRIQKNKLDPLITVNLVPIVNGENCFNFYETQMETNFLSPEFIKKPSMVDHKRDSEINAVTAVSADGSFSPLTETLSSTISTLSNDSLDGLSSQKNEFTGFNSNSEWIPNDTVDYICNSDASSVVSNLSDFEDCFDQFGVYDKEYEKKIEKTKRNFPKFQSSATYPPFSAHHQARRNNPQGFRNVKKRFQLFKDDCTALTDSDFLDALPFFNARVIIALYVEWRLRVYETMIIKGEESLKNLQRARDGPHNKLWLGVFGNKDTIKKLSNYDRRAISNPYVSNHLNFNVRRVKSDTVYIPTILQLLRSSTQLMTEQAFVASSNLKSTKGLRETRLIQKYKVKGDFEYVYAALYYAAFTQESTLKAVTIDDILSEDELEDWWYLNLRYTSFITPQLCFEFLDKEADSCRDRLTEVKSEPPKAVIYEEPLNKLSRFSSDRLFTSHELVAIAELISLNEPPLESGKKFYYEEFQKACQKKRDDYRYSPEIEFKAAFREKFLQSNEKVPFPRPGEIYEKRCDYFSKYACQNIFISKPLKRSGSIYEVFSDGIGRVIYGSVLDYEATRNNILLHFGFEIHCAPSEEELIEREEAFKDFHNMLSFKYSANEIYEFCGTHSRAEVHKNEVLKRMAYYLIDENKEISILRRILSLRIVEPTTSFTRYEYDLWRTFYPDVLYLNYSKSGRIPTGSPYIMNGQWRKDLCVSTPPMVDINSALFPHWFKLSASNLFAGAEHAGLNRQKPDKIDLDLYEPLPENSYLVAAELRVLRALRHKNPENIPLLEKWEVRALHQLMAKIRKYYTVPTDYLSLRMDGLQAMLRKREYMSCYTFNYFDYACLMDHAYRLYEGFNNQVVNLPPRIM Q9US10 YK68_SCHPO SPAC607.08c; CHAIN 1..579; /note="Uncharacterized membrane protein C6F6.13c"; /id="PRO_0000340088" MAEQKIISLFDDDACTRYTILIASTIGEMREKKESIIDNTDPEIVKYLSQLLDVFRENFDTWAMAVVNRTGCALDPSTPKDQVEVKKFRQFSETEKSECFIKCLLLLILSLGNYSPYSRNLLYSIAEKLGLSSIVVYKAELITSSMLLDTFQTMESNQEMYELSGTRKMRRRIAMGLAGLAGGALIGLTGGLAAPFVAAGLGTLFAGLGLGTMIGATYLGTLITSAPMITALFGGFGAKMSMQQMGDVSKGLTDFEFIPLSVQSHLPVTIGISGWLGDYNEVDAAWKSLTVGDKSYYWGDIYALKFEVEALVDLGKSLSRILFSAGLGWVKGEVISRTILAPLAAALWPLSLLKVGNILGNSWRIAFNLSIKAGEALANALCVRAQGMRPVTLIGFSLGARTILECLLHLADRGETNLVENVIVMGAPMPTDAKLWLKMRCVVAGRFVNVYSASDYVLQLVYRVNSAQSTAAGLGPVSLDSNTLENVDVGDLVEGHLQYRWLVAKILKERLGYDNISDAEIQSLAVQEEKYESKQRTYYSQKEQEEEIEQEVLFDASSDTELAIQKKEDEVNEVRENKK Q9US11 YK67_SCHPO SPAC607.07c; CHAIN 1..143; /note="Uncharacterized protein C607.07c"; /id="PRO_0000304113" MGTFGIVALSIICSIAFLFVAYGVLRLINSIRRRNMMTADVSSVKSSQTWNFLKNPFSNSAKFEALDADDMWDTRVEEAELNTIPSASPFIDHTSETVPFVNTEAPPPRLSSSFSRQSGENAETQSQVSASPFNDKNSPYVQE Q9US13 RPN9_SCHPO SPAC607.05; CHAIN 1..381; /note="Probable 26S proteasome regulatory subunit rpn9"; /id="PRO_0000173869" MDTEMSVNMSDFLHDQATRAPESLQQSYILMEDLYERKLWKQLTDALIVFFDTPETVPLRLPLYTNFVNSFRPNINQLKAVYMGLKAFESCSNDEALRNLNQIVNELDEEKYKDAYVYSIVAIARIKLISGKLDEARELLVKASKIIDHIDYVESLIHSSYYSVSADYYKAKADYAQYYRHCLLYLSCIDLDKCSHTELVERAVDLSVAAILGDIYNFGELLLHPVFELLVGTQHEWLHDLVIAMNVGDLPLFERLMGQINKMPLLQSSVALLGQKIRLMALIELVFQLPPNQRTLTFDTIARATRIPSNEVELLIMRALSVGLITGVIDEVTQIVTISSVQSRILNHSQIASMESRLREWNQNIKNLSNVVEISGKGVFV Q9US15 YK62_SCHPO SPAC607.02c; CHAIN 1..231; /note="UPF0653 protein C607.02c"; /id="PRO_0000350765" MPTKTKKRSVLEAERKKIGLDHAPKEDESVDDNFPKQFKRLLQQKEYHESKKKEIKKGNLKNKKKKDYGKIQRLPGERLSEFSQRVNKAIPVSFKSGPSKIDEFTDKKEKKKIAKRKEKRERDWNEIEENFEDKTWEADTTGQFIQIESRKKRKNSPDPWANLQTKPSFGETVQAPPELPELKIKETKYLENVPKVNNMGQTESMARRQALGKQRLELIEKYRELMKTKRK Q9US20 YLD2_SCHPO SPAC1851.02; CHAIN 1..279; /note="Uncharacterized acyltransferase C1851.02"; /id="PRO_0000317312" MGFIKSTLLATVTVFVGLCGINRFFTLPKCIRYHFRYFACHTFLAISSAYGVIASVVARLCGYPVMGQYLTAKAYYGLASTILDFRFKIENEEILRKHKSAVLVVNHQSELDILAIGRTFGPNYSVIAKKSLRYVPILGWFMILSDVVFIDRSRRSDAIQLFAKAARRMRKENISIWVFAEGTRSYSLKPCLLPLKKGAFHLAVQAQVPIIPIAIQTYGHLFHPPTKVFNKGEALIKVLDPIPTEGKTAEDVNDLLHETETAMNNALVEIDDYGKVKKQ Q9US28 YKA1_SCHPO COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; SPAC1783.01; CHAIN 1..583; /note="Uncharacterized FAD-binding protein C1783.01"; /id="PRO_0000310845" MISHVLVKDTSCLKVRTSYKCFVKYFPKCSVQSSFHSYDELAFSRRLYNLPRTLLNSRYYSNHSHGLVHGSKSPPSSQFLVPSFLQFNGQLKALCNNSAFQALPIKLSDLQKHWPSLKPHPLPPKRVSLGIPSISNPPVDTVISDSPTSPHPPSFVQPHPPYGIFAAPILDVRVLTNPGAVKRTYNLCLDISKYPLLEGKDWKIGGSFGIMPPNSDAEVLHLAHLLKIPQHELYVTKVLRTNGGRWPTIWGEDKPRCLYTSLYHIFKWCSDFISKPPTKSLIRLLAEHTLNPVEKSVLLALSDFRQDESYCRICTQSCVTLPDILEAFPSCHPPVDHLISALPQLMPRWYSISNDPSLANKRLEMAFTVQEYHSPNGQSRTGICTGFLEDLALAFLKARHDGSLANKKFTVPMFRGVQQNPFAKEFHNDGPMCLIGAGVGIAPFRGFVQRRLANAACTGKVWIIQGCRDQKLDELYHGEWNTVPGHHKNPKCRAKKLVVESRNGRREYVQDAVRRHGDVIWDVLSHKNGRIYLCGSGNSFVSEIEKALMDVAMKYGKLSKEEAQKELKNWQKPMNCKLIKEVW Q9US30 RT19_SCHPO SPAC1751.02c; CHAIN 1..93; /note="Small ribosomal subunit protein uS19m"; /id="PRO_0000130024" MFWTSVARARSVWKGPNVVDFGVNVQQCIKGNVPIKTAVRSATILPRMVGAQFMVHNGKSYANVKITEDMIGHKLGEFAPTRKAFHYRQTKNR Q9US33 SAT_SCHPO CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine; Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30; SPAC1039.08; CHAIN 1..270; /note="Putative serine acetyltransferase"; /id="PRO_0000339409" MTVQTAERTITLVQAIWPKLRKEAEKQCEVNPWLAKDLARKILSKKTLRESLSCVLALPLDHVTGSSESMENWFYSILGLNDEKIIRSAMIDLDRLYTTNPACPDLISAFLSFRGFHALQLYRIAHGLWSEGDKTSAVLVQNWTAVAYGVDIHPAASIGDGLFLDHALGIVIGETAIVEDGVSIWHNVTLGSTFKDSGARHPVIRKNAMLCTGATVLGRVEVGENAVVAAGALVTKDVAPNRLALGSPARDVGPVPQYFGALTNPNCTNK Q9US34 YFZ7_SCHPO MOD_RES 280; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC1039.07c; CHAIN 1..448; /note="Uncharacterized aminotransferase C1039.07c"; /id="PRO_0000358867" MSSHVSNNSILDPVTFWNQANKSLIRYGGDFAPKIIVRAKGCCVYDEQDNAILDFTSGQMSAILGHSHPDITACIEKNLPKLVHLFSGFLSPPVVQLATELSDLLPDGLDKTLFLSTGGEANEAALRMAKVYTNKYECVAFSSSWHGVTGGAASLTFAAARRGYGPALPGSYTIPEPNPKLSPFRDAKGNYDWQKELDYSFYMLDKQSTGSLACMIVETILSTGGIIELPQGYLKALKKKCEERGMLLIIDEAQTGIGRTGSMFSFEHHGIVPDILTLSKSLGAGTALAAVITSEEIEKVCYDNGFVFYTTHASDPLPAAIGSTVLKVVKRDNLVEKAKISGELLRSDLLRLKDKHPLIVDVRGLGLLQGIEIASCTDPSKPSDFLGTVIGDKCLELGMNCNIVHLRGIGGVFRIAPPLTVTDEEIHKAIEIFDSALTFTAKEFSGSY Q9US37 YFZ4_SCHPO SPAC1039.04; CHAIN 1..507; /note="Uncharacterized transporter C1039.04"; /id="PRO_0000372720" MEKSISSISKASMNSDEKLDKKEWDQQLPIDFGEGEDVTTEVYILDHKAERRLCRKFDFRILPLLALLYLFNALDKSNVSNAKTNGMDKDLGFVGDQYNIMISIFYIPFVLCAFPFSYLYKRFGAARILPFFMLSFGAMSLCQAAVKNFGGMMAVRWFLGMAESAVLPGVVYYLTTFYRRTELARRLAIFYAAANVSSAFGGLLAYGVFHIKGGKLQGWQYLFLIEGGVTFLCAIVIFLVLPVSVETANFLTDEEKTLAKMRIENDSSSAISEKLSFKQSLTVFKHPIAILWLLEEMALGVPLNSINNWLPQIVAAMGFSSVNTNLMTVAPAISGAIWLLVFAFISDFLKNRGIVLIAAISTTMIGFIVYGSIDIMNHIGVSYFACFLMTAGAAASSVLTSTWYNNNTPNESRRAVFTSVGVPLANVMGLVSANIFRPQDAPKYVPALGITAGFGGLGILLVASISVYMFFDNRRRDNAQGVKKTFADVSTKDLGEGPANPNFRWFL Q9US38 YFZ3_SCHPO SPAC1039.03; CHAIN 1..341; /note="AB hydrolase superfamily protein C1039.03"; /id="PRO_0000363393" MSQTTTETIIPLDSSVKDKLDPEYVNFYNKYVCSNLPIVKTHTYPVDFLRNNGNVMPGQSELLPVESTEDITIPRKHTKAPSGVPSRIFRPHGTAPEGGWPCFLWFHGGGWVLGNINTENSFATHMCEQAKCVVVNVDYRLAPEDPFPACIDDGWEALLYCYENADTLGINPNKIAVGGSSAGGNIAAVLSHKVAASPANFPPLVLQLLVVPVCDNTANAKTHKSWELFENTPQLPAAKMMWYRRHYLPNEKDWSNPEASPFFYPDSSFKNVCPALICAAGCDVLSSEAIAYNEKLTKAGVESTIKIYEGCPHPVMAMDAVLEKGRILNKDATNALLAAFA Q9US39 YFZ2_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPAC1039.02; CHAIN 25..601; /note="Uncharacterized protein C1039.02"; /id="PRO_0000014201" MKLSSLPSGLGLASLLGLISSATAYSATDLTTMYDWNQIIKPLEWGQLNFIHTTDTHGWLGGHLRDARYKADFGEFKSFALRMKELADFKGVDLLMVDTGDLHDGNGLSDASDPQGIYTNNIFTYLPYDILTIGNHELYQAAISNNTHEYFVPHWNGTYLASNVQIYNSSNELEQFGGESTYFITKHGVRTLAMGFLFNFSSNANNTVVTPVETAIKSEWYQQQINRTDVDLFLLIGHIPVRDYDEWKSLHASIRKVHPNTPIQILGGHSHIRDFAVYDEASVSLEGGRYCETVGWLSIDGLSASNATRQYVGRPVTNETRQSYPNLPKPATPLYYTRRYIDFNRQNFRFHTQQSEDSFDTPEGVELSKVIKQYRDDLNLSYVFGCIPKNYYMTEVSPQAEDSIFKLMVDHILPEVLVNENRSSVPHIIISNGGGVRGSMYEGTFGPDEMFQLNPFLTNYYNYIPDVPYKYAKKLYSILNGGSTLRNVNDYLAALNPGYVTSDDFGEDGDDTVHTYVSTYAVPNVLQAQVGFNTTSAPETVDVVFLNYFQTKVLKALNTMVNETIYTLSNVTQYWVREDGKDSSPYMFAQYVQQEWSDYCD Q9US40 YFZ1_SCHPO SPAC1039.01; CHAIN 1..567; /note="Uncharacterized amino-acid permease C1039.01"; /id="PRO_0000054171" MSSIMEKTDVSSSKHSFTFEPSSDEVGKAAEIVDTHENFYDDQGDIDNPEELAELGYKQEFRRQLSLFGIFSISFSVLGMLPSVASTLVFGLWYVGYPGLLWAWLIAMFFLICVSMSMAEICSAMPTSGGLYYAAAVFAPKGWGPLASWITGWSNYIGNIIGQPSVNSSAASMILGAVTVNRPDFVIQRWQWFLLAVAIQCFNCVLACLPTRIISRINGVATYLNTAFLFIAGITILAYGGKNHNFVKGTKIWGDYINTTQWPTGFAILLSFNSPIWTMSGYDAPFHLSEECSNASVNAPKAIVMTAVIGGVVGWIMQIIVAYTLTDIDSVMNTSGSMWTAYLVQAMPPKAALGILSLTIISAIIMGQSALIASSRIAYSYARDGILPFSGWIGTVNPYTQTPVNAVICNCIISILILFLTFAGTVTLDAVFSVGAVAAFIAFTVPIAIRVFFTKDADFRRGPWNLGKFSRPIGLLAVSFVALMIPILCFPSVKNPTAQEMNWTCLVYGGPMLFTLVWYAISARKWFKGPKASAHYKRPGEESSDIVEGVQADIPSSSDQLKIKGDL Q9US42 URG3_SCHPO SPAC1002.18; CHAIN 1..399; /note="Protein urg3"; /id="PRO_0000116802" MSTETVAKLLSLQDIRYKAQKVLQKAESQSLKSFLYDPSKLPEVADFVVSVIQADFKGKYSTIPPHGRWQHFEVGNVPRLSQLVSKWEKEGVDSLEICKRVLDVTFVSVLLDAGAGDVWKYTDGKEAYGRSEGLAVASLRCFESGLFSSNPDFVYQVDGKALQALTSEKLGAGFQVTEQNPLAGVEGRATILRSLGKQLGSGRPSDFVGRIFPTGDFSKGLNVLELWSELQTLLIPIWPVRTSFEGQNLGDAWYLSTIDAIQPFHKLTQWLTYSLLIPFKSLLKVPVVNEELLTGLPEYRNGGLFVDLGVLTLRPEFSYATEYEPSSVTIVEWRAMTVVLLDKLLAFVNERLKPELSEPLSLAQMLEAGSWKSGRIIAKKLRPSTAGSPILIKSDGTLF Q9US44 YIZG_SCHPO SPAC1002.16c; CHAIN 1..499; /note="Uncharacterized transporter C1002.16c"; /id="PRO_0000372722" MKSLSHTSSNKSNGSIFTKADESEKVISRSNTASPISIENTHLTKSERDSLLFRLDLVLAPTIMILYLVAFLDRSNIGNAKVAGLPEDLKLKGDQFNIIASVFYVTFILFEMPTTLLMKKVQPKRMLAFIVISYSLTTIFTGFCHNFGGLLAARLVLGFCEAGLFPCLALYLTMIYSRVELAPRIAYLFASSALSGAFGGLFAYAVLHMDGVGGFAGWRWLFIIEGLIGFVCGVAVYFIIPNDITKAWFLSKTHQEMMRKRQLERAADLEAAHFDWKGVKSAFTDFKVYLYALSEFGQDTCLYGFSTFLPAIISGMGYTSLSVQYMTIPVYILGAATYIAASFLSDRFHHRGIILIIGNIFPIVGYILLLACQNNKSVLYFACYLCSVGVYTGAGLNVTWLSANIAPHYKRATAISLQLAIANSSGILAGQIYRYPPKYIAGHLTSLIAIFISTVLHVVNIFFLKHQNSKKQKSLASSSTIDLSEQPKDDKDARFHYIL Q9US48 GAA1_SCHPO SPAC1002.11; CHAIN 1..581; /note="GPI transamidase component gaa1"; /id="PRO_0000316598" MSLFTFVQIRVFPFLQRHLFFLQLSLTLIGLSWIFILPRNEIIDRLHVSESALLPGQVNTYFENRYSKTVSSSLTAANTWSHLDASVGTNTMYDDLEQIFTAMGLPTQKQNYSINIPGSEFNGSNFITTLRAPRGDATESLLLCVPWKDHIGQYNEAGVALAISLLKYFQGWSLWSKDIILVIFDDPVYGPSSFLTSYFDQTTPYISYTPLKIRSGSIQAGLSLELVTTENNSDVLEVLYQATNGQLPNLDLFNTISRIFMQHFNYPLRLQGYDFHANSGSSYTSRLKSLWMGMLTQAVSNVTSAHALFPQYRIDMLTLRMKVKDPFSFDMFRFGQAIESTFRSLNNLLEHLHQSFFFYFILDHLHFISIGNYMPSILILAASFMLGAYRHWINHEKKIDLWRPFSFWLFSIFCTIAAYYLVSSSTKITVFIFLYLMLTFIGIIFSTFMTSEDAELVLSYDLMSKSLFISVVSTLNFSLSFVVAILLVPLQFISFRFNRRLSLLFAVLTYFSTFIFLCSLSKILNGPLVPFWLWAKEYELFNSWLMPSVFMILVLPEIIFSVTSFFSLWNEPSVKTKTKTL Q9US56 MUG31_SCHPO SPAC1002.02; CHAIN 1..229; /note="Meiotically up-regulated gene 31 protein"; /id="PRO_0000278496" MASTFSQSVFARSLYEDSAENKVDSSKNTEANFPITLPKVLPTDPKASSLHKPQEQQPNIIPSKEEDKKPVINSMKLPSIPAPGTDNINESHIPRGYWKHPAVDKIAKRLHDQAPSDRTWSRMVSNLFAFISIQFLNRYLPNTTAVKVVSWILQALLLFNLLESVWQFVRPQPTFDDLQLTPLQRKLMGLPEGGSTSGKHLTPPRYRPNFSPSRKAENVKSPVRSTTWA Q9USH0 YJH4_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPCP31B10.04; CHAIN 21..287; /note="Uncharacterized membrane protein P31B10.04"; /id="PRO_0000353807" CARBOHYD 120; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 154; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 166; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKVICGSVFLFSLFFQVVLGDYFSSSSGNPNLRTTKVYTVVSGTHLATAESTVSKTITTTKGLPTNAYYNCVPSKYIQSDIPMCAPNQGDRWVKGRKYKVSWDPLYFGVDNLLMVVSYLNDSGLIAATKKVQNSKGEIMLKANKGWLHDDSFQNVTIDLVTISENNMTLLTGPRILLAKDLDSATAAAENAAFYGPRRNIKAAIAVPSVILGLILVALVYYAYRKDTWKIYMAKIRIRRSAPGYGVRRSRRQRMQSRPVAYTSLPADAHFEDSDDEDYYQSQVKKFH Q9USH2 YJH2_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPCP31B10.02; CHAIN ?..143; /note="UPF0651 protein P31B10.02, mitochondrial"; /id="PRO_0000350762" MHLTLFKELLKQPKPKFHFEIEPNVSFLAVEEGPASLRSYSIGNVSRIYDGIRVPPKPEEPLNCCQSGCAICVWDVYADDLEEYNRARRKAKRHYLDKHLPVPPDLAKVSLKETSSLEELPPQLKAFVLLEKRLMKDKQSKNN Q9USH5 YJQ5_SCHPO MOD_RES 86; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 291; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC825.05c; CHAIN 1..301; /note="PWI domain-containing protein C825.05c"; /id="PRO_0000317318" MSGFYKGVAAEQETLFTTADKKLMRSTKFPASYDTKVDMKKVNIEVLKPWIATRLNELIGFEDEVVINFVYGMLEEAVEASKTSDSQNESTLDPRKVQLNLTGFLESNATAFTEELWSLIISASQNQYGIPEKFILEKKEEISKLKDRTEASKEESKTVTDHSNRRESRRESTYYDSRERNGKRTSRSTLDRKRFHDASDTERNRYGRSPSPHSRFSEKPRGERYDIRSYSRSHKERYEDRYRPTRRRERHYRTRDDEGFDEFGRSRDGRWRESRTSYREKHRYDRDALSSESDSGTQKHD Q9USK1 YJ2B_SCHPO SPCC4B3.11c; CHAIN 1..116; /note="Uncharacterized bolA-like protein C4B3.11c"; /id="PRO_0000316213" MKLAIGRLLSPLFLKNPQKPLIITKRFYSTPGERRIKDILTEKLSPSSLRVIDVSGGCGSMYQVAIKSKAFQGKNTLAQHRLVNSILKEEIRNMHGLNLSTEVEDDISAGGSTTSS Q9USK3 YJ2D_SCHPO SPCC4B3.13; CHAIN 1..539; /note="Uncharacterized transporter C4B3.13"; /id="PRO_0000316589" MEGENDPLLGSYKPKRRRSSLVYGLSRPQFLDTAASEVSPIPQERPTTSLRKPTPRVQRPATDVSYGALEETEENESIASGLSVQEDFNSKAWWKELTLLIKFATPVVLTSLLQYGEVVTTVFSLGHLGKTELAAASLSNMTATITAFAIYQGIVSALDTVGTQSFGSGNYEMVGLHLQRILAILLLIQFPIFLIWWKIEGILLFLRQDPLTCMFAAKYMRVMMLASPAYALFEALKRFLQVQGIFHPVTYILAIVVPINIFLNYLFVWSPWVGFGFLGAPVAVALTLWSACAVLIIYIMKVNGRQAWGGFSREALKNWGPLCRLAVPGVIMICSEYWAFELVTFASGVLGTTELASMSVLSTTSTLSYNLAFGVAAAAATRVGNLIGAGNTKLAKLATHVSINLGAAIGVIIAVILFLTRNTWTYIFTSDKDVVALVATIIPLVALINIADNTQCVAGGLLRGQGRQRIGGVVNFIAYYLLGLPVAIILCFKLDWGLYGLWIGIGAAILIIAGVETWCSLHVNWDHLVELANRQFDEA Q9USK5 TIP41_SCHPO SPCC4B3.16; CHAIN 1..252; /note="Type 2A phosphatase activator tip41"; /id="PRO_0000247902" MQKQDDFSFKYWTIKVQRGSILKSHEMENLQSTLGFPPPEMTFGNNYISIEYKNQPVVGFFTEDALKMVGTKPEDVMQVSFAKDWAKSRIKPGEEYPVIYPFDWTYYTDYQGTIQRPNAKFIEIDQVIPVQKILNAGQNLWFNEIILFEDELADNGKSMFDVRARVVQGHLILLARLVVRLDKVNVRLNETRIYIDLLNDFLLKDCRKKQATYDKIIKQIPVGGDKAALLDDNNWLSERLDTVDHKIYKLNF Q9USK6 CBP3_SCHPO SPCC4B3.17; CHAIN 1..283; /note="CBP3-like protein"; /id="PRO_0000206559" MSRCCLNLPLRPAFVKQPVWGKSIYGPLRRRFSFSPINVINHSPSETKRRDPVEELRYKPLTPPQDPRKVAPPNSFLKKISLIYQKYISPKQNLYYEATGTARYMYFEAARQATPEKNSLGAFEFWYQKCEIPMTFQSWFQITQLHLWILHTRIRGLPKNEKVAFSQALTTRFFEDMELRIHKDYRINSNRISGMYLKDLFQQQTGAIFGYDQGMLGSDAVLATSVWRNLFVGRPDVDLVILETIVKFIRLNVYRLSCLSTDDFINGKGVHFVPPEESAQTNI Q9USL1 THOC3_SCHPO SPCC18B5.10c; CHAIN 1..309; /note="THO complex subunit Tho3"; /id="PRO_0000316563" MCASVTESLPKFPELKTRDLQGQQGPIRSLGWNLSGSRLASSSSSGSVLVWNSDRLDFKFTTELGNRGYGLVEQLVWDPTHSDRLMAVYAGKMIRFWDFRSAKPIAEIESNYENIYATWSPSGNYCCASSRDDMLSFIDARERRIMETFQQPCETNECCWSFSEDLFFMTTGLGTVQIMEWPSLKRVYDIKAHNSNCFCIEFSPDNRHLAIGGADAITSLWDPQELICERSITRMDYPIRTLSFSYDSRYLASGSEDRYVDIADTKTGDQIWKIPTNGPLNKVAWHPTKHILAYAVSEPNSSGLKIFGL Q9USL2 YJK9_SCHPO SPCC18B5.09c; CHAIN 1..116; /note="Uncharacterized protein C18B5.09c"; /id="PRO_0000116814" MEEKNTVSLSKHIERPVEVVESHSTYILSAQGLYLTERVLRSYFKQPDLIITWKDSMRAYLTFSSPQEAQKAYLDSLRWGSQLNAIIKPFYGSHDEVLRLCKRKRIIPLQNFLTSG Q9USM7 TIM23_SCHPO SPCC16A11.09c; CHAIN 1..210; /note="Mitochondrial import inner membrane translocase subunit tim23"; /id="PRO_0000210306" MSWLFTRNKEEEPTSKIDSSELQVPTEATASDILSGSEFDPAKLHPLADLDKPLDYLLIEEDALSTLPGDSMAIPSRGWQDDLCYGTGTSYLSGLAIGGLWGLNEGMKKTKDITSTRLRLNGILNGVTRRGPFVGNSLGVLALVYNGINSLIGYKRQKHGWENSVAAGALTGALYKSTRGLRAMAISSSLVATAAGIWTLAKRSFTKRLN Q9USM9 COQ10_SCHPO SPCC16A11.07; CHAIN 1..164; /note="Coenzyme Q-binding protein coq10, mitochondrial"; /id="PRO_0000315896" MAFRCTLRRLECYRASRLMPYKPSFLFSLISNVNEYERFVPFCQKSKVTEYDPKTGYPTKADLTVGFKGLCETFDSKVVCDPVALTVLADASHHRLFRRLKTHWSIEEASRGRVRVDLEVDFEFASKLHGMMSKFVGSSVASEIIQGFVQQAKIKHKLESENEK Q9USN2 YCL3_SCHPO SPCC16A11.03c; CHAIN 1..466; /note="UPF0652 protein C16A11.03c"; /id="PRO_0000350763" MSIAQLFNQSWVEKSKYVPVRLSDEERKILSLLEAALEVIDYTGHVDIISYTTRTKLMVKYLNEMCSIVMGLVTAMDIKAGRDLLIGRDHKSNARFFQTVFEIGRRYKIMNPEKMRATYGAVMYMCQDSLIPDVRSQLGFDFVSPIKTVYNVLEKHKLLGLLEEKQLLNNLLKQSDPQSNANAKAELLKEREEASETLLKKYNPGKDEKLQKVLTDCFASLADHEAFLLANRNPVEKMRAYLHKFFNPHDTKNGSLKIGYMTGAKLNHDHKTQFFYVDQSLVFWSCMMDQMFLLWLESDASLLDKHSRYFISDTGQGLNRVQLCPLVRSTVTRILSSVQKQQEIPWMGSSVIHLGDRDVPNALMFIDKYRQVPHILAPLVKVLQQLEFLRDPYLVQYIENEYGSVNGLQKTILLDFFRHGFNGQGSDGGSCIDGRLTSAWNWTNEITKKKYYRILLMSGFLNFEGI Q9USN3 UTP13_SCHPO SPCC16A11.02; CHAIN 1..777; /note="Probable U3 small nucleolar RNA-associated protein 13"; /evidence="ECO:0000305"; /id="PRO_0000223893" MAPIGEKKRFELEKSIEPIYTGGPVAFDSNEKILVTALTDRIIGTRSETGERLFSIKKDEDDYVTALAITSDSKKLIAAFRSRLLTIYEIPSGRRIKSMKAHETPVITMTIDPTNTLLATGGAEGLVKVWDIAGAYVTHSFRGHGGVISALCFGKHQNTWVLASGADDSRVRLWDLNSSRSMAVFEGHSSVIRGLTFEPTGSFLLSGSRDKTVQVWNIKKRSAVRTIPVFHSVEAIGWVNGQPEEKILYTAGEGNLILAWDWKSGSRLDPGVDTTHSETNAIIQVVPFSENTLLSVHSDLSLLLRKRVPGEGFITIKKLNGSFDEVIDCAWIGDDHLAVCSNTEFIDVISTDGTQVFGVLEGHTDIVLTLDSSEDGVWLATGAKDNTVRLWNLNIEDNVYKCIHVFTGHTASVTAVALGPLDVNGYPTFLASSSQDRTLKRFNLGSQLNKSDFSNRAVWTIKAHDRDVNAIQVSKDGRIIASASQDKTIKLWDSSTGEVVGVLRGHRRGVWACSFNPFSRQLASGSGDRTIRIWNVDTQQCVQTLEGHTGAILKLIYISQGTQVVSAAADGLVKVWSLSSGECVATLDNHEDRVWALASRFDGSLLVSGGADAVVSVWKDVTEEYIAKQAEELERRVEAEQLLSNFEQTEDWQQAIALALSLDRPHGLLRLFERVMTAPHQPNSITGNKDVDNVLVQLPDHQLIILFQRIRDWNTNSKTSMVAQRLLRLLLHSYSPEHLLKLSGIKDILDSMIPYTDRHLARVNDLIEDSYIVDYVI Q9USN4 YJA1_SCHPO SPCC1529.01; CHAIN 1..491; /note="Uncharacterized transporter C1529.01"; /id="PRO_0000173446" MDLEKKPQDKVETAEIDVKEDPFLVTWQSPTDPKNPKNWIYARKWTQLILVSAFALLGPMASSMVAPCLDQIADRFHIQNSTEKALILSIYLLVFAISPMISAPLSEVFGRRMLLQVGNVIFIVFNMACGLARTKAQMYIFRFLAGFGSATPMGLGSGTISDLFTPDERGKAVAVMSLAPLLGPTIGPVVSGFIAEYTTYKWIFWSTTIFSGFIFALSLPLLAETYPKTLLGEKARKLNKSEKTNKYHTEWNLEHIPRLKLVTPALMRPIRMLFTQPIVILCSTYMAIQYGILYLVLTTYPTLWTEEYHERPSIAGLNYIASGIGLIFGSQASGIFIDKTFRYLKRRNNGKMAPEFRVPVILLGTFFFPAGLFIYGWTAQYHTHWIGPDIGAAMFNIGLMLGWRGIQTYLIDSFMIYAASSTAVACCVRSIAAFAFPLFGQDMYDTLGYGWGNSLLAFIVLGSSIITCSLLWFGGKRLRALSSMVIFKDDV Q9USQ8 YN1B_SCHPO SPBC577.11; CHAIN 1..239; /note="Uncharacterized protein C577.11"; /id="PRO_0000352827" MQQDLFGSDSICPISSDDVLKATDPNFESWRERIVQDALKIVEQIPKWKHLGNHDGVALYEKAPAYTGHTWYGRVSKHTRSLKTFKKGLLYEHIKKEADYDPLVFSAHQLETIIEDEIEIWMYKYKTPWFFRNRVYRQLVVSVMLDPDSFIVLQTPVTYPGSSSGGGNGVVALYDSVDFVSKKLDGDGKEEGVLWICAVRNDYGSMFSGLFSDTTFTKSLVRQVKLYNEWLNRTYPRKG Q9USQ9 PSB7_SCHPO SPBC577.10; CHAIN 1..262; /note="Probable proteasome subunit beta type-7"; /id="PRO_0000148072" MSFLELTEVWGKPQKDIFFPSGSEVEESTDAPIQRTVQPIVTGSSVLALKFADGVMIAADNLASYGSLARFYDVERLTKVGDNTIVGAGGDISDYQQIQRLLEKLEIKEGNYGDGYALQPSYIHEYLSKVLYARRNKLDPYWNQLIVAGVDGENKEPYVAFADLRGTTYSAPAIATGFAMHLALPMLRKATDDDRWKTLSKESARATIDECMRVLFYRDARSLNKFSVATITPEGIEFQTDQSVSSKWAFAEKQYGYGTQTV Q9USR6 NAT9_SCHPO SPBC577.03c; CHAIN 1..216; /note="N-acetyltransferase 9-like protein"; /id="PRO_0000310301" MKINQNTTVDCGNLILVPYQKCHVLKYHNWMKNEELQELTCSEPLTLDEEYQMQASWSTDEDKLTFIVLLNENDEAKKPSILDHVKAHSVESMIGDVNMFLTEEYADGIEEFDDSPSDANATNATKESEVHIVGELELMIAEPQNRRKGYGTKIVDAFLHYVESSGIAKNKQILKYRVKVGSQNKPSIRLFKKLGFSQVKYNAYFDHVELELMRTS Q9USS1 YOA5_SCHPO SPBC557.05; CHAIN 1..433; /note="Uncharacterized protein C557.05"; /id="PRO_0000303892" MDLWKKGKRFFRFSKEPVITCINTSYAGKEIIFDLIANPQMETKDVNLTLDFDAPIFHRKAGIDGLLTLTNKSKVNEIQLISIEVFIIGICKHKFHSSTVFLCLGTHIMEGQYIVPEELLDYAKKRGKNRIISIPNHSTVDIPFQVNFPKHVEVGPGRQIHSRVKVQYFAYANIIYQSADKLRSRRECQEINVLPSISPSSFLDSPSIMCVSKQPDLKKDRQRKSATRITVSLPRTDWLAGESVVSKIKIENHSKSSIKTLKLCLYRRIIGFDPPSWKTQQMMSHLNLSRKNSEVSKTCKCLQKETIRCNKKSNCYNWNGIAALETYTTECHIQIPDKEATITVGSNFEVDHFLKISVGNKLWTLNRVEIPFKIISANSLSLEQENVFLNLEKLTNKASPHGLPISVRLGNSLSYDALSAARRMRNTRYFLYS Q9USS4 YOA2_SCHPO SPBC557.02c; CHAIN 1..203; /note="Uncharacterized protein C557.02c"; /id="PRO_0000304065" MDKKIADLLQELQSSSNVTSNQLENVDKSSIPLSKARKPSDFELNNSIEDAEKIKTYPAALRYIFALNSRHPEKLQKLRKMKAMQERQERNWSLERQRLVQHFESKTKLQEILKPLSSDPKLKQPSNCLNDQTNNDSAQTLDDNRALQEFDEQVVQLTNRMYKEQLAILADLKIPLFLSVNNDEELSEDQKRLLQLLQDLLGA Q9USS6 PPA4_SCHPO ACT_SITE 35; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q9NPH0"; ACT_SITE 330; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P15309" CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000250|UniProtKB:Q9NPH0}; SPBC4.06; CHAIN 1..462; /note="Probable acid phosphatase SPBC4.06"; /id="PRO_0000311719" MSQMSSASVKFPDSVPGVDYPKQLQLKYLQVIFRHGERAPVKERLGSAGIPKDWKLCNNARRFFAQIKGEKEWSVLGFERKVESPVDTSLAAPTSDNSPSGVCIHGELTDFGRVTTRTLGEYLRERYVKQLKFLPDELNNYADVYMRATPMVRALESLEHVFSGLYPESKRKMGLPVIFTRNWSDENLLPNENNCPRLVQLYEEFAERAAKLYDPLLAGRASEMMSQFMNGQPVRVVSSHPRLSGLLDTINAAIGSHVDFNPNLRDEQWLRDAETAVVEEWFGGYKVSKLMRQLGAGSLLNDLSMRMENFVVAEKNGSPYHRLALYGAHDVTIAAILASLDAFDYRWPPFTSHLEMELFEDTSSKSDSQNQSGDNKTTDLKLFSDESTDASNSAIVAASNSARDMSDWYVRITYNSTPVVMGACRGQGYKGNDTICPLSIFKDTVRALKPVEYHTMCKPVKK Q9USS7 YNB3_SCHPO SPBC4.03c; CHAIN 1..891; /note="Uncharacterized protein C4.03c"; /id="PRO_0000205161" MAYPGQFGNYGNPETYRQNVAGNIASYGGPEIDTQLAAQMNAQMYIQQGSAMAPQPRRARRHKDAHAYDMSLTDAEPALAPVMSPAIPPSMNYPTPSTPSVLPESFSNDTNLLDPAALPSAPEVRYEDQQLFKNQIFNTMEKGSPPMSTTDFVGYEQGNSSSKFVQFTSYAIPATNDVCNASGIPLGMIVQPFAELRPDEAPVPVVDNTNSNPPRCKKCRGYINPFIQFTMASSKWTCNLCGSENSFNDDGFNPLVGSQHDGVESRPELNVGTIDFKVGKDYWIKEDPPKPARFVFMIDVSYEASSKGLPKVAAEAIRNILYGPVPLDPNVKIAIVCFDRSVNFFNLSPNLEQPHMLAASDLENPFVPFSSGLFVDPIASKVVIERLLDSFPAIFQDVKIPEPVVGNALEVVKLLLKETGGKAFVFVSALPTMGLGKLRHREDQRLYGTSDEKNLWNTQDKWYTSLADEYVTAGIGVDIFFTATAYVDVATVGSVATLSGGQIYHYSNFVADRDGSRLKQDLFRSVTREQGYRVMLKTRCSNGLRVSKYLGNFLQRTPQDIEFGSLDADKSVTVLFSYDGKLNGALDAHFQTAVLYTTPSGERRVRVVNYCCAVTSKSYDTISLAIVEPIVAVLAKIASTNIAAGSLKDTSVRLVEGVVKILSSYRKVAANRLTPGQLVLPKNLVLLPILILAVLKSSAIRSGSIHSDIRVSQLREVRAAPIQELMLNLYPNIYALHQLQPTDCLPDPENTGCLPINMPLCVRASRKFIEDGGAFLIVTGQKSYLWFHQRTSPLLLQDLLGVESLEDIDSLKALELPTLDTVLSVQVRNLLSSLRMQFPSMALHPQIVRQGLDGSEGEIFSTLVEDNTREGFGYLDFLTKIHESLHTQGYK Q9USS9 DNI2_SCHPO SPBC4.01; CHAIN 1..248; /note="Delayed minus-nitrogen induction protein 2"; /id="PRO_0000304045" MERGTSKFSWIGLVARIYNYIPHPSIFSNAILGIAWLFLIFLCCSCLTKSSIFARLLRVKNETTTVDVGFFGVCDQAINSTSRVCHELRNWDQTTGGLAYETSRFAWLQVHPVLLAIVVVFSTLSIVLTILKYLAPAYIRQWSISCLTTSTAACLLLALQMALAHISANSYAVGMNLTGKATAKFGVAAAVFGWISSGFFLLFSLIHLGLWTIERNKQKLFEETSLSFSFITTKLRLIETQYFICKDY Q9USV6 CBP4_SCHPO SPBC27B12.14; CHAIN 1..72; /note="Assembly factor cbp4"; /id="PRO_0000330137" MNRVVKSIVYGVGIVGFGYMTMKLTTPSPERVVNSLPPDLRASYEMNKKDRSQAEGVLRMIEDAKRNPKNLV Q9USW2 INP2_SCHPO SPBC21B10.06c; CHAIN 1..470; /note="Inheritance of peroxisomes protein 2"; /id="PRO_0000304024" CARBOHYD 204; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 221; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 385; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MNVDTQLSRDGLYSSLRTRYKVYISMHAFAIWHRFISFLAIYLWPCIMGSVNLNLQDRENEYFFDSIQYIIYTSELLVGDHELQRSHHEEQPSLVYPSSSFSSTSKFWRYFAYLLSLQIVIDFVLYKLSSAMASLHYLKFVKIIALSYICFSSLIRICHCWTYFIRIMGLSSLNKFVNLLHDFETTSNRVYSQICELEANSAANRSRLMDFLPANDPLLFNLTEQNTLSYELSGLYEKLLPRYQLVLSRIYPYAAASNLRNLLSLYRLPNCFGKLNSFDLRKGSSTSLKRSSMYLARKENQDFDDQSTQILNHIKTAYYELTIISKQVLCCILSFPVDSFLAERSSWLIVHREVGDLSNALSVSMVRLVDILKFSVESVNRNQHNTTSKPFPRIMCKENLRSLFNELHSVMMETHESISSYIQEGDNTAMQTYAMDEYDQVGLLLKDLLSEWDFNRALLLNLQHMHRKRK Q9USW3 YHZ7_SCHPO ACT_SITE 237; /note="Nucleophile"; /evidence="ECO:0000250"; ACT_SITE 242; /note="Proton donor"; /evidence="ECO:0000250" SPBC21B10.07; CHAIN 1..419; /note="Probable glycosidase C21B10.07"; /id="PRO_0000314117" MGIPDSTTDSRHSLSSAALSSASFENIYDPARKNESTNDVIDNHTDTEIDDHDNDHENLDSNNNNENNEAFNEKAAEKKLLPWYRRYFIWILIFIVALICSVLIGVLGGVLGHRTAVRDRHPSYKAKTYSLVKEYKGTTFFDGFDFMNITDPTHGFVQYLDRNSSAKLGLISANSSNVIMAADSKHNYSSGRPSIRLQSTQYFEHGLFILDLIHLPYGCGTWPAFWTLGDDWPNGGEIDIVEGVNVGTSNQVTLHTGDGCEMEDIKRVMTGTALQTNCWVDAPNSYNAGCGVENPSGPSYGEAFNKNGGGVFVLDWRSEGIRSWFFNRSEIPSDITSGSPQPAKWSEPVADFPDTKCDIDKMFSKQKILFDLTFCGDWAGSSVYSSAGCPGSCNDFVGNNPHNFTEAYWNIKSLAVYQY Q9USW4 YHZ9_SCHPO SPBC21B10.09; CHAIN 1..519; /note="Uncharacterized protein C21B10.09"; /id="PRO_0000116786" MVFKAHHRSITRQDIELEDLENAPASIASIENDTLEANVGSTPLTAKQKRNIYFLILLYLIQGVPMGLVRGSIPYFLKPNVSYSDLATYSLAAYPYSLKVLWSPIVDTYYCRSFGRRKTWVVPCMLLISSTLLLFSYNVDTWISKGSSYINSFTTWSFLLVFVCATQDIAVDGWSLNMLNPEQLSYASTAQTVGLNTGFFLSFTILLVFTSPEFANTFIRSIPSNEGLITLSGYIKFWAYFTFIASVLVCFWDESNHQEIANISDMWKTIRAALSLKNMRQLLIVHTLGKVGFVANETLTLLKATEFGLSNEMLSLIILINFPLGLALGVYTGRISNYRPLDIWLKGYWGRVVSILLNTILVYMVSNWKHRFPVFFPIFLCYTLNASFSTIQFVALGVFHSKISDPHIGGTYMTILNTLSNLGGSWPQYVMLRMADLLTVSSCSTAPHLTCSADAQKKECQALGGTCLYKRDGYYLTSIVGIFLAISICVSLITPVVRRLTKAPISSWHIHSKIAETYT Q9USW8 YHY1_SCHPO SPBC19C7.01; CHAIN 1..196; /note="Uncharacterized protein C19C7.01"; /id="PRO_0000116782" METNGSFSGARLVDGKWIIPESRRKDGSVRRERAVKPGYTAPEDIKRYRPGRGNFASLEKQMKKLQLSNDASTSKSIDRPPISELEKEKLERPLSNKKKEKNDHKAESLKHDYDSVGEKRISKDSVKHLDKTYSSIDSKKDFKYNFPKTQAPEWRRGAKPLSKTSEPSVYSEKMSKRENKKSINTVDKKTGYKEKE Q9USY0 MU131_SCHPO SPBC1861.06c; CHAIN 1..433; /note="Meiotically up-regulated gene 131 protein"; /id="PRO_0000118861" MDNQQRKVQGSSSNTFIKRAFQHLKSLFTVCFTGADYLESDIELICQNEIQPQGLEKLNADSSNFYCNSLTSNQSLTTSMEALDLSSSLTTPHADKLLKLSNLIAAKSFTTERKLSAAEFLDSREIHNPFTYGFLGILYGTSRTPYLHAQYANSFMSESAVPISIELNNREAKASMNLAEKNFPEGFEDFVSFLENPNIPLTVLLHHVMLYDLYSNNLKDAVWVAVTNYMKNLVGNYGYTELHIRAAQQMFGHPRFLLVHPEDIYCISGSSDWVCVSTQHFHCNIHVHSVSGNAIRKSRNPIIQDLSSICQNSTEFGWLALTHALRKKGAIFPIHAYLNFNAKLYEECIPPSILYFNKNDENINVGNIEDITNYMYETFINEASLCDKFMKRKHERIETPLSSQGREISNTLSRKRGAKGSNPFEIENMMPHA Q9USZ2 YNR7_SCHPO SPBC11G11.07; CHAIN 1..955; /note="Uncharacterized protein C11G11.07"; /id="PRO_0000116859" METLLSALATLYANTDREQKLQANNYLEEFQKSPAAWQICFSILNQDDSSIEAKLFAAQTLRQKIVYDFHQLPKETHIEFRNSLLQLFLAAKDSPRPLLVSLAVCMAAIALHMTEWHNVIADVFQACSSKDPSGRCVLQFLSVLPEEASDPRKTSLSWEELCIRVDELLRDNGPAVLELLVQYVDAVRASGSPSSADLGLVLTSLISWLREIPLDKVMASPLIELAFRSLDDDLLLEDAVEFLCALFNETKDVDETTDAILMLYPRLLELQPKLIAACDDPETFRALGRLFAEAGEAWVVLIARMPNDFLPLVNCIAQVAANDTELEAIKFTFAFWWDLKQMVELDVYAEARQLFAPIYLELVRIIVRHLHYPRTEDLAINEQMASNEVLFEDRDAEDRFRSFRHEMGDVLKDCCVVAGVSSCLVQISSQLIKVLKIKESGLPYYWQDVEAPLFALRAIGRMVPANEDQVIGSLFQILPQLPENNKVRYAATLFLGRYTEWTAQHSEFLELQLNYISAGFEVANKEVQSAAAQALKHFCYDCREQLVGHLSQLHMFYLNAKTYLAPDPLMEVAQGLAHIVDIQPVANVYQSVHSFLAPSLQSILLAQVKLNPTQAELEALADNIDIVTIFLSLVHPPSPAGELHPIVRLFQDIWPILSRTLDTFSDVLICERISKLLKNFIYTFKEKAIVTLPVITEALIKGFEKTQYGCFLWVSGACVRQFGVPEMDEQTLSAVWSFVGKQCTNMFYYMSNKNPKEIPDVIDDFFRLMMDALLANPQMVLESQMLESLIQAAMMSLQLEQQEPLQTVLNFLQDLLAFALHTPPYSLIEPLPDSLLKSLADLLLKNSQELYIILFNGMVFTFPRDNISDASAVLIPLIRLVFAADPSLCIKYMSNVLDQLPAMTIGQEEREKFLANFSKHCTSSEMPRLRAHLQDWTAMYRRRVLTPRAKLISDD Q9UT03 SLS1_SCHPO TRANSIT 1..41; /note="Mitochondrion"; /evidence="ECO:0000255" SPAP8A3.14c; CHAIN 42..677; /note="Protein sls1"; /id="PRO_0000374045" MVKGSLLNRNINALNCRCLAQKLTSWGLLNIRSIHADSNRGVVNSSNLIIIPPYKPKSKSVLRSPYLTSHYVDALAFKLVEDPTVHNTLEDVFQDIESYKPKSVNTSAKSFRQLVNTLEVAFRKEQLRKFAKVFHIKSSSLRKKEIIERILLDHWKLRIHGDAMDDMLAIKDVTLCPLEMFFLLLNNASALRDISQKHAAHVVINVTNNNIKIEAKKRDVAIVEELISGIFKHLKSKTIDVTEYYANIINKNAVLLSERCKAYIELSGKAQIKITTAFGNCSFDEIERKLLSFVMLFENTDKCLIDSECLTSKKSFTLNDFTYDFRLPWYLKDDSWKRWCRVKEYSWNTSVLSDEALTRNSLTLPVPIKPSINKDISSIEVKDLSQKNTTQSKKLNSYIRDSFHSVNDFWFSSHATNTEQCFTKRLTATFGYSLFSSSFLSHTKNPDVASFYVKERSKAHHFLFNTFVDQIPSYLKNHSILDETTRKSFYRIILSSNSLSTSLTYPLIEIILPIKNGFLMGKETFQIAFKKSRGYQILLPESELDLKINTTTFKTIANNKSVDAFLDDCVSFFSRPEMTQDSQLNASSGFLTNFSLKDSTDRFYKVLSYEKVSERFVKIDDSYITYSDIFSPLSHSHKDWFRIHTEENSSKNFYEIISEIVGGFPYYSQANERSLIS Q9UT04 YLWD_SCHPO SPAP8A3.13c; CHAIN 1..547; /note="Uncharacterized protein P8A3.13c"; /id="PRO_0000362153" MPRSLDNFQNEDSSHPNEQGAWADSGSGFPNPNSNDVSNSQRNHHRHMFPLARIRSELSEQDSSISFTHDPLHIPLPNPSNNNDNIFHPQVHSSFHSRSASRQRRRSGLSRSNATRYSRRSLSDWLETIRENNYDEASIPSFFSPHTERLVGRVLRLNRYLQNSELLDRNSSTFGSNPNSVFSAQPTEPSVEPPTSSFPIQPPLPPSRSISISNPQSLSFPSSFDQSNYNFQAASTPQFNPLIEHLRRSNSPLNPSHDSAGASTFNTYFPNSTYQNILNSLDNNPAVLDLNGPPNQESSSSASSYGSRTQTPNARSCSLNIVFHKHKKVCTYYMIRHYAKRRLFITPTWWLRSGSVFRGLQFGGVQSISGLPPLTNPKERWIVDVSIHVVDYKRRALEGQLNAQARSSDPSSTISTAWTGEILDFSEKLNFATEKWSAPLEIDVCYWRKLAPFQNMDTNTFLETITNPKKLYKICQKYIFMRWKDMLILKDQTDTSESRITGFYFCCLCRENGYIQGYYYDPKHAFCSQPLNLFPEQPSLSPSYHFV Q9UT11 YLW3_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPAP8A3.03; CHAIN 24..453; /note="Uncharacterized zinc transporter P8A3.03"; /id="PRO_0000316235" MFLLQRFFIYGLFLACFYTTVFGEKHFEAEEYRDSFLSQENMNKINHTTIERLFREMTENDPSLLSSSKTLAELSKGELAKAREDLKSVLSFLKNNLPVDTESSSEAFTIEKDNNSCVWLNSVKSFVEKQFSYSSGTNGILATFLTAIPPNIFILLVPKSFDTSMLNLFVAVSAGSLLGDVFLQLLPTVYSTNGGDFPASSVYSILIGALVFFLMDKGIRILIHERPSSLSKPKKDGEETSSVNKPSASSTQTDVKGVEGLRKRNVKDDQNSKGHEPDLIRHVVEEVSEEYNDKTVVYLNLLCDSFHNFMDGLAITSAFFTNTSIGISTTFAVLLHEIPAEIGDLAILLRNGYTKSQVLVLQMITMVTGLLGAIVATYIYTASSSSSPYGSFLLQLEDKLLPFTAGGFLYIAYLGVFPELLEINLSKGKLGNMIYTALYMMFIVGGFSFLYYV Q9UT16 ATP12_SCHPO TRANSIT 1..10; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC9.12c; CHAIN 11..291; /note="Protein atp12, mitochondrial"; /id="PRO_0000002420" MLRSLQFYRLSSKNLLSFKTCYSFYSTKASSPLPQPSFRRFWKNTATKIQNGEVLIQLDGRNLKSPSGKIVKVPKEMELLAHLIALEWDRLPSTSVRQHNLPITSLVSRAIDISQFKKEEKELLSTQLIRFLDTDTILIYSPETEYEGKLLEEQKENWWPLKETFENKLGVQLSYLDGDAGIIAHKQTQETHERIRNWLSSLNSWQLAAFERSVSCCKSFIVSFMILKGYLNSEKAAALTNLELQYQTNRWGSLEDAHEIDNEDLKNKLASSAILSRCIEDMHDKSNEHAH Q9UT17 YFYB_SCHPO MOD_RES 170; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC9.11; CHAIN 1..328; /note="Uncharacterized protein C9.11"; /id="PRO_0000304084" MDSANKNTKIFAEQLGNDFTISVDDEDMEMEYPLRSSTPTKVIDDQREILLQKASRISKLDEALCELNNESNGSIDLSIDSFIPSYDEFLHKKLLNEDTGHESKVSDQVKQVISTPMSTCFEQWFEGEEQSSTGNNQDISYSSVNSLSPKRRGISLMSIDANKLSPKKTSPNSGYITSPLRHPILLSETEPGTPTKNDSPAYIGLPSQPNSITTLNNTNQKFQVPDNDKPPMSSLNELSASYKPIVFDSSQHKTQGTDNNDSFYHDDTNCIHLSRLEKIRELLTFVQLELKYYVEPLKKELQETKTLLAQKEEEISNLKDKLQNAGLS Q9UT20 YFY8_SCHPO SPAC9.08c; CHAIN 1..282; /note="Uncharacterized protein C9.08c"; /id="PRO_0000317697" MFYSDYLKLLKIFVVGVFPCTLFVNAPHGKLAKQSKLFSKGYISGRVGWVLMELVAPLTFLYAIRNNRHFESTLPSLGDGSNRDYLDSCRKVLAGMFLVHYANRALVSPLLMAPQVSPMHWTVFVSAVLFNFLNGMSIGLYLVQASVQHHPVSIIRRYIGMFLWLMGWLGNMYHDNILYDLRRSSNKKKDPDNLDTVQSENSYYRIPYGGLFQYVSCPNYFCEWIEWFGCYLAAGPSAEPFWWFFLSEILLMLPRALKAHQWYCKKFPKYPANRRAIIPFLM Q9UT21 YFY7_SCHPO BINDING 70..77; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 116..120; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"; BINDING 247..250; /ligand="GTP"; /ligand_id="ChEBI:CHEBI:37565"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01047" SPAC9.07c; CHAIN 1..366; /note="Uncharacterized GTP-binding protein C9.07c"; /id="PRO_0000205448" MATTAQKIKEVEDEMAKTQKNKATAKHLGMLKAKLAKLKRELITPTGGGGGGGLGFDVARTGIGTVGFIGFPSVGKSTLMTQLTGTRSEAAAYEFTTLTTVPGVLQYNGAKIQILDLPGIIEGAKDGRGRGKQVITVARTCNLIFIVLDVLKPMSHKRIIEEELEGFGIRLNKEPPNIVFKKKERGGINITNTVPLTHIDLDEIRAVCSEYRVNSADIAFRCDATIDDLIDVLEGNRVYIPALYVLNKIDSISIEELDLIDRIPNAVPICGNRGWNIDELKETMWDYLNLVRVYTRPRGLEPDYSEPVILRTGHSTVEDFCNNIHSSIKSQFKHAYVWGKSVPYPGMRVGLSHVLLDEDVVTIVKK Q9UT22 YFY6_SCHPO SPAC9.06c; CHAIN 1..200; /note="Methylthioribulose-1-phosphate dehydratase-like protein"; /id="PRO_0000315889" MSLQLEKNLILELIPHFYSLGWMKFGSGNFCLKNNGYAICVKDRVQRDFITENDIVTFNLSNQSVTKDLVNWAYIFSWVLSNMDAVACIYSTSVAAVGASMYNEKFTTQSKEMIKGIPKGNPSAGYLCCFDTLEVPIIHNGDSKTILDELKKVIELYPQTCAVLIRGHGVIGWGATWEKSKTQMECYEYLFELDYKLKTL Q9UT25 YFY2_SCHPO SPAC9.02c; CHAIN 1..165; /note="Uncharacterized N-acetyltransferase C9.02c"; /id="PRO_0000310297" MVNIRNIERSEVEEVSKLEAICFPEAERASFARIKDRVKRAPEIQLGLFAPTQHTSTLIGHVLTSRTGSETVTHESMSKHDSKGENIAIHSLSIHPAHRKNGYAKKLIEELQFRCQHTITPKPSRMILISHKPLVPFYESLGFKNLGPSECKFGDETWYDMTHKI Q9UT29 YKGC_SCHPO SPAC8F11.08c; CHAIN 1..376; /note="Uncharacterized protein C8F11.08c"; /id="PRO_0000362151" MGFATILYSIWVVLSSFVILSAYQLEVRKFLVKLLSKIVIGASESNVASFFAFVSEKSLEAASVKFVATIIAERMGAQFSSFYDKIFFVDMLGLGSLFALAAVNVLAARKLESELPASLEPSIGNRDQQKNSSLAKCFSRLFINDLHGTTVKRYPYISYLPNWLLAKNNAERLVYKSHLLLNAYSPPKSASASSVIVWVCGAKKSESIIIPYLSSLGFFVVVPNYAQPPKFPLSDAVEFVSLCVDWIVENAIYYDADPERIFFLGEDTGASVALESLKHIRPNSVKGIFALCPRSIQNLVWTNQSTIPMMTLHAGDVNPVSDSNDRESSEKASLIKNFVVPGAVPYYYEFTSPRTISTATFIARWFFLVEDNKKTI Q9UT31 MU130_SCHPO SPAC8F11.05c; CHAIN 1..241; /note="Meiotically up-regulated gene 130 protein"; /id="PRO_0000014211" MICKYIYLAIFVFGTARIPKPSACLPGDFWKTKQEIEVQKKIDEFNQYRISALWSMVSKMEDPTLSGLDGRYIVVDQNQLYLSPISKKSEKLIFRFNLNHRGYLEVKSGFRAFIENKYSPLVFHATSWTNGFSIDVQKTNPISSYTPFVMQYLNSPWFSACRVESGNWQVFVGRMNMNEHEHCYPMSLIMKREDTWLRYYHKNNRNPIDWKLVQDCAMWPDGYPGTGRESEKGSNLEAITR Q9UT40 YIQ3_SCHPO SPAC824.03c; CHAIN 1..247; /note="Uncharacterized protein C824.03c, mitochondrial"; /id="PRO_0000362150" MWILKSGFNRCRNFSFMNRGLLGLRNLSVTHNNLVSYLEHLSVQKPSTSNTVAQGTLFEYLVQYVLKQHSFQLERCGGKGDGGVDLVGQFSIKNVLFEPTKVVVSCKSNKGSIGPRFVRELEGSLSSYPTDTLGILACLGSFTSSSLKTLSISNRPLALCRIYVDGFHSYMFQFVWNHQALAIFPDLSVRQIYKLPSPTANIVPLSQEFSQVNYVSLFELLQPLSRTEERPVPLVLVYKNQKISLNC Q9UT50 YFR3_SCHPO MOD_RES 222; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 458; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC821.03c; CHAIN 1..485; /note="Uncharacterized protein C821.03c"; /id="PRO_0000304011" MSSIIQNPIESSYFVEDLSAVGNSQLHSGRSLTYGDRKANIDTRSGGGRRFWSNLNDSGNSFGAVPASSMNLSYGPTKSATISSKDGAMSRSSRYYVSSELKATLPSLDGRRLSKRNAANHASHHRMPDESASYRTRGEYESSSPRVPQKSLRRYYSTRTAQRLDVRRPASRSSRYSKTSDLPPSDPGRFVDDSDLTPHTDFTNRFVDSDFDPDSGVGRSSSPDQMMSRNNNLNINARMTSTSSKPYAKENQQLISSMAPVEQKNSFSTAREQYVAPALSFAEPVETQHNHMPKTTPLRGTSTVMNGSPIGPYSSSSNATGMYGVSKGHSSSTRRPFFSDVGSSQPAEEFVGSSSSHGRQQDSYIADDSDSERSYRRVRDQYLSKPRLSDKNRYSTFSEFPGQGTPSASQSNLRRSNTVRPTSFYYEKLHIKNDNPSFQALPYETTTQERKPVVKPDSIKTVKPEKKKSKGFFKKLMHKISHIFD Q9UT59 YKJ7_SCHPO BINDING 39; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:A0A059TC02"; BINDING 166; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:A0A059TC02" SPAC513.07; CHAIN 1..336; /note="Putative uncharacterized oxidoreductase C513.07"; /id="PRO_0000316223" MSGKLVLVTGVTGFIGAHVAEQLLQAGYRVRGTVRSMEKADELIRLNPGLKDKIEFVIVKDVSASNAFDGVLKDVELICHIASPFFVENVTDNKSQLLDPAVKGTLGILEAAQGVKSIKRIVITSSFAAVGNFQIDPHNNKVYTEKDWNPITYEEALTTDNGIVAYCASKKLAEEAAREYVKEKKPSYDICTINPPYVYGPPIHPMKNMDSLNTSNQIFWKLIDGSKEATPFYYYYVDVRDVAAAHVFALENAKLSNGRMLVSKGVFTTGDICKVLRKEFPNKSDVIAEPVDITVDPSFFKLDNSFSKSLGFKYHSDEECYVDTAKKLWERAEEFK Q9UT63 YKJ2_SCHPO ACT_SITE 15; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250|UniProtKB:P62707" SPAC513.02; CHAIN 1..216; /note="Probable phosphatase SPAC513.02"; /id="PRO_0000318491" MASKGIDKTIYFVRHGQVSHDVDENGVHREHDPLLNDEGRKQALQLQHDLDAEKLPIELILVSPMRRALETMKIGFQHYIEDKHIPVKVIPLLQDCGDWACNVGSYTKDLEKQFPGYDYTACHEDPVFPKKEKIYKADYKTSIQRSRVLAEFFAKVPEKVFAVVTHGVDIRLFQKIQKPEDSLDAVPKEHSFSPCQHEEFRMHYEDDKNWNFEPVK Q9UT68 YJ53_SCHPO MOD_RES 257; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 260; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC4F11.03c; CHAIN 1..335; /note="Uncharacterized protein C4F11.03c"; /id="PRO_0000116808" MDAEGEQKSNGVKEPNTPLREALDEIFLNVGYLLRSLLANVPNALYHSQLQAACQKFQDYCDLEEIRIIEAKRVVERDLRSLEAKEVEEKSQFASFVSATPPGANSLQGNVSLPSGNNFFTSSFDSENISKPGEVSLSESQLLGNLNQQSSIQLPDRMPKTTNGTLADPNMPPKTTVNDQDVTKDASQQFGGSNFSNYLRDNDSFQFGMNTDASGDAHLQASEFLLPNLFGNSSTSPQDNFGTSNSALSRNLDLFGSPSSENKSTAGSASLFPNQQMGIDLQAQENYSAAFGNDGSFASHLTNTFDNALNLPTDIPTTESINDLFGENFDFTMTK Q9UT73 YIPH_SCHPO SPAC343.17c; CHAIN 1..576; /note="Uncharacterized WD repeat-containing protein C343.17c"; /id="PRO_0000316561" MDGTNNTIPLQFGKQAQTYDINALIARFIRPKESFLINSVEKESESKLNSKSTTLQSSDSEDWDSEENEDDITDVGVPGSHEIMFPGHSKIVTTTTFDKNGSRFYTGSLDNTIHCWDLNGLSATNPHPFKIIDPTDTNADNVGRYPVSKLSCSTKNQILALYTHSQPILYDRDGSLIVRFSKGDQYIRNMYNTKGHIAEITDGCWQPDSSQIFLTTGYDSTARIWDVNRTKSQLEVFVHVPEGSHTGLSRIPVTSCAWNPAKPDNFATAVLDGSIQFWQKGSRTKRPVMKIKDAHLPQQGISCLSFSQDGNYLLSRGEDNALRVWDLRNSNKCVNERIDILTPKAGGNAIFSPTQKLILAGSTAVNSMKAPLFVLDAMTLDTKATLFFDSKSTVTASVSAVSWNEKINQVSLGSADGNAYVLFSPNESIRGVKDAAMRPPKSKHIDDDLSSTVHINSLSGSAGTSDFGLVEETTESASAYFLEARRRRNAVRKDPKLSRQPQVGRLLEENSVDDIPLATMLNEDPREALLKYADVAKSNPMFTKMYSETQPTPIYQGVTEGDISSEEGNPSKKQKR Q9UT82 RT06_SCHPO SPAC343.08c; CHAIN 1..111; /note="Small ribosomal subunit protein