ID SSN3_MAGO7 Reviewed; 499 AA. AC A4QXX4; G4N9S7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 22-FEB-2023, entry version 93. 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; ORFNames=MGG_13931; OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast OS fungus) (Pyricularia oryzae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia. OX NCBI_TaxID=242507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958; RX PubMed=15846337; DOI=10.1038/nature03449; RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.; RT "The genome sequence of the rice blast fungus Magnaporthe grisea."; RL Nature 434:980-986(2005). 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; CM001234; EHA49585.1; -; Genomic_DNA. DR RefSeq; XP_003715904.1; XM_003715856.1. DR AlphaFoldDB; A4QXX4; -. DR SMR; A4QXX4; -. DR STRING; 318829.MGG_13931T0; -. DR EnsemblFungi; MGG_13931T0; MGG_13931T0; MGG_13931. DR GeneID; 5049253; -. DR KEGG; mgr:MGG_13931; -. DR VEuPathDB; FungiDB:MGG_13931; -. DR eggNOG; KOG0666; Eukaryota. DR InParanoid; A4QXX4; -. DR OMA; VYLHRNW; -. DR OrthoDB; 46620at2759; -. DR Proteomes; UP000009058; Chromosome 4. 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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi. DR GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt. 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 GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblFungi. 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 19; 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..499 FT /note="Serine/threonine-protein kinase SSN3" FT /id="PRO_0000312947" FT DOMAIN 61..442 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 332..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 463..499 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 358..376 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 193 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 67..75 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 499 AA; 55094 MW; 4D6D22BA3A00FAA1 CRC64; MSHSNPPTGA SGGPGSASAS AAPARGYYSL KRSIQTAFND PLDRGLGPPA YQSKVRVMDK YQVIGFISSG TYGRVYKARG RQGQPGEFAI KKFKPDKEGE QITYTGISQS AIREMALCSE LRHPNVIRLV ETILEDKAIF MVFEYAEHDL LQIIHHHTQQ PKHPIPPQTI KSIMFQLLNG CQYLHTNWVL HRDLKPANIM VTSSGEVKVG DLGLARIFWK PVRTLMQGDK VVVTIWYRAP ELLMGSHHYT PAVDMWAVGC IFAELLSLRP IFKGEEAKMD NTKKGGSRDM PFQRHQMQKI VDIMGMPTKE RWPLLTSMPD YDKLPLLQPP LSASGYSQQP AHSHHHHQHY NQGPQYGGRA GGPTSSSSAN SSSAAAAASQ SHLDKWYYHT VSQGQTAGPM PHAPPGSLAS LGVEGYKLLA GLLEYDPEKR LTAAAALQHN FFSTGDRVSA NCFEGCKAEY PHRRVSQEDN DIRTGSVPGT KRSGMPDDSM GRPGKRVKE //