A0A4S4L359 · A0A4S4L359_9AGAM

  • Protein
    E3 ubiquitin-protein ligase listerin
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular ComponentRQC complex
Molecular Functionmetal ion binding
Molecular Functionribosomal large subunit binding
Molecular Functionubiquitin protein ligase activity
Biological Processprotein ubiquitination
Biological Processrescue of stalled ribosome
Biological Processribosome-associated ubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase listerin
  • EC number
  • Alternative names
    • RING-type E3 ubiquitin transferase listerin

Gene names

    • ORF names
      EW146_g9950

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 108281
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Russulales > Bondarzewiaceae > Bondarzewia

Accessions

  • Primary accession
    A0A4S4L359

Proteomes

Subcellular Location

Interaction

Subunit

Component of the ribosome quality control complex (RQC).

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region21-75Disordered
Compositional bias34-70Basic and acidic residues
Domain95-219E3 ubiquitin-protein ligase listerin N-terminal
Domain1383-1597E3 ubiquitin-protein ligase listerin HEAT repeat region

Sequence similarities

Belongs to the LTN1 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    1,619
  • Mass (Da)
    179,151
  • Last updated
    2019-07-31 v1
  • Checksum
    C2A64E8BA965BCB8
MFASQSDVVFIAAHTYTMVKGGKSSATSGTRKKQARKSGKDTLAPEPLPREKKPKGKDKGKNKEPKKKVYIPPVKPAPVQQDPLDTLGIAHRIPPDLLVVLRRFSKKDAVTKTKALEELQVGWVDKARKEQDDSPVLESLVVMLPVWLHHIPVLFLHPSRRIRQLTAALHSSLLRIPRLHDQIFIFIQEVASEDQVESILGSWGMASRDVDRQVSTYARRSWEESISLTHSADQLRLSGSVLTSLLAFVQRAIMDPSGLYLYLNPVQVGVDLTPPKKDARAQHVECKSLDDLMDILLNPALWSSLHYAQICPFVDGESFGFAQPIVRVSAWTLLXALXQNWKVEMEPLLPLLSVTVLRSAFVEPDAQVRNAMWRPLLTILKGELSLNSICYEGHLNVNXFCVDFPRAWDLEASFELERQQEDEEDYSDDVHDSREXKPEVLITGSATQAAPTSSPHTKAYQEXLQFXQLGCSGSPLQGYPAVLIILSTIPSSILLTSSSASHPAADFFNSFWAAIDGRALSALERAATSKAFLSALLECMVFIVRRLRNGSTPDDGESXKEPVVDGVSASXRLVAEQFARVWEEVAARKLKAEDNVVGDLLAKNLKLLGEIDEXLFDSAWNALAPAMQVCAEASGANNSHLVSAVLKIFSEAFEEGSXAYAAANTLLHEIAKDVSLRCRIALASESAXVEVDATRRAVSSLVDVIDAFGNMLFKEGDFACLVDESIRSHANNLLTISPPLLISYLTHRQDQVGTLHLWLTLLSTVSIHPNAIYRTLPPLLDAAERGVLPDHLTAAEQEFDLSINKLFFDAAEGQNSLALPLLXRLVRHTIVCDFGDTFESLLSGRDESLARLDVVLEVLAVAFEAKYRLSLDEEVCSLLLPAVFLLAXLLPKCCDFDDARATTVAKGLWTAWLGCAPEDLKNRVVHLIXRQLYDSIYDVGIRPSPQDIVKVAMEGNPGLPVTSIEDILPSRARLDIEMHALRLDPAHPSLAIXYPLVPPSSSFDPAEGPGCTGDLHGFSSYARAVNALLCFLAEDRQAAKANFWALRHLLALSXYADEXLQMPMLPNPVFTEKVSKGQLGDIIMKVRQLSAYLLVVPPGGTWHAXVSASASGEKGRTEGDLAGFVXXVIKAGTTTDSYRDSRILHTVXQXVIADTDKGEADQWMGLARKLEKIAPQTSLAIXLAVAQFGPEPPRLERYRNELAAGIXGIPPRKANDDGVLLLRRLVATAPDPESDVVFLPQLRAVNFMKQCQQWITSDEDIXEDVESEMTAVFFHVVPLLQNVPGAHWDLIFDVIENNLENSSFDDDMTLVTLWRTIRLIQVIQDLVTYNKSLRADWQARQMVILILLRDLVASEPRTSSPSKPRSVCREAALSVIQTLPPSLIDHETLPKMSHLLSDPSAHVQKMAYDLLRRAAKKRSEYLVIETGVDTESKVKAQLPMELVSLLQQVMDDGEEQTGSKAFTFLLGWMVTFDLFSDTSMKVRSGYTEHLRDLDLIATQFMPFILSILNLYGGVSKAFKLNVWAVDEFYIELYDPDDTLSLRLFAAHLFFRGLVTVPSLIRSWLLDCKDVALSTAVTTYTSQHFSPIIISYELAEVKSPEAAAELNVDNMSVKVASNVN

Features

Showing features for compositional bias, non-terminal residue.

TypeIDPosition(s)Description
Compositional bias34-70Basic and acidic residues
Non-terminal residue1619

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SGPL01001034
EMBL· GenBank· DDBJ
THH05251.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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