SET1_GIBZE
ID SET1_GIBZE Reviewed; 1263 AA.
AC Q4I5R3; A0A0E0SH65; I1RTE2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9Y7R4};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=SET1; ORFNames=FGRRES_16832, FGSG_07445;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC specifically mono-, di- and trimethylates histone H3 to form
CC H3K4me1/2/3, which subsequently plays a role in telomere length
CC maintenance and transcription elongation regulation.
CC {ECO:0000250|UniProtKB:Q9Y7R4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9Y7R4};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESU13710.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231666; ESU13710.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970335; CEF85778.1; -; Genomic_DNA.
DR RefSeq; XP_011327217.1; XM_011328915.1.
DR AlphaFoldDB; Q4I5R3; -.
DR SMR; Q4I5R3; -.
DR STRING; 5518.FGSG_07445P0; -.
DR EnsemblFungi; ESU13710; ESU13710; FGSG_07445.
DR GeneID; 23554522; -.
DR KEGG; fgr:FGSG_07445; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G24837; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_0_0_1; -.
DR InParanoid; Q4I5R3; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IEA:InterPro.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1263
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269774"
FT DOMAIN 1121..1238
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1247..1263
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 72..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 1263 AA; 140732 MW; 23A313333318DD86 CRC64;
MTRPPGASFA EFFPTAPKVK AQAQTRADQV RDRDRFKTAS TPATINGTID STTGTAVLEA
DANVSLNGIV SASDTMPTQP DDTESPFTDI PNTVDSASSY SSAASSIFST STRHGAAATT
ASSRLPTSSL TPSAFKESPN SAPAAAKPDM STYQTSDRAA RQSSRNSPAT GPNVSISNGL
PSNERIPARD PLPSVKGLRC TYDPLLDRVH NKSVSKSAKP TYEEFGREDD APPPKDPRLA
RSDGRLGYIN TDYYLPKSRL RTAPENIKPY PYDPKTSIGP GPPTQIVVTR YNPLIPFSKV
TAIFASFGEI AESSNKMHPE TGSYLGFATI RYRDSKRPDR PPVSGIDAAR RAVRARGIKV
DADIVRVEYD AEGRRSRRML EEHLKREKEK FEKIEQERLA LAAKAPPTGP KSGTAPAFTR
PPPTAPKGPS AQRQSIPTGT PQIPLLGTQV QGLNLEPSNL AQKLADDPYI YVTGDSVPVL
PSILPHMKKR LKSYGFEEIR VDKSGYFIVF RNSFTGSSEA ERCFRAVNHT EFFNYDMTMQ
LCLPRPRRED GSGRRRSSAS SDRHTHAEPR YRDEKDRRRR EEEADLEEEK KQRAKNFDPV
IEAVEVVRRE MMEHLIRHIR TKVAAPALSD FLDPANHAAK RRKLNIEHPD DLQEIPSIED
GNDSSRVGTP NSRADPIERR TGRLEPKALP RIRKTKVKGQ AQKSAFVDPF ARKRPPVARN
AFRSLHHRLR SLDSDAESDD DTDTRALLAR ETEEADSRPR SRMSTDDEAS KDDFVPWEQG
EDDSMTEASF AIADTASTRK RKLVASLESV FKRQKKSDEE LFGVNLETLD SEFKGREDSV
DIIPEPETGD DVESRVSRSE TPASAIGKPL KKRPGKRKKT KKASFEEPEA AKTQPETEQQ
PGDEATEPSK VKQEKAEKTS MEELVPEKFD EKLFATEPLT PALELPEGAK PDLPIFQGLT
VSAQDIPDLA KLARRFNTKD IGNAELWLWT RNRIRELNSA RRTLDSPVTI GGYYVPNPTG
CARTEGVKKI LNSEKSKYLP HHIKVQKARQ EREARNKLGR DAAAEAADAA RIAAEKLVAK
GNSRANRATN RRYVADLNDQ KKTLGQDSDV FKFNQLKKRK KPVKFARSAI HNWGLYAMEN
IAKDDMIIEY VGEQVRQQIS EIRENRYLKS GIGSSYLFRI DDNTVIDATK KGGIARFINH
SCMPNCTAKI IKVEGSKRIV IYALRDIALN EELTYDYKFE REIGSTDRIP CLCGTAACKG
FLN
