FIG. 4.

Amino acid sequence homology of the predicted functional domains of ANV (G-4260) with those of HAst 1 (A/88 Newcastle). (A) Putative 3C-like serine protease domains (ORF 1a). ∗∗, putative catalytic residues; !, residues implicated in substrate binding (16); ∗, identical residues; colons, similar residues. (B) Putative RNA-dependent RNA polymerase domains (ORF 1b). Consensus 1 shows amino acid residues that are conserved in at least 80% of the polymerases of supergroup I (16, 19). U, bulky aliphatic residue (I, L, M, or V); @, aromatic residue, (F, Y, or W); &, bulky hydrophobic residue (aliphatic or aromatic); ·, any residue. Residues conserved in the (putative) polymerases of all positive-strand RNA viruses of eukaryotes are in boldface. Distances between the aligned conserved motifs and from the protein termini are indicated.