ID   CC2H1_TRYCO             Reviewed;         301 AA.
AC   P54664;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cell division control protein 2 homolog 1;
DE            EC=2.7.11.22;
GN   Name=CRK1; Synonyms=CRK;
OS   Trypanosoma congolense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=5692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IL3000;
RA   Ricard B., Mottram J.C., Muthiani A., Omolo E., Pandit P., Gobright E.,
RA   Murphy N.B.;
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
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 Ser-15 or Tyr-16 inactivates
CC       the enzyme, while phosphorylation at Thr-160 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; Z30312; CAA82956.1; -; Genomic_DNA.
DR   PIR; S42101; S42101.
DR   AlphaFoldDB; P54664; -.
DR   SMR; P54664; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000721800; -.
DR   VEuPathDB; TriTrypDB:TcIL3000_10_880; -.
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: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; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..301
FT                   /note="Cell division control protein 2 homolog 1"
FT                   /id="PRO_0000085707"
FT   DOMAIN          5..297
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         11..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         16
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         160
FT                   /note="Phosphothreonine; by CAK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  34468 MW;  4D31FFA7B952F256 CRC64;
     MGSRYQRLEK IGEGSYGVVY RARDITTDVI VALKRIRLES VEEGVPCTAI REISILKELR
     HENIVRLLDV CHSENRLNLV FEYMEMDLKK YMDRASGNLD PATIQEFMRS LLKGVRFCHE
     RNVLHRDLKP PNLLISREKE LKLADFGLGR AFGIPVKKYT HEVVTLWYRS PDVLLGSTQY
     GTPVDIWSVG CIFAEMAIGA PLFAGKNDAD QLLRIFRFLG TPSSQVWPSM NLYPNSTNML
     SKPEFQQNLI ATCDEQFQTH PAYAKLGPQG IDLLRRLLRY EPGERLTAAQ ALEHPYFSVE
     F