CDK2H_THEAN
ID CDK2H_THEAN Reviewed; 298 AA.
AC Q26671;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
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:0000303|PubMed:8930914};
GN Name=CRK2 {ECO:0000303|PubMed:8930914}; ORFNames=TA06730;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Ankara;
RX PubMed=8930914; DOI=10.1046/j.1365-2958.1996.00124.x;
RA Kinnaird J.H., Logan M., Kirvar E., Tait A., Carrington M.;
RT "The isolation and characterisation of genomic and cDNA clones coding for a
RT cdc2-related kinase (ThCRK2) from the bovine protozoan parasite
RT Theileria.";
RL Mol. Microbiol. 22:293-302(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara;
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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; X98768; CAA67306.1; -; mRNA.
DR EMBL; CR940347; CAI73372.1; -; Genomic_DNA.
DR RefSeq; XP_954049.1; XM_948956.1.
DR AlphaFoldDB; Q26671; -.
DR SMR; Q26671; -.
DR STRING; 5874.XP_954049.1; -.
DR PRIDE; Q26671; -.
DR GeneID; 3863999; -.
DR KEGG; tan:TA06730; -.
DR VEuPathDB; PiroplasmaDB:TA06730; -.
DR eggNOG; KOG0594; Eukaryota.
DR InParanoid; Q26671; -.
DR OMA; NNDVWPE; -.
DR OrthoDB; 1010560at2759; -.
DR Proteomes; UP000001950; Chromosome 1 part 1.
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; 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 2: Evidence at transcript level;
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..298
FT /note="Cyclin-dependent kinase 2 homolog"
FT /id="PRO_0000232673"
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 298 AA; 34231 MW; A4F8526448B4F727 CRC64;
MRRYHKMEKI GEGTYGVVYK AQNNHGEICA LKKIRVEEED EGIPSTAIRE ISLLKELHHP
NIVWLRDVIH SEKCLTLVFE YLDQDLKKLL DACDGGLEPT TAKSFLYQIL RGISYCHDHR
ILHRDLKPQN LLINREGVLK LADFGLARAF AIPVRSYTHE VVTLWYRAPD VLMGSKKYST
AVDIWSVGCI FAEMINGVPL FPGISEQDQL KRIFKILGTP NVDSWPQVVN LPAYNPDFCY
YEKQAWSSIV PKLNESGIDL ISRMLQLDPV QRISAKEALK HDYFKDLHRP SEFLNGVH
