ID   CDK8_CAEBR              Reviewed;         612 AA.
AC   P0C661; A8XFM1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Cyclin-dependent kinase 8;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=Cell division protein kinase 8;
DE   AltName: Full=Mediator complex subunit cdk-8;
DE   AltName: Full=Mediator of RNA polymerase II transcription subunit cdk-8;
GN   Name=cdk-8; ORFNames=CBG12346;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       regulated gene transcription of nearly all RNA polymerase II-dependent
CC       genes. Mediator functions as a bridge to convey information from gene-
CC       specific regulatory proteins to the basal RNA polymerase II
CC       transcription machinery. Mediator is recruited to promoters by direct
CC       interactions with regulatory proteins and serves as a scaffold for the
CC       assembly of a functional pre-initiation complex with RNA polymerase II
CC       and the general transcription factors. Phosphorylates the CTD (C-
CC       terminal domain) of the large subunit of RNA polymerase II (RNAp II),
CC       which may inhibit the formation of a transcription initiation complex
CC       (By similarity). {ECO:0000250|UniProtKB:Q9VT57}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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; HE600913; CAP31338.3; -; Genomic_DNA.
DR   AlphaFoldDB; P0C661; -.
DR   SMR; P0C661; -.
DR   STRING; 6238.P0C661; -.
DR   WormBase; CBG12346; CBP39634; WBGene00033308; Cbr-cdk-8.
DR   eggNOG; KOG0666; Eukaryota.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; P0C661; -.
DR   OMA; YFKNGGP; -.
DR   OrthoDB; 46620at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   CDD; cd07842; STKc_CDK8_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:SF495; CYCLIN-DEPENDENT KINASE 8; 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   Activator; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repressor; Serine/threonine-protein kinase;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..612
FT                   /note="Cyclin-dependent kinase 8"
FT                   /id="PRO_0000312930"
FT   DOMAIN          23..345
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          403..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         29..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   612 AA;  70642 MW;  CE8F21A8F5A384CC CRC64;
     MIDENFKKKL AVSRERVEDL FYFENSKEIG RGTYGLVYKA VPKHSNGRFP NKEYALKMIE
     GQGFSMSACR EIALFRELRH PNLICLQRVF LTNEKKVWLL LDYAEHDLWH VIKHHRTAKT
     KKVPIMVPRN MVKNILFQIL SGMHYLHSNW VLHRDLKPAN ILLMGDGGPD MRGRVKIADL
     GFSRIFANPL KPMAELDPVV VTFWYRAPEL LLGAKHYTKA IDVWAIGCIF AELLTAEPLF
     FCKEEDIKAQ NPYHYDQVKR IFHLLGYPSD TDWPDMKKMP DHQRLLNDAR NEGTPIQTFP
     NSLQRYFDKW KINSQSSPYR LLVKLLTVDP LKRVSCEEAM NDIYFRKMER PPRETDDVFN
     RYPIPYAKKE QQITIPIDQF QQQQQQQQQQ QQQQQQQQQQ QQQQQMQQPQ IGPPQMMGQP
     QMGQPQMGQP QMGQPQMGQP QMGQPQMVPS QMGQPPMGGP HPGVVAPDGH AHQMMQQQHQ
     SQHHMQYQQM HDSMQGGMDD GGPQAKMMRM GNVPVGRYGP MGPPYGPQDF HAPQGPPMMQ
     MMPQPGPSGY YQQRPGQPPG PGPQGYMNPQ MGMTMGMRPQ GVPQQAYMPG RGMPPPQGPN
     PQQQQQWQQY HR
//