SSN3_YEAST
ID SSN3_YEAST Reviewed; 555 AA.
AC P39073; D6W3X1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Meiotic mRNA stability protein kinase SSN3;
DE EC=2.7.11.22 {ECO:0000269|PubMed:10360183, ECO:0000269|PubMed:11331604, ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:12520306, ECO:0000269|PubMed:14749387, ECO:0000269|PubMed:15687503, ECO:0000269|PubMed:9702190};
DE EC=2.7.11.23 {ECO:0000269|PubMed:10360183, ECO:0000269|PubMed:11331604, ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:12520306, ECO:0000269|PubMed:14749387, ECO:0000269|PubMed:15687503, ECO:0000269|PubMed:9702190};
DE AltName: Full=Cyclin-dependent kinase 8;
DE AltName: Full=Suppressor of RNA polymerase B SRB10;
GN Name=SSN3; Synonyms=ARE1, CDK8, GIG2, SRB10, UME5;
GN OrderedLocusNames=YPL042C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-183.
RX PubMed=8164691; DOI=10.1128/mcb.14.5.3446-3458.1994;
RA Surosky R.T., Strich R., Esposito R.E.;
RT "The yeast UME5 gene regulates the stability of meiotic mRNAs in response
RT to glucose.";
RL Mol. Cell. Biol. 14:3446-3458(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH SSN8.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7877695; DOI=10.1038/374193a0;
RA Liao S.-M., Zhang J., Jeffery D.A., Koleske A.J., Thompson C.M., Chao D.M.,
RA Viljoen M., van Vuuren H.J.J., Young R.A.;
RT "A kinase-cyclin pair in the RNA polymerase II holoenzyme.";
RL Nature 374:193-196(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=9845373; DOI=10.1016/s0092-8674(00)81641-4;
RA Holstege F.C.P., Jennings E.G., Wyrick J.J., Lee T.I., Hengartner C.J.,
RA Green M.R., Golub T.R., Lander E.S., Young R.A.;
RT "Dissecting the regulatory circuitry of a eukaryotic genome.";
RL Cell 95:717-728(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SSN8 AND THE RNA POLYMERASE
RP II HOLOENZYME, AND MUTAGENESIS OF ASP-304.
RX PubMed=9702190; DOI=10.1016/s1097-2765(00)80112-4;
RA Hengartner C.J., Myer V.E., Liao S.-M., Wilson C.J., Koh S.S., Young R.A.;
RT "Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-
RT dependent kinases.";
RL Mol. Cell 2:43-53(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-304.
RX PubMed=10360183; DOI=10.1016/s1097-2765(00)80360-3;
RA Hirst M., Kobor M.S., Kuriakose N., Greenblatt J., Sadowski I.;
RT "GAL4 is regulated by the RNA polymerase II holoenzyme-associated cyclin-
RT dependent protein kinase SRB10/CDK8.";
RL Mol. Cell 3:673-678(1999).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-304.
RX PubMed=11331604; DOI=10.1101/gad.867501;
RA Chi Y., Huddleston M.J., Zhang X., Young R.A., Annan R.S., Carr S.A.,
RA Deshaies R.J.;
RT "Negative regulation of Gcn4 and Msn2 transcription factors by Srb10
RT cyclin-dependent kinase.";
RL Genes Dev. 15:1078-1092(2001).
RN [9]
RP INTERACTION WITH MED1 AND MED4, FUNCTION OF THE MEDIATOR COMPLEX, AND
RP INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=11555651; DOI=10.1074/jbc.m105961200;
RA Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.;
RT "The structural and functional organization of the yeast mediator
RT complex.";
RL J. Biol. Chem. 276:42003-42010(2001).
RN [10]
RP FUNCTION, INTERACTION WITH SSN8 AND TUP1, AND MUTAGENESIS OF ASP-304.
RX PubMed=11226276; DOI=10.1073/pnas.041611198;
RA Zaman Z., Ansari A.Z., Koh S.S., Young R., Ptashne M.;
RT "Interaction of a transcriptional repressor with the RNA polymerase II
RT holoenzyme plays a crucial role in repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2550-2554(2001).
