PROSITE logo

PROSITE documentation PDOC51535
Pestivirus NS3 protease (NS3pro) domain profile


Description

The genome of pestiviruses [E1] is a single plus-strand RNA and contains a single large open reading frame (ORF), a 5' untranslated region (5'UTR) and a 3' untranslated region (3'UTR). The ORF encodes a polyprotein, which is processed by viral and cellular proteases into mature proteins (the structural proteins in the N-terminal portion of the polyprotein whilst the replicative (non-structural or NS) proteins constitute the remainder). The pestivirus NS3 protein is a multifunctional protein possessing serine protease, RNA helicase (see <PDOC51192>), and a nucleoside triphosphatase (NTPase) activities located in two functionally distinct domains. The N-terminal one-third of pestiviral NS3 primarily serves as a protease to process the viral polyprotein. The helicase and NTPase activities are localized to the C-terminal of NS3 protein. The NS3 protease (NS3pro) domain is of some 180 aa with a catalytic triad of His-Asp-Ser. Positive regulation (activation) is observed by its interaction with NS4A. The pestivirus NS3pro domain forms peptidase family S31 of clan PA [E2].

The profile we developed covers the entire pestivirus NS3pro domain.

Last update:

May 2011 / First entry.

-------------------------------------------------------------------------------


Technical section

PROSITE method (with tools and information) covered by this documentation:

PESTIVIRUS_NS3PRO, PS51535; Pestivirus NS3 protease (NS3pro) domain profile  (MATRIX)


References

1AuthorsGorbalenya A.E. Donchenko A.P. Koonin E.V. Blinov V.M.
TitleN-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases.
SourceNucleic Acids Res. 17:3889-3897(1989).
PubMed ID2543956

2AuthorsRyan M.D. Monaghan S. Flint M.
TitleVirus-encoded proteinases of the Flaviviridae.
SourceJ. Gen. Virol. 79:947-959(1998).
PubMed ID9603310

3AuthorsWang P. Wang Y. Zhao Y. Zhu Z. Yu J. Wan L. Chen J. Xiao M.
TitleClassical swine fever virus NS3 enhances RNA-dependent RNA polymerase activity by binding to NS5B.
SourceVirus Res. 148:17-23(2010).
PubMed ID19951725
DOI10.1016/j.virusres.2009.11.015

E1Titlehttps://viralzone.expasy.org/39?outline=all_by_species

E2Titlehttps://www.ebi.ac.uk/merops/cgi-bin/famsum?family=s31



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)