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 01-MAY-2013, entry version 107.
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;
OC Schizosaccharomycetaceae; Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8065367;
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.
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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., 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
RP SER-1211, AND 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
CC direct or indirect interaction with the cut8 protein.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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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 ProteinModelPortal; P38938; -.
DR IntAct; P38938; 1.
DR STRING; 4896.SPCC1450.11c-1; -.
DR EnsemblFungi; SPCC1450.11c.1; SPCC1450.11c.1:pep; SPCC1450.11c.
DR GeneID; 2539208; -.
DR KEGG; spo:SPCC1450.11c; -.
DR PomBase; SPCC1450.11c; -.
DR eggNOG; COG0515; -.
DR KO; K08286; -.
DR OMA; INANHAN; -.
DR OrthoDB; EOG4BGD43; -.
DR BRENDA; 2.7.11.1; 5615.
DR NextBio; 20800378; -.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR GO; GO:0051519; P:activation of bipolar cell growth; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IC:PomBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IGI:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 1338 Serine/threonine-protein kinase cek1.
FT /FTId=PRO_0000085847.
FT DOMAIN 28 98 PAS.
FT DOMAIN 589 958 Protein kinase.
FT DOMAIN 959 1057 AGC-kinase C-terminal.
FT NP_BIND 595 603 ATP (By similarity).
FT ACT_SITE 713 713 Proton acceptor (By similarity).
FT BINDING 618 618 ATP (By similarity).
FT MOD_RES 525 525 Phosphoserine.
FT MOD_RES 748 748 Phosphoserine.
FT MOD_RES 1211 1211 Phosphoserine.
FT CONFLICT 1297 1338 FVYICEDETCIPTDLQSDGVLLKPITCENIESCLRKLDVWH
FT S -> VCIHLRGRDLHSD (in Ref. 1; BAA06551).
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
//
