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Literature summary for 3.4.22.66 extracted from

  • Wu, H.; Zu, S.; Sun, X.; Liu, Y.; Tian, J.; Qu, L.
    N-Terminal domain of feline calicivirus (FCV) proteinase-polymerase contributes to the inhibition of host cell transcription (2016), Viruses, 8, E199 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
feline calicivirus
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feline calicivirus P27409 genome polyprotein
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feline calicivirus 2280
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feline calicivirus F9 P27409 genome polyprotein
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General Information

General Information Comment Organism
physiological function the feline calicivirus strain 2280 proteinase-polymerase protein can suppress luciferase reporter gene expression driven by endogenous and exogenous promoters. The N-terminal 263 amino acids of proteinase-polymerase (PPN-263) determine its shut-off activity upon the expression of truncated proteins. The same domain of the feline calicivirus strain F9 proteionase-polymeraseprotein fails to inhibit gene expression. Residues Val27, Ala96 and Ala98 are key sites for the inhibition of host gene expression by strain 2280 PPN-263, and PPN-263 exhibits the ability to shut off host gene expression as long as it contains any two of the three amino acids feline calicivirus