ID   CDK1_EMENI              Reviewed;         323 AA.
AC   Q00646; C8V4M9; Q5B5J8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 160.
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 control protein 2;
DE   AltName: Full=Cell division protein kinase 1;
DE   AltName: Full=Never in mitosis protein X;
GN   Name=nimX {ECO:0000303|PubMed:7962194};
GN   Synonyms=cdc2 {ECO:0000303|PubMed:7962194}, cdk1; ORFNames=AN4182;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mycelium;
RX   PubMed=7962194; DOI=10.1242/jcs.107.6.1519;
RA   Osmani A.H., van Peij N., Mischke M., O'Connell M.J., Osmani S.A.;
RT   "A single p34cdc2 protein kinase (encoded by nimXcdc2) is required at G1
RT   and G2 in Aspergillus nidulans.";
RL   J. Cell Sci. 107:1519-1528(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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-180 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; U07169; AAA20597.1; -; mRNA.
DR   EMBL; AACD01000068; EAA59281.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF74540.1; -; Genomic_DNA.
DR   RefSeq; XP_661786.1; XM_656694.1.
DR   AlphaFoldDB; Q00646; -.
DR   SMR; Q00646; -.
DR   MINT; Q00646; -.
DR   STRING; 227321.Q00646; -.
DR   EnsemblFungi; CBF74540; CBF74540; ANIA_04182.
DR   GeneID; 2873604; -.
DR   KEGG; ani:AN4182.2; -.
DR   VEuPathDB; FungiDB:AN4182; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; Q00646; -.
DR   OMA; YLYQITR; -.
DR   OrthoDB; 244018at2759; -.
DR   BRENDA; 2.7.11.22; 517.
DR   Proteomes; UP000000560; Chromosome II.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:AspGD.
DR   GO; GO:0005816; C:spindle pole body; IDA:AspGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:AspGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:AspGD.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:AspGD.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..323
FT                   /note="Cyclin-dependent kinase 1"
FT                   /id="PRO_0000085719"
FT   DOMAIN          4..306
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        147
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         180
FT                   /note="Phosphothreonine; by CAK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  36779 MW;  3178CAFBDDC32224 CRC64;
     MENYQKIEKI GEGTYGVVYK ARELTHPNRI VALKKIRLEA EDEGVPSTAI REISLLKEMN
     DPNIVRLLNI VHADGHKLYL VFEFLDLDLK KYMEALPVSE GGRGRALPDG STLSRNLGLG
     DAMVKKFMAQ LIEGIRFCHS HRVLHRDLKP QNLLIDRDGN LKLADFGLAR AFGVPLRTYT
     HEVVTLWYRS PEILLGGRQY STGVDMWSCG AIFAEMCTRK PLFPGDSEID EIFKIFRILG
     TPDETIWPGV TSFPDFKPTF PKWKREDIQN VVPGLEEDGL DLLEALLEYD PARRISAKQA
     CMHPYFQHGS SYYSGRARRN GFH
//