A0A5E4FIJ3 · A0A5E4FIJ3_PRUDU

Function

function

E3 ubiquitin-protein ligase.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionligase activity
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-like protein conjugating enzyme binding
Biological Processprotein ubiquitination
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RMA
  • EC number
  • Alternative names
    • Protein RING membrane-anchor
    • RING-type E3 ubiquitin transferase RMA

Gene names

    • ORF names
      ALMOND_2B005922

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Texas
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus

Accessions

  • Primary accession
    A0A5E4FIJ3

Proteomes

Genome annotation databases

Subcellular Location

Endomembrane system
Endoplasmic reticulum membrane
; Single-pass type IV membrane protein

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region98-126Disordered
Compositional bias112-126Basic and acidic residues
Domain151-192RING-type

Domain

The RING-type zinc finger domain is responsible for E3 ligase activity.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    227
  • Mass (Da)
    25,029
  • Last updated
    2019-11-13 v1
  • Checksum
    F2A2756B33EF25AB
MASINESMPQVIKVGFQSRKPRMRVMKPPQVFHFRIPEAEPKECDLMDEEELSAYGYKPVALSCSEIKPCSPCEASSSMEGSNNGGDPFESDSFAVHSVGGSCSTSPPDAWSSPHHDDDDDEQESHELGASFCHASPEPSSPPRLAFYFDCKLCLKMAREPVVTPCGHLFCGDCLDKWLHFFTSQMECPVCHSKVLDSSIIPIRPTPVCNRDLDLNVPPRSKGGLCF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias112-126Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CABIKO010000131
EMBL· GenBank· DDBJ
VVA27974.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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