CEK1_SCHPO
ID CEK1_SCHPO Reviewed; 1338 AA.
AC P38938; Q9Y7N8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Serine/threonine-protein kinase cek1;
DE EC=2.7.11.1;
GN Name=cek1; ORFNames=SPCC1450.11c;
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].
RX PubMed=8065367; DOI=10.1128/mcb.14.9.6361-6371.1994;
RA Samejima I., Yanagida M.;
RT "Identification of cut8+ and cek1+, a novel protein kinase gene, which
RT complement a fission yeast mutation that blocks anaphase.";
RL Mol. Cell. Biol. 14:6361-6371(1994).
RN [2]
RP ERRATUM OF PUBMED:8065367.
RA Samejima I., Yanagida M.;
RL Mol. Cell. Biol. 14:7683-7683(1994).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525; SER-748 AND SER-1211,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May facilitate the progression of anaphase through direct or
CC indirect interaction with the cut8 protein.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D31773; BAA06551.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB40178.1; -; Genomic_DNA.
DR PIR; T40993; T40993.
DR RefSeq; NP_588310.1; NM_001023300.2.
DR AlphaFoldDB; P38938; -.
DR SMR; P38938; -.
DR BioGRID; 275778; 36.
DR IntAct; P38938; 1.
DR STRING; 4896.SPCC1450.11c.1; -.
DR iPTMnet; P38938; -.
DR MaxQB; P38938; -.
DR PaxDb; P38938; -.
DR PRIDE; P38938; -.
DR EnsemblFungi; SPCC1450.11c.1; SPCC1450.11c.1:pep; SPCC1450.11c.
DR GeneID; 2539208; -.
DR KEGG; spo:SPCC1450.11c; -.
DR PomBase; SPCC1450.11c; cek1.
DR VEuPathDB; FungiDB:SPCC1450.11c; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000709_3_0_1; -.
DR InParanoid; P38938; -.
DR OMA; EFCQICE; -.
DR PhylomeDB; P38938; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P38938; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IGI:PomBase.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1338
FT /note="Serine/threonine-protein kinase cek1"
FT /id="PRO_0000085847"
FT DOMAIN 28..98
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 589..958
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 959..1057
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 484..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 713
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 595..603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 1297..1338
FT /note="FVYICEDETCIPTDLQSDGVLLKPITCENIESCLRKLDVWHS -> VCIHLR
FT GRDLHSD (in Ref. 1; BAA06551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1338 AA; 149897 MW; 755DD0A13D3D2762 CRC64;
MKHIKNEREE VFLEDDQAQH SQAELLSSKD ENLQPSIPLS PVAFELDFSG NFQFISDNSS
ELLDIPKDKI IGHSVAEVLG TDGYNAFMRA VNCLLKDDSH SYHVRFQHSI NANHANQNYY
TAKGDLPSDE KITKPFDAIG ILIRHPGSAI PAHTMWVVNP ATNSLGSVSP LVTKLLDVIG
FGASLLDKYL CDLRTSYHKH NSLDALPLPT PEFCQICERE IQSWFFELHS KFCLSTSTYE
SVVQAAQDSL LYFRSTLLEI QEGMQKDSSL VPVYKNEPLI VDADDYFFTD ENKQTLSLCS
FLSQVMYYLE VAIDITIPPV KIIVNFDKVD SLRVQSPRSE KATIELDNYN PSLENCSSAV
IALWEDIKTA VDTKITGVLR LRNAIYYSER IRLEIDHHVQ EIIDDVVSNL VTNHSSTSLG
HLESKLAPSI TFPDACDALE AEECITRPGS ATNTPQSDRS LDINDLSRSS SYSRHLSHVS
LSNPDFAIGS PMSQDSSNYS SPLHRRKASD SNFSDPRFDD LKYLSPNSSP RFVASDGPNR
PASNGRSSLF SRGRASNLGD VGLRLPSPSP RIHTIVPNSA PEHPSINDYK ILKPISKGAF
GSVYLAQKRT TGDYFAIKIL KKSNMIAKNQ VINVRAERAI LMSQGESPFV AKLYYTFQSK
DYLYLVMEYL NGGDCGSLLK TMGVLDLDWI RTYIAETVLC LGDLHDRGII HRDIKPENLL
ISQNGHLKLT DFGLSRVGYM KRHRRKQSSS IPVLDLRDRS SAISDLSLST ASSVLEAQSL
ITPERPKRPS LNEKLLSLDG TSIRLAGQSF NYENSAEDSP TATNTPTSQV DESNIFRSTD
SPRVQPFFEN KDPSKRFIGT PDYIAPEVIL GNPGIKASDW WSLGCVVFEF LFGYPPFNAE
TPDQVFQNIL ARRINWPAEV FTAESSVALD LIDRLLCMNP ANRLGANGVE EIKAHPFFKS
VNWDTILEED PPFVPKPFSP EDTVYFDSRG LKGFDFSEYY NQPTVTEAQK LEEERPASSI
PQHVSGNRKG RLRSNTISTP EFGSFTYRNL DFLNKANRNT IQKLRKEHMA VKSAKTSVDD
TFSQYMSRFK AKLSTSQSVG PVKSSRRASM ADYEASTTTR VQDITTDSID SIDDFDSLKE
GRMLSFFDNL ALEDHKGVSS TMSASQSQSS MHTALPDVTE GTSSDEHTTI QKGRIDNLQA
QSLTHKRNAI SYPGLFQLDR LQMIIPKDEI ELAEILKKIF PKLTLVLIDD PWSILKKLLQ
NEQFNVVFLH FGNDKVSSSR LMYSVRTSAT INSRVPFVYI CEDETCIPTD LQSDGVLLKP
ITCENIESCL RKLDVWHS