bS6m"; /id="PRO_0000315945" MVMYELFCITRPAANATRTSSPTLAMNIAKNCGRAILDNKGVVVDVESMGLKELAKPIKKLNQSYSFGHWWSMTFYSNPTVQSEIQRILRLEPSVLRYMIVKKADKLSDLM Q9UT84 YIP6_SCHPO SPAC343.06c; CHAIN 1..381; /note="Phospholipid scramblase family protein C343.06c"; /id="PRO_0000317215" MLEILWANITPIQTFVSSNHLTMLYGLKRFGCRLYHHSKSTRYIDATAKVVSQEPAAISSTGAIPLNSPAAPLLSQDVLIVERQLEMMNVFLGYEQANRYVILNQQGQHLGYIAEQGASSILSSLSRQFFHTHRAFKADVMDSNGQLVLQLNRPFSWINSRLQIHSIDYSKFSSTLVGEVLQKWHLWRRRYELFLAKRSMFEQFAKIDERVLSWEFLLRNEQDRILGSVSRNFMGLPREFFTDTGNYVLRFTSTSAANGSVNENQLLQAAHGIANDVCARDMSLEERAVMLGSAVTIDFDYFSRIHGGPALGLNIPFMFGGSSSNHDYPAEDLSAQEILKNDQETTPSTNDSSSETKSPFLSDADLDQQDFWDIFDRDGDD Q9UT85 YIPC_SCHPO SPAC343.04c; CHAIN 1..507; /note="Uncharacterized WD repeat-containing protein C343.04c"; /id="PRO_0000343433" MALDEKFQLEVIHLLLQFLNDYGYDESLKALEKETGLVSETEDVKRLKQAVLQGDWITAEAAFSIMQLRDESKRKEAQFLLQKQRCLELARSGAICEAIYVLQNFESTDFNKEKERLVSIILESNNKSNNELITKNGYGNTRLDLLNQLSEYISPEILLPKRRLEHLLQQAKDYQVSSQVYHNVLKNFSFLSDYKADPSELPTKEYHVFHDHSDEVWQISYSHNGRYLASASKDKTAIIFDVVNLKRVFRLIGHIDTVAYIRWSPDDRYLLSCSCDKSVILWDAFTGEKLRDYKHGFSVSCCCWLPDGLSFITGSPDCHITHWSLNGEILYKWEDVNIYDMALTSDGTKLYIVGFEQLINAEDKHIAIYSVETRECIKKISLQSKVTSICLSKDSKYALTNLEPHTTFLWDLEENRIVRQYMGHKLGNFLIGSCFGGKDDTFVLSGSEDDKIRIWHRESGKLLATLSGHVKCVNYVAYNPVDPYQFASAGDDNTVRIWSNKDNPRRQ Q9UT87 IMG1_SCHPO TRANSIT 1..21; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC343.02; CHAIN 22..182; /note="Large ribosomal subunit protein bL19m"; /id="PRO_0000315958" MFNAKHFFNLGLGFQWLQKRGIGSLKRPYNFPKPVPGPKHKDVLSLFEKKCRSVLDEQSERFKMFHRSQPNRVRPGAVLLVESYSKYPSKDSVNRFAGYLLRIRHRGPKSSILLRNVVMGVGVEYLLPIYSPQIKRIVVLKENGLSKRPRRAYLSYLRQPRFRLPPVESLVRKYIEQNQHKP Q9UT95 YL44_SCHPO BINDING 297..304; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SPAC323.04; CHAIN 1..487; /note="Uncharacterized ABC transporter ATP-binding protein C323.04"; /id="PRO_0000310288" MASFVKFANTTFLDARFPLFKNVSFELARKQNWAIIGNTGSGRTTFLRCIQGSFTPSPSTSFSYPFLKGKSDSPWQAIQLLDFKSSGQQRAAYYSERYHSFRDKEHDTTLEKWLLGAYRGNEKFASQHVQEAASMTQLSHLLPSSLINLSNGQSRRAMLASKLVQRPQLLLLDEPYAGLDVTSRSVLSSLLGEMSNHCSPKIVLSLRPQDKIPDFITHVLELKNKKITYQGPKEQYIPMTSHSTNIPVKPQMKKSKPITIGKPLISMEHLNCVYWGRKVLSDINWTIREGERWALTGSNGSGKTTLLAYVVGDHPKLFASNIKFFGKSIGPGTGISIFDIQENIGHCSPEIHNHFPKQHTCFEALLSAWSTTFTIPKLTETRLAAISSILEEFELKDIKDKPLSSISVGMQRFILFCRAIVKQPRLVVLDEPFQGVDTKYVHMAHNYLNEKLSPSQAMVIISHYEDELPACVNRRAHIDNGKLVIHA Q9UT96 YL43_SCHPO SPAC323.03c; CHAIN 1..575; /note="Uncharacterized protein C323.03c"; /id="PRO_0000304041" MEEAINNVLLLLREDSISLETVLWETHYVLLNLHNEQNLRLVVAQLIACGRIWDYWNEHRSEYFAFWVELISRKKVTNNGLPFSSFVKSIVGILEVDASNEILCFRRICLLCVFYKLLSCDHIVNLQYPLKRAVSKALSKQIKTHQFSGFEANFLLQQLFASVDSSASDISFDAFSLLPHLLKWEEIVWSGFINYLDTEHKRDSLPTAVLCHLLLRLSTYQQISIIKRLITLIDKAIPSWKSRSSDSKYNDHQFVKKNFFSIIMVLESLAKSQYRKSNVLAADRSLCEYIILTLFHMEYLFSFVASSWSTLDFVITTCLSRVAQPAKFISETVREAIIDSIQLEGYVDLQKLSGSPVLVTLSFINNWQNLICRRLEKQTVNEKVITLSSTAKEISSLGLSFAEKLISQSDESTLCKHYVYASLYACLFCNLNEGSPKDYLDNDIYVHARCLFLLTKTLNLDSLKSILCSRVRLYYNIEIAYYFTDVLLKWFQPIIRYEFDNALIFYKASISLVSVLAPAAQKQFLSNYLNSIQGFSTETKEDLIFLVSSQIRQMPYQNATSLLSFWLSIVVGRAV Q9UTA0 YEIB_SCHPO TRANSIT 1..20; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC27E2.11c; CHAIN 21..81; /note="Uncharacterized protein C27E2.11c, mitochondrial"; /id="PRO_0000304099" MYSRVLSVAAIVTMALAVQAANSTAPYGNTTNSTGTTNGTNGTNTTTSSTATQSSAASITNFSSGAFVIAMIAVACSVMSL Q9UTA2 FMP46_SCHPO ACT_SITE 96; /evidence="ECO:0000250" TRANSIT 1..17; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC25B8.18; CHAIN 18..121; /note="Putative redox protein fmp46, mitochondrial"; /id="PRO_0000374044" MFGLTTKRILTLFTKKRQTLVEQKLTEYMIAGEKTDNQMLHFKLQVETATPTLDQLNIMLSNIGKDKSDLLVAGATSIEDALTKYQHDNQLFRRPCLVDWDKGKVSPYSILLQTRDFSKLL Q9UTA5 TYW3_SCHPO CATALYTIC ACTIVITY: Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282; SPAC25B8.15c; CHAIN 1..237; /note="tRNA wybutosine-synthesizing protein 3"; /id="PRO_0000281848" MNIKGIDVSFDAQKKEILEGLKSSVPDASPKGHPDSPIFPLLDVINSHPDWVTTSSCSGRISVYVQGANSRKGGGYWLFVSHQAHEELPPVLEDEKVEYGKVPSSPVEGNREIQYAFEPMILHVQTRSLANAQHLQRVAASCGFRETGIQGSEQKFIVAIRTSLRMDIPIGCLTASEKLQFYITREYMCFLFKRSVEYFTENGNRMARLKEQLERQVEKRMKPRRKLRNMDDYLVQS Q9UTA6 YL8C_SCHPO MOD_RES 63; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC25B8.12c; CHAIN 1..303; /note="Uncharacterized hydrolase C25B8.12c"; /id="PRO_0000339408" MSAVDKTNNLPTLDTLQMVISDVDGTLLDKHHRFHFRTYRAMKYIREKYPNFPIVLATGKQRSAVDLIRIPLDLDAFPAAHVNGCVLYNKGKIVYADHLKPEVVMEVVEATKGNPNIANVVYDEHYVYALTPGREDMKNVKRLAEIGEKVDFSMPCEEAIEKVKSGEIKVIKMAVCEDPDKLDVVRDILGKFPREKFATTQALEFCIELIPSNSNKGTALQYITSNILPEVKNENVISFGDGQNDLSMFAIAGWSVAIKNGMPIAIEKAKAVSRVGNEEGAVGEVLERIFNIPEDYTPPPYTF Q9UTA8 YL8A_SCHPO SPAC25B8.10; CHAIN 1..256; /note="Uncharacterized methyltransferase-like C25B8.10"; /id="PRO_0000339153" MAEQIDLKTFKTDVADYEAARPEYPIGITDWITDEFLIDETSIILELGAGTGKFTPRIIASHPKEIIAVDVYPEMLDVLRKKFPNVDCRAGSAMAIPLEDESVDLVLCAQCFHWFANEEAMKEIYRVLKPNGKLGLVWNTRDDTVPWIEKVSKILGRYRKDAPSFVSWKWAELFPGHGFGKLRYCAFPFSRCLTVEELHTLMNSFSFIYKLPEEEKEKVHAELDEIAKTIPRVQNTDQIKLCYQTMAFSSEKEPAK Q9UTA9 YL89_SCHPO SPAC25B8.09; CHAIN 1..251; /note="Uncharacterized methyltransferase C25B8.09"; /id="PRO_0000339154" MIGRTFKTDIADYETARPDYPPQITEWLNDEFSVNETSTILELGAGSGKLTPRIIASQPKEIIAVDTYVEMLDVLKKKFPNVDCRVGSAMAIPLEDESVDLVACGQCFHWFANEEALKEIYRVLKPNGKLALIWNIRDNSVPWVEKCSQLLEKCRGGPLNMFEKAAELFPGYGFTELKQSLFTSAKKYSIEDLHRLMNSFSSINRLPVEEKEKMHAELDEIIKTIPRAQNTDQVDFNILTVAYSSEKVPIN Q9UTB0 YL88_SCHPO SPAC25B8.08; CHAIN 1..590; /note="Dilute domain-containing protein C25B8.08"; /id="PRO_0000317098" MHTYCNTETVQLYRFIAMDQWSDNKDAIGMLSESLKEKVVTNEIAPALKEVKNHKYNFETEILNTGNVWNNDSKNGESGSAFGLDKIFQSSDSGNIAEGLELDLGNIMLETHNLESPAWKHADYDGVAASVNDNNNDWKFFVFDEREIDSMLQLFVRDFRADKPALRLAPSKLFYLASRFAFFYMPKEKELGTVLLNAFLCEVNQVTQQHPNDMVLCVQWLANVSLLLFYLKKDNKLDDLTVDIQNRCSELMNSLYITICQDAMRRMNENLEEGMVKYTGIQGLEDILRSRSWNLLRRRPTNDASTSPRSTPSASPRSITKIIASTLHLLEVFYIHPLIRAQCIEQLFSWLGARLFNIVISNKKYLSRAAAMETRFNISSLEEWSQTNSPKLQKPFDYPDEDLKVDLISKLLSLVQLLQWLQCLYRLSEDEDPRALQETLESLDALNPRQIYTAAKLYRPDITETKVSKTFLKKLDAFHEEKLREKINSSDKGDVSYEFELLKDETVFSPLKLPTKAQLINAYSYIVSGNGFNEDRKIVFQPHVSNILIDKLEENGLSMERAELPTSVFEDELQRREWRPDQEVEELLST Q9UTB1 YL87_SCHPO SPAC25B8.07c; CHAIN 1..113; /note="HIG1 domain-containing protein C25B8.07c, mitochondrial"; /id="PRO_0000372339" MSSKLPKKSEENLELPTFPASEESLSRSEKLKYVFVRNPFIPLGCLMTVGTFLASGYYIRRENHLMANKFMRYRVMSQGFTLAALAFSVLFIGPPRREAPSNSSGSINSEIKK Q9UTB4 MSS51_SCHPO SPAC25B8.04c; CHAIN 1..378; /note="Protein mss51"; /id="PRO_0000352654" MSFLKNLFKKKSPTHELFHPLSRSPLTALRRRSEHIKQVYRCPISGKSVEYECPESGFPTHCNRTHWEQDKIHQSLIPKLRQINEDYHDLARPNPLPELLKLPGPMEEDEVVSLLSWDSFFYTRDFPKFQSSRTARHITSLLTYPMSIGAILHKNSPYNLKNGLTPQGLQSLTALRYMLHRPLSAQSTDPRPTRIFVLGATKECSLPPSIWLQGLNFLFPGRLFQLHFIGPEVVVPSKQPNLPSPLSLHFHQDYYHNLHRVGAFEPFDPYYDTFFLPMPLISHPLYSSSWIPTLHDLVSTRCSVWLTSPSSQRTTKDLEVLNNVLKDSIEPLLLPTVNKFASLGWSVDDSNLHEVYHANQEVFGFRALYYNVQNVSKE Q9UTC7 YIDC_SCHPO SPAC227.12; CHAIN 1..462; /note="Uncharacterized WD repeat-containing protein C227.12"; /id="PRO_0000316560" MNENEGISLGELETRPFSEGITRFTKEQAAYYAEQKEKDRIKALKIPYEDSKVREYLRRYGEPITYFGEDALARRQRLQQLMIEKSLEGDNPLDVDQGASENIEKETYVQGSHELLVARKKIALYSLEKAKLRLKKEREISEIPVPEIVLSGKSSIEHLQKAELMGSQIGGERPIAIVRFSNNGNHFASGSWGGQVKVWNSDNLSEVQLFRGHTDRVSGLDWYPLCQAWDADSEQLTLATGAADNTVCLWKASQSTPLLRLEGHLARVGRVAFHPSGDYLVSASFDTTWRLWDVHTGVELLMQEGHSEGIFSIACQPDGSLVSSGGNDAIGRIWDLRSGKSIMVLDEHIRQIVAMAWSPNGYQLATSSADDTVKIWDLRKVSLAHTIPAHSSLVSDVRYIESGVNRFIATSGYDGCVKLWNPLNCSLIKSMVGHEEKVMSVDGYGDRFISSGYDRTIKLWYP Q9UTC9 PFD2_SCHPO SPAC227.10; CHAIN 1..114; /note="Probable prefoldin subunit 2"; /id="PRO_0000124840" MAEQPSRQQILQTQYNSYKSRLQQIAQKIVDLETDADEHKLVMDTLNSMDNNRRCFRMIHGVLVERTVGTVVPILKTTQEGIQTAMNGLLDQYKQLEAEFQKFQKDNKIQVVRQ Q9UTD1 YTH1_SCHPO SPAC227.08c; CHAIN 1..170; /note="mRNA 3'-end-processing protein yth1"; /id="PRO_0000238542" MTDYIKDKAIAADFSSVQFRFDNYLKQNFNFGRSALLNSGNGRDSGSKMGSVVCKHWLRGLCKKGEQCDFLHEYNLKKMPPCHFYAERGWCSNGEECLYLHLDPSKQVGVCAWYNMGFCPLGPICRGKHVRKPRPCPKYLAGFCPLGPNCPDAHPKHSEPPHPPQKRKDW Q9UTD3 YIP5_SCHPO SPAC227.06; CHAIN 1..249; /note="Protein YIP5"; /id="PRO_0000259417" MAHEIEIDSEADLGRTTFEAEDLYKQRTPITKPPAPRLQSRRASMQETPWTIKDSFNVETKDVVQRCIHTLIPTVNFFDVVDDRPDLYGPFWITTTVIQALFFSNSITEYARYATGHGTSGYSIKKLISAASIIYGYTTIIAVLLWGILVWNKCNPKLLDCLCLYGYANIVWLPVSLATPPFGLLSTLASHIVKYVLTGIGLLISIVFLTRNLYPICQQAGSNLCKLLLFGIIVFHCLLALSLQLIFFS Q9UTD4 PFD4_SCHPO SPAC227.05; CHAIN 1..123; /note="Probable prefoldin subunit 4"; /id="PRO_0000124847" MEQVPVLAEDQRNLNEFSVLHSRKAIQELDIKNLKTQIEDIVDAKNECELLDEDDGDDIPALKVGDAFFQVSLPVLLDQLEQSEESLEKQVDVLRSSMEKDETRIQELKSMLYSKFHDQINLD Q9UTD6 YID3_SCHPO SPAC227.03c; CHAIN 1..371; /note="Uncharacterized mitochondrial carrier C227.03c"; /id="PRO_0000310798" MVDDSLKDAIAGGAAGLASSLVVAPLDVVKTRKQAQKAFYSTGGGKNTMVLGGTLSSMRTIFHNEGIAGLYRGVGPMMLGYLPSWSIYFVVYEKCKVLFGVNKKYTSLHEIDSSKVGIKASLDSSDKQFYRYWGGQIFSAVIAGAASVTLTNPIWVVKTRLVTQSHPRASSFVDKIAAATTVQFRNLQTDAPSVKWRMPRFWLKRRTNVKSSPSQHPVNPPTGPACSPAYNNTFDAFRKIYKYEGLAAFYRGLFPSLFGTLHVGIQFPLYEYFKSFLDDFFGKKSNFHIVLAATLSKIAASTVTYPHEVLRTRLQSLDAPTHNSATLLIRDIWRSEGWRKYYSGMATNFIRTIPASSVTFLSFEIVRKWLN Q9UTD7 RRP15_SCHPO SPAC227.02c; CHAIN 1..205; /note="Ribosomal RNA-processing protein 15"; /id="PRO_0000363395" MAKSQRSQIKNEDISFVSQEDDSSKKFVKDDSENSEEELEDLNSEDEFYQSNSSEDEIEEEVQESTIADDIADILNQQVTQTDEQDTPVLSLSKKSKKALRKSNAEKKDSKLRTSRRRERLRKEMVGRVTSVVAVNAETAKALFTHERELRRIARRGVVQLFNAVRTAQLQSSLNRENISGGRTAREQKVKELSKASFLDLIKSQ Q9UTE9 TIM10_SCHPO SPAC222.03c; CHAIN 1..89; /note="Mitochondrial import inner membrane translocase subunit tim10"; /id="PRO_0000193621" DISULFID 39..64; /evidence="ECO:0000250"; DISULFID 43..60; /evidence="ECO:0000250" MSMFGIGKNNQTINPQNIAMAEQEVEMMSDIFNRLVMTCHKKCISPKYYEADLTKGESVCIDRCVSKYFEANQSLSQHMQKRGQENPTP Q9UTF0 YIN2_SCHPO SPAC1705.02; CHAIN 1..63; /note="SERF-like protein C1705.02"; /id="PRO_0000357055" MSRGNQRDVDRARNLKKSQASKKKQAGDPTKRLEAQAEIMRAKQRAADERKAAEANGGSKGKK Q9UTF8 UGO1_SCHPO SPAC1B2.02c; CHAIN 1..421; /note="Mitochondrial fusion and transport protein ugo1"; /id="PRO_0000362157" MNPYRPYVVVNNVEPTFSITPEPTFETQPTISKSEIFETLRSILVTKYLTTFFVQPLEVAKTVCQVEEYLPKRTKIERDGKQTKEPYDEDIPDGTEQEGLSDDEHEIYAYFETPTTEKAVTEQLAEKLCVDASGYVTDPSNLIERSYTIHSKRFSIKSIISELWEKEGARGLWKGHTISFLHNLLYSGLQSWLSATLSGALAIADPNIISPIDSVRPLLSLFIKSITSAISALILSPLDIARTKIILFPISSSSYLSSASETSGNSHKKFKPLTIRQCLKALPFYCPSSLILPTVCYVSLPPFVSSVLPLTFRNFLGSSPTLDAMVGLGTSAVQFLLKCPLEMVLRRAQAQYECNLPPQTIVPVGKYTGIVGTIWCLLSEEDPGKFGIEGLYRGWRVGIWGMSSTLALNYISSNLREEVEF Q9UTH2 ETFB_SCHPO COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per dimer. {ECO:0000250}; COFACTOR: Name=AMP; Xref=ChEBI:CHEBI:456215; Evidence={ECO:0000250}; Note=Binds 1 AMP per subunit. {ECO:0000250}; SPAC1805.02c; CHAIN 1..254; /note="Probable electron transfer flavoprotein subunit beta"; /id="PRO_0000167873" MSKIRILVGVKRTLDYMLKPRINATKTAVDLSGQKMSINPFCDIAVEEAIRMKETLKNRIEDTLVVTAGQTSSEPILRQCLAKGIGRAALINVGEKELEPLSVAKLLKATVEKEKSNLVLLGKQAIDDDAHQTGGMLAAMLGWPQFTSASKVRIEGDKVIVTREIDGGEETLSSTLPAIITTDLRLNVPRFANLAKVMKARKAPLGKMSPEDLGVTIDQRLQTVSVSEPVQKRQNIMVKSVDEMVKTLKELGAL Q9UTJ3 MEU1_SCHPO SPAC1556.06; CHAIN 1..776; /note="Meiotic expression up-regulated protein 1/2"; /id="PRO_0000096451" MSIPANVLMEISFQELTSKKSEEYERKRLNEIGDLLTPQKIEEVLNCKDTKQRNVSLEDIFQDFLNFIITKNQEMFSMDCNSICKSYVLKVAEEKIEKLLKENGTLKNEEKCLRMQIVAQEEYVAPLIQKLEIIEKKLDKSFRKNMEDELRITRLASENNVLISRIDRTKRHFSELFTQKQMLQLQNENFKDDYEKIKEENKRLYKERKSFLSKIEKSACEIHDLKESDSFKDHEILRLKEERTAAMQAIDDISGTIETIKSDCYKVESENKGLINEVMDMRNFVQQLEQELYAFEDDYSRIQNDEELLKVGMIHLNKSENRTVEEMKIGDFGNTEEAKDVCVSDEDIHNVNIKQITTLIGKMSQVQIECKRLRKENLFLQSERTHLLRELEELRHLATSAKEDFVKVEKLNKIIKDENENLKEYIRNNSLSFQATAGELTQCKQLPQPRITGNDQENSHYTGAGNNCLELVGKENNCKNQYPQYFSNIDESNAFINNQCLELEALNRKNDLIRGELDSLKEKNLVAQKQLKSANNTLHVRAKHIQILENTNQSLKKNLENGRAEFRLKEIALIDLANQQIKNQDKTIHDLNTELCSLTLDYCNTAVERDTLRFRALEYLDHNKQTNPLPYHIVYMFSFETSPTVFQTSPEEDKENVNNIKISQPRNSLQTNGYIEGMANNVLDASFNVEDESHAISDSELGYFCEDQSNIYEVEDMRYYLFYTEEEKNMLPGFIVNARPANLDLFPCCYETTDKRSKHLKNMLNKKKLIKHIFHL Q9UTJ4 CGR1_SCHPO SPAC1556.05c; CHAIN 1..111; /note="rRNA-processing protein cgr1"; /id="PRO_0000278960" MVNGTKGVCVSGKPWKTEKKAYNRSGLADAQRTPYEKRMEQKRKLDEIKEREKELKREKEEQRAAHAEKIRTRRQAKADRERMELLQAKLHQKVIDRRRRREKRNKMLKER Q9UTK1 COX16_SCHPO TRANSIT 1..12; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC1486.08; CHAIN 13..113; /note="Cytochrome c oxidase assembly protein cox16, mitochondrial"; /id="PRO_0000280653" MLFYRFKSWYRLQAKKSPFIYVGLPFLSSVLLVWSCLIPISQVKFNRRDEQVKSLSRDAELDIIKRRRKVDVNEEYYRILLDQLNLQNEEYENKRVKRLKGEPTWEGNSSDKE Q9UTL0 YIVG_SCHPO SPAC144.16; CHAIN 1..179; /note="MIP18 family protein C144.16"; /id="PRO_0000212698" MSANLQNENPEVKELNQLPSRVEEEEDLLLSSTKQWLTEIESEQTNIKEERDPIDPQEIYDLLAKINDPEHPLTLAQLSVVKLEDIEVVDNVEGDSYITVHITPTIPHCSMCTLIGLCIRVRLERCLPPRFHVDVKVKKGTHASESQVNKQLNDKERVAAACENEQLLSVLNGMMATCV Q9UTL3 RPIA_SCHPO CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; SPAC144.12; CHAIN 1..274; /note="Ribose-5-phosphate isomerase"; /id="PRO_0000339892" MDSAEKKLDLSPIELAKRLACHMAVDENYPENPKVIGIGSGSTVVYVVERLLTKPGVDSVVFIPTGFQSKQLIVNNGLRLGDPDCYPNVDVSFDGADEVDDNLQCIKGGGACLFQEKLIAFLAKRLVIVADSRKNSHVLGEYWKKGVPIEVMPMAYASILPQLVELGAIEPKLRMGAPGKAGPVVTDNGNFIIDAHFGLIKNPKELFAKIKLLVGVVEVGLFCDMISAVYFGSKDGSVTVKKASGEKHIIPAPVTAAANEVDAKVAETNAKPLN Q9UTM5 YIJ1_SCHPO SPAC1420.01c; CHAIN 1..580; /note="Uncharacterized protein C1420.01c"; /id="PRO_0000116792" MAKRVVSPNPMLSLETENIAKMGTLTADSLGSMWNVFTKCAENLENGRRLENISWRLWYREAMMSDANDACQIACQESSVPDLSSSCDSINSTVESDAGHVVDSNSFNRIDNVSVNAPIVNEVSLQAPMKGGSHSSIVRPQAKRSSSRLLSTDAFSQFISSFSPPEKPSMKDLALFHGNKSPSSKETIPKVSNSNSSDTSTDDQAYLNVSVSENEHADRSIKTHSSAPPLNQQKSSTSVNDAVSKAIQLVKSTSDLGSLSTNTSSTAQKNKSRKPTKSFSDAVAAASRAKELEKEKLSKVTVTPDDSTSIIRGFDPRLPVLSTKNVSHEEKSHSVQDDKSKQLLKPNPTQPYFYLRGSFDTGHSASSSICSAAVDSESVNSADFPHRTVYDPLPTHAIAESISQENVIEDDDDDDDAWVSVDEAESPHFTKRSPAPYLSKSFRNSALSLLLSQDEKLQHDVRSASSAALNLPRDTDIKATPNLSQSGNINSDNSDLSNYPYNDYRVYRMSHCSSNSNKVLASEISESLRRDLLWERRQKAAMNSAVLRRQSSQSSGANDDKEVRNRKVVEKGFANDCSVW Q9UTN7 MUG95_SCHPO SPAC1250.02; CHAIN 1..178; /note="Meiotically up-regulated gene 95 protein"; /id="PRO_0000278616" MNLFVYIAQNPTLTKWFFCCVCTILTMPFFKKPYRKRGISRTPYEWLTYADKCVIELSKSELKPNEEKELPKDIKEDCKTVEEKEKVVPRKPLQSEGINEDDSQKNGELIVLHGINHQAAMLTACGLFMVTSSNTNKWKIAFASFLLGMFFTQFGFQKSERSINAEKLESIEKPENDN Q9UTP4 YLL3_SCHPO SPAC11H11.03c; CHAIN 1..206; /note="Smr domain-containing protein C11H11.03c"; /id="PRO_0000303947" MEEYEKFRALASKEAEKRGYLFQEAQHAYSAGNKAKAHELSQEGKLCGERMENYNRQAASAIYLYKNSQCNPDEIDLHGLYIDEAVQAVQQRIENCIRRGDNHLHIIVGRGNHSANHVEKLRPAIVRMLEQQSIKYNSEVNEGRIYVYLPSATSPIQPNFNCIQEPQEAYSRPQHSTLTDQVEPEKIVEEIATNCFPRLKTCCAIM Q9UTP5 MU162_SCHPO SPAC11H11.02c; CHAIN 1..264; /note="Meiotically up-regulated gene 162 protein"; /id="PRO_0000278512" MDDEVYKQRLTALNNLRIVIFFDILIILLGYIGTWNLKTLQLVNPSLWSFSPSLWIYIRGTVLCADCIFTAGSANEYSAVQNSVFQVSSLMFYGLMMEFFGYSFDRVGCMELAFISFSAACYFNIRSIKSLSLKNKNWTIISIIEIPIKLHFILNVLLFLKFSEYMLPLLGRVHLSYHLFALWVINLYIWIKLIDSKDFVLGFLAGLSVLLLNTGSLITAKPLISYFNLLTSCLIIFPSIWIYAIEKKNFKNLSYEDDDYRNYW Q9UTQ4 YL3B_SCHPO SPAC1071.11; CHAIN 1..244; /note="Uncharacterized protein C1071.11"; /id="PRO_0000317097" MSIRFTHCFTSSSSLPCYILRHLPFSNFNRYSTASHDNVNAFRLLMRRFAQPVVIITSGFADGHRAGMTASSFTPVSLTPNPVISFNIKIPSRTANAIQQSNRVIVHLLSSSIKKHSEWASLLAKQKHQINPLMNSEKNSTSVEDLPGSNRTQQTSSHSLLHPLHPIDVSLSKEGLPCLVDSLGLLHCSIIHSYQVQDHILFVANVERVEHGSSPLESSSGLVYYNRNYCSTSPLSPIIDSFES Q9UTQ5 YL39_SCHPO SPAC1071.09c; CHAIN 1..282; /note="Uncharacterized J domain-containing protein C1071.09c"; /id="PRO_0000310358" MAGLLNLCYIKDECQFSLLPLTYSFIKMDIDPYSVLGVEKDASDELIRRAYRKKALQHHPDRIHDEEKKVEARIEFDKVAIAYGVLSDKKRRKHYDKTGQLRETDADIDFDWKEWLDELYQGVVSGETLNEFKASYQYSEEEKCDVLKAYEKGKGSMDVILEEVMCCEISDEDRFRQVINNAIKDGKISKYKRFAPNEKKRKRRAKAAEREAQEAEELSMELGLDENLKKRRKAGASDEEALSALIRSRQKSRMYNLISNLESKYSKSSTKPKKSKKSRSKE Q9UTQ9 SPC2_SCHPO SPAC1071.04c; CHAIN 1..167; /note="Signal peptidase complex subunit 2"; /id="PRO_0000362161" MPKYNVSDFKSKFDKELTNHFNKNGYKQSFVFEDIRLLIAIACIIPAGLAFGIEYVYGFGVLKSYLKYLLPLYFLASCLLTFWSSVVKGSTVYVATKKERHIKISADTFLPLKNKPLITTKFTVLKNRNAVQLEWSVPVAHIFEEDGQISSATFEAEISKYLSQIEN Q9UTR0 YL33_SCHPO SPAC1071.03c; CHAIN 1..338; /note="Uncharacterized protein C1071.03c"; /id="PRO_0000116839" MFSILGNSSKKKRNTQIYRIFFTLTFSLSNLFLAICYLFLNVRTVSSDSSVSLYDRQLFDQSSSVILNPDTSDPSIVLSSLETMRDLAHDIKFGQDVLEQPLCDQLFVLMDGKDYPNTIRSMSSVVLASALSNNFIAQKKALEMNIMPKIVNTLRQENHPVTLLKKLFLLSKSVQSFPLSEAFISKDLGSAILLQLYDFWSRNSHIDIPSAFQEKLLSRLSIIFENIARSLENVNFSKASKVIPIEWVFSTWCSIFQKYLMNNWHLRSISTLEVLLNTVSTIQSVSESCPEVNFYEWLNDKNLAYKNKLIYQDPDLATEFNLIIKEALSLPWPKKYNI Q9UTR7 MCP3_SCHPO SPAC1006.04c; CHAIN 1..952; /note="Meiotic coiled-coil protein 3"; /id="PRO_0000096289" MTKETHENHLRTHNGIFPVSLLSTQARQLLNFKLKSPSYYLLNSFKLLVKSEGNNQSTTADVTLTKSPNAYHASSAREEKDLQVSRRDTCFYCSRKIIKCICNEEHVGIESVQLKLILLLCQNLPNVTTNAKKYFSSLADGHNFTLTLYKFSLDNQTFSQLLSRFKSFATLTELLQVHNVMLQVNFSFQARQLNTEIQLRRCHSLEKTWKFLFGDYELPDVLKDMESSNSDWSDTSLKRIAYLCSLVEELKLHSSIMNDKYVCLVSKHNNALEDKFNSEAARQLLQKSLSIVASNLKQAENKTISYEEKLSIAQNSINEIQTQNRDLKLETEKLQDQIKALLERNQSLQEALETVKNDEKNLREMNANYETEMKEARQKLNNKEALISHYDDDFRAKELKISRLSESLREKAGLLEFQSSVSEQRDLLYQEQIQSSIKDMENVFRKNEYLMEELNELKNNLEVESSKVLRLDEEMKCLKDEQLSQFDTVFSLTDERDGLQKDLKNTKGNLDDEIGRSAFLKSQIRDQELTIEKLHDSLETLSQTNNSLQCEISEKNAELNSVNSKLSEGRAHLETANKENEILKQQLELSESKLASLLNSYQSFINKKEHLYSFLQLVEPSFAKSDSSNATESQISESVRKGISIFNLLFIVYKNVCSQAGINPSTKLEDLDEHTLSDELTYITKKFVQKDQEYQTKEIELRNYKITLQSLLEDKLIGVNTDCRSPSCSDFEQLGQESENNTSISGRVSKLVKSFNDSSSISNNTKISITKSPSGEKVSVFKEMSDIALRDMDKNRKLLGENVDVRNIVVQKDESLNIDLQNNAVVPELHFKEGMVYDSLENAYTYLAESKRMLANELQMKQEDLEKVILELEAYKEIFLEEKQIPCEEFMPGKNAKSEKSLRSVFQEQLMRETKRVRKLEKVNSELKLHCFELSERLREREHTLQQTFGDK Q9UU77 YQMA_SCHPO SPCP1E11.10; CHAIN 1..207; /note="Ankyrin repeat-containing protein P1E11.10"; /id="PRO_0000310324" MSTTTPNIWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVCEKLEIAHDLINQYNADTTVKNNDGLIAAQVIEANGEFPELAKYLYSFTDLEPKDVNTLPNDTKIEYAKLMTEQEMDEEAGQPLLDQKAKAEIDRILALRDTGVNVDDELRKILTGALSGHFERNVRPRSN Q9UU85 PPK38_SCHPO SPCP1E11.02; CHAIN 1..650; /note="Protein kinase domain-containing protein ppk38"; /id="PRO_0000256833" MNETNNTSLLPVSSLPSGLLPVGFSCTVEKFSVTVKRYLAEGGFSHVYLVQLVFPGKPPFEAVLKRIFATDAMALRAVHEEVRTMKLVSNQKRCVSYYGSEFFRTSKNQFEVLVLLEYCPCGGLIDFLNTRLQVRLSEQEILKIASDVTEAVAVMHYLKPPLIHRDLKIENVLLAAPNSYKLCDFGSACHPIPGAKTAAEAKQLEYDIEKFTTWQYRCPEMINVHKGFGIDEKSDIWALGVLFYKLCYYTTPFEHQGLAAIMNVSYAFPTFPPYSDRLKRLISTLLQQYPWQRPNIYQTFCEICKMRNVPIHIYDIYNGKNVSSCNPSGSEYLQHASKLENSGIHQSKSSVFPQPASAMKPMASPMLPNVNSMPYLSNGDHNNNGNTSSPVSRFSYGQHTSNVPSTQKLPSNFRVTQGAPPSHTYGPPPPVQPKPKISPTTPRLSTLALADDMFSSTAKETVPTNEAVFTGDVKSFDSQESNIIESEPLSASNASGKPRTSVNRLVDRYNHTSSLNKVAAAPAPVPKPVNLKSVENPQNNISAPTPSSLQSSNAPVGLGEVESKSVPPTNMATERGVVGRRASMSIAVNARRVSKPEKEHTNPNAEQGDVIPEKPMSIKERMNMLMTKTDYEKPKVEGYGRYTDVQQTKK Q9UU95 MU128_SCHPO SPCC830.04c; CHAIN 1..143; /note="Meiotically up-regulated gene 128 protein"; /id="PRO_0000278624" MEYANLHYVKESSNLERSSTYKSSKIQDEAKQLLYDYVYIKEKLLTTSSNSLTHYQWYLIYKHTCRCFQQVVRIVYWFLGNQVIRENFSIKKRKPHNHIPQLLEQCTCIAESFEGIYTKKQILYFKCYGTFKTWKKIANFPHL Q9UUA0 ECM1_SCHPO SPCC23B6.02c; CHAIN 1..111; /note="Shuttling pre-60S factor C23B6.02c"; /id="PRO_0000304032" MAKKQSIRSRNFRRSDPAYDLDSSTAIENETKLSVKEKVAKEIANIALRSGGSESNGISKKKKNKKQTSKKAKDKLAAALKAQAREERLDTKISKSLQKQEKLKARKQGDE Q9UUA4 SEC66_SCHPO MOD_RES 162; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC409.21; CHAIN 1..192; /note="Translocation protein sec66"; /id="PRO_0000311763" MVSIYVPLIYITILMGSMYGVSRFVRKSKNQESKPVSEEWFGENYSRNIFFSLLQQNPPAEDTLLKAALVLRATEGLRRLMKLKVSRMALNNLLNRGGVGDELIRKFGRLEKETELELMDIAKTANSLQPGWNQFIFQTCNEIIENEKIHSIIDNIPKDIDSISQRWQTEKILYEAADEELRIQAQKELGVL Q9UUA7 YHAH_SCHPO SPBC409.17c; CHAIN 1..222; /note="UPF0590 protein C409.17c"; /id="PRO_0000339161" MKCFLICGSKKEPISINGTPNVVKSKYFEGDVKVRLRDYETPDEEYFEQSNDTCSIMIRGRFLPTESTLTADDILFGNQFEKPLRDVLPMGSNLLMKGLQYVDPSIEFDLYCDQPWAFSPFFATMTKMQVSDALLPMEYFEDHSSRRSQMQQQVIRQESSIDPNKYILADFCNPFFNPSTLSISIPYTKMSFSIKNYYNGQPLRYFCKTRDGNVIFAVEFDL Q9UUA8 YHAG_SCHPO SPBC409.16c; CHAIN 1..120; /note="Uncharacterized protein C409.16c"; /id="PRO_0000304111" MCSVEKIVRLRHNLLCHVRIHFKTKEDLDIRAFLFSLQRELHAVAFLNQGSIRTLYEKRVVDITSESVQSHAIIETARNFALPNTAEEEENMDRKPELQLSFKGSMTSKIIHIYVQPFDS Q9UUA9 TSR2_SCHPO SPBC409.15; CHAIN 1..179; /note="Pre-rRNA-processing protein tsr2"; /id="PRO_0000362996" MFDDPSKRLTYFEYAVGVLLCSWPVMKQAVEEEWADVDTADKRDWMAGVLVDYITVTSDVEAWDVEELILQVLQDEFNVGSIEDDSPYILAQDLVNVWKAACEDNYEPIREIHERLGKQLLEKEEGKEKTREESNPPVLVEDETIVDAEDGGAAQNQQEKQQGPIVDDDGFTVVQKRRR Q9UUB0 RT17_SCHPO SPBC409.14c; CHAIN 1..90; /note="Small ribosomal subunit protein uS17m"; /id="PRO_0000311716" MKLNYVGIVISRAMPKTAKVRVAKEKFHPVVKKYVTQYQNYMVQDDLNCNVGDAVTIQPCRPRSATKRFEIIKILSTANRMSPASEISKE Q9UUB3 MEU18_SCHPO SPBC409.11; CHAIN 1..553; /note="Meiotic expression up-regulated protein 18"; /id="PRO_0000096450" MIYINFYELYNIKNIRPLIPSFHVCLLIMFLILYSQEILSFFFMCSKFSMNSLKFCVLFSFKTVYSLLKLIKTLIRKLLYCFHYALDLFADEYKVTANDKHYDYRLKSHRIKDKITTKCKGTTKYFNSRHFEIKNAVENLPSFSSNLTTIGNNLRIFWKNGKIRCIKLTCTPDAEIVNFTSNPNRYRFYETNMQELIRKTICEKSDKAIEKTFLCAQLFKTFCEDGVLQTFQPGFIQLDIASNLQEIKKGTKEYSLKSLEMTTTKESNETLCSNDSKHRIARLKNEDNTQKPISKKRKSKKASHKYLSSRTAPNVDFGNFAKERHRENDVSELYSKTKRTSKIRELYKEIGYDKNEFIHELRENEGPSVLYDSGLDQNGTNYDDAFAAPEAISIEKYVSINEEDPKSPKKETSYQVQEKLSQFFQEEMIHLLEMGEACTSRESQKTRKKNLKENIRKQRTTSTAIRDIAIKFLDDAKCETEDSTNLTNREGEAEKTLNTQPWKNLIENFISELQAEEEENNITEWSDIISVRNDEENQIYELPTCQLETNLLV Q9UUB8 YH9J_SCHPO SPBC1709.19c; CHAIN 1..260; /note="NifU-like protein C1709.19c"; /id="PRO_0000166193" MLFPRVVPFQSLRTAFQKKTFLPVSSAGNVFTPRFQLQAIRSIWIRSEETPNENALKFLPGLDILPPTIGSCEFMRGQGTVNSPLAQKLFDIDGVDSIFFGKDFITVSKGAGTEWAQMKPEVFSVIMEHLSNGSPVLSEEPLKGASDTQILESDSQIVAMIKELIETSIRPSIQEDGGDVEFRGFDEKTGTVSLKLRGACRTCSSSAVTLKNGIQQMLKHYIPEVENVVQVLDPEEEVAIAEFEKFEQRINGNKQKADNK Q9UUC2 YGR1_SCHPO SPBC365.01; CHAIN 1..355; /note="CRAL-TRIO domain-containing protein C365.01"; /id="PRO_0000210749" MADIPADRKKIVQEGWSRLFSDIEQPSYIQKFPSQESLYVSFFEQCAFDDFDLTLLRFLKARKFVVTDSSDMLANAIVWRQQANLRSIMVRGENGLNQNFVKASMYFIWGQDKKGRAIVFLNLHNFIPPKNTKDMEELKALILYAMENARLFLDSEQNAAKGVLGLVDLTYFSRKNIDLDFARVFAETFQNYYPEILGQALIVGSGFRMALFEGVWSIGKYFLDPEVRSKVTFCKPAQVSGYVDSKYIPLSMHGQFDETKLYERAPPETAGIGKPENYEELDKEYVDAAKEFIRLTREWIYAAGKPQEAEIEEKRKAFKYECKKLWRKGVALRPPNIYQRLGLIDANGHVDWSKA Q9UUC8 RM51_SCHPO SPBC19C2.12; CHAIN 1..145; /note="Large ribosomal subunit protein mL43"; /id="PRO_0000372633" MMIEIIPKISIPKNGLGSFTRPCRRIEFSYCNWGGSSKGMKEFLSTKLESLAKESQDVEFHVTNRQGKHPLIRAYYNTGREKVICTRKMSASSIFQKAILCRDSDGLKPRLIKYPVESTNPSVRGIWSPFSDQAKPHEIYKKKSP Q9UUD0 YNQA_SCHPO MOD_RES 285; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 414; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC19C2.10; CHAIN 1..501; /note="Uncharacterized protein C19C2.10"; /id="PRO_0000303940" MNKHFAKLSQWTGEKFGFDRQKTTLSDDFCSLKGETDAWLVGMDKIHRSCTRWVRNMDKRKGLLDEKDKQLPVTHVGSSFVELGQALSHSSSNSHTYIMYGKSMVEIGHLQEEFMDYLNNSFLANLENSLAEFKALDVKEKKMENRRLVFDALSTKIQKAKKEESKLEEDLRNARAKYEESLEEFEDRMVQLKELEPDRVENVVRLLQMQIRFHQKSLDLLKGLEMNGFSKKRDNVNIPKRTYSARSIPSNISSTNVATTPSNTIFEMDDTLKADSSSNEYHSPTNTLPSYHTEADLDNSSIASSNRTQHTEDNYNKDVSDAQNSLGQSAVDLTTPSSPPIPRHTKPKLSTTQSTPVKPASLQSEEDIQLSFKQPELSASSAELDEKLKSQCNVSPSPSNISDAPPSKLNRSYSSPLASISSRKVVRMKYSFEPETENELKLKKGDLLLVLKEIDEGWWVGEKLGEDGVFTGNTGMFPSNYCVPAHPWDKTFRAFLKKGFK Q9UUD4 MU124_SCHPO SPBC19C2.06c; CHAIN 1..145; /note="Meiotically up-regulated gene 124 protein"; /id="PRO_0000116857" MRLQSLSSVAIAETRRQIILTIINSLVYLVNFISCPSIHSIPFHISTHLTSCQANISLLKIVGLHCPFHRRGIASLSVCVALHWIAFSCSVMCHFAWSCALPCFVDSFFPSNFFLRTYALFTFSLQLWSGNDLQGNHSYLATPTR Q9UUD8 YOD1_SCHPO BINDING 305; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 316; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 316; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255"; BINDING 384; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 414; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 428; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="1"; /evidence="ECO:0000255"; BINDING 428; /ligand="Mn(2+)"; /ligand_id="ChEBI:CHEBI:29035"; /ligand_label="2"; /evidence="ECO:0000255" COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; Note=Binds 2 manganese ions per subunit. {ECO:0000305}; SPBC18A7.01; CHAIN 1..451; /note="Uncharacterized peptidase C18A7.01"; /id="PRO_0000185097" MVSFESSFERGTDFLNRNFKKCLFACISIFIFALLALSFLSLLQPDTVQRLYQCAVPSMIYVPPMINEAISIQHEEFNNRRRRLSAALREDKLDALIMEPTVSMDYFANITTGSWGLSERPFLGIIFSDDEPYPGDVASRIYFLVPKFELPRAKELVGKNIDAKYITWDEDENPYQVLYDRLGPLKLMIDGTVRNFIAQGLQYAGFTTFGVSPRVASLREIKSPAEVDIMSRVNIATVAAIRSVQPCIKPGITEKELAEVINMLFVYGGLPVQESPIVLFGERAAMPHGGPSNRRLKKSEFVLMDVGTTLFGYHSDCTRTVLPHGQKMTERMEKLWNLVYDAQTAGIQMLSHLSNTSCAEVDLAARKVIKDAGYGEYFIHRLGHGLGLEEHEQTYLNPANKGTPVQKGNVFTVEPGIYIPDEIGIRIEDAVLASDVPILLTNFRAKSPYEP Q9UUE0 CTO1_SCHPO SPBC17G9.12c; CHAIN 1..274; /note="CTO1 family protein C17G9.12c"; /id="PRO_0000351421" MLYIVDFDETITTYDTIHLLAEAVNKPEEWSVISDKYWQEYLAWREALPHSTTLTSYLPLLGGSRYLEEASIKRIEKSQYFSGLSEGALDNIVQLITLRAGFVEFINALVPDLRVSKTIFHVLSVNWSARVIEQTLLHHTDLTADLLCVHANDFDFDTSTNTTNGRILARNASSLLMNSTDKVREFRRIVQTDAVSSPLNVVYIGDSPTDFGCLQISPISILMRSNQKYYDILSRFEDVQLVDISEFPVQKAVPGKKIIYTCSDWCAIQKAFLA Q9UUE3 YNZ6_SCHPO ACT_SITE 286; /note="Proton acceptor"; /evidence="ECO:0000255" BINDING 248; /ligand="substrate"; /evidence="ECO:0000255" SPBC17G9.06c; CHAIN 1..334; /note="Putative lysine N-acyltransferase C17G9.06c"; /id="PRO_0000353804" MSFTVWSKTEPFKLSAVQESLITLEHDNKRLLLTYREESKTWDIDLNGFQDMDVNEILQLAFLSIFYVFPTLRTEVVLQWANIESQKGTLSLPVEYNELEGNVSIDRMSFWQIPSPWMYTRCSDWPLSYLPNQVIRRPKCPKPGSTLYERFIPSLNETLSFVSLDIEQHLQYFHEWQNKPRVEYFWNESGSWDQHHEYLTTLQNDPHSFGVIGCFNDVPFAYFEVYWVPEDRIAPFAQPWHTHDRGFHALVGNDKFRGPHRVPVWLSSITHMLFLDDPRTQRVLLEPRIDNSKFINYLIEENYSKRLEFNFPHKRAAFMEITRNMFFSCLGPRI Q9UUF4 AIM19_SCHPO SPBC17A3.02; CHAIN 1..119; /note="Altered inheritance of mitochondria protein 19 homolog"; /id="PRO_0000351438" MENKELRKSYFQRIYQSYIPAYAFGGALIASVPRAFKRPYGGPFVPGCLLCGGFNAIGGLAIASGDLTNGSGICTAWSIAYLMINATKSIKSFRLYPIALTTFATANAVGYGKTFMNEY Q9UUG6 YFT2_SCHPO SPAC926.02; CHAIN 1..443; /note="UPF0656 protein C926.02"; /id="PRO_0000351422" MSFSRNQVLKGLKTKKAKPKKNPTVDELFEIAIDLEESGDRWRLEPAKCLRFYQKSLETYDRYLLQCPNDFDARFNKARLLLNMATNCDMLYKDSQVCLQKSIEMHKHALLLQEAPDIWFNLAQVHLNLAEIWVDLDREDLAYPEIQQALQSISHSIDLQERERIEWENTIQTSSQQKYEEIPDIQARRLYFIEADKEASTLVTEIASLACSCKLLEESDFEKLCQIMLPITEKLDILKLMDWYLAKTKRLVLGGKENEVAWIDLLQVFDHQLSQLPQLNLQNPLDPNSSVKPLHIQLLCDKADAYIDFAETLLDSCVSTEESASIEIMTRAWNMLGVAAKSLKMANTYNPNHVRILISRADLEIQRAAIPIMVAQNSKLVLYKNAKVLYEKAFRDYSTKKTTRTFAEIVLKHYQLQKLTNPETIKMLDSLTEVAQEDILNTI Q9UUH0 YKIC_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPAC630.12; CHAIN 20..422; /note="Uncharacterized protein C630.12"; /id="PRO_0000310852" MKVGRFLVIIAFCFYVLYLEKIIHTRPHKKCDWRSWEQWESTGNPVRIALVADPQLVDDLTYDYPRPLIGIVKWISDQFLRRHWRYLHKSLKPDITFIMGDLMDTGREFATEEFKKDYFRMMNVLDPKFTNKLEIYPGNHDIGFGNHAIVKDIQRFESLFGPTSRSIDVGNHTLVIVDGIRLSNNVNPQVYQPARDFLKSFETNKDNSRPRILLSHVPLFRPAINSCGELREKDDVIKYGLGYQYQNLLLPELSESILKAVEPIAAFAGDDHDYCEVVHNYQVDTREAATTEYNVKAFSMTSGILYPGYQLLSLNYPYDNPKADQKSSYQTKLCILPNQIQIYVWYGASISIFFALILLRTAIFFFGTDRYSLPLYKTHARRFSLSTTIHLFKKIVRITLSTFISYTWIPFLLFIFLNIFII Q9UUH2 BMT2_SCHPO BINDING 111; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03044"; BINDING 131; /ligand="S-adenosyl-L-methionine"; /ligand_id="ChEBI:CHEBI:59789"; /evidence="ECO:0000255|HAMAP-Rule:MF_03044" SPAC630.10; CHAIN 1..270; /note="25S rRNA adenine-N(1) methyltransferase"; /id="PRO_0000351423" MRPIPVKNRIGKNNIDNAKGLKGNKLIRHYHNLLKEKSRLIASSAPIEKIKNVESELENIGIDAYQRASRSGQAEGKGGDSSKILIKWIRTTPCFSYCARLKEPKDLLEIGSVSVDNKCSTCGLFRVSRIDLHSVHPLIKQQDFLERTPEEGLFTGISCSLVLNFAPPELRAKMLLHCTGLLMPPNKEQPPWLFLVLPSPCITNSRYMDEKTLHSIMIQFGFICRQKSISKKIAYYLYSYECFPMKEIDWKKKIVNDGATRNNFFIPCIL Q9UUH6 YKI6_SCHPO MOD_RES 14; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC630.06c; CHAIN 1..188; /note="Uncharacterized nucleolar protein C630.06c"; /id="PRO_0000351432" METVKVTRKDLLLSPENKEIDSLDDVSALLSQRLSNVFEFSIASEEVQSDEVFEDTYPNDDQATFNLFSDVNTVVTKVTEPSIKNSRPLNYYILEDSPERQRQLQASVFTYDQLMKAKEEKWPACQKLHKVVSIKKEESKHRRRPSKKRRIRMKLLREKEEQLKRQAMAAKRNRFRKNVRKLPNKKKH Q9UUH7 GYP7_SCHPO SPAC630.05; CHAIN 1..743; /note="GTPase-activating protein gyp7"; /id="PRO_0000312838" MTTLESLDMPEMTEVEDDTVDIHIDNSKVALLFSKSKVFVHPTSKMKDNISGYLSLSKSKALGNSSVAGSDILLSWVPDSFLKNRPRDLSVFQNAETLSNGSIREWVEIPQHLDYSFSVRLCSIYSIIFRPPRYGWNYGSIVINLRDSGESLPPLFFHDDECISTIEYGKQITRDRFDPFDESGNMFWGGTHLLMQLKKYASLEQSSHESQLYLVNPSPEDTVAFQSVELQKVISNNRLNSSSTPPTPRSSSSIFNPFRRALHDLSFTVLERFSRVTNYGKSEVDRLMEHKVTKSILPHLPRELQVLLESKRVQKLTEEYDPARMFLARWAEGIVEQSESNNSQPVNNAGVWTDAQREEDSSLGPFELVYIEERVKRDDPLSVEQWNSMFNAHGKLQVDVHRVLGIIFHGGIQPSLRKEVWPFLLSVYPWDSTSEERRVIYLSLQEEYCTLKRKWYEDIHKQFNDRWFIEQRNRIEKDVHRTDRQHEYFQIEDLPHPDPQSTFTGTNMNMEMMKDILLTYNEYDTELGYVQGMSDLLAPIYVTFNDNALTFWGMVGLMKRLHFNFLRDQSGMHRQLDTLRLLIEFMDPELFAHLEKTDSSNLFCFFRMLLIYFKREFDWEVLLKLWDVLFTNYLSYDYHIFVAYAIAERHREVLLNQTSAFDEVLKYFNELSGKLALEPTLICAEQCFYQFKNKLALIDRKQMEETNSDEDGSKETDLPTIAPYLRNLLKTSQPQYTPSGKQE Q9UUH8 YKI4_SCHPO SPAC630.04c; CHAIN 1..166; /note="Uncharacterized protein C630.04c"; /id="PRO_0000304110" MGEEISAIDLVMANDQLVSTSDASDIPYDPYSQFWGKVLVLTFGIICVVFVIFMLHHERIKACRTIISAREQQRTQHSIHRRERSSSGASQQFEHHVRQTDCLPLYEPITALNQQYLKTLPTTSTPPPPAIFDENGEFVGDVPSVAGAIERPPSYESLPAPQNDEV Q9UUJ5 RM25_SCHPO SPAC1952.14c; CHAIN 1..145; /note="Large ribosomal subunit protein mL59"; /id="PRO_0000351440" MPVFTKEALERLPIQLGNFFKKFPPENPNAWTTNPNRQNPFLATRNPQNGLVINPYYSNRRQAEIYKEARLQNLDNLLPQQMSWQKDSTRHILKGLLNPKGKISERKRDEILENRRLKLSESLKKTSKFKNERQKASKIAKPSPF Q9UUJ8 YLOA_SCHPO SPAC1952.10c; CHAIN 1..361; /note="UPF0658 Golgi apparatus membrane protein C1952.10c"; /id="PRO_0000351425" MKKFLSFKPAEDFLRSLKKSSQWFLLIIIVEVTITLSFEGYVFHHFRLITVEKIDVFINAMVPSTFALFCMACPYLLYTAVDALLNKDVIQMSALLIFHVSLFCLSVVQYFQIFSKDPRAIFLSALYLIDPIRLVTSFNYHERIVVNSHMLLFYLKPFVIALPVLIGVTCILLSFLVYKMNKAFGWIMYQQHGPDLRMRRRYLVYKIFMSLIKSDYYFCLTATVQYAIFFSTISRVGLALTILVFPCTIATLMTCRYAVYRENRALLGIVQFMFMCGLAYFIYNCARLYLGVDYGDIAVANICMLVFSIVTIIYLFTTIVVGFYCISNFGYGLREYLRYIHQKQKVNAAPAVPKVRMPLDD Q9UUK0 PDXH_SCHPO BINDING 62; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250"; BINDING 69; /ligand="FMN"; /ligand_id="ChEBI:CHEBI:58210"; /evidence="ECO:0000250" COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; Note=Binds 1 FMN per subunit. {ECO:0000250}; SPAC1952.08c; CHAIN 1..190; /note="Pyridoxamine 5'-phosphate oxidase C1952.08c homolog"; /id="PRO_0000315948" MASKVDSSHEFPSQIKRCLSSSKYIQLATCFHDQPHSSLMTFTYLPAGSAAPYEVEDCIILSTGENSKKYFNISSNPRVSLLVHDWTTNRQETDPDASSLYTLLYKMNQAQFSNTSVTLNGLATVLPKNSKEEEFFREKHLNTNDKGNTKQYVEGEDMRIIKIKLESARICDQRLNNVQKWNARGDETPF Q9UUK4 YLO2_SCHPO MOD_RES 121; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAC1952.02; CHAIN 1..202; /note="Uncharacterized protein C1952.02"; /id="PRO_0000372368" MFSSKRYLNSFGWEEGNALKEGGLTKPILTSRKYNTHGLGAKHDIADQWWDNVFSAQLQSIQVNTDNGKVAVQSNGVSTKLRMAKYHSKYSALSSVFRYAGRLCGTFEEDLVDKSLDSSVSPVSSKKVKVRKTSGKESSKREKSKKKKEKKEKKDKLKKKSKRLKLDDSHTQKRKRKVRDKESKKSSKSGLKKVSGTKKVKA Q9UUN5 PRA1_SCHPO SPCC306.02c; CHAIN 1..171; /note="PRA1-like protein"; /id="PRO_0000220886" MSALSLSITKVSETFSEIYASRAQYLSGFKSVGEFLDVRRISRPRNFSEAQSRISFNFSRFSSNYLAIIAMLVIYALIRNPLLLIVIGIGVGGVYGIRKLQGADLQLSHRVISNQNLYVILACVLIPLGLFASPIETIIWLVGASCVCVFGHAAFFEPPVESAFETVEQQV Q9Y6Z9 SOU1_SCHPO ACT_SITE 148; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 163; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:O93868"; ACT_SITE 167; /note="Lowers pKa of active site Tyr"; /evidence="ECO:0000250|UniProtKB:O93868" BINDING 21; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4"; BINDING 95; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 163; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 167; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 195; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:O93868"; BINDING 197; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000250|UniProtKB:L0E2Z4" CATALYTIC ACTIVITY: Reaction=D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH; Xref=Rhea:RHEA:14609, ChEBI:CHEBI:13172, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.289; SPAC8E11.10; CHAIN 1..255; /note="Sorbose reductase sou1"; /id="PRO_0000054777" MTSMFSLKGKTTLITGGSGGIGFSIAKAFAAAGSNVGLLYGRNKKALEYAAELRDKHGVQAKAYSCPIENRSAVIETTNQAVEELGGRLDVMIANAGIAIPHLSLEDKNEDIWTKVVGINLNGAYYTAQAAGHHFKKQGKGSLIFTASMSGHIANWPQQWASYHATKAAVKHLARALAVEWAPFARVNSVSPGYIDTDLTLYADENLRKKWKEYTPQARIGLPDELPGAYLYLASDASSYCTGSDIIVDGGYCSR Q9Y7J5 YOI9_SCHPO SPBC1778.09; CHAIN 1..414; /note="TBC domain-containing protein C1778.09"; /id="PRO_0000312840" MENPSPTRTTNLQRIRSLYRLQEDKNNLNIPEPINGKVQEIDTKESLENVDRYGNYRSDFNVNNLGFYKVSKDPTLDKPNPAKRLGNKLIGHDDMLKYVDESIFMVVPGESHDRNEISAKELSRIQKWKSMCSIHLVSGNQLHSFRKTRKLILRTFKGIPDCWRSIAWWSFLVDSLPDKKLIDKYYQLNEQICDYDVQIDLDVPRTAATHFLFRKRYIGGQRLLFRVLHAVALYIPRVGYVQGMASIAATLLIYYPEEQAFIMMVNLLENRGMGDLFSSGFDTLLKAFDMLKHELSFTQSGRHLAEIGAEPSAFATRWYLTVFHQCVPFHTQLRIWDLLFLLGGSKGQTVRLLQATSLAVIQGMWDTLIDADFEVVMQALSGVIPIQNDNALLARIQLFWEKMPSENSSKSKRN Q9Y7J8 YGL1_SCHPO SPBC216.01c; CHAIN 1..836; /note="Uncharacterized protein C216.01c"; /id="PRO_0000116761" MDSTKEEEDLNNNIDEISDGENEEEELDEAIAAALQKIEVPSIPRRVKVYEMEDENWVDCGTGYCDGKIEGPLAYFIVRSEADNETILLKTQLIAEDIYSRQEETLIVWQELNGTDLALSFQESSGCIDMWMFLANVQKAISSVTRSYSNDDILTDEGALNENYLNTVDLPAPELANLKEIEEAVYGYMQSIQSRDSLVRYVSNENYIDRLIELFPLCEDLENTDDLHRLCSIIKSFVQLNDAPLLESLFSNDEKLMCVAGILEYDPEFPNIKANHREYLMDSKKFKQVVPIQDPRILAKIHQTFKLQYLRDVVVSRIVDEPSFSVLNSFIFFNQADIIQYLQTNEKFLHELFSIYVNEGEDDQRKQDGIFFIQQVCNIAKGLQFQSCSALFATFVKFNLLKALDYAMSHENNSVRNAGSDILVSIIDHEPAIVWQKFDQDRKDASSSLSNAHVSQHSLLSNLINILHKESNPGVLAQISEAFKMLLSLPGSYAYNNPYRNADGNVRNKTDNIIGINFIENFYDNSFNMLAAPLLELENVSSLDVKKLDMYMHLCELFCYFFRIHDYWSRRFDTYKTLTSKVALLLYSDRKYVVLSALRFIRSCLAARQSEMSLIMLETDTYGKVLDLMLKVKDQTNLVNSAALEFFEFLRSEGSEDTLDYLNKNYRPQLESLNNLSTFSELLNIIDGLSSDSRSPKTVGTHESNSYEFDGASNNNQRVGDDVSKDWEIQQDFSIENDTELSEKVGQRTVLDSIAPAELNIEDSCEQPKQPILEDRYFLESAVYDTSAESSGINVSNTRYSKRKSDFQVDDQQADDESPKKRLSIDSSSAQNGYAS Q9Y7K0 YGL3_SCHPO SPBC216.03; CHAIN 1..247; /note="UPF0659 protein C216.03"; /id="PRO_0000351426" MTVFVVFGGHGKVALLFTKIATEAGHIVYNVVRDYVQNEDIEKVHGRTSVCSLEKATPNDIAQFLAEIHPDVVIFAAGAGGKGGPERTRAVDYEGAIKVYDAMRIAGIRRLIMISAIDNRDMSQPPPPYYTAADIELSEKIHQSIGTYYHYKYLADQELVRRSSDIDWTILRPSGMTDEKGSGKVALGKISINCMMSRENVARTVLLFALDNQSIHLVVDMTDGNVPIYKAIAGFVVKGESSYTYSV Q9Y7K7 TVP23_SCHPO SPBC2A9.05c; CHAIN 1..219; /note="Golgi apparatus membrane protein tvp23"; /id="PRO_0000212836" CARBOHYD 34; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 95; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 108; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 200; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MFTSLDRNLYVDNHITLTKMDYQNTETIAEQERNASRLPQMFQMSSHPVALFFFLLFRTGAIVAYILGMFFTSSFMLLFIVIFTLLAVDLWTVKNVSGRLLVGLRWRNETGVDGESIWIFESADPSRPRNAVDQKTFWYALYLYPFIWIILGIVAIIRFEFLWLALVAVAIGLTSVNTAAYSRCDKDAKRRWATELADSNSSGFVSRFLSRAFIKRFIG Q9Y7K9 YGI7_SCHPO MOD_RES 130; /note="Phosphothreonine"; /evidence="ECO:0000250"; MOD_RES 131; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 243; /note="Phosphoserine"; /evidence="ECO:0000250"; MOD_RES 245; /note="Phosphoserine"; /evidence="ECO:0000250" SPBC2A9.07c; CHAIN 1..246; /note="PARP-type zinc finger-containing protein C2A9.07c"; /id="PRO_0000314104" MAESGAGYRVELAKTGRAECKGTVCGRSKIGKGDLRFGTFVDVGKFQSWKWRHWGCVTERVLRNVNKKFEGDIKNCLDGFNELNDPIVQEKILRAFEQGHVDEEDEERCRKMASDASEEKDRKIEEGELTSEEEKEPIQDLRKSHKRKSVEKSSVPNKKHKAERKRSPSPKIEILEDDEEIEDVASDKDEEEKPWSGDEEDDDELVVKDSEDETEGVSTIASQRPRRSARRKVDYAESGNEYSDSD Q9Y7L1 YGI9_SCHPO MOD_RES 222; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 223; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC2A9.09; CHAIN 1..233; /note="Phosducin-like protein C2A9.09"; /id="PRO_0000316246" MNPDEDTEWNDILRSKGILPEKEPDVDDVLDDALVDAKQLAHENRLENKDLDELAELEDEEDDEFLQMYRNKRMQEWKDQMSKAKFGSVYPISKPEYTAEVTDASKEVFVVVHMFQDSLPACKLLAAILERLAPMYPQIKFVKIPGKQAVENYPEAMMPTLLIYGHGDLQQQILTLATLGGMNTSVVDVAEALVRAGALKDSDIAALKDPQNAEDELGKRDSSVNDDLDDDFD Q9Y7M5 RM10_SCHPO TRANSIT 1..78; /note="Mitochondrion" SPBC9B6.06; CHAIN 79..254; /note="Large ribosomal subunit protein uL15m"; /id="PRO_0000315949" MFNILSRVCRSSSFHGFLRSSGYPRFGASFRGISMLNDLNNSANYQSKKRVGRGPASGLGKTSGRGHKGSGQRRGRRIKPGFEGGQTPITKLFPKVGHSTGHLKKPLRLGLGRVQEWIDRGRLDASKTITMKDLLDSRCCRGIKHGVELTADEPGLLKTAISIEVSKATVQAIQQIKNAGGSITTVYFSPLALRAHLHPSSFRTPPRPPLPVSKKDIRYYTNPHFAGYLANVKNIRELYYGDQRFPYEPIVKDK Q9Y7M6 RRP1_SCHPO SPBC9B6.07; HELIX 10..12; /evidence="ECO:0007829|PDB:8EUY"; HELIX 16..30; /evidence="ECO:0007829|PDB:8EUY"; HELIX 38..53; /evidence="ECO:0007829|PDB:8EUY"; HELIX 58..70; /evidence="ECO:0007829|PDB:8EUY"; HELIX 80..92; /evidence="ECO:0007829|PDB:8EUY"; HELIX 100..125; /evidence="ECO:0007829|PDB:8EUY"; HELIX 130..143; /evidence="ECO:0007829|PDB:8EUY"; HELIX 155..172; /evidence="ECO:0007829|PDB:8EUY"; HELIX 184..192; /evidence="ECO:0007829|PDB:8EUY"; HELIX 196..205; /evidence="ECO:0007829|PDB:8EUY"; HELIX 210..212; /evidence="ECO:0007829|PDB:8EUY" TURN 7..9; /evidence="ECO:0007829|PDB:8EUY"; TURN 71..74; /evidence="ECO:0007829|PDB:8EUY"; TURN 77..79; /evidence="ECO:0007829|PDB:8EUP"; TURN 93..97; /evidence="ECO:0007829|PDB:8EUY"; TURN 144..146; /evidence="ECO:0007829|PDB:8EUY" CHAIN 1..217; /note="Ribosomal RNA-processing protein 1 homolog"; /id="PRO_0000340114" MSAPSPFIKKLAANDRKTRDKALESLQRFLSQKKKFERLDFLKLWKGLFYCMWMADKPLYQQKLSDNLAALVPIVWIDNRILFQSTFWETMGREWTGIDILRTDKFYLLMRRFCAAAFRDIQTRSKTALLDKVVAEYNQMWMDGPFNTENLAFPNGILFHLADIWTEELRKVYPEDVPKADWYLPFDSTIKSSHNVVLRKTLPKRLDRVSEYTKDSQ Q9Y7N5 WTF16_SCHPO SPCC1450.08c; CHAIN 1..319; /note="Meiotic drive suppressor wtf16"; /id="PRO_0000193229" MKNNYTSLKSPIDEGDESKTGHEIDLEKGLLPEYDSEEEGALPPYSDHARVSNSPNTHRENNPSRSTDNSSPFLIKLLISFTPIYVLNVLAICYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWTKAVKVTAVGLYNSRKKWVVIIWLLWVVICFVLFGCIKFGNLNLDKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEATSLFVIGNFFFFYEMECPGALKRMPKFIRNGIASFLEGIGNAIGRIGNAFRGANDNNNNIPLEETEAESEV Q9Y7N9 YCKC_SCHPO MOD_RES 260; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 597; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 761; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC1450.12; CHAIN 1..821; /note="PX domain-containing protein C1450.12"; /id="PRO_0000315963" MDTASPEEIDALKRHYLKKELFSLLIADELNFVSEPTNLDHLGSPFVEKGKSVIPYEKSQIPVLRFIFKRFILTFPFLDPDSQNQLWNVNFRNLLKSLSKSNVSVLPDDSDATHLHKWLLKFQNMLTLLMSRAFHSIQDEKNINIELLDTPKLEKDLHKSELQQKPNILEAYVLGVRQSTQAKMLRTKRVYEYLIKVSYEENTFFIARKYSDFSHFHHLLLKSYPNAYVPRLPPKDDHDTYLNSSEDSTLSPLPSRSSDTNDPQSDSQHVLRQERMRIELRQYIKNILNDDELHLTEEVLSFLTDDPVTLTASELTDINFRQELDVIRQLEQQKFVEIASQRAKELDVYMEEFKRSLTENNGFTTLFTELKEKNSISELSPSLQKTIEWARVNLASTIYDTFIGKEKSLETYLQIKKMHQLFPYTVIKNIMRFSNPLSVMKRILDTLLAQPFGMKSLFQRLLSISLNENVRAIHKLISRYEARIVSPEILTKIQEQVENPCKAAREVLEKKQMKRHDYLYFILISDDVPPKLPDNLIRRVYAERTAWKAALDSEDYPTDPTVIRRSKRYGYMMKLMHLYAKQFNKRRSISLISEGATGEIMKSMVDSPELNPNILVEQFIDLVRRHEDSFYDFVHRVYLHDSGLFASLMEWIENIIGFLRQGTSAPIDMDLVVDALDEESRQALDVELNKLLKWNQRKKSALFLRKTTKYIPGEETSLPVTMDELGIDEEIMAELRGDEDDQDENDQVTKVEEEHMEDDDSVEEFDPIIEERQRMKRKANRPANIIPPKPKLRTVKTLLPAFKEQVYPILHKFVSENEKDI Q9Y7P8 YQ64_SCHPO SPCC191.04c; CHAIN 1..100; /note="Putative uncharacterized membrane protein C191.04c"; /id="PRO_0000303976" MHSVCSIFLSCSHRVIQAKHPPFPLFHSYFHIPDFLSFVFPFVASPPLAFARRKLDHVPKKFARSIGPFLLIVFLFFNLFPTFFFLPFFPDTTKRPNLAD Q9Y7P9 YQ65_SCHPO SPCC191.05c; CHAIN 1..211; /note="Uncharacterized protein C191.05c"; /id="PRO_0000372383" MTGTAKVSIPKAQPHKVPCVYLAGDLVFRPNAIELFDELKEICKDAGVQGVAPFDGQEGVEEMAPGAETSLKIAELDRKLMDRCDGGIFCLDPFRRAPDMDPGTAVELGYMAAQGKPLAGFTTDGRMYPEKVRSYRKQAWGDALKPRFTKGGSGSMEDADGLIVHSEGFLQNVMTEGFIRMSGGFVAVDFSIQEAFRTAIKDLAARLNSQH Q9Y7Q1 LTO1_SCHPO SPCC191.08; CHAIN 1..134; /note="LTO1 family protein C191.08"; /id="PRO_0000337685" MDWEEVTKLEENEYKRGYDEGILKGIEQGYEEAFLFGLEHAYNKYLLAGEIYGRVCFWLKEENSQHPKIKKAHRHLEQLKSLLESLPTNNELEETDAGFDSYWNKITAKAKVVSSLLGTKILPAEKIDANDGFE Q9Y7R7 RL1DA_SCHPO SPCC306.07c; CHAIN 1..284; /note="Putative ribosome biogenesis protein C306.07c"; /id="PRO_0000353841" MAITSEKKKNLKSLDKIDIKLLEKTIRALLQHIRSSDKPIEKEKVYIQVNTFQPVEKESLRRPSKVFLPHRIMHVTDACLIVKDSQQTYQDLVEQQGLDEVITKVLSIPRLKLKYKTIREKCELRDSHNLFLVDDRVLKYIPLLMGKVFEQKKIKPFPISVLQKKETLRNQVARCLHSTYLKLSAGTSHTILCGLATQTNEQLLENITTVLKCLLTNFIPKGWSAIDNVAIKTADSASLPIWTSDTNLAAHKRHIVHIQDARPLKKSELRAQKRGSSGEGKGNK Q9Y7S5 YQO6_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPCC569.06; CHAIN 20..478; /note="Uncharacterized membrane protein C569.06"; /id="PRO_0000352822" MKLFPLCLSALVMSTATCASSVEGAIEKVPQSLEQKGPSEMLSMKPDVKGGFGDRMMFIPFQSDLGLHSPVDRSGFEYCGYLDAIESEDGDSSRAPYAKLQLKENVEGIARFGLFYHPSPFQAFKHIIDNGGKYSGLDRVFLENLRKSLVVSLDSAVNRTYSIPVEDEGFYCFVGYQEVAHQETVIGENSEPIVTIEFDSFNSNVPVTLKLQRQIFLSFSIVYGLISLWWAIRCICSRTKLHLVQVCLFCWFSFFILNHPVKQRIFSIDNPDEYLVPFVVSCFTYFLGDGIEYALYSLFITTTVLGFGTIRRTSKKMVLFFSLLTCGQAFLVNVAPMVYPLLYISGSDKACVLRMVWVFNKFLYLPLITFLGAVLAFRFRLKKASQFDTRWNLFALTLAIIILFAFNDLVIFDKLQKLWKYDDTTLEYLKIVNGGIKFVAFSILLGPYSKLFAEPKSLQLDDFLGKHDGHKDPSLEKF Q9Y7S8 YCX5_SCHPO MOD_RES 68; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 92; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC2H8.05c; CHAIN 1..217; /note="Uncharacterized protein C2H8.05c"; /id="PRO_0000116559" MQDSSKNKQPCVSWKVSPLKAKAMSPDDVSRLFCKSSTSSATRKHDPFHKLWDRLQPKAQSTIQRTSSLPVPSSSNFKERLNNIGGLKRSRTLESSYEDETETANKLSRVSSLVSVIRQTIDRKKSLERRVREEQEEKTDNEDDNDVEISTQESLENNGLAEKKDDTSSLATLEDDIEGQEFSFDDQDLQMLQDIEDQWLSSQKQQGSPLTSDHISK Q9Y7T0 YCJ3_SCHPO SPCC63.03; CHAIN 1..612; /note="Uncharacterized J domain-containing protein C63.03"; /id="PRO_0000310354" MDEADSWELYLALGLPKDATSDQIKESYYRLSRLFHPDRHTADQKAAAEEKFQIIQHAYEVLSDPSKKEIYDNFGEQGLKTDWNVGFPGKSAEELKNKIREQIQERDIHEIDSLVQSRSETTIVVNMTPLFARNIRVQNALGLGAGTRMLTPYERFSLIQWVSFQIKSSFSIPTSFSNDLKKPSFNSFSSGSFDDEFSAPSDEDEGNHKTSSRLSIVTEASMRQNSKLQPSIFAVYHSQPSPNLSSEIGFSLLRPGLITVKSVYAINNQTFIVPLIQISGLKRPPQATVVIGRQITRFGTLTARWKTGVWSLGSWGIASPRGANSSFSLTWQQMKAIPNSLVPQLSWNAEVTAGLMYSGIAYNYNLKNATEDSPYQIKLGTSMSTVGGLQVSGDTSRKVGRYSTFGVNISVGVPTGSITFSLNWSRLGQKISLPIMWCSVFDRSAVFWGLVFPITSILGVEQFFLRPRRLSNQKRLRLLRLQKLKDSQERKKVSAIRAVKLMKEIVEKKQKLEMEKGGLVIEYAEYRVVNCGANEPDLKQDVTISIAALVENSRLAIPSSVSKSSIIGIYPLFSDNEKELEIVYTFHQQRHRVVLRDKQGVFLPSREHKILS Q9Y7T1 YCJ5_SCHPO SPCC63.05; CHAIN 1..323; /note="Uncharacterized protein C63.05"; /id="PRO_0000218624" MESKSLRELWEETEKLKDSSSTDEKTRSEIVEGYEKCLKLVLQLRIFSSNEEVDEIKTSELRYLMIDYELAKCVEQWTKGDRLKAVQYAKTHYETFLSICDDYGLKPMQDEKPKTEADTRTLKIARYRMRQNLEKELKALSKDSETNEEQERKFWLTKLQIAVEDTLDSLPHIEMEIDLLKRAQAELMKSEDSPEKDEETLRREERKQKEGSSWRLDLNTRDKILDKNNRPLQPFTIVSDRNETRKNVFGFGYNLPTMTVDEYLDEEMKRGNIISQKDNPPKSDSDDEDDYEKLDAKTMKDRYWDEFKEANPRGSGNTMVNRG Q9Y7T2 YCJ6_SCHPO SPCC63.06; CHAIN 1..331; /note="Uncharacterized WD repeat-containing protein C63.06"; /id="PRO_0000316552" MVTASSSVRVSNEDECFIYDIEQLKDNVVVSYSTGSWSCFDKGTLLEIFKVPKAHTNITGIISCDQLNGVITCGSEGEIHLWDIRSQAKSAVRSWTQQSTPFTCIALNKKNQFATGSELTRSLASVQLWDVRSEQKLIRQWNDAHNDDITHLQFHPKDNELLLTGSVDGLVSLLDTTKEEDSTDPEEDPLLHVINHGASIHLAKFVSKKRVMVLSHMESYAMYKLKRDKDEKTWSSNELFSIDDLRAELSCSYVINEVSTSDKQFCALAFGDFSNHETKFVLVDTSTGELKKEPTKLERASEEICRAISFDVKNDVYYSGGEDGLLQAFRV Q9Y7T8 PSB3_SCHPO SPCC63.12c; CHAIN 1..204; /note="Probable proteasome subunit beta type-3"; /id="PRO_0000148069" MSIMEYNGGSCVAMAGKNCVAIASDLRLGVQSISLTNNFPKVFAMGDKTYLGLTGLATDVQTLYELFRYKVNLYKFREERQIQPKTFANLVSSTLYEKRFGPYFSFPVVAGVSNDNTPFICGFDSIGCIDFAEDFIVSGTATEQLYGMCESVYEPNLEPDDLFETISQALLNAQDRDCISGWGCVVYVITADKCIKRLVKGRQD Q9Y7U0 YCJE_SCHPO MOD_RES 686; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 905; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 1018; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPCC63.14; CHAIN 1..1184; /note="Uncharacterized protein C63.14"; /id="PRO_0000351431" MSTLGNSTVKPTNAEFPGLHAMERYKPATSESLYVKGHYGPHPHKEHPAAYVAAKTGFNATSRRQSVREHHSSHEGSAQLNPDRILYMSAGAVTAAVPNKEHTDNVTTSQTIRYETSSQPSQEVYHPHAGKAAQSAHVMNSTESRPSSAHVSSSYTQKPFAFPLGPVFATSSQAAASETALPSGYEPDEARFIGASQLAKLSASHAHQTPAQTVDDDVPLPTRMAATELVGHIPLRAANYANEYSQDVPASTHRAASELVHGVPMRASGINDPKHDLDAATRHNINSVAAASYVAARSRVIEEEEEPPNEVKERMDYEADAQRRIRKMNVFGSAGAALRERTQQDLMANEQEHSGEFAGFSRNLTNTAAAPTTYEYKRPTSSYTAKDATSKVYRSNTYKPKSSVNGSVYRSKSVKSTTSHNKVPERNSVPAYNEKLMHSSAANAAILSHKNYSPPVQPTRDDEVSQEDARVKEIVRGMKLPLTSSSLSAAAYRPMEKQDPATVERHHIQAEATQRVRDMKLDLTKLESKTNDEIRSYRPRNVVIKPYAAATPPKNIPSTYRAPQAPSVLSPVVTASEGDFELDGITPERQQTMTRSTYQESSQRPFHEDPFRTHPGLLQAVARNHRNSLANIDERIMRQNQAATANTNTVSETDIEALERRLSKAYRMEAQEEAYAINIGGGRVISPEELEEIARRNVDPMVSELSERAAQERERKEQAKEAKRLKKLAKEEKRLKKKEEKARKAEEKRLQKERAKYAKQMSRESAHADQAIANTGPVAPPYFEHETEPSHYEEEEEEEPEERREESSHFSESSGNNEFEETEQEYTHGYGNDVLVQRTDVVNNFGESSHAHDNAVNEKRDLGRNGFGDVDEQDATEVYRHSIERIVPGDYLHDEKTRDTLTRESPAFRSEEAVVEVADEDHPHASEAERAHSYSNRKQASSESSPESQSTHYNDYEGTEDNIVRQTTTVDEDGHQEQTTSTTKVAHPIPVSNGLSSPPRERLDDNAKEILSRSSPKSPVAWFKRKFKNRKDKAAVKRMLEEDSSKQLSSGRDVVAPTSVNHDVSHVGESTKPAVNNSTKPVAVTSKNGHSRNGSHAAHSNNVIGTQPHVNVSAVPNTGNLKDALEGSAVSKTDDVDNVVSGHSNVNGVSKSRPNIVERSEDYVISHLPEQSRAPIGAAFQEDL Q9Y7U1 SFK1_SCHPO SPCC16A11.01; CHAIN 1..328; /note="Protein sfk1"; /id="PRO_0000351442" MDNDYTTSTTTSRRPRFWGFFFILFPLVSFLMWTIGLIVLLGLWSTQDKWHTPSEPDPVYLSDMGAYTKGFFIPMCVITGVFYFLTFIMIRLARQWGWIYPTGRKVETYLGWFAALTGAAAASCLISLSIRDDVHHDNVHWKFTAAFVVLAFVSAASNIFEWLSATRYYPQSSLLRVSFIFKFVIIVVGIICAIAFGGLHHNYRGRSARFEWVVCFLWSIYICLLCLDLAPALFYDSLASAPDLEKGAYATSVPESYVAPMEPPAAVLPDGEERYATPDLVPDTTAQYPYASATEPGVSNIPETRPERPVVYNMDVSQTTTTTRPVLA Q9Y7U8 RM37_SCHPO TRANSIT 1..50; /note="Mitochondrion" SPCC645.09; CHAIN 51..139; /note="Large ribosomal subunit protein mL54"; /id="PRO_0000339142" MPFIESMAPLSRAITRGISQFSCYSNTLVLRSSRNSSSSLVKRSYVSSRVSPKKPQHNSDATSSAQKVANKTHTSSVLPGTILKGLCIKAGGVDPVAREDHEYPEWLWSLLDEPAPNSKTARSHARKSAIRAANFLTKK Q9Y7X2 YOP2_SCHPO SPBC418.02; CHAIN 1..695; /note="N-terminal acetyltransferase A complex subunit-like protein C418.02"; /id="PRO_0000363382" MSKLSEKEAFLFDRSIDQFEKGQYSKSLKTIQSVLKKKPKHPDSVALLGLNLCKLHDSRSALLKCGYASSIDPKSQFCWHALAIVYRETKDYNNSLKCYQNALAISPNNESLWYDAAYLQAQLGLYQPLFDNWNRLLQLDSSNLEYRLCFTLSAFLSGNYKESLEQIQYLISSCNLSPLVVSRLISFLPRICEHIENGSQTVLEILLMNQNSFLNNFNFEHIKADFAFRQKNYEESIYLYARLLIKFPNRLDYSEKYLNSLWNFYKSGGLALDLLLKRTDSLIKTFSEILQTGISVLIFLLSKNLDYDFCLNHLISYSMHHFIPSFISLLKIPLKTNDAFSKKLITMLSNFREGDSAKNIPTHKLWCTYCLCLAHYKLGDYEESNYWLNLAIDHTPTYPELFLAKAKIFLCMGEIEEALCSFKRSVELDKSDRALASKYAKYLIRMDRNEEAYIVLSKFSRFRFGGVCNYLAETECVWFLVEDGESLLRQKLYGLALKRFHSIYQIYKKWSFLKFDYFTQCAEDGEFQEYVELVEWSDNLWSSTDYLRATLGALTIYLLLFESKFNMYGNKAEEISHMSEVEQIAYAREDNKKIMKLQKIEEDKIKSYIPSESEEPLVIDEDYFGHKLLITDDPLTEAMRFLQPICWHKIKGWGFLKILSSKLYKLKGIIFCYYALTNNIEGLHQKANSLETSVL Q9Y7Y0 YGR8_SCHPO SPBC365.08c; CHAIN 1..224; /note="Uncharacterized derlin-like protein C365.08c"; /id="PRO_0000351084" MASEFSGQIQELLSRIPPVTRYILLGTAATTILTLCQLLSPSMLVLHYPLVVRQKQWYRLFTNYLYAGTGFDFIMNIYFFYQYSTYLENFVFARNAKKYIIYLVKVALLIDAFSLISGLGSALNQSLAAAIAYNWSLFNSFSKIQFLFGFHVQGKYLPYVLLGFSFLTGGLPSLVVLGFGIISAMIVNFFDSIHTPVVHRSNSPKLNSQKVSGTFIGKGKKLGT Q9Y7Y1 SGM1_SCHPO SPBC365.07c; CHAIN 1..547; /note="Protein sgm1"; /id="PRO_0000351447" MENSKWGGFLKKAMSNVETSIDKVLDGNQIEEMSRGNAKSKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTNIRSNVKSKPKKIVTTGGIPENNDYTVGKVDTLKVTKEDEDPTTPTNAIPIPSSMSKRDEALENDKDNYFDDLHPLNISTSPQPSPLSFSEIPQSDTRNALENFLDNLPSPSEERSRISRSASEARKLGINAQSRYASISSAVLSPPSEASRKFSLYESEAISPTSGTPSNLEKGAGNVPDVSLLEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAYVNNDANEDSKKQVEELRLQLQNLEKEHASTLVTLKQKSDKVFELELDIKDMRELYVSQIDILAGRQ Q9Y7Y3 YGR4_SCHPO SPBC365.04c; CHAIN 1..233; /note="Uncharacterized RNA-binding protein C365.04c"; /id="PRO_0000310811" MSSKLSKKKLKSLEYRSKKFDKKSQSLEEHEKKVQQKNEELEKKAADKISRDELPEKQLAQSNDKDKHSVSNPPHKTLKSKRQKGKNNDRKVILFVGNLPKDSSVETLQLHFKRAGQVPSVRIPTDKTSGRQKGYAFVEFINPKTDVISKALKFHHTIYKERKINIELTAGGGGKTEARMNKIKEKNRKWKEEMRQRVASEEQQAGEEKMARKAVADEGLESGIHPDRLRLLQ Q9Y7Z6 YP02_SCHPO SPBC1539.02; CHAIN 1..386; /note="Meiotic chromosome segregation protein C1539.02"; /id="PRO_0000358936" MNQDDFRKLLATPKAETSQLKNFSSNKSQRLVFGRKHKTAKLEAPRALIKRKQLSHSTSSDITRHSNAKNSGKDTQFYEEPSSKQDIELHKLHEKLRNGQITTKEYSEKSKELGGDLNTTHLVRGLDRKLLEKVRSNELALDDSLLSSSEKEVDEEADKLLEKVAEESSHPESVSILEEKKKIPLYPNGQPKYRKILENGKKVKYLLDENGEILKRLVKKEKKLKNDNERLENEHRTEKLNVNANSLGKSFVKHDIPLPPVDLKLDIFEEVGEYDPFHENDKEPAELKAKDAFQLKGHHELDAPYHKKVFDTNQYSDLKPTNFMSQIHRLAKVQERKEEEERKKGKDGQIVDAGFGLVLSKDDTADIHELGESDDDDNVKRRKTKG Q9Y800 MUG97_SCHPO SPBC146.11c; CHAIN 1..345; /note="Meiotically up-regulated gene 97 protein"; /id="PRO_0000116850" MSILNSGSCMMTDTNQNMECKVDFKKGEFDLQPLQINQFGFTKTQLHKPLTRNLSNKEDTHVPKRQKVSEPYFRGETERNVKSHQDRAASIYHEAMNGASGIHKQMSLPEYSPQMGNSWEIQVPMTTRHSISETPTKPFTATTAIAGSAGSLPRNTTIGLPGPSALLKHESGKNENQVRVCLYHKHYSRWYLPFDKDDDNQLVEAYAKYFSSENRPSIFYVLQGISFGPECEYVLRRKHWWNPWAEKVMRREIVERKIDTHPGCRTVAERYEQIEASGSEELLIIPIYKINMWVLSLLLFSAGGSVLIGLWMRLSDPSFAHGMLLNLGIGSIGSFLYLLSNTWCR Q9Y810 SHY1_SCHPO SPBC1215.01; CHAIN 1..290; /note="Cytochrome oxidase assembly protein shy1"; /id="PRO_0000215658" MFWWKSATKFTFSKRGPCVFRYLSTLEGTTVRPKKNKFLVGLLSAVPIVTFALGTWQVKRREWKMGIINTLTERLQQPAILLPKTVTEQDTKKLEWTRVLLRGVFCHDQEMLVGPRTKEGQPGYHVVTPFILDDGRRILVNRGWIARSFAEQSSRDPSSLPKGPVVIEGLLRQHTDKPRFMMKNEPEKNSFYFLNVREFAQLKGTLPILITELQPSLTPLQEADHVKRGLPLGHPLKVEIFNSHTEYIITWYSLSVVSAIMLYVYFKRGSGTSSLNSAYERSKILNNKRL Q9Y811 YONI_SCHPO TRANSIT 1..18; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1105.18c; CHAIN 19..162; /note="Uncharacterized peptide chain release factor-like protein C1105.18c, mitochondrial"; /id="PRO_0000352814" MLCAARKCLNKTFISVRLNAFSCLAELNFRHTWYCSKKETPYQLERLQEEDIEETFICGKGPGGQKINKTSIVAQVKHIPTGIIVRSQDTRSREQNRCIARKRLTEKVDEFKHGNDSLLARKVQRIVKKKKQREKKSKRKYGNKIDDQDSSLNNNEAKQDVI Q9Y814 HTD2_SCHPO SPBC1105.15c; CHAIN 1..300; /note="Hydroxyacyl-thioester dehydratase type 2, mitochondrial"; /id="PRO_0000351436" MSAKVVLKDFLSQAPIDKLKATLSGHLPVSCITMDAKITSLQPGYHFLFFSLASPESNLNSDGYESLYSPKPNNPFSFKRRIWLHGVLRFHRPLHLFQTSECHELIQEESVKSPSITKEVEACLPKSSFLTKPTSEKQTKHVYIRRKIYDSQHQLCIEEDRTLAYLNRQELAIPKTLRSKSIPQHSWVFTPTPIMVFRYSALMFNAHMIHWNATYATKSENYPNLVLPGPLLVTSMLEYFRSVYPQMSKNMKRFEFRLLSPAFVNQPLRICISETGNLWIDRFTTDLDPPSLIARGRVYT Q9Y822 RM16_SCHPO TRANSIT 1..36; /note="Mitochondrion"; /evidence="ECO:0000255" SPBC1105.03c; CHAIN 37..215; /note="Large ribosomal subunit protein uL16m"; /id="PRO_0000310371" MALQQYNKFPFFFSGILGPTRLNGLQMPPIQTMVRWGHQYAPRSIRNQKAQKGRVPIPIGGSLRGTQLEWGEYGMRLKDRSIRFHAKQLETAEQILKRILKPIKAARVYTRFCCNVPVCVKGNETRMGKGKGAFEYWAARIPIGRVLFEIGGDGMRKELAEHALKQAAFHLPGKYEIIVKQTPKRLGTTLIHETPITTETSKMNYQEITSTTTAV Q9Y824 YON1_SCHPO MOD_RES 948; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 950; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPBC1105.01; CHAIN 1..1001; /note="Uncharacterized protein C1105.01"; /id="PRO_0000116874" MPKTDACERMLQSIRSHKNSKLENQRLPAILLHSIDNYIDSKSLQRTASVYFSALLALIKQSNGFDYSSIYILSIVMPATPSDEKLLHIDLLYTQIVPYLQKNNDDAPTIRCALNCTQEFLLSFSNESKELYLKAVDVVMPLLVKFSVDLRPKVRKISIQVLQTLKQKYDGLLPHLYPAIFDELQRSLSEVSNMDNPSFSKGLHTLHLLECLVDINQASGSDLGIICNALSRILTSNIPTSEPIFEMSIKLILKVLSERIDALSDAVIYELCDSLIPYWYRALSVTLLLYDNFVNRNPSRGIKGIQTLLEKILDFCISPLQSSESDVEYDGATSSDILNSLKFLRNKFTMKFVNKKNWATVLSNGIKKVIKTITASSRHANYAKALPRCSVYLQLLLGAIPEDQISELLPAFSVVARAIIKNKLVETPECLDLFKIFIQKLASPTFLECLGFADNFCNIQKSHWLPEVFRDNITGETPETFFDCFLPTIEAGNSQWWELLPLYTKAGCITNNLNENTLKKLASAIYNDRSCHSHVAQAFVDLTKIENVRQLISSNSSNLIGVLGNTLATMKNDDSNAEDLVMAATSIFSVAGDQQLQIITNLCESAPLSEPSLGSTGVIKLFPALLSISPADTWKPFLPHLVKLFDIAIPSNLSQSLSVLNFGPGLAYRLLQATLSNERMISAIVPVISRLYDSMNSVGDGSQALPKYVALERLKTWKLLFKLLPNDEFHLLPSAIAEVVLFSKHHDDDLRAMAFELLVEVGNRMKNGGKINMSLIDGEEPNKTVVEANINEYISMISANLMNDSLNLKVSTIFALTRIFYEFSDYIDDDYVNAVLEEVQSSLQSNNQEIARAAVGFIKMYITSFTKSKVLFHLDTLLPLILRWIKEHNAYVKLKAKQLLDRMLRVFSLKELEAFAENETDKEWLQRIWRVRRSRGDKKVVDNKRDASDSEDLAIKNPMNKKAKVGKVDFRKHEKKLNKASMHRDKFSTGMHTSKRVQKKN U3H041 YP32_SCHPO ACT_SITE 15; /note="Tele-phosphohistidine intermediate"; /evidence="ECO:0000250|UniProtKB:P62707"; ACT_SITE 92; /note="Proton donor/acceptor"; /evidence="ECO:0000250|UniProtKB:P62707" SPBPB21E7.02c; CHAIN 1..213; /note="Probable phosphatase SPBPB21E7.02c"; /id="PRO_0000429004" MDKNLEEKVIWLVRHAQAEHNVGPPGNHRRINQVGIKQWEALHNWLVDNPIPIDVIVCSPLRRTLQTMEISFKSYIHKELPVPIKISPLFEESGNWPCDCAMDLSSTEKLFPDYDFSSCYDDIYPLRRGLYGTTYDENYCRAQKPLKHLASLHEKNIVVVTHSVYLRFLLREQRPEDNMNFMPPEKVFRNCEIRKYNLCHTGFQWELIPLIDN U3H0P2 WTF25_SCHPO SPCC1919.06c; CHAIN 1..249; /note="Meiotic drive suppressor wtf25"; /id="PRO_0000429003" MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPLNTHRENHSYGTTDNSSPLLIILLISFTSIILFNAPAFCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWSKACGKGIKHFLKNWRNMIFAFCKSSLFCLVLLKAENKLSSHLGDQRWGWKCSASAFTFMAVSSILIFIAETVEPGSCSTDLVKRTLAFYGYEIRQHVNEDATILLREMNPESEA A0AAN2H5Y5 A0AAN2H5Y5_SCHPO MGKNEQKDPNVYFFVPNLIGFTRVFLVLISLYFMSWHPNYCTIVYLYSSLLDAFDGWAARKLHQATNFGAILDMVTDRCATSCLLCFLCAAYPKYAIIFQLLVSLDLASHYMHMYSTLHQGASSHKTVTKKHNWMLRLYYGNNKVLFIFCAANEMFFVALYLLSFTPRTPPKLGYLPVPSFIYSTGELPLSYPTLLAVLCGPICLAKQIINVVQLVNAANALVKMDVEQRRAAKKLQ A0AAN2H618 A0AAN2H618_SCHPO MIPIIRPGLVVKRLQSPKIFLTLWKTCYNVKTYSTESIKQKKPQDLNWPTFLKLRKSRRIFETLTSIPTALTGLGLGSAYFLTRTVDPTMTIMGLDLFTLYVIGTIASGGLGWLLGPSIGRKIWTLLHKSQARQIAAREQEFYRHLVKNRVTPQMESYSNPIPDYYGEKIYSLSDYRRWLRDQKAYIQRAFWRTSNR A0AAN2H635 A0AAN2H635_SCHPO MLRINDDDHPNEKIGFISAIKGDFHDLSSDYLKRIAAMAFPIMKEHGFGVTSLDEVAYNAKFWGRNWNKGECIELVLRDASNRWLPFEFVMDVFLHELCHIWQGPHDRRFFSHLSTLRAALIALYAKGYKGPGKYMTWDSFVLANVVGNYNTVVFNGITLERSTMHGVETCGGSLQRKKKIRRKPTPSSTKKRKLTRTGQKLGTDMNIRLELLKSPAKPQAQSMRGREARIAAALLRVDNSNEYKPKDHNSSTTLENYFVVE A0AAN2H641 A0AAN2H641_SCHPO MAGFKVPSWITYKSFWIAVSSSVTTACVILGTLEFRKHRSIRRLQSMIVPEAGKSIQLSSSGVPIEIYDAGEEDEGISKGVPYDENLIREQLARNYAFFGEDGMERLRNSFVIVVGCGGVGSWVINMLARSGVQKIRIVDFDQVSLSSLNRHSIATLQDVGTPKTLAIKKAIKKFAPWIEVDARNALFNPDSADDLLSGNPDFVIDAIDNIQTKVDLLSYCYNHKLPVIASTGSACKSDPTRVNIADISATSEDPLSRATRRRLRLLGIMEGIPVVFSTEKPDPRKASLLPLSEEEFEKGDVDELSALPEFRARILPVIGPMPGIFGLTIATYVLTSIAKYPMDPISTMTRPRLYEEAVKRLHAEARKAGVNLDKTFNASEMSYIIEEVYVGRSALPPHESQKVTVVRWNPQLPFDHTNLVAMTRNEARYHEDNVLAKNVDPSTVYGKDVIEVVHSFLRRLRMWEMLY A0AAN2H642 A0AAN2H642_SCHPO MVLNFNNSEDLVQELCRLRDQRVCIFGEKKSTVRSVTFKAPKSNYDLTSWRIWEQAFRLNVSNSKKCFDTISGHRITLPTNARGLFTGYDYESKRHRIVIRGYDKFFNIDEVPITTWDALSQHTKGPYELTVKENGCIIFIAALPDGQIIVSSKHSLGIVEGQSVSHANVGERWLEKHLQSVGRTKQELAHELLRRDMTAVAELCDDEFEEHILPYTGNSRGLYLHGLNRNCPQFITASSCEVAEFAEQWGFMKVSSFFMDSIHELKAFLENASKDGKWNNRAIEGFVIRCHSDHSSLEQQSSNDFFFKYKFPEPYGMFRQWREVTKMLISGKKPSYTKYKKVTAEYITFCDKKFKEDEDAKRLYMSNKGIISLRDEFLVLSKLDLMHLSVSNDNDCGKEFTLLVPIATIGCGKTTVAKILEKLFGWPVVQNDNLPSGKGGPKRFAKAIIEEFRNGHSVVFADRNNHISNMRSTLQTDILALIDGVRFVALPFKHTPEVPEFVQNRVLQRGDRHQSIKVSEGVDKVKAIMNTFYKQYKPFDPAGNKHDANYDDIIELDPLIGSLENARRIVNYFKKNIPELIPNDPSDDDYAAALNYAVNEYVPTYRKTFGNDSKKIKNKITAEGITGSSTCFKKAPRYFGVLLDRKTVESSLVQVLTIANLQWQEAFSRYTLQDSFHITMIHESQKPVNSRIWEQYLQHMHDKNTTKMGNISFRITHLVWDDRVICFRVTMNENSVWYGKTCNPQLHITLGTSSSDVKAFESNFLLKKLRWQGDEVDSTDGNVRYLTVLPKIIIEGMLEPVY A0AAN2H653 A0AAN2H653_SCHPO MLPPTIRISGLAKTLHIPSRSPLQALKGSFILLNKRKFHYSPFILQEKVQSSNHTIRSDTKLWKRLLKITGKQAHQFKDKPFSHIFAFLFLHELSAILPLPIFFFIFHSLDWTPTGLPGEYLQKGSHVAASIFAKLGYNLPLEKVSKTLLDGAAAYAVVKVC A0AAN2H660 A0AAN2H660_SCHPO MSNITISSHPVVNEQIAILRDRSLKPSQVRSVVDEISRFLAYESTKTLKSPSVSIVPVLRSGMSMMSAFSKVLPDVPIYHIGIFREKSTLQPIEYYNKLPKKSTDTAVILDPVMATGGTANAVITTLQEWGCKNIIFVSVLASEQALTRFSNIPGVEFVIGAVDKSLDAKGYLVPGVGDIGDRLYGATA A0AAN2H662 A0AAN2H662_SCHPO MEETVNKILRAQETRAQLYKELEDALNANQEKKIGLEQMGIIVQLVTEGLNEVSSDIRNYQASLTKELKLLVDSLQEKERSKLQATVKLEQLKVVSTNSPVENTQISELEARLSSLSKEINDILQNMKDEI A0AAN2H671 A0AAN2H671_SCHPO MLKIHRPSIDHPFGVDLWHLFEQLSIKTIGWNPSEFEYIPGKTPMSQWSSVIVSITAYYVIILSGRAIMTNRKPLKQRRLFQLHNFILTIISGALLALLVEEVFRNYMRNGLFYCVCDSRHFTQRLVTLYYLNYLTKYLELMDTVFLFLKKKPLAFLHCYHHGITALLCFTQLLGRTSVQWGVIGLNLYVHVIMYSYYFLAACGRRVWWKQWVTRVQIIQFVLDLILCYFGTYSHIAFRYFPWLPHVGDCSGSLFAAFFGCGVLSSYLFLFIGFYINTYIKRGAKKNQRKAAGKADNTSVAAAAGSEALAATTATNASPFSARSRKL A0AAN2H679 A0AAN2H679_SCHPO MEELLSKQREECKELQSKITNLRKQLKEGNKKQKRALQQKISQMEADLSQKHATERQKLDKGDEETNETQQEDLLNTLLQQMEDTKITTAEKSSVQSSLNTKENTPQQPKKSRNRQKERLERRKAEMKKMSEQAELESEKMADLKNEEKKKFSKILEEAGLVAVDIPADGNCLFASISHQLNYHHNVKLNSQALRNKSADYVLKHCEQFEGFLLDEESGEVLPVSDYCNEIRNNSKWGSDIEIQALANSLEVPVHVYNTEGPVLKFNPSTVKFEKPLCIAYYQHLFGLGAHYNSLLYRDN A0AAN2H683 A0AAN2H683_SCHPO MVHDGVHLISIKTILTDQPCPNTIYYAKYQVQRKDNEDAASLLEDKEAYLRNQDCIVHAKNDLLFVYDFQAIPSIPEESSSFMLLNSGAFSRLALFQKDELALLLDLYINFLQGLKKTVLYWLCKEYNFVPIYGVLLPLKLHPSFDTQLWNIYGYPVVDLQLSVLSKGHIEFYLKPTRQTVYRLSEVDNLVKKLDTVIRLAPTGCLATLTSVHANASAQTVDALKHRYGFSLTTTSKWVGVTLESSALEFSWPLELCFLETSALRMNDDSLSSNLTDLNNLVLPSNVVNNKKELTEFANEEAEASDKRKEGFTEKEETADAVVTLVPSHSSSPVNYSINSAKSTPASIKVNEEILVADHNVSDDILMEEIDDVGITEADFDYFDLPNVEEKVEMIEPNFANTMTTLDNEEINTSISQSNTSPNLNTHENIPKQMEIQSDDRMVTEDLNPYNVEVDIPEISLNISDSKIPTSAYMPSYYSAVIFPSSISSIFQKYNYGGKYWCPSPSLSTEDLFESFSVAESVTSTDEDICSTNFIQQDFTMEYNHDFFSSSKTPTNISEQSNPDSNYDTLSLAHQVLMNESKSANFDFSFLKSLDLQPTITLGKNDLLNAILSQNLWFRSLPFWKSMTTSFMMSQDVLNFSSYMRKPIRDYLEKILLGESSAVFLSKSPENYLSSINNGHHALNDNPPSQVNFSETLVNFSQPPRVLLKYNEKKLSLDSSAPENWISLCLQPYGESKDFEVFLLSSKSPDVSSKAISFFYDVQLAYENCKLGKLNLSETSINERVMGFSTNINETDNYDDNETTQSDTATSYEQLASVCVNELSGKNVLFFYFLEDDSEKLLKACQHFICVKDSIKRLGDNKFEDKSLRICTIPNSIFDSPNSHTTNSNSFFTKVSLDIYNNDPLLMDGSLKRREPAFLLKKPLLSTLNYQLKDINPRSSALGEYALHVTYTTVEEHLLICNWNDSYGEFETERRYFLQDLEIEDALQQILEVTFTFLNSMHMDWIVIVMKIGEMSDAEYLFWDQAIIPENLQGNVSLTVGYCSAEHGPGSTSKVFSRIPYSASSTVIRNNSSHELSLVAFIREMAMPVPNDEFKKISTILARGYLALDEDESYLPLLSIHLLISRNHDPYLMLNLILKHYLSMIYLQFRTYVSFSSLPLHISTVLYQKQLLQFMASDITHPVTS A0AAN2H689 A0AAN2H689_SCHPO MAELLHPNKVEMKPFLKNLDKNLFKKTYNLVAAKVSPKKVGLLNKVCKKDLLDWPRVKHVYQQNNEKLVLLNRDASLDGTRGLSDATVSFIKENNIELVPFQLTLDYDYWRADDILDAILPPGEKEDHPSGFTAVGHIAHMNLREEWLPYKYIIGKVILDKNPSIETVVNKTDTIDTKFRTFQMEVLAGKDDFIVTQSESNCKFRFDFSKVYWNSRLSTEHDRLIQQFQPGDAVCDVMAGVGPFACPAGKKNVIVFANDLNPYSYESLVENIFLNKVANFVKAFNQDGREFIRSSVQKLLGFSKDEKAITVFPPRKRARKLEENKDPVRQDIPIPPVFSHYVMNLPGSAIEFLDAFKGCYYGLEYLFKDRSLPKVHVHCFCRFPDPEEDLINRIYASLGYRFSPEEVDFYYVRKVAPNKDMYCCTFTLPGSIIFAKPVSG A0AAN2H698 A0AAN2H698_SCHPO MYIPNLRNYHDKVFPYGPSSNGYNPVIRLTDRTTQPDPSQHIYQEEKISKCEGLSYRAREWLLLSSNSNARVAIALAEPVLYLPGATSSEIQSEHSAVLRGSLCIQIYKPVKLKKIQLSFKGKSRTEWPEGIPPKLFDTYEENSIMNHCWVFFHSEQKVDENSHGAVWYKVLPHYADTAHYPRSMECFYPGEYVYNFELPISCTYPESIQTDMGRVYYFLETLVDRSSTFSGKSTGRIPIELIRSPCSTSVATSEPILVSKSWEDRLHYEVQVGEKCVVMGQVVPVNFKFTLLGEVKFHKLRLFLMERRYYYCRQRSVRRKEKTRQLLLYERSAPKNQCLLSDWKQVRPDVYELSDQVRIPGCHDMAANIVHFDTTYPNIKITHTVRTVLRFSCENSPELMGSAKYLEIYIDSPVRLLSCRCSDGSTMLPAYCPIIPSSEVNFCSIDNRIIAGMNRDLALDSDIIGNSPPSFDSWTAVPYQAPPPKYDDIFQSGSSHDENHDDN A0AAN2H6A0 A0AAN2H6A0_SCHPO MDQWSDNKDAIGMLSESLKEKVVTNEIAPALKEVKNHKYNFETEILNTGNVWNNDSKNGESGSAFGLDKIFQSSDSGNIAEGLELDLGNIMLETHNLESPAWKHADYDGVAASVNDNNNDWKFFVFDEREIDSMLQLFVRDFRADKPALRLAPSKLFYLASRFAFFYMPKEKELGTVLLNAFLCEVNQVTQQHPNDMVLCVQWLANVSLLLFYLKKDNKLDDLTVDIQNRCSELMNSLYITICQDAMRRMNENLEEGMVKYTGIQGLEDILRSRSWNLLRRRPTNDASTSPRSTPSASPRSITKIIASTLHLLEVFYIHPLIRAQCIEQLFSWLGARLFNIVISNKKYLSRAAAMETRFNISSLEEWSQTNSPKLQKPFDYPDEDLKVDLISKLLSLVQLLQWLQCLYRLSEDEDPRALQETLESLDALNPRQIYTAAKLYRPDITETKVSKTFLKKLDAFHEEKLREKINSSDKGDVSYEFELLKDETVFSPLKLPTKAQLINAYSYIVSGNGFNEDRKIVFQPHVSNILIDKLEENGLSMERAELPTSVFEDELQRREWRPDQEVEELLST A0AAN2H6A5 A0AAN2H6A5_SCHPO MSSSSGLKQQGLAQKKKFQLEFDPSSVSKNGTKTEAKVVGTEFGVLLVRARNTYFATAGKCSHYGAPLAKGVVTSDGHIVCPWHGACFNAATGDVEDTPAIAALRTFPVTEEGDGSLWIEVEDKNDNGASVLQPEGCWRNKATEVYNKGSVETEVTAPHVCIIGGGKGASVAAEYLREKNFKGKITIFTREDEVPYDRPKLSKSLLHDISKLALRSKEYYDDLDISFHFNTDVTKIDLAEKKIYCGSDEKPTESYTKLILATGGEPNKLPIPGLDSKNVYLLRSIADASKLAAVTTEAGDKKNIVIIGSSFIGLELAVVLKDHNVSVIGMESIPFEKVMGKEVGTALKALHEQNGIAFYLENSIKEVKTSSNDSSKAEHIVLKDGQSIPADVVILAAGVKPNLRYLGNAVSLEKDGGVKVDEHCRVLGAEDVYAVGDIAHAPFAGLPSSGEKSHTRIEHWDVAGNLGRVAADHILFGNKAGYTTKSFTPYFWSAQGKQLRYCGNNAAEGFDDVVIQGSLSDYKFACFFTKGEKVVGVCSIMKDPVVSQCARLFIKDAMPSKSQLKENFDVLSIPL A0AAN2H6B6 A0AAN2H6B6_SCHPO MHRVRSARDGIVLKYHFKEDWDETQNSPIDCIASSRLKFWKRLNFNIYLDPEVSNQNLKLLKTLTLHCDFQSPKKNLTMSKFKAMAVELIHEAFLKHIVSILSKECPLSFQPSYYSKMFNAMSNANIIAGSISRILTRESLDKSFEQSHFQLLMYKKCKLIYTRTLRKNEFDGIHKFPDLEDSKQKLQVADDEENKQYSESSLLDDSQLLCSSPPVDSTEEARTCNVEEDQDEILSVALVTTDTILSSDNFVNDMLSAAD A0AAN2H6B7 A0AAN2H6B7_SCHPO MKLVLFLVLLFSALINLTNADKMVVAHFIVGNTYPYTVSNWEEDIQDAIAVGIDGFALNMGSDAWQVERIEDAYDAAASVSSDFKLFISFDMSIISADADFIEGVVRRFADKPNQLYYDGKVFVSTFAGETDTFGYSDVSTGWDSAVKEPLASAGYPIYFVPSWTSLGQGALEESVADGFLSWNAWPTTDADMNDNDDIGYQNLANSLGKLYVAPVSPWFYTHLSYKNWAYKSDWLIIDRWNEMLSVQPDMIEVLTWNDYGESHYIGNIQGALPAGSEGYVDGFDHTAWRYLMSPYISAYKLGLSEPYINFESLFYWYRPTPKSATATADSLSYPSGGDYMEDEIFVLVYLLQSAEVTVTCGSTTQTFSGVPGVNQFTIPMETNASPSFTVARQGGTLASGTGPEIVDSLSIYNFNAYTGVLYF A0AAN2H6C5 A0AAN2H6C5_SCHPO MAENENHVLSIRMSHPYYSEKEISRILSTRDPKENNLRMQAFAWISTLSKTLKFPVRTSGLAMLLYSRFQLFFPVNEIPLLECATACLVVASKIEDTAKKFRDILLAHYLQKHPGSEVDAHSQLIEENKKRILGLERMTLELICFDFRVRHPHNYMVKFAKSLKFSSSTASIAWNVCTDAYKTYTMLKYPAHIVAVASISIACKLQQLPQPIIPRSFFAPPALTEAVIADILDLYMHYQPHTCIGNMYTTEKLLGLCVDFQRAQKNSGRPQKPPQIDPHSSSLADEYRESNKRLQESKESCARFILDCDRKYFNTEFEKRMLEERRNKGTV A0AAN2H6D9 A0AAN2H6D9_SCHPO MDYPSFHEDPTKDESTVAEQRKGQSNEEKPLIDLNDSLDEQRNAYNEHCKNHDQQPSQQVRNMEDEANQYEQTDSSSDQEVMNEKQSLDKENRNDNIPHENNPGQQEINEPIFDFHMFLEQLRSSSAEPVAKYLKSFLSEFTKRRWTVNYQVKLIRDFLKFINEKIEQYEPWASGSQAEIDNAKEGMEKLVLNRLYTSLFSPEIAKSGIPLSSEHSDDVEEDRVLSEKMELFQWITEENLDIKKQKSSSKFFKLAADELRRINDYHAPRDKIICLLNCCKVIFSYLRNVVKEESADMFVPILIFVVLQARPAHLVSNIQYIQRFRSPEKLTGEVMYYLSTLMGAMSFIETLDCSSLTITEEEFNAQIEKSIKKMEERKLSEKSESKTAVNENATYKDPVLSRGLSSSIDVSTGVALVNLPEELENMKYLQIDTPESKEYPRSTRPRGSSHSGSFTTDSGKRSRRNSNKYVGSSDRPPYRVSRAYSSSATHSPIVHEEQPVDDGLQQNDDLREATTASLETAEAERLQAREKAEAITALRAMFPAFDSEVIEVVLNAQQGRLSSSIDSLLEMS A0AAN2H6E0 A0AAN2H6E0_SCHPO MNRNVDKGWQAQIRPNERQSIALQIAQTLRIISPSISEVQLMNMALSFERQAFDGASSKNEYLTTCGKKTAQLRDQIRDTLQATQMKQMPSVYNNAGNVGALPTAGPNRLANNPRVMPRLQNQNVPMQAGMQQFARNMKLTPQQRQFLLQQSQIQQQRQQQQQQSQQPQQTQQPQASSPTAPNTEANQQRSGSVPGRIVPALTQQQLNNLCNQITALLARNGNPPIPMQKLQSMPPARLISIYQNQIQKFRSLQHMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQKQAPQNAFFPNPQGNVGAQSLQSMSPQDQPSTQQQQPQRTAAPPNNPNVNATNNNRINIEMLNIPVPKQLFDQIPNLPPNVKIWRDVLELGQSQRLPPEQLKLIGMLYRKHLQIILQHRQQQLNKIQNARMNSQNAPNTNKLGNPQPDNTGNPQAFSQQAFAQQQQQQQQQLHRTSNPTSASVTSQNGQQPINTKLSANAAKTNYQSYLTNKARNATQPTQPPVSQVDYSNNLPPNLDTSSTFRSSASPPSAFTKAGNEALSVPLSGARNTAASRPTNLAAGNSSASIVQQLLECGGTMGQQKMTSRIRELTERVMHSLMRPVPLDLPHDQKVMIASLIKSAYPMFSRTNQLICLFYCLTGNEEATIQLIQMRHIFKLQLEGLQQGVFTCAPQTLAKIKEKTSRYFAFVKAQLLRLHHEVNNNNMSIQNALAHISSLRTASINQQQQPQPQSQQQQQASQFPQAPSVSSNVRPINGSIPNAQPSVPGQAQPAAKANSVGNTSFPVDSKLAFQSLDVSQPDLQAKQKIASQVMKHGLKPEDLKLPPSKKKKIENLSTVQKPKDSVVNTPDVIMSSVDEIPSSVSPGTIAKEEGMAKAREEAIANPLKYAIDAFVAVDHEEEVSAIKSSQTPSSILKTPQSFFIPPSTPDLSFTDNKNSLSPSNILSLDGKFSFNDDSELWADLGNEINSEIGFLKEPDTMNLALDADKDKTKMQNKLTQINFDESCFLDPAIDDKDPWNEMLHEKKVLLKQLQVGNEDEDNIAFPTSTNIWQVVI A0AAN2H6E2 A0AAN2H6E2_SCHPO MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKIHKRFQLQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKEMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI A0AAN2H6F6 A0AAN2H6F6_SCHPO MAGDSVKSAIIGIAGGPFSGKTQLCEQLLERLKSSAPSTFSKLIHLTSFLYPNSVDRYALSSYDIEAFKKVLSLISQGAEKICLPDGSCIKLPVDQNRIILIEGYYLLLPELLPYYTSKIFVYEDADTRLERCVLQRVKAEKGDLTKVLNDFVTLSKPAYDSSIHPTRENADIILPQKENIDTALLFVSQHLQDILAEMNKTSSSNTVKYDTQHETYMKLAHEMARTSLSNREVPVSCVFVYKGEVIGRGFNETNCSLSGIRHAELIAIEKILEHYPASVFKETTLYVTVEPCLMCAAALKQLHIKAVYFGCGNDRFGGCGSVFSINKDQSIDPSYPVYPGLFYSEAVMLMREFYVQENVKAPVPQSKKQRVLKREVKSLDLSRFK A0AAN2H6F9 A0AAN2H6F9_SCHPO MASSKENNLKNSVYRDAFLDISSKSRKTAEKPSSKKMEKDTEELELENAVFGNINNFSSFLDKENETFDVMMNEAPELSEDNDAQEDELEKLEDAELFMFDTGSADGAKDSVPLDIIAGDNTVKEDEEASNEIPSIWEDSDDERLMISLQDHSRLRKLRQYEDEDMVNGLQYARRLRTQFERVYPVPEWAKKQDVTEEEDEFNALSEKSVIPKSLKSLFKSSVSYINQSSKLLAPGTINIKRLKDANFQAPSHSGIRCMSIHPYFPLLLTCGFDRTLRIYQLDGKVNPLVTSLHLRSSALQTALFHPDGKRVIAAGRRKYMYIWDLESAQVQKVSRMYGQENFQPSMERFHVDPTGKYIALEGRSGHINLLHALTGQFATSFKIEGVLSDVLFTSDGSEMLVLSYGAEVWHFNVEQRSVVRRWQVQDGVSTTHFCLDPSNKYLAIGSKSGIVNIYDLQTSNADAAPKPVTTLDNITFSINSMSFSQDSQVLAIASRGKKDTLRLVHVPSFSVFRNWPTSATPLGRVTCLAFGKGGELCVGNEAGRVGLWKLAHYD A0AAN2H6G1 A0AAN2H6G1_SCHPO MTSELQQELQILRSFNYTIEKLTDGLSASKEKIKSFETSINNSNRLIQLWSSVLSQTEHTQNLILNSDWKGLSFDNEELERLQHQKMLQIQAEEQRKIELQQEQERLEQERRQKEEAIALQKQQQQRLLRSKDPKVRPARRAASSYVPSRPSHVPRSSSMNVRSRVSMATTSNPNSLRTPSSSFASHRQSAIPKSATSSAPTIPTSNLPSVASSIPNNGLNSSNRKSIISKTSSRLRPPSRVSNVPSVPQHPSTRSRTSTRETTQPPFTTNPSNRSKRTTLR A0AAN2H6H5 A0AAN2H6H5_SCHPO MNRQSIYYFLLKLIFDGQKNKALRYFSVSIPCNALCQYFAKEKPKKSLTLHKLNTS A0AAN2H6H8 A0AAN2H6H8_SCHPO MNRDHSSNNTNRTVLNLPKEILIIIFSFLDPRSLLSAQCTCKYWKKLLSDDLSWRTAFFHHFAGDQSQIFSPLGNGTWRQEYLLRSTITRAYEKGKGQTVQYDCRVGQLTNLYYDFSSGRLYSGNWLTGTISVSDPTTGKVERSLLHASTDGSFTHGLSTMTLGKQIFGFGFMDGRVGVILMSRQAETPRKFRYCLDSHADSVTCIDALTGDLPPTGEIGMVTGSDDGSVHCWDVKTGVSLQSFQFRSSQILSLCFRPKYKMLLVDTFNYELNSYQLYLIPGYARSRKNEQPILLSSRKCVLTDEEEPPCLMTADCCAGVAFLSRGAPKNCICRVSFKEFLEKNDNVGVQTSSIPLNGKPTSISLDTNDRVLSKSTPGRGARLLAVGDENGLVYVVNTRTEDPNKAILRTITAYSNFPITDIYLNEVAMVVGSASGYCGVYDTVTGNFLKKIASARNAARREPINCILLDSNPLSLKGVITMSKHVKSWSYTIPKPFVNKRSKVLPLRPSVTHDNLSKSSDYSKNEVEREIMLGLDQIAQERREKMEARQKFEQHFGEGLVGLSEEEIIAYVTMLSQEEEAKRMVQLSMDVDKIEEDFKENDEQATSSLNALSSNHEPPQEQANVAELNEQEQIELAMRLSLMEM A0AAN2H6I0 A0AAN2H6I0_SCHPO MEQANVFRLEEKRYKCRADTIPDMSEVLDPNDPQSFGFEALVEIKPRVFSFQKAPGLLILKNYVSSELQMQLLKSIMFTQIQDPENKTNLSPFYQLPLGNDSIWRRYYNGDGESIIDGLGETKPLTVDRLVHKKLRWVTLGEQYDWTTKEYPDPSKSPGFPKDLGDFVEKVVKESTDFLHWKAEAAIVNFYSPGDTLSAHIDESEEDLTLPLISLSMGLDCIYLIGTESRSEKPSALRLHSGDVVIMTGTSRKAFHAVPKIIPNSTPNYLLTGNKAWDGWISRKRVNFNVRQVRPSR A0AAN2H6J4 A0AAN2H6J4_SCHPO MDLLCRKFSRLTNRVVQQRFFIRTMSNTHITDWSSKDGEFRRQVSSFRERISPEHKYFQPEKDRYHLYVSYACPWAHRTLIVRKLKGLENVIPVHVVGWLMGPNGWNFDKENDSTGDPLYNSPYLRNLYFRADPNYNMRFTVPVLWDSKYNTIVNNESAEIIRMFNDAFNEVIEDEEKRVVDLYPSSLRTKIDELNDYFYDTVNNGVYKTGFATTAEAYEKNVRVVFQGLDRLEQVLKESKGPFLLGDHLTETDVRLYTTIVRFDPVYVQHFKCNIGTIRHNYPHINQWLKRLYWKHPAFHETTDFKHIKCHYTQSHTQINPLGITPLGPIPNVEYF A0AAN2H6K0 A0AAN2H6K0_SCHPO MRLNAEFLSQVPSFISPLKETELDLRYIPIIENLGVLRDVHDAIDFTDNDIRYLGNFPRMKRLQTLLCGNNRITAIAPDIGKVLPNLKTLSLAQNHLQEIADLDPLASCPQLTNLSCIDNPVAQKQYYRLYLIWRIPSLHILDFERVRRNERLRAEEVFGQIQNPTEIASSIMGVKSRVFDLAALVQSHPEANSPITTGYTLTPEEREKIKEAIKNASSIAEINRLEAMLLEGKIPK A0AAN2H6K9 A0AAN2H6K9_SCHPO MSNADYIAKKYLRKDQGKKKKKKEKDFVEIQDEDVAGWDDDNSFSLVNRELTSLHDAPTIVANESLKDRDIDAIYQNIEKTTNKPAQLWKAVGNDEVVESEQQDSHDAESIPQFGLLTGKQVTFKAEERRKREEKSSNLDEEELRKSRETVYRDATGRRIDLVLARKEAKRKLKEKEEEARRQKEQQQGVVQVRQQKEYLKELERQKTVPLARYEDDPEYNKELKERSRWNDPAASFLTNKPVSSKATYQGYAPPNRFNIRPGHRWDGIIRGNGFENKWFQRQNERKAQEHEAHMWAIEDM A0AAN2H6L4 A0AAN2H6L4_SCHPO MIGAHISAAGGVFNALINMKNINANSCAFFVKSQRKWTSPDLSEDVAQKFLETASEMKFDASKQVLVHGSYLINMANADEQKREQAFNCFVDDLKRCERLGVGLYNFHPGSTASCTKEEGINNLAECINRAHEETKSVIIVTENMAGQGNCLGGTFDDFAALKSKIKNLDRWRVCLDTCHTFAAGYDIRTEESYKKVIDEFDEKVGAKYVSGWHLNDSKAPLGSNRDLHENIGLGFLGLEPFRLIMNDSRWDGIPLVLETPAKSPEQWKKEVELLRFMVGKSSDDVELMKESARLSNLGAASRKEHLNKFEKKEAKKDRKKKSKDGDQTTLLLRKKQKLGNAEVKSLDE A0AAN2H6M4 A0AAN2H6M4_SCHPO MRFETECDQKLRNWKRLAIEREVSEEQSGEVQFPRWIDEWANTKLGGIFERIFSKMDSMQNDMNSRFDAMQTEMSVMKNGIASIKGEMAEMKGEMTVMKNDIASIKGEMAEMKGEMAVMKNDIASIKGEMAEMKGEMTVMKNDIASIKGEMAEMKGEMTIMKSDIDSVKGETTTLKGEVTAMKDSISQLDRKIDLLDQRTEERFNNMAQTMQKIDDRSCKSMMLTRKYENMVRSDMHYSAVPVPFLNGDEPRDYELPPLASFEDIDNLTKEQCIQYLHGYGVNKFSPLETVKLKERLQEAIGLWSKGHESHKYHTF A0AAN2H746 A0AAN2H746_SCHPO MLFNCFGILALLQILPALAYPPCREQMSDPYEFGESDLMRPGMHDTPLSLMQKREALAISLSKRDSVGSYAPYNVTCPSDYMLRPASDGISSGEQSFIDKRIPKINTQMRSFISNTGLDVDVNSVINDSDGPRLGLAFSGGGLRAMVHGGGVLNAFDSRNGNGSSLAGILQSAMYIAGLSGGSWLVGSVAVNNFANITYLRDNVWNLEHSVFAPHGDNVVENLAYYDDLDDEIDQKKDAGFDTSLTDLWGRALSRKLVDATQGGPNITFSSIRNQTWFQNADYPYPIIISDSRLEEEKAIPANTSIFEFTPYEFGTWDNGIKAFLPMEYVGTHLKNGVPPDHKCIRNYDNAGFVMGTSATLFNTFLLEWSQEVTSNSTLYDIIHKVFEKLSEDQNDIAPYPNPYQNFTTTNTTVKNPFERFDTIDLVDGGEDDENIPIWPLLHPQRFVDVIFAVDATYDDSNGWPDGSSIVTTYERIITYNANKSVDVRGFPYIPDEDTIISLGLNTHPTFFGCDGRNTTAGNHTVDNNTPPLLVYFPNYPWVYYSNISTFTMSMNDTLSSGILENAALSATQNNSDSFAVCLACAMIQRSLERKNMSTPSQCSSCFEQYCWNGTTVNNPSAVSNYAPTVLSASTTSGTSSVRAKPIVFYLFASLLTVSLLL A0AAN2H765 A0AAN2H765_SCHPO MSTSSKLSTNIKDLSLFDLEEFPARSYIGGKWVTAASGKTFDVENPGLNETLAPVTDMSVEETRKAIKVAHEAFLSYRNSDIKERYAILRRWYDLIMENADDLATMMTLENGKALGDAKGEVVYAAKFIDWFAGEALRISGDSSMSSNPQNRIITIKQPVGVVGIITPWNFPAAMITRKVGAALAAGCTVVIRPAAETPFTALALAKLAERAGVPAGVLNMVTANSPSEHGIELTTNPLIRKVSFTGSTNVGKILAKQSSSTLKKLSLELGGNAPFIVFEDADLEKAADALMACKFRGSGQTCVCANRIYVHSSVYDAFVDLVTERVSKFKLGYGLDAGVTHGPLISEKAISKVKQHVEDAVQKGGVVVTGGKVASNLGPMYFEPTVIINAKQGMLISEEETFGPVGALFKFDTEDEVVAWANDSPVGLAGYLFSKDISRVFRVGEALQVGMVGCNTGLVSDVLSPFGGVKESGFGREGSKYGISEYLDIKSLTISTL A0AAN2H7F6 A0AAN2H7F6_SCHPO MTTGKPQSFEKMRTPFPGRSKAKGPQSDIIPSAPPNTPVTEH A0AAN2H7H4 A0AAN2H7H4_SCHPO MMPIPGSQALRKVSATEVLDLLVEHELAFPSEFFEELSNLSFSEKQTALSNPKTQVYTKGVFAAGQVAQRCIAGCLRKGNPNYWKSQQVVNAWARLFPRLRFLSRQQISGTQEIEVKFLPDNLGDNKDTCHLCGLSADDSVATLAPAEMLIRSQGAFWHEGCLKYYKHHFSK A0AAN2H7J7 A0AAN2H7J7_SCHPO MDERREELSAKSTVQNVKISEAPILDGKVNNEDSHMEIDQPEGSMEEDDHRQVKEKNTSENSVEQKRGRRMFGALLGTLGKFQQESEREQKSARKVKRAELEEKLAKRREQELQELEKQEKIEAEILESRLQEQRKVALDELELDRNDLKKVLDNKKSYYLRTKTQPSLFYRPYYLLPSQRTQLEQMKSEAP A0AAN2H7L6 A0AAN2H7L6_SCHPO MQFLERHFSVLFPVLFFFSFYPISFAPNFDWSTYVSLHYPLTLPNHLALMSSYTHQSHCGTSVFHQAQTLVHLHT A0AAN2H7N4 A0AAN2H7N4_SCHPO MDRYNPPRRNGNSKKNEVVITGGRTQRIDFEKDVNKTTILPPAGASVGRRGRGAGWYCEACNETYKDSLSWLDHLNSTQHLRKTRTVIIEKRATLEEVKERMEYWRRQLLEPEKGSEEYSLKERVERYHQELEAKKLRRKQKKVNKEKNSPRLVGENTELAAIMGISSFGSTNL A0AAN2H7N7 A0AAN2H7N7_SCHPO