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Database: UniProt
Entry: A0A0D9Z731_9ORYZ
LinkDB: A0A0D9Z731_9ORYZ
Original site: A0A0D9Z731_9ORYZ 
ID   A0A0D9Z731_9ORYZ        Unreviewed;       174 AA.
AC   A0A0D9Z731;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
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:OGLUM03G17160.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM03G17160.1}
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:OGLUM03G17160.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC       {ECO:0000256|ARBA:ARBA00024209}.
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DR   AlphaFoldDB; A0A0D9Z731; -.
DR   STRING; 40148.A0A0D9Z731; -.
DR   EnsemblPlants; OGLUM03G17160.1; OGLUM03G17160.1; OGLUM03G17160.
DR   Gramene; OGLUM03G17160.1; OGLUM03G17160.1; OGLUM03G17160.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_013137_15_2_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd16461; RING-H2_EL5-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45768; E3 UBIQUITIN-PROTEIN LIGASE RNF13-LIKE; 1.
DR   PANTHER; PTHR45768:SF25; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          91..133
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   174 AA;  17679 MW;  4ADCB24D85AA3792 CRC64;
     MDSPQMSLGG DLRFRAYAAA AAVGVVAVLA VCFWRLYRLT VSARPQDMLP VSAVSSGAGA
     GGGKAALGEL DISALPVFVH VAGGEAAAVE CAVCLGEVRD GERGRLLPRC GHRFHVECID
     RWFRANSTCP LCRAAVVAGE PGGAAAAAGD KGDAVAVAVV GVPDVVVHVQ VEEG
//
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