ID A0A8X7TH09_BRACI Unreviewed; 892 AA.
AC A0A8X7TH09;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=Bca52824_096559 {ECO:0000313|EMBL:KAG2241457.1};
OS Brassica carinata (Ethiopian mustard) (Abyssinian cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=52824 {ECO:0000313|EMBL:KAG2241457.1, ECO:0000313|Proteomes:UP000886595};
RN [1] {ECO:0000313|EMBL:KAG2241457.1, ECO:0000313|Proteomes:UP000886595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2241457.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2241457.1};
RA Ma Q., Huang Y., Song X., Pei D.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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 UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG2241457.1}.
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DR EMBL; JAAMPC010000993; KAG2241457.1; -; Genomic_DNA.
DR OrthoDB; 5835829at2759; -.
DR Proteomes; UP000886595; Unassembled WGS sequence.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IEA:TreeGrafter.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR CDD; cd20336; Rcat_RBR; 1.
DR FunFam; 3.40.50.2000:FF:000019; Glycosyltransferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11926; GLUCOSYL/GLUCURONOSYL TRANSFERASES; 1.
DR PANTHER; PTHR11926:SF1356; UDP-GLYCOSYLTRANSFERASE 74C1; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SMART; SM00647; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00375; UDPGT; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000886595};
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 122..308
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 126..172
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 102460 MW; 0CE5184199B37839 CRC64;
MDYSDDDGML YTGSGEENLY SEHTAESDYG TEEDMHNDST LKRAQLSYVV LKEEEICEHQ
KADVEQVSTV LLINQVEAII LLLHYQWGSS KVEDEWFTDE DRVRKTVGIL KEHVVDLNNQ
EVNTECEICV ESYLHKEIAT VSCGHPFCKN CWTSYITEKI NNGPGCLMIK CPEPSCSAVV
GQDMIDKFIT IEEDKEKYYR YFLRSYVKEG RNNIKWCPSP GCVYAVDFGT RNGTENYDVT
CLCSYDFCWN CSEDAHRPVN CDMPCPNCNC HIEKNQGCNR MTCSICNHSF CWICLCPYDG
GHTCHKFEGD DETKIKRKRA KRVKRTIDRY MHYYVRWANN QSSRLKAMED LKELQAVQLE
KLSVKQCFSQ TQLQFTVDAW LQIIECRRVL KWTYAYGYYL PREERTKKQF FEYLQGEAEV
GLERLHHCAE EELQHFVDET DDPSTDFDDF RKKLIVLNKT QKIWVKQKGL TVSLIIASNI
HREPYTSEDY SITVHTIHDG FFPHEHPHAK IKDPPRFNDS TARSLTDFIS RQKLSGNPPK
ALIYDPFMPF ALDVAKDLGL YVVAYFTQPW LASLIYYHIN EGTYDVPDDR HEDPILASFP
GFPLLSQNEL PSFACEKGSY PLIFKVVVSQ FSNLRRAECI LCNTFDQLEP KVVKWMDGQW
PVKNIGPVVP SKFLDNRLPE DKDYELGDSK TEPDESVLSW LANKPAKSVV YVAFGTLVAL
SEKQMKETAM AIKQTGYSFL WSVRDSERSK LPSGFVEEAL EKDMGLVAKW VPQLEVLAHD
SIGCFVTHCG WNSTLEALCL GVPLVGMPQW TDQPTNAKFI EDVWKIGVRV KTDEEGFVSK
EEIARCIAEV MEGEKGKVIR KNVENFKVLA REAISEGGSS DKKIDEFVAM MS
//