MIFGKTHFLSYNILRYSTKRWMNRHSYSHHAKCTVAQLLKQNLLTFENQRIQPEEELKENLTKVVNYFQAPIDVAVGYGSGVFRQAGYSQKENPMIDFIFQVEDPVKWHKINLQQNPSHYSFVKNFGPGFVSTLQESFGTGVYYNTHVEVEGNIIKYGVTSKKDVYEDLKNWNTMYLAGRFQKPVVILKGEDEFYKENSYNLSSALHVGLLMLADRFTEFDLYKTIVSLSYLGDIRMSFFAENPRKVENIVSKQIAFFRKLYLPLLYAEPGVHFIESSEVLKSMDPSDNSRYLSFHQNITKDSISRLLNGLPLNLVKILGLKPDTSSFEKCAELMLTNQISTRSLLISKSIKKLTSFSILTQSIKGIFTAGVIRSLVYVYAKLKKGLLSKWGR A0AAN2H7Q5 A0AAN2H7Q5_SCHPO MGDYLLSWSWILDAFETSDENLSQNKFEELLDARIAAFQQIESPVTGTLNSNKTTEGEEAKLSIYDSSHSISKSQLESVKKISDITGYNEAQVAYVLLVHQYELNTQYFSQLDNDSVLAQEFQRRYYAEIISCWKVLAFLLQACTDADSKWHKMATRLIVSIFQTAQRSGENAQSTTPSIFCVRIIDYLSKMTSQAAPASLTFNGEEAISQWYFFHFNLQLQLLRVIFLSTYSLVVCNSEMAISWFNCMKKTRYLHDQEFMHLDIDTGFSMCKEITNVAIIISINFISLEKQVLSFKDNPSFFMLSGNTIISLHDMITQLSNDSIGAAVSLTWGIALHLLSNSPDNIPLIQNSSVVSSKILQNPQNSFQALIIAALKYDPFTLIHRIISSLEDDPYIDGYSKIMATLFSSAVSYVKFSDSTMLCATTLFKTPQVYQLFENNDSVTRLLNFARARFPFEYSQFVLLLIPTFACLTSKQLVSSELLHMTTFTQSLPSGFKAYEIIPEPNVTGNALIELQESLHLDSYGFFFPNAERSLPKGTRGRIVSVDTYPPVVMWDLNYSLWEAVGISLNYIVRNGLINSHKSFVLTVLSSSVPLFQTDVSGACELVHLASEGLDGELDFINVICDLLDYFLSLSVIEDADYQICVSSLRLLREFTRFAATDVWAYVTRSLVCVGSEKGISLEDVIFDYESINGVYDFTLAFFDLYEILLDNCISTSVVPDDFSIRLKTDFVKRAMRFLCEVFANYLDWKYARIIQQYQIGHRFASLITKLLNVTFGIEYFNPKTTVNKKTLPLRELSHYIVQRFLVQQDSNRYLHPLLSVMDLINLLYTDIFSTISSPRAKAAKMWLISSFCAMKTLICLRGFLNLKPSELERELFSRSPDLFNCLPRLLCCIAPILQLLSALILAPWPSETPSLLAYMINSTDIVGRVCIQILTNPIQSTNIEGSVWKFLSSIMKGQQQGLAVLLFSGKKFPLDRMKSLNHNVDVQLTSKSLISLAEKRLDSFSINDILSQVPVFEFIFLSRNFWTASLGNLQQEANFWNRIVDAIKLPLTVKLDGLSSVAQADLYILAAHATRITAIQLHMSKLNKSNSSKKIIIDPLKDSMKDLVQHAFTITAYDSNIHNALTRAFKHENGDLHISDLRNTGLFPLRYGDNYFYNIKLAKNMLLNTEDTSFKISMMMSANENLSLLDAQAALLRSWSIFICAFVEFVKEDATLSILELKIMKWVLKSLAEDTIDVNVVQELSAERAALVFRISQQTLAIPISNEVKEHLQSILLLTWKAITTTKFSIYEDSNGEMAYYRPLLHVLYNTLNRLLSEEKENLSLSVGFVSGLLQLCHRKLSQLFEKAVINPTIEVYGDIVLLNSLHKCIVNSHLIRGLQSLYISYINDSFSVDNCLRLFSWSHSLLVDGQPYFADAALSFLLICSSSPAGAEQIVMNGFFYSIMESPLSTALSTGGLGLDGSSIQYKIWIRGILPLLFNIVKFLGNRIMNDMREFVLLAFPQIQYALLNWCQPPSSISLASIDESFMIVLLFDLLQQFNPALLQEIRLAELKIEMLEGIDYLISHPNFLSSLAIPASLYEQEYAIDVIGIPKELESDQLTKETKTSQFAKLIRIQLDKLRALLEH A0AAN2H7Q7 A0AAN2H7Q7_SCHPO MAMTNLLTILKRTDHLEESFLKNPNDNLKELENIIIEQEEALRFSSLSYADCYSLGVIVRDLYAKAAYTAPIVIDITLNGHQVFHLAYDGSSPDNDAFIKRKYATVQRFRMSSMRMGLMMAQQGTTMPAKYDVPAEEYGAFGGGFPIKLTSGIQIGVFCISGLRQIQDHCLIARSIAEFLTTKQ A0AAN2H7R6 A0AAN2H7R6_SCHPO MSLKSFFNFNKKTKLHDIEEDVISEIGSAGSALRTDAHMLKANDVYYKSETDSHTVLRFMKPSENEKIHPVRHSKYEDKSKLPFETIPDPVLKYVKRARDAELQPQLAKVSQKLFADISTATAAEKLQFTVPRRARFEINDPRNPTFSMMALQDIISVLEYRRNKNPTSTAHICIDKKGKEAVSYSWDKILNRAKQFASVAQNHVGLKPGTRVILYYRKSEASEYIISIFGCLLLGIVVIPLSPSSSSESLKLVVNEEKVRVAFTTEATYRIFIKDTEVNNAKSLAWWKSNDFTNYKFEQIKQYRMRANDTVLIDYTFSSSTYNDIKAVYTTKTFLSQMRNLTSSMITNPARQAGWKLHNFEDSKDVLITNFHPSMPLGLIMGVFNSVFAGYCTIFCDEEVLKTPGLLAYLITKYRCTYSLFDYAGLKQTVYNYQEDPKSTLSFKKNYTPNLSSLKLCMVECEVVDPEFNIIVSDRWLQPLGTNNSKEVITPILCLRKFGGIPISFKDWMISYTNRQKHERQMADTCYQEILVLKSSIEKEKVEIVPFLDIRKYSPNEVLCMSPFWYPIPEASVAVVNEDSKNICKVGEVGEIWVYSDCLPKLKAASVINNPQGEQLTDYENNQENKFEKNNSFMDSGLKGFLHNEKIFVLGNKDEQIRQYRKTMVADKLMEEKYVHYSHYLIKKIMKYVPEIFDGVAFEIEIDKAVYSVLVLESPIIKRSLIRNNRLKGRDLFSELVKITESSFQVTQDIFKLDVLSILIAPYKSLPRSRYMGIQAINTNKCKLAFLSGNLPVSYVRFFMDSALPKSKINLNNSKGIWSKDASKHHREIISLNVKQKMDPYKHQNKVSKARENLLNHFTILDFLKTKSAKTPTSPAILTFNAIEKTKVELTWAHFELKVASHVEYMQLSVKAKARSHILLLYYDPLEFLISIHSCFHLGVIPIPFQIREISQLIGEIEEFTKIAKAFNVEAILVDHKVLISLKSRDISNHFQQTCIDLNMKAPKIFETTGIPISKRAKKALNLITPGELNNKGKVALISINKLEDGSIIPTQFSHSSLLAFCHEQKEFVIGNEEKPIIGGIEFSSGMGLLHTALLGVYAGVPTLLIKQENLCNNGSLLFEAIEQNSLSKVMIPLNICQKSFSTAQGCNSIVINSTLSSIIVPCYDRPISSRVNSIIEDIARIGLAPNKVKLAYSHPINPFVCWNADSSMEKMKDYFDANQLRSGLVNVREDVLRNRQPLLYGSGTSTLYNEICIVHPEEKYICQEGEIGEIWINGKHGSYCENNELNSGCELLVQETLDKKSYSRTGQLGFIHHLKKKDQNMEKVPVLYTLDFIWNTLELNGLNHSVKDIEETIELVHPNICTDGCILFQASGSVVILLEVHSQQKFASLIPIIVATALAAHEIILDCVAFVPKGTFLRRPTGEKRRADILKQWTGGDLKHMTSYLIRQDFLLNEDFVGTELIGTTDSYDYSDENLIINSSQLNLL A0AAN2H7S4 A0AAN2H7S4_SCHPO MPIPIIAHIAQFKYEHLITHWAQYTKAAIAVSTIAAFKFWTSGRTTTWERKMNGMVVMVTGGSSGIGQVVVEKLASLGAQVVILLRTEPDQFTVDYIMDLRKRTKNQLIYTEVCDLSSMLSVRKFATKWIDCTPIRRLDMIVLCSGVLLPPFMDRQTTEEGVELQWATNFLGPYQLLRILRPVIYGQPGHREVRIVAATCSSYILGNIDFNDLDLSNHPYPRKSPWKVVGNAKLALMTYLYDFQKKAEAHERPDKMPCNLHTIMANPGVVRTPGFRRVVSFGKVWGLFLYLLLWPFWWLLLKGTIHGAQSFFHAICSPEFASITQPVLVNECSIVEYSRKEITDPEFAEKLIKAADAQIDEVEKQYKKKKIKKSKK A0AAN2H7S7 A0AAN2H7S7_SCHPO MIQDGDFVFQKAKKGTTIPKARKKTLTKDLQVQVAKELEQESSSTFRFAYVFPRKAQNHYYSPSRTHTSSIKKKRPKLCSNINLTPWSLIDSTSNKSIREQSREMGIISIQKWAEQARMRSLCFPKN A0AAN2H7T3 A0AAN2H7T3_SCHPO MRCLVRSADIQFKGICGLTRGFASFNKPPQTITEKIVQKFAQNIPENKYVRSGDYVTIKPKHCMSHDNSWPVALKFMGIGAKKVFDNRQIVCTLDHDVQNKSEANLRKYKNIESFAKGQGIDFYPAGRGIGHQIMVEQGYAMPGSMAVASDSHSNTYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPIARVNLVGQLPKGLSGKDIIVSLCGAFNHDEVLNHAIEFYGEGLNSLSIESRLTIANMTTEWGALSGLFPTDEKLLAWYEDRLKFLGPNHPRVNRETLDAIKASPILADEGAFYAKHLILDLSTLSPAVSGPNSVKVYNSAATLEKKDILIKKAYLVSCTNGRLSDIHDAAETVKGKKVADGVEFYVGAASSEVEAAAQKNGDWQTLIDSGARTLPAGCGPCIGLGTGLLKDGEVGISATNRNFKGRMGSREALAYLASPAVVAASAIAGKIVAPEGFKNAVSLVSAVDITDKVNKQTASKSSTEAVDSETAIIDGFPSIVAGEIVFCDADNLNTDGIYPGRYTYRDDITKEEMAKVCMENYDSEFGKKTKKDDILVSGFNFGTGSSREQAATAILSRGIPLVVGGSFSDIFKRNSINNALLAIQLPDLVQKLRTAFANESKELTRRTGWHLKWDVRKSTVTVTTSDNKEMSWKIGELGNSVQSLFVRGGLEGWVKHEISKSN A0AAN2H7U2 A0AAN2H7U2_SCHPO MEVSETDEHLTRLNQARDIVKTDQSLFPEIVRNILSVANYSDIRYKKWMANFLWFGFSSKNVKFEQKLDLAVTCLDTIVSLYAVDNEEVKKDVISCSCTIYPLVFLHCCTSPNDSSTWDTLTKLKNEIINDFDKGNKPLLISCIKFISCVILTQVPGIRDPRLVTKSDVSLSKVPTHHPFINSNILRIEANDLIEKIFSILFSDSLNVLYITSVLNILPVLVKRRKELAPKIIGSLLEFHLPNPKDEIELSNESKLAIRCIEKNLKLILLHLAKSTGASSSSVEKIHAYLSGQIYHTKVDESLKKRQYEGNISAASKRVKSSAVQSLVERMQPQLSSHDGLQNNPLISIFASQTAINPLANFDVTSIPVEVATEIVLTSLLKIDKNYFHQQINMLRERVRSLSEPESLGLDQQVDEDEDEDYEPPEVDVQTINASVEREAARLEGSAPSNVVTDAFELPTPDSLSPMAILEYFHGALSRLFDYAPQFERSIVSSSNLQNLTLENVDNTVWDKRHWAILLPRLCTRGLLNYQPVTSGEESGDASFTLSSFVRGQLFTYVASNWRSSTNLILNWLSEEWYNDRLMLENPDCHEYEDVKWEGPQYEKWALKVIDSILPYLEAKDKVFMIFMSELPELTDAIVDKIKFVCLDPDKTKLGFMTFQYLIMFRLPVREKCLDILETMWKENVDVKASAAKLLNRWRPSFLESVKSEETKEPSATDNTS A0AAN2H7U4 A0AAN2H7U4_SCHPO MLGLLLLLLIPALFTLIWIYKYIEPHSLISIPGIFVFLGLYVPFVVTLLIPIDVTWDVSLSIWRFLYWLTFVLSWIILPFVQGYMESKFSTPRSRLSDSFYKNLRYYLLLTFLTCVVIAYLRFALRTMSFSNFKELVISLTYFWGLLFVIFLLGNGFVYVPVSMWKKAFITKRAALLERQAVGVYSKLQARLESYSLPSSSISLNNGRNQSSSDFFTSSLTDHAFNPHSSPNGMSNVIALQTTWNQMVKEYNRIMLIKTAKASGSYRLYLPDSYIPIHPVVAYAFYVWILPAFRILFSIFMASMSVIIVVSEVFLHTQYSLVGIILQKFTNSSATSIFVSFLFVYYMRYCTYKSLMRTQFAPHYYYALVPFRATNTASLIYFASQLCRLTLPLCYNFVSLQPYPTQFHQFYGESIDLLPLGNLISKRYPTFILLPIIFSMISLKYRLRQFIYSITLRKSSSASSSDDFDDSSLNSENDDDLFNETSAAYLAEGRALLLGTNNAHV A0AAN2H7V0 A0AAN2H7V0_SCHPO MDRISAQKDIFKKVVNKENSSIFVSLGVFAVSVAILKSRLGNFLVPQL A0AAN2H7V9 A0AAN2H7V9_SCHPO MYTYDSSGETLKIAIAWKIILKKPKGKNIKDYIEALRKGIEDQEHCEKYASTLLEPRPKTKKDVVLKNSNVTECVALKAKPFSKKIEDMDIFLLTNVHENLQEKRQTSGSLAHLDIEYTFNGLFRFLKCTADIKLKQTKVYEGADFLRIKTLFEEIFMFLKRDCKSPLVLTRLVELGDYVLDLIIITQSIMQNNANNGTGVISRAKFLEFYVFLEQLIFNKLSFASVEQLEKLLDQIVKRMKICFTYCKNDNPSIRLLYSECFFSYAEIYFPCLHSFDAQLSSAASKCVQILRDIITNEELQTDKQELSKSAYSAPSILLIGLKDMLFPEDIS A0AAN2H7W5 A0AAN2H7W5_SCHPO MDIDPYSVLGVEKDASDELIRRAYRKKALQHHPDRIHDEEKKVEARIEFDKVAIAYGVLSDKKRRKHYDKTGQLRETDADIDFDWKEWLDELYQGVVSGETLNEFKASYQYSEEEKCDVLKAYEKGKGSMDVILEEVMCCEISDEDRFRQVINNAIKDGKISKYKRFAPNEKKRKRRAKAAEREAQEAEELSMELGLDENLKKRRKAGASDEEALSALIRSRQKSRMYNLISNLESKYSKSSTKPKKSKKSRSKE A0AAN2H7X8 A0AAN2H7X8_SCHPO MENGEILLTSWLNRSVHIEIFDERKFIGKFLCTDREGAAILSNTTEYNKGFSRALGLVVIPGKHIKSFSVRA A0AAN2H7Y5 A0AAN2H7Y5_SCHPO MKIDKAIFTNQFGVPLPSDNPYVALHDFVYDLEVAIPEDEFEAFKEQLANPRNSCIEVRESISKKDSIFQTYEMLQELKDGQSSLREDLNHLSHGQNVLKKNMVYLNGTFECISNVIRANNQILMLEFGKSNRINELKVSAQRSEEILNYKSAKQMNSNLSTIYRVLPLIKIFLMNIRNCLN A0AAN2H7Z2 A0AAN2H7Z2_SCHPO MNADLQHCLLADQNYLLNNSNKNKGSIIEENTRKPFQSARNLQTSLKTHPESAITRYGLGYAGFGNGWTALKPKILFPSQKRRVKGRFTFPFSRRSNLAQSKLPVDLVPIRLEIDADRYKLRDSFTWNLYDKCISLDQFAEQICIDYDIPLHNVHIVQNISKSIQAQINDYEPRKAQSNLSFVSDVSSSTSETVYAHEPSDSLAKASKQQIPTVQNDLRILIKLDITIGRLNLIDQFEWNLFAPESSAEEFATVMCLDLGLSGEFCTAVAHSIREQCQMYIKYLSLIGYLFDGSEIEDEEVRSYILPPLKNTLRFSDMESSSFAPMIYELNDAEMERQDRGYDREARRMRRRQGRAKHGIMLPDLRDIPKIHRSLFPSSSVPSDDDFMHALSLSTNSDGETLNEINTNNPEREHLIVRLKVDSQKLKIIVEQSQTLTLNNFQQRKLTPLPNSMSFDSLNEFESERNTPSTYGQNISPLPQFSSPSLSSDAFLTNSNSSESALVHMQKLNLPDFTPSWVKRCVIETFAKFPNDRFNVIVKPALNPAERMTVRICCHDCINEYFTAGPGFTFGNFHIHLLSSSHQQKKEVRMNTVLDRNT A0AAN2H7Z9 A0AAN2H7Z9_SCHPO MDVSQCEHWHNRLCDVGLDSKQKANTAIEIRDALDDVLVTEKTNFETFIPLLEDTLSLLEKERPVFSSLAATHRLRIALLELLKKSGSYKGFEAFVNRTFAVLLRIVVNDNEEMAVLALKLVVLLFKDHSSLAKGHVQEFLSIVVENYKSMTTVVSEAFPPRSAPNTPSSHPMSAASSASPAEIGMEHAGPKMIPKASSSFKVTAEFPIIVFLLFQTYKDLIPKMLPLLAPLVLQFISLRPPPQAEARRLAESQKEVFIGVVPSLRRNHLYNDLISAQIKSFSFLAYLLRSFGAALKQFESSIPICTLQLFMDCPSELYQTRRELLVATRHVLSTDYLRGFLPYVDQLLDTKILVGSGITSQHSLRPMAFSMLADMLHYVRMELSPQQIYKVILLYFSILMDDFYTSAIQAMATKLILNLVERIVALEDFSTSRSLLFAILLCLLRKLTSLNFEFMKLRDSLQENADLKQIKIEENKHDLPMFENPTGAAQPSGLDKLKDCIFLFKNTLLGIKPVLFGLKQRNIPLANGSIFTAQEWSEKLHLSSTNEVLLFRRLLVESLKGFSYYQTDEKTGVFKSSKNLAYSQLDSSLTTNPSKLLEEKELLEMLATLFLHLDPSVFVEILESEFPNIFECLVDNLALLHIFQFWMSNEVTSVNCTGIVLSFCCDNLAKIGSGQSTRVSVLLRLFKLAFMTVNVFPEKNAEVLRPHISYIISTSLELTTDAVEPLNYVYLMKALFRNISGGKFDSLYKEILPLLQVMLECFNRLIFTVTSTSQKELYAELCLTLPIRLSVLLPHMNFLMKPLIVALKGPPEIASQGLRIFELCLDNLTQEFLDPLLDSIMPDLLICLWNHSRLNQSNNQLHQSAVRILGKMGGRNRQIYLGTFGFDFLQDENIFPSIQFSFQGSSQNFSLEHSKFLMSSCAVLNNQNSDLEEKKQAFQMVKNSYLLLFASAKPDEDFWESIDTMCRAVVDRMDKNLQQVSNGRLCPDKDESYYLQRSIVSNIFKSLVGSMSCVEFVAEARETINRSLEWLIVLDLVNYADSLQIKDQNIFDNLQSIKMLDLTTCINGIFESLCSENENTRSNALSCIDHYLNAHKMLLNTTLDISKLPSFQNLVTVFCQSCHKELWYQKNAGFLGLKAILSYDSHHKLWIQDRLHDILKALFFILKDTPTDYGVLKLTEVRSFIVDITTQFCILQDVLAPKERANNIINAFSPFFLELLHPNDHVRNTVQQAIENISNNSKLSVVDLLLPIKDRLLSPIFGKPLRALPFTIQIGHIDAITYCLHRSPSFLDLTDELYRLFRETIALADAEDEALVTMLKTSQSKDSSSLRKLRATCLHLLFASLVAHKFDQPQHAQTRTKIIAIFFKDLYSPHKEIYSVAIDALRHVLSQNQKLPKELLQSGLRPILMNLSDHNKLSVNGLEGLSRLLRLLTNYFKVEIGRKLLQHLNVLSDSKVLETASLSLLKTNPRIEIIVSLVNVFRDLPPLSAQFLGDLLSSVVNIEAVLRKYSNSPLRKPLYSFMDLHANDTWMYILNNARNGDLITRFVGALNDPMSEKLRETAGNYWGKLLELISQPVSVENLAPMYAVDIIATVFPYISANVDAGVISAKFIVLSKSLYGMLSSYNEYLFLPIRRCISSITKMLLSSLKKIEKKLEFSLEVFRFKADDDNDFLPEYIDSLCGCLITSTSAAEKKSIFLVCCSIVGDKSVRPFFKAFLLDKVINPLVFKSCGENNFIDKDVVHSVYTHVWRVSIRDFAEVSGATDSFYMGIMCLTTALCKYHSALLNDYRKSVIMSAWNYIKLEDPMVKQAAYATIACFISAYDTPAKIVTPVYVSILKTYQPEVRAFIEFSLASLLSVLTARLSSPSDSTFPLWAKLPRLVISEDVQGISQPLTVYQFICKAPDLFFSCCSHFIVPMVNALPKLVSFSSASTEPRKLALDIVQTFINWQRKQNESENSETTLFSNSHIEAILTFLIKFLSLFPEPVEENPLSKKGLSLFNDLFSFPRWKDCQLNSNFFEKILVDMDFNDNNYRTVANTLFVFGVILKNRGMEYIQREYSHIIALIDKSLRCGKLPVTHSLEQIILLLLQSHPTQAEEEEDTNEADDFKQLLLSVIHDNLAAATNIESAICYLQIVKSSNPEALDGLLLPLNKCFQKVARDHIVACMQSAIQASGKVTLPSASDTVSKLLISFIEIIRVRMASLGDQRRWFLSVVVQLLEKSSSFELCEHILNVTKEWVIVKRDSFLTVKEKTALLLKMRTFEGRFDNKLYIEACDLLSTIYRDPIFAHTELTARLKQAFLLATASKDTKIRMDFMDIFDSSMSRNVYSRLTFILDATSWDTIPSIYWIKQANYILLGAINAKQPVRLTDNSLRFAPVPMTKPILSSLPEVFSKHNGSAIPLGRFTFFKQLDLFLKRNKELTVQKIIFPLAHIQMLSDADANKLWQYIFPLAWKILSSDNRSDLSKSLIYLLTRDYHIKQVNNRPNVISTLVSSFVKCAAKLELPPHLVKYLGKLYGVYHESVSLLEIQLSDKYDMYQNAKVQESRADAVAELYASLNEDDMFYGHWRRNCKYLQTQVALSYEQLGMWGRAQQLYEQAQTKARSEAIPFSESEYNLWEDQWVMCAQKLQQWDVLTELAKHEGSSELLLECAWRISDWSNNRESLEVAIKSLSDVPTPRKLTFQCFMTLQKSVSQPLAIKEFQQVLSEAIQLALIKWHQLPEKVNQSHYSLLHLFQQFVELQEAATIYSHLNAINFQNLPTNVQLIKSALQVWQERLPNVWDDINLWRDLISWRQIVFSMINRVYLPLVPTIQANSSADSSNPPNTSFLFRGYHETAWLINRFAHVARKHKLPSVCLNQLTKIYTLPNIEIQEAFYKLREQVLCYLQNPRDLKTGLEVVTNTNLMYFNSRQKSEFVTLKGKFLEKLNRGEEANQMYAAAVQIDLGLPKAWAEWGRYNDLLFNKSPDNLSAACNAISCYLQAAGTYQSSKARKMLARVLWLLSLNDSAGTIVKAFESYKGDIPVWHWLTFIPQLLNSLSKGDTKCAPVVLKKIAKSYPQALFFTLRTAREDIAQVKRTEMAAWKSNTTDENKRNEDILSIQSNFLSTNQSTNAPATNKEDGLSKKVWEYIDEIMSILKTAYPLLALTMETLVDQIQAKFKCKNDGDAFRLVVALLNDAVQHSIRLGIVTDEMKLPSSTESNLSLFADNILPDYCKQLFKEDFIVNSNGLKSYIFKLRKWRSYFERLLSKVPKKQYLEQYSSFLCEFHHQKFDEIEVPGQYLLHKDNNNSFSCIERFLPEVELIVGHGVCYRRLSIRSNGGTIHPFVIQYPSARNSRREERFMQLTRYLNDALALNCETRRRCLKFYIPAVIPLSSHIRLLEDQPSSITLQKIYEIYSERNNFSRDDPKELFTNELSKHMMELNSQISQESTDAEKLANRKQLFSRRIGMFENIQKLYSPSTILKDYFSSIFTNYSDLWLFRKNFSYQYACFSFITYILSINNRIPAKLVFSRDSGGVWTTEALPSMVSSTPVYHNGEIVPFRFTPNIKEFIGKTCTEGLLGPSIMAIARALSKPDFDLDMYLGIFIRDDLFWWLAQQTKGVPADFSMLNKVNSNTDLIMRRVASLSQVAYGNLPVNQTAIDYLAQASSSKVLAQMDVLWAPWL A0AAN2H803 A0AAN2H803_SCHPO MSSQNTSNSRHPASSASALPNRTNTARRSTSPRTSTGSSSTNTNTKTVDHAGTTFISSTSKRGRSTKAGSVHSVPMKRTKRVRRTPAQRIEHENKENIQTEKVYRIKPVQRVLSPSDLTNELTILDLFHVPRPNETFDITDRVNNTSR A0AAN2H813 A0AAN2H813_SCHPO MADSEEYKTVIGISFGNQNSSIAFNRDGKTDVLANEEGNRQIPSILSYHGDQEYHGVQARGQLVRNADNSVTNFRDLLGKSHDELTLHHCHYSANPVNVEGQIGFKITVQEDEESDPKEKILTAHEASVRHLRRLTESAEDFLGTKVNGCVMSVPVYFTDAQRKALESAANEAGLPVLQLIHDPAAVILALMYSEEVLIDKTVVVANFGATRSEVSVVSVKGGLMTILASVHDENLGGEQLTDVLVNFFAKEFEKKNGIDPRKNARSLAKLRAQCEITKRVLSNGTTASAAVDSLADGIDFHSSINRLRYDLAASATLNRMADLVTEAVEKANMEPFDISEVILAGGASNTPKLTSLMESIFPEQTIIRSSSSVTPLQLDPSELTAIGSGVQASLIGHFDAADIAASTDAQVVDVPHLTAPIGINEGENFVTIFDIETALPARKTVEVIAPKEGAAFIPIYEAERSVKVTKVEPEPIDEEEAFSDDEEEEPEEIKERIAIPKTLIATITLPDVSPNAKIELVLQIDAEGKLTASARPKDGKGTNVRGSTA A0AAN2H818 A0AAN2H818_SCHPO MAEEEHVDFEGGEAGASLTFPMQCSALRKNGHVVIKGRPCKIVDMSTSKTGKHGHAKVHIVALDIFNGRKYEDMSPSTHNMDVPVVKRDEYQLVNIDDGYLNLMTTDGTTKDDVRLPEGELGNEIEEGFEEGKDLIITVVSAMGEEIALACRDAPSA A0AAN2H820 A0AAN2H820_SCHPO MVGTINESMQNMKIGAKETAQSAKQGIKNAGQSSSKTARDVMGNPVPGSYTAGNTANDGDSSYASSKNLPGNADIGATSSERTAYAAPQRAAVDTSNVSPPSTQTGGYASKDTTSTYEGAQPLSSQSSRSSNYTNVKITATQNNVDALTGAPIRIVTTTNARIQPDEKTLQDLLEQRQVALREAREAEEELQRARQYNDRSTSEALELEARAKKAAQDAELASERAREAQSSIERSASLREKQAREEAERAATALREAELKHRLAQANADVDVANSKLDIALKNEAAWKAERESSLAHQKAVIDSARAELERARHEAAVADATYKKEHYEYNALVAELEERNDNTLRTASIREAEARNLEVHMEDTLKDARMRSRNATEQVEVVKREINSEIDVYRSSVEKTKAELASYQKGLPSQKEACDRELDDATRALQAAFQDRFNAAKLRVNQFDVDSRQQLAMLTKKVRDAEDAEEKYRISCHQREEEITRCATQAYDAVKAAEKRNETIAEAARAKENEAKDLYSKAESITQDLNAKRSHPPQPANLDYSSAIQRAQERLTLEESKLTDLRTAEPSQYVNDVEVARRALRDAQAEQSKVESEYNSVKGSKLYTTEPVHPHAVTTNEPTDVSTKSKSAAYHYPATTETVSSKAARSATTPAYVGGATKTPSTTKAVESTPSTLPTSASTNAAATTTTKKPKAAKSTAVRDDVSSASSDSDKGTTGLGKSESKSSRKERRSSTSSGHGLMNNVRHALGMSNK A0AAN2H832 A0AAN2H832_SCHPO MVFAIRIRQFHTTLVSAEKNGLQKLIPPRLKTIWNQMLVETKGAGNGPERFEMIRQKYKALTADEIQKYKNKLQEQFDAEKKRFMETLRSFTPTEIDSENRRRSKEAHSTGSRYYRLRHPDVPKKPSSAFILFYKELRNNPKLRQELGIPEAISTLVEETQNASKAWKELAEDKKKPFIDKSKALKEQYDKFMKEAGFR A0AAN2H837 A0AAN2H837_SCHPO MPDRLKRRIEEIDHQDEIIDREASTASPVSGAGKIDQNGEIKDLLERNLTWSQQTSRKYPSFFTATKDIQTPQVLWIGCSDSRVPETTILNLLPGEVFVHRNIANVVPRSDINALAVMEYSVTVLKVKHIIVCGHYGCGGVAAALGPNLNNLLDHWLRHIRDVIEDNREELDAIEDPQLRRLKLAELNTRAQAISVTRVGFVREAMEKRGLQVHGWIYDLSNGQIKKLDITDAIKKAKYGTYDS A0AAN2H839 A0AAN2H839_SCHPO MLKESSLFQLFRKHKGYLNVTDLVLPLWCEVQHEYYLLRRIKKKTPKMERGIKLHQILEYETSPPSERRVLDRTSKEEPWALRLLRQLEGIMLLQKNGITREFPIWGYYKESSIFGIIDEISLNNPSKSNFNSDIRNYFNFKMYDLSFVDNKTRFSSRKPGASQILSSKVQLMYYVHLFLNYFPSLGEKQQSIFRDISPTYSNRLHSQSHWWNMFLSQLSLDGTKDLGPKFLEQSILSIPDIPEDVFAGHNSLNGLYALVFASAKKLHLRLTDDNLTIAYRNDKTGEVVYKDKFSFSNKLLEASYTKAYQFWHNLREPEGVPAEEVYKCRSCEFQKECWWLKKKQYYPLSSP A0AAN2H850 A0AAN2H850_SCHPO MDSGLKSDSHEVERSNFQLNKPEKSLKRYALLSFYVIILLAIPVWWKTTHYERSSLPFEDMENAPSTVQTHLRFSPTFRILDDKGNNLTKEVQKVLEAEPQIYSYNLKVLEDDPVDYRIVLRESTDLQWFWDENNFIIDTPSKGPSELAILIVNCLWEAFSPQVMEVWSKFTRFSSTVEPSRAETKRTVQFSPQYRVLLSLLVGEGNHEPINWDIENAIQKYFNPLIEQLASLAKLNIETQIQYFVEDAEAYIKDDKFCTKHADLPNLVNNFEKYLSFSPHIREPTIHFVLYVPSPQIQPLWLENEDSNIIPTNSMLLPQWGSITTINFNVTEKKLLHDVDLKDYFRVISRDLLLLLGINDVPVSSLSATLADRLLRQRIAESCIEASDTLQNLAKLVHSMQSMAVPKEIQMYVKDTLLSLDMAYKALSQNNLNEALSYSNNAFSKSQEALFHPSMVTTIYFPDESKYGIYAPLFAPILIPLLISFIKEVKDMLRERKLHRVANVPKPN A0AAN2H855 A0AAN2H855_SCHPO MKTQEIKNVTLEDVDFLKNLGVWVEIYHHLEKGLLQQCFNLVKKNMEALYRQSSFGWDDSEKLKEMEMEKLEYICIFEKTSKKLVGFLSFEDTVEAGLTCLYIYEIQLDEHIRGRNVGKWLLKNASILAYRRNLKYIFLTVFSANLNALNFYHHFDFVPHESSPQEKKFRSGKVIHPDYYILYTKSRKDW A0AAN2H856 A0AAN2H856_SCHPO MSGASASLTEGSAIIPFSNPNEVFYNPVQQFNRDLSVTAIRAWSETRSKKIVAKSHHRHQLLDQNSELSQENLTKCDTTHDFEKNCSEKTDSTSADNIAGFTILEALSATGLRSIRYAKELPNVKRILANDLLENAVKTIEKNVNYNNVSDIVIPNKGDANAVMHMNKFHYDVIDLDPYGSAAPFLDAAVQSVSKDGLLCITCTDSAVLAGNAYPEKCFSNYGGSSLRSNFCHEQAVRHLLYAIAASAAKYGRAIKPLLSLSIDFYFRVFVQIKAKPVLVKNLQSQSLLIYHCSGCGSFAEQPLGKTSPGRLPGTTKFSNASGPPVSANCEHCGYVHHVGGPLWGGPLHDAEFLKKMRAIAEDLDPEVYGTKRRILGMLALADEELPDVPFYFVLSQICSVLRSQSPPQNIFVSALLNAGYRVSGSHAKSNAIKTNAPWSFVWDVLRSWIKDHPVKLENISKTSAGAAILEKTPTAEVDFTFRPDSEFASKKEGYTRYQMNPTENWGPKSKPGKRTIAEVDSKS A0AAN2H875 A0AAN2H875_SCHPO MTSTPKNLEKQPINFDNLPLYLQGTNYGENVLRSDPRWLKWEKYLREFDMTREGNVTNTPKAIPSSWNPNDKSDSLELMNNNMGVYFFGPEAGTEHDAASVKADHAIPSNTSIYYYEIQILSRGKEGKMGVGFCRKSMQTNRLPGCTAESWGYHGNSGEKFNCSKTGEAYGPEFTTGDIIGCGVNFINRTIFYTKNGAYLGVAFKKVSDVLYPVIGLKSHGEHVEVNFGQNPFLYDIDYAIQMEKNKLFEQATKSPKQEELKQRQEFLNELISSFLLNNGFVETAKKFCPENTEVSDASIRKEISSMLANGQLDLAMTKIDCQYPVAIQECPDLIMSLRFLRFLQLVKVTHDQRLTKSKGTKQISQEEDLRILQPLMNYAQELSNDYEHTKSSNLQAMIKLSMGLLAYFDPFSSPLSFFMSSDFHKYMAEQINCLLLELTGHSPDSELRRFLQHTVCLNDLLCRNGCRSNTLFNVQSDFLSPY A0AAN2H877 A0AAN2H877_SCHPO MLNLTKVGLRRFWSQSPRRNAPKKELSSLLESTITPKAFSKRTEEPNPIMQGTDTIPMPFYLHAKCLKNNTHITLCSPERKIIFRASGGTCGFRKGKRRGYDAAYTICSKVLEQIQVKRLGIENLHVIFHGFSQAREAVQNCLLGQEGAVIRDKIVKVMDRTPIKFGGPRGRRERRI A0AAN2H888 A0AAN2H888_SCHPO MDFYRILVICIHVYTRLVFAPLKKDLKLLRLISLCIPIIRPFSFLIYPPPKSFSPLNSILPSILPIIPFAISSSLLFSYTFHVFYRFLFQPLLSVPYANSKQTNCLLVASFVYLPYRSPLPVVIEIMVQRYL A0AAN2H896 A0AAN2H896_SCHPO MSAGSQTKLNFSVRKTRSSSKRSNAAIIEPPKNPEDSQIIPAVKRLKENLDTESLEQNEVLPPVKNESVLFLEKVFNAVDICVKFHLSINTKPTFVLLENKVSGLTKISLKITHLAQILTVWPESFAITPCFTIHQGKRVATYELSYPRNANLPEAFSRSIEFKRRLEKWLLEHCSETEIPAQQLQALPSLSKNTVNESSLVRKLNLEKSTSRELRIPTQTLEPKFTTNTAKYANELVSCSMLDSSSTLSKSVNSKINLKSHQSSSSVQNSSRKLTSSQLTLRQSSLFDRVRKKQKAMEAKKAEEFKNNLVVHTLAKEKVSFVRIIDLIFVQLSTWPTKRSFSMSEIVTSMQMSISSSLSPDQCAKAIELLSKALPAWCTINLLGNIQVVTFSRIVNGKPYLRSQLIEELQTKASITILSNS A0AAN2H8A8 A0AAN2H8A8_SCHPO MSYANYRYMKARAKRWRPENLDGIQTSDEHLINLFAKILSKHVPEIGKFDPNKDVESYISKLDQHFTEYPSLFPNEHTKRQYTLNHLEELEQQFAERMFSENGSLTWQELLRQTGKVQGSNKGDRLTKTFEGFRNQLDKVQFIRKLMSKANVDDFHTRLFILWMLPYSLRKLKERNYWKSEISEIYDFLEDKRTASYGKTHKRFQLQNKNLGKESLSKKNNTTNSRNLRKTNVSRIEYSSNKFLNHTRKRYEMVLQAELPDFKCSIPCLIDTGAQANIITEETVRAHKLPTRPWSKSVIYGGVYPNKINRKTIKLNISLNGISIKTEFLVVKKFSHPAAISFTTLYDNNIEISSSKHTLSQMNKVSNIVKEPELPDIYKEFKDITAETNTEKLPKPIKGLEFEVELTQENYRLPIRNYPLPPGKMQAMNDEINQGLKSGIIRESKAINACPVMFVPKKEGTLRMVVDYKPLNKYVKPNIYPLPLIEQLLAKIQGSTIFTKLDLKSAYHLIRVRKGDEHKLAFRCPRGVFEYLVMPYGISTAPAHFQYFINTILGEAKESHVVCYMDDILIHSKSESEHVKHVKDVLQKLKNANLIINQAKCEFHQSQVKFIGYHISEKGFTPCQENIDKVLQWKQPKNRKELRQFLGSVNYLRKFIPKTSQLTHPLNNLLKKDVRWKWTPTQTQAIENIKQCLVSPPVLRHFDFSKKILLETDASDVAVGAVLSQKHDDDKYYPVGYYSAKMSKAQLNYSVSDKMLAIIKSLKHWRHYLESTIEPFKILTDHRNLIGRITNESEPENKRLARWQLFLQDFNFEINYRPGSANHIADALSRIVDETEPIPKDSEDNSINFVNQISITDDFKNQVVTEYTNDTKLLNLLNNEDKRVEENIQLKDGLLINSKDQILLPNDTQLTRTIIKKYHEEGKLIHPGIELLTNIILRRFTWKGIRKQIQEYVQNCHTCQINKSRNHKPYGPLQPIPPSERPWESLSMDFITALPESSGYNALFVVVDRFSKMAILVPCTKSITAEQTARMFDQRVIAYFGNPKEIIADNDHIFTSQTWKDFAHKYNFVMKFSLPYRPQTDGQTERTNQTVEKLLRCVCSTHPNTWVDHISLVQQSYNNAIHSATQMTPFEIVHRYSPALSPLELPSFSDKTDENSQETIQVFQTVKEHLNTNNIKMKKYFDMKIQEIEEFQPGDLVMVKRTKTGFLHKSNKLAPSFAGPFYVLQKSGPNNYELDLPDSIKHMFSSTFHVSHLEKYRHNSELNYATIDESDIGTILHILEHKNREQVLYLNVKYISNLNPSTIMSGWTTLATALQADKAIVNDYIKNNNLNI A0AAN2H8B3 A0AAN2H8B3_SCHPO MLGFHNWRRTYWLYLKKLRPINDTYDAPFAIGCKNVAYEASQYPRMNATFMVLARNSDLDGVLSSMNSIERRFNRHFKYPYVFLNDEPFTTEFKKAVKDATDSSIQFGVLDDELWNFPKDVDKDMIDESIAEQVGVVYANFPSYHKMCRFFSRNFYKHPLMQQYEWYWRLEPEVTFSCDISYDPFYYMDKHNKVYGYVIAIKELAKTVPNLFRYTVAHQKISNLPTTDLWSFFLDKRYETRIKKLKEEQKDQGYYVLPEPPLNRIDGQIYNLCHFWSNFEIARLDFYNSKEYNEYVDALENAGGFWTERWGDAPVHSLAVGLLLNRSQVHYFRDLGYQHSTIQHCGQEYGCNCDCPFNIPDYETKPGSCINEWASVMGGFLDE A0AAN2H8D3 A0AAN2H8D3_SCHPO MLQRLEQLQMQTSNILKELHSTSIFTDSTTSQLHNGGENSVMDTEESSAIDKLSASLQQVNISSPSVPTSQSRVTQGQSLGNTQISNPTSKTNNVRAKARNIRNPSQRLRPSTSLARLSNNAPRIPKEASLHENSISSKESPSVTTSKHVATITKPSTSSIARMSSNARIAAIPRAKSSMAVRSPSRLGNGPNVRSPKVGFNAKSDDSPVVKSPGSNDKPSASPRISVRSLGNSSVVRPPTRTSTTRPLSRVNVTNASGSISKNSTSPSKVKVNASTKIVRPVSAAQTVRPGSRIFRENSASNTQRPNVSATSNSTVRVASSLAVRPVSRNAQARTPSRLEQREVNVKNSSAKIVRPGTSLGVRSPSRIQSTLSSRTTTGNVRTKAANIVRPSSSINRRPPSSINQRPPSNLRILAPSRSRATIHERPSSSILHRHAHSLTSSSFSTKTLATTKEIQNSPTLVESSTVVHHDPSYLQNQTSEINDTNHSSHSSPLDLNRMI A0AAN2H8G1 A0AAN2H8G1_SCHPO MIGLKGILKVIDNSGATLAECIRVVRAGKFASLGDEVVVVVKKARSGSSVTAANKVKRGDIHHAIIVRTKSPVRRPDGRYVRFDDNACVLVNKECEPLGTRILSVVANELRTKHHTKIASLAPRTI A0AAN2H8I1 A0AAN2H8I1_SCHPO MANFYIFPLLLEARSDHFYEGNEYIKYLSHRIHGLRKSLHITQRGGKPKSSVDKRYAEILLFNADRAFQQFVFLRSSQRRHALRRLKRADQFGKELVSFTNAFDCNDHIFYLEAIAFAKYIEGTLNYEKRDWEGSLSAFSISRLSFLVLQNKIDTLAEHEKSVLGELQNQIDSNLRYVAQRTGLQNQTKSLDILMLSSIPKDEEVIQHVNSVDSEILQMTGDEQDSLQTITVIEWRDQRVKIEHPDVVLALYAIHDVKNSPGTIDSKRDRLLAAWARAEEITKSVLDNTGLEDEQKFQTLSICYTYLAYNVVLLRIQRDLAVENDSELVASQAQLRSRQSLYDSIIKNIEIAKELPGIARDTGMTAQLEAQISLAKSKRCQAIADAYQAQDKLASLAMCVRAASYLQQVNDILRNFEEKPHLIAFDIIPELKKDEKELKKKILLLQSLASMGNINQPPKNLSLVETLDSYQTLAELEPSWNLTDADIRAIPAKPLFFDLAITYLGQQTSFDKKKAQPEKPVTSVSKEPKQKNKGFFSSLLGR A0AAN2H8L1 A0AAN2H8L1_SCHPO MGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFGVWCAICLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILGGIGNAMMGLANAFRGGNDNNNNIPLGEMDVEGEV A0AAN2H8V2 A0AAN2H8V2_SCHPO MAQETRAISSISEAANKRARKLSKRRAKKPVEEGSSGHVLLLEIENLIEKPVLANVPFERFQEIEVKISYLSSSGDGIGLVCNDQYAVVVPFTLPGDIVKAKLHFLADTYALADFLEVISPSEDRDDTLIKCPYFAKCGGCQYQMLSYDKQLLQKKRVVEKAFQYYSKLDSSLLPAIKDTVGSPLQYNYRTKITPHFDVPKGGTKGPLIIGFQEKGRRRVMDIEECPIATKTINEEYPKIIEDVQSRANTFKRGATILMRDSATEDGKHCVITDHKMIVREQFGDLSFTFPAGAFFQNNNSILEKFTSYVREQLLNPFGRKEHQRPKYFVDAYCGSGLFSVACSKGFLSVIGVEISADSVRYAEENAKRNNVSNATFIVGQAEKIFSSIETPPNETAMVIDPPRKGCDQSFLNQLLEYSPYRIVYISCNVHTQARDVGFLLSQEKGRSYKIDEIRGFDLFPQSHHVESILTLTKVVS A0AAN2H8X1 A0AAN2H8X1_SCHPO MRVGVQGCCHGILDNLYILAEKRKVDLLIIGGDFQALRNVSDYHGISMPPKFKRLGDFFNYYNGRNKAPILTIFVGGNHEASNYLDELPYGGWVAPNIYYMGRSSVINVGGLRIAGISGIYSAMDYKKGRYEGLPYNYKMLKSIYHTREFDVLSLKSLQKPIDIFLSHDWPRGIEQHGDVAKLLRHKPFFRNEVERNDLGSPALEELLVELKPRYWMAAHLHTKFTAVVHHNSQEDDGKLSCSSKDVTSSGFSMKGLNEPSQERLPVEKEQNDKSDEEGSNNEQEEKQDKKQSTNRDLCRKESCKKEPSLSSSDQVTKFLALDKCLPRRSYFEVVEIEPVEIPDSGAPYMQYDSEWLSVLRAMHPFQSHTIEQDPPLPSLEVVKTLKRKEEIWVDENLVKKDKLGIPRNFCQTAPPHSRDITENMQPSSYINPQTVAFEILIGLKERTVDSPPPVKNPNEIVL A0AAN2H904 A0AAN2H904_SCHPO MKSSSLENGTLANAGVYEDDLDSDEELVSEEEFENFNNEDSEDDEDSNNESKTAKSQLAEIPFDTLLNAQRDLLKEQQKTKDNDRKNMKHTEKVDQKIFGERKKHAPQELSSKKPVSRFREVISEPKKFTRDPRFDSLSGNLSKDKVKKNYGFLNEYRVSEIQQLRDELKICKDQERAESIRQTLKSLLSKMERHLEEERAERVMHEFRAQEKERVKEGKKPFYLKRNEQKKLIQMDKYKSMEGTKALDKYIEKKRRRRAQKEKKHLPRARPSANSQNK A0AAN2H921 A0AAN2H921_SCHPO MAISSLSSPSGARVSSVTVKNKVLKTPCFFLPTSRGTVPHLTPDNVEEFDIPALYVGLEDCLDRLEASPILTNEGTIKKWIAAPSVQPTLLAPRRTSPLPSVSAGQSHINIVTASGAKKLTNDLYIKAVLKLCPELVIPLNDTPTSPPGVKRKPKIVERSVNWTTELLLALKATDAFNTTKVFFPVPDLDTQYLTPIFQFFQENQLANNIAGLAFSNNVNPLPADLVGLPRLSIQKFESPLEILKCIQRGIDIIVPDMITQATDAGVALTFSFPPPSKDVLNSKIELGLDMWDERFATDMEPLQSGCVCKTCRRYKRAYVRHLLQARELVAWILLQLYVYIKEHGKES A0AAN2H954 A0AAN2H954_SCHPO MFRSLAKLRCFASSLGLSSHKNIKSVPLIRNIHYIPDNPSYFTQNARFNEIYLHLENILKFAPKIIAAEEDVPKVKWKTLEQYQKEFSDPKTTKVGYRKITRLLNELNEIVPEYRTEAVQKALEKFIRPDIVVKTTLKSQMLDENGMSITKGKRKSSKATVKMLPGTGKFYVNGSPFDVYFQRMVHRKHAVYPLAACNRLTNYNVWATVHGGGPTGQSGAVHAAISKSLILQEPSLKQVIKDTHCVLNDKRKVERKKTGQPKARKKYTWVKR A0AAN2H976 A0AAN2H976_SCHPO MKKRSETLGSDQSSSEIIEHVLEELNLKNIERRVKKYDQIESEYKTNIENEKKAFIKDVSQVQQKIKEFEIQKANQIKQLNEEKLSIEARKQQLEIEIRNQLLQYAEKLRIVVKTPMNQPTNTEV A0AAN2H995 A0AAN2H995_SCHPO MVVIANKGALWAYYCKRLLNSVTYMMYPLIRKRTMKKLLLIVGLLLACSTVMRRIPLFHESFHLPSLDPRASTTTSQKFQEYRSDFLEKLETAEPPEDVIMFTAYGLGVHTHNLFMLACDMAKTSDSQIRFLLLTDGTILPEALYDYNRETVSTCPLSFLSYSTGVERLSKELILKDLLSLQFQQALLAISPSVIVTSEHSPLVMFQAINPYLNNNYYTHDTVDTNALEENSWITKLDMQSLQHFRTPRINVVLIVEDGTYKYLLNLMRDLGRDFKNSEEYPHLFIHLFMSENIPNLSSIRANWPQHRLFINLHFNQKDLNLIEVWTPPNDYTYALVVDLQPDSPPQLSSNLITWLKYKILLIYYHKSSSTYKNNIAAIVPSFDFSNEEAVILSQTINSNIVLFAPVVFQKFQEYMAVRLLNPNFELPESNGIEFAHEDSVLGHSKPSLTEFHAILGLYSLVISYNHFEGSLSNELRLDNLIAYFLKNPSVINFEEISEKNLYFTYDSKRLSFQGAKNESKKLYNSVTSCPYYGSLSSFPIRSIFCEPLM A0AAN2H9B4 A0AAN2H9B4_SCHPO MVENVSSTPKKGVLEDPSTLTPEVVTPRTPGHRIIKAKGAYTKDRSAKRRRGRIEIERHLLGEFDDNVGSNSLLDVPLYSLEAEPLSPSVMLEDESMEGINQSPQGISVEKLGKEDNRSRSSTPASPSLESHEFSESREAGLSQSNGFEARSHGTGFDEYFDKFSQRKTSSNTLSQLPVLDNQVYLDTVKEICTETEQHTQTLVHFQSRNFHQWYFELVNNFNLLFYGFGSKEHFLSSFVEKKLPCFPIFVVKGYFPQLQLKNVLSSFLEFLEVTPAASVSDMLIQSLSIINSPSFSLGKIVFLVHNIDGESLIDERFQSALAAIASSKNVYFIASVDHVNFALLWDTSLESSFNFVMHDATTFARYYNETTYENSLGIGRANVSNKEKAIKHVLYSLPANSRGIFKFLLIHQLERMMDTQDFDARQGEKVGIEYRSFFQKCSAEFLCSNEPNFRSQLTEFFDHNIIESKRDVSNSEILWVPYPKNLLEILLEDMMEDV A0AAN2H9C9 A0AAN2H9C9_SCHPO MYQKEAFYRGRSSTRQFNNTRSPSGRSASRSSNFSHRSSSRDSFSSNRSYSSSLSRSPEEPLRTILVENLTRNVTKEHIAEIFGIYGLIDHIFMPIYKKSELNKGYCYIEYVYHDQAANAVDKMNNAELDGEELFVSIKRFPFESLHKNHKHYENSYRPSRSQNNSHYNDKSFHRSRYSRARSRSPGSNISEYSDQSPPYHSYRHRP A0AAN2H9E6 A0AAN2H9E6_SCHPO MYPKMKNDLILRAAKGEEVERPPVWIMRQAGRYLPEYHKLRAKQSFFEMCQTPETACELTLQPVTRFKGLLDAAIIFSDILVIPQALGMQVVMLEQKGPHFPKPLVVPEDIDLLEKTPNISAKLGYVMDAISLTREKLDGQVPLMGFSGAPWTIMAYMIEGGGSKTFAKAKSWLFRYPEASHKLLKIITDATVSYLIQQVYAGAQLLQIFDSWAGELSPEDFTEYAYPYLVRICQEVKQHLKKKKRDEVPMIVFAKGAWYAIDQLCDSGYDVIGLDWTVSPKEAVRIRGNRRVTFQGNLDPNILYGTREIIEARTKEMIQDFGGGKQGYIINLGHGITPGVNPDDVRFFLEKCHQYGSA A0AAN2H9H5 A0AAN2H9H5_SCHPO MSSLKSFIKAVRASKTTAEEHTTILKESAQIRKNIRQGSNDMRMRRKNVAKLLYLFLLGEPTHFGQIECLKLLSSSRFMDKRLGYLAAMLLLDENQEVLTLLTNSLQNDLKSRDKFIVGLALSAFGNVAGPELARDLSNDIAELCSNHHNYISKKAVLCALRVIQKEPDLESLYIEKTDELLHSKSHGVLMAALAFAISACKINPSLISRFESQADDLIYRIRQLSTSTYSSEHNIGNISDPFLQVKILQFLSILGQNNPKIYDKMSDLLAQVCTNTDSSRNAGNAILYQAVRTILDLNSDSSLRVLGVNILAKFLGNRDNNTRYVALNMLKLVVNSEENAVQRHRSTILACLNDVDSSIQSRALELSTFLVNEANVRFMVRELLSFLDNVSDELRGSTAQYITEVTNAFAPNKRWHFDTLLRVFKSAGNFVSESTLSTFLRLIASAPELHEYAVVKLYAALKEDVSQEALTLSAFWVIGEYGQMLLSPTMNFDDDQTLPHSVSESDIVDIIEEVFNSVEASRYIIVQYGLFALTKLSARLGSSSTASRIDKIIYSYKRNKNTEVQQRSVEFHLILNDSKLSKTILEPTPAPLPPPRTTPYQNAEQKLKANKHVEKRVQESNELLDLIGLTTPSVAEPLETPVDEMTQSPQSSLSRAPSTSKKSHFEDILGLFASPAPSAQPVDSLASSFASLDFNASASQPSNNLSLLSSIPSTSKSYPPIVVFDKHDVTLTLVPSKEESTKTAVIEAKFKNKNPMTRVEKIHLEVAVPKSQKLKIQPLRTTSMEPGGETSQTLRVHGPSGSQVKLRLRISVVRQGGSNTLDQVDFGKLPSDLLQ A0AAN2HA63 A0AAN2HA63_SCHPO MVLPFAFVGFFIFPICLASLLDWNDAYEYPKYSFEWSNVSILEGDIDSIKEKTEKTKLSSLFYAGKHEYFCVYPNASLIKQNSTTEPSYDLQELRIQGTEKINELANVFLIENRGYWTYDYVYGQHVRQYHLEPQQGSDKVLANPMYILGTAPNTQTKKNLEENWAIGFVEGKAYLQTTFRNGTMCDITKRPRHVILSYECSTNSDTPEITQYQEVSSCAYSMTIHVPGLCSLPAFKIQEDIPSEKIVCYNVIKEKSNEVDHKDSQHVVDEVAQTSPPEVKEVETQSS A0AAN2HA83 A0AAN2HA83_SCHPO MFIDLNVVWPTLGVKDLNLVKTVKTLERLGYTAIALNYQYDGKLQNVIKNPIVKELYPEQKIKIYSRITLTIESMPQNKVLSNVTKEFDILAIRPIGDRLLQQTCSDLEFDILSIDFTQRLPFYLKHTFMGLAVSRDIGIEISYSSGLRDVSNRRNLITNATSLVRATRGRGIIVTSETRTPLECRAGFDVINLATFWDLKQDQARKSVGESCRSVLLHAETRRDTYRSILKVVTDEAPSKKIRLSE A0AAN2HAA0 A0AAN2HAA0_SCHPO MLRNRLFKTPHQTGFQWRLGAPATGITIRNQPIRSYSGLRGNFLIDKRLSPVKFNKYSPSDIVFYNIGSSRLYSTETPTPSKVKEAPKQVAAEETKPTTVVKKPSIWQRVKGGVLHFWDGTKLLGVEIKISSKLVYKMAVGYELTRRESRQLTRTLKDIGRLVPFSVFVVVPFAELLLPIAVKLFPNLLPSTFEDAKDKEAKKAQLRKTRNEVSNMLRSTLKSGKFTFSNETRESKEFRDFFQKVRTSGQSPSREELIEVCKYFKDDITLDNLSRAQLVAMCRYMNLNAFGTDPLLRYNIRHRMRQIRRDDRAIYIEGINSLSIPELFNACNSRGIRTQGLSPAKLKEELSVWLDMRIKHGIPSVILMLSNAFSYGYNEGTYDSRWDALQDTLASIPDELYHETVVDMPTKQVSNKERLEILREQEELIEEEAEHVAEHPDLAKKQTEENKATSKPAVSAKSPESNIPKNERK A0AAN2HAC0 A0AAN2HAC0_SCHPO MGDNVFLEPDPWASSSNWGSPVKPLNYKTAIGNSSIPLQYRNYWDVFQANNVLLFPEEESYSDIFHVPQDVMKEFFTLIESSSNQPLRQIQFFVLLALVACYQLGVPSTLEQIFKQRNVLPILQRFNPELFNRSSDNETPLFPNNSPPASTTALNLSSNIVPSINESKILEQEDDDVSNKSLPHAQQSIIRSFPDIQKQPKGFFSYPSSTVSSIAPSTLEAGNLHSQQPPKFSVDSSVDDNAITPRKPFSKIPNRLSPSTQPLLSNSRHSSFRLASSSTSFPASLEMNVDIDLEPSGYFFYRHNNYIISDSSNTREVLRRYSDFFWLHSYLMKKYPFRRVPLIPLKKFHFAKRNASTQNSFLEHRRQELSDFVNDLSHHPIFSNDEVVRVFFTEPNVFKNWRRENQKRIDQEIEQFLVVPQSQVPDASETVKERLLKLNMSTTTAINNQLNIFRIFEKMIFTLQHFHEDFLRLQNSFNCLLDSGLYHQVFTSTFAQNESKIMSMASGHFYNIDSLLHQQNDAVKHTFLLGLSKEIKILISLRLLIERISEVFSTDLTKVRHTISNDENLLRETANSDESGRNRTFLNRSSKKRAENSLKSKKELYLKNLNQRYQIAHELEQELSYLQDYVFSLGNPYVEYCKQHVKLEEESLKIWHTLESDFSRLET A0AAN2HAD7 A0AAN2HAD7_SCHPO MQLHGKMTATAKSCALDFLDFVNASPTPYHAVQNLAEHYMSHGFQYLSEKSDWQSKIEPGNSYFVTRNKSSIIAFSIGKKWKPGNGFSIIATHTDSPTLRLKPKSQKSAYGYLQVGVEKYGGGIWHTWFDRDLSLAGRVMVEEEDGRVIQYNVHIDRPLLRIPTLAIHLDPSANSSFSFNMETEFVPLIGLENELAKEETSDNGDKYHHPVLLSLLANEISKSLETTIDPSKIVDFELILGDAEKARLGGIHEEFVFSPRLDNLGMTFCASQALTKSLENNSLDNESCVRVVPSFDHEEIGSVSAQGAESTFLPAVLQRICELGKESSLFSISMVKSFLVSADMAHAMHPNYSSRYENSNTPFLNKGTVIKVNANQRYTTNSAGIVLLKKVAQLADVPIQSFVVRNDSPCGSTIGPKLAAMTGMRTLDLGNPMLSMHSCREMCGSKDFEYAVVLFSSFFQNFANLEEKIIIDE A0AAN2HAF2 A0AAN2HAF2_SCHPO MHQNALNNATLNVLGHKKNGSSSIQELIEMDEEEAEMNQNVVCIGPNETAVSVELGDEYEKFNIITSLKKDNLFSKDGLLYAYYELCQEKFEKCLKEDDEEWIELWDLESRTWDLIQRLYSFRLSEQQGHIQSHAFSSRAVLEEEYYSQNPEAFENNIVFNWARDNSSDPPSIEIRGNRWFYTREDIKMKNRGGSRFSSNISGTIVSNLDPDADIRDDKRLDERDDNFERQFFHTAFCLFRSGSFEELLELCRRTGNHWRSASLQGILEYRDNLIDDVLQSETSGNKRKELLRRSCLALTKNKRIDSYERALYGALCGDLNSVLDVCTTWEDAMWAYYNSMTQYNLDVYLSSKAPQTETQLPPVDSGLGLTPELIFNSLSNSSIASIQEEASHPLIKLQTHIICNKISEILSSAHIQLEAIRTGNAPESGDLVTPPLLRILTHIILFLKISGLAVDEYTSDSIIQAYIELLASAKKVNLVPLYIQYLSNQVQYEAYSRFLILVDEESARSEQLQLAKKYSLDINHAALLAVEYVYDEVVSVSPEEVHTVYLKSIEEPVEPSYKKLICTLEWLLITSQTDELLRFANLVYRFFLSIGELNSAYDLYTHIPSDALNTLSSSDGEPENDSKFRDAYELMNYRALCRALKFYQEWEELSKQEVFEDSAVTKASTSYKVWKKKLNFASRKCVKSFTDLLQANWLHPSTLELKPDDDPLLYKTLMTIRNLYVPELILGLHNVYFSLEDYDSCFALANEVASEDLKLYHCLIKSGRLVEYVSYLGKAGECSLSTPNGLFSL A0AAN2HAG4 A0AAN2HAG4_SCHPO MAPISKVFDYLVIGGGSGGLASARRAAKHGAKVALIEASGRLGGTCVNYGCVPKKIMWNIADLVAKMKTAKQNGFPNSQLGSFDWGMIKRKRDAYIGRLNGIYERNVNKDGVAYISGHASFVSPTEVAVDMNDGSGTQVFSAKYILIAVGGHPIWPSHIPGAEYGIDSDGFFELESQPKRVAIVGAGYIAVELAGVFAALGTETHMFIRQSKFLRKFDPIISDGIMDHFQHIGINVHTNSLEFKKVEKLPSGELCIHQQDGSTFNVDTLLWAIGRAPKIQGLRLEKAGVKTLPNGIIIADTYQRTNVPTVLSLGDVCGKLELTPVAIAAGRRLSDRLFGGIKDAHLDYEEVPSVVFAHPEAGTIGLTEQEAIDKYGESQIKVYNTKFNGLNYSMVEQEDKVPTTYKLVCAGPLQKVVGLHLVGDFSAEILQGFGVAIKMGATKSDFDSCVAIHPTSAEELVTLV A0AAN2HAH3 A0AAN2HAH3_SCHPO MSLNDEEDDIEFINYIPLLASPINSSTCSTSIHDKCPFKQHISENGQNFGSAISSNISQRNFKTLRASHLSQYRDCNRENNTEDKNVISTGIAVNEKYQSVLKLKEKAPQISSAAKRKSFIKERGMLAKCFLARLEDEVFQGRLTSSLEKKEIGIVWSKSFSTTAGRANLKRNNKDAPLGKKTYAYIELSDKVIVTKERLYNTLAHEVCHLACWIIDNEMQNPHGACFKAWGKRIMNNMPYIEITSKHNYDIDFKYKWLCINEKCNKLYGRHSKSINPQKQVCRLCKSQIKQICPKIKQPNAFQIFLKENSKRLRKLHPHITHKELMKKLSDEYHRTKDAKQNVSKSVSLISSSDL A0AAN2HAI6 A0AAN2HAI6_SCHPO MSQEVSWTDILEKHPALRWIKPIPEDWEIFPKHLCAFESFLYVAVGQEVRSLDCRLLKHKNEASHKNFYKKLFNPELDFMIEQICLSKNGRFLAVVGKSKIVILGLRSKLSEQNPLAESVSNFGESVNNFSNSEHQENGTNSLKLSEVTICSVAVINPSSQIVSVRFHPLGKSGRSLVVLTETSLLLYEAGNGVLMPDYEIPLKLTHQASNSFDADVDLHIPTAFCFSNVSQGWGVFTIYILTRGGDVFSVCPVMPANAMIPQDVLKQIRLILTKKEDDADAENHRRNVHWITKLLGEAALANDLSTSFVISEGSSELFDSSDYVSVRRPDDFSFIPSMQGPFLLQPAVADDELIEDYCDIYSFGMNPIDVLAIGGSEGRLDLLLLVSEVSGRWSKLNDHGLASMKLIVSQVHSLYLSNNNPYMVLQPDIQSPYSLIAYHANGLHVVDIESWARDLNLNFENSEFLNNEEENDEDELSNVLVSIPSRTSVLERLDTNPLNESTDAVVGCAQLYYPSLGKILISLTRNWQTTVFDDSDLATMGVNKESLSNEMDYSKSLGTSSLEQVDDLDEKLTYTPLYVSLLEKTPFTDPSIPSLVERTIVPAELQNEITVSSASLRFLGKVVARYRETLNLLDHGCSELHHRLKLQREEYERQQNHIYKLSDRISNFREKAWSTEHLEHLTSDMSMCEKRIDQVLQRVMDLRVPDLSDKEKQFIKEIGNYKEKVTGERGIEKRVETLKTLLQRTKPRDAQTTLVASSSDMRLAAIEQLQKLLAQQSLSIKELKTKTVSFQRLLQTS A0AAN2HAK5 A0AAN2HAK5_SCHPO MASSTIYNIFFRRNSSFYATIFVSAFFAKIGFDVFTDSVWKRANAGLTWDEVKPRFLNKDEDAEDDE A0AAN2HAN8 A0AAN2HAN8_SCHPO MPSIILYPIYFDKSRPRRFRCVPKDKAILNPLAKNIADVVRDLGYKCKLEPLKTHPADWVNPGRVEMVLPEKIQKKYVINEIAKVLLLRPTVKTDPLSLPIQNVPARLPENPPAYPKGVLGNTILPLHSPALSGGGISENMFQEMMQEMQKQPGLAGGMNPMAALAGMGGPAPPMPTPQASSSQRKQKSIEPEYDLDLE A0AAN2HE77 A0AAN2HE77_SCHPO MNTSENDPDGHYDFPEMTEHHSDRASSYANANNVNSTQPQLVSSEQALLAILGGGLQSITPNSVNQNAYSRSTYRTDGGLNSQPVSSLNNQWGNYNPAFLPSRYDSSFHPYTISQAANQPFPQHLLGNSNAGVAQQSGMRTIGLPPTVGSSFPQQKSSTYENFFDANSPSSQQFPSTYPSRSQNPLSSSGDGSTAIHAGPIQHQNSNAFSNYPYPLDASHLSSQQLLSMYRDQVSHGVTPSTFRNHESFMPTQLVSATELSKSVDNAVLPIPPTTAPAVVSPPASSFPLMSSAATSGNISSPALFDSELGARPEGSVAIEPSRVLLQWSSQSSSHTIPSAGASIPTSSLKSFFEHAAEAARKCNLDPRALESFEQHMLSDRLHDPVVLFHYFQIRNSICWLWIKNPTHAISRVEAQGVCVDRCLFQLASLAYEFLVRYGYINYGCLSFDSSFTNETNTGTTSSSASKQKTIAVVGAGLTGLICARQLTGLFSQYSSSFLSKNELPPKVIILEAKERTGGRIYSRALPVSHTSATQINHHTSNSNSISSNSTSLNPKDVTDPSHIPSAIDLGFQFLFSPMDDILLNLLNKQLGIEVTEMTGSDLVYDETDTKVLDMVEVKKLNILWEKLLEYVSVCFFINVEESVRISWISQFQLFIDEMFPDHLSKSLSLNASHEFSFKKTMLILIDEVSSYAKLGNSQKKFLIWCFKVAELDDTLYPLNTVDTDFSKDILIPKVARRGLSQLPWALQSYPSPLNIHYEKFVSKVTIENDKCTLDCKDNSSYEVDQVVIACSPSHFSSNIEFSPGLPNFVTENIKSIDFKPGKKVILRYAAAFWRKNIRSFGIIPKSLSQEMNNDENDGKSCFVLRIWNMLPETGVPILVADINPQMTSSSSNETSHLIQELHSLIVDHFQNDSNSSADLLDAWVTNWSRNGVYDGLNSYPNFANDKQQYEKRFRQSQLSYNLGRLHIAGDYIFSCVGCRTLQRSFLSGLSVCTGIIDSLAPISLTIPIIGETSRKELDQFLRNSKVNNFDPNAEAQRHLSYQARYRLKKQERLDEHKEEQEQLVTELLGYLPEPPSKPNANPFLLYQKMQWHVCRALADEDKRRLTGDSTAKATINETRAKLGKTWRQLDDLGKKPWIDEIAAQREAYAGKILRYQRLTKEYEMRAEQIRNDYAAKCQDEPIPDDEARLFMQAQREEEQRKQTQDDNISKSREASDEEYHDDGSSDSGYNGTRY A0AAN2HE97 A0AAN2HE97_SCHPO MTDKKPEVEHLQGENPPKDTYSAEDTATAILRKKRKPNSLVVDDATNDDNSVITLSSNTMETLQLFRGDTVVVKGKRRKDTVLIVLTDEEMEDGVARINRVVRNNLRVRLGDIVTINPCPDIKYAERISVLPLADTVEGLTGSLFDVYLKPYFVEAYRPIRKGDLFVVRGSMRQVEFKVVDVAPDEFGIVSQDTIIHWEGEPINREDEESSLAEVGYDDIGGCRRQMAQIRELVELPLRHPQLFKSIGIKPPRGILMYGPPGTGKTLMARAVANETGAFFFLINGPEIMSKMAGESESNLRKAFEEAEKNSPAIIFIDEIDSIAPKREKTNGEVERRVVSQLLTLMDGMKARSNVVVMAATNRPNSIDPALRRFGRFDREVDVGIPDPTGRLEILRIHTKNMKLADDVDLEQIAAETHGYVGSDLASLCSEAAMQQIREKMDMIDLDEDEIDAEVLDSLGVTMDNFRFALGSSNPSALRETVVEVPNVRWEDIGGLEEVKRELRETVQMPVMYAEKFLRFGVTPSKGVLFFGPPGTGKTLLAKAIANECSANFISVKGPELLSMWFGESESNVRDIFDKARAAAPCVVFLDELDSIAKARGASAGDSGGGDRVVNQLLTEMDGVNSKKNVFVIGATNRPDQIDPALMRPGRLDQLIYVPLPDEEARFSILQTQLRHTPVAEDVDLRAVAKATHGFSGADLEFVVQRAVKLAIKDSIEEDIKRENETGEAPADDVVMDEDASVSQVQRHHVEEAMKMARRSVSDAEVRRYEAYAHQLLTSRGLTGFQFDSADSNTNGPSFGNDGADDLYA A0AAN2HEB8 A0AAN2HEB8_SCHPO MPLPESVGDLVVLHFETNLDDHGISIGRAPCEIHEICWVILDGKTLEKQHCESCSIREDSSRHGICGSASSLTEAIFTLDNSIQERLNFQGKPFTFVVMNGRELRVLLPKEARDQGITLPSYMRHPRLFDLSSEYAKWQIRMGAVPPYTITLSHIFGKLDVDSLPPITESKAIELSPSDAPYITKGLTQCWRLANATTLLLRKAEKDSRGHSLPSVLTQPINCQADARSFYAERSKIVHVAGLTNDVTQLELESWFTNHGVHPVALWTLKTPEPYKSTGTGFVLFASHEDAADALAFNGYCLGDRMLEIIPSSTKVLDKASDILIPFPSSKNRPRPGDWNCPMCGFSNFQRRTSCFRCSFPGPTHVSAATGSNTFSPDFPYGNSYGNGSSHFIANYGGSVHHSNENTMQSDLQHQNGNNAVNHHHSSRSFGGNVPFRAGDWKCGSEGCGYHNFAKNVCCLRCGASRATAAVVADHASGPVNGSYSHNSYSHIPPVMSTSPPNHSVYPYSQLSINSVTANHGQNFGGQNGGNVSRFDDHGRFKEVSRPSVTTDQGDWLCECGFTNFRRRSNCLRCNAPHYSNMQIPASLPSDFNAYV A0AAN2HEE3 A0AAN2HEE3_SCHPO MAWSQVEISKPHLAYAIIGGFTSLFMLCSLIIKEKLFLGEATMATATGLIFGPYVAKLFVPTSWGNTDYITEELARVLLVVEVFAAGAELPRAYMLRHWRSMFVMLLPVMIFGWLVSTGFMYALIPRLSFLESLAIAACITATDPVLASSIVGKGKFARRVPGHLRNMLLAESGCNDGMAIPFLYLAIYLIIEKPARHAGRDWVCIIILYECTFGCVLGAIIGVIARKMIKFSERRGLMDRESFLVFYFVLALFCGGIGTIIGVDDLLVSFCAGAAFSWDSWFSKKTEESHVSNVIDLLLNLSFFVYVGAIMPWPQFHMPHMDLSVWRLVVLAICILIARRIPAVLLFKSFVPDIINWREALFAGHFGPIGVGALYTCLVARAELEVHSTVPEPNDAIENPEIPNWYCIQVMWPVVCFLVLSSIIVHGSSIAFFMLGKRINTLALSFTRTRDSHFAFNLPRVRQGQSLPIKRVDALRSSANSIASSIRRRHPVNIQEDEDADISTVSLPEAAHLREERAESPRGGHYDAEEFPSEDYESRQPRRSNEEDREEEMNPGDETYLIGEDLVVEDSQGNIISHTSSRDANGPSIDEKLAQGDPKAKSFGRKFRSFLRRSYDTFQRNLHEPDDERQREPTLGHIESSIENHRPRYSRQNSESHLRENSVERRRREQVLTNIGDSESEDDNIPRPGIVPFYNENNESSSDTRNGLLSDNVSESRSRRPSRAPSAAVSSEGSPVEEDNEAQHRPNIRFLELPVPGNNNRRRSHSSYRRGSFNAYS A0AAN2HEH2 A0AAN2HEH2_SCHPO