RN [11]
RP IDENTIFICATION IN THE SRB8-11 COMPLEX, FUNCTION OF THE SRB8-11 COMPLEX,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-304.
RX PubMed=12200444; DOI=10.1074/jbc.m207195200;
RA Borggrefe T., Davis R., Erdjument-Bromage H., Tempst P., Kornberg R.D.;
RT "A complex of the Srb8, -9, -10, and -11 transcriptional regulatory
RT proteins from yeast.";
RL J. Biol. Chem. 277:44202-44207(2002).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND MUTAGENESIS OF ASP-304.
RX PubMed=12520306; DOI=10.1038/nature01243;
RA Nelson C., Goto S., Lund K., Hung W., Sadowski I.;
RT "Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the
RT transcription factor Ste12.";
RL Nature 421:187-190(2003).
RN [13]
RP NOMENCLATURE.
RX PubMed=15175151; DOI=10.1016/j.molcel.2004.05.011;
RA Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J.,
RA Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M.,
RA Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P.,
RA Fukasawa T., Gustafsson C.M., Han M., He X., Herman P.K., Hinnebusch A.G.,
RA Holmberg S., Holstege F.C.P., Jaehning J.A., Kim Y.-J., Kuras L., Leutz A.,
RA Lis J.T., Meisterernest M., Naeaer A.M., Nasmyth K., Parvin J.D.,
RA Ptashne M., Reinberg D., Ronne H., Sadowski I., Sakurai H., Sipiczki M.,
RA Sternberg P.W., Stillman D.J., Strich R., Struhl K., Svejstrup J.Q.,
RA Tuck S., Winston F., Roeder R.G., Kornberg R.D.;
RT "A unified nomenclature for protein subunits of mediator complexes linking
RT transcriptional regulators to RNA polymerase II.";
RL Mol. Cell 14:553-557(2004).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH RNA POLYMERASE II.
RX PubMed=14749387; DOI=10.1128/mcb.24.4.1721-1735.2004;
RA Liu Y., Kung C., Fishburn J., Ansari A.Z., Shokat K.M., Hahn S.;
RT "Two cyclin-dependent kinases promote RNA polymerase II transcription and
RT formation of the scaffold complex.";
RL Mol. Cell. Biol. 24:1721-1735(2004).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF ASP-304.
RX PubMed=15240822; DOI=10.1091/mbc.e04-05-0412;
RA Green S.R., Johnson A.D.;
RT "Promoter-dependent roles for the Srb10 cyclin-dependent kinase and the
RT Hda1 deacetylase in Tup1-mediated repression in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:4191-4202(2004).
RN [16]
RP TOPOLOGY OF THE MEDIATOR COMPLEX.
RX PubMed=15477388; DOI=10.1093/nar/gkh878;
RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
RT "A high resolution protein interaction map of the yeast Mediator complex.";
RL Nucleic Acids Res. 32:5379-5391(2004).
RN [17]
RP FUNCTION.
RX PubMed=14988503; DOI=10.1073/pnas.0400221101;
RA Hallberg M., Polozkov G.V., Hu G.-Z., Beve J., Gustafsson C.M., Ronne H.,
RA Bjoerklund S.;
RT "Site-specific Srb10-dependent phosphorylation of the yeast Mediator
RT subunit Med2 regulates gene expression from the 2-micrometer plasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3370-3375(2004).
RN [18]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16076843; DOI=10.1074/jbc.m506067200;
RA Nair D., Kim Y., Myers L.C.;
RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription
RT in yeast extracts.";
RL J. Biol. Chem. 280:33739-33748(2005).
RN [19]
RP FUNCTION.
RX PubMed=16109375; DOI=10.1016/j.molcel.2005.06.033;
RA van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P.,
RA van Leenen D., Holstege F.C.P.;
RT "Mediator expression profiling epistasis reveals a signal transduction
RT pathway with antagonistic submodules and highly specific downstream
RT targets.";
RL Mol. Cell 19:511-522(2005).
