BRE1_DEBHA
ID BRE1_DEBHA Reviewed; 691 AA.
AC Q6BWW6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 112.
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; OrderedLocusNames=DEHA2B07986g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382134; CAG85307.2; -; Genomic_DNA.
DR RefSeq; XP_457303.2; XM_457303.1.
DR AlphaFoldDB; Q6BWW6; -.
DR SMR; Q6BWW6; -.
DR STRING; 4959.XP_457303.2; -.
DR EnsemblFungi; CAG85307; CAG85307; DEHA2B07986g.
DR GeneID; 2913667; -.
DR KEGG; dha:DEHA2B07986g; -.
DR VEuPathDB; FungiDB:DEHA2B07986g; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_1_0_1; -.
DR InParanoid; Q6BWW6; -.
DR OMA; GAIYRQM; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000599; Chromosome B.
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 PANTHER; PTHR23163; PTHR23163; 2.
DR SMART; SM00184; RING; 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..691
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055851"
FT ZN_FING 639..678
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..83
FT /evidence="ECO:0000255"
FT COILED 147..459
FT /evidence="ECO:0000255"
FT COILED 491..620
FT /evidence="ECO:0000255"
FT COMPBIAS 213..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 79669 MW; 9CAC0E8B8AE3B068 CRC64;
MDHDNDKKRL HEDSDNSEIK KHKPLDVLSE DGPLTQKDVV YFKKEAIWRQ MRSYKQKCTL
LTRDLNDIKS NYESNERKIN VLDSWYESII NLFGVKKESN VELNETILIQ LTNVPIGDLD
ALLEKRRAQL LTILSPIIEN SKLSNIDKSD VLEKIEVLNA EVATLKSENN TLSKLKSQFE
SKVEDLQAQL LTLVKDNDRR SSKTLQRIDE SLTNGSDVKE EASETVKSEV NKDTTVKNEN
SVDNEEFERI SSEIEELKSD NRLLKESMNQ INTNYDKVVK ENLQLSDKLE NLNENDLINS
VSYQELAAHN KQLNESVNNL QKINDTTVNK LNELENKQTN VKHLLDKELR EENETLKQQL
QKSENDLVRI RTARDELLSK QTILKADFEN QTTNDELNKL NKVLNERINA LESERHETGD
NSKISELSKD ELIQRINMLN SEIKEIEQAF QETRENSLSK LMSVTDQENM VKKLTIEKTK
ADQKYFASMR LKDSLSSENK ILKTQINKSQ ELVSKLNDLE KSYLDKIEIL TKSNNDFKII
RQSALQENSK LQESLRAIDV RKASLEKELS GMKDKYSDKV QENTSFTQEL NEKNLMMGKL
EHKLKSTESL LKKYKTNNTS SILQEDERQL EALRSIAKCS VCSKNWKDTA ITVCGHVFCS
GCTQERLAAR LRRCPTCNKG FSANDLLSIH L
