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   27-MAR-2024, entry version 111.
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:PVW1_110020500; -.
DR   VEuPathDB; PlasmoDB:PVX_114825; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   OMA; YLYQITR; -.
DR   OrthoDB; 244018at2759; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07829; STKc_CDK_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF46; CYCLIN-DEPENDENT KINASE 5; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//