ID   CDK2H_PLACU             Reviewed;         288 AA.
AC   Q4Y4B1; A0A4V0K9I8;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=cdc2-related kinase 2 {ECO:0000250|UniProtKB:Q4Z6R1};
GN   Name=CRK2 {ECO:0000250|UniProtKB:Q4Z6R1};
GN   ORFNames=PC000220.01.0, PCHAS_1132700 {ECO:0000312|EMBL:VTZ69322.1};
OS   Plasmodium chabaudi chabaudi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=31271 {ECO:0000312|Proteomes:UP000071118};
RN   [1] {ECO:0000312|Proteomes:UP000071118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS {ECO:0000312|Proteomes:UP000071118};
RX   PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA   Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA   Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA   Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA   Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA   Janse C.J.;
RT   "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT   expression.";
RL   BMC Biol. 12:86-86(2014).
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; LK022888; VTZ69322.1; -; Genomic_DNA.
DR   RefSeq; XP_016654040.1; XM_016798662.1.
DR   AlphaFoldDB; Q4Y4B1; -.
DR   SMR; Q4Y4B1; -.
DR   GeneID; 3496351; -.
DR   KEGG; pcb:PCHAS_1132700; -.
DR   VEuPathDB; PlasmoDB:PCHAS_1132700; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   OrthoDB; 244018at2759; -.
DR   Proteomes; UP000071118; Chromosome 11.
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_0000232669"
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;  32965 MW;  83472DB68D3A2704 CRC64;
     MEKYHGLEKI GEGTYGVVYK AQNSDGESFA LKKIRLEKED EGIPSTAIRE ISILKELRHS
     NIVKLYDVIH AKKRLILVFE HLDQDLKKLI DVCDGGLESV TAKSFLLQLL NGIAYCHEHR
     VLHRDLKPQN LLINREGELK IADFGLARAF GIPARRYTHE VVTLWYRAPD ILMGSKKYST
     PIDIWSVGCI FAEMVNGRPL FPGVSDTDQL MRIFKILGTP NSQNWPDVFK LPKYDPNFPV
     YEPLPWETFI KGLDDTGIDL LSKMLKLDPN QRITAKQAIE HPYFKETS
//