BRE1_CRYNJ
ID BRE1_CRYNJ Reviewed; 820 AA.
AC P0CQ62; Q55N50; Q5KBI0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 56.
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=CNI02470;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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; AE017349; AAW45565.1; -; Genomic_DNA.
DR RefSeq; XP_572872.1; XM_572872.1.
DR AlphaFoldDB; P0CQ62; -.
DR SMR; P0CQ62; -.
DR STRING; 5207.AAW45565; -.
DR PaxDb; P0CQ62; -.
DR EnsemblFungi; AAW45565; AAW45565; CNI02470.
DR GeneID; 3259443; -.
DR KEGG; cne:CNI02470; -.
DR VEuPathDB; FungiDB:CNI02470; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_0_0_1; -.
DR InParanoid; P0CQ62; -.
DR OMA; GAIYRQM; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002149; Chromosome 9.
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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR Pfam; PF00097; zf-C3HC4; 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..820
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055850"
FT ZN_FING 767..806
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..92
FT /evidence="ECO:0000255"
FT COILED 164..226
FT /evidence="ECO:0000255"
FT COILED 287..738
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 92837 MW; 2942A566354DEE49 CRC64;
MNADLKRVRE NTLDDSPSPS AKRRLNSNAS SPIQPSDDEG MAEWMKIVEV KRKEAIYRQM
LEYRRISEHE TKRANDLEAQ RRVLEASFHA VELCWTQIVA AVRDLAGAEN LQLKEEEVLE
PLLDPSTPVP ELEKALRSRL PTTRQLVTRF VDLVAHNATR PASEADLQAR CLKLEAEASA
LRSNSKLLES EISALKGSRD EAQRDLQRIR KALDRERMEH GKAQEEWKEE RTRGGQATPN
LRANGSGHST PNGKVEADKK FYSGAGPSMA GVLQDTSELE QLAASRLKQL EQLRFEQTQL
QQEVDRLKIL ANHPSEAALR ESPFFQVYLH QLSTSINRAE SLQTRFTATE SKLDQLRDSN
GEFREAVLAE ARGQTETLRA QMAKKDSDIA RLRGQRDELN SEIMERRAKE VEKCKYTEQI
ENLANSRQER ISFLTSEVRR LKGKLAAAHS SDGYLSFLKE SGIDGDYVKD LEAKVVTSQD
QINALTSQLE RVSSDTAAAK SETEVRTELE SAKRLLARYE RILGPNPEAA EDVRYLSQQL
EKKEKERASL EMKLEEAEAA TNALYSEVEG LSKLWEALDQ TVKSKVLELR DGEQKITRLA
TEKAKADNKY FAAMRAKEAV DMEAKAAQRS VEKQLRLLER AQEVETSLRS QITANEKGLT
ALKNNALDLQ NQLATVVAEK TQLELRLQQS QNALVEAQQI MHQRVAEAIA EKEARAKLQD
EADGQMKIIK KLKERQDAVA AASQTGMSDH EWAITQERDK LLKLLKCSCC EQNFKQQVIV
KCMHTFCKQC LEQRIASRQR KCPACGLAFA KEDIQTLYWQ
