UniProt: A0A1J6IMW9

Database: UniProt
Entry: A0A1J6IMW9_NICAT

LinkDB:  A0A1J6IMW9_NICAT 
Original site:  A0A1J6IMW9_NICAT

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (19)   

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ID   A0A1J6IMW9_NICAT        Unreviewed;       251 AA.
AC   A0A1J6IMW9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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};
GN   Name=RMA3_1 {ECO:0000313|EMBL:OIS99054.1};
GN   ORFNames=A4A49_14705 {ECO:0000313|EMBL:OIS99054.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451 {ECO:0000313|EMBL:OIS99054.1, ECO:0000313|Proteomes:UP000187609};
RN   [1] {ECO:0000313|EMBL:OIS99054.1, ECO:0000313|Proteomes:UP000187609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC   TISSUE=Leaves {ECO:0000313|EMBL:OIS99054.1};
RA   Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Baldwin I.T.;
RT   "The genome of Nicotiana attenuata.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIS99054.1}.
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DR   EMBL; MJEQ01037190; OIS99054.1; -; Genomic_DNA.
DR   RefSeq; XP_019251705.1; XM_019396160.1.
DR   AlphaFoldDB; A0A1J6IMW9; -.
DR   STRING; 49451.A0A1J6IMW9; -.
DR   EnsemblPlants; OIS99054; OIS99054; A4A49_14705.
DR   GeneID; 109230748; -.
DR   Gramene; OIS99054; OIS99054; A4A49_14705.
DR   KEGG; nau:109230748; -.
DR   OMA; VCKSHIS; -.
DR   OrthoDB; 276791at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000187609; Chromosome 8.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16745; RING-HC_AtRMA-like; 1.
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:SF45; E3 UBIQUITIN-PROTEIN LIGASE RMA; 1.
DR   PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 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:UP000187609};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, 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   DOMAIN          44..91
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   251 AA;  27705 MW;  44BABE39E9713D12 CRC64;
     MDLEQSFGEP LISFGSDEDV SLKTRNSVPV PMVNSGNMMG CFDCNICLDS AHDPVVTLCG
     HLYCWPCIYK WLQVENSNPG SEETPKCPVC KAHISNSSLV PLYGRGTSSA EHRSTESQVD
     VAIPRRPPAI WTTTQVNTSS PTSHVHQQLH HTSLYYPHAF GGFSAIAPST VGGTAMTRLF
     SPMVVMFGEM FLTRMLGGSD ASSFSYPYPS PYLIPGNGNS RMRRQEMQVD KSLNRVSIFL
     FCCFILCLLL F
//

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