Comparison of the primary sequence of spring viremia of carp virus M protein with that of vesicular stomatitis virus.
The nucleotide sequence of Spring viremia of carp virus mRNA coding for the matrix protein (M) has been determined from a complete DNA copy cloned in the Escherichia coli plasmid pBR322. The clone is 710 nucleotides long and, excluding the 3' homopolymeric end (representing the mRNA polyadenylic acid sequence), encodes a protein of some 223 amino acids (25,600 Da). The protein has more basic than acidic amino acids and no significant amino- or carboxy-terminal hydrophobic domains. The predicted amino acid sequence of the M protein of Spring viremia of carp virus can be aligned with that of vesicular stomatitis virus, revealing a significant amount of homology (28%). The carboxy-terminal regions of the two proteins exhibit much less homology than their amino termini.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001483:Base Sequence; D002347:Carps / Q000382:microbiology; D004247:DNA; D009693:Nucleic Acid Hybridization; D012333:RNA, Messenger / Q000235:genetics; D012367:RNA, Viral / Q000235:genetics; D012209:Rhabdoviridae / Q000032:analysis* / Q000235:genetics; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis* / Q000235:genetics; D014763:Viral Matrix Proteins; D014764:Viral Proteins / Q000032:analysis / Q000235:genetics; D014766:Viremia
D000596:Amino Acids; D012333:RNA, Messenger; D012367:RNA, Viral; D014763:Viral Matrix Proteins; D014764:Viral Proteins; D004247:DNA