PEF1_SCHPO
ID PEF1_SCHPO Reviewed; 288 AA.
AC O74456;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase pef1;
DE EC=2.7.11.22;
DE AltName: Full=Cyclin-dependent kinase pef1;
DE AltName: Full=PHO85 homolog;
GN Name=pef1; ORFNames=SPCC16C4.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10982385; DOI=10.1091/mbc.11.9.2845;
RA Tanaka K., Okayama H.;
RT "A pcl-like cyclin activates the Res2p-Cdc10p cell cycle 'start'
RT transcriptional factor complex in fission yeast.";
RL Mol. Biol. Cell 11:2845-2862(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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=2.7.11.22;
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=2.7.11.22;
CC -!- SUBUNIT: Interacts with the pas1 cyclin.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA20750.1; -; Genomic_DNA.
DR EMBL; AB045127; BAB16402.1; -; Genomic_DNA.
DR PIR; T41101; T41101.
DR RefSeq; NP_587921.1; NM_001022912.1.
DR AlphaFoldDB; O74456; -.
DR SMR; O74456; -.
DR BioGRID; 275932; 444.
DR STRING; 4896.SPCC16C4.11.1; -.
DR MaxQB; O74456; -.
DR PaxDb; O74456; -.
DR EnsemblFungi; SPCC16C4.11.1; SPCC16C4.11.1:pep; SPCC16C4.11.
DR GeneID; 2539366; -.
DR KEGG; spo:SPCC16C4.11; -.
DR PomBase; SPCC16C4.11; pef1.
DR VEuPathDB; FungiDB:SPCC16C4.11; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; O74456; -.
DR OMA; HQCVLER; -.
DR PhylomeDB; O74456; -.
DR BRENDA; 2.7.11.22; 5613.
DR PRO; PR:O74456; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0042764; C:ascospore-type prospore; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IPI:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; EXP:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:1905412; P:negative regulation of mitotic cohesin loading; EXP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:PomBase.
DR GO; GO:0007165; P:signal transduction; IC:PomBase.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IGI:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..288
FT /note="Serine/threonine-protein kinase pef1"
FT /id="PRO_0000086505"
FT DOMAIN 3..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 288 AA; 32737 MW; 7A3077D33F40A8FA CRC64;
MNYQRLEKLG EGTYAHVYKG QNRVTGEIVA LKVIRIDADE GTPSTAIREI SLMKELRHPN
IMSLSDVLQT ENKLMLVFEY MEKDLKKYMD TYGNQGALPP SQVKNFTQQL LKGISFCHEN
RVLHRDLKPQ NLLINSRGEL KLADFGLARS IGIPVNTFSN EVVTLWYRAP DVLLGSRVYS
TSIDIWSVGC IMAEMATGRP LFAGSNNEDQ LLKIFRLLGT PTEQSWPGIS LLPEYKPTFP
IYKAQDLAYL FPTFDPLGLD LLRRMLRLQP ELRTTGQDAL QHAWFLTA
