BRE1_CANGA
ID BRE1_CANGA Reviewed; 693 AA.
AC Q6FWF3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=CAGL0D00638g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380950; CAG58352.1; -; Genomic_DNA.
DR RefSeq; XP_445441.1; XM_445441.1.
DR AlphaFoldDB; Q6FWF3; -.
DR SMR; Q6FWF3; -.
DR STRING; 5478.XP_445441.1; -.
DR EnsemblFungi; CAG58352; CAG58352; CAGL0D00638g.
DR GeneID; 2887150; -.
DR KEGG; cgr:CAGL0D00638g; -.
DR CGD; CAL0128055; CAGL0D00638g.
DR VEuPathDB; FungiDB:CAGL0D00638g; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_1_0_1; -.
DR InParanoid; Q6FWF3; -.
DR OMA; GAIYRQM; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002428; Chromosome D.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0010390; P:histone monoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:EnsemblFungi.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
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..693
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055849"
FT ZN_FING 641..680
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..166
FT /evidence="ECO:0000255"
FT COILED 251..384
FT /evidence="ECO:0000255"
FT COILED 483..609
FT /evidence="ECO:0000255"
FT COMPBIAS 196..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 79771 MW; 438ADBCFDA920CDB CRC64;
MSSEEPPIKK QKLELSDPDE PLTQHDVISF QKEALFRCLN SKRVELEALT KQYSTVHDKW
EQNVHTLATL MSVLSTAASH LRGLCNEESE KTLCDEMINA GESVDKERTD EFLNLLRKYT
NSNGSSDSKI DSLGLELQRA NKTKSELRLQ NKKLTDEIDS LKAYYHGLVR SYDREDSMTV
KRVFNKQKTD DNTDNISNTE QRPTSVSPVL TNGATHVKNE VKTEQEALNN HTDSSQSSGI
TEEEKKKLFL QYENKITDLE SHNSSLNRII EELENYKQLN EKELAQTRLE ISNLLSEKHS
NEEEREDLLH QIEKLKASNT DLTLTNESFL SKFQELAKEK DTFQEKISSD FEKTLESLKA
QNLALEKDLV RVRTTRDELI SKVAILEAET SKSVLISDLK QALDILRDQW EKIEFRNNQS
PSSDALLKEI QDLESAFKEL SSLTHKKYSE YLNHESVISK LTIEKTKADQ KYFASMRSKD
SILVENKNLS KSLNKANELI LQLKDTDKLY KQKIESLHKQ LALSQNNEKR LVDSNKAANL
KVMNLNSEIQ KQKKLLDFTS SQKNELINEL TEANGMLKSK ELEIEFKENE LQTALKKNEK
LEEFLSKENY NMNKPSSLAT TNLDEDSMAE ELENFRTLVY CSLCSKNWKN MAIRTCGHVF
CEDCCKERLA ARMRKCPTCN KPFSSNDLLM VHL
