KC1_DICDI
ID KC1_DICDI Reviewed; 426 AA.
AC Q556Y4; O96300; Q86AI9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Casein kinase I;
DE Short=CK1;
DE Short=DdCK1;
DE EC=2.7.11.1;
GN Name=cak1-1; ORFNames=DDB_G0273059;
GN and
GN Name=cak1-2; ORFNames=DDB_G0273737;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AUTOPHOSPHORYLATION, FUNCTION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LYS-38.
RC STRAIN=AX2;
RX PubMed=10880352; DOI=10.1042/0264-6021:3490527;
RA Moreno-Bueno G., Cales C., Behrens M.M., Fernandez-Renart M.;
RT "Isolation and characterization of casein kinase I from Dictyostelium
RT discoideum.";
RL Biochem. J. 349:527-537(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15548420; DOI=10.1016/s0074-7696(04)41003-1;
RA Graef R., Daunderer C., Schulz I.;
RT "Molecular and functional analysis of the dictyostelium centrosome.";
RL Int. Rev. Cytol. 241:155-202(2004).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Can phosphorylate a large number of proteins. May have a
CC role in DNA repair mechanism and support vegetative growth of the
CC cells. {ECO:0000269|PubMed:10880352}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DEVELOPMENTAL STAGE: Present in vegetative cells.
CC {ECO:0000269|PubMed:10880352}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AF003547; AAD01192.1; -; mRNA.
DR EMBL; AAFI02000009; EAL70747.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70559.1; -; Genomic_DNA.
DR RefSeq; XP_644485.1; XM_639393.1.
DR RefSeq; XP_644765.1; XM_639673.1.
DR AlphaFoldDB; Q556Y4; -.
DR SMR; Q556Y4; -.
DR STRING; 44689.DDB0185182; -.
DR PaxDb; Q556Y4; -.
DR EnsemblProtists; EAL70559; EAL70559; DDB_G0273737.
DR EnsemblProtists; EAL70747; EAL70747; DDB_G0273059.
DR GeneID; 8618867; -.
DR GeneID; 8619109; -.
DR KEGG; ddi:DDB_G0273059; -.
DR KEGG; ddi:DDB_G0273737; -.
DR dictyBase; DDB_G0273059; cak1-1.
DR dictyBase; DDB_G0273737; cak1-2.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; Q556Y4; -.
DR OMA; IFDWTFL; -.
DR PhylomeDB; Q556Y4; -.
DR Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q556Y4; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0006281; P:DNA repair; IMP:dictyBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR030509; CK1.
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 PANTHER; PTHR11909:SF409; PTHR11909:SF409; 1.
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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..426
FT /note="Casein kinase I"
FT /id="PRO_0000352351"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 340..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 38
FT /note="K->R: Abolishes growth."
FT /evidence="ECO:0000269|PubMed:10880352"
FT CONFLICT 201
FT /note="Y -> L (in Ref. 1; AAD01192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 49215 MW; 7B5B7008A2415236 CRC64;
MDLRIGGKYR ISRKIGGGSF GEIYLGTNIS TNEEVAIKLE PAKAIHPQLL FESKLYKIFQ
GGIGIPAVKW FGFDGDYNIM VMDLLGPSLE DLFNYCGRKF SLKTVLMLGD QMLRRIEFIH
SNNFIHRDIK PDNFLMGIGK RGHVVNLIDF GLAKRYRDPK THQHIPYREH KNLTGTARYA
SLNTHQGIEQ SRRDDLESLG YVLMYFNRGS LPWQGLKAYT KRDKYEKICD KKAQTKIDTL
CQGFPSEFAT FLNYTRFLKF EDKPDFLYLR KLLREMFVRE GYRYDYMFDW VIVRKLREKP
PLERPLSNDN KQIQQQIQQQ QQAQQQLQQQ AQQQQQQTTT TTTTSSSQPS NVKNISTVSN
IATTTTDEQF RQLLSTPSYN NVDSDQSPQQ TTTTTSSSNP NQTTFYRQNK VVVPQSSSTT
TKPPAK
