ID G8JX28_ERECY Unreviewed; 682 AA.
AC G8JX28;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific {ECO:0000256|ARBA:ARBA00018028};
DE EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN OrderedLocusNames=Ecym_8108 {ECO:0000313|EMBL:AET41402.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET41402.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000256|ARBA:ARBA00000317};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP002504; AET41402.1; -; Genomic_DNA.
DR RefSeq; XP_003648219.1; XM_003648171.1.
DR AlphaFoldDB; G8JX28; -.
DR STRING; 931890.G8JX28; -.
DR GeneID; 11469872; -.
DR KEGG; erc:Ecym_8108; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_1_1_1; -.
DR InParanoid; G8JX28; -.
DR OMA; CQEKWIA; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000006790; Chromosome 8.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd19172; SET_SETD2; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR025788; Set2_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006790};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 53..108
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 110..227
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 234..250
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 477..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 516..591
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 79225 MW; 2C393EB53EEA6927 CRC64;
MSTSSSPSNS LPLQGTVGLF LDKEDKTEQA KKTFIELEKS TYAHKRLGNS PSHEFMECDC
FEEYRDGKNH ACGETSDCIN RLTLIECVNE LCTSCGDNCQ NQRFQGRQYA DIAVFQTEKK
GYGVRAEKDI EANEFIYEYI GEVISESEFR ERMVDYDVRG YKHFYFMMLQ TGEFIDATEK
GCLARFCNHS CNPNAYVSKW DVAGKLKMGI FANRKIFKGE EITFDYNVDR YGATAQPCYC
DEPNCIGFLG GKTQTDAASL LPQNYADALG VKPSIEKKWV KMKKAKGEEI DKGDSNNINV
EFVNSLELEP CIKYSDVNKV MSVLLQIDNE FVCSKLLQRL LLTEDETMCY QIIKLHGYKC
FDKLLTMFDD EETQYTILNY LSKLPRTTKN GIISSQIDKK INSLKSNPRL EKIATQLSER
WDTFEIYQRI AKRDPADSSA NGISNVTDFR RIRIPAGQEN HEGGNSVNFT QRQLTRGDQS
NDFHKSNSPN SINSSRSNGT FFDRTKKRPL DPDLYEKRKR RRMEWEKQEL EKKKQEEVRY
LKKKLEIEKQ KKSELQQIIE EANKQKEQEL QERLQKEKEE IERRERRKQT HSVSRSEHKW
NKFFASLVPN LIKSYESGLD RGRIKDCARD IVKILSNKEL KKDPNKVPPS EVTKEKKKKV
KEFCKIYMDK LVLKIHQKPP SK
//