SPS1_YEAST
ID SPS1_YEAST Reviewed; 490 AA.
AC P08458; D6VTE3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Sporulation-specific protein 1;
DE EC=2.7.11.1;
GN Name=SPS1; OrderedLocusNames=YDR523C; ORFNames=D9719.27;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7958886; DOI=10.1101/gad.8.18.2162;
RA Friesen H., Lunz R., Doyle S., Segall J.;
RT "Mutation of the SPS1-encoded protein kinase of Saccharomyces cerevisiae
RT leads to defects in transcription and morphology during spore formation.";
RL Genes Dev. 8:2162-2175(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 396-490.
RX PubMed=3023934; DOI=10.1128/mcb.6.7.2443-2451.1986;
RA Percival-Smith A., Segall J.;
RT "Characterization and mutational analysis of a cluster of three genes
RT expressed preferentially during sporulation of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 6:2443-2451(1986).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
CC -!- FUNCTION: Serine/threonine protein kinase required for spore wall
CC development. {ECO:0000269|PubMed:7958886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; U13018; AAA64833.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64963.1; -; Genomic_DNA.
DR EMBL; M13629; AAA35079.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12353.1; -; Genomic_DNA.
DR PIR; A55162; S47946.
DR RefSeq; NP_010811.1; NM_001180831.1.
DR AlphaFoldDB; P08458; -.
DR SMR; P08458; -.
DR BioGRID; 32573; 108.
DR DIP; DIP-6598N; -.
DR IntAct; P08458; 47.
DR MINT; P08458; -.
DR STRING; 4932.YDR523C; -.
DR iPTMnet; P08458; -.
DR PaxDb; P08458; -.
DR PRIDE; P08458; -.
DR EnsemblFungi; YDR523C_mRNA; YDR523C; YDR523C.
DR GeneID; 852135; -.
DR KEGG; sce:YDR523C; -.
DR SGD; S000002931; SPS1.
DR VEuPathDB; FungiDB:YDR523C; -.
DR eggNOG; KOG0201; Eukaryota.
DR GeneTree; ENSGT00940000176215; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P08458; -.
DR OMA; KYDPMKV; -.
DR BioCyc; YEAST:G3O-30039-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P08458; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P08458; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0051229; P:meiotic spindle disassembly; IMP:SGD.
DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IMP:SGD.
DR GO; GO:1903024; P:positive regulation of ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Sporulation;
KW Transferase.
FT CHAIN 1..490
FT /note="Sporulation-specific protein 1"
FT /id="PRO_0000086679"
FT DOMAIN 18..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 454
FT /note="N -> NVN (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="G -> R (in Ref. 2; AAA35079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 55704 MW; 6143055E85BAF4FF CRC64;
MESKEISIRS RTPPSKLYSI QSCIGRGNFG DVYKAVDRVT QEIVAIKVVN LEHSDEDIEL
LAQEIFFLAE LKSPLITNYI ATMLEDVSMW IVMEYCGGGS CSDLLKRSYV NGLPEEKVSF
IIHEVTLGLK YLHEQRKIHR DIKAANILLN EEGMVKLGDF GVSGHIRSTL KRDTFVGTPY
WMAPEVVCCE VDGYNEKADI WSLGITTYEL LKGLPPLSKY DPMKVMTNLP KRKPPKLQGP
FSDAAKDFVA GCLVKTPADR PSAYNLLSFE FVKNITITNL KSDVDLIKQK KVQERYTKVP
KYPLQNRLYK NSNTVRGKEF WNFESTRLST TQISKEELSP ITQDSPTSSL NMESPYLLHG
QTVTPITNPS SSSFRKCTQP VFELDSGMDI DSGCPNAQAE TEIVPLSNHN KKHKKNDIQA
LKIEKFDYLK NIVSHILNRM YDRARDDETR KYVNEMLKQF IKTEANVPGF NEVFIEEISL
RIEAIKKGFV
