ID   CDK2H_PLAYO             Reviewed;         289 AA.
AC   Q7RM49;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
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}; ORFNames=PY02339;
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=73239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL;
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA   Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA   Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
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-159 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}.
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; AABL01000639; EAA21777.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7RM49; -.
DR   SMR; Q7RM49; -.
DR   STRING; 73239.Q7RM49; -.
DR   PaxDb; 73239-Q7RM49; -.
DR   EnsemblProtists; EAA21777; EAA21777; EAA21777.
DR   InParanoid; Q7RM49; -.
DR   OMA; YLYQITR; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
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   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..289
FT                   /note="Cyclin-dependent kinase 2 homolog"
FT                   /id="PRO_0000232672"
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         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         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24941"
SQ   SEQUENCE   289 AA;  33121 MW;  701FCFCEEA4F5CA3 CRC64;
     MEKYHGLEKI GEGTYGVVYK AQNSDGESFA LKKIRLEKED EGIPSTVSIR EISILKELRH
     SNIVKLYDVI HAKKRLILVF EHLDQDLKKL IDVCDGGLES VTAKSFLLQL LNGIAYCHEH
     RVLHRDLKPQ NLLINREGEL KIADFGLARA FGIPARRYTH EVVTLWYRAP DILMGSKKYS
     TPIDIWSVGC IFAEMVNGRP LFPGVSETDQ LMRIFKILGT PNSQNWPDVF KLPKYDPNFP
     VYEPLPWETF IKGLDDTGID LLSKMLKLDP NQRITAKQAI EHPYFKETN
//