Figure 3

Sequence (lanes 1 to 3) and secondary structure (lanes 4 to 6) comparisons among (a) MCP and (b) SfAV1a ORF061 orthologs from CsIV (lanes 1 and 4, typed in black), DpAV4 (lanes 2 and 5, typed in blue) and SfAV1a (lanes 3 and 6, typed in purple). Conserved positions among the amino acid sequence of CsIV and those of DpAV4 and SfAV1a are highlighted in grey. Secondary structures in the three SfAV1a ORF061 orthologs were calculated with the Network Protein Sequence Analysis at http://npsa-pbil.ibcp.fr/ and the statistical relevance of the secondary structures were evaluated with Psipred at http://bioinf.cs.ucl.ac.uk/psipred/. C, E and H in lanes 4 to 6 respectively indicated for each amino acid that it is involved in a coiled, b sheet or a helix structure. Using default parameters of Psipred, upper case letters indicate that the predicted secondary structure is statically significant in Psipred results. Significant secondary structures are highlighted in yellow. In (a), the comparisons were limited to three of the seven conserved domains (Additional file 3a, b and 3c), the 2, 5 and 7. Indeed, classical in silico methods appeared to be inappropriate to predict statistically significant secondary structures in conserved structural protein rich in b strand such as iridovirus and ascovirus MCP. In contrast, a complete and coherent domain comparison was obtained by HCA profiles (fig. S3b, c).