ID A0A0D9YWT0_9ORYZ Unreviewed; 410 AA.
AC A0A0D9YWT0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G29350.8};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G29350.8}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G29350.8}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR AlphaFoldDB; A0A0D9YWT0; -.
DR EnsemblPlants; OGLUM02G29350.8; OGLUM02G29350.8; OGLUM02G29350.
DR Gramene; OGLUM02G29350.8; OGLUM02G29350.8; OGLUM02G29350.
DR HOGENOM; CLU_671543_0_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20341; BRcat_RBR_RNF14; 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; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685:SF237; E3 UBIQUITIN-PROTEIN LIGASE RNF14; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 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:UP000026961};
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 102..282
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 106..150
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 46193 MW; B4937DD63FA11176 CRC64;
MIAVESELLG RWAASSATMT LSKKKIWAEQ PAGQEVVYRW VDWLSTSSWS CIASDDQIVF
GPDADSDGGD DRAIGRSCSL DSMIPLIQRY SKERSHEIFA RRIHECGVCL SENTGRNFIQ
LPCSHSFCVK CMETQMLDTM PDVAYCPRCS AACVAAGDDA QCSRCFFTFC AVCRERRHVG
DTCVSPNQML DIMLERQKEK RPSAAPSPNS QAVSEKRKME ELLSLREVMR TSRQCPSCKM
AVSKTAGCNK MVCSNCGRPF CYRCSRAITG YEHFAGECKL FESVGKGWFP GQAMWMNLEY
DYDEIAEIGT PSWIRATRYP CPTCGAKRTK RMPNPLLRAV LEEGMEHRRA LWAISINVET
EHSSKLETGT LKPVGVPVDL TPLSRNPSIF RYAPEERERE AEITLHYGEW
//