SET6_YEAST
ID SET6_YEAST Reviewed; 373 AA.
AC Q12529; D6W3K3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Potential protein lysine methyltransferase SET6;
DE EC=2.1.1.-;
DE AltName: Full=SET domain-containing protein 6;
GN Name=SET6; OrderedLocusNames=YPL165C; ORFNames=P2545;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=14718668; DOI=10.1073/pnas.0307490100;
RA Giaever G., Flaherty P., Kumm J., Proctor M., Nislow C., Jaramillo D.F.,
RA Chu A.M., Jordan M.I., Arkin A.P., Davis R.W.;
RT "Chemogenomic profiling: identifying the functional interactions of small
RT molecules in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:793-798(2004).
CC -!- FUNCTION: Involved in resistance to compounds that target ergosterol
CC biosynthesis, including fenpropimorph, dyclonine, and alverine citrate.
CC Since a deletion in the absence of these compounds does not have an
CC effect on growth, is more likely to be involved in compound
CC availability. {ECO:0000269|PubMed:14718668}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; X96770; CAA65556.1; -; Genomic_DNA.
DR EMBL; Z73522; CAA97872.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11269.1; -; Genomic_DNA.
DR PIR; S65176; S65176.
DR RefSeq; NP_015160.1; NM_001183979.1.
DR AlphaFoldDB; Q12529; -.
DR BioGRID; 36018; 52.
DR IntAct; Q12529; 55.
DR STRING; 4932.YPL165C; -.
DR PaxDb; Q12529; -.
DR PRIDE; Q12529; -.
DR EnsemblFungi; YPL165C_mRNA; YPL165C; YPL165C.
DR GeneID; 855938; -.
DR KEGG; sce:YPL165C; -.
DR SGD; S000006086; SET6.
DR VEuPathDB; FungiDB:YPL165C; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00940000167335; -.
DR HOGENOM; CLU_038964_1_0_1; -.
DR InParanoid; Q12529; -.
DR OMA; FRKEVCH; -.
DR BioCyc; YEAST:G3O-34061-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:Q12529; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12529; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 2.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..373
FT /note="Potential protein lysine methyltransferase SET6"
FT /id="PRO_0000269653"
FT DOMAIN 12..338
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 373 AA; 43750 MW; 15FD75076A063C5D CRC64;
MTIDGDVHEI SPFFQVRQTK WGGRACFSNG NIPKGTTVLQ VSNFTGTSIS YEFRKEVCHN
CFAYANAKTM KYKLNYDYLR DLVCNAHYQI NPKKFLGAGL WFCSEHCRTS YLQIPNIIEL
IECYEILLHH FPSMLKRYNY TSEQEEKLNS ILISENVIQS SWDEIESKWI PRINNMKSAK
RINQLPPTCE DEYCCIRFVC ESLFNLKYMD PQCITYRAFN MLQSNELSKI SKFPVLLHFQ
KLVFQTLYIL LPSHLHRMLS IPLLRHILGT EYGNAFGLWQ EGEASDSREY FGYWVFPEAS
YFNHSCNPNI TKYRKGNSML FTMNRDIKKD EQICIDYSGV LDLPTVKRRA FLADSWFFDC
ACERCKSELQ SVH
