CC2H3_TRYBB
ID CC2H3_TRYBB Reviewed; 311 AA.
AC P54666;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cell division control protein 2 homolog 3;
DE EC=2.7.11.22;
GN Name=CRK3;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ISTAT;
RX PubMed=7557404; DOI=10.1016/0378-1119(95)00350-f;
RA Mottram J., Smith G.;
RT "A family of trypanosome cdc2-related protein kinases.";
RL Gene 162:147-152(1995).
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-33 or Tyr-34 inactivates
CC the enzyme.
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; X74617; CAA52688.1; -; Genomic_DNA.
DR PIR; S36619; S36619.
DR AlphaFoldDB; P54666; -.
DR SMR; P54666; -.
DR BRENDA; 2.7.11.22; 6520.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005524; F:ATP binding; ISM:GeneDB.
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:0004674; F:protein serine/threonine kinase activity; ISM:GeneDB.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:GeneDB.
DR GO; GO:0006468; P:protein phosphorylation; ISM:GeneDB.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..311
FT /note="Cell division control protein 2 homolog 3"
FT /id="PRO_0000085709"
FT DOMAIN 23..306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 35047 MW; 168D97820100E016 CRC64;
MTMLGALTGR QLSSGLKDQF DRYNRMDILG EGTYGVVYRA VDRATGQIVA LKKVRLDRTD
EGIPQTALRE VSILQEIHHP NIVNLLDVIC ADGKLYLIFE YVDHDLKKAL EKRGGAFTGT
TLKKIIYQLL EGLSFCHRHR IVHRDLKPAN ILVTTDNSVK IADFGLARAF QIPMHTYTHE
VVTLWYRAPE ILLGEKHYTP AVDMWSIGCI FAELARGKVL FRGDSEIGQL FEIFQVLGTP
MDAEGSWLGV SSLPDYRDVF PKWSGKPLTQ VLPTLDGDAV DLLSQMLRYN PAERISAKAA
LQHPWFSDAM F