CDK2_ENTHI
ID CDK2_ENTHI Reviewed; 291 AA.
AC Q04770;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cell division protein kinase 2 homolog;
DE EC=2.7.11.22;
GN Name=CDC2;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [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).
CC -!- FUNCTION: Probably involved in the control of the cell cycle.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-158 activates it.
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
CC subunit and with a cyclin. {ECO:0000250}.
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 PIR; JN0631; JN0631.
DR AlphaFoldDB; Q04770; -.
DR SMR; Q04770; -.
DR STRING; 5759.rna_EHI_065280-1; -.
DR PRIDE; Q04770; -.
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 BRENDA; 2.7.11.22; 2080.
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: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; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..291
FT /note="Cell division protein kinase 2 homolog"
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 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 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"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 33845 MW; 205A078246E153B7 CRC64;
MTRYEKKQQL GEGTYGVVCK AWDTVCNRYV ALKKIKQERE DDGIPVTSVR EIAVLLELKH
PNVVDLYDIY LEDKFLYLVF EFCDEDLYQF MSRSSKIPIN ETRSIVYQIL QGLAFCHYHQ
ILHRDMKPQN ILINKNGTIK LGEFGLARLT TINDRKYTSE VVTLWYRAPE ILLGATQYGG
AIDIWSTAAI FGELINKEEL FKGRCKIDQL FKIFSQLGTP TEDIWNGVTK LPFYLSTFPK
WKAKDLHTIF HTDERAVDLL QKMFIYTPEK RISAADALKH PFFDPLNKPN N
