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   27-MAR-2024, entry version 104.
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   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:SF571; KINASE, PUTATIVE-RELATED; 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; 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
//