ID A0A8X7W393_BRACI Unreviewed; 600 AA.
AC A0A8X7W393;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Bca52824_014863 {ECO:0000313|EMBL:KAG2321650.1};
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:KAG2321650.1, ECO:0000313|Proteomes:UP000886595};
RN [1] {ECO:0000313|EMBL:KAG2321650.1, ECO:0000313|Proteomes:UP000886595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2321650.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2321650.1};
RA Ma Q., Huang Y., Song X., Pei D.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|ARBA:ARBA00003861}.
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:0000256|ARBA:ARBA00000900};
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:KAG2321650.1}.
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DR EMBL; JAAMPC010000003; KAG2321650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8X7W393; -.
DR OrthoDB; 7537227at2759; -.
DR Proteomes; UP000886595; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR FunFam; 1.25.10.10:FF:000082; RING-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000292; RING-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR058678; ARM_PUB.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR057623; PUB12-19-like_N.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23315:SF52; U-BOX DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF25598; ARM_PUB; 1.
DR Pfam; PF25368; PUB10_N; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 4.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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}.
FT DOMAIN 224..298
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 358..400
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 399..441
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 440..482
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 481..524
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
SQ SEQUENCE 600 AA; 66014 MW; E7803E611A020A4F CRC64;
MAGVAVSPAS LLLAIAEISE TPASTGVFKK DCADLARRVC LLTHLVEEIR DSPPTPQESD
ASSSLVSYEC DWWSDLVVGL QAAKRLLCAA TCFQARESSE GAAKRISFQF QCVTWKLEKA
LGNLPYDRYD ISDEVREQVE LARLQLRRAM QRYGSLNSKS SLLLFPSQWR KMHRAKCEET
GITATKELFC FLGLLLSKDA DSERLEKAIT KSNDDDSKKS DNLTIPEDFL CPISLELMKD
PVIVSTGQTY ERSYIQRWID CGNLRCPKTQ QKLGNFTLTP NYVLRSLISQ WCAKHNIEQP
GGYMKNCDGD LSGDMSAIRA LVRKLSTRSL EDRRTALSEI RSLSKRNTDN RILIAEAGAI
PVLVNLLTSE DVETQEKAVT CVLNLSIYES NKELIMLAGA VTSLVQVLRA GTVEAKENAA
ATLFSLSLAD ENKIIIGASG AIPALVHLLE NGSVRGKKDA ATALFNLCIY EGNKGRAVRA
GIVNPLVKML SDTSSHRMVT EALTILSVLA GNQDAKKAIL KANAIPPLVA LLQKDQPRNR
ENAAAILLAL CKRDNEKLIF IGRLGAVVPL MELSRDGTER AKRKANSLLE QLRKSSQKVC
//
