CDK2H_CRIFA
ID CDK2H_CRIFA Reviewed; 474 AA.
AC Q01917;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Synonyms=CRK {ECO:0000303|PubMed:1437562};
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1437562; DOI=10.1093/nar/20.20.5451;
RA Brown L.M., Hines J.C., Ray D.S.;
RT "The Crithidia fasciculata CRK gene encodes a novel cdc2-related protein
RT containing large inserts between highly conserved domains.";
RL Nucleic Acids Res. 20:5451-5456(1992).
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-17 or Tyr-18 inactivates
CC the enzyme, while phosphorylation at Ser-230 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; Z12149; CAA78133.1; -; Genomic_DNA.
DR PIR; S26381; S26381.
DR AlphaFoldDB; Q01917; -.
DR SMR; Q01917; -.
DR VEuPathDB; TriTrypDB:CFAC1_120018200; -.
DR BRENDA; 2.7.11.22; 1365.
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: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; 2.
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; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..474
FT /note="Cyclin-dependent kinase 2 homolog"
FT /id="PRO_0000085737"
FT DOMAIN 7..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 150..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 18
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
SQ SEQUENCE 474 AA; 53473 MW; 57CA1361E3651A9D CRC64;
MSTLGRYRHV VKLGEGTYGM VYKGTEIQTG RVVAFKRMVV TSDDEGIPGA AIREICLLKE
LRHNNVVELF EVLFDPPKIT MIFELCDCDL KRYMESRPQR LLDANTEMRP ILKQIFLGLE
YLHGRCVVHR DMKPQNIFVN VRGPDFAAMT ALPSSPQQSM RVPHAGGTNG EAGRASANGN
EHAPRPTAAE GSVSPWEEAA NTKDAPNQLI IKIGDFGLAR VEEIPVKKYS HEVVTLWYRS
PDVLMSSALY SYPVDIWSMG AIFFEMATSK VLFSGRNEDE QLLRMFWLLG SPTKETWPSM
MTYTGTMERL ERSSRAAAER QDLTVNGDVY VQQQQLQAQQ QQPQQGSSPS HSSSRAPDLL
TQLAHKRFYH SESAMQQRRE SASSAANSYR LPVELWFDRP LFKEYMAATR CDVSVSPEGI
DLLRRCLMYE PNQRITAAEA VHHPYLERVP VPTAGSLDVL ISSLMQTMET IHLL