MAEIQTAQNPLKELEKILERNNKQKNKKSRNQVRREKKKLLREKTNSGAKLAEKNSDDKDQLTENNDNLYNDKKSNGNFYDTNKTDSVDGMVYTTIVDSVELDPNDPLIEQFKDVFNRFKADGQEKDFEDTDKGQIMYSDDEILSEGEEDALQKQQEEKLSKKKLRKLKRMTVAQLKMLSEKADVVEWWDVSSLDPLFLTHLKAYPNTVPVPRHWNQKRDYLSGQRGIERQLFELPSYIRATGIVQMRNAVHENEADMPLRQKMRERVQPKMGKLDIDYQKLHDAFFRYQTKPVLTGFGECYFEGKELEADVKEKRPGDISEELREALGIAPGAPPPWLFAMQRYGPPPSYPDLKIPGVNCPIPTGAQWGFHPGGWGKPPVDQFNRPLYGDVFGNVKPRIHAGTGSPVSTQHWGELEEFEEEESSEEEESEDVEYPTEEITERETIEEYQSASEPRSQREDLHAEPLTYFNQSNVEVDNVELRKNTQPSSDAANRDLYQVLPEKSTNISGFMGPQHQYDIPTAEDTLPQKRNAHSMLSSTNKGDVALNQSSNWQDELSELVSEQAMKVGAAKRQKTQSKRDKFRL A0AAN2HEJ3 A0AAN2HEJ3_SCHPO MSDLDGFCQNAFSDLNSLNQQVFKANYAVRGALAILADEIQDDLLENPSSYPFSEIVYANIGNPQQMGQSPITFVRQVLSLCQYPTLLDHAEEKWFQNLFPTDVVQRSKMLLKESGSLGAYSASQGIPLVRRHVADFIRARDGFDCEPSDIYLTSGASHAARLIMTLIIARPTDGVMVPAPQYPLYGAQIDLMSGSMVSYSLSEENNWDIDFDQFKKSFDEASKKGINVRLCVVINPGNPTGACISENSMEKVLRFAKAKGIVLLADEVYQNNIYQNKFHSFRRKLGELREKEPDNHWDQVSLISVNSVSKGQFGECGQRGGYLDVVNIPEPAKDQILKLATIDICPPVAGQLLVDMLVNPPKPGDPSYDLFIKEVDEIHEALRLQCRQLYEGTKRMKRVSCLEPHGAMYLHPSVSLPEKLITTAKAQKIQPDEFYAIELLKRSGICVVPGSGFGQPEGDYHIRITFLAKGTEYIERFVKAHNEIMDLYE A0AAN2HEL6 A0AAN2HEL6_SCHPO MGSHSDSEVDWDNEEEVWEDEVHEFCCLFCDSTFTCLKDLWSHCKEAHNFDFYQVKQQNNLDFYACIKLVNYIRSQVKEGKTPDLDKLSDILRSDEYMISVLPDDSVLFSLGDELDSDFEDDNTLEIEVENPADVSKDAEIKKLKLQNQLLISQLEEIRKDKMNELTSQTTDQLSVTPKKADNDSYYFESYAGNDIHFLMLNDSVRTEGYRDFVYHNKHIFAGKTVLDVGCGTGILSMFCAKAGAKKVYAVDNSDIIQMAISNAFENGLADQITFIRGKIEDISLPVGKVDIIISEWMGYALTFESMIDSVLVARDRFLAPSGIMAPSETRLVLTATTNTELLEEPIDFWSDVYGFKMNGMKDASYKGVSVQVVPQTYVNAKPVVFARFNMHTCKVQDVSFTSPFSLIIDNEGPLCAFTLWFDTYFTTKRTQPIPEAIDEACGFTTGPQGTPTHWKQCVLLLRNRPFLQKGTRVEGTISFSKNKKNNRDLDISVHWNVNGKADSQSYVLN A0AAN2HEP1 A0AAN2HEP1_SCHPO MNSKTPTLGIVCSEGTISLSLEEGFEFVGVPLSGEGLKLRVEALAPSERLQEFLDDEVAYHPEENVHKVVGLSSAWLELDSEDTLIADRSEEVLLKEASYASYCGLSSIILNGPTSPMNVMRYARAVSSALNSTMNLKFLVQLAIESGHEDYFETWKMWDTIRSACGYHPRLKVALELPPACSPPIELVNRWYAEPIEMITMSCMAFVPNPNGYPVLGRKLRAIYALYLRLNPRILLWDNDAPEKIGDSPDYSIYMKHLFDSQPPAPLVEDLADSYKDYLQVPLQPLSYNLENITYEIFERDPVKYAQYEQAIFSALMDRDESSVTRIAVVGAGRGPLVDCALRAAISSSRTVDMIALEKNPNAFSMLLMRNRQDWAGKVTLVFGDMRTWNPDYKIDILVSELLGSMGDNELSPECLDGVQHVLDEETGICIPSSYISYVTPIMSPKLWSEARNMNDPNAFERQYVVLMNSFDFLAADDEFRFQSLWSFHHPNKDSEVYTKNLHNKRFASVRFQASSPGILHGFAGYFEATLYKDISLSIMPATMEAKSPDMFSWFPIYMPIKKPMYVPENSQLEFHMWRLTDGMRVWFEWCANAYLVLRNGSQIKLSSTEVHNISGKAFSCNMY A0AAN2HER6 A0AAN2HER6_SCHPO MLRKLPINFAKWTVKKVPVQQKRFNSQQKEISPHIMFYKNYARPLGKVTLFALATYYGLEIVWWKLDASEQEAIKNSELRNLENAK A0AAN2HET8 A0AAN2HET8_SCHPO MSGSYAPIEDSADELSVHSGNDNEIDLEKGLLPKCNTGNGGTTPCSEPPHYDSDAVVEMDMYENNIYMRTFKLRPFAKSGVTNSSNVVFQMKTYENNRHMQTFRLRPFAKNGVTNGVKLAQSLFLLLPFNFIFFACLFFRKASFTDFSLMGWILFGIWCLTCFLSSFILYAYHESWTKFARERSQEFSLILFGLLFPGIVTMVVFYALYMRSMYG A0AAN2HEX1 A0AAN2HEX1_SCHPO MGANNPNLFNTDESTTPPDYGEDSLSITHRENHSSGTADNSSTSPLKKAFLSFISIFVLNVPAVCYLTYKDALFKDYGKDEWVYFAVWCASCLMIFISLWYFYETWIKAVKVTVIFLAQCIKVTVVFLAQCVKVTSISLAKCVKLTAVFLAQCVKVTAVFLAQCVKVISIGLFNIRREMMIIIWLLWLIICCILFGCVKSGDLNLNKALIYSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVFLLQSGIVLVLNGTMFLRGKHFEWTGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILEGAGRAIRGANDNNDIPLGEMEVESEV A0AAN2L0E2 A0AAN2L0E2_SCHPO MATSNVSSRVNELLEAVKKEFEDICQKTKTVEAQKDDFEYKAMISAQINEMALMKQTVMDLEMQQSKVKDRYEEEITSLKAQLEARRKEIASGVVPQSSKTKHGRNSVSFGKYGNAGPFNSDNSSKPLILNNGSSGGTPKNLRSPAIDSDGTVLAPIQTSNVDLGSQYYSSPHVRPAVGATMAGSAMRTFPSNLPLGHPPPPSDSANSSVTPIAAPLVVNGKVSGNPPYPAEIIPTSNVPNREEKDWTVTSNVPNKEPPISVQLLHTLEHTSVICYVRFSADGKFLATGCNRAAMVFNVETGKLITLLQEESSKREGDLYVRSVAFSPDGKYLATGVEDQQIRIWDIAQKRVYRLLTGHEQEIYSLDFSKDGKTLVSGSGDRTVCLWDVEAGEQKLILHTDDGVTTVMFSPDGQFIAAGSLDKVIRIWTSSGTLVEQLHGHEESVYSVAFSPDGKYLVSGSLDNTIKLWELQCVSNVAPSMYKEGGICKQTFTGHKDFILSVTVSPDGKWIISGSKDRTIQFWSPDSPHSQLTLQGHNNSVISVAVSPNGHCFATGSGDLRARIWSYEDL A0AAN2L0F2 A0AAN2L0F2_SCHPO MAPRVASHFLGGNSLDKAPAGKVKDYIASHGGHTVITSILIANNGIAAVKEIRSIRKWAYETFNNERAIKFTVMATPDDLKVNADYIRMADQYVEVPGGSNNNNYANVELIVDIAERMNVHAVWAGWGHASENPKLPEMLSASSKKIVFIGPPGSAMRSLGDKISSTIVAQSARVPCMSWSGNELDQVRIDEETNIVTVDDDVYQKACIRSAEEGIAVAEKIGYPVMIKASEGGGGKGIRQVTSTEKFAQAFQQVLDELPGSPVFVMKLAGQARHLEVQILADQYGNNISLFGRDCSVQRRHQKIIEEAPVTIAPAATFHEMERAAVRLGELVGYASAGTIEYLYEPENDRFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQVAMGLPLSRIPHIRELYGLPRDGDSEIDFFFQNPESFKVQKVPTPKGHCVACRITSEDPGEGFKPSSGMIKDLNFRSSSNVWGYFSVGTAGGIHEFADSQFGHIFSFAESRESSRKSMVVALKELSIRGDFRTTVEYLVRLLETKEFSENEFTTGWLDRLIAQKVTSARPDKMLAVVCGALVRAHATADTQYRAFKSYLERGQVPSREFLKNVYDIEFIYDNTRYRFTASRSSPGSYHLFLNGSRCTAGVRSLTDGGLLVLLNGHSYTVYYRDEVTGTRISIDNLSCMLEQENDPTQLRTPSPGKLVRFLVETGEHIKAGEAYAEVEVMKMIMPLVATEDGVVQLIKQPGASLDAGDILGILTLDDPSRVTHALPFDGQLPNWGEPQIAGNKPCQRYHALLCILLDILKGYDNQIILNSTYNEFVEVLRNHELPYSEWSAHYSALVNRISPVLDKLFVSIIEKARSRKAEFPAKQLEVAIQTYCDGQNLATTQQLKVQIAPLLKIISDYKDGLKVHEYNVIKGLLEEYYNVEKLFSGINKREEDVILRLRDENKDDVDKVIALALSHSRIGSKNNLLITILDLMKSEPSTFVSLYFNDILRKLTDLDSRVTSKVSLKARELLITCAMPSLNERFSQMEHILKSSVVESHYGDAKFSHRTPSLDILKELIDSKYTVFDVLPAFFCHTDPWVSLAALEVYVRRAYRAYSVLEINYHTEAGTPYVLTWRFQLHSSGAPGLGANSTNGSNFPASTTPSYENSNRRLQSVSDLSWYVNKTDSEPFRFGTMIAAETFDELENNLALAIDRLPLSRNYFNAGLTLDGNSSSANDNTQELTNVVNVALTSTGDLDDSAIVSKLNQILSDFRDDLLEHNVRRVTIVGGRINKSAYPSYYTYRVSAEQKDGNLVHYNEDERIRHIEPALAFQLELGRLSNFNIEPVFTDNHNIHVYRATAKNMDTDKRFFTRALVRPGRLRDEIPTAEYLISETHRLINDILDALEVIGHEQTDLNHIFINFTPAFGLAPKQVEAALGGFLERFGRRLWRLRVTAAEIRIICTDPSTNTLFPLRVIISNVSGFVVNVEIYAEVKTENNSWIFKSIGQPGSMHLRPISTPYPTKEWLQPRRYKAQLMGTTFVYDFPELFRRAFTDSWKKVPNGRSKVTIPQNMFECKELVADEHGVLQEVNREPGTNSCGMVAWCITVKTPEYPNGRKIIVVANDITFQIGSFGPQEDEYFYKVTQLARQRGIPRIYLAANSGARIGVADEIVPLFNIAWVDPDSPEKGFDYIYLTPEAYERLQKENPNILTTEEVVTETGELRHKITTIIGSSEGLGVECLRGSGLIAGVTSRAYNDIFTCTLVTCRAVGIGAYLVRLGQRAVQIEGQPIILTGAPALNKVLGREVYTSNLQLGGTQVMHRNGISHLTSQDDFDGISKIVNWISYIPDKRNNPVPISPSSDTWDRDVEFYPSQNGYDPRWLIAGKEDEDSFLYGLFDKGSFQETLNGWAKTVVVGRARMGGIPTGVIAVETRTIENTVPADPANPDSTEQVLMEAGQVWYPNSAFKTAQAINDFNHGEQLPLFILANWRGFSGGQRDMFNEVLKYGSYIVDALASYKQPVFVYIPPFSELRGGSWVVVDPTINEDQMEMYADEESRAGVLEPEGMVSIKFRREKLLSLMRRCDHKYASLCNELKRDDLSADDLSTIKVKLMEREQKLMPIYQQISIHFADLHDRVGRMVAKKVVRKPLKWTEARRFFYWRLRRRLNEHYALQKITQLIPSLTIRESREYLQKWYEEWCGKQDWDESDKSVVCWIEEHNDDLSKRTQELKSTYYSERLSKLLRSDRKGMIDSLAQVLTELDENEKKELAGKLASVN A0AAN2L0G5 A0AAN2L0G5_SCHPO MSESTKETIEVLYEIGTLLGTELDKTTLSLCISLCENNVHPEAIAQIIREIRMAQEQTVDTEPS A0AAN2L0H4 A0AAN2L0H4_SCHPO MKEGNELEKYSKIELNSEIWEDEEEEDNSGIVSQNERLMKLVNKQREIIYELHKDLEKVKKDNTSLRMRLSKYESTDSFPSSQPSRANSPQSDSYSSPYEKGKLFPKISLKSSKDVPTASAHISSSDHEKSSSVSLSALNNYNKTTDIKARSLDRLSDMTRPKLLLNTKRSHRSSEEPGASSPVTSPILKDSQKERIQALRNKAIKTYSVSTESAERIDSIRSDNLSPLSLNTSSFRRPITKPTPFNSDSNISIDPKDNNSNKQDHFAEIEDELRQQFLDIKVGRANASSPRRKSISIVKPHGISSPKHSTNNLSSKSGKFHSDFRVVSENVLLQARSETNSPIIENKEANNFLAPTSNVPAYSTPARPTESPPPPPISSSSTTPRPDDKPSLPPRGLSEDNDSLSLQKTGSSDTRRSSFSTLKIPDSDICFTRRRSDSNRTWTVIDPHHSQSFDNDILAEIPTSKLDNSSQKSPGKLSSKGLLNSFSPISPFSKSKSHNHHPSSQVEKSTSNSKGSMLPLDTLYNNKLSFRLDESLVRYLRFELMKTSLASLSPDFDCIGLQFVVGVSASSHLASQWKDEVWSFTRSIGECRSFATSFVLDIGAPPFPTLDWFTNDSSVIQNELLRRSVDTYFRYIFQTDLKLEQRIKLLEFLSSDTLREYLHDVFFLPPEHAQKEGVLLKYIENSGLVSRYFYLKDNILYFAENRNSPVLGTIHLKDAQVNRYNANLPIFSIIDPPHEFLTGENYQSAFVIQEKQTETRTGTATVHVLLARDVEDQKSWLRAILRQVPGSTSPLNASPFSVLSSDFPGSSRYRDQSSPIRFYGKADSRPVSQEAILSQDISSSPSPVLPPSENVASYADDSLVSNLTMSPKLRDSMEQVPLENHREFEISDRVSELSFDSSTGSVLEIADTRRNQDAPEKHVPVIEIQSSRPSLEKTDQSTPVELLIDSHSQNSQNEEKRSRMKFWAFPHHKAENYEQISDTNIPVIETNVMLSPSSTTSAEPLQKHIVRKSGIFGLPLNEAVNISTQFNDSGLPIVVYRCIEYLESCRAEKEEGIYRLSGSASTIKHLKEQFNEGVDYDLLSSDEEFDVHVIAGLLKLYLRNLPTNLLDTSMHKLFELLPNVPNDSAALGELCDVISKLPPENFALLDSLLHHLRRIIAFEKVNKMNIRNVCIVFSPTLNIPSDIFMMLILNYDHIFTDISRQTNGAQNESDSDVSDDNGEDNEFF A0AAN2L0I3 A0AAN2L0I3_SCHPO MSSFMPKIYLKLTLKLHPELDERDCQAVQAMLHLVFSWREKKILSEICYNKYSLRKTPARFEVYLKRHFQKRILASAIRRETIIKC A0AAN2L0J4 A0AAN2L0J4_SCHPO MTEKARTVSDLTISQAIFELSSPFLENKSQKALDTLFSAIRDHDLAPLYKYLSENPKTSASIDFDSNFLNSMIKKNEEKLAEFDKAIEDAQELNGEHEILEAMKNKADYYTNICDRERGVQLCDETFERATLTGMKIDVLFSKIRLAYVYADMRVVGQLLEKLKPLIEKGGDWERKNRLKAYQGIYLMSIRNFSGAADLLLDCMSTFSSTELLPYYDVVRYAVISGAISLDRVDVKTKIVDSPEVLAVLPQNESMSSLEACINSLYLCDYSGFFRTLADVEVNHLKCDQFLVAHYRYYVREMRRRAYAQLLESYRALSIDSMAASFGVSVDYIDRDLASFIPDNKLNCVIDRVNGVVFTNRPDEKNRQYQEVVKQGDVLLNKLQKYQATVMRGAFKV A0AAN2L0K4 A0AAN2L0K4_SCHPO MQISEESKERLVKVFNIGKTVTHYGWIPLILWLGYTQSNPKPQLMRVINPLA A0AAN2L0L7 A0AAN2L0L7_SCHPO MNKRQSQLKFGNEGISLAVPKQSLQECSYMSNLITDRESTFLSYFVPSKDPKMLPVYRFMFQESADLKHCNHKMQAWRFPNEIEAFNDDGEEYSGQKLLNVLRKEDVYGMVVCVRWYGGQLLGPVRFQHITITAKQSIDKYKSVLEEERKKQLLRTETGLLRQSSSRSSSLLDQRIRQITAKDKTVNLLRKTLNRPLLHEVDYHGKSLEILDMLLQSRNSMISSLRSELQEKNQKDKKKEVNKLEEKMTNAKEPNVNVPSMKASSAISVETPETIESEASVDHKEASKIIKDVEKEE A0AAN2L0N1 A0AAN2L0N1_SCHPO MAKRSVEELKRSADEEASVKRKEKKSKHEHKKHKKDKPSADKDRISKKDKKKSKKGKSKTKEESIEINAEEGAKIAQPAIGSANASNHNDEEAYDRYIKKHNISFADPKSSENLLPILQFDELDVSAKLREGLKNYKEPTPIQAATWPYLLAGRDVVGIAETGSGKTVAFGIPALQYLNGLSDNKSVPRVLVVSPTRELAIQTYENLNSLIQGTNLKAVVVYGGAPKSEQARAAKNASVIIGTPGRLLDLINDGSIDCSQVGYLVLDEADRMLDTGFEQDIRNIISHTPDPTRNGSRQTVFFSATWPESVRALAATFLKDPVKITIGSDELAASQNITQIVEILDDPRSKERMLDNLLRKHLSSGGKDDKILIFVLYKKEAARVEGTLARKYNVVGIHGDMSQGARLQALNDFKSGKCPVLVATDVAARGLDIPKVQLVINVTFPLTIEDYVHRIGRTGRANTKGTAITFFTPQDKSHAGELVNVLRQAKQDIPEGLFKFGTAVKPKLNAYGSRVVDVPVKAATKIVFD A0AAN2L0P5 A0AAN2L0P5_SCHPO MLSLAYHTLEQVSDKVLLRKSSYNLTDDDLQAVVNCTTTILEQRAVIDQIAYLGQKYYWVSVDGYNNNNYTISDEMENLLRQCINNYDDRANVALVTHNVYAVSGSHSELQLQEHYDYFGYGLPEDYDGQSSEYYDTDLDVVTDSSIQLSRRSGNKPDTINDNSWSRYGVALAFYLFTNGVQYVATKHTPWCGKC A0AAN2L0Q3 A0AAN2L0Q3_SCHPO MKNNYTSLKSPLDEEDELKTDHEIDLEKGLLPEYNSEEEGTLPLYSDISKLANPVPEDSSTGPTEIANPNVERRQEFKDSHPNIYFLLRLLISVLAVSVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPILFIATFCFFETWTQAVAQCIKVTVIFLAQCVKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLEGIGNAFGGIGNAIGRIGNAFRGANDNNNNIPLEETEAESEV A0AAN2L2Z0 A0AAN2L2Z0_SCHPO MKVQDDFILTIDDSEDDIHYDDYDADAVDEEMPSNVELKKKSKKATPAKDSDFNGEFLFEADVNKDLSSATDMNWDFDMGSKTESNRASNTVDLDAIISRNRKPDDDEFPSSFPSEEELQEPEQENIDSDDEDLAIDGFGAGAIAENEDESSQDESESEEEDDITEPVPSFANISTQDFNSDSAAGSSDSEEDEEEIAKKNAFFAEGDKEKSMMTTTHSSFQSMNLSRPILKGLSNLGFEVPTQIQDKTIPLALLGKDIVGAAVTGSGKTAAFIVPILERLLYRPKKVPTTRVLILCPTRELAMQCHSVATKIASFTDIMVCLCIGGLSLKLQEQELRKRPDIVIATPGRFIDHMRNSQGFTVENIEIMVMDEADRMLEDGFADELNEIIQACPKSRQTMLFSATMTDKVDDLIRLSLNRPVRVFVDNKKTTAKLLTQEFVRVRPQRELLRPAMLIYLCKELFHRRTIIFFRSKAFAHKMRVIFGLLSLNATEIHGSLSQEQRVRALEDFRDGKCNYLLATDVASRGIDIKGIEVVINYEAPATHEVYLHRVGRTARAGRSGRAITLAGEGDRKVLKGVFKNSSAQNTKLVNRNLDFNKVEKFGKEIEELEPVVQKVLDEEKQERELKIAERDLKKGENIMKYGDEIRSRPARTWFQSEKDKQASKASEAKDKKSLAKRKKQMEKEEVPRAYKKTKNDRLSNKKSTKKSKSKRK A0AAN2L303 A0AAN2L303_SCHPO MRFLFFLPPSFITSFLYLALYSFPVPYCII A0AAN2L314 A0AAN2L314_SCHPO MSNRDSANPPGFNDAVPLAICYIDSSTSSHDEYLTLLQSKVSAPDKNFRDETVDGAPFLAGDAISKGHRYSPPVRSDRASAQGLLQQHLEKSSTLENLKRYSSTLLGRQNDAVIDEPFAPFRPPPRVTLSESRRDRWLQGLSDPMVPLSSLIKTIPHGLWGEDILRMLVKFRVPFTRAIWFIRCAGVNEARSFLRKVQTTDITEWVKNWTDVAAGFLISFISSFLNADIYSFADDYTYLLKLFGRLLAEELVSPKHFLLRIVSFSGDSSLKSFSLHFFALQFFSTSLIQYTHICRKCVITILQSYQQLIVDQPANLLKFSLLSKKVSHFLFTLAQKNIESFFFPTEWDKLKPTIILLWKDFPNYSTLLSIMQERNSKAMYMYKPVTSSIRFLQIISCLSFPVGWRTLAKDLFKLLPVYTGVPLLLHWCINCRSIFSGDRNFIVSSIFDNANFDRNLIVDLTLSFVLKLHPLEYNECVAAAQLLDHLAACGYFFFSKYIARLASLGYLRESMLNSSFMDDQRKILVQLPILRMSQQLKNKIYYILSKGNYFVDWSICDEYVKRFKEDHFSFMFKKEENYAIITLSLVKIASTPMSKLYEDYLVMLFAFHYSMFQVMTKLIADNLVHFSFQSCALIFLYKISSYFVLDAKLFSSICSVVPKTESQKLLLNEMGKLFQVELNFSYDSPDVNLLIEQFYEITSYESNYDDAFVEYKDATVANRKDFIEFLFHNITVSSKHTAVIFTSDLLMVLKIALNHPPYFDDLATTTFSSLLKRDECTILSFFKILQFYGCKLLSVDQIWAVVSDVYEAQDNNTTLKQFFNYLLDESTWPEGYLEERHWRSILCKEARKHDSGLKLFKLGIKLCTRNEQIMKTIWSFIHVHDCNVISEVIPDQRFLRTLTEHFMIDLRQLDIVTCLKKALVTLDEFSAPLYATWLTTLDDDELSELTDDVVQKKVLESLDNYKSGIWKLVLSGLPNCKTVFEHLLLFSLEERLDLPAAFLQDLIGASAYVMEQVPDSWFLEKLPCPLTQSLQSFSHLSNHIEVLDSTRQSRLTFLCHLILHMHGFVELTDQLATLESLTIRKCIYRNQELLDLLLFSIHLVKPNVETNDEVCNTLKAWENIESRPYTIDFPEALQQYSPRIVLYEPTFW A0AAN2L325 A0AAN2L325_SCHPO MDIFHKSYNVILSPPKVQQADETISKLCDRLEHATLFEDRKAAALGIKSFAREFKELVAAHGLKGIIQSLHRDYDDPELLKVTLETCLILTRHDDDSRASDTGLWIADQFILNQDNIQCLLQSISHKDFYVRLYSVELFSAILSCRPTELKDCLQTFPSAISSIMVPLRDSIEPVRNADLYFLSELVKDCTSIQKLVVFENAFETLFSLLENEGGVDGGIIALEALKFLNVLLKDNISNQNYFRESNHIPSLLKLLSVDTFVDGTWDTSRVQCVIEALYALQSLVPIGLSSSIANQNAVVSNHGIDVLLTLATHPDLLFFDVQKISWITLAHVVYSNARAQNSFVDSTFFDIKNTDVLTCLFDYLFLSSISPSHRYSVAFFLRSLTSENDELSSKFLKQIIHAYTHKQDNRLNIIQGYLDLVHLSDQDQYDNWFTSTILTYLVIDNDQRKYLLCSIPLFQDMDNDEDSESEDKVTFIQCVSTKLIATLRHENALQNCVGYLTLLIALVYGNPDSVKDFLSESSILQTFLTALMDESSSANSVIQGMIAVFLSLVYYYCPIESPVSKSDVYNAITSAVKRDVFINRLQRLRKDELIRDHVPVNEAEDGNCNDILFDTTFVNFFKDNFYRLKHAIDDAADAFNTKIGEINTLDAFDEAQKQLKSLREEIDNTKEALDLSVKERSIQEEKLNESLKTSKTNLEEQTQLAEKYHEELLDNQQKLYDLRIELDYTKSNCKQMEEEMQVLREGHESEIKDFIEEHSKLTKQLDDIKNQFGIISSKNRDLLSELEKSKSLNNSLAALESKNKKLENDLNLLTEKLNKKNADTESFKNTIREAELSKKALNDNLGNKENIISDLKNKLSEESTRLQELQSQLNQDKNQIETLNERISAAADELSSMESINKNQANELKLAKQKCSNLQEKINFGNKLAKEHTEKISSLEKDLEAATKTASTLSKELKTVKSENDSLKSVSNDDQNKEKSVNNEKFKEVSQALAEANEKLNARDEEIERLKVDIIGLQNASLNMQSLKDSDNRTISDLESKNKELEKKLKEADEYWLLIVEELESKRTKDKELLRQCGQAVSEDEQSEEE A0AAN2L337 A0AAN2L337_SCHPO MIPSDYSNKFYPVDGVVPKHETQAYEFLKKFPEYDGRGVTVGILDTGVDPGAPGLSVTTTGLPKFKNIVDCTGAGDVDTSVEVAAADSNDYLTITGRSGRTLKLSKEWKNPSKKWKVGCKLAYEFFPKDLRKRLQKLETEDMNKSNRKLLQDATDEYAKFKDKFPEAPLDKDNLQTQKELEARIECLKQLAEKFDNPGPLYDVVVFHDGEHWRVVIDSDQTGDIYLHKPLADFNVAQEWSTFGSLDLLSYGVHVYDNGNITSIVAVSGTHGTHVAGIIGANHPETPELNGAAPGCQLVSLMIGDGRLDSLETSHAFSRACSEIIKNEVDIINISFGEDAGIPNKGRVIELLRDELAGKRNVVIVSSAGNNGPAYTTVGAPGGTTFDVISVGAYVTSGMMQAQYNLLSTVHDTPYTWCSRGPTLDGDTGVSIYAPGGAITSVPPYSLQNSQLMNGTSMSSPSACGGISLILSALKAQKKPYTAAAIKKAVMYTSKDLRDDFNTGMLQVDNAYEYLAQSDFQYTGARSFTINGNIGNSKRGVYLRNPTEVCSPSRHMFNVAPKFEDGEEYEKSHFEVQLSLATTQPWIQAPEYVMMAGTGRGIPVRVDPTALAPGHHFGKVLAYDASNESRRCVFEIPVTVMKPSSISNTCFSLRDVSFEPTLIKRHFLVPPKGATYVEIRVKATSELESTNMLWISVNQTIPQTKLNEASTELIMPVTQNEVTTKLVSIDDSYTLELCMAQWWSSLEPMVLDIDVNFHGIKVVNGKEINLISSQGLKRVDCASIRRENFKPDITLKDYVDSFKPTNTVIKPLGDRDIMPDGQQLFELMATYSVEISEKTELKADFAVPHNMYDNGFNGLFFMVFDSQKQRVHYGDMYTSSHTLEKGEYLYKFQLLSVDPSTLERFRNVTLRLTKKLKKPITLPLYADHIDFCDNKTYERENIDAGVVESFVVGTNIEGEQYASELKENSLLTGELKFGDCEKGTVPVTLVLPPKISTKEDTKLGEKCANIVQLQVDLLSKLADQEKEKHLKYLQSSYKNSLEVQLAKLDIVKETNERLSTADSILSLIDTEALSRYYSCQQKVEDTIPRDVVLEKKMALQRDAFIRALVVKCETFSTQGHKDKDNYFQNYQLLLNWLENSDPRVWQIKKDYYKSQNQYGLALKALLELLKENGNSGKMDVAKLLSEEKELLVNLGWNYWHDIVFVETVKRVPPYSYALF A0AAN2L350 A0AAN2L350_SCHPO MAIFEINNSFLICAVSIALNPLLWNIAARSEYNHKTLTKLANGDSKKACYMLAACIFVAGIVRDLIYQNALKQQPTLGIFMNPLVQGIAKLIFCFGSVLVLSSMYKLGLVGTYLGDYFGFLLPERVSGFPFNVNDNPMYNGSTLCFLSTALRYGKVAGLLLTLEVFFVYRIALKFEEPFTAKIYAARDSKQAKKSE A0AAN2L356 A0AAN2L356_SCHPO MSFSKFHCGKLMSLKLADLRTMFEALEK A0AAN2L357 A0AAN2L357_SCHPO MYSLKDLCIQVAQKHVHDIDDIGDCPFELVKPILEKARPEHLIDLEEKSPHLKVDTQPLWKDHVLRDFGLELQKRTILNNIDDWRGLYGKLKKKRNAHYNVASAKLRSAYTKLEQSKQNKRIVPLEREPRAARPPKRPRPMSNYCPKSSLMARAKSDFLKKASATRHIVSATSSSRSFPQLHPLGRSSSNATNTSTKRPLTSNTYPSIPLPPKSFTSQNFKSFNAVKTQPSSSSSPSISRPTSFPMSFFPNPSRFSSQVPKRI A0AAN2L366 A0AAN2L366_SCHPO MLHTINYRSWHLAARQLGRSTFRKFTTESSTKSPIADVCFAFDSIDGVLIRGGRGLKEGTKTLKFLQKNNIPFILLTNGGGMHESVRAQRLSKTLSVSLTEDDFCQSHTPFRALADKYKHVLVLGGKDNSVRETAEKYGFKSVINELDVIAKLGTPFWPFTSFNEEDIKDAKDFDVTRPIEAVFTYVDPVRLGLDLQLVMELGQSKNGVLGTVSKTANEGPDIYFSNADLIWPNEYPLPRLGQGAFAICCESVFKELTGKDLRNTKYGKPHKLTYDYAKNILMKKHKTLGITNPPKEIFMVGDNPESDIRGANNYGWTSILVRTGIFQGDNSPKYSAKHVSDNVWEGVRWALSKHVPAAKLNKSMGEVRGFHTSSRVLNTVTKSNNSKPIQRPLRENIFTLPNLLTFSRLLSAPLIAYLYIYDYTKAAACFFLYAGFTDLVDGYIARKFDLGSIAGTVLDPLADKTLMTCLTICLAVRETMPLTLASLIIGRDVLLVSAVSYLRYKSLPAPKTFRRFFDFAIPTTELKPTRISKWNTALQLLLLGLLITEPILPFDASFAKSPLFYIVGCTTIASGASYCISRNTFRNIGKSKLQ A0AAN2L372 A0AAN2L372_SCHPO MDYQNTETIAEQERNASRLPQMFQMSSHPVALFFFLLFRTGAIVAYILGMFFTSSFMLLFIVIFTLLAVDLWTVKNVSGRLLVGLRWRNETGVDGESIWIFESADPSRPRNAVDQKTFWYALYLYPFIWIILGIVAIIRFEFLWLALVAVAIGLTSVNTAAYSRCDKDAKRRWATELADSNSSGFVSRFLSRAFIKRFIG A0AAN2L375 A0AAN2L375_SCHPO MFDLDKNTNIESNHVKIGNKNTTRRLIIKSSKNSVRIAYAPPEKHFVDVTDRFLLPETETQNLKTRLGIFELEPLPPNGLVCCVLPNGELIQPNDFVLVNSPFPGEPFQIARIISFEKSRPCVSTNLYDSVRLNWYFRPRDIQRHLTDTRLLFASMHSDIYNIGSVQEKCTVKHRSQIENLDEYKSQAKSYYFDRLFDQNINKVFDVVPVTQVKNAPDDVLEDLFKNYDFIVTEYGKGRALLNEPSNCKVCKKWCAFDFSVQCADCKKYYHMDCVVPPLLKKPPHGFGWTCATCSFATQRKKSTFQKENANVDANHATENNLEGQATQKSVSILKGHNKALSNVSLQEDHGKRRNLKSLRSSRNLHQQSRKSLDENKPNSFSNVSKLKRLPWNMRYLDLKSDLTVEKKSDIYPSRARISISPMLPTSSEDNLHPLQPLTTADEEMDLDLKSDERFKVDIPTFFERWPFLKDLPLKGYLFPLCEPNLQSAMLLVPITYSDALLDDYLCSCWNLWKKLRLPVSAFVFLELTITALYETKLSPAAAFEKLKSWMPGFGDPKNCTGKRVDEHKINSLVKEFGVSLQCFVEKLKFEYSLKEIFFSFLSWASSPKGLNTFKKLSDSSLSTTTTDSHGLPTCCYDIGMYDLQKILKLKKTPICRWCHSKRSSEWFVAPPIEESSPKDKSKIVALCQRCGYVWRYYGYPLQQATPSDLRNCDFEPVKKRKADWDHLSNHDNEVKKENNRIRNASSLMENPRVSTKTFDNFTLTHDSTINVKADTVKRARQNNIKNKDDVNFSEDRKKCCALCGIVGTEGLLVCFKCGTCVHERCYVCDDYAENEQMLVSASHLSGRTTRNSASPGIVSGKKSYAKKDQVLSWACLSCRSNDNLGQNNDNHCVLCLQSASHSLMKKTVEGNWVHLICASWTPDVYVPAEESEPVCGIAQLPPNRWEKKCEVCGNSFGVCVSSPNSGLTSHVTCAEKANWYLGFEFVKQDQSPFSMLSNLKSLSFFGNVTEINTNKCMINSWTSLRPVLFGPSEQLPRNFLLRNDIVPNTNNSAWSEYIRNLYPKAYIYLLQYTIAVCKPTIAPTNVACCCSKCNSTMSPFWWPGNICQACHCLRVE A0AAN2L379 A0AAN2L379_SCHPO MRTTKKSSKKGIPLNLMVVGDVGLGRTAFINTLCEKPLIRHNNNFDPAEASSVSPVEIVPYQTDIILEDGTKINLTVLDTPHFGEAIDNENNFDIILQYIESQYDNVLEEESRIKRNARFCDDRVHALIYFISPTGHGLRELDIELMRRLAPRVNIIPAIAKADSLTAQELQTTKEMINADIEYYKIPVYDFPYDIEEDEEAIINLSQQLRATIPFAIVSSDRLIEMNGQTVRGRAYPWGVVEVDNPRHSDFLALRSALFATHIEDLHNITSNQLYETYRTEKLSTSQLLLDSTVGLDGKNLSQHDQVLREDRLRAIELSVQKEIEEKRRQLLAREEALRALEEKLAASTAAMANASVSTLPSSVSSTNHSQS A0AAN2L382 A0AAN2L382_SCHPO MFGQNNSSGFGGGTGAFGQNNQQTGGLFGSNSNTPGNTLFGSQNTSTTGFGQNTTQPLFGSNTNGGLFGNRNNTTTTGGTGFGMSSGTGMFGQSNTPAFGGTNNATNPSGGGLFGSNTANNNANTGTSFSFGSNAGSTGFGNTASNTGTGGGLFGSQNNAGNTAGNTGFGSQGTGGGLFGSSTTPATTNAFGTSGFVSSNANAVNGTANPPYAVTSEKDPQTNGTSVFQSITCMPAYRSYSFEELRLQDYNQGRRFGNASSTNTTSAFGSTPAFGASTTPFGQNLSGTTNNATPFGTSNATNTTPGSGLFGGGSAFGSNTTNTGFGSGTNNASGGLFGQNNNTTSTPSTGLFGGSTFNQQKPAFSGFGSTTNTTNTGTGTGLFGSNNATNTGTGQTTGGLFGGAATGTGTGFGSSTGGFGSNTNNQPNSGTMGTGLFGFGANNNTANNNTAPTSTFGGNNSSNFSFGANNNAATKPSGFGFGSTTTTPASGGFSFGQNANNAPKPAFGSTATTAPKPAGTGLFGGLGAGANTNTATNATGTGGSLFGNANTAGSNMFGSANSSTPGTGLFGSTQTNNATSNTGTGLFGSNNANTTNTGGSLFNKPSTTTGGLFGNTTAQQPSTTTSGLFGASNTNNQAQTSNFGTGLFGGSQAGQQQQPLQASIDQNPYGNNPLFSSTTSQVAPTSIQEPIASPLTSKPTPKKAASLPQFWLSPRSHNTARLASISSFAKSAVMNSTSASGKPKSLHLFDSLNDDVLLSADAFTPRQNIKKLVITHKISKDDILQNGVKNGNDAKSDSKVQEKAPQNEADGSLKKDEHVVLSDDYWMKPSIEELSKYPKEKLCSVHQFSVGRTGYGQVAFLKPVDLSGFEKLEDIPGKVVVFERKICAVYPVEGSSPPLGEGLNVPAIITLEKTWPLSRETREPIKDPQNPRYIQHVKRLHRIKDTEFIDFNDGKWIFKVQHFSRYGLLDDEEEENDMSSTSNEAGNLKKYDQPNLKVSGKNDSFVTHHTPGAFPNDSKNKELNRHFLKVDDSAPLDDTFMSKKVKLDFSSDSNVSERGDYDDNAKKVDEVISIEKVDGYSKENNVPLSEDDLSNSSESSNESVYSLVEESDASLAADNMDIEDISEESDREELSSMRFGAQDFHGLVVTDNWRDQLNLSVQRSALIKAAFPESQSNANLKNSRGIYYNEHDLVTDIFGNQNLDTDRPWQSLDKPGAFIPSKFHFTANGSCIYVLKSSDVKIRSIYDFIPTKDPNGTKLLEYQLDQTEVYLDLSGTHAASPRSSMTVKPLSLCSSGYESIVWDLTSILFDPKNYSLPSELSSEAREVLYQKLVRESLSEWITKTLEHETTTLAKEAETSEERIYILLTGNLIGQACEEAVQSQNNRLSTLIPLVNSDVDIQQEVKQQLEEWRKHGDLPFINKFTRLIFELLSGNTDIAEGCGTKGDEDYVQSIPITKNMTWLRAFGLKLWYNTDISIGEAMQLYVESLQKFPEIMQKPIATSAVQGIEVYDIIYLLLKAYAMGTSLEELTIPESAKCSPLNYRVVWQLAIYLSKARSLCDFSDRVVDINMAEDLKPISVHSDQLTLAYASQLEASGQWLWSLFVLLHLENVETRTSTITSCLARNLRGGLGAGAVEMIEKLCIPESWLNEAKALYARYVGDHLNELYFLQEAALYEDAHKVLLDTLAPQAVISGNKTQLKKALEGFNGQTDGLASWRFGGQIYSDYLDLLEGNFDANQELKLFTLRKISVALKELNATNLLQKAALHKISRFVNALCNEESLTDAICNLPLPLADSLANLQNISVQF A0AAN2L384 A0AAN2L384_SCHPO MKAAVRSVKNFSKGYTDTQIKVRNATTNDSWGPSGTAMAEIAELTYDQNEMLEVMDIIDRRLNDKGKNWRHVFKSLSLLEYCLHNGSENVVRWAKDNIYIITTLREFVYVDDNGHDQGQNVRTKAKEITSLLEDEHALKEARGDSRERDRDRDRTRSSRFDDDDDDRAPYEESRLSRAPSRASRYDDDDRDHRSRRRSRSRRPGRSRSRRRSRRPSPSAEHNSAEENDPELQRVIEESKRQAEEDAKRRNMANDSEAELQKAIQLSKEEDEARQRHQREREQQEQAFMGNQQNAYQPVDFFGNPVQPQPTGFLQQQPTGFIRPQNTGFVQPQYTGFVQPQHTGFVQPQATGFMQPQRTGFVQPQATGFVQPQATGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFIQPQRTGFVQPQQNGFFNPQPTGYMQPQRTGMMQPQRTGFSQPFESNNPFPVMQPQRTGFGQTPNAPMMAPNHTGYVHPQPTGLQRQTTGYTGNNNPYSRPLQSQSTGILQQQQQQSAPRLEPTKTGSNNPFAQFSNLPSQSTAPATKPMKPVRTGDDRFSNIAQAISTGNPMGTDSFGNIGLTRVPTQHTGSKFTNSAGQTIQAQATGNTHNPFQSQQATGYYKQPMQQQQNMQQPYYNQQNYNYQNQQPMQGMQQQSMQPQVGSLIDL A0AAN2L388 A0AAN2L388_SCHPO MGELQDGITQEDSIEKKSKNVASHGEKRKVKRKKEDLSMDGSNDGVKDSPDSNDDSQSKKKKKKKLKKSQQPLNEENYPRLQTTENNLQKPLKISDLQELVFWCLADGQAPSWVLVRNKQMIHRAVILLVPGLEPSQFGFQPVRGNKHSFLLPNLLNENGPIQLPDFCEVFDRAWPTRSPGDRFRVFSPVNAFLQSPLSNEQKKKRDKETRAMASFSKPSDYLMSYESFIEDEYPLHPTVMKGEEVTQPSGWVASAGDFHSPPINPKILAIDCEMVRTENGLEIARVTIVDMKSEVIYDEFVKPESPVTDYVTQYSGITEEKLRNVTTVLSDVQSYLKKTVDNNTVLLGHSLNSDLNCLKFTHPHIIDTANIYNHTRGPPSKPSLKWLATKWLRREIQKAGALGHDSAEDALACVDLLKLKVKNGPAFGLFNQDFESIFHRLSRQQPTPLIGAIADYGNPESCIGKAAHKSVSCANDDEVVSAVVSLSDMHNFVWGRFRELEHAAMWNANRNTKQENNSDTDTENDSVEEDQVTSYSSALERFNRRIRLLYDSLPKGSLLLLYTGTGNPIEMSKLNAIRQQFRKEYQTKKWDELSVKWTDEENMKYISAVENTRNGLSFMTIK A0AAN2L394 A0AAN2L394_SCHPO MSGGWDESKYVDNGEDEVVRQVSEPSVEEPIEASVTRYRSDEEKLDDKSSGAHVTEKEAEFDIEGGSRETSQWKHFLNVAVAGVALMSDGYCSNSIGTVITILRKLYPEETTHNKSLQDIGMIAYVGTIVGQLSFGWYSDRFGRKNGMITATIILIVSTALCTGAYGYKGSINGMLSALIAYRFFLGIGIGAEYPCGSVAASESSNELKSGLRHAAFIVVTDGAIDFGFVVGALVPYILVCIFGEHHLRIVWRLSIGLGLVIPCVLLPFRIAMKDPKTYVKHKVPLTKIPWLLVLKMYGFRLFILCLIWFVYDLSAFAFGLYSSTIVDGVLPADASTARSFGWNVLINTFYLPGALLGGVFSDLLGPKYCLITGLVLQSIFGFFMSGFYNQLVHKIAGFCVIYGIFLTLGEFGPGGNIGLLASKTSPTAIRGVYYGIAAAIGKCGAIAGVYAFGGDQVRNYFYAASAMAIFVAVLALLFVPKLKQTCIEDEDKRFIQACIDAGYGNPYNYEKNEPEQLEEPDRPPAFK A0AAN2L3A6 A0AAN2L3A6_SCHPO MADSPRDPFQSRSQLPRFLATSVKKPNLKKPSVNSANETKNPKLASLEFQLENLKNDLKRKELEFEREQIELQRKLAEEHEQKNSLQLRLTLVEKQLEEQSTSYQKEIEEVRNEKEATQVKIHELLDAKWKEIAELKTQIEKNDQALSEKNHEVMVSNQALQMKDTNLTNLEKLFADSREQLETKCKELAAAEQQLQELSVHNQQLEESIKQVSSSIELEKINAEQRLQISELEKLKAAQEERIEKLSSNNRNVEILKEEKNDLESKLYRFEEYRDKVATLELENEKIQTELNSWKSLITNELPTPEAVSNKLVFLQNTNANLGERVSSLESQLSNKPANQPLGANEKDAAHITELETKLKELHEQNRRLQRQKSLATQEIDLLRENLKSYDDEEAILSEKNTDMKKLERIEGLVKLVDEYKLKLESMPVSLDVDETSDEVSLQKRRRKNEHKDAGYVTELYRKNQHLLFQVKEKTNIEAFLREQIITLESSIATLRQELAQVTEINSCRVLQHRSNPTLKYERIKAAQLEMLNAENSALKALLEDKKVDCLPIQSFKIAERKALDLKKEVAEREKRIQRLKEIFSVKSLEFREAVFSLFGYKLDFMPNGSVRVTSTYSREDNTAFIFDGESSTMKLVGNPSGPEFERLIRFWCDERKTIPGMLAALTLELLDKND A0AAN2L3B7 A0AAN2L3B7_SCHPO MFFAFLITYLLGGVTFLPFILFIYLLTRPTHKSEELRIIEPNNDCLTKLDKDIRIQGWIRVTTKFLQGKSGSVKVQEIPQDQLPKSSSDNAVTDRKTISPSGINNQYVIRNPKDVYYATVQAGKLHLFDPVKTSELLHVINLHEYLVVFYPGTVTENELFSNRNAIFLKYPAVSHKKESSTKSLLNKDLYVYGRTPSNKEDWNYALLSYSKISPAIKPLEAPIDFDYASVHHNLTALSSPDTDWLNAFIGRIFLGIHKTEGFKSLVVEKLTKKLSRIKTPGIMTDVKVIDVDVGEAIPTVNGLKFESLSNGGELIVSADIWYEGDCSFKAETTANIKFGSHFPSKTVPLALVIRLTHVSGKVRLLIKPPPSNRVWYAFYEKPRLHLIVEPMVARKQLTNNYLINFITQKLVELVHETIVMPNMNDLAFFIDNEAPIKGGLWDIELFRAPTIQKPAEKDAKAERKKSGLSSSTSEESLNRHISKRSSNSNDTAPSSHIIADKNLEPTSNIQLKKNPDGNLVETSELSDSDENSVLSNKSSTLSKKVVENTSPLKYTHSASKSFIGEVQDSLQALKTKAHKPRSIGGDSSQTTLSETTKKYGSVAKKSFFQGVSDAKSFVKKIKSTYIDDSSSNSPSDIESNYSADDNEISKSKAQNAIDFNVTNTHSPSRSISSEKSYKAAERGQQDKHNDVLVDLNPNVEAEKSNPHSNSQKTSKNDMSRNQRNKYAKEIMTGQPTLHPQGQLPIQNVEQRATHKPLPRPPVQVETREPVRPVPPIPKL A0AAN2L3C8 A0AAN2L3C8_SCHPO MSASKIAFLGPRGTFSHQAALLARPDSLLCSLPSFAGKLIFALKFILICFLAVLEALSSRQVDYAVLPIENSTNGAVIPAYDLLKGRDDIQAVGEVLVPAHHCIIGKSLENVQKILSHPQAFGQCSKWISANVPNAEFVSVSSTSQAAALASKDITGTIVAISSELCAVENQFNLLVKNIEDDSNNRTRFLLLRSGGFQDDLSPLKEKSLLQFYLSHPKKLSAVFEVFAAHKVVITNLVVRPSCKFPWTYIYFVECLGMEKHLIDRVGKYCDTFTFMGSYTNQISYF A0AAN2L3D8 A0AAN2L3D8_SCHPO MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIVIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV A0AAN2L3F0 A0AAN2L3F0_SCHPO MLSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV A0AAN2L3T9 A0AAN2L3T9_SCHPO MPVSAFYIPSFNLFGKGCLAEAAKQIKMSGFKNTLIVTDPGIIKVGLYDKVKALLEEQSITVHLYDGVQPNPTVGNVNQGLEIVKKENCDSMVSIGGGSAHDCAKGIALLATNGGKIADYEGVDKSSKPQLPLIAINTTAGTASEMTRFAIITEETRHIKMAIIDKHTMPILSVNDPETMYGLPPSLTAATGMDALTHAVEAYVSTAANPITDACAVKCIELVNKYLKRAVDNGKDEEARDNMAYAEFLGGMAFNNASLGYVHAMAHQLGGFYGIPHGVCNAVLLAHVQKFNSRDPRANARLGDIAFHLGCEEHTAEAALDRISQLVLEVKIRPHLVDLGVKEKDFDVLVDHAMKDACGATNPIQPTHDEVKAIFKSAM A0AAN2L3V1 A0AAN2L3V1_SCHPO MLHTINYRSWHLAARQLGRSTFRKFTTESSTKSPIADVCFAFDSIDGVLIRGGRGLKEGTKTLKFLQKNNIPFILLTNGGGMHESVRAQRLSKTLSVSLTEDDFCQSHTPFRALADKYKHVLVLGGKDNSVRETAEKYGFKSVINELDVIAKLGTPFWPFTSFNEEDIKDAKDFDVTRPIEAVFTYVDPVRLGLDLQLVMELGQSKNGVLGTVSKTANEGPDIYFSNADLIWPNEYPLPRLGQGAFAICCESVFKELTGKDLRNTKYGKPHKLTYDYAKNILMKKHKTLGITNPPKEIFMVGDNPESDIRGANNYGWTSILVRTGIFQGDNSPKYSAKHVSDNVWEGVRWALSKHVPAAKLNKSMGEVRGFHTSSRVLNTVTKSSFQLH A0AAN2L3W2 A0AAN2L3W2_SCHPO MDDLLNSVSFSNASNPHNAWGSENISNSNSAIPSITNDVSFSMEASVWKENALNLDTFNLKDINEKLDYTFGVVKPPKRISLASKDYIGITATSETNFRQLIRLGYNEKSLGELKQGTISRLLKEHMTLWNQERSNVNRKSNVLFCWSTAYQKQKRKTASYTNSPVTPPINDKNILLPEQSPLSNFSTTKISSINVPSDILDFSNLSSNEIPKDYSSSTALLNNTVAVKQDHKLSANTFLSSPVKLIERESNSCSTISINKEDEVVPKSPLSLDRKKVDEVEEHSSIAKLDSEEKIRETKKKNSSTSLSPDPTSDNFEWGSWVSSQDTSKNSSNLASASVDDNFSSPSTSLSAPKDTPAVIQSINTSFLNNERAGRGNIKTVDQNQLINRIVDKLPDLSYLVD A0AAN2L3X1 A0AAN2L3X1_SCHPO MKFGESLQLALIPEFAEQYVDYNGIKRKIQLVAALPEDERKKLLRRNSDGSWPKGSIDEMLENDLQKVVNLFNTRIVQLDNYVTRLSTEKSPNTEITQALSSSYEAEEKAKQLKELDFRLQQLSSFCEWNKLAFEKLAANMDKHLGTERLVTFYEQKVCKLDFANSSKIYESMIALKALNSSQNDSEVKDKLEKLSIHHPLKKDLLAFIQLDIAAEVVTACINAPDSVLVDILAASIIAGAKACMREVIGRIGLRSECLASALRRAINNLCGPDEGVLYFLEVLKQICSVVYVDSYHSNRLLSRILLVERNSKGQSVMHSVAKLGWAGLCSKFCEIVSSIPDSEPLNWMLPCWRDVMHDTPLTLAIKGNHVEALHALLSAQDKETTSTKPGPVPPLVLTCCVGDYDLIVEELILAGFNPNEVDASSNTALHTAVRYNRPECVKMLLKLGANPSARDFLNSWTPLMLASATGLSEIVSILVASGASVDEVDSSGWTAMEQAVVRGYLHLADKLRTQVALSDKPVNLHTLYIKASSSEMRSRKRAMDLQLSRSVVIIRISDLAGRIRVSLQGDDAVYVSGRSPSFAASRPSSVDFMSQSTDSLSKNDTTASNGSMTPSSSQNNSVIIDIPRSHFDNAGEVCLENLAEPDEIADDSIHLHYDAAQENSPQPVNGSSPPYELVFVTRNTEEATITIDLLANRSHKILGRTVCCLTSLVSDLGNHMQSLKPLAPLPLLSSKTLKPIAHVNADVLISKVTVDDRFSSNDGISTPALSLEAVSNVSRTALEDAERSLHKSATTTSESGKSNGVAVIGHRGLGKNQPDRLSLQLGENTLQSFIKAADLGASYVELDVQMTKDMVPVVYHDFIVNETGTDAQVHSLTLEQFLGASHSPSEEIKDDASDIQQKRRPRAYSSSFTPSGSQVNFGEFAEENARLKPKVYKGNALGHTICAPFTTLKDVLKEVPQSVGLNVEFKYPMLSEAEEEKLLPIAYDYNFYVDTILSIIKKYGGKRKYIFSSFNPDICILLSLKSTNPVLFLTEGGTAYRTDVRAASLRQALKFASQWSFLGIVSACEPLIMCPRLIKAVKQLGLSCYTYGVLNNDVDNVRRQVRFGVDAVIVDNVLAIRRALNQYDESLESD A0AAN2L3Y4 A0AAN2L3Y4_SCHPO MSFFEALGAGICAGLAVDLSLFPIDTLKTRLQAKGGFVKNGGFHGVYRGLGSILVGSAPGASLFFTTYENMKSRLSQSGLGLSDPQIHMCSASLGEIAACIVRVPTEVIKQRAQASGGTLSSRNILQTILKSNNVWRDFYAGYGITIAREIPFTLIQFPIWEHLKLKWRIKHSRNKNLAHEAAISGSIAGGIAAALTTPFDVVKTRIMTSQQRLSYVFTIKSIVAHEGFLALYKGIVPRVLWLSGGGAIFLGCYDVILNFMKAEGL A0AAN2L3Z3 A0AAN2L3Z3_SCHPO MLAAESSNKELFIKNDGKALSFPYDWKLATHVICDDFSSPNVQEGSKRSLRLAKTNWIRDCVDKNTLLNYSFYSCNPYLLFKGICASSCQIDSYQSSLIDDALETFGGRFSKGLMKSMTHLFTYSGMGAKCKKVLDKPSLSIKLIHPQWLLDCLQFGQLIDQDPYLFPNPSYKKNDSSISKAEPTSLFRNVLHGKRIYFSNDLNLPTNFRHSLQKFSVGIGAKIAESINDCDIFIGLKRDTIEFNLASNKNTTIGTISWLLNLFVLGSWKSPLLNALHYPFPSVGFLKDQMVAVTNYTDAARIYLEKLLLACGATYTKDLKPTNTLLIAASSYGQKYGAAKVWNIPTVHHSWLYSSFKNLSSQAFTDFPVPLDDSYMDFIFPCPLNVEKGSFEDTLKSSLTKGNSEVLLDDLSDPSVSSIKGNKTNEELEKEFKSTSDNFGKHIILTSSFSNQSADKGSSLAAEDDRNDEGSTITGVNRELQDEGRLEIDAKSSKTNTPPSPLLVGTPSKESLKEASSDDELPVLATKLVDNVIKEKSPLSLTPKVVVPSHKETYTDEKKLIDELDRVNPLNSSQLLRSKRKSAATALSMLQNVIMPDVLAFEREKKRRQTHRSVSSGEVSRESSESRNTNAKASKRVYITFTGYDKKPSIDNLKKLDMSITSNPSKCTHLIAPRILRTSKFLCSIPYGPCVVTMDWINSCLKTHEIVDEEPYLLNDPEKELELGCTLESALKRARAQGPSLLEDYVVYLTSKTVAPENVPAVISIVKSNGGVCSTLNVYNKRLARHLEDGNVVLITCNEDSHIWTNFLDNASQNKTIFLQNYDWLIKTVLRQEIDVNDRIADEFARAV A0AAN2L411 A0AAN2L411_SCHPO MNQKTPSTVEEIRIALQELGLSTNGNKEKLKRRWKFREKRLEEKRKQERYQKFSTSNENKTCLRYLLIVDVEATCEEGCGFSFENEIIELPCLLFDLIEKSIIDEFHSYVRPSMNPTLSDYCKSLTGIQQCTVDKAPIFSDVLEELFIFLRKHSNILVPSVDEIEIIEPLKSVPRTQPKNWAWACDGPWDMASFLAKQFKYDKMPIPDWIKGPFVDIRSFYKDVYRVPRTNINGMLEHWGLQFEGSEHRGIDDARNLSRIVKKMCSENVEFECNRWWMEYEKNGWIPNRSYPPYFAS A0AAN2L421 A0AAN2L421_SCHPO MFSYGKENAFPVTPISNRNGTKGAGSKRAPLGSTKQSNAPSSVTVPRTVLGGKSTNISKFISAPSTKKMSPMDISMDSPTILEPNSQGISRSAVQERSKRLSASPRRSSLTDTPLPNELEEDIEYMPPPVHLDPIQSLGFDDVAIDCETLDPWPSMQNKATSVTIRNTPASDFHVYKEFSDDDPIQFPLLSVDGDSPLTEKDTNLTTPATLKASDQQRKVLEKPSVSKQSSSRTRLSTVYRTKLASGKSIPRPLSHKLTRPRVTASGNSRRRPLSRSIHSLSSSRIDFSSLDTGLL A0AAN2L432 A0AAN2L432_SCHPO MEFLSTIIGAGYPIYKTYLLLELPSKRSQLLPKAFQLRNEEHKSIEEERRRLMAYWCVYGCVTAAESILGRFLSWVPFYSTSKIVFWLWLLNPRTQGAAFIYASYISPFLSDHKAAINNFLEKLVQFTTRQPLVLNAWALVKSLIDKLPKGDVEAPGSDADTKKSK A0AAN2L444 A0AAN2L444_SCHPO MLSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIVIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV A0AAN2L457 A0AAN2L457_SCHPO MLPHTAFSNHIHYHFINEAPFRLCIYTLFHAHTCFSCGLSLSLMEVIMDISQLLIS A0AAN2L580 A0AAN2L580_SCHPO MTKDAESTMTVGTYLAQRLVEIGIKNHFVVPGDYNLRLLDFLEYYPGLSEIGCCNELNCAFAAEGYARSNGIACAVVTYSVGALTAFDGIGGAYAENLPVILVSGSPNTNDLSSGHLLHHTLGTHDFEYQMEIAKKLTCAAVAIKRAEDAPVMIDHAIRQAILQHKPVYIEIPTNMANQPCPVPGPISAVISPEISDKESLEKATDIAAELISKKEKPILLAGPKLRAAGAESAFVKLAEALNCAAFIMPAAKGFYSEEHKNYAGVYWGEVSSSETTKAVYESSDLVIGAGVLFNDYSTVGWRAAPNPNILLNSDYTSVSIPGYVFSRVYMAEFLELLAKKVSKKPATLEAYNKARPQTVVPKAAEPKAALNRVEVMRQIQGLVDSNTTLYAETGDSWFNGLQMKLPAGAKFEVEMQWGHIGWSVPSAMGYAVAAPERRTIVMVGDGSFQLTGQEISQMIRHKLPVLIFLLNNRGYTIEIQIHDGPYNRIQNWDFAAFCESLNGETGKAKGLHAKTGEELTSAIKVALQNKEGPTLIECAIDTDDCTQELVDWGKAVASANARPPTADN A0AAN2L592 A0AAN2L592_SCHPO MIIKPIASPARYFLRTPSWSAVAIFQAVKIKPLQLRTNSSNSVTPNLISPSKKSWKDLFSKRWQYYAEISRAGSPTGTYLLYSPCTWSILMAAYAYDSSLVNVTKMLALFGVGSFLMRSAGCVINDLWDRELDAKVERSKSRPLASGKLSVRQAISLLSVQLTASLGILLQLNPYTIKLGVASLVPVCIYPAMKRITYYPQVVLGLTFGYGAVMGWPALAGEACMNWSVVAPLYLSTISWIVLYDTIYAHQDKRDDVKANIYSTALRFGDNTKPVLCGLAALQIATLATAGIMNGQGPVFYTLGVAGAAYRLSSMIYKVDLDDPKDCFRWFKRNSNTGYLVAAAIALDWLAKSFIYDS A0AAN2L5A4 A0AAN2L5A4_SCHPO MGILQHLMHILDIPGFPWKIVIAGFSIGKYAWDLYLRRRQVPYLLREKPPAILAEHVDEKKYQKALSYARDKSWFSTIVSTFTLAVDLLIIKYDGLSYLWNITKFPWMDKLAASSSRFSLSTSITHSCVFMFGLTLFSRLIQIPFNLYSTFVIEEKYGFNKSTLKIFVIDLLKELSLGGLLMSVVVGVFVKILTKFGDNFIMYAWGAYIVFGLILQTIAPSLIMPLFYKFTPLENGSLRTQIEELAASINFPLKKLYVIDASRRSTHSNAFFYGLPWNKGIVLFDTLVKNHTEPELIAILGHELGHWYMSHNLINTIIDYGMSLFHLFLFAAFIRNNSLYTSFNFITEKPVIVGLLLFSDALGPLSSILTFASNKVSRLCEYQADAFAKQLGYAKDLGDGLIRIHDDNLSPLEFDSLYTSYYHSHPILVDRLNAIDYTTLKKNN A0AAN2L5B7 A0AAN2L5B7_SCHPO MLSNSEIKPSENSQKTKVLLTKANNASNERAPPPLSHFIAGGVAGMLGAIATAPLDVVKTRLQSDFYKDRFLKQTAKSKSPLTAAYRHFMDTCIILKNVKVHEGTRALFRGLGPNLIGTIPARSINFFSYGNGKRILADLFNNGQENSQIHLMAAAIAGVITSAATNPIWLVKTRLQLDKKSGQAAQYRSSIDCIIKTIRLEGFRGLYKGLSASLLGVGESTLQWVLYEKFKHAVAIRQLRRKELGIQETIYDKVLDWGGKLGGAGIAKFMAAGIAYPHEVVRTRLRQSPSINGTPKYTGLIQCFKLVWMEQGIVGLYGGLTAHLLRVVPNACILFGSYEVIMHFIG A0AAN2L5C9 A0AAN2L5C9_SCHPO MTSRKEQLDAFLSRTLSETIAHIPLEKFAQCFPSMKKGKVIAVIHQQLIEFFEKSCKQEYANLIKERDLNKKLDMLDECIHDAEFRKLHGESEVDISNKQPQEILKAHLYSHKRELLDKLNQDLLDIDKENEGLSTQIAGEEKATEDCISRMQSLIQKLEKTVYGMNEKNLAKEAHDTLNDLLPYIQNPSSTWTNALNEQGNIER A0AAN2L5E0 A0AAN2L5E0_SCHPO MSNEESFTEKPLKKRSRAHRLGDPRFYCTYPDCPKSFTRKEHLRRHERTHENVKAFSCSFCNRAFARSDVLNRHVQQMHLQKQNLSERLPPPQFFHSEAGERPTPSVGAPSSLASSMDSVRVAPSMLAASHQIVPQYSENNPRVSNEPPRVTIENASLKPFSGYIKSHMSTSNFLNGEPDLNVNVDLSPFPNLPATVPITQAASTANAFQQPSNQFQTQKLPSGLDTRPVSSYPDELTQLESNPDSFSRLDLQGDCTCIFKNRSSIASSRTMDDVVRWLFSSGKRRQKYESSYPYQTQSNQIPSQDQYSDTDSNFLSYYFSASGPMYVPQKCPATVYNNLLNFLEGSFHLQPNFLAMFTLESVSSWLNAYWSMFHVRWPILHRGTFQITQAPLDLLLSMITLGMHSSNDLSIRSLAVEIHTTLRYNIYQKQEFGPPVSLWVYQALFLIQVFELFTSNLKQHRLAQMFHPVLIEAMRQAIPSDALTVRSETFGESNTPLTLQQWHKWITRESVKRIAFFVFALDSTSTLVFGNQPLLYVTDVSMPLLAEEHHWEAENFEVWAAQKPTIEPPTILHMLKAFVQCEQCESPLPKLSPWNMLLLLHGLLSVDISLKQKKFVPGMKLSKREIDGWCSLVFEAYQKWNRCYYSIFLNNNILPFGHPFVKECRSLYNLACIYSKTRLTYLQAFAKAVTDPVDGSVTSKTVAPLRYVKIWANTENARYSTSNALEILDMLLREKIESAPRYDTLIYHSWCYYVAALVLWSIGFALDEENKKTEEVTNLHSQMSRYVTKVRQALEQGEPLFAVVEKSKNPIILHVVLQALDVFPWDLLGEHKKIIQQLLSKGND A0AAN2L5F2 A0AAN2L5F2_SCHPO MNPQTKTFEGAINRLNSLQSNAKVLEVLRKRGKIPNDQSMVEMRHWLRCIGYQPSDLNRLNVIHVAGTKGKGSTCAFTSSILQQIQKSGERSIPKCIGMYTSPHLRSVCERIQLNGKPISQELFTKYFFDVWERLENAVGSDSEKPMYFRFLTLMAWHVFISENVDAAIIEVGIGGEYDSTNLIEKPYATAVTSLGLDHTSLLGNTIAEIAWQKAGIYKESAIALTCEQAPEAMNVLKNRAAERNTSLKVVIPPAELTPDMIGLSGVHQLGNTSLAVSLVQEFYEKAGCPFDRDPYQDPAILDGLKYVKWPGRCQIEEINNIKWCFDGAHTKESLEATGLWLASKKNLYEDADARILLFNQQSRDDPIALLRSFLKGLESSGTGISFTHVIFSTNVTWKDAGYNPELLSINTITDNKPVLHVQEDLCKWWKESKGTTSEATVAPTIQEAIETVMSIKQKSRNTFVCVTGSLHLTGGVFVVLDQAVF A0AAN2L5G4 A0AAN2L5G4_SCHPO MLSEYQCLKNIGFSHKTVLKRRLFRKECTPALKSFYSTQDPALNEVRTEKLKNGVTYVCDPRPGHFSGLGVYVKAGSRYETKKFSGVSHFMDRLAFQATERTPVGEMKAKLENLGGNYMCSTSRESMIYQAAVFNDDVKSMSKLLAETVLAPKIQEDDLVHYRDSIIYENSELWTKPDALLGEFAHVTAFQNNTLGNCLLCTPDKVNGITATSIREYLKYFYRPEHLTLAYAGIPQEIAKEITKELYGHLPSSSLPPLEAIPSHYTGGFMGIKKSEAPPVPYQQEFTHVVIAMEGLPVTDPDIYALACLQFLLGGGGSFSAGGPGKGMYSRLYLNVLNQYPWVETCMAFNHSYTDSGLFGMFVTILDDAAHLAAPLIIRELCNTVLSVTSEETERAKNQLKSSLLMNLESRMISLEDLGRQIQTQNGLYITPKEMIEKIDALTPSDLSRVARRVLTGNVSNPGNGTGKPTVLIHGNVDEVGDVFALCKKAGIGH A0AAN2L5H4 A0AAN2L5H4_SCHPO MEKEDKSFGIGMLDYNRENPESSGHSRVAVIRKQKTEQENNNLSWEDRHYIPDLHKSNKIKTPTSLADEKKSHNELDPKAQIKKLMETRSGGTYIPPAKLKALQAQLTDVNTPEYQRMQWEALKKSINGLINKVNKSNIRDIIPELFQENIIRGRALYCRSIMKAQAASLPFTPIYAAMTAVINTKFPQIGELLLTRLIVQFRKSFQRNDKSMCISSSSFIAHLINQKIAHEIVGLQILAVLLERPTNDSIEIAVMLLREIGAYLAEVSTRAYNGVFERFRTILHEGQLERRTQFIIEVLFQTRKDKFKNNPTIPQELDLVEEEDQITHYISLDDNLDVQESLGIFHYDPDYEENEKKYDAIKHEILGEEDDDENEEDEEDSEETSESEEDESVNDEKPQVIDQTNASLVNLRKSIYLTIMSSVDFEECCHKLLKIDLPEGQEIELCNMVIECNSQERTYAKFYGLIGERFCKLSRTWRSTYEQCFKNYYETIHRYETNRLRNIALFFANLLSTDSIGWEVYDCVRLTEDDTTASSRIFLKIMFQEIVEALGLKSLVERLHDPNLVPYLHGLFPVDEARNVRFSINYFTSIGLGALTEEMREYLLTMPKSEPKEQDSEGYSSGSETGSTYSSSYSSTYSRGRSYSRSTRSYSKSRSYSRSRSVTPINNINHKKYIRKDRELSPRGRERSSNRNSYSDLSRSSSLSRGRSRSYTPEGRLIESEDKGYRSRSSSPASRKYRSRQRYRRSYAGSTSRGRSFSRSPSYRRRLSMSCSVSYSRSPSPAARPISRSPARNKRSYDSLSYNRQYSPKVSRKRSNESRSPSPYTLRKQKTYHLNKRNEDFVVKMDKKGSESPVILAPWLREVDDGELYKDRNSESDSVRKQPRAD A0AAN2L5I6 A0AAN2L5I6_SCHPO MIRFCPSCFALKRTAPVLNHTSRLGNYFNNTFSKFSVNRMSVSSYSSDASSTVMDESPPNGVTKSVSGKGPTAVVMMNMGGPSNLDEVGPFLERLFTDGDIIPLGYFQNSLGKFIAKRRTPKVQNHYSDIGGGSPILHWTRIQGSEMCKILDKKCPESAPHLPFVAFRYAPPLTEDMLDELKKANVSRAVAFSQYPQWSCATSGASLNELRRKLIEKGMEKDFEWSIVDRWPLQQGLINAFAENIEETLKTYPEDVRDDVVIVFSAHSLPMSQVAKGDPYVYEIAATSQAVMKRLNYKNKFVNAWQSKVGPLPWMSPATDFVIEQLGNRGQKNMILVPIAFTSDHIETLKELEDYIEDAKQKGITGVKRVSSINGSMTAIQGMADLVAEHLKAKVPYSRQFTQRCPGCTSESCAERINFFQDF A0AAN2L5J7 A0AAN2L5J7_SCHPO MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV A6X969 YI9B_SCHPO SPAC806.11; CHAIN 1..72; /note="Putative uncharacterized protein C806.11"; /id="PRO_0000303983" MLCPTHGPTTWNPHSCTVVEKCITNLLITTILLCFFNATTYWKLFFGAMFDFIHYQLLFRNSLSEILLLGLG A6X970 YF64_SCHPO SPAC23C4.04c; CHAIN 1..140; /note="Putative uncharacterized protein C23C4.04c"; /id="PRO_0000303982" MFCYFLSKSYDDCSRYYIISNMAFYFPVYDSDSPTTVHHDERKESWRSHGFIVCLHIRCCICCKYNSKIKKPSLNIALRIQSLKIIKILIFQFYSTKPLWDKNSPEYKQLRSEIEATKRDEEVKNGELIDPNVTTEDEKL A6X974 YFQ8_SCHPO SPAC8E11.08c; CHAIN 1..100; /note="Putative uncharacterized protein C8E11.08c"; /id="PRO_0000303986" MDFTTNEVLFSRLVVCKNLTRKNFPFLQLKGSSILRFEWSEEMYRLYIWLLPYRKDYNEKFKGILINPSIFLLGCHHVQICSFPNNLVFFMGKCDLFRFC A6X978 YF12_SCHPO SPAC9E9.02; CHAIN 1..98; /note="Putative uncharacterized protein C9E9.02"; /id="PRO_0000303988" MDVDFANAKHKLHCLLKKNFLLTIRFSSLVSIQYIPFSNRLYEIISIALNPCNFSKSLFWLRKKIKNSVLLKTSFDSNETIFFLYSLHRCVYYLFIYL A6X992 YCGL_SCHPO SPCC16C4.21; CHAIN 1..81; /note="Putative uncharacterized protein C16C4.21"; /id="PRO_0000303989" MQLYPANVKGLRYSECCILTANPSVQHFVMHDDAGVPLTYSVSTLHAELTDHLYLPTTRKTVAVGKKTLFVVQKKRFKPET