ID   CRK1_LEIME              Reviewed;         301 AA.
AC   Q06309;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cell division protein kinase 2 homolog CRK1;
DE            EC=2.7.11.23;
GN   Name=CRK1;
OS   Leishmania mexicana.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MNYC/BZ/62/M379;
RX   PubMed=8407941; DOI=10.1016/s0021-9258(19)36891-7;
RA   Mottram J.C., Kinnaird J.H., Shiels B.R., Tait A., Barry J.D.;
RT   "A novel CDC2-related protein kinase from Leishmania mexicana, LmmCRK1, is
RT   post-translationally regulated during the life cycle.";
RL   J. Biol. Chem. 268:21044-21052(1993).
CC   -!- FUNCTION: May be involved in some stage-specific role in the
CC       promastigote cell cycle.
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   -!- ACTIVITY REGULATION: Phosphorylation at Thr-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   -!- DEVELOPMENTAL STAGE: Expressed in all life cycle stages, promastigote,
CC       metacyclic and amastigote forms but is found in the active form only in
CC       the promastigote stage.
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; X60385; CAA42936.1; -; Genomic_DNA.
DR   PIR; A48041; A48041.
DR   AlphaFoldDB; Q06309; -.
DR   SMR; Q06309; -.
DR   VEuPathDB; TriTrypDB:LmxM.21.1080; -.
DR   OMA; IWRIRTI; -.
DR   BRENDA; 2.7.11.22; 2951.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..301
FT                   /note="Cell division protein kinase 2 homolog CRK1"
FT                   /id="PRO_0000085878"
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         160
FT                   /note="Phosphothreonine; by CAK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  34473 MW;  58EB39D006D88461 CRC64;
     MTSRYERQEK IGEGTYGVVY KARDTSTAAT VALKRIRLDS EEEGVPCTAI REISLLKELR
     HENIVKLLDV CHSEHRLTIV FEYLDLDLKK YLDRENGNLD AATIQHFMRD LLRGVAFCHQ
     RSVLHRDLKP QNLLISREKE LKLGDFGLGR SFAIPVRKFT NEVVTLWYRP PDVLLGSMQY
     GPPVDVWSVG CIFSEMATGT PLFAGKNDAD QLMRIFRFLG TPNNRVWPSM NQYPNSNNML
     SQPEFLQNFE PEWSNVLGSV PGYEKLGCAG VDLLERLLRY EPSERITAAD ALNHPYFSLQ
     F