File:F2.large-cruciviruses-ProteinConservation.jpg

English: Protein conservation in cruciviruses. (A) (Top) Distribution of domains, isoelectric point, and conservation in a consensus capsid protein. Four hundred sixty-one capsid protein sequences were aligned in Geneious 11.0.4 with MAFFT (G-INS-i, BLOSUM 45, open gap penalty 1.53, offset 0.123) and trimmed manually. The conservation of the physicochemical properties at each position was obtained with Jalview v2.11.0 (88), and the isoelectric point was estimated in Geneious 11.0.4. The region of the capsid protein rich in glycine is highlighted with a green bar. (Bottom) Structure of a cruciviral capsid protein (CruV-359) as predicted by Phyre2 showing sequence conservation based on an alignment of the 47 capsid protein sequences from the capsid protein-based clusters. (B) Conserved motifs found in cruciviral Reps after aligning all the extracted Rep protein sequences using PSI-Coffee (94). Sequence logos were generated at http://weblogo.threeplusone.com to indicate the frequency of residues at each position.