BRE1_NEUCR
ID BRE1_NEUCR Reviewed; 724 AA.
AC Q7S304; U9W5C9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 25-MAY-2022, entry version 114.
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=upl-1; Synonyms=bre1; ORFNames=NCU07544;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; ESA43429.1; -; Genomic_DNA.
DR RefSeq; XP_011393936.1; XM_011395634.1.
DR AlphaFoldDB; Q7S304; -.
DR SMR; Q7S304; -.
DR STRING; 5141.EFNCRP00000007905; -.
DR EnsemblFungi; ESA43429; ESA43429; NCU07544.
DR GeneID; 3875195; -.
DR KEGG; ncr:NCU07544; -.
DR VEuPathDB; FungiDB:NCU07544; -.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; Q7S304; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
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..724
FT /note="E3 ubiquitin-protein ligase bre1"
FT /id="PRO_0000055854"
FT ZN_FING 672..711
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..100
FT /evidence="ECO:0000255"
FT COILED 177..656
FT /evidence="ECO:0000255"
SQ SEQUENCE 724 AA; 82276 MW; 98CA043D25AC8BB7 CRC64;
MPVATSPSAV PRPTTVKMED RKRPAANADD VAPPSKRQAV NGTSKSKDDS NDSREEAWIE
EYQKGAIYRQ MLEYKRSKVD LEHRLQEAEK SAAFHDDHLR VIKYWLSQLT QELELIVEGS
LKSIALKPVD SNWVSSLAFK DSKEFRQHLD DIKKPVILKV ESLLNKLASS RGEVKPDVAQ
LEAQVKSLLA NQKELAVKID RLQAENATLS EQYDTATLKV IKAERKLDRV RSAQVQKLEQ
QALANSTTRQ TTNDENGTSS IAENGDGAEY KTKYKEAIAV ANKQKEQIES LLAEIKTLQE
ENASFKIKKE GISEEDYART DVFKQFKAQN EDLIKRINNL EAVNKQFRED AEKLRAERTS
YRATLEQEAQ ALTSDLEDQI QQKDQDLTRI RSARDELLAE LAMRKASQEQ EKTASAHLNE
LVEAMTDRVT QLESELERLR PTEDVAKAAP TDDLSTLSAE ELREKFAKLE RDYEAINKEL
PALEKSYRKA MGIAHKKVMD FTALEERVAI LTAEKSKADQ KYFAARKDMD IRIAEIRTLR
GQNSKSSEII SQLKDVETQH RALITTLEKQ IADLKQSNIT IVTESKKLES LSSEATRRAD
SVKSQIENLQ NLVKSKDTAG RELKEKAIDK EQEAEKLKVR LDKVSSERDK WKTKCQSNST
EEEEMLRNLV LCSVCRSNFK NTILKGCGHV FCNECVDNRL ANRMRKCPSC NKAFDRSDAM
PAHL
