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Database: UniProt
Entry: A0A0D3C7Y9_BRAOL
LinkDB: A0A0D3C7Y9_BRAOL
Original site: A0A0D3C7Y9_BRAOL 
ID   A0A0D3C7Y9_BRAOL        Unreviewed;       518 AA.
AC   A0A0D3C7Y9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   18-JUN-2025, entry version 43.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g007070.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo5g007070.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|EnsemblPlants:Bo5g007070.1,
RC   ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo5g007070.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC       complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC       enzymes and then transfers it to substrates.
CC       {ECO:0000256|ARBA:ARBA00003976}.
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};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   RefSeq; XP_013586033.1; XM_013730579.1.
DR   AlphaFoldDB; A0A0D3C7Y9; -.
DR   STRING; 109376.A0A0D3C7Y9; -.
DR   EnsemblPlants; Bo5g007070.1; Bo5g007070.1; Bo5g007070.
DR   GeneID; 106294886; -.
DR   Gramene; Bo5g007070.1; Bo5g007070.1; Bo5g007070.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_009823_3_1_1; -.
DR   OMA; THDEYEE; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000032141; Chromosome C5.
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:0071456; P:cellular response to hypoxia; IEA:EnsemblPlants.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010224; P:response to UV-B; IEA:EnsemblPlants.
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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
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          115..327
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          119..170
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          496..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  60395 MW;  C8812C01AFDF49DB CRC64;
     MDDSDIKRLG EILITAEEEE ELNTPDEHDH TETSTHQSYV TILKEGDIRS RMKEEIQRVS
     NTYSISKDDA TLLLAHFRWD DIELHKNWSD NAKTVRESVG IFELERPLDL PSDDKNFYCG
     ICFKIHSLER SASVSCGHRV CKFCWRSHIN KRIKEIADVD WYGTLKCPYC PASFGWDMIE
     SFACQEEKTK YYRYLFRSYV EGSKVIKCCP AKGRSCDVHL TPGSGNFDVL CLCLLSFCWN
     CSQDTHSPMD CESAAKWLRM NSSDYQDPNW VRENTVPCPR CKLRIRENQD WSLKMRCFPP
     CNYDFCWRCR GQWTEHGLDL YTCTHDEYEE TVFGNMAEYA AGRYKDCHEK WMSNESLMQK
     AKAKLQQLHT DVIPDLSNKQ LATVQQLEFI AEAWSQIMEC RRVLKWTYAY EYYLGEDQVE
     KQAFLKLKQD NAEIPLEKLN YLAENQLNML LDSDGPSENF NRFRSDLTDS TRITRNHYEL
     LVRDLEDGLS NVVGASTSQR ARNEDDASGS SSIHDDLF
//
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