ID A0A6P5XT39_DURZI Unreviewed; 298 AA.
AC A0A6P5XT39;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC111285941 {ECO:0000313|RefSeq:XP_022731385.1};
OS Durio zibethinus (Durian).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Helicteroideae; Durio.
OX NCBI_TaxID=66656 {ECO:0000313|Proteomes:UP000515121, ECO:0000313|RefSeq:XP_022731385.1};
RN [1] {ECO:0000313|RefSeq:XP_022731385.1}
RP IDENTIFICATION.
RC TISSUE=Fruit stalk {ECO:0000313|RefSeq:XP_022731385.1};
RG RefSeq;
RL Submitted (MAR-2025) 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_022731385.1; XM_022875650.1.
DR AlphaFoldDB; A0A6P5XT39; -.
DR GeneID; 111285941; -.
DR KEGG; dzi:111285941; -.
DR OrthoDB; 10009520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000515121; Unplaced.
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:UniProtKB-UniPathway.
DR CDD; cd22582; BRcat_RBR_unk; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR FunFam; 3.30.40.10:FF:000230; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 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; 2.
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:UP000515121};
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 93..298
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 97..145
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 298 AA; 34188 MW; B1A908C39EBFFCD4 CRC64;
MGFFQKYFSH HIQQRISLKS KLAALRISYS KKSRNMGNKM GKFLNNVKCK KSVETPSSNV
EEEVNYYFTP SEDLEMEHNF SSLSSETHDD TSPTYVCEIC VEPRPLDISF NVKGCAHFYC
IGCTVKYIES KLDDNVTRIP CPVTNCQGLL EPDFCRDILP RDLFNRWGKA LCESAFLGSE
KIYCPYKDCS ALLINDGKNA TKNFRCPFCK RVFCVQCKVA WHSGVDCAKF QKLKKLGSDA
MLVDLAKRKK WRQCPKCNYY VEKSAGCYYV KCRCGNAFCY NCGAKSNRVT HFCSECYH
//
