Abstract
The genome sequence of the rabies-related virus Mokola virus (genus Lyssavirus) has been completed by sequencing the L gene, which consists of 6384 nucleotides encoding a 2127 amino acid polymerase. Alignment of the Mokola virus L protein with other polymerases from the virus order Mononegavirales defined three domains: a divergent NH2-terminal domain, a highly conserved central domain carrying most of the functional motifs and a COOH-terminal domain with alternating conserved and divergent regions. A statistical study outlined the stringency of conservation of glycine, acidic (D, E) and basic (K, R, H) amino acids in polymerases, particularly as key residues of the conserved motifs.
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