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PMID: 2543956 Published · ppublish English Comparative Study Journal Article

N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases.

Nucleic acids research ·Vol. 17 ·No. 10 ·1989-05-25 ·Pages 3889-97

Gorbalenya AE, Donchenko AP, Koonin EV, Blinov VM

Abstract

Recently we tentatively identified, by sequence comparison, central domains of the NS3 proteins of flaviviruses and the respective portion of the pestivirus polyprotein as RNA helicases (A.E.G. et al., submitted). Alignment of the N-proximal domains of the same proteins revealed conservation of short sequence stretches resembling those around the catalytic Ser, His and Asp residues of chymotrypsin-like proteases. A statistically significant similarity has been detected between the sequences of these domains and those of the C-terminal serine protease domains of alphavirus capsid proteins. It is suggested that flavivirus NS3 and the respective pestivirus protein contain at least two functional domains, the N-proximal protease and the C-proximal helicase one. The protease domain is probably involved in the processing of viral non-structural proteins.

MeSH Terms
Amino Acid Sequence Flavivirus/enzymology,genetics Molecular Sequence Data Pestivirus/enzymology,genetics RNA Helicases RNA Nucleotidyltransferases/genetics Serine Endopeptidases/genetics Viral Nonstructural Proteins Viral Proteins/genetics
Chemicals
NS3 protein, flavivirus Viral Nonstructural Proteins Viral Proteins RNA Nucleotidyltransferases Serine Endopeptidases RNA Helicases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gorbalenya A E
Institute of Poliomyelitis and Viral Encephalitides, USSR Academy of Medical Sciences, Moscow region.
Donchenko A P
Koonin E V
Blinov V M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1989-05-25
Pages
3889-97
Language
English
Region
England
NLM ID
0411011
PMCID
PMC317867
Subset
IM
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