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Database: UniProt
Entry: A0A0E0B438_9ORYZ
LinkDB: A0A0E0B438_9ORYZ
Original site: A0A0E0B438_9ORYZ 
ID   A0A0E0B438_9ORYZ        Unreviewed;       376 AA.
AC   A0A0E0B438;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
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:OGLUM09G13900.2};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM09G13900.2}
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:OGLUM09G13900.2}
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}.
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DR   AlphaFoldDB; A0A0E0B438; -.
DR   EnsemblPlants; OGLUM09G13900.2; OGLUM09G13900.2; OGLUM09G13900.
DR   Gramene; OGLUM09G13900.2; OGLUM09G13900.2; OGLUM09G13900.
DR   HOGENOM; CLU_040108_4_2_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16461; RING-H2_EL5-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044600; ATL1/ATL16-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46913; RING-H2 FINGER PROTEIN ATL16; 1.
DR   PANTHER; PTHR46913:SF1; RING-H2 FINGER PROTEIN ATL16; 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   4: Predicted;
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        62..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          156..198
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          234..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  40307 MW;  B17181F9DA35BF13 CRC64;
     MYPERPSRVN GTATVDCSAY PLDCHPVCPG GSCYEIAEPP PPSQVVPRVD VAVDDHHLPV
     RLLLTVSLLS AFLFISLAVS TILLYRRRVV LRRRRRAATA PLPGDDGFGD GDEEAGGGGG
     DVHHLWYIRT VGLDEATITS IATAEYRAGV GWGGDCAVCL GEFRDGELVR LLPRCSHPFH
     APCIDTWLRA HVNCPLCRSP VVVPSDLPAT ATEGEAEGGG QAEEHQVFDE ISLSESRADV
     SEDSDASSDT QSEDTAASPE DGGRVMPKPI RRSASMDSPL FLVVVPEAQD DAMRGDRKFP
     NSQEMKLFSV KEKDATGTSS SSCQAGRFGI GRSMSSSGQG FFFSRNGRSS SADIHELKSN
     AVASPADLGR IHQIKT
//
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