A0A0B2QDR6 · A0A0B2QDR6_GLYSO

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 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
      D0Y65_035356
      , glysoja_026035

Organism names

  • Taxonomic identifier
  • Strain
    • cv. W05
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja

Accessions

  • Primary accession
    A0A0B2QDR6

Proteomes

Genome annotation databases

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type IV membrane protein

Keywords

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-21Disordered
Domain129-170RING-type
Region247-279Disordered
Compositional bias320-393Polar residues
Region320-404Disordered

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
    404
  • Mass (Da)
    43,968
  • Last updated
    2015-03-04 v1
  • Checksum
    D030B8BFBF53C63C
MELDLNQEPSDPTHASPDEFDSLLEELESAHEHVQDRIRRLEAITSRTRQYSSWPLFHTPIQITNSTGQTSALADAREEEMPSREVEERVVESGRGFKRKGAHLVAKALGRIETDANKEGGSTGNFYDCNICLDRARDPVLTCCGHLFCWPCFYQVQIVYSNARECPVCKGEVTETGIFPIYGNSSADGSCESGLKGAGLRIPPRPAAPRIESFRQQLISQGASSSVILNIRRFHHLIGGLGARVQSQNPNAATDRNNGLLAQSRPPSSNDRGTGSSQTPISTLLVQGAASFSSLSSALNSAMDSAERLVEDLESYFHNHQTNGVNTSSTHNGNVAATDSTPAASTSPFSRNVDTTANIGSEIQTTDNNIQTETSTLDPSSSRRGSTRVSTSRQVTNDRRRRSR

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A445HUQ1A0A445HUQ1_GLYSOD0Y65_035356398

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias320-393Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN659065
EMBL· GenBank· DDBJ
KHN19420.1
EMBL· GenBank· DDBJ
Genomic DNA
QZWG01000012
EMBL· GenBank· DDBJ
RZB77426.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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