Unexpected close relationship between the large nonvirion proteins of filamentous potexviruses and spherical tymoviruses.
The amino acid sequences of the large proteins of potexviruses and tymoviruses were aligned. It was shown that three domains of these proteins display significant similarity between the two virus groups. In contrast to central (putative NTPase-helicase) and C-terminal (putative polymerase) domains, the conservative N-terminal domain of the potexvirus/tymovirus large protein displayed no obvious similarity to the respective regions of the large proteins of other Sindbis-like viruses.
Rozanov
M N
MN
V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow.
Morozov
S Y
SY
Skryabin
K G
KG
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D009029:Mosaic Viruses / Q000235:genetics*; D010942:Plant Viruses / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D014764:Viral Proteins / Q000235:genetics*
D014764:Viral Proteins