ID   CAK1_YEAST              Reviewed;         368 AA.
AC   P43568; D6VTK1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 197.
DE   RecName: Full=Serine/threonine-protein kinase CAK1;
DE            EC=2.7.11.22;
DE   AltName: Full=CDK-activating kinase;
GN   Name=CAK1; Synonyms=CIV1; OrderedLocusNames=YFL029C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8752210; DOI=10.1016/s0092-8674(00)80129-4;
RA   Kaldis P., Sutton A., Solomon M.J.;
RT   "The Cdk-activating kinase (CAK) from budding yeast.";
RL   Cell 86:553-564(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- INTERACTION:
CC       P43568; P00546: CDC28; NbExp=3; IntAct=EBI-3953, EBI-4253;
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; U60192; AAB17052.1; -; Genomic_DNA.
DR   EMBL; D50617; BAA09209.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12411.1; -; Genomic_DNA.
DR   PIR; S56225; S56225.
DR   RefSeq; NP_116624.1; NM_001179937.1.
DR   AlphaFoldDB; P43568; -.
DR   SMR; P43568; -.
DR   BioGRID; 31117; 249.
DR   DIP; DIP-1637N; -.
DR   FunCoup; P43568; 422.
DR   IntAct; P43568; 6.
DR   MINT; P43568; -.
DR   STRING; 4932.YFL029C; -.
DR   BindingDB; P43568; -.
DR   ChEMBL; CHEMBL5003; -.
DR   iPTMnet; P43568; -.
DR   PaxDb; 4932-YFL029C; -.
DR   PeptideAtlas; P43568; -.
DR   EnsemblFungi; YFL029C_mRNA; YFL029C; YFL029C.
DR   GeneID; 850515; -.
DR   KEGG; sce:YFL029C; -.
DR   AGR; SGD:S000001865; -.
DR   SGD; S000001865; CAK1.
DR   VEuPathDB; FungiDB:YFL029C; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; P43568; -.
DR   OMA; SIDITHC; -.
DR   OrthoDB; 413582at2759; -.
DR   BioCyc; YEAST:G3O-30431-MONOMER; -.
DR   BRENDA; 2.7.11.22; 984.
DR   BioGRID-ORCS; 850515; 4 hits in 13 CRISPR screens.
DR   PRO; PR:P43568; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43568; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:SGD.
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:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR   GO; GO:0060633; P:negative regulation of transcription initiation by RNA polymerase II; IGI:SGD.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   PANTHER; PTHR44167:SF24; SERINE_THREONINE-PROTEIN KINASE CHK2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..368
FT                   /note="Serine/threonine-protein kinase CAK1"
FT                   /id="PRO_0000085690"
FT   DOMAIN          1..368
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
SQ   SEQUENCE   368 AA;  42186 MW;  852AFD1E95B90C42 CRC64;
     MKLDSIDITH CQLVKSTRTA RIYRSDTYAI KCLALDFDIP PHNAKFEVSI LNKLGNKCKH
     ILPLLESKAT DNNDLLLLFP FEEMNLYEFM QMHYKRDRRK KNPYYDLLNP SIPIVADPPV
     QKYTNQLDVN RYSLSFFRQM VEGIAFLHEN KIIHRDIKPQ NIMLTNNTST VSPKLYIIDF
     GISYDMANNS QTSAEPMDSK VTDISTGIYK APEVLFGVKC YDGGVDVWSL LIIISQWFQR
     ETSRMGHVPA MIDDGSDDMN SDGSDFRLIC SIFEKLGIPS IQKWEEVAQH GSVDAFVGMF
     GADGDGKYVL DQEKDVQISI VERNMPRLDE IADVKVKQKF INCILGMVSF SPNERWSCQR
     ILQELEKP
//