SET2_USTMA
ID SET2_USTMA Reviewed; 972 AA.
AC Q4PBL3; A0A0D1CU33;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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; ORFNames=UMAG_02500;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003144; KIS69988.1; -; Genomic_DNA.
DR RefSeq; XP_011388777.1; XM_011390475.1.
DR AlphaFoldDB; Q4PBL3; -.
DR SMR; Q4PBL3; -.
DR STRING; 5270.UM02500P0; -.
DR PRIDE; Q4PBL3; -.
DR EnsemblFungi; KIS69988; KIS69988; UMAG_02500.
DR GeneID; 23563234; -.
DR KEGG; uma:UMAG_02500; -.
DR VEuPathDB; FungiDB:UMAG_02500; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_1_0_1; -.
DR InParanoid; Q4PBL3; -.
DR OMA; MTSIECT; -.
DR OrthoDB; 453286at2759; -.
DR Proteomes; UP000000561; Chromosome 5.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd19172; SET_SETD2; 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 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; 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.
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..972
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000269793"
FT DOMAIN 191..244
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 246..363
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 370..386
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 25..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..806
FT /evidence="ECO:0000255"
FT COMPBIAS 55..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 107431 MW; 7A128A157E625DB6 CRC64;
MDWDHNVTFS AVRSLQATTA VAQATDNVVD LDRNRVDSRP GVLPTKNESS PHSSASLPPP
SPHPPPPPAF TPSPSPSPSP SPQTATARSS VTDAAPAPKR SPRSPLHSNG SFPPVSDPIS
SIDSRDALDI DHESTAMLAS SSSARKSKPK LQPQLINHLP LAQQAAMATF HEITFNDYHD
KKLGRPPGKF DDYMICDCTP NSGNLDMACT DYSGCINRMT QIECSASKCR WGKQCRNQRF
HRRQYVDVDI VQTEKKGFGL RACQDIPKET FIYEYVGEVM NQTTFLQRMQ QYRIEGIRHF
YFMMLQPNEY LDATKKGGKG RFINHSCNPN CAVSKWQVGK HLRMGIFAKR NIQKGEELTF
NYNVDRYGND AQECFCGEPN CVGTLGGKTQ TDLSGMDDLF LDALGISDEV EQTEAKGSRR
KRGKRLDLDF IPQMRAIQEH EATRVMTAAR QAGPKREILE KLLRRMEMTT DVNVQKSLVK
LHGFILMQFL LEQWWNDRDI VILIINVLAR WPLIARNKVI DCGVEDQVRI LAQTYRPRSP
EDQKPSLDAL RQVKQDDSAA DRNDYTQVQP TLAPVRIGAP PAPDAEVSAR AEHLLEAWKK
LDMTYRIARK DALKPDADDH KDATAVTTWI DRRRMQDLDD PLDLEHAQAP NAVSSELGNA
LSGDQELREI KPSWQPPPAP PSMPNAPAKR MGGAVHHRSP PGSFTPTRLQ SSGQSPLTPD
QVTSVLSSSL VKSLSGLVSS LKQQGIQLQQ QQQQQPPAQQ QPSAQPAAPS AKSIEDIIRE
ANEQEERARK EAEAAAKAAR ELEVNGGQTS GSSRKRPSSA SRHSDKRAKH SSLSSSSQAA
SKLISSNGSA ADSTSKAGSV ESVAANERRL RKLVGELVVR QMSKYKDDLE RESFKRHAKE
LTNAIVGKEM RNPKSWPPAR GALTELSLDK RAKIKAFAKE YIDKLLARKG KGKGSSTPSN
NEGAGSSNNG IV
