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A0A1B1J0V4 · A0A1B1J0V4_9VIRU

Function

function

Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F. Upon virus binding to host cell, one of the spikes dissociates from the capsid and the virus interacts with LPS through the exposed EF loops on the F proteins. After the genome had been ejected, the channel formed by the F proteins at the unique fivefold axis remains open.

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
Molecular Functionstructural molecule activity
Biological Processsymbiont entry into host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Capsid protein F
  • Alternative names
    • F protein
    • GPF

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Viruses > Monodnaviria > Sangervirae > Phixviricota > Malgrandaviricetes > Petitvirales > Microviridae > Bullavirinae > Gequatrovirus > Gequatrovirus G4

Accessions

  • Primary accession
    A0A1B1J0V4

Proteomes

Subcellular Location

Virion

Keywords

Interaction

Subunit

Pentamerizes and interacts with H protein, G and B pentamers to form 12S pre-assembly complex. By binding with protein D, induces joining of twelve 12S complex to form the procapsid. The procapsid has an external scaffold made of 240 copies of protein D, 60 copies of the internally located B protein, and contains 60 copies of each of the viral structural proteins F and G. Upon genome packaging, interacts with protein J. The mature virion is composed of 60 copies each of the F, G, and J proteins, and 12 copies of the H protein.

Family & Domains

Sequence similarities

Belongs to the microviridae F protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    48,658
  • Last updated
    2016-11-02 v1
  • MD5 Checksum
    D3DEB5E411A424AD0A7A7722A6C0A700
MSNVQTSADRVPHDLSHLVFEAGKIGRLKTISWTPVVAGDSFECDMVGAIRLSPLRRGLAVDSRVDVFSFYIPHRHIYGQQWIDFMKDGINAAPLPPVTCSSGWDAAAYLGTIPSSNLKVPKFLHQGYLNIYNNYFKPPWSDDLTYANPSNMPSEDYKWGVRVANLKSIWTAPLPPDTRTSESMTTGTSTIDIMGLQAAYAKLHTEQERDYFMTRYRDIMKEFGGHTSYDGDNRPLLLMRSEFWASGYDVDGTDQSSLGQFSGRVQQTFNHKVPRFYVPEHGVIMTLAVTRFPPTHEMEMHYLVGKENLTYTDIACDPALMANLPPREVSLKEFFHSSPDSAKFKIAEGQWYRTQPDRVAFPYNALDGFPFYSALPSTKLKDRVLVNTDNYDEIFQSMQLAHWNMQTKFNINVYRHMPTTRDSIMTS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KX266303
EMBL· GenBank· DDBJ
ANS06365.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266310
EMBL· GenBank· DDBJ
ANS06442.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266317
EMBL· GenBank· DDBJ
ANS06519.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266331
EMBL· GenBank· DDBJ
ANS06673.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266338
EMBL· GenBank· DDBJ
ANS06750.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266348
EMBL· GenBank· DDBJ
ANS06860.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266354
EMBL· GenBank· DDBJ
ANS06926.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266360
EMBL· GenBank· DDBJ
ANS06992.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266367
EMBL· GenBank· DDBJ
ANS07069.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266381
EMBL· GenBank· DDBJ
ANS07223.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266388
EMBL· GenBank· DDBJ
ANS07300.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266398
EMBL· GenBank· DDBJ
ANS07410.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266402
EMBL· GenBank· DDBJ
ANS07454.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266408
EMBL· GenBank· DDBJ
ANS07520.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266418
EMBL· GenBank· DDBJ
ANS07630.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266432
EMBL· GenBank· DDBJ
ANS07784.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266437
EMBL· GenBank· DDBJ
ANS07839.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266441
EMBL· GenBank· DDBJ
ANS07883.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266446
EMBL· GenBank· DDBJ
ANS07938.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266453
EMBL· GenBank· DDBJ
ANS08015.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266459
EMBL· GenBank· DDBJ
ANS08081.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266469
EMBL· GenBank· DDBJ
ANS08191.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266483
EMBL· GenBank· DDBJ
ANS08345.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266489
EMBL· GenBank· DDBJ
ANS08411.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266497
EMBL· GenBank· DDBJ
ANS08499.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266503
EMBL· GenBank· DDBJ
ANS08565.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266505
EMBL· GenBank· DDBJ
ANS08587.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266519
EMBL· GenBank· DDBJ
ANS08741.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266524
EMBL· GenBank· DDBJ
ANS08796.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266527
EMBL· GenBank· DDBJ
ANS08829.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266532
EMBL· GenBank· DDBJ
ANS08884.1
EMBL· GenBank· DDBJ
Genomic DNA
KX266546
EMBL· GenBank· DDBJ
ANS09038.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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