BRE1_GIBZE
ID BRE1_GIBZE Reviewed; 703 AA.
AC Q4I7N9; A0A0E0SCG0; V6RER5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q07457};
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1 {ECO:0000305};
GN Name=BRE1; ORFNames=FGRRES_06769, FGSG_06769;
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: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for
CC epigenetic transcriptional activation and is also a prerequisite for
CC H3K4me and H3K79me formation. {ECO:0000250|UniProtKB:Q07457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q07457};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07457}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; DS231666; ESU12911.1; -; Genomic_DNA.
DR EMBL; HG970335; CEF84123.1; -; Genomic_DNA.
DR RefSeq; XP_011326418.1; XM_011328116.1.
DR AlphaFoldDB; Q4I7N9; -.
DR SMR; Q4I7N9; -.
DR STRING; 5518.FGSG_06769P0; -.
DR PRIDE; Q4I7N9; -.
DR EnsemblFungi; ESU12911; ESU12911; FGSG_06769.
DR GeneID; 23553884; -.
DR KEGG; fgr:FGSG_06769; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G23141; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; Q4I7N9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010390; P:histone monoubiquitination; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..703
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055852"
FT ZN_FING 651..690
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..75
FT /evidence="ECO:0000255"
FT COILED 170..459
FT /evidence="ECO:0000255"
FT COILED 512..569
FT /evidence="ECO:0000255"
FT COILED 603..635
FT /evidence="ECO:0000255"
FT COMPBIAS 216..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 80210 MW; 1F76A11C045ADDE4 CRC64;
MEDRKRPAIS SADEIAPPSK RVAVNGSKAK DDPLDMKEES WVEAYTKGAI YRQMQEYSRK
ASTYESRLEE LHKRSVHHDD HLRIIDAWWR QVLDEMELLL ADSGVTSQTP SEPPYLSSVS
FKDLHDFQKH LSEKGKGIKL RAEAILARLA SSRGSIKPDA AKLESKVAGL LAAQKEYFAK
LDRLKTEKDQ LSEQLNAATL RYFKAEKKLD RAKSSQVQKM EQQAFANATR PSASGDVNTD
SGETNGNSGE LLLKYEEATA AATKQKEQLD VFLAEIKALQ DENSTLKAKR DTLTDEDFIR
TDVFKQFKNQ NEDLIKRINT LEATNKQLRE EAERLQAERT AFRTMLEADA NQVTQELESE
IILRDQDLAR VRSARDELLA ETTQHKARLD QERASVEQVK ALASAKEDRI TALESQLSRL
QQSETQQAVS PDIEALTVEE LRLKYTKLQQ DFDSINMELP AIEKAYKKMK ELAHRKAMDF
SATEERMSIL IAEKSKADQK YFAARKDADT RNNEIRSLRH QNSKSSEIIA QLKDLESQNR
VLLGNLEKQL TDLKQSNASL MTENKKMEVT SLDAVRRTES LNKQVSDLSN LVKSKDAASA
VVRERNVMQE TEVEKMKVRL EHAQKDRDNW KNKALSNSSE EEEMLRTFAL CTICRNNFKN
TALKTCGHLF CNQCVDDRIS NRMRKCPTCS RAFDKMDVMP VHH
