CDK1_EMENI
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 03-AUG-2022, entry version 153.
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; 162425.CADANIAP00004488; -.
DR EnsemblFungi; CBF74540; CBF74540; ANIA_04182.
DR EnsemblFungi; EAA59281; EAA59281; AN4182.2.
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; NNDVWPE; -.
DR OrthoDB; 1010560at2759; -.
DR BRENDA; 2.7.11.22; 517.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0007165; P:signal transduction; IBA:GO_Central.
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; 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
