ID A0A8S9LUG6_BRACR Unreviewed; 561 AA.
AC A0A8S9LUG6;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-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=F2Q68_00001254 {ECO:0000313|EMBL:KAF2582207.1},
GN F2Q70_00008214 {ECO:0000313|EMBL:KAF2611650.1};
OS Brassica cretica (Mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=69181 {ECO:0000313|EMBL:KAF2611650.1};
RN [1] {ECO:0000313|EMBL:KAF2611650.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PFS-001/15 {ECO:0000313|EMBL:KAF2582207.1}, and PFS-102/07
RC {ECO:0000313|EMBL:KAF2611650.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF2611650.1};
RA Studholme D.J., Sarris P.F.;
RT "Genome sequencing and annotation of Brassica cretica.";
RL Submitted (DEC-2019) 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 RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:KAF2611650.1}.
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DR EMBL; QGKW02001660; KAF2582207.1; -; Genomic_DNA.
DR EMBL; QGKY02000089; KAF2611650.1; -; Genomic_DNA.
DR Proteomes; UP000712281; Unassembled WGS sequence.
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; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR CDD; cd23141; RING-HC_ARI6-like; 1.
DR FunFam; 1.20.120.1750:FF:000005; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
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; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 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 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 142..355
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 146..190
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..549
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..561
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 64090 MW; 233B50F5608FA6E6 CRC64;
MDSGDDMLDM YSGEDDFYSD DYKDSDNDDD DDDDDDDDDD DGEPDYGFVE EDADDSAMIA
SHRSQKNYCV LREEDIHRHQ VDDIERVSVV LSITEVEASI LLRHYHWSVG KVHDEWFADE
ERVRNTVGIL ENPVVPPSDD DTELTCGICF DSYPPENIVS VSCGHPFCTT CWTGYISTTI
NDGPGCLMLR CPDPSCLAAV GHDMVDKLAS GEDKEKYNRY FLRSYIEDNR KMKWCPAPGC
DYAIDFVAGS GNFDVSCLCS FSFCWNCTEE SHRPVDCSTV SKWILKNSAE SENMNWILAN
SKPCPRCKRP IEKNQGCMHM TCTPPCKYEF CWLCLGAWMD HGERTGGFYA CNRYEVAKQE
GQYDETERRR EMAKNSLERY THYYERWASN QTSRQKAMTD LHQLQTHNLE RLSDKQCTPE
SQLKFILEAW LQIIECRRVL KWTYAYGYYL PDHEHAKRVF FEYLQGEAES GLERLHQCVE
KDLLQFLNAE GPSKDFNDFR TKLAGLTSVT KNYFENLVKA LENGLADVDS HAACSSKSTS
SKSTGCSSKT RGKGKGSSRT G
//
