ID   CDK2_ENTH1              Reviewed;         291 AA.
AC   Q04770; A0A175JUR6; C4M6K6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2023, sequence version 2.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Cyclin-dependent kinase 2 {ECO:0000303|PubMed:8500762};
DE   AltName: Full=Cell division protein kinase 2 homolog {ECO:0000305};
DE            EC=2.7.11.22 {ECO:0000250|UniProtKB:P24941};
GN   Name=CDC2 {ECO:0000303|PubMed:8500762};
GN   ORFNames=EHI_065280 {ECO:0000312|EMBL:EAL47010.1};
OS   Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=294381 {ECO:0000312|EMBL:EAL47010.1};
RN   [1] {ECO:0000312|EMBL:AAA51480.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8500762; DOI=10.1016/0378-1119(93)90720-n;
RA   Lohia A., Samuelson J.;
RT   "Cloning of the Eh cdc2 gene from Entamoeba histolytica encoding a protein
RT   kinase p34cdc2 homologue.";
RL   Gene 127:203-207(1993).
RN   [2] {ECO:0000312|EMBL:EAL47010.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:EAL47010.1};
RX   PubMed=15729342; DOI=10.1038/nature03291;
RA   Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA   Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA   Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA   Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA   Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA   Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA   Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA   Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA   Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA   Barrell B.G., Fraser C.M., Hall N.;
RT   "The genome of the protist parasite Entamoeba histolytica.";
RL   Nature 433:865-868(2005).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC       the cell cycle. {ECO:0000250|UniProtKB:P24941}.
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:P24941};
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:P24941};
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: Forms a stable but non-covalent complex with a regulatory
CC       subunit and with a cyclin. {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; L03810; AAA51480.1; -; Genomic_DNA.
DR   EMBL; DS571302; EAL47010.1; -; Genomic_DNA.
DR   PIR; JN0631; JN0631.
DR   RefSeq; XP_652398.1; XM_647306.1.
DR   AlphaFoldDB; Q04770; -.
DR   SMR; Q04770; -.
DR   STRING; 5759.C4M6K6; -.
DR   EnsemblProtists; GAT97124; GAT97124; CL6EHI_065280.
DR   EnsemblProtists; rna_EHI_065280-1; rna_EHI_065280-1; EHI_065280.
DR   GeneID; 3406705; -.
DR   KEGG; ehi:EHI_065280; -.
DR   VEuPathDB; AmoebaDB:EHI5A_179010; -.
DR   VEuPathDB; AmoebaDB:EHI7A_147660; -.
DR   VEuPathDB; AmoebaDB:EHI8A_167750; -.
DR   VEuPathDB; AmoebaDB:EHI_065280; -.
DR   VEuPathDB; AmoebaDB:KM1_177710; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   OMA; HKEKCIY; -.
DR   OrthoDB; 244018at2759; -.
DR   BRENDA; 2.7.11.22; 2080.
DR   Proteomes; UP000001926; Partially assembled WGS sequence.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
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:SF254; CYCLIN-DEPENDENT KINASE 2; 1.
DR   Pfam; PF12330; Haspin_kinase; 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; Kinase; Mitosis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..291
FT                   /note="Cyclin-dependent kinase 2"
FT                   /id="PRO_0000085775"
FT   DOMAIN          4..283
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   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|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"
FT   CONFLICT        143
FT                   /note="D -> E (in Ref. 1; AAA51480)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   291 AA;  33831 MW;  615A0692572A336C CRC64;
     MTRYEKKQQL GEGTYGVVCK AWDTVCNRYV ALKKIKQERE DDGIPVTSVR EIAVLLELKH
     PNVVDLYDIY LEDKFLYLVF EFCDEDLYQF MSRSSKIPIN ETRSIVYQIL QGLAFCHYHQ
     ILHRDMKPQN ILINKNGTIK LGDFGLARLT TINDRKYTSE VVTLWYRAPE ILLGATQYGG
     AIDIWSTAAI FGELINKEEL FKGRCKIDQL FKIFSQLGTP TEDIWNGVTK LPFYLSTFPK
     WKAKDLHTIF HTDERAVDLL QKMFIYTPEK RISAADALKH PFFDPLNKPN N
//