ID A0A6P5N726_ARADU Unreviewed; 401 AA.
AC A0A6P5N726;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC110278398 {ECO:0000313|RefSeq:XP_020992294.1};
OS Arachis duranensis (Wild peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=130453 {ECO:0000313|Proteomes:UP000515211, ECO:0000313|RefSeq:XP_020992294.1};
RN [1] {ECO:0000313|Proteomes:UP000515211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. V14167 {ECO:0000313|Proteomes:UP000515211};
RX PubMed=26901068; DOI=10.1038/ng.3517;
RA Bertioli D.J., Cannon S.B., Froenicke L., Huang G., Farmer A.D.,
RA Cannon E.K., Liu X., Gao D., Clevenger J., Dash S., Ren L.,
RA Moretzsohn M.C., Shirasawa K., Huang W., Vidigal B., Abernathy B., Chu Y.,
RA Niederhuth C.E., Umale P., Araujo A.C., Kozik A., Kim K.D., Burow M.D.,
RA Varshney R.K., Wang X., Zhang X., Barkley N., Guimaraes P.M., Isobe S.,
RA Guo B., Liao B., Stalker H.T., Schmitz R.J., Scheffler B.E.,
RA Leal-Bertioli S.C., Xun X., Jackson S.A., Michelmore R., Ozias-Akins P.;
RT "The genome sequences of Arachis duranensis and Arachis ipaensis, the
RT diploid ancestors of cultivated peanut.";
RL Nat. Genet. 48:438-446(2016).
RN [2] {ECO:0000313|RefSeq:XP_020992294.1}
RP IDENTIFICATION.
RC TISSUE=Whole plant {ECO:0000313|RefSeq:XP_020992294.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_020992294.1; XM_021136635.1.
DR AlphaFoldDB; A0A6P5N726; -.
DR GeneID; 110278398; -.
DR KEGG; adu:110278398; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000515211; Chromosome 3.
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; cd20346; BRcat_RBR_ANKIB1; 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; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR054694; Parkin-like_IBR.
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; 1.
DR Pfam; PF22605; IBR_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000515211};
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 189..401
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 193..243
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 46932 MW; A76B9A0B25DA3759 CRC64;
MNNNYTYETE DEEDEDEESV EDEEDDESLE DEEEESLEDE EDDESLEDDE DDESLEDEEE
EPLEEEEDDE SLEDEEDDES LEDEKEESLE DEEDDESLED EEEESLEECT TSRKRSRFTT
LTKSNIKKLQ KTKINEVSSN LSITKSEACL LLIHHGWSAT KVDEAWFDDK ERVRKLVGLL
KHNTGEIVTT QTCEICFDNT VCLEKKLKSA KCGHAYCVDC WKLYINEKIK EGPHECLKPM
RCPHPSCEAS LEINMIRRFA SQQNRKMYDR FLLRSYVETR KNIKWCPRPD CDLAVRYKSD
GNYVNKYVEV SCRNGHRFCW GCGEDAHRPV SCEMMAKKNQ ESGDSKSLRW ISTFTKKCPS
CKQPIERNGG CMHVTCTVCS YQFCWLCLSD WFLCSARCNR F
//
