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Database: UniProt
Entry: Q4I5R3
LinkDB: Q4I5R3
Original site: Q4I5R3 
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   10-APR-2019, entry version 105.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.43;
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 PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
OS   (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   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=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
RA   Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
RA   Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
RA   Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
RA   Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
RA   Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
RA   Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
RA   Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
RA   Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
RA   Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
RA   Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
RA   Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
RA   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=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
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
RT   Fusarium 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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ESU13710.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   SMR; Q4I5R3; -.
DR   STRING; 5518.FGSG_07445P0; -.
DR   PRIDE; Q4I5R3; -.
DR   EnsemblFungi; ESU13710; ESU13710; FGSG_07445.
DR   GeneID; 23554522; -.
DR   KEGG; fgr:FGSG_07445; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   InParanoid; Q4I5R3; -.
DR   KO; K11422; -.
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:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
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; IPR017111; Set1.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF462; PTHR22884:SF462; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF11767; SET_assoc; 1.
DR   PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 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; Complete proteome; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1263       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269774.
FT   DOMAIN     1121   1238       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1247   1263       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   BINDING    1237   1237       S-adenosyl-L-methionine.
FT                                {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
//
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