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Database: UniProt
Entry: A0A0E0KT51_ORYPU
LinkDB: A0A0E0KT51_ORYPU
Original site: A0A0E0KT51_ORYPU 
ID   A0A0E0KT51_ORYPU        Unreviewed;       279 AA.
AC   A0A0E0KT51;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=E3 ubiquitin-protein ligase RMA {ECO:0000256|RuleBase:RU369090};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU369090};
DE   AltName: Full=Protein RING membrane-anchor {ECO:0000256|RuleBase:RU369090};
DE   AltName: Full=RING-type E3 ubiquitin transferase RMA {ECO:0000256|RuleBase:RU369090};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC04G17310.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC04G17310.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC04G17310.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000256|RuleBase:RU369090}.
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         ECO:0000256|RuleBase:RU369090};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369090}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU369090}; Single-pass type IV membrane protein
CC       {ECO:0000256|RuleBase:RU369090}.
CC   -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 ligase
CC       activity. {ECO:0000256|RuleBase:RU369090}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369090}.
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DR   AlphaFoldDB; A0A0E0KT51; -.
DR   STRING; 4537.A0A0E0KT51; -.
DR   EnsemblPlants; OPUNC04G17310.1; OPUNC04G17310.1; OPUNC04G17310.
DR   Gramene; OPUNC04G17310.1; OPUNC04G17310.1; OPUNC04G17310.
DR   eggNOG; KOG0823; Eukaryota.
DR   HOGENOM; CLU_055198_1_1_1; -.
DR   OMA; YHVAAQN; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000026962; Chromosome 4.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045103; RNF5/RNF185-like.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR   PANTHER; PTHR12313:SF103; OS04G0530500 PROTEIN; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU369090};
KW   Membrane {ECO:0000256|RuleBase:RU369090};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW   Transmembrane {ECO:0000256|RuleBase:RU369090};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU369090};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU369090};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369090};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..279
FT                   /note="E3 ubiquitin-protein ligase RMA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002365838"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369090"
FT   TRANSMEM        261..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369090"
FT   DOMAIN          65..116
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          168..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  31130 MW;  DBE8CF6EC4727205 CRC64;
     MSCAFLVTSF CLLNCSAVFA RKVIVRMDQI YMAAVNNQTS LPDDEPMKKI SGDMPVTAGN
     ACFDCNICLD FAAEPVVTLC GHLYCWPCIY EWLRPGVEST AGNNSSLARR QCPVCKATLS
     PDMLVPLYGR GGSLKKSLNG VPIPRRPTVQ REAVEHQNTQ NNIYDRHHEN MEPSPPLQPL
     RHSSHHSSST EFDFIYPPSP MGRGLIHSTA GGVLGGMAVA VLPWAFRGQV PPSMFMSPHY
     VTAHNMSSRA RRQQMEVERS LHQIWFFLFV FVVLCLLLF
//
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