KCC1_SCHPO
ID KCC1_SCHPO Reviewed; 335 AA.
AC Q9P7I2; O74235;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type I;
DE Short=CaMK-I;
DE EC=2.7.11.17;
GN Name=cmk1; ORFNames=SPAC25D11.02c, SPACUNK12.02c;
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 [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-192, AND MUTAGENESIS OF THR-192.
RX PubMed=10617667; DOI=10.1074/jbc.275.1.685;
RA Rasmussen C.D.;
RT "Cloning of a calmodulin kinase I homologue from Schizosaccharomyces
RT pombe.";
RL J. Biol. Chem. 275:685-690(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 -!- FUNCTION: Important in cell cycle regulation.
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=2.7.11.17;
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=2.7.11.17;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10617667}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AF073893; AAC26005.1; -; mRNA.
DR EMBL; CU329670; CAB76233.1; -; Genomic_DNA.
DR PIR; T50290; T50290.
DR RefSeq; NP_593464.1; NM_001018897.2.
DR AlphaFoldDB; Q9P7I2; -.
DR SMR; Q9P7I2; -.
DR BioGRID; 278904; 27.
DR IntAct; Q9P7I2; 2.
DR STRING; 4896.SPACUNK12.02c.1; -.
DR iPTMnet; Q9P7I2; -.
DR SwissPalm; Q9P7I2; -.
DR MaxQB; Q9P7I2; -.
DR PaxDb; Q9P7I2; -.
DR PRIDE; Q9P7I2; -.
DR EnsemblFungi; SPACUNK12.02c.1; SPACUNK12.02c.1:pep; SPACUNK12.02c.
DR GeneID; 2542442; -.
DR KEGG; spo:SPACUNK12.02c; -.
DR PomBase; SPACUNK12.02c; cmk1.
DR VEuPathDB; FungiDB:SPACUNK12.02c; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9P7I2; -.
DR OMA; RPKVQPC; -.
DR PhylomeDB; Q9P7I2; -.
DR BRENDA; 2.7.11.17; 5613.
DR Reactome; R-SPO-9619229; Activation of RAC1 downstream of NMDARs.
DR PRO; PR:Q9P7I2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:PomBase.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IMP:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0106057; P:negative regulation of calcineurin-mediated signaling; IGI:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IGI:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Calmodulin-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..335
FT /note="Calcium/calmodulin-dependent protein kinase type I"
FT /id="PRO_0000086089"
FT DOMAIN 31..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 310..334
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 192
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10617667"
FT MUTAGEN 192
FT /note="T->D: 15-fold increase in activity."
FT /evidence="ECO:0000269|PubMed:10617667"
FT CONFLICT 115
FT /note="E -> A (in Ref. 1; AAC26005)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..295
FT /note="KR -> NG (in Ref. 1; AAC26005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38164 MW; 8761BBCFF6882B02 CRC64;
MQQTYKPNTS ALKDGAPKAT VDQKQLLPCK YRVGRVLGGG TYATVREAVH IETNKMYAAK
IMNKKMMEKK QDFVKNEIAI LKRVSYEHPN ILHLVDFFET VNNLYLITEL ATGGELFDRI
CAKGSFYEAD AAALMRTTTS AVKYLHDNGI VHRDLKPENL LYRSKDPNSD LLIADFGLSH
FYEDSQYYML MTACGTPEYM APEVFRRTGY GKPVDMWAIG VITYFLLSGY TPFARPSQVE
VIEAILANEY TFNDPCWSGI SETAKDFIKK CLENDPSKRL TAADALKHPF LSEKRPATSN
LLPNVRENFN ARKTFRTAYN AVRAFNTWKK LENKH
