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 24-JAN-2024, entry version 115.
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 VEuPathDB; FungiDB:I7I51_07101; -.
DR VEuPathDB; FungiDB:I7I52_10599; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07835; STKc_CDK1_CdkB_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; 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
//
