BRE1_YARLI
ID BRE1_YARLI Reviewed; 700 AA.
AC Q6CF78;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=YALI0B09559g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG82928.1; -; Genomic_DNA.
DR RefSeq; XP_500684.1; XM_500684.1.
DR AlphaFoldDB; Q6CF78; -.
DR SMR; Q6CF78; -.
DR STRING; 4952.CAG82928; -.
DR PRIDE; Q6CF78; -.
DR EnsemblFungi; CAG82928; CAG82928; YALI0_B09559g.
DR GeneID; 2906810; -.
DR KEGG; yli:YALI0B09559g; -.
DR VEuPathDB; FungiDB:YALI0_B09559g; -.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; Q6CF78; -.
DR OMA; GAIYRQM; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001300; Chromosome B.
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; IPR013087; Znf_C2H2_type.
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..700
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055856"
FT ZN_FING 648..687
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 39..78
FT /evidence="ECO:0000255"
FT COILED 178..383
FT /evidence="ECO:0000255"
SQ SEQUENCE 700 AA; 78824 MW; 289AC9C886B4138B CRC64;
MEDKRNAESA SLGASSGGDS KRARVAARPV SLEDVAEFQK EAIFRAMETY RREKETLEKQ
LETQGEKERE LEERVVRLGT WWDKVADRLA LVVGKYEFEK SKVKTEDVKK EEDTERDAGD
EDEVEVAPGP TGLATDLELE EKSASISSHF STLLDLIGDK ISKQDKTEVS RLSAGYTDMA
EQRHLLVRKI QDLEHEAQTM KNQYLAAAKK LDRYKSPTVK LIEGEDVEEK AEENGDQKTA
QMEEKKETED SPDTKDTGDT KALRETIQVQ EEQMKELDAK IAALEHEASL FNAKMADLSE
SDLLDHSGAF KAAKEQLSDK TGQILALEKS RDAISAEKMA LDENRQQYRS TIKREFEKRE
SELRSQLSRA ETDLVRIRTA RDEILADLSQ KKATEADKLK TIESLKELGE VYKLRIGTLE
SEVQRWRKEG NEGVNMSSNV EGKSLEELKK EVTVLTLTNQ SLMAEIPGME AAFVSAQKMA
ENKALDVADR ESRLTKLLAE KAKADEKYFA AMRHKDALGA ENAKLKAQMV KSSELVNQLQ
EVDAKTRAKI DVLEKTLSEY VSLHAKQQEA AKRLTSQVAE KTHMLNGAQK YLTTLKEEMK
QQGTKLSVGE HRARKLALDN AKLTKQIELS SFGGSSDEID ELRSIAMCSL CSKNWKDTAL
KVCGHVFCHQ CAQDRLDARL RKCPNCNKPF SQNDLLTVHL
