CDK2H_PLAVI
ID CDK2H_PLAVI Reviewed; 288 AA.
AC Q9XZD6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cyclin-dependent kinase 2 homolog {ECO:0000305};
DE EC=2.7.11.22 {ECO:0000250|UniProtKB:P61075};
DE EC=2.7.11.23 {ECO:0000250|UniProtKB:P61075};
DE AltName: Full=Cell division control protein 2 homolog {ECO:0000250|UniProtKB:P61075};
DE AltName: Full=Pvcrk2 {ECO:0000303|PubMed:11312574};
DE AltName: Full=cdc2-related kinase 2 {ECO:0000303|PubMed:11312574};
GN Name=CRK2 {ECO:0000303|PubMed:11312574};
OS Plasmodium vivax.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5855;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11312574; DOI=10.1006/expr.2001.4596;
RA Speranca M.A., Vinkenoog R., Ocampos M., Fischer K., Janse C.J.,
RA Waters A.P., del Portillo H.A.;
RT "Primary structure of the Plasmodium vivax crk2 gene and interference of
RT the yeast cell cycle upon its conditional expression.";
RL Exp. Parasitol. 97:119-128(2001).
CC -!- FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in
CC the control of the cell cycle. Required for entry into S-phase and
CC mitosis (By similarity). Probable component of the kinase complex that
CC phosphorylates the repetitive C-terminus of RNA polymerase II (By
CC similarity). {ECO:0000250|UniProtKB:P04551,
CC ECO:0000250|UniProtKB:P61075}.
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 Evidence={ECO:0000250|UniProtKB:P61075};
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; Evidence={ECO:0000250|UniProtKB:P61075};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC Evidence={ECO:0000250|UniProtKB:P61075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P61075};
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-158 activates it.
CC {ECO:0000250|UniProtKB:P24941}.
CC -!- SUBUNIT: May form a complex composed of at least the catalytic subunit
CC CRK2 and a cyclin. {ECO:0000250|UniProtKB:P61075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04551}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AF136377; AAD29423.1; -; Genomic_DNA.
DR RefSeq; XP_001616353.1; XM_001616303.1.
DR AlphaFoldDB; Q9XZD6; -.
DR SMR; Q9XZD6; -.
DR GeneID; 5475652; -.
DR KEGG; pvx:PVX_114825; -.
DR VEuPathDB; PlasmoDB:PVP01_1115000; -.
DR VEuPathDB; PlasmoDB:PVX_114825; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR OMA; NNDVWPE; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..288
FT /note="Cyclin-dependent kinase 2 homolog"
FT /id="PRO_0000232671"
FT DOMAIN 4..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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 32
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|UniProtKB:P24941"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
SQ SEQUENCE 288 AA; 33094 MW; 16A484C4B6CD313C CRC64;
MEKYHGLEKI GEGTYGVVYK AQNNYGETFA LKKIRLEKED EGIPSTAIRE ISILKELKHS
NIVKLYDVIH TKKRLILVFE HLDQDLKKLL DVCDGGLESV TAKSFLLQLL SGIAYCHEHR
VLHRDLKPQN LLINREGELK IADFGLARAF GIPVRKYTHE VVTLWYRAPD ILMGSKKYST
PIDMWSVGCI FAEMVNGRPL FPGVSETDQL MRIFRILGTP NSENWPNVTE LPKYDPDFMV
YEPLPWETFL KGLDDTGIDL LSKMLRLDPN QRITAKQALE HAYFKESN