RN [20]
RP FUNCTION OF THE SRB8-11 COMPLEX.
RX PubMed=15601835; DOI=10.1128/mcb.25.1.114-123.2005;
RA Larschan E., Winston F.;
RT "The Saccharomyces cerevisiae Srb8-Srb11 complex functions with the SAGA
RT complex during Gal4-activated transcription.";
RL Mol. Cell. Biol. 25:114-123(2005).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15687503; DOI=10.1073/pnas.0409671102;
RA Ansari A.Z., Ogirala A., Ptashne M.;
RT "Transcriptional activating regions target attached substrates to a cyclin-
RT dependent kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2346-2349(2005).
RN [22]
RP FUNCTION.
RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
RA van de Peppel J., Werner M., Holstege F.C.P.;
RT "Genome-wide location of the coactivator mediator: binding without
RT activation and transient Cdk8 interaction on DNA.";
RL Mol. Cell 22:179-192(2006).
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 RPB1 at serines 2 and 5. The SSN3/SRB10 and
CC SSN8/SRB11 kinase-cyclin pair may also positively and negatively
CC regulate numerous transcriptional activators in response to changes in
CC nutritional and physiological conditions. Phosphorylates GCN4,
CC promoting its ubiquitin-mediated degradation, and MSN2, promoting its
CC nuclear exclusion. Phosphorylates STE12, thereby promoting its
CC degradation and inhibition of filamentous growth. Phosphorylates GAL4,
CC and this phosphorylation is required for efficient galactose-inducible
CC transcription. Also phosphorylates BDF1 and the TAF2 subunit of the
CC TFIID complex. {ECO:0000269|PubMed:10360183,
CC ECO:0000269|PubMed:11226276, ECO:0000269|PubMed:11331604,
CC ECO:0000269|PubMed:11555651, ECO:0000269|PubMed:12200444,
CC ECO:0000269|PubMed:12520306, ECO:0000269|PubMed:14749387,
CC ECO:0000269|PubMed:14988503, ECO:0000269|PubMed:15240822,
CC ECO:0000269|PubMed:15601835, ECO:0000269|PubMed:15687503,
CC ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16109375,
CC ECO:0000269|PubMed:16630888, ECO:0000269|PubMed:7877695,
CC ECO:0000269|PubMed:9702190, ECO:0000269|PubMed:9845373}.
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 Evidence={ECO:0000269|PubMed:10360183, ECO:0000269|PubMed:11331604,
CC ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:12520306,
CC ECO:0000269|PubMed:14749387, ECO:0000269|PubMed:15687503,
CC ECO:0000269|PubMed:9702190};
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; Evidence={ECO:0000269|PubMed:10360183,
CC ECO:0000269|PubMed:11331604, ECO:0000269|PubMed:12200444,
CC ECO:0000269|PubMed:12520306, ECO:0000269|PubMed:14749387,
CC ECO:0000269|PubMed:15687503, ECO:0000269|PubMed:9702190};
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 Evidence={ECO:0000269|PubMed:10360183, ECO:0000269|PubMed:11331604,
CC ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:12520306,
CC ECO:0000269|PubMed:14749387, ECO:0000269|PubMed:15687503,
CC ECO:0000269|PubMed:9702190};
CC -!- SUBUNIT: Component of the SRB8-11 complex which consists of SRB8,
CC SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates
CC with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin
CC pair also associate with the RNA polymerase II holoenzyme. Interacts
CC with TUP1. {ECO:0000269|PubMed:11226276, ECO:0000269|PubMed:11555651,
CC ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:14749387,
CC ECO:0000269|PubMed:7877695, ECO:0000269|PubMed:9702190}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Protein level and kinase activity are reduced during
CC nitrogen starvation. {ECO:0000269|PubMed:12520306,
CC ECO:0000269|PubMed:9845373}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13785.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L27151; AAA35193.1; -; Genomic_DNA.
DR EMBL; U20222; AAC13785.1; ALT_INIT; Genomic_DNA.
