SSN3_MAGO7
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 03-AUG-2022, entry version 91.
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; 642369at2759; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
