ID SSN3_CANGA Reviewed; 567 AA. AC Q6FKC6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Serine/threonine-protein kinase SSN3; DE EC=2.7.11.22; DE EC=2.7.11.23; DE AltName: Full=Cyclin-dependent kinase 8; GN Name=SSN3; Synonyms=CDK8; OrderedLocusNames=CAGL0L12650g; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a CC regulatory module of the Mediator complex which is itself involved in CC regulation of basal and activated RNA polymerase II-dependent CC transcription. The SRB8-11 complex may be involved in the CC transcriptional repression of a subset of genes regulated by Mediator. CC It may inhibit the association of the Mediator complex with RNA CC polymerase II to form the holoenzyme complex. The SRB8-11 complex CC phosphorylates the C-terminal domain (CTD) of the largest subunit of CC RNA polymerase II (By similarity). {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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of the CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR380958; CAG62292.1; -; Genomic_DNA. DR RefSeq; XP_449318.1; XM_449318.1. DR AlphaFoldDB; Q6FKC6; -. DR SMR; Q6FKC6; -. DR STRING; 284593.Q6FKC6; -. DR EnsemblFungi; CAGL0L12650g-T; CAGL0L12650g-T-p1; CAGL0L12650g. DR GeneID; 2890604; -. DR KEGG; cgr:CAGL0L12650g; -. DR CGD; CAL0135266; CAGL0L12650g. DR VEuPathDB; FungiDB:CAGL0L12650g; -. DR eggNOG; KOG0666; Eukaryota. DR HOGENOM; CLU_000288_181_6_1; -. DR InParanoid; Q6FKC6; -. DR OMA; MVTVDGC; -. DR Proteomes; UP000002428; Chromosome L. DR GO; GO:1990508; C:CKM complex; IEA:EnsemblFungi. DR GO; GO:0016592; C:mediator complex; IEA:EnsemblFungi. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC. DR GO; GO:0060258; P:negative regulation of filamentous growth; IEA:EnsemblFungi. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi. DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:EnsemblFungi. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IEA:EnsemblFungi. DR GO; GO:0031648; P:protein destabilization; IEA:EnsemblFungi. 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; 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; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW Activator; ATP-binding; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Nucleus; Reference proteome; Repressor; KW Serine/threonine-protein kinase; Transcription; Transcription regulation; KW Transferase. FT CHAIN 1..567 FT /note="Serine/threonine-protein kinase SSN3" FT /id="PRO_0000312939" FT DOMAIN 68..470 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 88..179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 546..567 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 88..123 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..170 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 293 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 74..82 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 190 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 567 AA; 63532 MW; 4CED3A8B663AC2EF CRC64; MQNSGRDLWQ NQSGYMSSLQ QGLNKSNMVG ASTSHGKTPM LMANNDVFTI APYRTRKDNA RVSVLDKYEI IGYIAAGTYG KVYKAKSRQS SKSSSSTGSD SLAQDTKPTT EFSNTSSLQN AGTYGDMMGA HGPNSNNISA GGNTNPELST RNNPNNPRVP TSTIISGDKR NSENTDNRRK AETTMYYAIK KFKTEKDGIE QLHYTGISQS ACREMALCRE LDNNHLTKLV EIFLQKKSIY MVYEFAEHDL LQIIHFHSHP EKRMIPPRMI RSIMWQILDG VSYLHQNWVL HRDLKPANIM VTMDGVVKIG DLGLARKFSN MLQTMYTGDK VVVTIWYRAP ELLLGARHYT PAIDLWAVGC IFAELIGLQP IFKGEEAKMD SKKTVPFQAN QLQRILKILG TPTPKSWPHL QKYPEYEQLS KFPKYRDNLP GWFHSAGGRD KHALSLLYHL LNYNPIERID AINALDHSYF THGDMPVCEN VFEGLNYKYP ARRIHTNDND ILNLGLHKPK VPAKVVQPTM NNSTATLGGL GVNKRILAAA AAAAAAVSGN SSSQSSRNME PMKKKRK //