(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 113.
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}.
DR   EMBL; AE016820; AAS54242.2; -; Genomic_DNA.
DR   RefSeq; NP_986418.2; NM_211480.2.
DR   SMR; Q751F5; -.
DR   STRING; 33169.AAS54242; -.
DR   EnsemblFungi; AAS54242; AAS54242; AGOS_AGL249C.
DR   GeneID; 4622711; -.
DR   KEGG; ago:AGOS_AGL249C; -.
DR   HOGENOM; HOG000233024; -.
DR   InParanoid; Q751F5; -.
DR   KO; K02208; -.
DR   OMA; VCENVFE; -.
DR   Proteomes; UP000000591; Chromosome VII.
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: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;
DR   PRODOM; Q751F5.
DR   SWISS-2DPAGE; Q751F5.
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   NP_BIND         91..99
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        37..42
FT                   /note="Poly-Gln"
FT   COMPBIAS        549..557
FT                   /note="Poly-Ala"
FT   COMPBIAS        567..572
FT                   /note="Poly-Ser"
FT   ACT_SITE        298
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         195
FT                   /note="ATP"
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
//

If you have problems or comments...

PBIL Back to PBIL home page