ID Y4007_DICDI Reviewed; 680 AA.
AC Q556J6; Q86AM9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Putative cyclin-dependent serine/threonine-protein kinase DDB_G0272797/DDB_G0274007;
DE EC=2.7.11.22;
GN ORFNames=DDB_G0272797;
GN and
GN ORFNames=DDB_G0274007;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
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).
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=2.7.11.22;
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=2.7.11.22;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX 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; AAFI02000011; EAL70437.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL71036.1; -; Genomic_DNA.
DR RefSeq; XP_644362.1; XM_639270.1.
DR RefSeq; XP_645052.1; XM_639960.1.
DR AlphaFoldDB; Q556J6; -.
DR SMR; Q556J6; -.
DR STRING; 44689.Q556J6; -.
DR PaxDb; 44689-DDB0230050; -.
DR EnsemblProtists; EAL70437; EAL70437; DDB_G0274007.
DR EnsemblProtists; EAL71036; EAL71036; DDB_G0272797.
DR GeneID; 8618728; -.
DR GeneID; 8619248; -.
DR KEGG; ddi:DDB_G0272797; -.
DR KEGG; ddi:DDB_G0274007; -.
DR dictyBase; DDB_G0272797; -.
DR dictyBase; DDB_G0274007; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_404632_0_0_1; -.
DR InParanoid; Q556J6; -.
DR OMA; GIHKITH; -.
DR PhylomeDB; Q556J6; -.
DR PRO; PR:Q556J6; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF246; CYCLIN-DEPENDENT KINASE 17; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..680
FT /note="Putative cyclin-dependent serine/threonine-protein
FT kinase DDB_G0272797/DDB_G0274007"
FT /id="PRO_0000372696"
FT DOMAIN 4..381
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 243..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..633
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 680 AA; 79758 MW; 6DB9FE3034BAC068 CRC64;
MEDYIILSKC GQGTYGSVFK GIHKITHSLV ALKRVTDIAQ EDGEPVEVKY LNQLKNLSNI
VNLRDHFYID KNSVLVLIME FIEGDLWKIM SNPQCTLSLG QIKNFTKQLL EGVKQCHVNG
IMHRDIKPAN LLITTNGVLK LTDFGLSTSY SKRSEKFLSS NVVSLYYRPP ELLLGSCIYG
PEIDMWSVGC ILMEMINNSY LFAGADETAQ LDLIFKLFGC PTEKSWPGVS SLPGYNDLFN
KQQQQQQNEN NYSKQHNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNKYNN ISTSCLQSPS
SSPPIGGYAS SLSSDFNSNE YNGYNQTFSN EDCLAISQKK LIDKFPHLVL LPSVLDLASK
MLTLDPKKRI NSLEALEHPW FKSSNDMDQI VPFSKDFTDL ANRYIASTRQ LQQQQHHHQQ
QQQQQQQQQQ QQQPHQQQLI QRQHQEQQQQ QLIQRQQEQS KQQLIQHHQQ SVNQQQLAQQ
QQLAQHQQYN SQQHQQHHQQ QHQQHQQHQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQY
HQHQQQYHQY QQQYHQPSQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
HQYQPPQQYN HQPPQHQHQH QHQHQHQHQH QHQPQPQHQH QPQPQPQPTP TPTPTSTPTT
TTIPPTITTT IQPTISKSNG
//
