SET2_DEBHA
ID SET2_DEBHA Reviewed; 731 AA.
AC Q6BM04;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE EC=2.1.1.359 {ECO:0000250|UniProtKB:P46995};
DE AltName: Full=SET domain-containing protein 2;
GN Name=SET2; OrderedLocusNames=DEHA2F09350g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys-
CC 36' forming H3K36me3. Involved in transcription elongation as well as
CC in transcription repression. {ECO:0000250|UniProtKB:P46995}.
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:0000250|UniProtKB:P46995, ECO:0000255|PROSITE-
CC ProRule:PRU00901};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: The AWS and SET domains are necessary for transcription
CC repression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00901}.
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DR EMBL; CR382138; CAG89108.2; -; Genomic_DNA.
DR RefSeq; XP_460767.2; XM_460767.1.
DR AlphaFoldDB; Q6BM04; -.
DR SMR; Q6BM04; -.
DR STRING; 4959.XP_460767.2; -.
DR PRIDE; Q6BM04; -.
DR EnsemblFungi; CAG89108; CAG89108; DEHA2F09350g.
DR GeneID; 2903609; -.
DR KEGG; dha:DEHA2F09350g; -.
DR VEuPathDB; FungiDB:DEHA2F09350g; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_1_1_1; -.
DR InParanoid; Q6BM04; -.
DR OMA; CQEKWIA; -.
DR OrthoDB; 453286at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IEA:InterPro.
DR GO; GO:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.1740.100; -; 1.
DR Gene3D; 2.170.270.10; -; 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 InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF82199; SSF82199; 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.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Chromosome; Coiled coil; Methyltransferase; Nucleus; Reference proteome;
KW Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..731
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000269787"
FT DOMAIN 52..108
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 110..227
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 234..250
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 477..511
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 436..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 539..618
FT /evidence="ECO:0000255"
FT COMPBIAS 438..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 84410 MW; 05C22BD4D8ACD30C CRC64;
MSDMEELDVK AKQYTPQLFL ESEDKTDEAR STFNELQECT YSSKSTGSSG QHEHMTCDCY
EDWDSDKQQN MACGEDSDCI NRVTSVECSN KFCTCGNDCQ NQRFQKKQYA NVTVIQTELK
GYGLRANEDI SESSFIYEYI GEVIDEESFR KRMIDYDTKK LIHFYFMMLK KDSFIDATMK
GSLARFCNHS CNPNAYVDKW VVGEKLRMGI FSKRNIQKGE EITFDYNVDR YGAQSQPCYC
GEPNCIKWMG GKTQTDAALL LPDGISEALG VTHKQERQWL KENKHLRSKQ QSDESIINEA
FVKSIEVSAL TESDVSKVMG ALMRVQDLNI TQKLIERIYL TSDDSINSSI IRVHGYKTLS
QTIKAFKDED KELISKILII LAKWPKVTRN KISSSQIEDV VKDINTNSND DNLKKLSSDL
LAEWGKLQMA YRIPKNIGND KESNSPALYG RNARSRSRSR SPDRGKSAEP QHVETDEALP
DGWQTAFDPN TQTNYYYHAE LGISKWERPI KEVPKGPKGP KALPVSEPIQ RPNSNSNGRS
YNEEELTRRE EERLKREKEE QFKEIQQKER LLQELILQSQ KELEEKKSFE EKMKLEKLEK
EKERQALKRK KLKKSKSSIP PAPPVPIDGQ WTKTFAKHVP NFLKKYEAEI GRDNIKGCAK
ELVKTLVAKE MKKNPDTKPP KELDNAKLKK IKEYSKMFMD KFLIKYRSKH DKKRSHNEEN
GGTKRVKPDV E
