(data stored in ACNUC6288 zone)

SWISSPROT: SSN3_DEBHA

ID   SSN3_DEBHA              Reviewed;         472 AA.
AC   Q6BM25;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-MAY-2019, entry version 103.
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=DEHA2F08844g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       a regulatory module of the Mediator complex which is itself
CC       involved in regulation of basal and activated RNA polymerase II-
CC       dependent transcription. The SRB8-11 complex may be involved in
CC       the transcriptional repression of a subset of genes regulated by
CC       Mediator. It may inhibit the association of the Mediator complex
CC       with RNA polymerase II to form the holoenzyme complex. The SRB8-11
CC       complex phosphorylates the C-terminal domain (CTD) of the largest
CC       subunit of 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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         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(+) +
CC         phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216,
CC         Rhea:RHEA-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
CC       the Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
DR   EMBL; CR382138; CAG89087.2; -; Genomic_DNA.
DR   RefSeq; XP_460746.2; XM_460746.1.
DR   SMR; Q6BM25; -.
DR   STRING; 4959.XP_460746.2; -.
DR   PRIDE; Q6BM25; -.
DR   EnsemblFungi; CAG89087; CAG89087; DEHA2F08844g.
DR   GeneID; 2903762; -.
DR   KEGG; dha:DEHA2F08844g; -.
DR   HOGENOM; HOG000233024; -.
DR   InParanoid; Q6BM25; -.
DR   KO; K02208; -.
DR   OMA; HAIKKFK; -.
DR   OrthoDB; 642369at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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: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: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   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; Q6BM25.
DR   SWISS-2DPAGE; Q6BM25.
KW   Activator; ATP-binding; Complete proteome; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Repressor; Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    472       Serine/threonine-protein kinase SSN3.
FT                                /FTId=PRO_0000312943.
FT   DOMAIN       59    418       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      65     73       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    237    237       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     125    125       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
SQ   SEQUENCE   472 AA;  53783 MW;  0B4DE36D27A15AA2 CRC64;
     MNSGYNPGNA NHITSHSNRT KNGVPTIPQP ALMASNAILT IGPYKHRKDL IRESVLTKYQ
     IIGYIAAGTY GKVYKAKSKT NGNSNSNSAL MNDNVISIGN GQKEAGLQKT NNESMEDKNQ
     LFAIKKFKSD NHSNKNNHDI NGNEVIHYTG ISQSAIREMS LCRELSNKNI TKVVDILLEN
     KSIYMVFEYC EHDLLQIIQY HSHPDVKPIP DFTIKSITWQ ILNGVTFLHK NWIFHRDLKP
     ANIMVSSSGV VKIGDLGLAR KFNNPLQSLY TGDKVVVTIW YRAPELLLGA RHYTPSIDLW
     AVGCILAELL SLRPIFKGEE AKIDMNNKKS VPFQKNQLQK IVEVLGTPTT KNWPTITKYP
     EYSAFQQHFS NTYPPNLISW YKLIGRTSKQ CLNLLRCLLE YDPTIRITAD DALTHAFFLE
     LPKMSENSFE GLSQKYPKRR IYTHENDIVS NSQHVNNKRH GYDDNMTRKR QR
//

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