BRE1_CANAL
ID BRE1_CANAL Reviewed; 681 AA.
AC Q5A4X0; A0A1D8PMX1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CAALFM_C500210CA;
GN ORFNames=CaO19.8591, CaO19.976;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017627; AOW29467.1; -; Genomic_DNA.
DR RefSeq; XP_716814.1; XM_711721.1.
DR AlphaFoldDB; Q5A4X0; -.
DR SMR; Q5A4X0; -.
DR STRING; 237561.Q5A4X0; -.
DR PRIDE; Q5A4X0; -.
DR GeneID; 3641568; -.
DR KEGG; cal:CAALFM_C500210CA; -.
DR CGD; CAL0000187022; BRE1.
DR VEuPathDB; FungiDB:C5_00210C_A; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_1_0_1; -.
DR InParanoid; Q5A4X0; -.
DR OMA; DVVYFQK; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5A4X0; -.
DR Proteomes; UP000000559; Chromosome 5.
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:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IMP:CGD.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
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..681
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055848"
FT ZN_FING 629..668
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..77
FT /evidence="ECO:0000255"
FT COILED 136..190
FT /evidence="ECO:0000255"
FT COILED 224..446
FT /evidence="ECO:0000255"
FT COILED 477..628
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 78522 MW; 82E6002053F50C6C CRC64;
MAVDNEKKRS TPDSLNSPHA KKSKPMQELS ESGPLTQADV VYFQKEAIWR QMIQYKQQMM
SMRSELIRLQ RESDASKHIV TVLTAWYEQI LALFDELNSE ETSDLLLAIT KNDDEQLDLI
RKKLSNLISS KVTFDSAKYE KVSGELALLS RQNEQMTEEK RSLGERIDEL ESKITELAKE
HERAQSKTLK RLDSQRHIKT EEDEQSTTKE ENPQPNGHHK ENDKTAVVDS EELDNLKCEL
DKLKTANQLL VQQVEQLTKE NQSLIQKSLN LENKLHNLEE SDLEDNTYYK KIVKNNQSLQ
EQIGKLTKLN SSNVSRLNEL ERQQNDLKSV IEGEIIEENE KLKQQLQESE NNLVRIRTTR
DELLSKNNIL TSQLQDQKTN ESLVELNNVL SKRVESLTEE RLEAIVGTPG TGKLEDLSQQ
ELIHKISQLN NEIKEVELAF KQTREITLKK LTSSIDQENL TKKLTIEKNK ADQKYFSAMR
VKDSLTNENK LLKAQIAKSQ DLIKNLNDLE KKYLNKIDLL SNQLVDFRII KENSLAENSK
LHDELKTLNI AQDALHQEVE RVNAKLESTL KEHTDLQESN KKRELELAKL QKQLQSTENI
LQKYKTNNTN SLLQEDEQQL EALRSIAKCS VCSKNWKDTA ITVCGHVFCS KCTQERLAAR
LRRCPSCNRG FSANDLLSIH L
