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Serine/threonine-protein kinase SSN3 (EC 2.7.11.22) (EC 2.7.11.23) (Cyclin-dependent kinase 8) (KlSRB10)

 SSN3_KLULA              Reviewed;         593 AA.
Q6CR51; Q70W23;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
10-OCT-2018, entry version 98.
RecName: Full=Serine/threonine-protein kinase SSN3;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=Cyclin-dependent kinase 8;
AltName: Full=KlSRB10;
Name=SSN3; Synonyms=CDK8, SRB10; OrderedLocusNames=KLLA0D11814g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15116433; DOI=10.1002/yea.1117;
Nunez L., Fernandez-Otero C., Rodriguez-Belmonte E., Cerdan M.E.;
"The KlSRB10 gene from Kluyveromyces lactis.";
Yeast 21:511-518(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is
a regulatory module of the Mediator complex which is itself
involved in regulation of basal and activated RNA polymerase II-
dependent transcription. The SRB8-11 complex may be involved in
the transcriptional repression of a subset of genes regulated by
Mediator. It may inhibit the association of the Mediator complex
with RNA polymerase II to form the holoenzyme complex. The SRB8-11
complex phosphorylates the C-terminal domain (CTD) of the largest
subunit of RNA polymerase II (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of
the Mediator complex. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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EMBL; AJ532841; CAD58722.1; -; Genomic_DNA.
EMBL; CR382124; CAH00684.1; -; Genomic_DNA.
RefSeq; XP_453588.1; XM_453588.1.
ProteinModelPortal; Q6CR51; -.
SMR; Q6CR51; -.
STRING; 284590.XP_453588.1; -.
PRIDE; Q6CR51; -.
EnsemblFungi; CAH00684; CAH00684; KLLA0_D11814g.
GeneID; 2892704; -.
KEGG; kla:KLLA0_D11814g; -.
eggNOG; KOG0666; Eukaryota.
eggNOG; ENOG410XPPA; LUCA.
HOGENOM; HOG000233024; -.
InParanoid; Q6CR51; -.
KO; K02208; -.
OMA; IMWQILD; -.
OrthoDB; EOG092C2FL8; -.
Proteomes; UP000000598; Chromosome D.
GO; GO:0016592; C:mediator complex; IEA:EnsemblFungi.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
GO; GO:0060258; P:negative regulation of filamentous growth; IEA:EnsemblFungi.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:EnsemblFungi.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi.
GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IEA:EnsemblFungi.
GO; GO:0031648; P:protein destabilization; IEA:EnsemblFungi.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
Activator; ATP-binding; Complete proteome; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
Repressor; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
CHAIN 1 593 Serine/threonine-protein kinase SSN3.
/FTId=PRO_0000312946.
DOMAIN 90 489 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 96 104 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 516 555 Asn-rich.
COMPBIAS 560 570 Ala-rich.
ACT_SITE 312 312 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 211 211 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CONFLICT 50 50 N -> T (in Ref. 1; CAD58722).
{ECO:0000305}.
SEQUENCE 593 AA; 67013 MW; 4B4CC0E3731164BC CRC64;
MYGNQQNNSN PYQMSYYRMN NGQGQGTNRW PQQLSHQEML AGHSQQILNN NKPAGNQSKP
PIVMASNNVF SIGPYRQRKD SSRISVLQKY EIIGYIAAGT YGKVYKAKAR DYQNGMNRDN
VIILDSPDSV SADSNLDINS INRSTRQQEA NDNLTTMDFR KPSHKRFTPP NNSNSTQIRS
NSGSETNVRI NSSSITNNSR KPSQIQFYAI KKFKTEREGV EHYTGISQSA CREMSLCREL
DNNHLTKLVE IFLEKKSIYM VSEFAEHDLL QIIHFHSHPE KRLIPPRMLK SIMWQILDGV
SYLHQNWILH RDLKPANIMV TVDGCVKIGD LGLARKFNNM VQTLYTGDKV IVTIWYRAPE
LILGARHYTP AIDLWAVGCI FAELIGLRPI FKGEEAKMES KKSVLFQANQ FQKILEVMGS
PDHKIWPNID SYPEYLQLAK MPKYRDNLTA WYQTAGGKDK TALDILYRLL QYDPIKRIDA
IDALDHVYFT NGDPPVCENV FEGLNYKYPP RRIHTNDNDI TNVGNDNNQA NHSQKQPMHG
NNNNKNGNMN GLGVNKRILA AAAAAAAAAA VSGNGNNPTS NTATGGSARK KRK


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