[Amino acid sequence analysis of barley stripe mosaic viral proteins: tentative identification of viral serine proteases].
Analysis of amino acid sequences of barley stripe mosaic virus (BSMV) proteins revealed the pentapeptide GDSGG, the sequence unique for catalytic centers of serine chymotrypsin-like proteases, in protein p14 encoded by open reading frame 4 of RNA beta. Computer-assisted comparisons revealed a statistically significant similarity between amino acid sequences of p14 and chymotrypsin-like proteases. The catalytic His and Asp residues tentatively identified in p14 together with the Ser residue of the GDSGG sequence, presumably, constitute the "catalytic triad" characteristic of chymotrypsin-like proteases. Based on these observations and on the presence of a potential N-proximal transmembrane domain in p14, this protein may be suggested to be a serine protease involved in processing of the replicase precursor within a membrane-bound replication complex of BSMV.
Gorbalenia
A E
AE
Kunin
E V
EV
Donchenko
A P
AP
Blinov
V M
VM
D000595:Amino Acid Sequence; D002523:Edible Grain / Q000382:microbiology*; D001467:Hordeum / Q000382:microbiology*; D008969:Molecular Sequence Data; D009029:Mosaic Viruses / Q000201:enzymology / Q000235:genetics*; D012367:RNA, Viral / Q000032:analysis; D012697:Serine Endopeptidases / Q000032:analysis*; D014764:Viral Proteins / Q000235:genetics*
D012367:RNA, Viral; D014764:Viral Proteins; D012697:Serine Endopeptidases
Analiz aminokislotnykh posledovatel'nosteĭ belkov virusa shtrikhovatoĭ mozaiki iachmenia: predpolozhitel'naia identifikatsiia virusnoĭ serinovoĭ proteazy.