ID A0A8X7PEK8_BRACI Unreviewed; 412 AA.
AC A0A8X7PEK8;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 02-APR-2025, entry version 11.
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_089046 {ECO:0000313|EMBL:KAG2249418.1};
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:KAG2249418.1, ECO:0000313|Proteomes:UP000886595};
RN [1] {ECO:0000313|EMBL:KAG2249418.1, ECO:0000313|Proteomes:UP000886595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2249418.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2249418.1};
RA Ma Q., Huang Y., Song X., Pei D.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KAG2249418.1}.
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DR EMBL; JAAMPC010000017; KAG2249418.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000886595; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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; cd22582; BRcat_RBR_unk; 1.
DR CDD; cd22584; Rcat_RBR_unk; 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; IPR002156; RNaseH_domain.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF13456; RVT_3; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
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}.
FT DOMAIN 178..392
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 392..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 45733 MW; EC602ECF4BE60436 CRC64;
MDNELELARQ KLGLVSLGES STYRLYSKGL VSEEVIKDDT KLVGGSGLFL CDSNDNSKKS
ETNKALRNHQ VLAAHPEAVG LAAIIQGLSW ALKLGVKSIQ FFCDDDSIIL DYVTGKAAPP
KESIVVAKLL KQLALIQTSF TSCQALPLLR SDDINSSLIK LARDAIASQT TWQREGDEYE
TCPACYAHVS PRHKLEVRSG CFHRICFTCI RDCVSSQLAR GDTLLCPYPG CEKELVLEDC
RGIVDDDALN LIIHRKKEKA IPVLDRVYCP KPSCNFLMSD RDLIDPRQKK SVERTCVECG
LCFCKKCHVP WHYKKTCDEF KKSPSYLTSD AALFESLVKT QGWIKCPQCA TVVQKNGGCQ
RISCRHCNHK FCYACGAACT RKKMSCNCSP EDGPSKMSSP SGESHKTRLL RA
//
