ID A0A2H3THT3_FUSOX Unreviewed; 919 AA.
AC A0A2H3THT3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=FRV6_12339 {ECO:0000313|EMBL:SCO88212.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO88212.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) 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:0000256|ARBA:ARBA00003901}.
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; FMJY01000007; SCO88212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3THT3; -.
DR VEuPathDB; FungiDB:FOC1_g10008739; -.
DR VEuPathDB; FungiDB:FOC4_g10008600; -.
DR VEuPathDB; FungiDB:FOIG_05113; -.
DR VEuPathDB; FungiDB:FOMG_08159; -.
DR VEuPathDB; FungiDB:FOXG_09334; -.
DR VEuPathDB; FungiDB:FOZG_12626; -.
DR VEuPathDB; FungiDB:HZS61_017366; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 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 InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_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; PF08711; Med26; 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 SMART; SM00456; WW; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF51045; WW 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.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SCO88212.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCO88212.1}.
FT DOMAIN 110..164
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 166..283
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 290..306
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 553..585
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 102306 MW; D33CD853DCB7970F CRC64;
MEEIKLEEGT NGAQVKQEER TPMSVTNGGQ EESRSPSASH DGVKSRSGSA DTPSSNRPSK
LSRKASQKLA ASREPVLFDH LPDMTAESCN FFQLIPDCLY GSKHLGSTDN DALDCECREE
WHDGENIACG EDSDCINRAT KMECSAEAGN CAGGCQNQRF QRKQYANVSV IKTEKKGFGL
RADSDLQAND FVFEYIGEVI NEPTFRRRMM QYDEEGIKHF YFMSLNKSEF VDATKKGNYG
RFCNHSCNPN CYVDKWVVGD KLRMGIFASR KIQSGEELVF NYNVDRYGAD PQPCYCGEAN
CVGFIGGKTQ TERATKLPIA TVEALGIDGG DGWDTSVAKK PRKKKPDEDD EEYVNSIPSR
SLNEDDARKV MAALMQCKEK WIAVKLLDRI LRCDEERVIH CVMRMHAYQI LKTTLNTFIE
DHNVVLQVLD ILDKFPRLTR NKIQDSKIEA TIEGLTRSEH EDVASKSKYL LDEWSKLEVA
YRIRRRKFDP NAPTANSFEE RRGAGRDEEV AQSSKTASPQ TIDAPKGPRN SMPQRNVAFF
QNGGRPRRPP FNGGLPQGWF TAKDAAGNTY FYNKQGATTW QRPTQPVAES AVKAPSKAMK
EQLAIQSIIN QVTEKGTPKH TSVSTPKTAD TPPKEVKEEK WRSLPVEKQM KIYENTVFPH
IKHVLDKFHH KLPKEELKRF GKEIAKKLVS SDYKNNRVGD PNAPLSEKQA RKMKQYVKDF
LDRAVKKFGD QQKPRAGENA DTQMKGDQGP SAAGSSTGSV AGGLEGTSLV KVNGTPADGL
DAATASDNEG SGSLGSPERK RKRESEVEGP LSISPSDGPN MKRLREDELD APSPPPPPPP
PPQSAMEGVV NAEQQALREQ EEALMRENEE AQRLEDEANH TKDLEDATRG AEKDLLDASN
ELSRLNHEAR GIGSQKTSA
//
