ID   BRE1_USTMA              Reviewed;         817 AA.
AC   Q4P3X7; A0A0D1E1X2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
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; ORFNames=UMAG_05186;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003143; KIS70114.1; -; Genomic_DNA.
DR   RefSeq; XP_011388235.1; XM_011389933.1.
DR   AlphaFoldDB; Q4P3X7; -.
DR   SMR; Q4P3X7; -.
DR   STRING; 5270.UM05186P0; -.
DR   EnsemblFungi; KIS70114; KIS70114; UMAG_05186.
DR   GeneID; 23565145; -.
DR   KEGG; uma:UMAG_05186; -.
DR   VEuPathDB; FungiDB:UMAG_05186; -.
DR   eggNOG; KOG0978; Eukaryota.
DR   HOGENOM; CLU_019713_0_0_1; -.
DR   InParanoid; Q4P3X7; -.
DR   OMA; GAIYRQM; -.
DR   OrthoDB; 782448at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000561; Chromosome 4.
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   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..817
FT                   /note="E3 ubiquitin-protein ligase BRE1"
FT                   /id="PRO_0000245303"
FT   ZN_FING         764..803
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          160..222
FT                   /evidence="ECO:0000255"
FT   COILED          265..505
FT                   /evidence="ECO:0000255"
FT   COILED          532..579
FT                   /evidence="ECO:0000255"
FT   COILED          658..739
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        13..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  91239 MW;  4824D49A29B026D9 CRC64;
     MLQSMSGADD RKRALTGTVE DGPRKRLHSD EATSKSAATP TNDNEDDEAL HPAYAGLEAF
     RKEAIYRKLL EARRDLQRIE RRAGTFQDDL AVSEQRAAVL QRFWNLLLTE LAARLAIQDQ
     DVFALSSASD SRSDLTAMEQ QLEQQSSAVL RCLSQQGDVN IVELQQKLHD LADEGSRYKQ
     DLFLTQSKLQ RAQDALAQTS QKLSKVEHEY VRYQSNLLRA TEGKPTIPAG TIVSASEPAP
     ATEQTADTAV KKETATLAPT DGAPHTSETL QKAVDELESA RQDVELTRRE SDSRYAEIQT
     LNEEVRTLKC KLHETQTKLT TLPEEVLLSS ALYRELQTLL RNAQQDLQSS KEAMQALETE
     ATALREDRAA FQQTVEAEAA SRSEDLEKLI KAKEADVTRL RSQRDELNAE LTERRSREQV
     KFTQIEEMKA LLNSKEERLI LLSSQVRRLR MAVAAFHGQS AGVSALATAE SEEDQFEQVS
     RAAQQAQARV AELEQRLGVA GQNASPNGTG ATAKTEKGAD VDTKAEKSVE AASESELQGE
     IQRLRLSLQA AEASSKAVDD ELEKISAAYA DLERQASVKV TDVSRMEEKA LRWVTEKSKA
     DNKYFSAMRA KDAVDAELRT AKQVHERQQK TIEAFADVER NYVVQSGLHE KAISTFKKVT
     DAQTHRIETL QRELELAESR LTELARVKEV ASDSAKELIN TANLEKDQRK RAEERIVRLE
     KDLESSKRQL AKAAASAAKN KGRRDADAGD GASEKDFLNA LLQCSSCKER YRNRILTKCY
     HTFCSECIDS RVQTRQRKCP HCALAFAVSD VQPLYLQ