ID   BRE1_ASPOR              Reviewed;         760 AA.
AC   Q2U9B0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=AO090701000102;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007164; BAE61855.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U9B0; -.
DR   SMR; Q2U9B0; -.
DR   STRING; 510516.Q2U9B0; -.
DR   PRIDE; Q2U9B0; -.
DR   EnsemblFungi; BAE61855; BAE61855; AO090701000102.
DR   HOGENOM; CLU_019713_2_0_1; -.
DR   OMA; GAIYRQM; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006564; Chromosome 5.
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..760
FT                   /note="E3 ubiquitin-protein ligase bre1"
FT                   /id="PRO_0000245302"
FT   ZN_FING         708..747
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          210..263
FT                   /evidence="ECO:0000255"
FT   COILED          309..561
FT                   /evidence="ECO:0000255"
FT   COILED          594..691
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        33..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  85245 MW;  26293372FE2C8FDD CRC64;
     MPVAEASPVA SSEPGFVKME DRKRAATSDH NDSAPPLKKQ ATSVNGGSKP HPDADMPWKD
     DLEVSLGLAG VVGFMSFQGG LRYPSSAEPT TSLTIKDAIW RQMQEYKREK VSLEAKLKDM
     SKAATRHNEH LRVIDTWYNQ VCGSTLIDEV KLLLGAAEDI KGDRPTFQSS LSFDDVDNFE
     KHLKSRSNDI RDIISRLVKN TPKSPPEICE LQSQLAKKLA EEKATIAELD KALSEKQQLE
     ESLEEASLRY MVAEKKLDRA RSLTVAKLEK QYILGPQRPG GDSASGQREE QSVSNGATPS
     AERGPELDEA HNKLVAISEK QKEQLQKLET ENANLLSQIT DLNIKRSKLT DDDYAHTDLF
     KQMRSQYDDV VKRINHLEAT NVQLREEAVK LRSERTAYRN QVDEETQNVI AEKEAQLIRA
     ETDLARIRNA RDELLADQQM RKAAQEQEKT AVLKVQELAE ARNAQIASLE SEVERLRLQV
     ENAKATQADS SDIPVEELRG KYQVLERQYA MLNTELTSMQ TACKKYSTLA SQKVTDFSAL
     EEKMARLTAE KSKADQKYFA AMKSKEARDL EVRTLRMQNS KSSDIVSQLK ESEAATRSLL
     ANMEKQVSET KEALNSMMNK HHATQQQLAE NGIVIEGLKG QINELKTLST SKDATLASTS
     SACRQAETEI EGLKATLADT KKSLDNWKNK SLGNSSSEYE MLRTLALCTV CRRNFKNTAI
     KTCGHVFCKD CVEERLTSRS RKCPNCNRSF GNNDYMHITL