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Database: UniProt
Entry: A0A0D9Y2M3_9ORYZ
LinkDB: A0A0D9Y2M3_9ORYZ
Original site: A0A0D9Y2M3_9ORYZ 
ID   A0A0D9Y2M3_9ORYZ        Unreviewed;       247 AA.
AC   A0A0D9Y2M3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=E3 ubiquitin-protein ligase {ECO:0000313|EnsemblPlants:OGLUM01G01660.2};
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:OGLUM01G01660.2};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM01G01660.2}
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:OGLUM01G01660.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. It probably triggers the ubiquitin-mediated
CC       degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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DR   AlphaFoldDB; A0A0D9Y2M3; -.
DR   EnsemblPlants; OGLUM01G01660.2; OGLUM01G01660.2; OGLUM01G01660.
DR   Gramene; OGLUM01G01660.2; OGLUM01G01660.2; OGLUM01G01660.
DR   HOGENOM; CLU_040603_1_1_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632:SF16; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 10; 1.
DR   PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          53..114
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   247 AA;  26362 MW;  82A05CF3B7820B82 CRC64;
     MGDRTNFCIV HVQCKHGHPS CKRCLAGLNN KCHICRQPIG DMRCRPLENV LAGMTVPCAF
     ARFGCQEGVR YTERAQRHGH EASCQHAPCH CPFPGCSYAG AAAQLFAHIR GAHAAGSPSA
     VSSIRCTPVA LPRGMPFHVL LREEDSRVFL LLNGGDVPKG RSLSVVCVAA AGEAELYTMA
     VSGGAPGALS LSASGSVPRV RRWVRYPTGG FLFVLDTYWR ASGGSVSVTV HVKKLPPPEL
     EEDTTAA
//
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