GenomeNet

Database: UniProt
Entry: Q4IB50
LinkDB: Q4IB50
Original site: Q4IB50 
ID   SET2_GIBZE              Reviewed;         921 AA.
AC   Q4IB50; A0A098DW97; A0A0E0SI82; A0A1C3YJN6; I1RNH8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 3.
DT   10-APR-2019, entry version 102.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain-containing protein 2;
GN   Name=SET2; ORFNames=FGRAMPH1_01T18203, FGRRES_16499_M, FGSG_05558;
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: Histone methyltransferase that methylates histone H3 to
CC       form H3K36me. Involved in transcription elongation as well as in
CC       transcription repression (By similarity). {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         Evidence={ECO:0000255|PROSITE-ProRule:PRU00901};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {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
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00901}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ESU11532.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DS231665; ESU11532.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; HG970334; SCB64774.1; -; Genomic_DNA.
DR   RefSeq; XP_011324108.1; XM_011325806.1.
DR   SMR; Q4IB50; -.
DR   STRING; 5518.FGSG_05558P0; -.
DR   PRIDE; Q4IB50; -.
DR   EnsemblFungi; ESU11532; ESU11532; FGSG_05558.
DR   GeneID; 23552737; -.
DR   KEGG; fgr:FGSG_05558; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   InParanoid; Q4IB50; -.
DR   KO; K11423; -.
DR   Proteomes; UP000070720; Chromosome 3.
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:0006354; P:DNA-templated transcription, elongation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 1.10.1740.100; -; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR025788; Hist-Lys_N-MeTrfase_SET2_fun.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
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   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; SSF47676; 1.
DR   SUPFAM; SSF51045; SSF51045; 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   3: Inferred from homology;
KW   Chromosome; Coiled coil; Complete proteome; Methyltransferase;
KW   Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    921       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 specific.
FT                                /FTId=PRO_0000269789.
FT   DOMAIN      120    174       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      176    293       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      300    316       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DOMAIN      564    596       WW. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   COILED      858    894       {ECO:0000255}.
FT   COMPBIAS    842    852       Pro-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00015}.
FT   BINDING     292    292       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   921 AA;  103101 MW;  0E41453F0653E4F7 CRC64;
     MEDDEYTTSK MEEIKLEEGA NDAQVKQETN TPMSITNGDH ESSRSPTASQ DGLKSRSESA
     DTPSSNRPSK LSRKASQKLA ASREPVLFDH LPDMTTESCK FFQRIPDCLY GSKHLGSTDN
     DALDCECRDE WHDGKNLACG EDSDCINRAT KMECSAEGGN CAGGCQNQRF QRKQYANVSV
     IKTEKKGFGL RADSDLQPND FVFEYIGEVI NEPTFRRRMI QYDEEGIKHF YFMSLNKSEF
     VDATKKGNYG RFCNHSCNPN CYVDKWVVGD KLRMGIFTSR KIQSGEELVF NYNVDRYGAD
     PQPCYCGEPN CVGFIGGKTQ TERATKLPAA TVEALGIDGG DGWDTSVAKK PRKKKPDEDD
     EEYVNSIRPR SLSEDDARKV MAALMQCKEK WIAVKLLDRI MQCDEERVIH CVMRMHAYQI
     LKTTLNTFID DHNVVLQVLD ILDKFPRLTR NKVQDSKIEA TIEGLTQSEH EDVASKSKHL
     LNEWSKLEVA YRIRRRKFDP NAPAANSFEE RRGAGREEET VQSTSKTASP TPIDAPKGPR
     NSMPQRNNAF FQNGGRSRRP PFNASLPQGW FTAKDAAGNT YFYTKQGATT WQRPTQPATE
     PAAKAPSKAM KEQLAIQSII NQVTEKGTPK HTSVSTPKAA ETPPKEVKEE KWRSLPVDKR
     MKIYENTLFP HIKHVLDKFH HKLPKEELKR FGKDIAKKLV ASDFKNNRVE DPGAPLSDKQ
     VKKIKQYVKD FLDRAVKKYG EHKRKADEDA DTQMKDDQGP SAAGSGAGSV VDGSDGTALA
     KVDGTSMGEV DVTAVSDREG TGSLGSPDRK RKRDLDTSGS PYVTSTDGPN MKRLREDELE
     APSPPPPPPP PPQSDMDEVV TAEQEALREQ EEALMRENEE AQRLEDEASH TKGLEDVLDA
     SNEISRLNKE ARKPGSQKMP A
//
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