Q50LE5 · CAPSD_HPBVH

Function

function

The capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry made of 120 subunits.

Miscellaneous

Picobirnavirus particles are capable of disrupting biological membranes in vitro.

Features

Showing features for site.

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TypeIDPosition(s)Description
Site65-66Cleavage

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 ComponentT=3 icosahedral viral capsid

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Segment-1
    • ORF names
      ORF2

Organism names

Accessions

  • Primary accession
    Q50LE5

Proteomes

Subcellular Location

Capsid protein

Virion

7 kDa polypeptide

Virion

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003795221-657 kDa polypeptide
ChainPRO_00003795211-552Capsid protein precursor
ChainPRO_000037952366-552Capsid protein

Post-translational modification

The 7 kDa polypeptide is acetylated.
Autocatalytic proteolysis releases a post-translationally modified peptide that remains associated with nucleic acid within the virion. This peptide is observed only when nucleic acid is packaged in the capsid.

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-41Disordered

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    552
  • Mass (Da)
    62,029
  • Last updated
    2005-06-07 v1
  • Checksum
    F6D977879662A99C
MKQNDTKKTTQRRNSKKYSSKTNRGTKRAPRDQEVGTGAQESTRNDVAWYARYPHILEEATRLPFAYPIGQYYDTGYSVASATEWSKYVDTSLTIPGVMCVNFTPTPGESYNKNSPINIAAQNVYTYVRHMNSGHANYEQADLMMYLLAMDSLYIFHSYVRKILAISKLYTPVNKYFPRALLVALGVDPEDVFANQAQWEYFVNMVAYRAGAFAAPASMTYYERHAWMSNGLYVDQDVTRAQIYMFKPTMLWKYENLGTTGTKLVPLMMPKAGDNRKLVDFQVLFNNLVSTMLGDEDFGIMSGDVFKAFGADGLVKLLAVDSTTMTLPTYDPLILAQIHSARAVGAPILETSTLTGFPGRQWQITQNPDVNNGAIIFHPSFGYDGQDHEELSFRAMCSNMILNLPGEAHSAEMIIEATRLATMFQVKAVPAGDTSKPVLYLPNGFGTEVVNDYTMISVDKATPHDLTIHTFFNNILVPNAKENYVANLELLNNIIQFDWAPQLYLTYGIAQESFGPFAQLNDWTILTGETLARMHEVCVTSMFDVPQMGFNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB186897
EMBL· GenBank· DDBJ
BAD98235.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

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