A6X993 YJZ3_SCHPO SPCC338.03c; CHAIN 1..141; /note="Putative uncharacterized protein C338.03c"; /id="PRO_0000303990" MVISSVFSAFADIPSVYLISVNCGARELWLTITSIHFVSLREQRYEFLANSLGERTSSLKSQEEMVSVSRNGKQLLSEASFFRLGKHVHLNFLPFENTFEMALRNDFQIFCTSILFTCYIQSFSLLISNFFIAIEVSRSFF A6X995 YC7F_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPCC417.15; CHAIN 23..43; /note="Putative uncharacterized protein C417.15"; /id="PRO_0000303992" MKRKIIAIGIFFRLFIIHIHFSHHCCENHFINPLVCLIALFCI C6Y4A2 YD1V_SCHPO SPAC4G9.22; CHAIN 1..94; /note="Uncharacterized protein C4G9.22"; /id="PRO_0000389126" MSLKMFVNEKFIEDWCRETGEQVDHQLVCTVGEKSKEKICLLERTCSLEGLSTVLMSENFKDTLEEELKDCDSHLDRAANDSPSLSCILGNAND C6Y4A4 YKQP_SCHPO SPAC688.16; CHAIN 1..109; /note="Uncharacterized membrane protein C688.16"; /id="PRO_0000389150" MSCLNLHVPKNPVGKYIPLVVLLQMYIIYVEPYYGLHYFESVRQFLGPKILYGTVYFLVICHSIESAIAFLLCLKKGLPFCSSMKWIVSTFIFGGPTLAMLNKQKKHIA C6Y4A5 YELS_SCHPO SPAC6F6.19; CHAIN 1..122; /note="Uncharacterized protein C6F6.19"; /id="PRO_0000389128" MELEKKGIELTLQRAHPFYKGIMLEEKLADLEKMKQKKLFSRISLSNAKASQEIDLESAIKEEANSDALYVEFESLEESKQLDVVLHLLRDRFLYCLYCGCHYDSQEDLIENCPGINEEDHE C6Y4A9 YAEQ_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPAC23D3.17; CHAIN 17..78; /note="Uncharacterized protein C23D3.17"; /id="PRO_0000389125" MNPSRNPGHGDKPFEERKLVGKYIFPNKDDPRATVEESELPKSYRVLQPNSFCTRDFMPDRVNFHTDSNGKITHVTKG C6Y4B0 YEIN_SCHPO SPAC27E2.14; CHAIN 1..34; /note="Uncharacterized protein C27E2.14"; /id="PRO_0000389146" MRLRRLFKQPSTRVLGVTNCPRQQGHQKRREQPD C6Y4B1 YE39_SCHPO SPAC20G4.09; CHAIN 1..24; /note="Uncharacterized protein C20G4.09"; /id="PRO_0000389144" MTLIKYKRKNIQFYKKIIANGYAK C6Y4B2 YDMO_SCHPO SPAC57A7.15c; CHAIN 1..137; /note="Uncharacterized protein C57A7.15c"; /id="PRO_0000389127" MFYSTTSWFQKATLAIGIGTTLYVLFKDLVRDQEAKSESKSRKKVMILVDETTSEEDIKKWSDYDLFLASRSTLLSKHTSRLESYVSHPSKALRCDDPDSILTFLKHLDINILVWNAHWSSERLKTQCENLVYILVE C6Y4B4 YEHU_SCHPO SPAC23H4.21; CHAIN 1..122; /note="Uncharacterized protein C23H4.21"; /id="PRO_0000389145" MYQVSNLDLKCGVHNGELLTVLLPNIMDSGNATELGIGVEEWHKRRSSWLLGKKSTEETDSSNEVVVPENVYLNVYEALVYRRQKLKRPVKLSIVIAVLKAGWIRDGFWPAPSNSNGVSVPP C6Y4B5 YM0C_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPAC212.12; PROPEP 97..123; /note="Removed in mature form"; /evidence="ECO:0000255"; /id="PRO_0000429009" CHAIN 21..96; /note="Uncharacterized GPI-anchored protein SPAC212.12"; /id="PRO_0000429008" LIPID 96; /note="GPI-anchor amidated glycine"; /evidence="ECO:0000255" MSPLIVGTLIIILLSGLATAFYVTWQGRLICAGVGLILEQAYEGGQMFNTLMAHCFETYNGVEKSGTQCVADWLKVGLLAVTFGAGGPRLVNTLGGSSPTTKRVIYIVMILLVLITLAVNLKH C6Y4B7 YIDS_SCHPO SPAC227.19c; CHAIN 1..83; /note="Uncharacterized protein C227.19c"; /id="PRO_0000389129" MMGSMVSNGYLLLFTCWFLFVFGLMTIFNFVEIPLYVDGDVSPIRSYYPCILILTCTVVFFVWLFFNWLGLKYFRHSPSAMRR C6Y4B8 YA8O_SCHPO SPAC22F3.15; CHAIN 1..123; /note="Uncharacterized protein C22F3.15"; /id="PRO_0000389168" MYNTYAIIVHVSKLRNSHLFANASAIPNLQAVIRKKLLDSMKSRQKDVASTLKVFLSEIEYANKSSKPVTTDLDVLRVLKKNIKKRKQAIEQFRKAERLDLAEKEESQIQTLRQFLPEHASNI C6Y4B9 YFMQ_SCHPO SPAC222.17; CHAIN 1..89; /note="Uncharacterized protein C222.17"; /id="PRO_0000389148" MEEKVQEFLKDSTKEQKVFFESLNNQTERVCQQTESGDISCIELAAAETKLFATMQSLGFICTLSADPNRPTVFECKRELDTNERKERL C6Y4C7 YJ7O_SCHPO SPCC757.15; CHAIN 1..69; /note="Uncharacterized membrane protein C757.15"; /id="PRO_0000389130" MNRNRIYDIVQKGSVSILIFGTVGGTVLLGQSYYSHRQRRLAALQEFQQREKIKEEGFAEDEFNQLALK C6Y4D4 YQO9_SCHPO SPCC569.09; CHAIN 1..99; /note="Uncharacterized protein C569.09"; /id="PRO_0000389152" MSDFPPSYQQHENDRMVPQESSTSNNASEFNVPKKSNRRLSVVQQDESVLNREFDDLTPEVGFDADKWERKTKHPNPQKPFDFKRKPEKKYHSKSDVGF G2TRJ5 TAM6_SCHPO SPAC1F7.14c; CHAIN 1..81; /note="Uncharacterized protein tam6, mitochondrial"; /id="PRO_0000416515" MMPSSSFQQTPKPVDLDDPRFEQYDCLPCRLVGAGAFTGLGIYAYSQSRIPLNTPNYKLKRFGILGMAYGFILTGVYRLFQ G2TRJ6 YLE7_SCHPO SPAC1093.07; CHAIN 1..78; /note="Putative uncharacterized protein C1093.07"; /id="PRO_0000416650" METNILAWTKRASSVKKEDKKNCGSIFLRQVYRPNANSKADDIEIDLRSGTSASFAAASKRGQVRNTFYRVRRFSNNS G2TRJ7 YFVD_SCHPO SPAC1834.13; CHAIN 1..78; /note="Uncharacterized protein c1834.13"; /id="PRO_0000416631" MIFARRLVLEVTYVSKRASVLNLKSENDHFLSRPRISESLPTSGEVGIAKVPAKLASALPPYSVFAPVSLSFVRMNCG G2TRK0 YIP21_SCHPO SPAC343.21; CHAIN 1..158; /note="Uncharacterized transmembrane protein C343.21"; /id="PRO_0000416642" MVSYNVLTKLFFIFSGGLVFFFFEFFLNHFNYYPTKLLYYITFYFIKNHPSLFLLFNFFLSTASFSYSFPSKSHLTFYSKGAPSVFFLSLKSSPCPGYCSSTLLYSTSNLLPSLPSPLHAPPPLGSRLLHVFFYRRSNASAYPSFTPRYSFFPSFTLR G2TRK1 YE9J_SCHPO SPAC17A5.19; CHAIN 1..92; /note="Uncharacterized protein C17A5.19"; /id="PRO_0000416628" MSLRRIPNKNLIPEIPPFPEESINLLQNGVNTIPRINLEDVDVMSTKLPTDEELTENYQNWKKNLEVERLEKLKRIAPGYSASSPLLPSKSD G2TRK2 YDPM_SCHPO SPAC29A4.22; CHAIN 1..73; /note="Uncharacterized protein C29A4.22"; /id="PRO_0000416626" MELRVKGRVRHTYIQCSNPIRMTFGHSKEINRRLGTKSENSIPKIQYIYISSFVITNTESYSYPPLLIISESS G2TRK3 YLV4_SCHPO SPAC2H10.04; CHAIN 1..124; /note="Putative uncharacterized protein C2H10.04"; /id="PRO_0000416651" MPFLYMLFLTVTVKLLNSTENFLFHKFFFSFFTLLSSPYVYPFFFSLLVLTIPYHTILSYPVLYNTIPYHTIPYLTMPCLALHFRLQPTLLLQWCPLRQCALPFQSHLLFTPRFLLPQITGIFE G2TRK4 YI36_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC1399.06; CHAIN 22..124; /note="Uncharacterized protein C1399.06"; /id="PRO_0000416639" MFLLSLLHFFHPSLIPSLSLSHTHSSSLPPYRLHCTALSYRDLLTKKSANFRSPIYRSHVNEKGTLTHSFRPTKDMQSGNCWFTILRKARNLLNHGILLSSNNRSFCFIIQISKINPFERFLEM G2TRK5 YK35_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAC110.05; CHAIN 23..30; /note="Putative uncharacterized protein SPAC110.05"; /id="PRO_0000416644" MRFLFFLPPSFITSFLYLALYSFPVPYCII G2TRK6 YE8E_SCHPO SPAC9G1.14; CHAIN 1..81; /note="Putative uncharacterized protein C9G1.14"; /id="PRO_0000416627" MNVVYIADLKLPEILHTVSTDFALQKKLFQGFRATALKALAFTIYQISISIQTSYPSDYCCSCWLLDTVRCVAILYAIHLS G2TRL0 YLX9_SCHPO SPAC922.09; CHAIN 1..71; /note="Putative uncharacterized protein C922.09"; /id="PRO_0000416652" MLQKHNKVKQTSVVRLMKYRGGHFGGGGLSTAIYSIFAFFSIPLWEKFMTFYLELFSILNNLVTSISKGIL G2TRL4 PRL65_SCHPO SPAC19A8.16; CHAIN 1..65; /note="Uncharacterized protein prl65"; /id="PRO_0000416665" MTKYSKGNKVEYHPIGGPSGTSTSTGVIQQVIKNDSGEETRYEILNDHTGKAATYKERNISRILD G2TRL5 NEW2_SCHPO SPAC1805.18; CHAIN 1..95; /note="Uncharacterized protein new2"; /id="PRO_0000416503" MIIEKSINAKQLSLKLWDSFVKEKQVSFVAEGDATVKLVSLVELLKRRCNEQKIPFNQTIELIPSEEQSSDTLIHGNRRSLPQLKIDLQILEHDS G2TRL6 YKF6_SCHPO SPAC1B2.06; CHAIN 1..84; /note="Uncharacterized protein C1B2.06"; /id="PRO_0000416645" MPKAHPKCEILEPSELLTFTKSSSYSSYFFARLCAIVQSICCTIRVCAIILIDYRLLVFTIGPHHKINGERWILNFPPSVKVCL G2TRL8 YEAK_SCHPO SPACUNK4.20; CHAIN 1..74; /note="Putative uncharacterized protein CUNK4.20"; /id="PRO_0000416629" MRRSIDYFTEPSCLSSGIVDILNKGFLSNKSKSHTQTHKKTAVQLFRNLELSTTKNVMEMWGKQDILRFLCFSE G2TRM1 YI7I_SCHPO SPAC977.18; CHAIN 1..133; /note="UPF0768 protein C977.18"; /id="PRO_0000416684" MFYLRVLCVQRRLVREINKLSSFESNWLFLLFLVRVCRQLKTVTVLIVPVLPVYTNKVLRCSQCDWHEPANLDSIYQRSSHDDDLPTIKGSDASTQQYERKTYITDASPESQNLFLSKSKEEGVIFLCIQVSF G2TRM2 YI82_SCHPO SPAPJ695.02; CHAIN 1..70; /note="Uncharacterized protein PJ695.02"; /id="PRO_0000416641" MSDFNLRRYYTSNQLLKFSNEYPKSMTEIKKGELKGYDIFTSSTINMVVGNLLRDVQNRIDQADQIEKRS G2TRM3 YAOJ_SCHPO SPAC11D3.19; CHAIN 1..77; /note="Uncharacterized protein C11D3.19"; /id="PRO_0000416616" MVPYTETSICLTNVPCGYMNVSGCFKGADALTILHECDEANVYTATFWSTSSGTRRNSAVICTLIANLMAFFMLLTM G2TRM4 YFQC_SCHPO SPAC8E11.12; CHAIN 1..102; /note="Uncharacterized protein C8E11.12"; /id="PRO_0000416630" MISLLSIKMQAIKELDSEEEPKVGEFYKGNTISFCKNSLENDTQLPQILFCINPKSIRNFLFPPIAISDPKEAQNHCSSYYYIKYRYYIVQSRCGMMGRMSF G2TRM5 YKVB_SCHPO SPAC959.11; CHAIN 1..121; /note="Putative uncharacterized protein C959.11"; /id="PRO_0000416646" MYYVACVFVYNKYIFTFEKENFVEKMNYRLRDKTFNFNQMAQKRNKQSKKPKQTSKGVKKSSKQNKNSSKNNKYQQNVLLQSIDDYNTTQSVLRSAHNSGSKMSDISNSIQLLSMTKKQEN G2TRM6 NEW4_SCHPO SPAC3H5.13; CHAIN 1..146; /note="Uncharacterized protein new4"; /id="PRO_0000416504" MDKQIPKFEITRSSLLDQCKSFLPELEKANQTLLEHPDSQQDVQNLSDESNYIEMDLALGVLEKQPENSISEDTESEIQANENQGTLEHLMNLYNSRDREKGNEVTLTDFLHEKLSRAAQADLEHEESASIDQDEMVAIETRKTKK G2TRM7 TAM5_SCHPO SPAC16E8.18c; CHAIN 1..156; /note="Uncharacterized protein tam5"; /id="PRO_0000416514" MSTNDHVLSLLQSLETREQLQKQLQIRSHEAFSLLLKNKSDFSVASLLSNQNSPTFKKPRISIAWVDPMFGKQQKRAVNLGTGDEEYQHLMFENAIFQKEPIPEGLIKSDSVCFHDTDVGFTNVLEQCLKLCQVNQKIVFLMQLIRNEQEKQREQF G2TRM9 YAYH_SCHPO SPAC4H3.17; CHAIN 1..86; /note="Putative uncharacterized protein C4H3.17"; /id="PRO_0000416618" MFGVSTFSLKKTLRFLFFFEFFSHFRVNCYMIFDINWRKFMLCWCNPNRTTIDNLQSFTVHCIHRNRLFYKSFILQFLGRKRIILQ G2TRN0 YAYG_SCHPO SPAC4H3.16; CHAIN 1..107; /note="Uncharacterized protein C4H3.16"; /id="PRO_0000416617" MKRCRSEHVPSRLPRKKCKNHLDMRSFLSLFASKKSNAHDASSIVLNEKVNFVTDNDHLPSSTGVCEFCDNVLYLSTCDRCQRNICRNCSTLMYFKENTVARCLDCL G2TRN1 YL3D_SCHPO SPAC1071.13; CHAIN 1..105; /note="Putative uncharacterized protein C1071.13"; /id="PRO_0000416647" MGRSNHLFIFIHWKSRSIFSGNNKVYRFSNLYVRTNSWQKVRHLESLHTNAYIVPLEMRLIIMKTRQTFKVHGMRKRKYYWKNDYMRGKNRNGNLPTKKHQSKKM G2TRN3 YL66_SCHPO SPAPB15E9.06; CHAIN 1..89; /note="Putative uncharacterized transmembrane protein PB15E9.06"; /id="PRO_0000416648" MKLNVCFRICNFLFQFSLEFFSISSLHSISSLHSISLSLSLFFLVAILYNIYIYLFRSKKKPKRILFAIPPLCPLCSPCFFFGTSSMLL G2TRN5 YL8K_SCHPO SPAC25B8.20; CHAIN 1..72; /note="Uncharacterized protein C25B8.20"; /id="PRO_0000416649" MSPRASLEKELNSARLLHATINAMDVYTQNLINELQEARDSINDLQRAHERLKLVGAKAKLQIKRDEKKPKS G2TRN6 YLZ1_SCHPO SPAC750.01; CHAIN 1..325; /note="Putative aryl-alcohol dehydrogenase C750.01"; /id="PRO_0000416678" MSFGKKEYWEDWVLEEEDEVFKIMKAAYDAGIRTFDTANIYSAGVSEELVGKFIRKYEIPRSSIVIMSKCFSPVRKDLIKLYMDLSSRGVQLHDSPELANQCGLSRKHIFDAVQDSVKRLGTYIDVLQIHRYDPHVSAEEVMRALNDVVESGKVRYIGASTMRYYQFIELQNTAEKHGWHKFISMQNYHNLLYREEEREMIPYCQKTGVGLIPWSPLARGLLTRSIDANEETIRSKTDLYTRALEFGAGYKAILSRVEELAKKYNVSMATLATAWSLHKGDYPIVGISKVERLQDALASVTLKLNEEDIKYLEEPYCPVPIQGEI G2TRN8 YI74_SCHPO SPAC977.04; CHAIN 1..155; /note="Putative uncharacterized transporter C977.04"; /id="PRO_0000416683" MPINQKFYSYLVKRNGGEGEPEFRLPMGFIGITLFEIGILLFGWTARYKIFWFVPTIGSAIMGGGYIMTSNPLNMYVVDSYGIYSASASAGVKIFQLLLGAIFPLFAESLFRRLNYGWGCTLLAFILLACGCSLPILFKYGKQIRNLRPFDPSKY G2TRP1 YND9_SCHPO SPBC30B4.09; CHAIN 1..51; /note="Putative uncharacterized protein C30B4.09"; /id="PRO_0000416657" MAQTFQEKQQSRRIKMSTGNFFSRMWNAVVFGFGAAIGASVANAALGACCG G2TRP4 YHZF_SCHPO SPBC21B10.15; CHAIN 1..60; /note="Uncharacterized protein C21B10.15"; /id="PRO_0000416638" MGMSLKGQLLTFFGIFITVGPISFLVLKNDLNNKKREYFKLYKQEQAKQLENAKSSKENK G2TRQ0 TAM13_SCHPO SPBC56F2.15; CHAIN 1..95; /note="Uncharacterized protein tam13"; /id="PRO_0000416522" MQNFMNNLSGGSNKEGGEKSNDFLSSALGAEKQVKQAQTMKKISDMFPGSTSEKLAILNKINSASGGRVLETLGEIENSSSSQDEIITKLKGFLK G2TRQ1 YNHF_SCHPO SPBC32H8.15; CHAIN 1..101; /note="Putative uncharacterized protein C32H8.15"; /id="PRO_0000416658" MTFRYSNIAHTLFISIMCLFSIPLCFSLSIFFFLSSHSLSFAIHCYAPLSTSLHCGWPHKVDMQYFFPWSRILRPTWVGRALLSKGGVIEMLGGEAGMLGK G2TRQ2 TAM8_SCHPO SPBC3H7.18; CHAIN 1..77; /note="Uncharacterized protein tam8"; /id="PRO_0000416517" MNRTSESVEPQQNEKTAVHWSREWVPVVVDTYSNEDDEDNEEGDESRPQRTFLVKRWVQDNVQVEKKGDEETAAADN G2TRQ3 YB7K_SCHPO SPBC16E9.20; CHAIN 1..189; /note="Putative uncharacterized transmembrane protein C16E9.20"; /id="PRO_0000416619" MLVVVSLTPPVGVCVGLFHHLLSLGGGITTCITSMETGITKWSGSLRCNSQMQKEKGERKGKEEERKRGKEEKIWFHSKKMKIHDYCIVLYCILFYFYFVLILFYFIALYFILHPFYSTILFFFPLFIKCSHLHTLTSFYSLLSSLFSSLIPKHSLHLAPLRKLNLSHFVSPLCAMFPHVGLRLLQTTQ G2TRQ4 YH6H_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPBP23A10.17; CHAIN 23..118; /note="Uncharacterized protein P23A10.17"; /id="PRO_0000416636" MKMSYLRSGIVGFLAGASLSYAAGVQALISTSKQNKDELLTATEALETDKQLYKKIEKKIEELESSCVKKSSWEIQESEWKAMFQTMRVEYLELLEKQKTLGEVLNKLVEDRQTKFQF G2TRQ5 YHXH_SCHPO SPBC3E7.17; CHAIN 1..60; /note="Putative uncharacterized protein C3E7.17"; /id="PRO_0000416637" MLTVECLIYAINFTSDSIGRSLKLWGTSRRLRFAETESFHNKKPTSLFTQHEFSYSCAYQ G2TRR0 YGOG_SCHPO SPBC336.16; CHAIN 1..71; /note="Uncharacterized protein C336.16"; /id="PRO_0000416634" MYHSYSHDLTNYLYNYFSSTTSWLVFIILSLDTINATFSNITFVDILMETGFTKNRSLDQTTCGIKFGFVN G2TRR3 TAM12_SCHPO SPBC1105.19; CHAIN 1..66; /note="Uncharacterized protein tam12"; /id="PRO_0000416521" MSTTSSSSTFSTRTASLSQSYTNSLKKEAAQKTLENWEYQAIHALQNNSSFPAIRRSMRKILADPS G2TRR5 YORW_SCHPO SPBP8B7.32; CHAIN 1..74; /note="Putative uncharacterized protein P8B7.32"; /id="PRO_0000416659" MESNFLLFIVQQNLFDHYIISIVSNRIIGIRASTRKVEYQFFLAFKSFPSIMGRTSPKFHIINKHFLSLFKREK G2TRR6 YGIE_SCHPO SPBC2A9.14; CHAIN 1..66; /note="Uncharacterized protein C2A9.14"; /id="PRO_0000416633" MTENETLQKSSWKRHFTSTFPNRVKKIFKIKHSSSIPIVRVQPPTPRNSALFTTADFISYTTVYKV G2TRR7 YBBG_SCHPO SPBC13G1.16; CHAIN 1..62; /note="Putative uncharacterized protein C13G1.16"; /id="PRO_0000416620" MQHNKENHFVEDAKQFQEKAKLYQGNYYTLDGELITIIPSSKEGFRSCKSLYYKKKQPIPGR G2TRR8 YP3A_SCHPO SPBPB21E7.10; CHAIN 1..84; /note="Uncharacterized protein PB21E7.10"; /id="PRO_0000416660" MQKLNKSSSKGKNNIETEEAEDSAGRGSTYGFGPYGGGGFSSKSSGEEATTGDTKKLKGEVEEGTGKLLHSKKLVDKGERKESE G2TRR9 YP3B_SCHPO SPBPB21E7.11; CHAIN 1..164; /note="Uncharacterized protein PB21E7.11"; /id="PRO_0000416661" MLCVRSSSSNLESDTYLSRYSTRASAGTGSTYGFGLAGDRGYSSDSSSSSSESKPSNNKNIDFIYNNNAESNLSEYLGKDIPEDLSGFRDTASAPDTQSDVRNCDSIRKYQSLSSAGSGSTYGYGAGGNRGFMDESNESPKEDYINQKKHSKLFLLLYRIFHLI G2TRS0 YH0H_SCHPO SPBC1685.17; CHAIN 1..81; /note="Putative uncharacterized protein C1685.17"; /id="PRO_0000416635" MLSYGMPCHVLRRNTRILMKEKKKRLGIMFWQNVERRRCPETHSNEGASQGKRKRSERLKSVDFKKGVYCACACACTFQQE G2TRS1 NEW14_SCHPO SPBC839.20; CHAIN 1..80; /note="Uncharacterized protein new14"; /id="PRO_0000416508" MQKKEKIIENLEKAGNTFHLIIKCNTIARILKNLSTYAILLNSNILEEHVDLLLIYLSTQRMWKLNNLKKTLQYKGSKKK G2TRS2 STEEP_SCHPO SPBC839.19; CHAIN 1..115; /note="ER exit protein"; /id="PRO_0000416509" MSNQGKDSFKAYSYFCPCGQLFLTIHVSLTRLPQRQLDKRHVVDEKLNHIAHFSTGNKYYITRSDGGYEQRIQLLCRRCTLECAYALEAAPGYIYVDPTLVNEKPVTVSVSNLKE G2TRS6 YN8H_SCHPO SPBP35G2.17; CHAIN 1..106; /note="Putative uncharacterized protein P35G2.17"; /id="PRO_0000416656" MVREFYVTGRGRKLLPTVFRIKSFHGIVRQCVKQQRDFTSFLASSPAMGVAQGQQVKLILMLLIETWETKHQSCHSHFILLEFTHLFVRKFSQIFFEFRLFAHLLS G2TRS9 YBJ2_SCHPO SPBC337.02c; CHAIN 1..305; /note="UPF0612 protein C337.02c"; /id="PRO_0000416681" MMSNENFDNDYNLPPPNDSAEDLKIFIERYERSVDSTLLEIDENKREALEKNILRKDRKMKYEIECNERLQGWKKLAIEREISEEQSGEVQFPRWIDEWANTKLGGIFERIFSKMDSMQNDMNSRFDAMQNEMTSMKGEMAEMKVEMVEMKRETIRLNTRIDLLEQKTEARFQSIEQRFNSIDQRFDSMEQRLDSMDQKMETIDARSCRSIMLTRKLENATRSDQGYLASPVPFLNGNEPVSSGLPPIERVEDIDELSKEQCVQYLKGYGITFSPAETIKLKKRLRDTVGLWSKASTEYEFHQFH G2TRT2 NEW22_SCHPO SPCP20C8.04; CHAIN 1..78; /note="UPF0612 protein new22"; /id="PRO_0000416497" MNDNNSCKLTMLTRRLENMTQEYGQPDLPVPFLNGDEPGKLKLPLSERHEDVDYLTKEQCIQYFNGYSIHLIPPRISS G2TRT4 NEW25_SCHPO SPCC330.21; CHAIN 1..89; /note="SAP domain-containing new25"; /id="PRO_0000416510" MKIANVLTLSFAAIIAASSLAVVVSPITDNSRETASSSISQSPPSQWSKKQLIEYCKKNSLKTSGSHEELVIRVQNHLRTASKKVDARP G2TRT5 SLO1_SCHPO SPCC663.18; CHAIN 1..65; /note="SCOCO-like protein 1"; /id="PRO_0000416671" MSTDSLPRSLMEQKAMELQQQLQALLDEIDQNKQESENISRESEYLCQYIGSMMAFQNRQTVPKK G2TRT7 YCYH_SCHPO SPCC1235.17; CHAIN 1..150; /note="Putative uncharacterized transmembrane protein C1235.17"; /id="PRO_0000416624" MGRCGTHTQINFLAGFVVRFNNVKTCLAQFWVNMGQNKEGNADKSSYFKVVSVILTLRGYVQLGYMVIHLVTHTLHCITLYITITHYTIYIVNIVIQLWLYRYIERFFYSLLVEYCENLCDSKEKRKVVIRFYFHFYFFFSFLFFIEKKK G2TRT8 YCYI_SCHPO SPCC1235.18; CHAIN 1..159; /note="Putative uncharacterized transmembrane protein C1235.18"; /id="PRO_0000416625" MTPRNPSNYDSLFDSSIFSSTLFSSSLYHSAFDCSFGISFTIQPPIEYIVLSKPCFFAITPLLTLRCNGIAWHDSLDMTIWVSTVTSLPISHCLIVSLSLSHAFPSLFYSALVLSCLSLLCLAFTPRIPFHLHSVVCSYFGRECLSPLFPSPYFTCHNG G2TRU1 YQ9K_SCHPO SPCC18.20; CHAIN 1..72; /note="Uncharacterized protein C18.20"; /id="PRO_0000416664" MSLYWNRKKSDTEKTRPMDIFLVSDFIVYYRRNMIANLMNDYRTLSIRVSCLNINKNWNLNRALYLLNIKNT G2TRU3 YJO7_SCHPO SPCPB16A4.07; CHAIN 1..69; /note="Uncharacterized protein PB16A4.07"; /id="PRO_0000416643" MSAPYKNLDRDTKHTHPKLNETERNLNRGWGDVKKEELYEDLAQSDADKQLAEDKMETKYEKSKPAPSD G2TRU4 YC5G_SCHPO SPCC1259.16; CHAIN 1..70; /note="Uncharacterized protein SPCC1259.16"; /id="PRO_0000416622" MSQKSHKEKLEKPAYKCMKQYICEKVSAHENDVVCITVQRFFQVVDGHMKEVRPMSNQIGLQSGPVVEKN G2TRU6 YQ3E_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPCC188.14; CHAIN 19..79; /note="Uncharacterized protein C188.14"; /id="PRO_0000416663" MPTTISLIIFTFLSLGDSWNDFPSSNVPVYNMVTGIYAKFMKNSPNWPLSRCWLFIPQFAVYPEYFILSIRNTRRRNVL O13647 YGWB_SCHPO SPBC8D2.11; CHAIN 1..122; /note="Uncharacterized protein C8D2.11"; /id="PRO_0000116766" MGRPLIESSSNDHVANFNRKTKKLIDQALEHYNGRLPEQLENFSFENFVEVLDTESSVVNRVFEVLVREVAGSFRQRKRAHMPRTNTTAQVVQRQLAPSISTVFSRDSNDPLVDDMDQEYIL O13689 YDYA_SCHPO SPAC11E3.10; CHAIN 1..162; /note="Uncharacterized protein C11E3.10"; /id="PRO_0000116678" MMLPSYLHFAIRKKVLAIFIVLLIISAYLGFAPALPVPINDKVCHFFVFFLLTLVFYWVFDLSRRRATQLTILVCGVFGGLGSEFVQSFLTYRTFDLFDIVANLLGCSLALLLNILYHKRRLEKIRLQRYGHVPTIADDLEMQASAAEEEEEGEEDVSKSTP O13695 YEN1_SCHPO SPAC11G7.01; CHAIN 1..536; /note="Uncharacterized serine-rich protein C11G7.01"; /id="PRO_0000116725" MSFTNNTSSVDTSLSSSASSSIPASSSSAAASTSLSSSSVIPSSSSSMLSSSSATAISSSSSSSPLSSSSFTSPASSSFITSLVSSSSQQSSSSSASLTSSSSATLTSSSSASPTSSSSSHALSSSSSSLVASSSSSGMSSSSLSHSSSVPSSSSSYHSSSMTTSGLSSSASIVSSTYRDGPSIITLVSTSYVSEVVTPTTTNNWNSSSSFTSSTSSTPISSSYSSSGTLPSKSNKSSNHVGVVVGCSVAIPVGVVLILIGLGIFLWKRHQRSKRIKAERMQEVEEYGFNPNQPSNFRSPNRAPSTNNRYRGWNGSPTPAAGNNTNGRPVAPRPSAGAGGANPPAASQPGLLGGSSNSAGPIAAATAAGVGADASDAANTGGSFTRPQGARMVRPIGNPPDLSASNEAEATMPPSNGSNFSEGLSASPFESGPAVGAAGAAAEAAEHSGSGSDSYPEGPLATIPESDSESMASDLAGESSYGSRAALSSRSQSNLLSPTSTGASNQPNYSPFADNPSSSNVSIPRSSSEARRLNLF O13711 YDZ4_SCHPO SPAC14C4.04; CHAIN 1..267; /note="Uncharacterized protein C14C4.04"; /id="PRO_0000116681" MSMPIVREVNSDGSMLQPFSNPLWVPTPVGRSGRKHRTLKMCIVLPDTGYDVTQVCDPWQFFVKEGFMVNFATLTGIVAQADQRLLSGVKSWFIGATYKTKDIYERMSTTKEFLSPSNMSDMSFTFENFDLVYVPGGQDPAVLELVESPRLSSLLADYIPLCARVSGTRVLATMAQGAIAVQRAAPNLEIKSTTTPLYMERASYLFGASNPPAYTYTYIPESKYVPGPKTAHWVYSDEKFFYASGRYSGDVELLCKALRNLVASALH O13727 YDO7_SCHPO SPAC15A10.07; CHAIN 1..162; /note="Uncharacterized protein C15A10.07"; /id="PRO_0000116644" MSVVFRTVEDPELKSICTTFTSSISAEFDSNTLVCDLVETDLFTEEGTSQIFTFKKNVLILPANVPEGIELRILEENVSLPLKEFEPIKVPAGAHCFLSWEKVPLRKRIKIISSSQPDDNDEESTWPGVFIKFGVENSSSAEFGEPLKSQIEIPDDQKLIVQ O13730 MDE6_SCHPO SPAC15A10.10; CHAIN 1..700; /note="Mei4-dependent protein 6"; /id="PRO_0000119148" MERKELSYTIQSWSSYSGAFHPINILIDNPHQANSRWSCNTSICKPNNSEEQYVILKLDKLALVTDITFGKFHTPHLCNLKDFIVYGGREQHLMFPLLRAGLTNDSNRETFPLCIKKYNKIENSIACKYIKIVPLQAHAHEFNMSIWYVALHGIDSASALSCTEKNRALHLEKKALNCLLSYFAFKGKLDICSVILQSYQLSIPHSPLMRMYDAFCRLGDTQKTILLFQQELQAEIIEKWPKHKLTKLRSHRIATFLKGISRRSGHQMVYNPKDNCIYLYGGWDGVKTFSDFWIYNVDKDLWIMENEYGIPGERVCHRMVIDTSQQKLYLLGNYFGSSRETEVPPDARTDFWEFDISKKVWTCLSYDTSKDGGPAAIFDHGMSVDEKRGIVYVSGGCKWDPDELVFEGLYAYDTKNRIWEQLAVRYEDRQKHCEFKIERMGHCMEYFPDENKLYIFGGQSYDQEFILDMCYIKLETREAVQHVRKNDTSQSPSPSFCQRSIMDSKNHRIFTMFGFEQRNIHKVLRPSLWIFYITTEEWVKISDINEEEGNEHPCSRFGHAVAADLNRNIIYLMGGNASTHPLRPMKLSDFWKLDILDRWGIKHCLSNVSLQLHLHRFHELVSENLAKAVEYLQKSMQPQFDKSPLFWNALILDAFSGTHKNKDIAQRRFETFQTIYDLLPVDENTVAPNESLLNMIEFFT O13740 MDE1_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAC16E8.05c; CHAIN 23..209; /note="Mei4-dependent protein 1"; /id="PRO_0000014195" MLHATQLCYLLLFCFLPISISSAVLIEREINVPTTHVLQTLYTRFWSFKAHLGVDMELGIKGSLIHYRDDKLFLGEYPKSRLLRVCYDDNGTFKVKDKRGLVYVQGERLILERDAPSKFSIELVEERREPESPYLLFFSNSSRFSACEESGEWVIYSGDVYSAETTCIPIELVGLRYRGWKTNDKKPFRIIEPGKEPLDAPWNDELIVM O13761 YF2B_SCHPO TRANSIT 1..?; /note="Mitochondrion"; /evidence="ECO:0000255" SPAC17A2.11; CHAIN ?..217; /note="Uncharacterized protein C17A2.11, mitochondrial"; /id="PRO_0000304104" MVCPSPLRECHPFLQRSFFPSFALSHRDIISTRACLNDNSPAFDRRYHWVWEEDRRCLNLGKTLASTIHHKGGNLSLQWQRGNTTTHIATRWDANKLLLARAILKEKRNILQDKTSVNVNVNKLIPIPKKKVLKNRAKSLLSIKSHVHFHLIPFINFFLLYHQIILSHSLFHISHLISFHFLFFSFLSFPLLSFILFPCFSLFLSSNSFSLASPFSS O13767 YE95_SCHPO SPAC17A5.05c; CHAIN 1..247; /note="Uncharacterized protein C17A5.05c"; /id="PRO_0000116707" MSWRPTHSVRNAPYSMRDNYAQGVDVYYKKVGGTYRNLHFRGLRLLLLQCLSHFWDHDEKFKSHGLHVIDLACGSGEVSETVIEWEHLGRELGIHGGAFKVRKEISIRSIPPELPPFELIATDPFTLEAYTNRIGKPCLTLNFQDIADEKLPPSSAEDGIYDLVICSFALHLLTEPSKLFSTCYALSVQCRWLLVLGPHKKPELKPEWGWDAWNIDTWCPLGYGISHDYVLERVHARFFKSRNLIDG O13886 YKB2_SCHPO SPAC823.02; CHAIN 1..43; /note="Uncharacterized protein C823.02"; /id="PRO_0000116825" MLNYVTSRYLATFLQPLSQKWIAFLLKKIFSKRSSIRKTLPFS O13913 YDW7_SCHPO SPAC23C11.07; CHAIN 1..110; /note="Uncharacterized protein C23C11.07"; /id="PRO_0000116672" MASHFLFTGKPWLQEKTPRLHLHPTWDLKASKSLARFPYTPLESLLAPISAFHPTYLNSAAPSKAQSHPVLLAAGVGGIVVRCPSRKPIYRTTRIQYLLLISHFTTALFK O13948 YEH5_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAC23H4.05c; CHAIN 22..97; /note="Uncharacterized protein C23H4.05c"; /id="PRO_0000014197" MLLHGLGRMNIIFICFPSLACLLTSRTPLCAPLFSHLDGMTPCPIDCGFAVGRSRGGGFGGKPESNSLHYDTMHKQHAMPFFIINPTEWKRNFCNTG O13957 YEHG_SCHPO SPAC23H4.16c; CHAIN 1..328; /note="Uncharacterized protein C23H4.16c"; /id="PRO_0000116719" MLGKEWENTSFAEIGLLHQAPNDNDLEKFQHALTLMSEADNSSDLLIPLISDFLIWFYYQKTPLKWIPFLGHFFNTWQSCSFPPRRYLLAKILSGRISELLKVSPFELAASVTSQDVVEADSLVEENELQAWLEKQELVPSSSNFLNSFWISGGERELTEEEQNSLLQSNTTYTNSDLPASKQLESFISMNLSYSKVFFLHLLQHSDSSFNDKFLLLLANIPVTVSNVEVLLYLLQQEESLAQFDLNGKSFLYHMLVSLHNQVTNTSHLEKQRISTVATLFISKLFEIPSLSEYLSSTLFLDLQAFCIVALPQSAKLFQKVKALKNNP O14037 YEY4_SCHPO SPAC2C4.04c; CHAIN 1..125; /note="UPF0538 protein C2C4.04c"; /id="PRO_0000328904" MTGATLTVRVIRNFEYRTLKNVVFHDIDLATTTVDQFKKIIDERIQTDPSLKIYRTTHFDTLKIYVKAQQHKTQNLAINLDHDDWILNDGAKTLSLCGIENETELSYFELAAYKAYQANPVQKWL O14041 YEY8_SCHPO SPAC2C4.08; CHAIN 1..243; /note="Uncharacterized nucleolar protein C2C4.08"; /id="PRO_0000352826" MNRLQAKKAVNVSRHEQKRIRYKLTPEEVKAERKERKRRAAIQRAEKKLIRAKGEALVAFQAVSNPSCNFLVIDFEAYEFNQKIITEAGITMRINGEWDYHHYRIKNFLHLRNGRFVPDEADNFQFGDSKIVTKIAFISILKKILKTPNLHLVGHGVENEIKYANVLGIPIPKDVTVLDTQNVFSFFQSLFLKEISNSNNISLAKMLTHLNIRAFCLHNAGNDARYTSEALREMTNKFTLSNF O14067 YFF8_SCHPO SPAC1687.08; CHAIN 1..96; /note="Uncharacterized protein C1687.08"; /id="PRO_0000116737" MFIFNVLTIRCTFHVLFAICYFCDHLLQYISNSRDSKAGLKIFLVFELAVTIFNTVMLQLANRVKNGLTLAILIVSVVMFVYHQQLIVNCKKMLAL O14068 YFF7_SCHPO SIGNAL 1..24; /evidence="ECO:0000255" SPAC1687.07; CHAIN 25..124; /note="UPF0357 protein C1687.07"; /id="PRO_0000045285" MASFHIIVSYVTVVLAIIIAITFAARRFWISRYRSIRYSPVENSFEADFNNGLNSSSFDIAQNILAQDTRAGLDEAATSQIRGLMKQLQCSFDQARLIYIRKVMSDNNVDSTGMPLDNKAVTKL O14090 YER7_SCHPO SPAC2F3.07c; CHAIN 1..101; /note="Uncharacterized protein C2F3.07c"; /id="PRO_0000304052" MLVRENNSNDRSIIEYVIKILLISGISRIIILILAMFESIRHIIFHNDTNPSDARKFQMAICRLSSQKSRKLKNPIESSTTSHKKKGYVRKCYECLQIQVS O14143 YEW7_SCHPO SPAC3G6.07; CHAIN 1..125; /note="Uncharacterized protein C3G6.07"; /id="PRO_0000116730" MSEQSSPYLTLAPADYEGEDVSNEKEKNSVIPDVIDYYNKGRQYYQSFVVYKATANTIFQFSYLLYIYIDLTKADQTEVLQFLKTYVEDESFVGDDFVMPKYTLVLPYRVYRDHVKKHGDIITPK O14155 YE72_SCHPO SPAC4A8.02c; CHAIN 1..142; /note="UPF0047 protein C4A8.02c"; /id="PRO_0000088523" MDVIQRIITLDRRSKGFYIITNDLVKKLPELKSFSSGTVNFFIQHTSAALTINENWDADTRADMNDILDKIVPESAGYRHTAEGLDDMPAHVKSSLIGPSLTVPITNGKLSLGTWQDIQLAEFRRQPHSRTIVCTIIGLRSN O14166 YDX3_SCHPO SPAC4C5.03; CHAIN 1..302; /note="Uncharacterized protein C4C5.03"; /id="PRO_0000116676" MEFSTSSFIFDDDTPPKCPLATKASFIFSVYIIIGLIISYLLQIFRIVRLGSSQGLSFSYLILGYIGVLNAFSNVIALQISPLTECCQNYYSKKQCFANTTGLIQVGSQVLIMGCVLMAFWMFLPRPIHFVAADDENGLPIPEPLSVTKSRKWRKASYGLLGVFTWGLFIICLSATVLSSNFAWAAFLGFSASFCAVVQYVPQIIKTIRHQSHGALSIPMMMMQTPGGFLIGYLLSRLPGTNWTTYMMYIVSACLQGLLLMLCMFYLHKEKSRRKREELQATLQEEESQRAVRILEAETGPE O14208 YDT3_SCHPO SPAC6B12.03c; CHAIN 1..302; /note="Uncharacterized protein C6B12.03c"; /id="PRO_0000116663" MKLRDKWKIYLGLTTIKVQCPCFFLFHNDENRTTTSNLDSVKSKKKRRKTISDASIVSNGSLVSHPSIDKGKLSILKRYKMSHRLTAIDKLRPLTVLVAWKQLNIAMRPIFPQHRYTEQDKKNWKKKVIIEDLNFLVLRCICACEAISDFEELLGNMRIGLIIDISLLGMNSNESSFLHYLVEVWSIFYLEILPYIEATFLPVTFAKFEIAQLFEEPMKTYWLKKSANIDLKLFSIWVFRKFVVMPKLKKTNRFIEIPQLNTQQQILLVQMISIISLIKPQDESEDLLMNWLNELTLKFLYV O14219 YDTE_SCHPO SPAC6B12.14c; CHAIN 1..154; /note="Uncharacterized protein C6B12.14c"; /id="PRO_0000116668" MDTNLNFSPSQSNDLSTSSGYENVLSHFKQAALSVTQLYQASTTEVLKAQKAGYNQALREVLELIESGASIDFISQYCLEKLASSDNDSSVHNHHDNSVLRNEDTQLQPHIVCNRTVRAGRPVLDEDDEEMNIATPHKRRVYDLNSSWMKRGRR O14220 MEU26_SCHPO SPAC6B12.16; CHAIN 1..344; /note="Meiotic expression up-regulated protein 26"; /id="PRO_0000096453" MNSNEIENFIYLNNTLLSEVPEPNSVFYTPKCFSNSKLPHQSDLEEPSSACSLSKNTIIDGGADEPYDSSDSCATFEFADFFKDNLDDFALDGPIININHVNQTSPYTHHNAEPLHDLQTFSSNLNHSNNRRQTICNFNMANDASKENETPYMVLNNKFNPVLTTEYTQQHLVQCKMVLENHITSRFPHFYTKLPDVSLVPNNMPHYPDEVTAKSAPKDDFYVPRFTRGHGISKLGLCPICSHQGEFIWLRTKTSAYWYHMNFVHGIHSKGRPYQPPIEFRTVRLRKTRNAIGVPNKKYMIEGKCHQCNKWIRCQGRKDVSVKIPEIFWWRHAHRCHIITTDLR O14256 YE6A_SCHPO SPAC6G10.10c; CHAIN 1..194; /note="Uncharacterized protein C6G10.10c"; /id="PRO_0000116703" MGPSGAGTRGGQAQFQWEEVRNDKQKGRYLGQSIYAASGRWAEGKDLEWWSKGRTTQSAINSENSDKEKYKKEILEIKEREQRMLAEALGLPQPSALALTSSKAANRSSTNTEKDSRSIAHSTSRSRSTSPANRHRRKEKERTRSNHRHGSHRRHEPYRTHLSRHHRHSTTNYHSKRDDRYERRREHSPNDGGS O14263 YFP8_SCHPO SPAC7D4.08; CHAIN 1..96; /note="Uncharacterized protein C7D4.08"; /id="PRO_0000304087" MNFVSSILIRWCDVPVYILLRKCVIYKFAYSSRKIESVHCAITDDEVMSYNNEDMVPFSAINLPIRFLIFYNAFRSNTSWNYNESQIGNLTISKQS O14268 YFPD_SCHPO SPAC7D4.13c; CHAIN 1..312; /note="Uncharacterized protein C7D4.13c"; /id="PRO_0000304074" MSLFIGTHNIKNSAIQLLKTKLKNEFLKGVKCITKYPENAHSIFKVQEYTGYKGVTFIVSTKWNLTVDSIHKLIPEIKSSPSACLLLVNQPYPVIEKITDILTKHGITNANLLEFSKSSLLHPFKRNRHLLSFVPYPMTAETLGDISWSFSRRENMKFEKDQQYILSKFKSPRNLLIPYPSFLIQKFLDMAILPPMAALRILFYQYSKASTMSLTDDFYNKYVLENLNIINNLQIFLHLDLEPLHIKSLAKARKRFYETDLKTTFLNAFSRDELLMLVNYFIFRGTELKLSVSMNLAFRDILLSSAYLNKTK O14287 YF11_SCHPO SPAC9E9.01; CHAIN 1..99; /note="Putative uncharacterized protein C9E9.01"; /id="PRO_0000303980" MADGLELSAELSVHTGTVTHTIFVYVFLGKSKRLKTFSDSNVGSVIKLEAGFAVWSRCEAANGEWMEADNEDRCRLYQIYRESKLKEFARYNVLSRVNW O14291 YF15_SCHPO SPAC9E9.05; CHAIN 1..313; /note="Uncharacterized protein C9E9.05"; /id="PRO_0000304038" MDSDDSFVKTAHVIETSTPENKKLSHRFKSVEIVPPSSSNDDPFGFSSTKGIRLSSINSNDLVNTLSKGFNETSNMSYNRILPSSPPTLEIGEIDYNEALQIRSADENQQSVPTVSIASPSTPELPPSSSPLLPPNGSESSSPIPLSLLSTSSLQQRKITPSNLSNTSKPMDSKQLERLIPVPHGHHLTRLRKKRRRDDDIDLSGLYETKSSSPPAIHSDEDPSYSDSIARSPVKSAFNLRKRRKGVKEKKILKTYHSQDKDTASDNDNNTGSSDEENDNLKELTPGKKEYLKSIKKYFQDVDDYQLHVVNEG O14303 YE87_SCHPO SPAC9G1.07; CHAIN 1..418; /note="Uncharacterized protein C9G1.07"; /id="PRO_0000116706" MDDLLNSVSFSNASNPHNAWGSENISNSNSAIPSITNDVSFSMEASVWKENALNLDTFNLKDINEKLDYTFGVVKPPKRISLASKDYIGITATSETNFRQLIRLGYNEKSLGELKQGTISRLLKEHMTLWNQERSNVNRKSNVLFCWSTAYQKQKRKTASYTNSPVTPPINDKNILLPEQSPLSNFSTTKISSINVPSDILDFSNLSSNEIPKDYSSSTALLNNTVAVKQDHKLSANTFLSSPVKLIERESNSCSTISINKEDEVVPKSPLSLDRKKVDEVEEHSSIAKLDSEEKIRETKKKNSSTSLSPDPTSDNFEWGSWVSSQDTSKNSSNLASASVDDVSEESQVEPNTLIFQNFSSPSTSLSAPKDTPAVIQSINTSFLNNERAGRGNIKTVDQNQLINRIVDKLPDLSYLVD O36029 YEKH_SCHPO SPAC4F10.17; CHAIN 1..123; /note="Uncharacterized protein C4F10.17"; /id="PRO_0000372358" MAFRAARIAFAWKATNPANTTIRQYIKETLEEAPEKISQTVKKATGKASKKIDENKDKSPQEMAENAKQSVKQTAKDAKDTDYQQKAKDAGKKIKEEFSQRSENVLEETRREGMNRDGGVKKE O36033 YLM1_SCHPO SPAC19B12.01; CHAIN 1..817; /note="TPR repeat-containing protein C19B12.01"; /id="PRO_0000106417" MVAIENKEVLFGGSLKSTEEYDQFFCPSIDIPKFLFKYWDSKPLGKNVSSDQFAETAIQMLEYFIQNNYTGPYLPIKPEIWLPQRLRDEATLKDAIIKSLTVEGERPYRLAPKLLFLLLSQTLFNYANSKDPLHIWYKARLDFLHQQMLKEHVSELFNQIMEGMHIVSSHVSSLDRDLQGRFTMEMGLIQSYYGRDTLALQLMKESAKVMDFHFELTGALGRRTKFQTFDTSQLVVLAKSRDRCKDTEQNKSTSTQPITFELNDDTLLEKISFKEDQKSLAPSEELDPILSSEDPNHPSKLDPLDASLLLAFCHIIKNNNPDDGLTREEMAPYAERVLVYPVNWSVYTMALLVRARLEGFKSRTVERSVLQMQALLDQLNDQLSFGKSPEGVDKPENDEGLGSFLPKPQDGENSASLKERLNYFYNLLMPSRWQLEAELAERFISVGATKSALEIFERLQMWDCVVMCHCSLNRQDLAVQVIKRELENDPYDFLLRTLLGDIENNPKHYVEAWELSCKRFAPAQRSLGKYYYKKGDLLQAMNCFNESLKINPLSYPTWFTYGCAALELQKYDAAMEAFSRCLSINPEDGESWNNLASAMLKAKDHTKEQAWHAMQQGIKYMYDNWRIWENYMLISVDVNKWSEVIRALRRIIEIKGKDEGERAVDVQCLDLVVNYVMQSCDNDASGLARMLNELLKMVVPLITNDVRLWRIVARYYLWRRHFAESLNATLKAYRILISSPNVTSDEATWNKTVEGALELVEAYANLGEMPGRMGGVVAKDWKFKSRSVLRSLIGKGKNIWENTESYQKLESELENLK O42653 YF9E_SCHPO SPAC10F6.14c; CHAIN 1..535; /note="ABC1 family protein C10F6.14c"; /id="PRO_0000310290" MLTSWRTISLLQKTTSRFIKRSKTYADVRYNSQALQNHGVPGNKRKWMKRFVFVGAAGIGVYAWDRVYNAHALTRSIRTVYTASIIAADYKLNFSEKKADKIDALHQRVAQRLFKTIYKNGGLYIKMGQIIAMQSNNLPEAYGKAFQGMFDNAPQVEWEELQDIFKEQYGRPVEEVFASIEKRAAASASIAQVHRAVLPSGEKVAVKIQKPDVAKQMSWDLLVYKYMMYVYDKWIFHIPLYFTVDYVSERLRSEVDFTTEANNSEHAREGVEETDYLRDKIYIPKVYKEISGKRVMVTEWADGIPLYDQTALSEAGMSKKEILTNLFRFLAFQMFHSKQVHCDPHPGNILVRKNQAGLCQTVILDHGLYVFESEKFRKEFALLFTAAYSLDKKSILQVMDAWGIGQPELFANRMLNIPMDEEQPHTGEKIISKKEAFQQQLAERKKFIGFLQDCTRLPKELLMLGRCLMLIQKNNQNFGYPVNSIAVMAKVADKYTTDKPSPTWYQRLLSPIFWVFQHLFYPGNFRLPELTNDKK O42883 YFQ6_SCHPO SPAC8E11.06; CHAIN 1..33; /note="Uncharacterized protein C8E11.06"; /id="PRO_0000304072" MLLVSRNICRIKGNTIDWRNLKKDLSMTWIILK O42968 YB93_SCHPO SPBC1E8.03c; CHAIN 1..477; /note="Uncharacterized protein C1E8.03c"; /id="PRO_0000372349" MVVIANKGALWAYYCKRLLNSVTYMMYPLIRKRTMKKLLLIVGLLLACSTVMRRIPLFHESFHLPSLDPRASTTTSQKFQEYRSDFLEKLETAEPPEDVIMFTAYGLGVHTHNLFMLACDMAKTSDSQIRFLLLTDGTILPEALYDYNRETVSTCPLSFLSYSTGVERLSKELILKDLLSLQFQQALLAISPSVIVTSEHSPLVMFQAINPYLNNNYYTHDTVDTNALEENSWITKLDMQSLQHFRTPRINVVLIVEDGTYKYLLNLMRDLGRDFKNSEEYPHLFIHLFMSENIPNLSSIRANWPQHRLFINLHFNQKDLNLIEVWTPPNDYTYALVVDLQPDSPPQLSSNLITWLKYKILLIYYHKSSSTYKNNIAAIVPSFDFSNEEAVILSQTINSNIVLFAPVVFQKFQEYMAVRLLNPNFELPESNGIEFAHEDSVLGHSKPSLTEFHAILGLYSLVISYNHFEGSLSNEYV O43018 YGV4_SCHPO SPBC354.04; CHAIN 1..163; /note="Uncharacterized protein C354.04"; /id="PRO_0000116765" MSENPAHKDLDSLQVDEKAKSWIAEKVEEELRRLESVGAKAIPLDVKNYSVMLDEDTDTVVNRIELMTSFDFDHVQQILLSAVQPYPYDKNLMFVYLVILTPLPHPMLIPYLFAPKVVGKNLLPRADGLVENTLKRWTFINDKLKRSDTVVREFQEIEEEATK O59779 YCY1_SCHPO SPCC1235.01; CHAIN 1..658; /note="Uncharacterized protein C1235.01"; /id="PRO_0000303999" MTATIIAAITITTIVIITPMEEITTMTIPMEEITTMTIPMEEITTMTIPMEEITTMTTPMEEITTITTPMEETTTITPMVETTTILPMAAMTTPMVETTTIPTVETTTTPMVETTTITPMVETTTITPMVEAMITLMEETMTTPMEETTTILPMAAMTTPMEETTTTTPMVETTTIPTVETMTTPMVEAMTILPMAAMTTPMEETTTTPMEETTTTPMVETMITPMVEAMTTPTEVVGRSMVSTIRTTTPMEAMITPTVETTTLPTAAMTTPVEETTTTPMVETMITPTVVTTTTPMVETMITPTVVTTTPMVILVMAVVMETTINIVGNNDSIPSQNFKSGKTFVSNANSSNSNDGSSSKSLDVGSFVNAFKQLNVNDNSSNNNSSGNTDSSTIGYAAVFAAAGKFFSQHSCDLASGNKSAQEGQNQFLSMVESEAKNLMNKTNYSANQSQNGNSQNSGNPVSQAIDLAKSLFQNRNLLTKLAQSGVLTNAAQGSSGGLSAAAVSGLIGSFMGSSSNNSNSSNNNSNTSNNNSNTSNNESMVSKLSSLSGMASSFLGSSGNNNNNNNSNSGNYNNNNSGNNNQQHQQSSSSLQGLASSFLNSSSGNSNKQNYNNNNNQNYGNNNNQNYNNNNNSSQGGNSQGGSGLLGQAVNMFLKS O59783 YCN6_SCHPO SPCC320.06; CHAIN 1..289; /note="Uncharacterized protein C320.06"; /id="PRO_0000116553" MVLISNTLHCADAYSSADSKHVPLTLSTRRINLQSFQSISARNCGSDARVLDFVKSIDNDNSWKRRNLDSKRNIGSRKKNRFLNDLHILKQAADDPDEVVYKDLFTHRPAFGFLTVGDEFYKDGVNNISSLLTSSSNQRFNDNHHKSIVKRIRHEIKCYNSLQLVLLLDECLNNIMNEKLYAYDHDHSPAIYASESFNIKAEIDTSSFLETQRSYRIYMLIDCPSNPKATAFARYWMHLICSYYGIYTTSTQILSNKIMTLGVSKKRKHLSFKTLSELLNHDELTNINR O59813 YCT3_SCHPO SPCC794.03; CHAIN 1..554; /note="Uncharacterized amino-acid permease C794.03"; /id="PRO_0000054177" MRLFGNSKEQGICQVGESDVAVSEIKKDEALLQKMGYKPKLHRTYAFFENFASSFAACDCMSNIRGSFYIGLLTGGPSAYWITYIIAIPLQLISAATMAEVCSALPTAGSLYFWASAAGGKKYGRLIGFIVAWWVVVAWTSFVAVNCQSTTKFIFGELPVFNSGFSVSSSDVKFRAVQWAVGEAILLVCVLLNFIPPKWFRYIFRVSVAVILLDFVLNMIWLPIAVSTKYGFRDEAFMKSTNYDLGKVNNGWSWCLTFFCTARILVGYDAAGHVAEETKNASKTASRGMFYSAFSNAILSTGIIVMFLYCLPPSNVMYELIKSNSQQPFVSFYAYALGKRAHVFMNVVGILGMIFDTSLSIVASSRLVFAVARDGVLPFSGWLRKVDSHGQPTNAVTFIFLISAALLCSNLPSAVAFTSLLSAAAVPTIMAYAAVAFGRLFLSRNDFPKSEWSLGKLSKPFQLITFLWNLFTAVILFSPKAYPVTGKNFNYAPVIFGAITIFGLISWLSIPASRWSTFYDASKLDSNSFDDSSSDKKSLEKAASIAEGSITQII O60082 YQK8_SCHPO SPCC1494.08c; CHAIN 1..274; /note="Uncharacterized protein C1494.08c"; /id="PRO_0000116891" MSIFIPKARRPTFELHLRIHDVVNIPLITGVIFVKWNIEGIHSRHANDQTEAEPVLEHRVTWEYETCVSVRMIIDNDNLLKDKFLILQVLCDSHTDSGVIRLGILKINLTEYVYVGQDTRKYLLADSKINATIRIGISLKQTSGNKDFRVSKTLGKPQVFSGLTGLLTDGKELKRRDDEVYTSTGLASAWAEKMLHSIKDFNQKTTVFHMHTRNNKYDTREIVDDIFFGGTGWAEPPKIADIVDAAGDTDLISLEIRQKSWVLPSEKVLNKRLP O60083 YQK9_SCHPO SPCC1494.09c; CHAIN 1..157; /note="Uncharacterized protein C1494.09c"; /id="PRO_0000116892" MALELTEHQLNKLRDFLDEILLDVSQKYQKKFHPGGYQKLEELAFDLEPYFQVVSSIPLEKHTFLVTNFTLRGIDFFVDTIVGFPASPETTFKVFSLLDSLCLRLIQSGNLSTTDTIRLKSLMENCRMVVISKLSDVQGYEMDCASIFEKSLNSIDF O60092 YO2B_SCHPO SPBC14C8.11c; CHAIN 1..159; /note="Uncharacterized protein C14C8.11c"; /id="PRO_0000304115" MQFDDIITKILKVGIISILFIINMAKNAVNSHFGIRTPRSVCHVRNRENIYLYWTTFDAHKLPNGGNADMAHFSANCLHAGHTVKFVSADRLGSTTWECNIKFGILSFPNFGKDDAAQNCFAEPSMKSISADTQHISAREYISGTSKGFKTATPKLLNI O60098 C14F5_SCHPO SPBC14F5.01; CHAIN 1..278; /note="Uncharacterized protein C14F5.01"; /id="PRO_0000116880" MKRSYKDIIRFLKLIGISHSTAIKLVDGILPVMIGLKTSYLVDCVFLEISELREIIEFVGPDCLRGIYFTEPISQCFVLHVANWEEWSSIDSLVPIVVDLPSKKQNRLLQSCITKHVDRLLDLCKRNLSTFTIDISSSWRQNIIENNEQKEFECTSTAITGCLLNYGATYNYDHTLFKDNGLSCETLKLYTLEVHSKKKDVSDTLIQFSCVNQFEEPVTSNIQRLTSLYQTRWKRINSEEKRNWEEWIKHKYKIPNDTNIELEFCFSVTDRKEQSVIL O74313 YOG8_SCHPO SPBC15D4.08c; CHAIN 1..138; /note="Putative uncharacterized protein C15D4.08c"; /id="PRO_0000303975" MPESAPSTPPSVNRRHEPEMLSEYPSLMFEHSYLASPSSPIDQVHDELKHSQKRPRLTNDEETIPEEDDSTVRLTDSELEDPVSSNELIQTSCHLLTSVLTQLQTNLDKLKDSHQKALLRIQELEKKVSELSKNNKDS O74337 YH24_SCHPO SPBC1A4.04; CHAIN 1..249; /note="Uncharacterized protein C1A4.04"; /id="PRO_0000304100" MESCTRSSLQQLVAADSKSSNFCFRNLSQSSNNNVSYASSSNRNFVPQNVLNNEYQSFQHSSTSQPSVLRQGKNAFLKPSQLSFNMNSSEISNTHWARDFNILTSNFASSSVTSAPTQSSHISNFTNSQKYFANDLPNSLTDQPLAQPSASQRSTWLPCSAAVSTSSPSSDPFFDSYLEQAFEKAERLANEQQKISKVEKTFGTLDSIGTEQDDCFDPDYSNLPLFPQENASPPLFRKASCNSGFTTKC O74342 YH2B_SCHPO SPBC1A4.11c; CHAIN 1..124; /note="Uncharacterized protein C1A4.11c"; /id="PRO_0000304081" MPEKDWIGEFGPSKFKSPIDKLNQLLPESNDPSILYETSQHLLSEFDKTLNDSLRVLNQQINQVSEVLPRLPTMISALDRESKRLFESCEKMDPEPSALMPLQELEKIRSNIQLTISQIDNLTP O74437 YJE6_SCHPO SPCC1682.06; CHAIN 1..238; /note="Uncharacterized membrane protein C1682.06"; /id="PRO_0000304079" MPDEKLPQYNEVWNDLEKGCLHSCPSYSVNNHVNNPIVKQNSTLTQPSLRKKNTMAAPARLRKRSENVRLTQARYAIFHIFLPFILTLLLYHNFYNYFDQALADLNSVVKYVIETIVLIFTYVMTVIIVYFSFSLIKLAFEEAYVYAPSVAKANEGLAKAIAGLAKYVAKAIQGLAHIILSLLLFILGLEVIEQDEETGDVEMSSMRGQAITTEPASDNTMAEETDCNTSKDVESGSN O74449 YCG4_SCHPO MOD_RES 176; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517"; MOD_RES 178; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517" SPCC16C4.04; CHAIN 1..266; /note="Uncharacterized protein C16C4.04"; /id="PRO_0000116545" MASATLPMDYKTPFGYAYKLYVEGKDEHSLYILDNYLKNANCSENTYEQALILCLTIMCEQRRSWTEMEEKLLHNYQGKIPDSIVVNWIITYLENSEFTKENYAQMINSLYRYQDAILKSELKDSILPKLVNCACSVQLTEPLKAILANSRGELENSLLLRIQAQEEELKMNLERSKTPDPSEDEGEFALTLKLQFSKVSRLINQGLTPLLSRLQLIDKNIKIVGAIFGIILLLFRLKKYISHSKKSAFSPQRWKFLLDQFLLAIS O74506 YJD3_SCHPO SPCC594.03; CHAIN 1..108; /note="Uncharacterized protein C594.03"; /id="PRO_0000116813" MWVTCHLLKREKDEMKKKWREWAKEVCQFGKRILCISITDAALVNLEVLEPKNFEPGTLDGAGLFGCWSANGLGIALAYEITNSRFEINSGYTVKVKCLKRFQGEARG O74780 YGB8_SCHPO SPBC25B2.08; CHAIN 1..125; /note="Uncharacterized protein C25B2.08"; /id="PRO_0000116755" MLPHQNSSYTRQGTNDAQANDMRSPSQLPTSVNIEDPSKLCISSEKLNTPMHNRSRSGIKKHTSVKRSRSFKLFDTLFFGILRLRKQRIRSVKKVRSISSPVLISTTSALALATIEQQPVIGECS O74886 YQE2_SCHPO SPCC576.02; CHAIN 1..236; /note="Uncharacterized protein C576.02"; /id="PRO_0000317100" MPTILVINPNSSTFITTSMEEKLVPLVPSDVKLRFLTCPQPGAAVIDSITEATLTAALVFQALTPSVLDGVDAIAVACYSPTPLVDMIRESFALPCMGIVQASVLSALSVGQRIGILTSTYRSECLLYELLDSFGVSRTRVAAIASTGRTVLQLSQMPSQERETLLVQKAQELANTKGADVICLGGAALAAIRDQIQVAVGPNIPIIDGVHAAVELLAGLARQNLHTSKFGIYTYP O74913 YJ72_SCHPO SPCC757.02c; CHAIN 1..405; /note="Uncharacterized protein C757.02c"; /id="PRO_0000372341" MAEEGYVAIVTGATGLNGAAIIKRLSEDDNCKTIHCISRSLKDEYPRKIKHHSIDLLNEEPKDIAKKFSLEGVKGINYAYFAAYKEENNEEKLCEVNGNMLRNFVQALELTSIQTLRRVILTTGLKFYGLHLGEVRLPMIETDIRVPETFSGTPNFYYVQEDILKEFSNGKKWDYTIAMPNDICGVSKGSYMNEAFTIALYALVCRELHEPFRFPGNEKFYLGFDDISYSKLIADFQLWMTFKAECSEEKFNIVNGDIHSWSRTWPKIAEYFGVEVPKNQFATDFTLSTEVTLSTPSPINLYEKELGIKHTPNSKIINQISLQQWVKQKKVQDAWRTIAEREKLNAHALEVGTWAFCDFLFGRTYNVISSMSKARKLGYTDYYDTFDGFKETFDELKKQKQIPQN O74917 YJ76_SCHPO SPCC757.06; CHAIN 1..116; /note="Uncharacterized protein C757.06"; /id="PRO_0000304057" MVNPDKTSRVYCKYTCCGYVGSLDHDKQDAHVCKLGCQLFYGESCYKEMSNALNGTSRPIFLLSVPAIEVAQLQTLGEMSLKFLIKLIVKMTDCPRQSFSCSELITVLPTVQKLTF O74949 YJBC_SCHPO SPCC553.12c; CHAIN 1..521; /note="Uncharacterized protein C553.12c"; /id="PRO_0000116811" MSDSFDAAASHFHARSSVNDSSFHLSRQEEAELLEGALHAPYPEELLFDDDEYTAKTQYDGPRYAMPTMFYPNKPTPGWPLNYVFGNERSRFEKILSNFVLRNLMLQVLAPCFVLLWCAVPMPRYEDSQGTVRIRFWFFLIFYYGIYNAVGLLWITKLFHIYSVNWCPSKLGGTITYILFWMFSLLVGSLVVYFTAWRQITFTWITLMFISMIIPIGISFSKLWKKHSRRTAQFLTQLALLEPEVRSNAVLETIGWKDAYAHYSWFIVVLLVTLLVYIVGEYLTNLYMSTLPHSSTVAIMYVYSWTGTVSLCNLVSSWILNTKTHSYALVTVFKLYFELTLQVYVRNLYARLESPQQFVLVQIASSLTMMSVIPLITMSRTVFRLNVLMTKSMDSYVVYRKNMGRNFYVKCVASNVSMLSFLGWSLILHFGSNAPLYPYFSFSKEEPYSFKLTFYASTAVWISEMVASYLTRLIMRKFYDFEVALEAIRDFVEYPDMIPTFIAVSIHVLQNVVFSIISLHF O74951 YJC2_SCHPO SPCC736.02; CHAIN 1..286; /note="Uncharacterized protein C736.02"; /id="PRO_0000304103" MGKKRKQTIKNDYNEKITKRKVKNNLTDGKARALTVFESLPLEVLRLIFLLSNNSNLAVTSRSLRHRLSLRNNTPIFMPIDFTLSMVPKSIILSIQRGLLRRYFTLQILTKIDELVISGFVKKSPNEDIKDGRVIHAGHEGFIPKRILFLPNAEDFIAELEHRNFLFKASSLRNGFLLALKQRNIPVIRQVGKIVTERLISIPDDEVEFCFLTWFEYTMEQNSVELLDIVFGFWNNIIEKRFSKSFIDSYLTRLVDIAISKNVTEIMYYLIEKGAIPQLPNLLKLF O74973 YOKC_SCHPO SPBC4B4.12c; CHAIN 1..110; /note="Uncharacterized protein C4B4.12c"; /id="PRO_0000116873" MVSGNDQQVIEYTSVLKEFSDGVDLMELKENFLYIRTREKIEAKLIWAGEWEWKPVNETNENNLERGRQYPSANSALMENSPEFAKWFHGQLFNRLCVLGSTSSSRKDML O94245 YJ14_SCHPO SPCC737.04; CHAIN 1..421; /note="UPF0300 protein C737.04"; /id="PRO_0000118860" MSISNQSGLDILREVDDEGQENSFLRKTTRKIQQFFKSDPGYQSRKAEYNSPAKATGDVNINVTSQDWLSKLDRNLSIENLTGKSLGIVVVSGRNKGLIKNPFLGGLVDIVMRRQDKLYLKSVEQVSSEYSPMQEQVYEFKVDMPLVQKRLGAFLKKNRVDGLSLSMHFSTGNYSLPVLIRHVLLYDYYTDDMKDSLWRAMIIYVSRQVTSNKYTKFHLWCVQKRIGNIRMYLVRPGDVYSFQGQTSWAAICNKSYMCNIQLEQSPEVSVKSSLPKYSNEPIFQSKTISQEEVGWLLFMLSIGNHARAFPIQNYLANTVMETVLPVELRCPFLSRSVDCEIFQKNTKRRVMEKWRQEFKKDLNVCEELEFKNVKKSGYMQPLFDLTMPLGCFDSLETKEMFYLRHNIAGFQADLTPYPMRI O94249 YCM2_SCHPO SPCC13B11.02c; CHAIN 1..138; /note="Uncharacterized protein C13B11.02c"; /id="PRO_0000116552" MHFTLFLYFDAIRHANQRRWCHECTIKIFRRSFDIARHTVHLCVRKIFSLHPLTETDFLPNELRSEEDQTLIGIFWFLPPIIEGEDERSRFPRRSMSENHLIITKKSLHNVASKDYIRGSHVPCFQPYEDVYELNIEE O94293 YOO8_SCHPO SPBC887.08; CHAIN 1..124; /note="Uncharacterized protein C887.08"; /id="PRO_0000116875" MDLLAIDLDFDVSESKLERNKRLKQKVSIETDGWTPRVQCFGHLSKNGVVLGEEAYILEQSKFAAEEQYYLGNYSLAKKFAFQALDVPTDSSSIEYHRLSSGEINEIEDIIRRCEMKLENKQSN O94299 YOOG_SCHPO SPBC887.16; CHAIN 1..109; /note="Uncharacterized protein C887.16"; /id="PRO_0000116876" MARTNLQYPYKVLWCAQVKVVKTGLINFFAPSIQRQRERVCEGYLHETPLLLMQVVEREAITLAKTEFKNSFSNLHFFFLFWLLNFILFFRIHLYSCNFRMSIICEEYY O94341 YHM8_SCHPO SPBC1271.08c; CHAIN 1..140; /note="Uncharacterized protein C1271.08c"; /id="PRO_0000116777" MLISRSSMPNLQKRHSDFKTPVYISRSISILNKIFHPCMYIYSRGITNDTYSSDTYELDWYDLGFVHFSKWVELAWCFLTLATWSFMKLLKTLRIVIYICTSDHWTHSLRFYYIELSKILLYLLICGVSLYGAIRIFINL O94349 YCB5_SCHPO SIGNAL 1..19; /evidence="ECO:0000255" SPCC61.05; CHAIN 20..469; /note="Uncharacterized membrane protein C61.05"; /id="PRO_0000371801" MRINFVLLITLILPWFVSGDSSEEAVDAPLDVKDDTGNKDYYKDSTGAYHFDKLIVTPLEYRDGESWKQSVIYCDLIFAKENKEEKGSFVKAQLKEDAEHPFIYRLLKLQTPLETYRGFIDGKNTEILDEIKSINLFEDFLSESLVPEISPSVNIPIDETALYCFIGIQETEPIRIPWPVLTVEFYGDAPPPESYFRTIKSTLLAISMFLGFITLTWLLRCIKSQSGVQPAQISLAFWVFIFVFTHSYQVYSMVAIGRGSFSTWYVVSFLFSLVFEEGLEQSAYTSFLLVLCFGLGITKPALVKYYVYLAFVAFVQGLFVTFAPLSYPVMSFYGVRGILLKLIWNIYTFVYYGLPFFAVYRLYKQAGESRKLGFEAKYSLLRTCYIALAAVTVSNCLFLGVVRPLLGSQLSLGFQLITSCITFVDFLVFAFLFDCSKFVFLKYQPIPFEWYALESMESLNLEPAPDRKV O94369 YG03_SCHPO SPBC1604.03c; CHAIN 1..330; /note="Uncharacterized protein C1604.03c"; /id="PRO_0000116751" MGAILSTPKTPIEVRRKRIVPLFRANHTRFRPVDEKNRINAVPLLLLGCLYGKYKDDDFVDFFDKAIPLLVPQTHKGLDTYEIDVSTYKTHIGHPKFIEPFVLFYGDRLVHDARYNLHELVWQTLSRNPEYIKGLCYDSCTPLANLAVGLSLNIQEVLIDCFATAACFTTEDTSINPIPTLPSVFCTIVDDEGISLKELLYIIEESLLKNAIPDPFSVSTYTLKSAFEHLVKKDFLKYYTAYLASSAVDYIDAYFTESFGSFFISRLASQFLVSFQTLPSFFSFPLVTDNWQHLAALPFNSTYETFRAFDHPSTNGPAIGPLYNAAPAPR O94425 YHK5_SCHPO SPBC660.05; CHAIN 1..143; /note="WW domain-containing protein C660.05"; /id="PRO_0000343150" MSVYQTYKGLPAGWVAQWDPTYQAYFYINETFEGAQPQWEPPIPGLHIPPPPGTTTVVYQKDVPRSSDGSRSMTAGLGGFMVGALAGSVLRGHRAYYAPPPPRGPLFGPRIGGGHHGPLHGPHGGFGGRGGGRMGGRGGRGRR O94426 YHK6_SCHPO SPBC660.06; CHAIN 1..273; /note="WW domain-containing protein C660.06"; /id="PRO_0000343151" MSVYQTREGLPSGWVAQWDAEYGTYFYVNESAQNPQPQWEPPVENLKLAPPPGATSVNTAVYNNNNNTSAANTNAAYNANTAANANANTATTTNAAATTSAAYNPNAPANTNAAYYPNAAATTTTNADGSDKGLFSGLTSSNGYTTGNSYSRPSYVAPVAAGLGGLALGGLASHALGNLFHHRGHNGGGFGGFGGGSGGPPPGPGGFGGFGGFGGEGHHHGGHGGFGGGPGGFEGGPGGFGGGPGGFGGGLGGFGGGPGGFGGGPGGHGGPGW O94433 YHKH_SCHPO SPBC660.17c; CHAIN 1..172; /note="Uncharacterized membrane protein C660.17c"; /id="PRO_0000304082" MEQLRKRVVRFTNNDDDDFEPVFLNEQDQDAFVEQLRLTNNRDNRMFSIIFSFLYLLLIVPLFLYPEYWAFKLVELLSLFYCAYVMYFLPLEVGLFNPKTPNKWKFLFILNIGVTALITVLGWSQHTSFFYAFLNIRTLVCGITIFTEIARYSMYHSTLSVEKLDEMRFAHM O94440 YFE3_SCHPO SPAC637.03; CHAIN 1..269; /note="Uncharacterized protein C637.03"; /id="PRO_0000374021" MQITRESKYIIGLVLALGVSFATLLAHLFTKPSLEWVYNHHATPFFANKFMLGGYLLVEYLSFLLMIVPLLMLGDQVNDFTFSIIHTSIWYNVFVVFTVWAFTREKLYWTAFFSLCLFSSSFTMYGQSLRLRNGFVEMISMKLPSKLVFGKSLWFVVYAFSAALHCTGIGCRVFSNVFIWFFAAMYLVPILGFHDWALSLVSAYLFLSIGIGQMFIHLFALQHIFAFIIAGLMTLFAALLFLLPYRQRRAALTGESAPLLQDNNAGPAV O94470 YBRE_SCHPO SPBC23G7.14; CHAIN 1..131; /note="Uncharacterized protein C23G7.14"; /id="PRO_0000303932" MSKEDEEVLESYFWTLQESIPLRRRIREIRELQERNKNKYEQLLQARKDLDRFRSNLNVQQEQLQNEILGFKQDVKLLNNVLVSYSSEELEKRFEESLLKEKATSMEMESKLCSKSITPLEYVSWLLNSIE O94484 YC73_SCHPO SPCC417.03; CHAIN 1..46; /note="Uncharacterized protein SPCC417.03"; /id="PRO_0000116537" MLPHTAFSNHIHYHFINEAPFRLCIYTLFHAHTCFSCGLSLSLMEV O94578 YQ75_SCHPO SPCC1442.05c; CHAIN 1..177; /note="Uncharacterized protein C1442.05c"; /id="PRO_0000353133" MSYYYETEEVNNNPELKSNFPWLADRIHEGRSSIFHALGYVGLKTENAFGWFLSTERKTISTAKNEVFSSDERKLPGVAYVVVGGMAGNIFARNRIAPARWLITSLSTAATFMFCFPKTSKNIGAFVEKRFPAIRKQRMLVLEQTQKNIQNAQKSMTSAVEGVQKHYENAVKKIKGD O94583 YQ7B_SCHPO SPCC1442.11c; CHAIN 1..182; /note="Uncharacterized protein C1442.11c"; /id="PRO_0000304042" MLIVNRNPKSLVRGYCKKDIVLRNLDGWLFDMITISTIFKLYNQICSLSSTDRKKTSISNKLQQEFCIMDINKVGRNFISLGKIRSSKRRNAILSYQTIISSFPHNHVQKLFQRTQSTNMIYTKLEYFGHSLFFYFTAFTLSFKDRKILMQADVFFRLKLVFKIAFFFTQTTFLNKKENREL O94592 YC82_SCHPO SPCC622.02; CHAIN 1..127; /note="Putative uncharacterized membrane protein C622.02"; /id="PRO_0000303961" MAANISKLEAIIDNTPNSSPDPEVSHKLWVSSLNKFQYTLPLLISNFAGLGIAFIYCLIAFIREMSHPSSRKDTMEHGLPIILCSTLMLVGNILYYFLSKHPLKVTVPEDLVQIPMQQMSSPAQEAP O94593 YC83_SCHPO SPCC622.03c; CHAIN 1..132; /note="Putative uncharacterized membrane protein C622.03c"; /id="PRO_0000303978" MNPKKSIQLWELQSLLKGATYKKLIEKKTYEAGKERADNYDFLFMSFISFIVSCRLFILVFTFIFKGFPSAIQVIAMIDAVVNALLILIVLAMLFIGSRKLTVEIRRGEVEDFQENLKAREDTFNSSPYQRY O94594 YC84_SCHPO SPCC622.04; CHAIN 1..140; /note="Putative uncharacterized membrane protein C622.04"; /id="PRO_0000303964" MTQPDIEIVIKEDFTYRECSDVANDVFKKTQWLLYVFLFIIFANCVVDVKYYFEGFSHSLLFVYFFLTLIILLVSFMGFHYLNSIPKPEAEPDYRKKQESKNQDFLKSQSNEPLEYASSSAVELEKEKNTREGLTILESS O94596 YC86_SCHPO SPCC622.06c; CHAIN 1..122; /note="Putative uncharacterized membrane protein C622.06c"; /id="PRO_0000303962" MSPKESIELQEFQSLLQDEAYEELINKKTYEAIKYRSNDGILPIIITLFIFSFVISRMIIFFISLFNKNTYCELPAVADAIINSIALVCIIVILYFSSRKLNVEIRRGEVEDYRANLERNQR O94645 YBV3_SCHPO SPBC21.03c; CHAIN 1..239; /note="Uncharacterized protein C21.03c"; /id="PRO_0000317092" MTEDAEKRRYWLMKAEGEPRYVKGINVAFTFEMLEEITEDGKMESWSGVRNYEARNMIRDEIKIGDYAFLYCSNCKFPHIKGVMRICSNSHPDDSAWNSNDPYYDPKSTPQNPRWYSVGVQSEYKLDRPVTLRELKMHKENQLKSMELLNRSRLSISRVKPEEWKFIHELSKQPEPEEIIKARLQEEEKVAKRKRKLNLSDGENKAKSPYSSISENDASLDIIKRSRIKDVRSQKDNAL O94662 YBW4_SCHPO SPBC651.04; CHAIN 1..237; /note="Uncharacterized protein C651.04"; /id="PRO_0000116525" MSSAELGKLHIYASPEQWEKWSPRWKSIVFRTQYESIFKNPKHHGEKKPFHCLFKLAGTMKSISLSHLDIPEHRMSNAVAFPITTSTTPMQLDVTLQFRGHKIPLVVGEASVSLEDIFTHGTVESVIPLFMKKRHPEAYLRIKLVYTRSKRKSARKHKVPSSFHRFSGRRGLGIHYNHSGSQSSLITLPLPQKQPDFLRMNNDTNELKTNGFEPIRFVFTTTPYSPASFEVPKTLKT O94696 YG1C_SCHPO SPBC83.12; CHAIN 1..161; /note="Uncharacterized protein C83.12"; /id="PRO_0000116754" MKRVNFTISGHGYILIKPNYPDHFNYRLPADMKFYKCVLTINYISVSSMSGPFTGPYEKYSSGYFSEFGPQHLFSINRYHGLRFSRQSSQEYDSVGHILYSPITYYVSGAEHVTMDSIDQRREFQDSIYTHDSSDSENIMSDSSQSECDYADLMINLDKLI O94713 MEU27_SCHPO SPCC1259.14c; CHAIN 1..736; /note="Meiotic expression up-regulated protein 27"; /id="PRO_0000118856" MNSKIAYPEIKISGAFRPDKIQEKGKSNRCDTHCSGSSWTSFKSKILKICAPLCCMGSDNDESMAEMPLEPQVEPKSIENNYTLKKKNEEGFLSQQENKSSNQNPSKANNLFDKLGVSKPITFIACILQLGGTSFMESELQTKLSTINSSPFKSLSQYWNAAYNKKESISSSTNSNIKLHLAARKYQTKPEKFNENSSISQVTSAIKATKAFSHLTQPKRALLKESNTGDKDIFKPRYPQLLSCRFTTLSKLAPINNSKSAPKGTHKPNHSENAELKDIKQSSELSDLSLSSQILYPESTTLSEISPIYDSELAIENILESKCFENEQAIIEGVKDFTEFPDLEETQIIYSDLIASSEVSPIYDSELKYESVLESKSSRNEQATIKEKKDNERVLDLSQQCTKFLFSDQKVITPSFCKFAQVSDMCSTEIPWVNFFCDNLDICIEDVQFKSKAFFPPTVTITIFEHEDKNLMNVFDTKNGTSKTLVKPQITNSCLENMLSLVNKNSCIKRLHLKLSKGIMDIKVLTHQLMLYDLYPPAHQTYLWKALERLVNEKVSLGELTPVHKVAAEKRIGDIRMHLIESSDIYVVTENHRWLHIVCEGFNCFLELPEVLHGKKFLKVDEATREDMLMSAETPDDILWITTLISTGSSMSHFPLHAYLEAKERQEFTKKNLLLFCKEDEFLYSDQENEDLLESFERVISEELSLLKSNEPSDISLKKRKRRKNCEKRILGTMMY P0CAN9 YK1G_SCHPO TRANSIT 1..38; /note="Mitochondrion"; /evidence="ECO:0000255" SPAPB1A10.16; CHAIN 39..143; /note="Uncharacterized protein PB1A10.16, mitochondrial"; /id="PRO_0000373861" MKYWKYLSQLTIRRPLTYNNALLYRNRFPSILTWKRSATTQPDDTIFKDPVMDEQVQKLEEKMSSLVVNDPELAQKVGRLRQFFEKYGLEAGSKPSPLTILKITRDPEFKQLAETITEIFKKSGIQNDPAFLELVRRNLKKEK P0CS84 YI4F_SCHPO SPBC1348.15; CHAIN 1..129; /note="Uncharacterized protein C1348.15"; /id="PRO_0000306379" MSIEFDDSSRHNMNMTQLMQLGAFDRRSGDDFMVQDFKNGIRDCSGIPVNNRNLAFKAYDAVKQKYDSSIKVFNIQDITIKGATWQHHNCQSTGKWYSQLYDYQNTFIGKQEYNILFDCYSYLKYNLNG P0CS85 YP43_SCHPO SPBCPT2R1.03; CHAIN 1..129; /note="Uncharacterized protein CPT2R1.03"; /id="PRO_0000416662" MSIEFDDSSRHNMNMTQLMQLGAFDRRSGDDFMVQDFKNGIRDCSGIPVNNRNLAFKAYDAVKQKYDSSIKVFNIQDITIKGATWQHHNCQSTGKWYSQLYDYQNTFIGKQEYNILFDCYSYLKYNLNG P0CS87 YP41_SCHPO SPBCPT2R1.01c; CHAIN 1..269; /note="UPF0494 membrane protein CPT2R1.01c"; /id="PRO_0000416942" MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDLFTEFSKFHNSYYPDGRISTRSNFRWPLLIIWSIIIVFAVDKKFEVQKFLSIWINENRFYSEIWVPIAIYVCLLVLMLLSLIFFAEFAVLALRVTGVIIAVLGMIIAVLGMIIAALGATITGLLYFGHWALYKLVILSLGFKIVTPGDVCVSNTLPTHNGETALHSETTVGSDIEQIELQNMPTPVKK P0CS92 YKV6_SCHPO SPAC959.06c; CHAIN 1..225; /note="Uncharacterized protein C959.06c"; /id="PRO_0000417962" MGENIEISTKVIENQEIRFRCYKADSTKIAVLAHPYAFLGGSVDDINIIALSKKINSKGFTVYVLDATTRRSALLSGKHDTMIFTLFVKYITSLNHPEYLLLGGYSYGARISMHKSITLAIDKRISHVSYLFLAPYLGLGSSILSWSWGLGFESFSTDSKVLFVWPDNDEFTREGTFETTLAKLKNRCPETTPLKLTDCSHMLSPSSRKILLETVDKWLASALNV P0CT98 YM01_SCHPO SPAC212.01c; CHAIN 1..280; /note="UPF0494 membrane protein SPAC212.01c"; /id="PRO_0000306283" MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDLFTEFSKFHNSYYPDGRISTRSNFRWPLLIIWSIIIVFAVDKKFEVQKFLSIWINENRFYSEIWVPIAIYVCLLVLMLLSLIFFAEFAVLALRVTGVIIAVLGAVLGMIIAVLGMIIAALGMIIAALGATITGLLYFGHWALYKLVILSLGFKIVTPGDVCVSNTLPTHNGETALHSETTVGSDIEQIELQNMPTPVKK P0CT99 YP44_SCHPO SPBCPT2R1.04c; CHAIN 1..280; /note="UPF0494 membrane protein SPBCPT2R1.04c"; /id="PRO_0000437226" MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDLFTEFSKFHNSYYPDGRISTRSNFRWPLLIIWSIIIVFAVDKKFEVQKFLSIWINENRFYSEIWVPIAIYVCLLVLMLLSLIFFAEFAVLALRVTGVIIAVLGAVLGMIIAVLGMIIAALGMIIAALGATITGLLYFGHWALYKLVILSLGFKIVTPGDVCVSNTLPTHNGETALHSETTVGSDIEQIELQNMPTPVKK P0CU06 YLZ4_SCHPO SPAC750.04c; CHAIN 1..146; /note="UPF0742 protein SPAC750.04c"; /id="PRO_0000373862" MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVYHNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR P0CU12 YHEF_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPBPB2B2.15; CHAIN 17..203; /note="VEL1-related protein SPBPB2B2.15"; /id="PRO_0000326039" MFKNLIFLFFIGLATAIRFNLTDLECSRLRGPHCGTYLLKVVGTNATYVGEKSFIGLDALTESKGEFFQRMLEQEPRLIPRLFTIAENDTANFTPLTFTTYLKTCNPQSIENAMIPFVNTVTSEISFDAWAYTAQNSSRITGLSNQLMNSTLYNVQVATCTPGFSALLLDSPTINVFNNEEGMPSWCQPIELTPVCPLDEGFN P0CU13 YI46_SCHPO SIGNAL 1..16; /evidence="ECO:0000255" SPBC1348.06c; CHAIN 17..203; /note="VEL1-related protein SPBC1348.06c"; /id="PRO_0000437233" MFKNLIFLFFIGLATAIRFNLTDLECSRLRGPHCGTYLLKVVGTNATYVGEKSFIGLDALTESKGEFFQRMLEQEPRLIPRLFTIAENDTANFTPLTFTTYLKTCNPQSIENAMIPFVNTVTSEISFDAWAYTAQNSSRITGLSNQLMNSTLYNVQVATCTPGFSALLLDSPTINVFNNEEGMPSWCQPIELTPVCPLDEGFN P0CU21 YN5E_SCHPO SIGNAL 1..26; /evidence="ECO:0000255" SPBC713.14c; CHAIN 27..75; /note="Uncharacterized protein SPBC713.14c"; /id="PRO_0000437261" MQFLERHFSVLFPVLFFFSFYPISFAPNFDWSTYVSLHYPLTLPNHLALMSSYTHQSHCGTSVFHQAQTLVHLHT P0CU23 YKN6_SCHPO SPAPB1A11.06; CHAIN 1..42; /note="Uncharacterized protein SPAPB1A11.06"; /id="PRO_0000437263" MTTGKPQSFEKMRTPFPGRSKAKGPQSDIIPSAPPNTPVTEH P0CU24 YAOK_SCHPO SPAC11D3.20; CHAIN 1..28; /note="Uncharacterized protein SPAC11D3.20"; /id="PRO_0000437264" MSFSKFHCGKLMSLKLADLRTMFEALEK P0CU25 YDPL_SCHPO SPAC29A4.23; CHAIN 1..162; /note="Uncharacterized protein SPAC29A4.23"; /id="PRO_0000437265" MKIDKAIFTNQFGVPLPSDNPYVALHDFVYDLEVAIPEDEFEAFKEQLANPRNSCIIFQTYEMLQELKDGQSSLREDLNHLSHGQNVLKKNMVYLNGTFECISNVIRANNQILMLEFGKSNRKSEEILNYKSAKQMNSNLSTIYRVLPLIKIFLMNIRNCLN P78797 YJ4A_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPCC70.10; CHAIN 22..155; /note="Uncharacterized proline-rich protein C70.10"; /id="PRO_0000014206" MFFIVAAGFVIAALIAAIGMAINRFFVRRRQARAGQTKPATTRPMAEARARPGATAVPRRSPTSPQSAYVPATVYTSPIGSPRRGSVRYTHVMAHPNTTTTVSENLPEEVPPPYSPAATASNTPQNEASPAATEAVNHERPASPPPVYRPPEEMV P78833 YHZ8_SCHPO SPBC21B10.08c; CHAIN 1..198; /note="Uncharacterized protein C21B10.08c"; /id="PRO_0000116785" MSFPASTHVYIAKIIGKKGEGDKILDLLSKVNEHVLKSEPFTKTYYFARDAKNPDYIFGLELYDSKEVLENSHKTSNPFLAFANYLTSTHAPLAEPLQLLNFKVVDGHLDKDNLGPDAKDYVLYTEYTGDSATLKQQLTVNPKADTSLIIHSLDDPSLYAVVTRYSKSGIEPGPAEISGATSVSQQVIYSGVGFLNRP P87318 YB2H_SCHPO SPBC31F10.17c; CHAIN 1..135; /note="Uncharacterized protein C31F10.17c"; /id="PRO_0000116496" MTTTPLGKMIQDGDFVFQKAKKGTTIPKARKKTLTKDLQVQVAKELEQESSSTFRFAYVFPRKAQNHYYSPSRTHTSSIKKKRPKLCSNINLTPWSLIDSTSNKSIREQSREMGIISIQKWAEQARMRSLCFPKN Q09678 YA07_SCHPO SPAC5H10.07; CHAIN 1..89; /note="Uncharacterized protein C5H10.07"; /id="PRO_0000116380" MTVLTSYKLYCGPDFPAPLEKKEKREKGKIRNISFLIVLTKGPIWKVSSMESTSYNGCIENLDCKFRKSFIEEIIAYEGFGKYIEVINF Q09700 YA29_SCHPO SPAC2F7.09c; CHAIN 1..491; /note="Uncharacterized protein C2F7.09c"; /id="PRO_0000116384" MSFTKFCRGCGQTLQSANESATGYIKPLKLSGIFSKGSVSNLLKKNLDEQAIFNNAFKNLNPQIKKHFPNTTSFPFHEKEIGRTDLLWCQRCHDLKFHSRIRPKELLQEPQTTLPDIISTVNNDKSTCLIIQVIDVTEVIFQDFVSATQYTHFPVFHLFTHADVLPPKKPYWLFPGLGISSKYAMLYTSHSFNLVDKLLGRINPLLCSRGHVYVVGEANSGKSTLLKTLAKRGNGVFNELLLDSFLPGTTQAIKGYPTQYFGSCFKQLSEGLIFDTPGYRGNLKSLLPWVDTKLLTSLVPKTRSRNKQLTSKPVQYRVRFGQSIILGGLVRVTPFEINEDGNHEVGKPIMFKKEDPSSTTIHFLFSTLKNKKTKGNTNNMKPLLIKLFTKLPAHITSITKLQSLENSTKNDNVPLVTHSPSPMHSSFTVSIKPTQLSENVFDPTSSGELVIHNFGFLSFSASRPMNLLVESVNPKAVSWRSAKPVVPKFNK Q09721 YA4A_SCHPO SPAC31A2.10; CHAIN 1..460; /note="Uncharacterized protein C31A2.10"; /id="PRO_0000116392" MDQVLSKVTTTAATYATAYAVRTGLQLAGSLVAKRFSKYIQTSAPKSSQFNLELVKSRLEQKIQAITPAVDLIQLVAARGNSSLQNLVPLIIRLRDHIDDFLEFIDYEASGSEKKSPEKADEASEKIFRRCEVLLREIEETIPLINLSLTTAGITLNTALSNTISPSRLLQAQCFLELSDKRFEESHTEIQIGPKFTVVLYTSFSQPSKSDGPLDVRWQETFAKSDLYIKRVVSASQKFSYVICIDEDLNDGRYHEETVGKPTSAPVFGKKLEISLQRMSLLCYTVSGRLLNISQAKSPVLALQLTSIKDVSALDKAHQDNSEDLNNPFIKNNDKTKFHQNIDWIALEKYFEVNALDISDSESEDLSDILSDSEFSIGNRNKNIGNNEYSAQISSDPAEEEIANAMHSLKLEPETSIYLTNPGSLSLLEYLLRLCSLQELHQISCLEMTDSQLAAMLNSN Q09742 YB61_SCHPO SPBC12C2.01c; CHAIN 1..318; /note="Uncharacterized protein C12C2.01c"; /id="PRO_0000116503" MYNVTYRLLRLSLISSHSLRKSRSFDVKNFANIHFFIPLPNTPKKFYSVNAFSPLLKARRMTATIVSNHNVGCSCCYFRQYSTKQFRDLNTSEALSPCKAEPIPYKIMSSMSNFSDFKSRFSQYRESHLKLLNELQNVKDTNDLKDRIRLLHLNSSSKLNAFLHDLINAPNVSAEMKENCVRLIFFGRKYDPFLRSRMFTLTIRYFLLQKNRLRTSFYLLKHMELLALPASYELKTTLLEWFLRKRKFETAQKIFLSLCFSQHFPSEKLLMVLLLHGTETMQEYAMIQAINFVNTEQKLRFYDRLHSICSKLKFSSTG Q09745 YB64_SCHPO SPBC12C2.04; CHAIN 1..384; /note="Uncharacterized protein C12C2.04"; /id="PRO_0000116504" MTALSTNSSSGGIFKIAIVGAGGINFGTPEGPWNNAQRVEKVLGKSLRVTALINPLINESERVLKSKCASDVAFAYENTKTYVSVTEYLEYLDSHPEDVPSAYLIGIPPDFHGCTTPGMDMELEILRKYPNAALFIEKPITSAPVQGAFNLVHELEKYHAIISIGYMFRYLKIVQAAKKYVADNNLNIACTIARYNSAYEHNNKLFWWYMSKSGGPVVEQATHFCDLSIYFGGDVDTSTVKVNRVNWYDPCGKLAKVPVDEESIPKEERIPRFTAASWKYKSGAVGILAHSIILQGTNYDTCLELQADGHYVRMVDFYGQPRLYIRSPEADSERIINFPEDDPYYNEFDAFLGVVQGRYPPSRILSKFDDGAKTYELTKIITNN Q09762 YA78_SCHPO SPAC24H6.08; CHAIN 1..220; /note="Uncharacterized protein C24H6.08"; /id="PRO_0000116396" MTSHQTGKIEVHWNDPSSGIFLSQTQRTSSTSSLKKSASSRRLVYGDDMLAPKPLAGQVLSKSPLPPFSPSKIMNRSISVPPTNISVPQISSNPLNLMKKSSDNDIFTTFNDTTNDCMNEASCEDVRHSLLQIIESKSNLSDSVHKMLGERVKTNLLLQGQLENMEGFWLQKLSQTCRLALTGNISEAKAFIVEIMCAGVVTNCVRWCPVLKTLIENLAI Q09787 YA99_SCHPO SPAC13G6.09; CHAIN 1..274; /note="Uncharacterized protein C13G6.09"; /id="PRO_0000218325" MEDVDLGFLSQEKLDEKDYLDIECSRVGGAPLFIRKNDAAFLNESLENSFEFLMQLYAPKNSEISYHRILYIFINRDGDSQTAGWTRGVKVFREQARETDEIDFQLITSKVTKLIDSSEIEVDAEPKEENKKEIPEKLKNVKVDTENPSAEPYTKAKGDVSFLKFQKRLSRAPDQIMRYYHATSNEFPGLWCNNECIPSSIPNCACGAKRQLEFQILPTLISSMNIDHSAKNALDWGILSIYVCSASCDLANCGLAEELCWLQTFSEQGIIAPE Q09789 YA9D_SCHPO SPAC13G6.13; CHAIN 1..115; /note="Uncharacterized protein C13G6.13"; /id="PRO_0000116403" MFQLPMIVEANDMKIKYYKRRNCYTLLIFKYKESKKINVYKRKKSDEVVEDCNKLKCTFFMIEEWHLLAILYDKSKYIKIIICSVLLKLNTTVIIRRNTHTKVYVMNKFYQKLKK Q09797 YAA3_SCHPO SPAC22G7.03; CHAIN 1..236; /note="Uncharacterized protein C22G7.03"; /id="PRO_0000116405" MQQLIKEHFGNGGKVRSTSIEYPIFVHSGSISAMLLTLVNALECNDVDEGVLVYPTGSTNPMENILRMENPFDGFLAKEAYSIHFQSVLERIQLIPCSHVDDLEKIVEVRLKHAKLILGIADISKLLKIRGCLNGRYLSRYLMLCLQNSKILIVCETGGLQERIPIIEDISINEDTQRTVSLETIYATWIPTFWESKRKSHEKDEGRLVDRRHKVLVDWLANTCFRGMSLKDHSAL Q09839 YAC1_SCHPO SPAC16C9.01c; CHAIN 1..361; /note="Uncharacterized protein C16C9.01c"; /id="PRO_0000116413" MDYPSKDVEFVTTGMFIIDEIEFDGGKKIKDIIGGAGSFALIGARLWTSEPESQQLGMIVDKGSDFPQVILDELNDLHTGIVYRETPWRKTTYGYNRLRDNGFRLFEYLTPKKPIRAPDLLETGLIYAKTIHIITNPKTFVSVCEELAKYGNLKNRPKIVWEPTPESCLPENWHILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKEFVSAFQEFQIGHDSQGWVVLRNGSDGCLIGACTSSTNATSDAVVPVREILHLPSVQMKNGSVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHGLPAHTKNSEGIDLWNGESVFQRLKEYYEFLASHEASAIKELTKRGV Q09844 YAE3_SCHPO SPAC23D3.03c; CHAIN 1..472; /note="TBC domain-containing protein C23D3.03c"; /id="PRO_0000208060" MESLESVDASSGSVGSYMSKSVRKHWWSRKGYHPTGSSKNGSRLKISSDENFQDELVVLDDAFLCNVPLELPSTSNAQKTAAESFSKLSPQDQLLSLQLNNVQESVFQQSTFNLPDALLDPGPASKEKQAVLSIGRPSWLPPKSKEEEKKHMREFEQIKKSAMRYDRQKQKEKIKMVEQKNKRNLYLVNVWEREILRNWPDALKSSRYAGIWRQGIPSRVRGRVWEKAIGNNLKLDYQSFFNARANAQKREAAEKAEQMNNANQFREDVCALELDLQSTMPHYSLFHTEGPLRRDLIGLLRAYSYYRFDTSYIPGTSFIGALLLLNMNLTSAFNCLANLLDKPFLQAVYTQDTSSLKSFYQTFLDTLKKNEPELATHLLIKLELVPDDFVYPLLRKLFIPMVSPEIASRILDCYVFEEDSFFIQLLMAVFKLLKPKLLVDDSRLVLSALLFENWDLGPEDEFMHFVYDISLS Q09861 YAF7_SCHPO SPAC29E6.07; CHAIN 1..116; /note="Uncharacterized protein C29E6.07"; /id="PRO_0000116423" MEYYIRETLITDFQDVKTLKNKRKCFSFFFELRLFSPQCLFIVYFFYLLHVRINTSPLFIKTTTRPTALIHITKYSEALASRLLKGHMTQLSLRTILPPAHTKNLHRQQPTTWLDS Q09862 YAF9_SCHPO SPAC29E6.09; CHAIN 1..339; /note="Uncharacterized protein C29E6.09"; /id="PRO_0000116424" MLSELPEVIFKGTEFEEQLSNLTSDSQANKRVYEDYDFKDETSAKPIPTEKKLKVFKKDDNVETLLSALEIQNEKSKQQVEYSFIPLKQDDGDILTSPGDFENASTSPVSDVTYVNTKLVDFISSVLLEENQGLALHQLTLKLINIGESFHSLLPINLPYEPYVIANYVERQLRSYISDTSSSKQSLLSLKNSSNGTVYVSTTLPCPVELKPNITAIDTAERNSYLWGILQPPEPSAEGPFTWNGASSHEGDINNNDTELGLIENPMNLETPKIDYATPHIKESNTPLFTYNFNISGFDGDSCIEKFTPLDALGIKPSPIDVDAHFQPEMLPPLFETFS Q09871 YAG7_SCHPO SPAC12G12.07c; CHAIN 1..412; /note="Uncharacterized protein C12G12.07c"; /id="PRO_0000116427" MPSQGNNKNSENITQNPIEGELGSVIVEHLTKRIRNFTKKKQKILKLEEIAASDSNSLNDDQRKALQGKDAVLTTLNELKELLSQIDATRIRDEKHKRQFEATENAKRKEEIEAQYREGYDTAQKQVSSLVRFLRFASHNCVHPSDDAPFNSAVEKLLVIVYEGTEKSEKAVADLNDSSTDVVPESEVSFQTISSRVDNFFAAPLPSEQAEELIEDDYAEQPEQAVGQPIEQQSISDDEARQTNRPLNRGIQFLNESEIEGQHVEEPALPSETSVPANSTLQVPTENVEVDVLGKDGTNIYPTQNQVVEQKQMQQKLDSMSPEWYQAADPSNGVVDGTPKLNSNTRGSSKRPSVNRSQGSGQRGRGGRGFYRGGRGRGGFFNRSKRGQYSNSNNSTSQPSPNAELSNFNPVA Q09890 YC9G_SCHPO SPCC584.16c; CHAIN 1..231; /note="Uncharacterized protein C584.16c"; /id="PRO_0000116542" MASSSSSSGSSSPASKRSSRKRQTPPMPELPSFLLAFPHAPPLGFLRPKLNSLVVQVKRQGITAEPVFNLYSRFSVHTLSHNLVLDNVSSESNKTSAVFCKRHVGSSQVVIKIYSPHIKDYLPWTISCTKNEWVFDMLASFSIENSLRIKWVAPDKAKLNETWKCYLHIQDVKKSYFLASLTSRSLQFEGGSVGLSNRIITHRELEMVILSTSLCVQLSLLNLLPNYFPKP Q09921 YAKA_SCHPO SPAC1F7.10; CHAIN 1..238; /note="Uncharacterized protein C1F7.10"; /id="PRO_0000116441" MIRILVINPNSTVQMTESVKSVLDDCTPPNVQLEYLTCPPEGPKAIECVSDGVRSAAVLMKYFEDHPPQVDAFLVSCYSDHPLVTTLRETYRKPCTGIMQASILTALSLGRKVSVVTTTKRYEPLLTDGIHAMGISDSVFAGIASTGLAPLELDSKPRAEVDALLARTALRAVNEMGADVICLGCAGMTHMAHVLEKAVGPNIPIIDGTKAGVELLASLVRMNLFTSKQGVYQAVGSD Q10082 YAO3_SCHPO SPAC11D3.03c; CHAIN 1..302; /note="Uncharacterized protein C11D3.03c"; /id="PRO_0000116452" MTEISELASSSQKPEKTKYNLPKPLPAYYPHPGSPLYADKELYARIANAPKKLVGRHVCQPRTGLAVKIPQKSIFSIVVPEGPQVCDLNIWNFHNPRERFWAARTRQIHSAHVSTYDRLWSTLPYLRPLVTIIGDSLQARHDEWGGRVHDTLGTRCDPYIDKLISGKDNDLHCHSNLTRAIMPYGLTEFDVHDVLNVFQVTGLNEYDQYFMETCPATSKDYFQCFAEQDLLVAISACPGGDLSNWGWGEDATDVESSKMVDCCRPLAIEVYELEDEENSLKGWVPPQVVNYTGNHGLKAPSS Q10083 YAO4_SCHPO SPAC11D3.04c; CHAIN 1..130; /note="Uncharacterized protein C11D3.04c"; /id="PRO_0000116453" MSQDSESFIRQLFKAFTDFSTDVESLRGFLTPDYRQLVDGRELTLDDFISHAKALRTHLHRLDINVQQIVCQGNKAATVHIAHAIRSSGESSRIKVIAFYSFKDGRISLIDELTYVLEGGNADRELGSVQ Q10089 YAOA_SCHPO MOD_RES 216; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250" SPAC11D3.10; CHAIN 1..434; /note="Uncharacterized protein C11D3.10"; /id="PRO_0000116454" MNALAKIKAFRSYVPLLQGNTKTIYLNQSFQAPMNMLVSTALQGYINEGLYNPHPKPMWKERTEETRSLLAKLLNASTKDSITFTRDTTEGLNLFQRSLKWKPGDNVVILDNEHPNQGFGWIALQNDGLEVRLVPNEGQYHANASTFAPYVDSRTKAIGLSSVMFHSGQKNDVKDIANAFRPKGIHVLADLTQQVGLSKIDVQDLNVSACAFSCHKGLGCPTGLGVLYVSPLAISELRSTPPFVGGGAVEDFKEDLKLKLNAKYHQSALRYEHTNNAYMLITALRAYLKFLLKVGISNVERYLQGLGKDLIKELESLNVSVIGYKDFDKHSSHSYVLKILNPEWFDFLRQQGVCVSRFESGIRVSFGLYNTSKDIIKFISVIRKGLALNIPLNIRPPQRIAVMDNPLVGISDEAIAAMKLPANTLSNRPLAANI Q10095 YAOG_SCHPO SPAC11D3.16c; CHAIN 1..131; /note="Uncharacterized protein C11D3.16c"; /id="PRO_0000116455" MTTLKVDEDLECALMEQFIEALHQRCTDIPRTQLCVLAISFNRFILHKSPDIFTYIQYYQQKLNSYGFPLPPVVLKSLQMPLTSPEPDADERFRDGDTEFDTAGVTASSCFPVDVKSPSVRAFGNVTFQSD Q10098 YAP1_SCHPO SPAC15F9.01c; CHAIN 1..227; /note="Uncharacterized protein C15F9.01c"; /id="PRO_0000116456" MEQIRPFSDNYLDRLRTVEEDDYNDWEGSSDTKTLYSSVSDSKIGHKKSFHKDGKGLFKTLRNFLSLKTNKVPKNRKFSLLKGSKCNNVEIKVFIRNNDKQSNVHNFKGKDSIHEAWSQYLIFDSMGLSPLIHISGEDKYKVLCLFSIWRRKLGKCSIFTVHDPDIQKKIKSILSYLWELSNTNDPPHVIVWHTAKGTNVMTMGPLGLKDEDLWNYANERSNLNGTT Q10102 YAQ1_SCHPO SPAC18G6.01c; CHAIN 1..259; /note="Uncharacterized protein C18G6.01c"; /id="PRO_0000116457" MFGTRFFAYQFCKNWLSKRPGLVFWSSVATINAMYQTRPLYCESVTKTIQQTYEGLVQKRINNEDELFLLGSGPRYVSFLSIHVYDIELYIQKKDVQTVHTILQKEVDPKLGLEMSMKDEEIGSRIVAALLKNEMKYAIKIVPTRNTNFSHLRGGFVRGLQSRMSQNDPAEQAAVSKFRSTFPVNRTCFKETALWMKLYGNDFCYIYKDSEIGHMHDENYMVSNLFLKGYLVGPRVNSEQARESVCLTLRRIMDGTLLF Q10111 YAQC_SCHPO SPAC18G6.12c; CHAIN 1..309; /note="Uncharacterized protein C18G6.12c"; /id="PRO_0000116461" MAFSFQVSKMNSFDNYNAAIHPKHDLISVNAPVFGKDAKLSPHLAIVLADKGFMLEQVCLPWRYFTDRGFVVEFVIAESIFPPRPPKPNDSYMTGWKSHVLGASKEILDIYSVLCTLNEFNNPKCYRSNGFTFDNFSAVFITGGRNPFVREMLEDPLLHASLVPYIHSCRTIQPDEEVKDNRKIKVLGAISQGAAAIYLAEPNINMKTTTIPAWMERSNSFLNPTPDNSTYPYAATIIPKDKYVSGPYRRVAFTYQDENYYYISGRSNKDIGELSKKMYLMYKQAYKDLNASLRERRRRSTSNRRNSGI Q10112 YAQD_SCHPO SPAC18G6.13; CHAIN 1..114; /note="Uncharacterized protein C18G6.13"; /id="PRO_0000116462" MRLKVSCTEFPIQQWVETSSLELVDSVNCVADLCHAIWMFNGGCADWRLQILKEGFTVPMTGIISQYLKTDDHIKIVKEIYPPNLPVLPFRVYTTQNTSVESELVEWEDVEMEA Q10140 YAS4_SCHPO SPAC3H8.04; CHAIN 1..338; /note="Uncharacterized protein C3H8.04"; /id="PRO_0000116465" MPACYCATSTSLENNELLYKNIRNLFSTSRSFPIEQEWMNLKSISQMKDFFSNFPGNSKANNHFLCNSPLKFEIFNNEKSVKPSNGPHLFTRCSCRCNKLLSGDYITQQQPIDASAEHSLNAKGINTYSLKNCFQRSGFIGSYEESLFSGHMPYCSSVPFEFSIEIGVISFCRCKPSLVFPPHLKINFVAYSLVGNVDNVQFPYIGRFRLRSQKSDKVMNKGYPFGYRIPSVGQLQLILRQTNGLVIKVFLVPYNVSSMVDCSKTWIRQKHYLQQLDDKSGKILSHLKFGLQLQIICTSAGHHYLYDSQRIIFVQQSLGGLYGNTKIVNETLLSESCR Q10203 YBX5_SCHPO SPBC17D1.05; CHAIN 1..368; /note="Uncharacterized protein C17D1.05"; /id="PRO_0000116530" MSFVDGVNSWFSAASYWDGLGPTNVVQPEDDLAFVSQFEEVESAYDNLVKNGMIAPRRKNSFASSVNNPFSTSALSEALNGSVSMSHVPSSGLLKSTLSSTPTAGSNLLGTSPAEPASGLVGSSGFGSSMLGSSLPGNATSNFGSQASTSLLHPRRSTTSLLSSSAHHSRSSYYDLATPTRSSFSYNTVGAASLPSGGLSNLSSSLRSSSKSAGFSLFESASNSFTPSSFIESANMESLSIPSRRRPSSIAPIGTRPSRKEIAFSNSSTPTDQTLRPPNPPAANGNATPVTAVNNVSAVADSPQSTGSSVSSSLPTLSLDFKQEYSGNNHDMSGLSSSLSKSHNSTSALSSQIWSSPCASTLGGVNVW Q10207 YBX1_SCHPO SPBC17D1.01; CHAIN 1..584; /note="Uncharacterized protein C17D1.01"; /id="PRO_0000116528" MKAVYLDYLLRIRYTYVFNLKVSYQSERRTYGATEHFVGCLVPKAWNCLADDYTDIKTLLDLLFGVTAVIIFACTFKCFTMTEDGLTKLNLEAFLGVSGNTQELLESLGISAIPDLSNLGASNNNNSGLTFDPNDPSAAAFYIAQQVAAIEHPPPRKMTSSEKTRSENRERKKRWREQNEERNKDNDLRCRVNKKAKKLFGSEPSIEKTNWIEAEFTRRHTKRKEKERACLSQNQSSNASRANSQSLLPDLDLLATNSSANAVLQGSAINNALNALAKDPNLIHSLLTQIDFDPSKSKDGLNLGSLTDVVPPQPPQPEHELAALQEHNEAHDAAMRQYELERQQNAMLPGLASIDGLQALPHLDFSDSAVTNQSHSQSQNSLHPLISQSETHSIFSALSETPTPVSGNGNVADAPPDFSLSQVMPLDLIAPSMQPSAVSSPMSESHVQISSEMPRTGMSALPMRPRSQNVDKHRKFPYYNKRNAVTTPSSPYDGAQSGSPQFPPFELPPHNYSQAQSPNLATPSPSFSSLPDVSLPPIVKPNLMSEPTPTNSDEKSHALGFPPPPGQKIEFQRSSSKNGTAKSD Q10212 YAY4_SCHPO SPAC4H3.04c; CHAIN 1..309; /note="MEMO1 family protein C4H3.04c"; /id="PRO_0000134397" MSQAIREATHAGSWYLDDTELLTKQLKSFIKNPTPETGKRFVISPHAGYMYSGKVASQGFQQLDFSKIQRVFVFGPSHHIFTRKCLVSRASICSTPLGDLKVDEDLCQKLVASDNSFDSMTLDVDESEHSLEMQFPLLAFHLLKQGCLGKVKIVPIMIGALTSTTMMAAAKFLSQYIKDESNSFVISSDFCHWGRRFGYTLYLNDTNQLEDAVLKYKRRGGPTSPKIYESISNLDHIGMKIIETKSSDDFSEYLKTTQNTICGRYPIELIMKSMECANFSERFKFISYAQSSHVELVTDSSVSYATATA Q10261 YD2D_SCHPO SPAC56F8.13; CHAIN 1..101; /note="Uncharacterized protein C56F8.13"; /id="PRO_0000116571" MNATQKKKNEKKTKNPYSHNHVNTKLILPHNTFLTNILFLLGLIKHTNQLTFPSIPHSSAISTLLKQTPLPTRILFLSLCLTPSSASARSSDGIILFPHPS Q10263 YD2F_SCHPO SPAC56F8.15; CHAIN 1..176; /note="Uncharacterized protein C56F8.15"; /id="PRO_0000116573" MFFFLVFSACEVFVGFSLCTLVISVPFFFLQMTPFYSILCFLSFFALLLHLPCSIYSHTLHFFHHFTIACYHYSLCLSLVALLLFYTLYPFQSITLPLMPFLEKTESSILTISHVYSPPTIITFDGFKRLLRMHVPFYTLSFDTFSTHTNFFPRHTFPIFIARVSLHFVKQLSLSI Q10273 YD39_SCHPO SPAC13G7.09c; CHAIN 1..135; /note="Uncharacterized protein C13G7.09c"; /id="PRO_0000116576" MESSLDRLNFDEFVAKLLIHESKKKNKSFVDHGYIEKEKTKLRPNKVFLNNMVRNVQSHNRGINNRRRDQKRKQLISIKQDNDLNVSSERLSRRIDVPRPTSKKKRLYKETPDLDEPGSREKRVSQKGQLKIEKV Q10300 YD46_SCHPO SPAC22H10.06c; CHAIN 1..93; /note="Uncharacterized protein C22H10.06c"; /id="PRO_0000116580" MSCRYRICRDIWRGKCIYVFRCLYTNHAVVSWNQTNEVIGLYKANEHKFMNNRKQSHIKNGLVVSYSILYPVGKGRSLRSTGVVLILGPVKEY Q10302 YD49_SCHPO SPAC22H10.09; CHAIN 1..646; /note="Uncharacterized protein C22H10.09"; /id="PRO_0000116582" MLKTLSKVSKNLSNTSAFLVKSKPLYISFCTCKAYFEDNTSLSRRFFSAKKSLQFKSLIRKYSEDSTLAWRDYENYNDDDLLYQRELSEIYNKCLKALHPFYPVFEVNSNLYYQLLMFTNYSNPKDNGFSKLLFSQYSDEKKVLVNFVYNVLRLDPDLQRQKRILESIISAALNICVSTVNLSRTDLKSSLKIILQTIDLFKYDSSFSSIYFRKDGPYHKVEKLLKSANIRSSLNSKTFNDFRTLFLLLIRDYSLFHGNSSHCMLANSMLPPSIAFSKMEKAEIFLRLRAFFQLMEHIDNERITPSEQFLDKVFISLLSAKNSCSLKMWLIHSFNKGWPVKIEFFVSFFKNFSNIVEGSMEVYSAYLHIIRDHYNLSDLADVQAIFLSRFILLRKKEDCKKLLEHVLPIRQLFLLNCYSLLNVLANYVVVFKDRLIFQEINQNWEEHKGQIPENFIFSLLKMFGEMQENQGFLNACIYYINKKKNLNEVSRYKINLLLLQGVNSFEVKDFYRKRGIEIMPKNLPRFFCYCLKKNKLSYALKYIRLSGLQFDYIVDCFRNSSDWTRTLISILSKKMGTEFAIRFLKIISFPLLSNDKVLREIEFFAIHEVNFRSLKWVADQQLRILPGWSSRPQKATFPLCTVHLKK Q10327 YD72_SCHPO SPAC32A11.02c; CHAIN 1..851; /note="Uncharacterized protein C32A11.02c"; /id="PRO_0000116594" MAVAYPTDKHVVHEETGKGLEVYSIWTAISNGKMPSNKQLRGLGSSLTDGAKSVAKERQKKISDPARKFFSDFSKLIDNSFNVFAKKNEGDLLQNAIYELSQAEGSTNVNEVWNDITEDMQSQDFSTEDLKQLFLLIFNNGKLRTLLQNAIVLLGQQTTNVASKKLNEQDGKKSDNLRNGVNKVKQNMRNGASARDQAREQGSKAKDKIKNDPDAQKAKEETKQKLQDLYEEFKSVAVDLQGDPKYQHPVRSLLNLIDKFIDKLSEQSGNVTADTNEHYDRAMQYLKQLVENILNRSLDNLIDTLKQVQHDAENDEELKDWLESTRQFVRKVLLKKGYAKSDASDKEFNKLRDKGDELLNGRYKKRWQQLSSEVKKISDSASSDKDVKQLFSNYKNIYGDLIKREGGQISLKTSMCLEILRLGVPVILEKMQYFPIPRLEIEQPDFDVVLENLNLQTANVLPKLAEFRNNNFVRFSPYANITSFRENMINVHLSNIQCDLKDVNYYIKRKQGFPTFTDLGVVDLLIGKQGMVVNLTLSSFSNTMFENELPDSFFKVEDVKVDIHHIKLKIRKSRHRLLLAFLKPSLMTYVRSTVARSMELSIRHAFEQVDREWYEIHKEAKSEIEKDSSKPTEDQESKLKVYGRVAYSRISNLHKSSKEKGKDSQVRVALHKENTALNNIVLPSGNLQRSEEKRRAALSGSTWHSPAFNIFGVDDSEDSDSPWATDRGSRLYQRTKGSVKSRESRLKKEKHKNRPASKGTYTTYTSSEERQRSTEDPLSHDTLSRTILNDQIVKGNVTEIPLPPLAVNEKRASVAVSSIPSFGDDQHDIELLNSTDPRKNRILYNQPPAVA Q10346 YDA4_SCHPO SPAC1F12.04c; CHAIN 1..191; /note="Uncharacterized protein C1F12.04c"; /id="PRO_0000116601" MSYMHSLNLMLQNPSGIDKIAAILVNVARLDPASSKSTAQLVSMLNEFRCILRLPGLYKLIVNFRKDSSPETYMSNAINIGYYVTEGLAFLGGKQIISISKPLEDKLWLWSSRFWLLDTLLTIYQLLREKTEDEKEHQLDLASNLASLPLCIHWSVENGAGLHKHQIGVLGLFSAIVQTRKLILSLHNKRA Q10413 YD88_SCHPO SPAC1F3.08c; CHAIN 1..108; /note="Uncharacterized protein C1F3.08c"; /id="PRO_0000116598" MVIYCNWLELKGLLETNDFLYLMRCCYMYDTVSLVSNAPNIYSIPFFYDRICYDYKNILLKYELFIIYYYYYLLICLSPHFFPIKRIRPFHENPLHSFVYRIMISSEA Q10486 YDFF_SCHPO SPAC17C9.15c; CHAIN 1..94; /note="Uncharacterized protein C17C9.15c"; /id="PRO_0000116619" MSDSFHYQYDRASPERLKPTIYSWTRLRQSTRAQNENEQAKRRQGILEHKRGGSMEMNKFIDESAYMEWEKQLENASEDYAIEPSDLEEEVDQL Q10497 YDGB_SCHPO SPAC26F1.11; CHAIN 1..105; /note="Uncharacterized protein C26F1.11"; /id="PRO_0000116623" MIIITAKENVPTNQKLDTCKNQSTVHQKVNKSLGNSNKVLRSNAVQSDKANREPRRITKSVKKKENNTISAVKKVITTESRIEGESKNGNSRKNTRKFENIKKTP Q2EEM0 YEIC_SCHPO SPAC27E2.12; CHAIN 1..76; /note="Putative uncharacterized protein C27E2.12"; /id="PRO_0000303971" MGIQGLYQKRFCLFVCLERFQWRGAIFLVCYPLYCVVCFVSVLCRLYCILMSAASATQTICDQSILHVHGVENMKA Q2HQL6 YGEE_SCHPO SPBC1347.14c; CHAIN 1..121; /note="Putative uncharacterized protein C1347.14c"; /id="PRO_0000303972" MLLSNKIKHSIFQFFVFPFYYFLLIITEIGFSSCIQYSGLSAYFPIKCTLSLLSSPIRRVQVISDSLNVKGKRLLLVVTAHSRLRVNADIGGLISNIGCGKRPTILSTVNTGSNTSREGKS Q4ZGE2 YB1G_SCHPO SPBC3D6.16; CHAIN 1..95; /note="Uncharacterized protein C3D6.16"; /id="PRO_0000303935" MRTGRKTCTDYINKSFREQIIYKEEWLPRSIPTSLLTAAGSKSCIGDRGTNGRTEAEHDGIPHSRKKVSSAHFNPSTLLFLLKRLGHPVYLREGE Q65ZA5 YFSA_SCHPO SPAC19D5.10c; CHAIN 1..87; /note="Uncharacterized protein C19D5.10c"; /id="PRO_0000116747" MYTSASLFFIQIVISIFNSHLAVLYSIALCYSVQGRILGSSTTNFVHDSTIGVKSSWSRHLIHGINIFSFSISLFLIFLTIPLFDIG Q6MX60 YP42_SCHPO SPBCPT2R1.02; CHAIN 1..119; /note="Uncharacterized protein CPT2R1.02"; /id="PRO_0000304797" MTALMNHIYIDNPLISNSTNNVTHELLIDLHELYNDGEISRIVLLRTLVTQSADDATWIINLTDDVLNGLPLLKKRDRYTTQCHSTNMASTYDCDTGANAVGARGGATLAADYRGDWGG Q7LKY2 ADDH_SCHPO SPBC1289.14; CHAIN 1..324; /note="Adducin-related protein C1289.14"; /id="PRO_0000353840" MLSKKFTPLSLKNAAKCINNSLRSTYAITGVNLTRGLATNSKVDPKTYAPKPEFSSIAVREMLRKSCLHEFTDEEVATRIELAAAYRLFGLEHWNENILNHLTAKVEEPDGTASFLINPYGLRYGEITASSLIKVDEDGNIKHPGVTGDVFGINRAGYVIHSAIHRARPDVKSIMHNHYPYAAGVSCVKHGFLELAQTSHQSGPVTYHDYHGIVVDKGEQKSLAEDIANKDILILRNHGIITAAESVGAAYYLMYQFLAATEIQTHASANALGDMNNLFIPNNKLVEKTFDVTREKHFSGAKYGIKELSAYMRLLDDLDSSYRT Q8J1M7 YJ8J_SCHPO SPCC330.19c; CHAIN 1..90; /note="Uncharacterized protein C330.19c"; /id="PRO_0000116809" MVVLNKSEAHDRSRKLELLSIRINIFGLQLNIIINLIPLVLLFAFFCPCIYFLHTFLADCEIAKSTCITSVFNCLIFHMPNLSGDWNITV Q8J1M8 YLO4_SCHPO SPAC1952.04c; CHAIN 1..137; /note="UPF0768 protein C1952.04c"; /id="PRO_0000116848" MFLFLPIPLNVQDIWKVNSKYKHVLLTCPVCQNKTVRVYRLVKSLALIVLPVLPVYTSKVLRCSHCGWYEPVDSAMIDQRRRREDLPTPERPEASAQQHAFFPGSSSQQTDIPNVRPQPHIPPPRKSDEAPPPYSYK Q8NIL4 YP35_SCHPO SPBPB21E7.05; CHAIN 1..127; /note="Uncharacterized protein PB21E7.05"; /id="PRO_0000304059" MVKKFQSKLINLQFNIILTFFVYEWNHDITCLNFKVKKRRGDFYVINERFFIKYIIKKNKNPQNLTKSICNSKTSINSMRQYLATINKKLRAFVQTFLAIGGYYSITTQIVKIILITHPVLLCQCSS Q8TFG3 YL55_SCHPO SPAPB18E9.05c; CHAIN 1..90; /note="Putative uncharacterized membrane protein PB18E9.05c"; /id="PRO_0000303970" MNEVISQPPCNIFRPLILSMHLSPVSILSPVLLIYLVIHSQNELVSMSWLFRSTICFGVSLFLSFFLVRILWGIAYSYNSNSMSIYFSYI Q8TFG4 YL54_SCHPO SIGNAL 1..21; /evidence="ECO:0000255" SPAPB18E9.04c; CHAIN 22..800; /note="Uncharacterized protein