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Database: UniProt
Entry: A0A384JSF8_BOTFB
LinkDB: A0A384JSF8_BOTFB
Original site: A0A384JSF8_BOTFB 
ID   A0A384JSF8_BOTFB        Unreviewed;       353 AA.
AC   A0A384JSF8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   02-APR-2025, entry version 24.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=BCIN_09g01870 {ECO:0000313|EMBL:ATZ53317.1};
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648 {ECO:0000313|EMBL:ATZ53317.1, ECO:0000313|Proteomes:UP000001798};
RN   [1] {ECO:0000313|EMBL:ATZ53317.1, ECO:0000313|Proteomes:UP000001798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10 {ECO:0000313|EMBL:ATZ53317.1,
RC   ECO:0000313|Proteomes:UP000001798};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
RN   [2] {ECO:0000313|EMBL:ATZ53317.1, ECO:0000313|Proteomes:UP000001798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10 {ECO:0000313|EMBL:ATZ53317.1,
RC   ECO:0000313|Proteomes:UP000001798};
RX   PubMed=23104368; DOI=.1128/EC.00164-12;
RA   Staats M., van Kan J.A.;
RT   "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL   Eukaryot. Cell 11:1413-1414(2012).
RN   [3] {ECO:0000313|EMBL:ATZ53317.1, ECO:0000313|Proteomes:UP000001798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10 {ECO:0000313|EMBL:ATZ53317.1,
RC   ECO:0000313|Proteomes:UP000001798};
RX   PubMed=26913498; DOI=.1111/mpp.12384;
RA   Van Kan J.A., Stassen J.H., Mosbach A., Van Der Lee T.A., Faino L.,
RA   Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA   Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT   "A gapless genome sequence of the fungus Botrytis cinerea.";
RL   Mol. Plant Pathol. 18:75-89(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR   EMBL; CP009813; ATZ53317.1; -; Genomic_DNA.
DR   RefSeq; XP_024550743.1; XM_024694950.1.
DR   AlphaFoldDB; A0A384JSF8; -.
DR   EnsemblFungi; Bcin09g01870.1; Bcin09p01870.1; Bcin09g01870.
DR   GeneID; 5430943; -.
DR   VEuPathDB; FungiDB:Bcin09g01870; -.
DR   OrthoDB; 1431934at2759; -.
DR   Proteomes; UP000001798; Chromosome bcin09.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20335; BRcat_RBR; 1.
DR   CDD; cd20336; Rcat_RBR; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001798};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          124..339
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          128..180
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          78..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  39671 MW;  917F115A69287CAC CRC64;
     MSIYDRSSNL PGFFLGRGIS DYRRDVLQQI MKFSEQTRHS RYNKSQMIDC LNELLTTGNI
     SRNKINAIET WLQRGATGSI ADHHNPRKRG SSAPEAPQAT NHTRAIKRPR RSVREEVVEA
     PEPQLKECSI CAEERAFADF PDRITAGCLH DSSCCNTCLS QSIGAQIESI QWDQISCPEC
     PELLSFDNVK SFASEADFAR YDKNALLSYI SNDPKFTNCL GPNCGDGQIH QDGENQPIMT
     CGTCSFKTCF THKIPWHTGL TCGQFDVQNR GAASEQEKKS QRLIKRATKP CPSCNAPILK
     NKGCDHMTCT HCDYEFCWLC LADYETILTT SNAAHRPNCF HYRPDGSGPR YAF
//
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