caa a22 4500 465795188 CHVBK 20180323112035.0 cr unu---uuuuu 170327e19900901xx s 000 0 eng 10.1007/BF00265630 doi (NATIONALLICENCE)springer-10.1007/BF00265630 Sequence of the 3′ half of the Murray Valley encephalitis virus genome and mapping of the nonstructural proteins NS1, NS3, and NS5 [Elektronische Daten] [Eva Lee, Carol Fernon, Richard Simpson, Ronald Weir, Charles Rice, Lynn Dalgarno] We have determined the nucleotide sequence of the 3′-terminal half of the RNA genome of Murray Valley encephalitis virus (MVE) using seven overlapping cDNA clones; an estimated 80-90 nucleotides at the extreme 3′-end remain to be sequenced. In conjunction with previous sequence data for the 5′ half (16), we can conclude that the MVE genome contains a long open reading frame of 10,302 nucleotides that encodes a polyprotein of 3434 residues. Comparison of the MVE deduced amino acid sequence with that of other flaviviruses shows that MVE is most closely related to Japanese encephalitis virus, consistent with serological studies. Using N-terminal amino acid sequence analysis, three nonstructural proteins (NS1, NS3, and NS5) have been identified and mapped on the MVE genome. MVE NS3 contains sequence motifs suggesting that its amino terminus may function as a serine protease. The central region of NS3 (in the linear amino acid sequence) has motifs that are found in NTP-binding proteins and helicases. MVE NS5 contains a conserved Gly-Asp-Asp sequence that is thought to be essential for RNA-dependent RNA polymerases. Kluwer Academic Publishers, 1990 flavivirus nationallicence nucleotide sequence nationallicence genome mapping nationallicence nonstructural proteins nationallicence N-terminal sequencing nationallicence sequence homology nationallicence Lee Eva Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut Fernon Carol Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut Simpson Richard Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research (Melbourne Branch), Parkville, Victoria, Australia aut Weir Ronald Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut Rice Charles Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, USA aut Dalgarno Lynn Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut Virus Genes Kluwer Academic Publishers 4/3(1990-09-01), 197-213 0920-8569 4:3<197 1990 4 11262 https://doi.org/10.1007/BF00265630 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00265630 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lee Eva Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut NATIONALLICENCE 700 1- Fernon Carol Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut NATIONALLICENCE 700 1- Simpson Richard Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research (Melbourne Branch), Parkville, Victoria, Australia aut NATIONALLICENCE 700 1- Weir Ronald Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut NATIONALLICENCE 700 1- Rice Charles Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, USA aut NATIONALLICENCE 700 1- Dalgarno Lynn Biochemistry Department, Faculty of Science, The Australian National University, Canberra, Australia aut NATIONALLICENCE 773 0- Virus Genes Kluwer Academic Publishers 4/3(1990-09-01), 197-213 0920-8569 4:3<197 1990 4 11262 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer