ID   CDK1_AJECA              Reviewed;         324 AA.
AC   P54119;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cyclin-dependent kinase 1 {ECO:0000250|UniProtKB:P00546};
DE            Short=CDK1 {ECO:0000250|UniProtKB:P00546};
DE            EC=2.7.11.22 {ECO:0000250|UniProtKB:P04551};
DE   AltName: Full=Cell division protein kinase 1;
GN   Name=CDC2 {ECO:0000303|PubMed:8125338}; Synonyms=CDK1;
OS   Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=5037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26032 / G217B;
RX   PubMed=8125338; DOI=10.1016/0378-1119(94)90729-3;
RA   di Lallo G., Gargano S., Maresca B.;
RT   "The Histoplasma capsulatum cdc2 gene is transcriptionally regulated during
RT   the morphologic transition.";
RL   Gene 140:51-57(1994).
CC   -!- FUNCTION: Cyclin-dependent kinase that acts as a master regulator of
CC       the mitotic and meiotic cell cycles. {ECO:0000250|UniProtKB:P04551}.
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         Evidence={ECO:0000250|UniProtKB:P24941};
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; Evidence={ECO:0000250|UniProtKB:P04551};
CC   -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-181 activates it.
CC       {ECO:0000250|UniProtKB:P06493}.
CC   -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
CC       subunit (SUC1) and with a cyclin. {ECO:0000250|UniProtKB:P04551}.
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; X74361; CAA52405.1; -; Genomic_DNA.
DR   PIR; S36437; S36437.
DR   AlphaFoldDB; P54119; -.
DR   SMR; P54119; -.
DR   BRENDA; 2.7.11.22; 221.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; Cell cycle; Cell division; Kinase; Mitosis;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..324
FT                   /note="Cyclin-dependent kinase 1"
FT                   /id="PRO_0000085718"
FT   DOMAIN          4..307
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
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         14
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         181
FT                   /note="Phosphothreonine; by CAK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36824 MW;  3B80A7F5BD4E748B CRC64;
     MENYQKIEKI GEGTYGVVYK ARDLTHPNRI VALKKIRLEA EDEGVPSTAI REISLLKEMH
     DPNIVRLLNI VHADGHKLYL VFEFLDLDLK KYMEALPVSE GGRGKALPDG STLDMNRLGL
     GEAMVKKFMA QLVEGIRYCH SHRVLHRDLK PQNLLIDREG NLKLADFGLA RAFGVPLRTY
     THEVVTLWYR APEILLGGRQ YSTGVDMWSV GAIFAEMCTR KPLFPGDSEI DEIFKIFKLL
     GTPDENTWPG VTSFPDFKAS FPKWKREDTR KLVPGLERNG LDLLDAMLEY DPARRISAKQ
     ACMHPYFQAG SSAYSGRERL QPYP