ID   CC2H2_TRYBB             Reviewed;         345 AA.
AC   P54665;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Cell division control protein 2 homolog 2;
DE            EC=2.7.11.22;
GN   Name=CRK2;
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 Ser-56 or Tyr-57 inactivates
CC       the enzyme. {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; X74598; CAA52676.1; -; Genomic_DNA.
DR   PIR; S36607; S36607.
DR   AlphaFoldDB; P54665; -.
DR   SMR; P54665; -.
DR   OMA; QWNSGEE; -.
DR   BRENDA; 2.7.11.22; 6520.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:SF254; CYCLIN-DEPENDENT KINASE 2; 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..345
FT                   /note="Cell division control protein 2 homolog 2"
FT                   /id="PRO_0000085708"
FT   DOMAIN          46..328
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         52..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   345 AA;  39238 MW;  6E4E88D2571931B8 CRC64;
     MQVQVQEGQT ACDGSLRPLP SAGPASFVPR SLRPAPLRGT STPDRYSRIE KVGEGSYGIV
     YKCHDNFTGR TVAMKRIPLI VNDGGVPSTA VREVSLLREL NHPYVVRLLD VVLHEAKLLL
     IFEYMEQDLQ GMLKQRNTAF VGGKLRRIMF QLLLGLHECH SRRFVHRDIK PSNILIDRKE
     SVVKLADFGL GRAFRVPLQT YTTEVMTLWY RAPEVLLGDK QYLPAVDVWS MGCVFAELAR
     RRSLFAGDTA INQLFSIFQL LGTPTEATWR GVTSLPHHNV NFPRWTAKPL RTAVPALDDD
     GVDLLRRMLC YNPRERITAY EALQHSYFDE VREEEVEKLM RFNGA
//