PB18E9.04c"; /id="PRO_0000304075" MNRFFISTLLLLAQHLAPAAASCGLANEASLSANEVQDIYHDFVATSINYADLLKRNEDLNASLSTGSPVEITSTSCTTDTSASTPIITESTSSTSSASTTGSSSSPLPSTSTSCTTSTSIPPTGGSSSLSTPITPTVPPTSTSSTSIPIPPTSTSSTDTNSNPLPTTSTSCTTSTSIPPTGGSSSLSTPITPTVPPTSTSSTSIPIPPTSTSSTDTNSSPLPTTSTSCTTSTSIPTGGSSSLSTPITPTVPPTSTSSTSIPIPPTSTSSTDTNSSPLPTTSTSCTTSTSIPPTGNSTTPVTPTVPPTSTSSTSTPPPPASTSSTGTSSSPLPSTSTSCTTSTSIPPTGNSTTPVTPTVPPTSTSSTSTPPPPASTSSTGTSSSPLLSTSTSCTTSTSIPPTGNSTTPVTPTVPPTSSSTPLTTTNCTTSTSVPYTSTPVTSTPLATTNCTTSTSVPYTSTPVTSTPLTTTNCTTSTSIPYTSTPVTSTPLTTTNCTTSTSVPYTSTPVTSSNYTISSSTPVTSTPVTTTNCTTSTSVLYTSTPVTSTPLATTNCTTSTSVPYTSTPVTSSNYTISSSTPVTSTPVTTTNCTTSTSVLYTSTPITSPNSTSSSSTQVSWNSTTPITGTSTSKVTSSTSIPLTSTNRTSTTFTSSTSISTSSSSTATSSTSFASESSSFYSNVTTSSSTVSTPPPTTSFPSTFTTSFITSSSLSSIPNNSTEVKTASTSSGTEIKTASTSSGSSSSSSYTPASSTSTTTSSVSSRQSSSSSSFTPSSAISTAKSSFVLSTLSILIALYMVA Q8TFG8 YL62_SCHPO SPAPB15E9.02c; CHAIN 1..188; /note="Putative uncharacterized membrane protein PB15E9.02c"; /id="PRO_0000303969" MTGMFFFASLFSSFESLFFRLFFVCSFFFPLLYSFIFATLHAFVFLFSHTLVSSQFRRLKLPYHHHHTFTIEAFFYWFFFFFFFFSHCRRFHIAIFIHPYDSNVVPFFCFFFYFSLFSFFSFLFTSLHFNFFFRLCRHKHLLDIPDQTTLSSLLHRHTRLPRDVRRKHTCFHTSVWCDMSSYCIAWRS Q8TFI0 YIB4_SCHPO SPAC1751.04; CHAIN 1..103; /note="Uncharacterized protein C1751.04"; /id="PRO_0000116787" MVVKKSKPKNQIRVEDLDLPKLNTSKNPQTKIQKKGKKKGKIFAETKDDLQNILNQVTYELDDKIKSKLQVAHEREAVFSKQSDRKISNNKADKKTGRKNEKK Q92346 YDH1_SCHPO SPAC6G9.01c; CHAIN 1..95; /note="Uncharacterized protein C6G9.01c"; /id="PRO_0000116626" MEIDDIFASKKANPANEKSNDSKSEAKAPKKGAKTKSTPSRPKPTNNQDDLFLDPKGASGRKRTEEGFLVYDEEELNIGQGGGTPDCPFDCQCCF Q92363 YEJL_SCHPO SPAC31G5.21; CHAIN 1..118; /note="Uncharacterized protein C31G5.21"; /id="PRO_0000116722" MDYVGGSLKLKNVKKKPLKKKKKDSKKLAEKVQEHSSRDKSPLEENGVSTYQMLRSKDTDSAMPMTEAQKHFESVQEQRLLQKAKNERLKTHKDRIDEYNRLLESQSEHFDMPKIGPG Q96VG0 YH7J_SCHPO SPBC16G5.19; CHAIN 1..105; /note="Uncharacterized protein C16G5.19"; /id="PRO_0000304088" MCTFVFESLCAMISTLKVNKIERGYWFIQCLRYCFIYIIKKQHRQADLPRNFGMRSKALYIGRSVGKWIETFCLDSNYSTHVYSLWAKSFLIIQFENVDPFVDHF Q96VG3 YL93_SCHPO SPAC683.03; CHAIN 1..105; /note="Uncharacterized protein C683.03"; /id="PRO_0000116842" MEKCINRYKDILPLNRYSDGSGKCWGLLGCEISSVVGQTGVKRLLLGSITKFVYCSMRLFSLYTIVQYFKSLRCLRNGRTEVRLYTHYKRHLPRSVNSIYLQTNC Q96WS6 MEU15_SCHPO SPCPJ732.03; CHAIN 1..150; /note="Meiotic expression up-regulated protein 15"; /id="PRO_0000096449" MEETLPSYEAASGAANLQEVKPQVLPLEEIKKIYKISYWWLCSIALIQTWWVLLGLLPIFFALEHYEVPYKWIFIIEMLYYELYLTLYVCWCYKLRSDFWNEAAKNRPNEERLSALGGWDFLRIPKKRVLVLRDAQSEKKQNNADASNLV Q96WU9 YJO6_SCHPO SPCPB16A4.06c; CHAIN 1..126; /note="Uncharacterized protein PB16A4.06c"; /id="PRO_0000116818" MQASSEPANVHFEGQNQSSEGQLSTSPPRRWRNCTLQRHGSRASADEFCEQYRSRSHGPQGRRSLEHDNQFFNSRTYYGNGGNTTDTEALQKSVGSQSADEFETLREQTVPNPIAEAWRKYFRKVH Q9C0V2 YQEJ_SCHPO SPCC576.19c; CHAIN 1..119; /note="Putative uncharacterized protein C576.19c"; /id="PRO_0000303974" MPTSSNDLYQTRLDVQTPNRWFLYISLELFNNMYSPFRSSSVLLSGAQSDIPKVGKCLFLPCRSLEFRASANSLSVHFLLNVISAILSMLIERYAVEVIMSKITWPRSNEDWRFHGIKG Q9C0V4 YOM2_SCHPO SPBPB7E8.02; CHAIN 1..749; /note="Uncharacterized protein PB7E8.02"; /id="PRO_0000372373" MGTVVGETELNRLNNGLSSNNGSSADEGLEHWNPLKKIHSADSSRRRSTSSQLNQPSNYHMHSSLHEEVSVGSSIASPSSRIPDKAISQYYETSPPSSTSSLSSNNQLMNSSVILSPGQFLPDDANAYGPKASLPPSEMPSHFHPLWSKSASKDSNAFNDPSAIPNPSPLFSSAYATRINGSLRNDKWNRSSFSEALSSSRFSRPQVGQQQPLSSAFPFQPVKQPTEQPGSLHPFMQESKTSPFATRRPSLNTDHHGRPILLSPLNYQNSSLNPSTPSPFGGSPVMHPPVSNLSPRTPAVPMSSDGHLAPAFDFLNENPIWSKRFSISSIKYSAPSTSNASNIAPDSAPPASSQFSVPFNAAAENINDTPDSVLANSPTPRHLPYTWSRHSTSGPSRSTVLNPSTSRMSNYTGLESHLAQLSFKRRSNSATLPSLGSIRPFPISEHSPNINPLDEAAVEDEVKEEKSRFHLGHRRSSTADNGTLSSNVPLYPAYNSSPVQTRTSLFSSRLSKPSNPIVSSVSQANAPKNALHSMPSPTSLANLPSNLSDTQYKKLYNLYLVEFKAGRADVFYIDDNIKLSLNLNDYVVVDADRGQDLGRLIAQNLSQSEVASHIEKIPSDRNGQLQNLDGAILEGDTSQSLHPKRILRKAQPHEVDQLIQKTQDEAQALLVCQAKVRQRKLPMEVLDGEYQWDRKKLTFYYHAKQRIDFRELVRDLFKVYKTRIWMCAVSGTNMSSPASINASTNQFVL Q9C0W4 YG1J_SCHPO SPBC83.19c; CHAIN 1..119; /note="Uncharacterized protein C83.19c"; /id="PRO_0000304118" MVIDIVTNQFSNLQNIKIFTWKANFESIRINLQHMHLYHYEHIHLFTSSQSYMYHPNARFSYSPFCCFTDTLAYLRCEPYRGYRKCIYRKVKMPNLILRNPLVRYDVSPARYPTIGIRS Q9C0W5 YHLE_SCHPO SPBC800.14c; CHAIN 1..160; /note="Uncharacterized mitochondrial membrane protein C800.14c"; /id="PRO_0000341602" MSLVYLFQSVGILTPCGSAGAIAYITSQVLPAILIGPADVALAQWKYIYSMGKKSFPFLAIANALVQGYLSYSERKRSIFSSKLYAISALSGLCIIPFTLLFMKKDINSLQTLNPDLILKDVKATQNFRSIIHRWGFKNLFRSAFMFFSGLASIAGSIYF Q9C0X0 YB8L_SCHPO SPBC29A3.21; CHAIN 1..100; /note="Uncharacterized protein C29A3.21"; /id="PRO_0000303936" MLRYNFRYLHNVLSHTVVFCFTEVSLHIVKQLGVESYACTVHASRFQKSYSASIDYCQRFLFSSNLKHNYVNLNIIFTSCIFRSLREFLRFYIAAIMCFL Q9C0X1 YBSE_SCHPO SPBC18E5.14c; CHAIN 1..127; /note="Uncharacterized membrane protein C18E5.14c"; /id="PRO_0000303933" MISLTALDLLDELLNDSSSNMIWLYEVYMLYKTYTSYFFMSSKSFVRGVKRYLIYFCYCANFIALFRVIFGTIFVYSPDGITPFMTDFVRWILIYLKGSINSLLYMASFTKQISLLRGWRTEHAELS Q9C0X3 YBBF_SCHPO SPBC13G1.15c; CHAIN 1..111; /note="Putative uncharacterized protein C13G1.15c"; /id="PRO_0000303981" MASCCIFCAQFVLNRNLLEANKYKLSEITFKVYISIRRLLIVVITLYRRIVECCASLCSLIFSKYYLHYKTFRILTIIQSWSDKVSVLPNRLYCLPFCNAFIEFVKKLTET Q9C0X4 YB6E_SCHPO SPBC12C2.14c; CHAIN 1..111; /note="Putative uncharacterized protein C12C2.14c"; /id="PRO_0000303973" MEELQYNFKKRRKTHNGISRFQRSALPLTIVYTIWSTFGSPCSGDQRVTLSITSILRKVQDRRESEKKVKGKGREEYRRYYFFLLFYVSFPHIFLGLFFFIDKKILPFQSV Q9C0X5 YLNA_SCHPO SPAPB8E5.10; CHAIN 1..73; /note="Uncharacterized protein PB8E5.10"; /id="PRO_0000116847" MAVLSRIMKPYRAFQRLPFELKPLAILIGIAGSTAIFTMGYKIYSDPEIRRSPSWVAQTQQKEETKVKKPQFH Q9C0X7 YLN8_SCHPO SPAPB8E5.08; CHAIN 1..103; /note="Uncharacterized membrane protein PB8E5.08"; /id="PRO_0000304123" MRKLRCKQMIPKLLPFIFIYLSVANKIMFYCILNERAFKHYKTYRRITDCPEIKNKKSRRKNQRNSSSIGLSNPNKFSIYIYIYFFFYSFLCSPYLFKYISLF Q9C0Y7 YKM7_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAPB24D3.07c; CHAIN 23..300; /note="Uncharacterized protein PB24D3.07c"; /id="PRO_0000304049" MKSFVWTLLGALSLGSLTTAYGANASNSSVPTPDNTLVVSYTNTSCYTSGPLSPDTRFNRTTRGTFSKVRDALKFRLNGPIHHWDIANELFDTALGVEIIDTQYGINNRTSRDWCTAVSALEKGDLIEFAAAFTAFDDVNPTKEVVPDALVGTLALWAKYSYEYDLTSIVSLFGKNWTVDELGWGTYIAHSLNEISSNTTGAANATLFIDTQTKSDCYKLASTIESWKYAPLSAFPNYGPFYIYGQCVATFTSGYSPLVEPAFTFASALNTTLNSFPNGTLPTQTQVVGDIGVKFLQYFA Q9C109 YIOG_SCHPO SPAP27G11.16; CHAIN 1..104; /note="Uncharacterized protein P27G11.16"; /id="PRO_0000116795" MGSCLRFFKQGAILHENNTNFTERSSSVFFECNPCYSIEKLKSNRILIAVRLFSFAFSSFSTTLRILRDFIIAASKCEFEKIWSTTFSISFLSFNFKSSESPSL Q9C111 YIPK_SCHPO SPAC343.20; CHAIN 1..113; /note="Uncharacterized protein C343.20"; /id="PRO_0000116796" MKVTMLPLQLNDEINSASFGPASSSTSHSSTIFCVHHRVRYIYVPRHCLLRSLTYATTNFTKFSKFVYYLAITLHTSLLTKLIYCHADLYALQSIKYKRLRINNGMLDSPKRE Q9C113 YDI8_SCHPO SIGNAL 1..22; /evidence="ECO:0000255" SPAC1F8.08; CHAIN 23..120; /note="Uncharacterized protein C1F8.08"; /id="PRO_0000304004" MSTSGMLFIFATFCPCFLSCCAFMSHWKLKDFSFRFLRMCGERSLVVCYPLKLLKQIRSLFSIAIGHLSLMLIEGSANLLSLEEISRTLLRILDFVGNKNMRTYLEVPLCRWHISQARPN Q9C114 YEXB_SCHPO SPAC1A6.11; CHAIN 1..106; /note="Putative uncharacterized protein C1A6.11"; /id="PRO_0000303977" MNHNVYLLTSFNLWSHGVYKISSISLSNSFFPHSFMFVKSLHLMTSQHIFKCLSSCNYALSILHNICLASFLYLSKCYYHTHILTSVRLDFCKSHAHTYIKSKAST Q9C116 YKO4_SCHPO SPAC1786.04; CHAIN 1..111; /note="Uncharacterized protein C1786.04"; /id="PRO_0000116830" MTRRFKVKMNQPRFYFLSLQSYVLVNWQYAICDSQDSNYKQVGGLACIYMRETLFGIHNLSVASPFMIGSLQPLVPWLIRQKWHKIDEPRQLPSTHHALPEGRWRSLTVSL Q9C118 YFFN_SCHPO SPAC1687.23c; CHAIN 1..104; /note="Uncharacterized protein C1687.23c"; /id="PRO_0000116740" MWILEKKNIFFKIIHIKSSRKFDFSNAIRIVLLPFSSNCCRNSYTVNNGTFTGRQIYTSICKSRIPPCLKGKNGKTTKSESEPMSQKHLKYVKKYINKVRILKK Q9C121 YIZK_SCHPO SPAC1002.20; CHAIN 1..101; /note="Uncharacterized protein C1002.20"; /id="PRO_0000304020" MTFQRSLRDGFHRLINFYFYPSYHDTVVHNLAFSTSDYIYFKHLTDRNDDALLKVDQTINKTNRFIFRKLKILCPSFLNYSFINIYCFGPYTMVGEEFLFF Q9HDT7 YJ52_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPCP20C8.02c; CHAIN 18..111; /note="UPF0321 protein P20C8.02c"; /id="PRO_0000036321" CARBOHYD 20; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLLLFCICCVFIKLVLAEVNLTFVDYAKLPPNYAELLANLIDQHGLMLFDTADVRIEAYNYLLNSITETNTDTDAYLCQLLTGQYTTDCYIFGDSVYEGPENINPSTRYID Q9HDT8 YJ51_SCHPO SPCP20C8.01c; CHAIN 1..247; /note="UPF0612 protein P20C8.01c"; /id="PRO_0000343139" MMSNENFDNDYNLPPPNDSAEDLKIFIKRYERSVDSTLLEIDENKREALEKYIEERDRKMKYEIECNERLQGWKKLAIEREISEEQSGEVQFPRWIDEWANTKLGGIFERIFSKMDSMQNDMNSRFDAMQNEMNSRFDTVQNEMTSMKGEMAEMKVEMVEMKRETIRLNTRIDLLEQKTEARFQSIEQRFNSIDQRFNSIDRRFDSMEQRLDSMDQKMETIDARSCRSIMLTRKLENTTRSDQGYLA Q9HDT9 YHEI_SCHPO SPBPB2B2.18; CHAIN 1..153; /note="UPF0768 protein PB2B2.18"; /id="PRO_0000116771" MLFFFFSSKKTVRVCRQLKTVTVLIVPVLPVYTNKVLCCSQCDWHEPANVYSIEQRRSHDDDLPTIKGSDASTQQYERKTYITDASPESQNLFLSKSKEEGVIFLCIQIKKLLGKWESKLKIIKFNKLAKYVYEGNQFFLFIFFLSICQIRNF Q9HDU1 YHEE_SCHPO SPBPB2B2.14c; CHAIN 1..230; /note="UPF0494 membrane protein PB2B2.14c"; /id="PRO_0000306278" MVRDTRNVDLEWGLELCKPEKVNKQNLFTNIIKPQKDKINIKTDKIKFFLDNLFTEFSKFHDSCYPDGRISTRSKLRWPLLIIWCILIVFAIDKNFEVKDFLSIWINESFINENRFYSEIWGPIAIYICLFVLLLLGLIYCSKIVVKAIPLISIVIAAVVVIIAVAMVKILYICHWLIYKILILAFGIKVKPLGDTLPTHNGETGSHSKATVGSDIEQIEFQNMPTPVKK Q9HDW4 YFW7_SCHPO MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:18257517" SPAPB2B4.07; CHAIN 1..239; /note="Uncharacterized protein PB2B4.07"; /id="PRO_0000116750" MGQCLSGNQVAGVANNGGEQPSGSNILRLPKLYTPNPLLTKEEVEVRRNEFWETCWAYGGSKEIWDVLHKVVTLLYEGNAEAATEMALAADLTIPENDISKGVYDSKGTFYEIPKIVARIPRAFAERKDSLDDEDDNMISSNDPTKSPEEHDTTTKSIASLKDAELDSSLETVLIRYSKDDKDYSIQINPNLPFSHAKSQLEEVGLENVQRFFFLGRVLQFKKSLSQQGWTSGMIIQAM Q9HDX3 YKN2_SCHPO SPAPB1A11.02; CHAIN 1..339; /note="AB hydrolase superfamily protein B1A11.02"; /id="PRO_0000363394" MAELEFTDEKFTKVDPELKEILKKHPAGTENITNIWQMRAMDEECRKQLAETILPLPDDVSVTDILIPTRDGTEIDGRVFTPVSVPADYRSLMVFYHSSGWCMRGVRDDDSLFKILTPKFGCVCVSVDYRLAPESKFPVAHNDAIDSFKWVASNIEKLGANPKRGFFLGGASAGGNFVSVLSHIARDEKIKPELTGLWHMVPTLIHPADLDEETMAQFRSYKETIHAPVITPKIMDIFFENYQPTPKSPLVNPLYYPTGHKDLPPSFFQCCGWDPLRDEGIAYEKALKAAGNETRLIVYEGVPHCFWVYYPMLSLRKKYFEDAIDGFTWLLSHVKKEDD Q9HDY5 YK15_SCHPO SPAPB1A10.05; CHAIN 1..294; /note="Uncharacterized protein PB1A10.05"; /id="PRO_0000304105" MKRQRPQDSMISVPLQNENSTTTPTKEVSHLNFPLKRPRLHSFVPTSKQAALSDITPDTPPAFKTPYSSLPYNLVPQNSSTSKKRPRAEDLLVIEPSQNSLVPSTQNNEWNEIARKRVSLESDHPDKSGQVIDLATGQILDKQTEDIDDDRNKSAVSKSLVRHPHRLKMLPFGIQSAHPYISSLNSNYPTTWHFASHYYPTDSKQLVKYHPTEVHPSWTVEEPVHYNTYDGVVNEPNSSVIIEELDDDYDELNDPMNNNDTPITNSTHSAQMSNLPTHDSMDIDMGGAVPSTST Q9HDZ0 YK01_SCHPO SPAP11E10.01; CHAIN 1..330; /note="Uncharacterized protein P11E10.01"; /id="PRO_0000317233" MSGSCQFLSRETLSSSLGWIPLINALREIFTENVVCPTRLHYPIDEDNPSSTANNILLIMPCWIPGKFLGVKQVNVFPENTKHGLPSLSSHYLLSDATTGCHLAQLDGNELTSRRTAAASALASSYLSKEDSTSLLIIGSGKVAEKLIHAHCSVRPIRSVRIWNHRFESAKSLASRASKELPSIQIDAVPIQNLENAVKCSDIISSATLSKKPIIVGSWINPGTHIDLVGGFTPHMHEADSKCIQISNVFVDTRKGALHEAGDLLTPIKEGLFSPNEVIADLFDLCNNKHSGRSQLKNPAEAITLFKSVGDSREDLAAASLAYKVHNKSS Q9HGP9 YM03_SCHPO SPAC212.03; CHAIN 1..129; /note="Uncharacterized protein C212.03"; /id="PRO_0000306378" MSIEFDDSSRHNMNMTQLMQLGAFDRRSGDDFMVQDFKNGIRDCSGIPVNNRNLAFKAYDAVKQKCDSSIKVFNIQDITIKGATWQHHNCQSTGKWYSQLYDYQNTFIGKQEYNILFDCYSYLKYNLNG Q9HGQ0 YM02_SCHPO SPAC212.02; CHAIN 1..136; /note="Uncharacterized protein C212.02"; /id="PRO_0000304107" MTALMNHIYIDNPLISNSTNNVTHELLIDLHELYNDGEISRIVLLRTLVTQSADDATWIINLTDDVLNGLPLLKKRDRYTTQCHSTNMASTYDCDTGANAVGARGGATLAADYRGDWGGGVMLYKPLVVKACLTEI Q9P3B0 YIL3_SCHPO SPAC1565.03; CHAIN 1..166; /note="Uncharacterized protein C1565.03"; /id="PRO_0000304054" MSVLSLSDLPSRFTFSSESSSSSSILFASTLASESRLSDLSTGSIRDSDCFSFNVHELNQSDEILEIDFRFFSKKKKNEHFSKRRKLSKVLTPPTNDEIKFVNRHTGSKPQPNFYSSSESSEKELIWFQPKMRVFLQSLSNMSYLSPSKFRYTTVYSKQPNACCIV Q9P3E3 Q9P3E3_SCHPO BINDING 82; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR000106-2"; BINDING 126; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR000106-2" SPAC750.08c; DRCGLLLERHAKIATDGQKPFLKKDSDFKEVPSGDIDLETAISLIKPTVLLGCSGQPGKFTEKAIREMSKHVKHPIIFPISNPTTLMEAKPVQIDEWSNGKALMATGSPLPPLTRNGKEYVISQCNNALLYPALGVACVLSRCKLLSDGMLKAASDALATVPRSLFVADEALLPDLDNAREISRHIVFAVLKQAISEGMSTVDLPKDDAKLKEWIIEREWNPEYRNFV Q9P3E6 YLZ5_SCHPO SPAC750.05c; CHAIN 1..344; /note="Uncharacterized membrane protein C750.05c"; /id="PRO_0000371805" MIDFVKSRDTVIQKSFFEEFNSQNREMGSFAYSGNSESVWTGENITSIWKTILINETGSYCVAARPMTMDGAEFNLDLMGYSVSEDQINNDEIGIWNYISVAEMGGVLLFLSYWIWTCLHFSKIIFPAQKVICLYIFLFALNQTLQECIEEYVFSSECIKYRQFYSVYEIIDFLRTNFYRLFVIYCALGFGITRTVPKYLMIKGISIVIALCSVYWISLYKDVYVVSEIFDMIQYEVFPAIWVYSICHLLKQCTSVTTYENASKARFFRRMLNAFIFIFCASPMLHYLSNIIFGNFDYRLSVIIGDLFTFMEKIAFPCYIMFPTHNEALAYNRNVAEEAQEKMI Q9P3V7 YI43_SCHPO SPBC1348.03; CHAIN 1..146; /note="UPF0742 protein C1348.03"; /id="PRO_0000373863" MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVYHNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISQ Q9P6K8 YLF3_SCHPO SPAC30C2.03; CHAIN 1..210; /note="Uncharacterized protein C30C2.03"; /id="PRO_0000304101" MTSNLKRNFEYLVQYIQPHLRPKSSHSISLGYLSKEKISQEEMQIIRATQKLARTKYMTLYCIPRAWLIPFHEFLNNRSYRFPKLDYSQTPIRLAIRSGKKSVHKSAVVRHHNTTRIRETFIDIIKALYVNEKHHYLPKQAIDVVIDSYNGGCVNLPPETLFYDMQRLWLTAMNTYENQKPPNLKLLLHDHGTVVSLGSDNVPLYRKLDS Q9P6M2 YKQ3_SCHPO SPAC688.03c; CHAIN 1..193; /note="Uncharacterized protein C688.03c"; /id="PRO_0000142372" MDKKEYCYYCFEVVAATLEHRKVRDKWNAKSWTRSIPLFVKFASGKGHDKQLRGCIGTFRARPLVTNLTYFSKQAAFCDERFRPISLGELALLECQIDLLVDFEPIDDPLDWEVGIHGVSIKFTANGIRYSSTYLPSVAAEQRWDQEETLESLIHKAGYYGSIRSLQITATRYKSLEIGCTYEEYLHNLELLG Q9P6M5 YKS1_SCHPO SPAC652.01; CHAIN 1..108; /note="Uncharacterized protein C652.01"; /id="PRO_0000116833" MLCLRYFIPMLLVANAAPYFFYPIFMLSMIARKYPCPYCMIILGLLINTRTLWSDSTFFSFNRNIFDTKAFPTELKEAGYRLVRLSWIRWLAGKESIHIPWLDATIKL Q9P6S2 YNL5_SCHPO SPBC27.05; CHAIN 1..108; /note="Uncharacterized protein C27.05"; /id="PRO_0000116856" MVHTTVYGLAYLFYSGINCILLYQLEIESKFYIRYQLIMRVQKETTDAFTLQLASKEVITSSIYNTFNNTNEHMYLQPICNRIFLMTSIIDIASFKAQVLFLNIFMIK Q9P6S4 MEU25_SCHPO SPBC27.03; CHAIN 1..622; /note="Meiotic expression up-regulated protein 25"; /id="PRO_0000096452" MSSIFGENIVSDSIVNMELTNPDNTTTMHPIYETNIEKEVQQEFSDNVSEKETIDSTKSKISLENIQQEMGALAKKIFHKLGVKATDLGFSNEHDDSQDSLQTLAPSPSYVPLLKVIGSSEEVNSNLVLTDLETNTDGYDPKFLISVRKFLMGSPNSGFVVKHEKRLPDGPRVLALRAISSVDEENRKERLSPDSDPVETESVYVDNGELSNQKVETVEISEKEQNDDPAGYSQYLLEFKKSKCQKKVPTLESIEENEGTEPHDNLTFMTDLGTPYYSLGNEFERKQILDEYGLLANDENLVIGHTLRAEYCFMFDESDILQLRNYEHTEKELSVLQFKGVSSRWDFRCCREERLLRLLLCFDSEHTGQSFIQLNDPENENEKEEQNSISIRELSYFSTKLISLILPKEAHKQRYIMLSSLAKTREADFFWSEEEKTNYTNELLSNPCKFLCELDHFDSFPHQQQDLLWKYLAEFSASLELDPNLALWKKQVIFSKIGHPKLLVMPISSFHCVQRFPDLVCVQTSTAETFLSVDRELTTYDLNTIKLLNTAPSRTAQNWLFIMHHLEIVGYLFPHLVHLDKQYSLLDYAKSVEHIPELGTVQRKGFLNKVAFDDNEALLYQV Q9P776 YNYF_SCHPO SPBC1711.15c; CHAIN 1..32; /note="Uncharacterized protein C1711.15c"; /id="PRO_0000116865" MKKRFDWCLILIDIIEKLLNEADLSILIIVIC Q9P7D1 YOFI_SCHPO SPBP4H10.18c; CHAIN 1..314; /note="Uncharacterized protein P4H10.18c"; /id="PRO_0000304050" MVASLIKRAKATSLRSLFQKNEMNFQSIRFNIHQFSTQPALRSEGSELIFGGRSFDSLLSSIKETMEEKKKKSSSFEKRDKRRVQLKEKSPLRTPRNRTQIIDARSTRKDTENESLRKNNFKRRTQFAFTGRATKSNAGVMDVQSPSTMSTSKNNVRNAERPASKKPVFGSKKYFDVINDSNVENKEETKDRNLDRALSKFTQSREKNEQNLSSKASVLRNKKSILLKKRNQDETQLTTEEDFSANNDSTAKIETSIHDHRDISRITPFELPFVNPKLFASFTPMSVALPAGRLLLIKQLQEKSTQSSSMTGLK Q9P7F5 YKY9_SCHPO SPAC1142.09; CHAIN 1..115; /note="Uncharacterized protein C1142.09"; /id="PRO_0000116836" MEDSLLLSVNISDSLFTFSLKPLFSQYRKHIYFNDCFYSTFNKTKTIIVVILSGKLSDLIDFKSYIEFVLKTNNSYSAILISYYRCIFIISLFHRPLTIHFLTNLTHGCTRSFTK Q9P7K1 YJN4_SCHPO SPCC24B10.04; CHAIN 1..199; /note="Uncharacterized protein C24B10.04"; /id="PRO_0000304014" MFSRNFTTPSIRIYLNSCVSHRSFHNTTVSQSWLSRIRDRFRGTKEDEKKQIADKDMAAMKVVIPPKKRVSKWKDIQLFEKFAEPSLNREDSLKMINEIRKSLQLQTPWSPEARLQAVKLAYQKTGRIVYDAPLQNIHNWDDLYNYYDKIVDYGDTTLHGRLAWKPTPGLMSLPNVVLHVDENGYPLERKKRRLSRSVA Q9P7L7 YOS6_SCHPO SPBC21C3.06; CHAIN 1..122; /note="Uncharacterized membrane protein C21C3.06"; /id="PRO_0000304109" MAFDKLANVATVDAIFAISSSTFLWSTWVLQRTILKRPNFFSPNPVVEKMVHPTLITWKLFSFTSVLTVSTFTFASCLIMRTIGVENIKEFGLYAREKLSFARAKPVKDDITSFPNHKISIT Q9P7M4 YIOE_SCHPO SPAP27G11.14c; CHAIN 1..689; /note="Uncharacterized protein SPAP27G11.14c"; /id="PRO_0000304019" MNLLSHQLRDRFPIKAIISKADEVIFANYKHTNDFFKITATTYALINSVIVSNNCCNRRFHSTWQKKKHDDLTATVPVIDFRKNQKLTSIVVNAIQAIYWYARRSNCLTGINEAEYIWKSLIPESIFYHFVSLQSFIRKYLTDVFYCSAQKVILLSTDDSVVSSEKLYIRIASILSNANDKVSFKESSINTNTVFKDVYVEVSSHNDEFLLKNSSKCWAFTSLLVDPLHFMFSQIVFEDLSGKKIMKFEDTAVSTASNHSKQFTKGNLLAIKYIGGLYNAVYLMGLKKNLLAFVENEKDDLFVAKIFLLAYSSSKNRKKIVPVDVWDAMIDSLYETINVEETKKETYKFTRSIKTVIPNKLISNESISILSIPESEKTIYQNFDLYVSKFNVARKELSEKELFNNSFSSSFNTLLASLLVKPTLCLISYLMIAKKMVVLQEANRLFLKSFAHPFHLERYHLHAVAAMGGLYQIMSSTHLKNLFFCSRKGIALTKLHSQQYNESTLFQYLSEFVHQRQKSLTPKQRIAIQELILKFMQRNFENSLYHQSFSSHWFISRLLINPIRMLCWHITDVGKTLDLGEAEKLLKYNHKQCPYIIYPSSLKAVQKLGGLQCIIRNDNLSHIFNCSRKYIRVQRYSDDDLSESSLLPRLVNLLLFFENSMGEVAWNKLSQTLMDMFEKETKSNSLSDY Q9P7M7 YIOB_SCHPO SPAP27G11.11c; CHAIN 1..73; /note="Uncharacterized protein P27G11.11c"; /id="PRO_0000116794" MTCNHENPHFLFKIDSYSKTFLLSCYCVSIYRLEECSGRFKPSSYSLHLLKSLSIIICENPSQTFNIGLNQPK Q9P7Q5 YFVA_SCHPO SPAC1834.10c; CHAIN 1..178; /note="Uncharacterized protein C1834.10c"; /id="PRO_0000116749" MNMPSEILLGARRWFASTSFSLAAVYDAPLKKAIGNIKKFSIGSLGLTYMISPVMLLLDAGGLSLGTRMSMVFLACTTTSLSTAIIHWAAKSYVSEATLKGNVLSLNTFNILGKKRLSQYTLDKLKIPDTNNSRPFANLESTTVPKRYFYLHPELATPIFNAIRQAQQPKQINKNDSK Q9P7U3 YI76_SCHPO SPAC977.06; CHAIN 1..189; /note="UPF0494 membrane protein C977.06"; /id="PRO_0000306281" MVRDTRNVDLERGLELCKPEKVNKQNLFTNIIKPQKDKINIKTDKIKFFLNNLFTEFSKFHDSCYPDGRISTRSKLRWPLLIIWCILIVFAIDKNFEVKDFLSIWINESFINENRFYSEIWGPIAIYICLFVLLLLGLIYCSKIVVKAIPLISIVIAAVVVIIAVAMVKILYICHWLLQNFNFGFRHKS Q9P7W1 YGQ9_SCHPO SPBC1703.09; CHAIN 1..202; /note="Uncharacterized protein C1703.09"; /id="PRO_0000304089" MQDNQVLANTASMIMPKSSFITTKQLWEIVLQGKVEATEFIPADVSDSTQTVDRSNKISPITSQLTIEPNKSQTIVKKNPDNLIFVAVNQNVQLQLSILKQQQNRVAAMESALQRIHLEITAMSEQLILQKYQKNRFFFMSSINALIRISRNCIKLLFKNSLVLLAACYFMNTTPSRLVINLIRSGYLILKRFANPSYISFY Q9P7Z4 YGID_SCHPO SPBC2A9.13; CHAIN 1..48; /note="Uncharacterized protein C2A9.13"; /id="PRO_0000116757" MQVVVNNAGDLQIVYEMKSAVVKRAEFLGVGGCTRTIGIDLKKGVSNF Q9P7Z8 YOUD_SCHPO SPBC26H8.13c; CHAIN 1..124; /note="Uncharacterized protein C26H8.13c"; /id="PRO_0000304046" MVIKRGFIGNTPKPSRCKRTKPIFREPNSPVNGGLVYNHPLHTAAAVKEAFSENRGFRTCHVCHRKNNMRLKVGTCESCKKHTCAICIRQCHKCESNVCSMCSKQERTFESEAFCPSCYPLDTY Q9UR21 YAIE_SCHPO SPAC24B11.14; CHAIN 1..166; /note="Uncharacterized protein C24B11.14"; /id="PRO_0000116435" MFAYNHKTLHVCLRLISLRNCSNTWTFVPYANSNRGLNINQQLKLFNRRSKIALSSFIIPTSVDILVKVAGFQRYIVNVEFSNVQSYFRYYNYISLYFVTHSKVPLNRLPNSMIPYTVFAHFDIVPYTTYSILTKYRCAQDKEREIVGLINASQSKLRYKFCGLRN Q9URV4 YBL7_SCHPO SPBC106.07c; CHAIN 1..167; /note="Uncharacterized protein C106.07c"; /id="PRO_0000116514" MSNLWRNLKSVRLPFRRAPTLPLYNVPVRRSISSSSSIPPSSSPPPRLTITQRVKELTKKYGWWSLGVYIGISVLDFSASFVLVRTLGAERIGYLEHSILNSIRRYFNWEIPESTASGEPEAYHSSIWTELAFAYGIHKALVVARVPLTAAIVPPLAKRFRGPRIRP Q9URW1 YI81_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPAPJ695.01c; CHAIN 18..117; /note="UPF0321 protein PJ695.01c"; /id="PRO_0000036320" CARBOHYD 39; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 65; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 71; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 104; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLLLLYICCLFLKFILANVDLTFVEYAKLPSKYAELLANATNQQGVMLFSTGDIRIGAYNYLVNNVTEINNDTDAYLCQLLTGQYTTDCYIFDTNSDDKPETFNSSIHLLNSDLDPK Q9URX2 YLX4_SCHPO SIGNAL 1..18; /evidence="ECO:0000255" SPAC922.04; CHAIN 19..117; /note="Uncharacterized protein C922.04"; /id="PRO_0000014213" CARBOHYD 86; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MKFFWVSSLLGLLGLSTAIPLSTEADALLDRKTIYFGMKAYDDVNCKGSTSYTISFNKCQAYPNINSINALTDGAVCTVYVYSSNNCTGEPVFQTDSDGIECINVDAFETGSWKFKC Q9US01 YIRD_SCHPO SPAC664.13; CHAIN 1..117; /note="Uncharacterized protein C664.13"; /id="PRO_0000304120" MDLEELQKIIQEEQIRCEREIAEAAEARNSSNSLIVVDEYSKESEDVLENGLEHVQSNEFTESEDYKSIERSLAVTEAVMARFEKEMGSLRDQMNFFHQILDNDNLDGFLTGSSKPC Q9US57 YIZ1_SCHPO SPAC1002.01; CHAIN 1..179; /note="Uncharacterized protein C1002.01"; /id="PRO_0000116800" MLPPTIRISGLAKTLHIPSRSPLQALKGSFILLNKRKFHYSPFILQEKVQSSNHTIRSDTKLWKRLLKITGKQAHQFKDKPFSHIFAFLFLHELSAILPLPIFFFIFHSLDWTPTGLPGEYLQKGSHVAASIFAKLGYNLPLEKVSKTLLDGAAAYAVVKVSYFVENNMVSSTRPFVSN Q9USI0 YCTF_SCHPO SPCC794.15; CHAIN 1..86; /note="Uncharacterized protein C794.15"; /id="PRO_0000116556" MSTSRLLLPTTNQQQNSSPVIKEVDLNQNTPIPVVWQKTKKPPFVSFPRHEPSETIVISSKPRLFSFAKKIKPEAEQRKRKRTTEI Q9USM2 YCLF_SCHPO SPCC16A11.15c; CHAIN 1..117; /note="Uncharacterized protein C16A11.15c"; /id="PRO_0000116551" MSLRHSTQLIVQTVKLGLPTARKACSLPIQNPVVAANRFFASSVHSRNPQEEDVIPPKENASREDATDSEAYVRSDWDNTPIPELEKETAEKAASERQHSEKVTINDKTSPPSVDEM Q9USN6 YJY3_SCHPO SPCC132.03; CHAIN 1..176; /note="Uncharacterized protein C132.03"; /id="PRO_0000116821" MNPKRLRITGPEDLTDAYDTMPFRCLNGSMPPKTPLNFVFKENDSHVSNGVGLKKDCIESIDDLNLDDWSEQQESILLMCYENELQKPITCTPMGPICLWAPPEPVLRSVHNTLLKMGWSISEKKMKKKLLELLAKNKKRRTMRKLEIDTNLSFLTDVQRDSPIIENAPLQSPFHF Q9USW0 YHZ2_SCHPO SPBC21B10.02; CHAIN 1..141; /note="Uncharacterized protein C21B10.02"; /id="PRO_0000304034" MSDEAYAAFLETANKPVPSYSGDSSQLPSKWLRSSKNMLEDPSFKTLAGKVKDEYFVSESDEKFHPICIDNIPDEFEEIDAKTFDPHQKYKKVIHAIEQSSGSKDIHYFSYEESSTKTVYYVLAHLNDNKWFGVATVGIYT Q9USX2 YO74_SCHPO SPBC1921.04c; CHAIN 1..117; /note="Uncharacterized protein C1921.04c"; /id="PRO_0000116867" MSHTKNLKLILQSKKLSELPTHRKSINMTIPVRALRCPIWLWPTYDAQTIPWKKKKKSEQHELWASVYNRTIGKLQLNKLTFIDLCDCFLNPTLLSNLFAAFSGYYPIEVTIMSRKV Q9UT14 YF1H_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPAC9E9.17c; CHAIN 18..72; /note="Uncharacterized protein C9E9.17c"; /id="PRO_0000042792" MSLGLAIAVGIVLGVVASSLCNKNNHLNRSREFSVIQKDEELNVLEINFNDFYRTTLNVGELSMSTRKTNNC Q9UT54 YI95_SCHPO SPAC806.05; CHAIN 1..125; /note="UPF0593 mitochondrial protein C806.05"; /id="PRO_0000339167" MKKEHASAFRQLWRAGMAAAISTRFPGHRFVIRDLLRNGFRQNNCSFYSKEKVENTVIFLEMAASRKSVEHLILKNRLHIQMFRRKAGQRLAHYSTAKERPYFLSAYDTYEWCLQRVGTIYNLYL Q9UT62 YKJ4_SCHPO SPAC513.04; CHAIN 1..100; /note="Uncharacterized protein C513.04"; /id="PRO_0000304090" MTAKMAEPLYFRIWSSLNIICLMVTFLNVQLSKTPIVLMPLFIALLKNNRKRETKKQTISVLVQKREEKTKLVLDDANNHNHAFLYHCQYLGQKKHVVIQ Q9UT66 YQA5_SCHPO SPCC4F11.05; CHAIN 1..80; /note="Uncharacterized protein C4F11.05"; /id="PRO_0000116887" MEIDLLSFSIKRILNLSAFIHIYSRYFRPDTFLSSKQSITMSVKKPYKHPNCTSVIHINRVAIVIEQEKGKKSKQNLIPS Q9UTC2 YIDH_SCHPO SPAC227.17c; CHAIN 1..121; /note="Uncharacterized protein C227.17c"; /id="PRO_0000116789" MNNFKENDEKSTFGQYAELDKILDLKKGIPEDPCSLQYYFDQMAMCLTVFSQMNHYYRYGEYNRCKGNFKDFKWCLSTKSKAHEEAQEGLRKRRLQQWMKFRQGPNSEDIWKMRTSPKSSE Q9UTG3 YKEE_SCHPO SPAC1805.14; CHAIN 1..452; /note="Uncharacterized protein C1805.14"; /id="PRO_0000304108" MFRRNTLTPGKGRNSLDMFSVNDFMTWIDGMKKTSDENGCSPFTLKPIKSTSDRKRRRHSRMSIVNVWNQSPTSYRDQLLHFNHESDVSIDDTSEVAGEETFGQIERFEYLLSSDGDGDGDVEIENPEVDDYQVSEHDFGLEDDFNGDGCQQMIEIESDEAISEEEEDLSNENKSESQLGESFSFNQDNTFVNYASPASITEEFVEPKDSQFNHDVNLMQGSAPGYSTVEPEDNFASEIQTNAPEVHLNYENSDYTEDHIDLLDHHFCDLSEISKFNHQHSGKPDHPSLVSNASLAPFIVEGNGIKNGLLHYNMETAETDESYTDLDDTFARLKNLSQRHTNHSTDHHDDTVDSHLLHSFVSAENANEPTNDVDDNSLQEQVADASQFVSFLETTKTVATSNLRSTKRKLSEILENGQSGDCSLTDTNVDFDISEKQASGNSRSMIPLRKKR Q9UTG5 YKEA_SCHPO SPAC1805.10; CHAIN 1..527; /note="Uncharacterized protein C1805.10"; /id="PRO_0000116826" MVLVEHFCIHRCTPDGVIEMLWMYQSELMGNKQPILNKDEMAANNPELEALKNQIALFHGMYGFSVETKDILKEQPTDSKSTTSSAPKNSPFSLLESYDCLQVDTATVQKVLIKRPEGCRELHSCNVLMNNDEKNTLSLTPSIFLSVMKPCPKTSVLVTTVAALWEQFNIFHGSYLFDEIEKKSSFEIIDRWWTSVLSPLECGGYLLKSLSVLPVLHSLDDPLVKKMNDVIRKEDGTMGSLILFTKSGQPRLLSLQGLRLKPEFRNLLSYYCSHNYQHLIENESADINIAHRPLTTLFSDTDSNLAITNEVGEMTLRIFCLKKKSNKRLLAILWKLGQTSSEEVSNAFTNYIIGLAPLSQSVFDSQASTGFNFKIQKRVETELDMFWYIVANCTTGLAVVNTDFPLNDAHHLWNHLENLCNNQSFNSCQLQKITRGYWISLQQKEYNSRIYVDTVADQSQTYTPTRRFTKQGSQGDFNAIHSRKVPVTHTFTYILISKTNRWNSLHDTKAKIQRFIDQFDLTPTLYD Q9UTI9 YKZ2_SCHPO SPAC15E1.02c; CHAIN 1..148; /note="UPF0591 membrane protein C15E1.02c"; /id="PRO_0000339165" MPSYTHMPYVRPSAILLGIAFDHAASFLVYGPLMGDIWKRAMSTAPHVEYDAGSKTKKVATTYVSNFLSTAVQSYSIAALLQLTGTVTLKGAFFVGLYVFGASGLPDVVDYMFTESRGTPYILVKTISSLVKSVGLSVALIGYGVRRI Q9UTM1 YIV1_SCHPO SPAC144.01; CHAIN 1..112; /note="Uncharacterized protein C144.01"; /id="PRO_0000304007" MSKLKAQSALQKLIESQKNPNANEDGYFRRKRLAKKERPFEPKKLVQQQQRLKEKKKNENIIYLKKTMRVTPSEEKIHEMINQKRETKKRKRKQKKKNDDDYGVFEEDMLEL Q9UUD9 YNZD_SCHPO SPBC17G9.13c; CHAIN 1..317; /note="Uncharacterized protein C17G9.13c"; /id="PRO_0000116866" MRFISTVTKRRPFQAPNDLVHPLSNILGSLVTYDSRLHLPQPKDRQCSTLVPLYRRLLKATRRFWDPMASQILISHFQAYARKARKSNPNPHKRRIKRFRNLLKTFACRIERANDGDHQAIWQTLRYAYSQTGPLRHRRLHYLQDNKIRPSKIPKSLPSNSPVRLPYISSLLSAVFEINMENAKIRHLPSVIFDGLIEKNKDRPYHINLSCKRAYDELLPRIAVPLLPHEYHHLHSLLLDVTLRNPQISRPPFAPLNPRKGFCRILQRSLITFLSAVCYLPYNPHPTSKPVVSWDSLSDIQLRLNVGKVLKKSVKKR Q9UUH5 YKI7_SCHPO SPAC630.07c; CHAIN 1..430; /note="Uncharacterized protein C630.07c"; /id="PRO_0000304021" MDQYRDLPKEDPDTAIEYESGVDEESSLKIEKFRVLIFGKDNSQDDLVKSVFNLSKLSEKEKMPFGIKCESEENPNFESYHSKVGKKSCKRFMRWLKANAFAEERDIDCIWYQLNLLDISDEDILCLQYLQGCLIPIVSIIYDFNEFLSPFTKSFLSKIGESNTITVKGMPLADVLVFRKKVLKLVSQLSFMTDRKELVYTTCLALEDDDAYTNFVSAQQEDSSCKFYGGILIGVSHCKYAAAGASYPLPIPASGLLAQKLAIGLLCKDIIKLWNLCPESSILTKEILLELPKASDVAKSIGKMILTSMFVPLWLLKGIWEAPATAKIIIGSIADVTLPVQRMYYFIKAGGKLDVPTIHAFYQHYKEFVRPKCLEHIAEITTFNVVTAFSSEAVYQEAIRLLDRFRYVSKSSEEDLIVPSFVVNDLITYD Q9UUI9 YIY3_SCHPO SPAC22F8.03c; CHAIN 1..133; /note="Uncharacterized protein C22F8.03c"; /id="PRO_0000116798" MSTVLIPTFVPYGKNLLNTSFSFSSLLCILCFYKDGPLLFLYSPLSASYYCLLYASYTWNFVLSDEAYFQAAPGRSVRFAVLCLKPMATKKANKMHVFMQAACFHFRIATMTVIGNMARSDHDTALNCVKRIN Q9UUM6 YGF2_SCHPO SPBC405.02c; CHAIN 1..447; /note="Uncharacterized protein C405.02c"; /id="PRO_0000373867" MTFENLGGHAQRRDESAYRLGEEDGRQKGESSRKKRPPLSRKNPSNVSFWSNEPIIRHSSVKTDRPQFHRADSTVTEQSSEILFDGNAESAEPLSKRSPPFLAYTPKRAVSATLATTQSSPISTSFNPQLPSNSNTNRFDFGSESQLSSNYTNDTGLSLLSLPKSVPHSPAMHKRTPSSDPNNPFGSTFANKFLDHIPAEPLPLPARPQISDLSFFRKPSLPSALQNIVIEKNASQRSVSEPLHNLSSRYSHFTSPHIDDSQHFPPMEFFARSDELPNPFVPFFDLDSKPNLSTLQDNASLTSQGSNLSSQNSGLSSSSSGIFGRMPIPAQSLDTTMLRTDSNSNIRRATTSFIANSEKENSSNFIDPQKYASIKFKNGNGVSKFMFLFTFGIVFPPLWILASFLPIPRTKIHQMRVKHVHWRIINRVVACLGVAITFLFIGLGVSG Q9UUN3 YQ86_SCHPO SPCC297.06c; CHAIN 1..230; /note="Uncharacterized protein C297.06c"; /id="PRO_0000116886" MQGKINYKDITQKEMFNEIFKEYVKEEKQIDLGTCDQDSVHDLWRRFVKRWNDGKMKSKWYSLGKRISQPSYARLVGPSRPTLENLQDRRELQEQLNELRKLSRKSAFKSQAKRETELLDEILPKEPAGSKEAMQQKKKEKRAALKHYREASDNEEDLKETDLYGDRDSFQSRLKQKKQRSEFRASKREMERLERDQELRNKIEERNKKELETIEKLRELAKARLQGFSS Q9Y7I1 YE1K_SCHPO SPAC1B3.20; CHAIN 1..78; /note="Uncharacterized protein C1B3.20"; /id="PRO_0000116693" MSSNSNTDHSTGDNRSKSEKQTDLRNALRETESHGMPPLRGPAGFPVNPRPFSHGGNANLDRLNLKEPVDLEGPKDEQ Q9Y7I3 YD53_SCHPO SPAC6C3.03c; CHAIN 1..100; /note="Uncharacterized protein C6C3.03c"; /id="PRO_0000116585" MDVFFLGLLVVIAIFTNAKRYSSFRFLFPSKNLDPNETKWGWNIRIATFRSLLNTIPSIPHWRTMWGTVRVGIVHTPSAKVRERVDCSYYFLARGFKTQK Q9Y7K4 YGI2_SCHPO SPBC2A9.02; CHAIN 1..295; /note="Uncharacterized protein C2A9.02"; /id="PRO_0000318142" MRIFVTGAAGFIGSEIVRQLLEAGHEVVGLVRSEENAAKLRAAGGTPYIGTLEDLDTLKKGVAQCDGVIHTAFVHDFSIYQEACKLDARVIEAIGEVLRGTERPLITTSVTAVLSSNGKLGTEISEVPQPPIPRQLGEVTTLKFASQGVRASILRLPPTVHGAGDHAFVPMLINVAKNKGVSAYIGNGMNCWPAVHRTDAANLFVLALEKETAGSIYHAVAEEGIPIKEIAGMIGKRLDIPVISVSSEEATEHFGFLSSFLSVDNPTSSILTQQRLGWKPTHSTLMTDLASDAYF Q9Y7K5 YGI3_SCHPO SPBC2A9.03; CHAIN 1..426; /note="Uncharacterized WD repeat-containing protein C2A9.03"; /id="PRO_0000316559" MSNGEFIDQYLLPESGAILQDYLDDYFYTSWYTGNRNLIQLDHYGFPTASNFELNPKSTDNCGTVDFQGIPWGNKAIGKRKNFRLYRLHTYSLSCNHSDWSPEELSLDTVQVAAEDSFYEFQRFLKNPNCLRNHHHLCKSVKVVGEHSVIYVSNNSIRMENTLHDNSVQIIDLKNNILQKKAISCLDTTNAVGCLGTLYGQYCIFNFKNGSFSTRKLSDDSINHIQLFSEKKFILGCNDGAVYVEDVQRTSPILVYRCSNAVNCVQLFDETPLALVCTDSKDAMLIDIRSNSVSAKLPHSDSVLTGSWHPNGNILATGGQDTTAKVWDIRALGKSFRNLGSQMSAVTNLCFSPLGESLAVTEQADFVQLFDTKLFNTSQVIDFFGEIAGTAYSSSGDSLFIGVDDPMLGGILEFRRPLQHPLSFIF Q9Y7L5 YGJ3_SCHPO SIGNAL 1..20; /evidence="ECO:0000255" SPBC685.03; CHAIN 21..452; /note="Uncharacterized protein C685.03"; /id="PRO_0000304033" MQFFGSLFVSLLGAAGLANALPSPGIPSNDKDLAIYPPVDANNTTSQDVVIDVVLFNGTEWISSRERFSLVSPGWASIYGPSGQSSVGSVLYSPILDYIDNAQLLVLDDVSFGVFSSLANSVTGYASNYTQSSSNSTSTMNSTGSVSGGSVYPTNSTTNSSISWNSSTSAATNTSSSSSSSSQSSVVSVNSEIFSYFGLSQQYVNYSTSRLCVVGTPRANMSTVSVTNNGSAVSNYTVNTNGWTSSNFKCVDDVVANIFGLDFYTAAVLSEVSILRSFALCNATTSSSLFRQIASYGVYGSFHFSSSESGSFANLIGTNNYFMTDVKSSSVVIVQSETSCSINSASMSSNTTYFYWNSTSSLSSSVFTNTTSSSNSTNSSIPTTYPSNSTTYQNITTSYPWSQPVVNITDYLSDNGDGHFVLAGDGNQTIGDFYVMNWTTIASGEYLVPFNY Q9Y7L9 YGJ8_SCHPO SPBC685.08; CHAIN 1..97; /note="Uncharacterized protein C685.08"; /id="PRO_0000116759" MVLVKFKREKLTVMLEVQPGLSVYDAVKLLKSALNLPPDSILRIGSFEQNDWVAMENDALSKTIITNNTEYAFAEGEEPLLVEKPKDYDDMSEEISP Q9Y7P7 YQ63_SCHPO SPCC191.03c; CHAIN 1..117; /note="Uncharacterized protein C191.03c"; /id="PRO_0000116883" MRSNNSSLVHCCWVSPPSLTRLPAFPSPRILSPCYCYNKRIRPFRGLTSYRQASYSLGFPLGLLVFLHSLIVARFFVASKSRSCIVRSLLFWINLDSADSRISVLFQCFFCIDIWTV Q9Y7Q0 YQ66_SCHPO SPCC191.06; CHAIN 1..138; /note="Uncharacterized protein C191.06"; /id="PRO_0000116884" MSHLFILSCSVYDFSSILLHQYFTQFFVLRYASPSMHLDWRFPSLRIHSYPKDQSTHAWKMHCMPTEIIAYQPIPVFQRLLHSNDIYFPYFQTRYTTLIMFNTVCSSSPNPVFTLTKVIARKKGKHWIGSPCHSAESS Q9Y7Q3 YQ6A_SCHPO SPCC191.10; CHAIN 1..149; /note="Uncharacterized protein C191.10"; /id="PRO_0000116885" MHSSRRKYNDMWTARLLIRSDQKEEKYPSFKKNAGKAINAHLIPKLSPKMNIMRSSCGRQEISQFQTKIRLFFLPHSCGVNDVTDLGGKDDELVGKRKKWKTEVRIETSMAECNGGKDFTEMTRIYLSIRKNFFQICLKTHSPQLPLGR Q9Y7R1 YCX4_SCHPO SPCC2H8.04; CHAIN 1..266; /note="Uncharacterized protein C2H8.04"; /id="PRO_0000303998" MSAAWRKKITNAHRNECLQVYRSLLRSCDEIQNRPLGEKLSKIVKARTRHYQNVGNAYKAEALLKDAKKQCETLKSALNGKLPEVNIESHMLSKYRKYLNEGGKQGDVGITKPHTKTKKLKSNSIFNYVRNGEVLYHLVSTTGGDTFLRPKFWPQSQRISGMLKKRITMKENKHRLIQSMSCMLRHAKLEDEFMKAYISEEDVGYADEIHKCIQMVLSDLDSIYKRESKNWHIVSQFYNMLELEAARQKLENRYLNFWKVSRRSSP Q9Y7R9 YJFB_SCHPO SIGNAL 1..23; /evidence="ECO:0000255" SPCC306.11; CHAIN 24..283; /note="Uncharacterized protein C306.11"; /id="PRO_0000304040" MFAFASFAISAIFFLCSFSYVSSIKLCGIPGAPACKRREISLYKRATDTFPDLSSAIASTSYYNISEGTYCHVSGSNLCVSPDVIAICANHSTVLLNCPTVLGYPKGRGSACVETNSSYGLTRGLCQIGSSNYSTSANSSNFDNANVINVTTSVSSGSTSTHSKRSSGISLSYTNIVDQPILFTRDSSMDWSCNMTLCNTDYPYLVNTCFNGTQYPVNCNSALRTPFGGATCRNIGYKGQGICVYTNDSRIPVADDHVIVNTTSKINPNITSVFNYRDNAFLW Q9Y7S0 YQO1_SCHPO SPCC569.01c; CHAIN 1..323; /note="UPF0612 protein C569.01c"; /id="PRO_0000343138" MMSNENFDNDYNLPPPNDSAEDLKIFIKRYERSVDSTLLEIDENKREALEKYIEERDRKMKYEIECNERLQGWKKLAIEREISEEQSGEVQFPRWIDEWANTKLGGIFERIFSKMDSMQNDMNSRFDAMQNEMNSRFDAVQNEMTSMKGEMAEMKVEMVEMKRETIRLNTRIDLLEQKTEARFQSIEQRFNSIDQRFNSIDRRFDSMEQRLDSMDQKMETIDARSCRSIMLTRKLENTTRSDQGYLASPVPFLNGNEPANSGLPPIERVEDIDELSKEQCVQYLKGYGIMFSPAETIKLKKRLRDAVGLWSKASTEYEFHQFH Q9Y7S1 YQO2_SCHPO SIGNAL 1..17; /evidence="ECO:0000255" SPCC569.02c; CHAIN 18..113; /note="UPF0321 protein C569.02c"; /id="PRO_0000036322" CARBOHYD 20; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 39; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255"; CARBOHYD 65; /note="N-linked (GlcNAc...) asparagine"; /evidence="ECO:0000255" MLLLFCICCAFIKLVLAEVNLTFVDYAKLPPKYAELLANLTDQHGMVLFDTADVRFEAYNYLVNNITEINTDTDACLCQLLTGQYTTDCYIFDDSVYEGPENINPSTSILIKD Q9Y7S2 YQO3_SCHPO SPCC569.03; CHAIN 1..375; /note="UPF0612 protein C569.003"; /id="PRO_0000372417" MTSNENFENGFDLPPPDDSAEDLKLFIKKFERSLNSALLEFDENNQETIENFRQAKEHKMRFETECDQKLRNWKRLAIEREVSEEQSGEVQFPRWIDEWANTKLGGIFERIFSKMDSMQNDMNSRFDAMQTEMSVMKNGIASIKGEMAEMKGEMTVMKNDIASIKGEMAEMKGEMAVMKNDIASIKGEMAEMKGEMTVMKNDIASIKGEMAEMKGEMTIMKSDIDSVKGETTTLKGEVTAMKDSISQLDRKIDLLDQRTEERFNNMAQTMQKIDDRSCKSMMLTRKYENMVRSDMHYSAVPVPFLNGDEPRDYELPPLASFEDIDNLTKEQCIQYLHGYGVNKFSPLETVKLKERLQEAIGLWSKGHESHKYHTF Q9Y7S3 YQO4_SCHPO SPCC569.04; CHAIN 1..121; /note="Uncharacterized protein C569.04"; /id="PRO_0000116896" MSTSYLCDENRKGENRKVEIQELVPYLYSVLLRGVPSRPVFDSRLKFAVKVPVYPKRPLYTTDTRTHYYLKNCFRILEWEIVSHVGGNELLINRRVIDVNNFFICQDANSGPFCTAWRFTH Q9Y7V1 YCHC_SCHPO SPCC645.12c; CHAIN 1..198; /note="Uncharacterized protein C645.12c"; /id="PRO_0000303994" MSSARELLRKVKQERLGQKRGLKASSQELKRQKTRDHKSFENLGRDQSRELAVSDFNEKQSTEPPKDTRAVSALPENFFDESIAKNKELIEEEWNDFQNEIGIIEENAVEQEITLQQQQLLAEKDEENEIADNDLEPEVYDILYEEESKLGESRDLIRRLKQKRFETKKNNFSVKESSNLSNNDSDASLDEDTLLWGL Q9Y7X4 YGRG_SCHPO SPBC365.16; CHAIN 1..277; /note="Uncharacterized membrane protein C365.16"; /id="PRO_0000304027" MALNSQPPLSPKPVPSNTWKRIGIDAFAATAASAMISPFILTIDRSIVENTSGRSTLLRSVSRSIKYVLSKPGAFFFSAPFALVFTLYSGTYMTANSIDTLDNIRHKNPVFKAETSGWFKFCSVTAANSGLSILKDSFFTKFWGTGSPRPLPWSCYGLYGLRDALTIAFSFNIPPMIAPLLPGGLITAQLLTPCAVQFISTPLHLLSLDIYNRGGPNISAANRVMQVRKHLLKSTFARMVRILPAFGIGGVTNRKLRTTYLDSLQQRTMKKQQFALA Q9Y807 YN92_SCHPO SPBC146.02; CHAIN 1..263; /note="Uncharacterized protein C146.02"; /id="PRO_0000304098" MNGIRKKPATLQLHNIKTSCFIDGSDDQSDRTRSSSGDSTSNSLKLSHHISDELINAIYKELKSPVSPWDKNISQHSPWLLEAASNSIGDSSPLLSPISPLKLRFHKYSVSKQLNSVGKQGFGLSSNHSRYASPSSPARLARGALGEELSNSQYRLECAAIQKLVAQKRANRRSSKSTLKNSANDIEFFDIEEVSSRKGLIDRTPSKRNVTSRVSDAYSRLKSAVKGESSLSFKRNRSKSKRKIQHLGLTEFNGWEHHQCDWL Q9Y816 YOND_SCHPO SIGNAL 1..26; /evidence="ECO:0000255" SPBC1105.13c; CHAIN 27..142; /note="Uncharacterized protein C1105.13c"; /id="PRO_0000014214" MITEFIKSFLLFFFLPFFLSMPMIFATLGEFTDDQTHHYSTLPSCDLLLIRGEVKENARCFLHNPKISHQHHSFWSLIEGCLEALQFGLLAILQGLFSQFAWEACSCTFACMLLTSERTEPSYPFSEITEVSRGGLHFVKLN Q9Y826 MEU31_SCHPO SPAC1A6.06c; CHAIN 1..185; /note="Meiotic expression up-regulated protein 31"; /id="PRO_0000096454" MSCISEIGKFVKSIEYIKLPCLFIFAAIVGMNLSLLYCLLKGWKNVMIWGIETMLFGAIGIFFAWKKKLSWEHLVLLWSTIDAFFSMCLRSCTIIYFSMNPYMLCEILNARNVISCSLNTQKFFFIIVAASNVYSIFQLCGCLLMFNNIISIRPSERTEPEFNFDLEKGVAFASDSEFPEKSICI U3H040 YBS9_SCHPO SPBC18E5.09c; CHAIN 1..128; /note="Uncharacterized protein SPBC18E5.09c"; /id="PRO_0000429005" MTGPFRYNGGSVRSFALTTNFSFPSYDLSFNETEHGVFCYVSRPLTKERSCSHPYISLGSSYGIPDAENIEYPRDARYHSPLLFTVRLLLFSTYWSYSLASQHFKVFTVKESLLLLIISSNFGEPFFS U3H0A9 YJ61_SCHPO SPCC1884.01; CHAIN 1..478; /note="Uncharacterized protein SPCC1884.01"; /id="PRO_0000429006" MNIQKYGLSSDISIKLKTKVDKIKEKKEEVLKLNTSTFYGKAEVRLINDVSILDGINKSVVRYDTGKISEGLLHQEEMKRGVEKRPNCSETRKTHFHDNCVGLLYNILRLFYLIDINFDEYDAYATYFQDNALLVINVHLFGDQPFSSLENFVVQPVSVNVICKPELNETFNSNSNYLKVGNTIDEHFLKELVNGTQDIENIIVRLVKDNRLFTQFDIAYGMVAQVFMQLKPFLVEGTYWIAEPLLMNIPELKTQRGRYPSLLDGHLWKLTNSLKLLLKIASYTQKYLLSIEKYSEEREKKMLLNGEINESSGLLHDVVLAAELFNVKHASYYNVHAGLDRFQFLRKPLKSLVMFTDVVKERDGTCDFCGTYFEDSRMSTSYLCDENRKGENRKLEIRDLVPYLYPVLLRGVLSLPVFESRLKFAAKVPIYPKGPLYTTDTHTYNYLMNCFVPMNEEQVLSACYRFFAKSAENELFEA W6JQK2 YBW7_SCHPO SPBC651.07; CHAIN 1..268; /note="Uncharacterized protein SPBC651.07"; /id="PRO_0000434007" MIVIEPTILYEAAALYTRYTANGGDSNDVVALLVGPIVQTLSIPSSTSSAPLVTSVREILELACNDAVLDKSFLNERLEHCKLQDFPLVGCLVLGNRVDHRVRSIAHQLQEATAFPYLMLFPSNFDLTQLKLFRLPDFNNKDQFWKEEWSTEQYEIAENPSGYASALHTLTQLDDGSETNAINVSTQKFAIQKLQSCAMRVREQLEYNPTTFASRDLSSISYICRLLDTMDLPSDTFSHQKSQASFLCALQQILRCTELIEKVYSNGS