CDR1_SCHPO
ID CDR1_SCHPO Reviewed; 593 AA.
AC P07334; Q9P6Q4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Mitosis inducer protein kinase cdr1;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase nim1;
GN Name=cdr1; Synonyms=nim1; ORFNames=SPAC644.06c;
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=2004705; DOI=10.1093/genetics/127.2.309;
RA Feilotter H., Nurse P., Young P.G.;
RT "Genetic and molecular analysis of cdr1/nim1 in Schizosaccharomyces
RT pombe.";
RL Genetics 127:309-318(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3453113; DOI=10.1016/0092-8674(87)90459-4;
RA Russell P., Nurse P.;
RT "The mitotic inducer nim1+ functions in a regulatory network of protein
RT kinase homologs controlling the initiation of mitosis.";
RL Cell 49:569-576(1987).
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-550, AND IDENTIFICATION BY
RP 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: This protein, a dose-dependent mitotic inducer, appears to
CC function as a negative regulator of mitosis inhibitor wee1 by
CC phosphorylating and inactivating it.
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. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35317.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X57549; CAA40774.1; -; Genomic_DNA.
DR EMBL; M16509; AAA35317.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CU329670; CAB90133.1; -; Genomic_DNA.
DR PIR; S16153; KIZPMN.
DR RefSeq; NP_593874.1; NM_001019304.2.
DR AlphaFoldDB; P07334; -.
DR SMR; P07334; -.
DR BioGRID; 280080; 46.
DR STRING; 4896.SPAC644.06c.1; -.
DR iPTMnet; P07334; -.
DR MaxQB; P07334; -.
DR PaxDb; P07334; -.
DR PRIDE; P07334; -.
DR EnsemblFungi; SPAC644.06c.1; SPAC644.06c.1:pep; SPAC644.06c.
DR GeneID; 2543666; -.
DR KEGG; spo:SPAC644.06c; -.
DR PomBase; SPAC644.06c; cdr1.
DR VEuPathDB; FungiDB:SPAC644.06c; -.
DR eggNOG; KOG0588; Eukaryota.
DR HOGENOM; CLU_465517_0_0_1; -.
DR InParanoid; P07334; -.
DR PhylomeDB; P07334; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P07334; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0110115; C:Cdr2 medial cortical node complex; EXP:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS: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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..593
FT /note="Mitosis inducer protein kinase cdr1"
FT /id="PRO_0000085844"
FT DOMAIN 12..258
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 252
FT /note="V -> F (in Ref. 1; CAA40774/AAA35317)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="A -> I (in Ref. 1; CAA40774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 66955 MW; DE30AE06B070F458 CRC64;
MVKRHKNTIG VWRLGKTLGT GSTSCVRLAK HAKTGDLAAI KIIPIRYASI GMEILMMRLL
RHPNILRLYD VWTDHQHMYL ALEYVPDGEL FHYIRKHGPL SEREAAHYLS QILDAVAHCH
RFRFRHRDLK LENILIKVNE QQIKIADFGM ATVEPNDSCL ENYCGSLHYL APEIVSHKPY
RGAPADVWSC GVILYSLLSN KLPFGGQNTD VIYNKIRHGA YDLPSSISSA AQDLLHRMLD
VNPSTRITIP EVFSHPFLMG CTSLSSMDST TPPTPSLSID EIDPLVVDCM CVLWKKSSSK
KVVRRLQQRD DNDEKYVYKV LSEILRDDML KKQRFDENKY LSLYDLIHDN NLFTKASIST
TSLVKSNVST NSRKSSNFED ELARRVSSPL SALNQMSQSP IPIRVSSDKD YDSYACHEVV
SNPSTLDDDY NYMFVCPPEE YTYSTDNVRT DSLDLQSLPT PTLEQLESVP FNRYGYVRIF
PSTTLSSTAS GYYTPDSLST PEPSIDGLTN LDDVQVGGFV QGSGNQNRRP ISFPVISNMQ
PNITNVRSAS APLCSSPVPS RRYSQYATNA RYTPRKVSSG SVLRKISSFF RKD
