SSN3_ASHGO
ID SSN3_ASHGO Reviewed; 581 AA.
AC Q751F5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=AGL249C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 368.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR EMBL; AE016820; AAS54242.2; -; Genomic_DNA.
DR RefSeq; NP_986418.2; NM_211480.2.
DR AlphaFoldDB; Q751F5; -.
DR SMR; Q751F5; -.
DR STRING; 33169.AAS54242; -.
DR EnsemblFungi; AAS54242; AAS54242; AGOS_AGL249C.
DR GeneID; 4622711; -.
DR KEGG; ago:AGOS_AGL249C; -.
DR eggNOG; KOG0666; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q751F5; -.
DR OMA; MVTVDGC; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:1990508; C:CKM complex; IEA:EnsemblFungi.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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: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; IBA:GO_Central.
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: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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblFungi.
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..581
FT /note="Serine/threonine-protein kinase SSN3"
FT /id="PRO_0000312932"
FT DOMAIN 85..475
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 34..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 91..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 581 AA; 64530 MW; 11B88D39F280B640 CRC64;
MGIRLQSSDS MNNQHQTQQN KYFNVSNQAS TRSLWSQQQQ QQLLDTKGSA STSKSPMLMA
NNNVFSIGPY RQRKDAGRVS VLEKYEIIGY IAAGTYGKVY KAKAKETQEE QENSIHTHNQ
TLGSVSVAGI DGGMASREVE NGGDDPLRLD GHGGIAVAPA AGGGLSSAAA HRARSNGAVK
ALPKKSAFTP FYAIKKFKTE REGVEQLHYT GISQSACREM SLCRELDNKH LTKLVEIFLE
RKSIYMVSEF AEHDLLQIIH FHSHPEKRLI APRMLKSIMW QILDGVSYLH QNWILHRDLK
PANIMVTVDG CVKIGDLGLA RKFYNLVQTL YTGDKVVVTI WYRAPELLLG ARHYSPAIDL
WAVGCIFAEL IGLRPIFKGE EAKMDSKKSV PFQGNQLQRI LEVLGTPTHH TWPNIHKYPE
YEQLSKFSKY RDNLSVWYHS SGGRDKAALS LLYSLLKYDP ITRIDAIDAL EHEYFTNNDP
PVSSDVFEGL SYKYPPRRIH TSDNDIMNVG ANKNKSGFNH HPPQQQTVNN NGVTNSSIGG
LGVNRRILAA AAAAAAAVQV NGTNIVSGSS SSNGPIRKKK R
