ID   CDK7_DICDI              Reviewed;         360 AA.
AC   P54685; Q54MR4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Cyclin-dependent kinase 7;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=CDK-activating kinase;
DE            Short=CAK;
DE   AltName: Full=Cell division protein kinase 7;
DE   AltName: Full=MO15 homolog;
GN   Name=cdk7; Synonyms=cdcC, cdcD, mo15; ORFNames=DDB_G0285417;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=V12M2;
RX   PubMed=7662315; DOI=10.1139/o95-006;
RA   Michaelis C.E., Luo Q., Weeks G.;
RT   "A Dictyostelium discoideum gene, which is highly related to mo15 from
RT   Xenopus, is expressed during growth but not during development.";
RL   Biochem. Cell Biol. 73:51-58(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalytic part of CAK which activates cyclin-associated
CC       CDK1/CDK2/CDK4 by threonine phosphorylation, thereby allowing MPF
CC       activation. {ECO:0000250}.
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   -!- 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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC   -!- SUBUNIT: Probably associates with cyclin H and mat1 to form a
CC       multimeric active enzyme. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Only expressed during vegetative cell growth.
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; S79590; AAB35208.2; -; mRNA.
DR   EMBL; AAFI02000079; EAL64546.1; -; Genomic_DNA.
DR   RefSeq; XP_638229.1; XM_633137.1.
DR   AlphaFoldDB; P54685; -.
DR   SMR; P54685; -.
DR   STRING; 44689.P54685; -.
DR   PaxDb; 44689-DDB0191429; -.
DR   EnsemblProtists; EAL64546; EAL64546; DDB_G0285417.
DR   GeneID; 8625277; -.
DR   KEGG; ddi:DDB_G0285417; -.
DR   dictyBase; DDB_G0285417; cdk7.
DR   eggNOG; KOG0659; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; P54685; -.
DR   OMA; DDNWPGV; -.
DR   PhylomeDB; P54685; -.
DR   BRENDA; 2.7.11.22; 1939.
DR   Reactome; R-DDI-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-DDI-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR   Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DDI-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-DDI-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-DDI-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR   Reactome; R-DDI-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-DDI-72086; mRNA Capping.
DR   Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-DDI-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-DDI-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-DDI-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-DDI-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-DDI-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   PRO; PR:P54685; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070985; C:transcription factor TFIIK complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07841; STKc_CDK7; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR037770; CDK7.
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:SF0; CYCLIN-DEPENDENT KINASE 7; 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; Meiosis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..360
FT                   /note="Cyclin-dependent kinase 7"
FT                   /id="PRO_0000085796"
FT   DOMAIN          4..288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          333..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
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         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        360
FT                   /note="V -> VKK (in Ref. 1; AAB35208)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40567 MW;  F6FE0441F21D6B37 CRC64;
     MDKYNIEALI GEGTYGVVSR ATVKATGQIV AIKKIRKILI QNQTDDGINF SAIREIKILQ
     ELKHDNVVNL LDIFAHKSNV YLVFELMQWD LQEVIEDKSI ILKPADIKSY MKMLLQGIEA
     CHRNWVLHRD LKPNNLLMSI NGDLKLADFG LARQYGSPNK VFSPQAVTIF YRAPELLFGA
     KSYGPSVDIW SIGCIFAELM LRTPYLPGTG EIDQLRKICS ALGTPNESNW PGVTCLPNYI
     KFTDHPATPF KQLFTAASDE AIDLISKMLL FNPSNRISAA DALNHPYFTS GVKHTNPADL
     PVPFAKKASL LQQRQVLAQV QQQLLQKQQQ QQQQQQQQIQ SQPEPIQVDN VEQTQQAQQV
//