DR EMBL; U44030; AAB68178.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11387.1; -; Genomic_DNA.
DR PIR; S50157; S50157.
DR RefSeq; NP_015283.1; NM_001183856.1.
DR PDB; 7KPV; EM; 3.80 A; A=1-555.
DR PDB; 7KPX; EM; 4.40 A; A=1-555.
DR PDBsum; 7KPV; -.
DR PDBsum; 7KPX; -.
DR AlphaFoldDB; P39073; -.
DR SMR; P39073; -.
DR BioGRID; 36137; 385.
DR ComplexPortal; CPX-1853; CKM complex.
DR DIP; DIP-2574N; -.
DR IntAct; P39073; 25.
DR MINT; P39073; -.
DR STRING; 4932.YPL042C; -.
DR BindingDB; P39073; -.
DR ChEMBL; CHEMBL5395; -.
DR iPTMnet; P39073; -.
DR MaxQB; P39073; -.
DR PaxDb; P39073; -.
DR PRIDE; P39073; -.
DR EnsemblFungi; YPL042C_mRNA; YPL042C; YPL042C.
DR GeneID; 856065; -.
DR KEGG; sce:YPL042C; -.
DR SGD; S000005963; SSN3.
DR VEuPathDB; FungiDB:YPL042C; -.
DR eggNOG; KOG0666; Eukaryota.
DR GeneTree; ENSGT00940000175924; -.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; P39073; -.
DR OMA; VYLHRNW; -.
DR BioCyc; YEAST:G3O-33956-MON; -.
DR BRENDA; 2.7.11.22; 984.
DR BRENDA; 2.7.11.23; 984.
DR PRO; PR:P39073; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P39073; protein.
DR GO; GO:1990508; C:CKM complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0060258; P:negative regulation of filamentous growth; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IMP:SGD.
DR GO; GO:0031648; P:protein destabilization; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Kinase; Magnesium; Meiosis;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Repressor;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..555
FT /note="Meiotic mRNA stability protein kinase SSN3"
FT /id="PRO_0000086784"
FT DOMAIN 75..463
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 100..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 81..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 183
FT /note="K->R: In UME5-4; loss of activity."
FT /evidence="ECO:0000269|PubMed:8164691"
FT MUTAGEN 304
FT /note="D->A: Abrogates kinase activity and transcriptional
FT repression."
FT /evidence="ECO:0000269|PubMed:10360183,
FT ECO:0000269|PubMed:11226276, ECO:0000269|PubMed:11331604,
FT ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:12520306,
FT ECO:0000269|PubMed:15240822, ECO:0000269|PubMed:9702190"
SQ SEQUENCE 555 AA; 62847 MW; C7B6DDC868CCD61E CRC64;
MYNGKDRAQN SYQPMYQRPM QVQGQQQAQS FVGKKNTIGS VHGKAPMLMA NNDVFTIGPY
RARKDRMRVS VLEKYEVIGY IAAGTYGKVY KAKRQINSGT NSANGSSLNG TNAKIPQFDS
TQPKSSSSMD MQANTNALRR NLLKDEGVTP GRIRTTREDV SPHYNSQKQT LIKKPLTVFY
AIKKFKTEKD GVEQLHYTGI SQSACREMAL CRELHNKHLT TLVEIFLERK CVHMVYEYAE
HDLLQIIHFH SHPEKRMIPP RMVRSIMWQL LDGVSYLHQN WVLHRDLKPA NIMVTIDGCV
KIGDLGLARK FHNMLQTLYT GDKVVVTIWY RAPELLLGAR HYTPAVDLWS VGCIFAELIG
LQPIFKGEEA KLDSKKTVPF QVNQLQRILE VLGTPDQKIW PYLEKYPEYD QITKFPKYRD
NLATWYHSAG GRDKHALSLL YHLLNYDPIK RIDAFNALEH KYFTESDIPV SENVFEGLTY
KYPARRIHTN DNDIMNLGSR TKNNTQASGI TAGAAANALG GLGVNRRILA AAAAAAAAVS
GNNASDEPSR KKNRR
