CDK5_DICDI
ID CDK5_DICDI Reviewed; 292 AA.
AC P34117; Q54II5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cyclin-dependent kinase 5 homolog;
DE EC=2.7.11.22;
DE AltName: Full=CDC2-like serine/threonine-protein kinase CRP;
DE AltName: Full=Cell division protein kinase 5;
GN Name=cdk5; Synonyms=crp, crpA; ORFNames=DDB_G0288677;
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].
RX PubMed=8218353; DOI=10.1016/0167-4889(93)90132-9;
RA Michaelis C.E., Weeks G.;
RT "The isolation from a unicellular organism, Dictyostelium discoideum, of a
RT highly-related cdc2 gene with characteristics of the PCTAIRE subfamily.";
RL Biochim. Biophys. Acta 1179:117-124(1993).
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 -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L00652; AAA16056.1; -; mRNA.
DR EMBL; AAFI02000120; EAL63070.1; -; Genomic_DNA.
DR PIR; S40021; S40021.
DR RefSeq; XP_636601.1; XM_631509.1.
DR AlphaFoldDB; P34117; -.
DR SMR; P34117; -.
DR STRING; 44689.DDB0191155; -.
DR PaxDb; P34117; -.
DR EnsemblProtists; EAL63070; EAL63070; DDB_G0288677.
DR GeneID; 8626776; -.
DR KEGG; ddi:DDB_G0288677; -.
DR dictyBase; DDB_G0288677; cdk5.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P34117; -.
DR OMA; NNDVWPE; -.
DR PhylomeDB; P34117; -.
DR BRENDA; 2.7.11.22; 1939.
DR PRO; PR:P34117; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:dictyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IPI:dictyBase.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:dictyBase.
DR GO; GO:0031157; P:regulation of aggregate size involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..292
FT /note="Cyclin-dependent kinase 5 homolog"
FT /id="PRO_0000085740"
FT DOMAIN 4..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 126
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"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="Y -> N (in Ref. 1; AAA16056)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="G -> L (in Ref. 1; AAA16056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 33219 MW; D6829B15C0458526 CRC64;
MEKYSKIEKL GEGTYGIVYK AKNRETGEIV ALKRIRLDSE DEGVPCTAIR EISLLKELKH
PNIVRLHDVI HTERKLTLVF EYLDQDLKKY LDECGGEISK PTIKSFMYQL LKGVAFCHDH
RVLHRDLKPQ NLLINRKGEL KLADFGLARA FGIPVRTYSH EVVTLWYRAP DVLMGSRKYS
TPIDIWSAGC IFAEMASGRP LFPGSGTSDQ LFRIFKILGT PNEESWPSIT ELPEYKTDFP
VHPAHQLSSI VHGLDEKGLN LLSKMLQYDP NQRITAAAAL KHPYFDGLEP IN
