Using the MEME suite (), we first calculated the most common sequence domains. We obtained 10 domains, but kept only the 3 most statistically significant domains (with the lowest E-values) for each subset. The results are illustrated in Figure . For the selective peptides, the most popular domain was an 8-residue long domain found in the C-terminal region of 13 sequences (30%), the second domain was a 15-residue long domain within 7 sequences (16%), and the last 14-residue long domain capped the N-terminal and intermediate region(s) of 5 sequences (~12%) -Figure . The three domains were enriched in valine, alanine, glycine and isoleucine, in agreement with our analysis AAC (fA,G,V,I = 0.355 vs. 0.244 -Table ). The most popular domain among non-selective membranolytic peptides was an 11-residue long domain that capped the N-terminal region for a third of the sequences (33, ~35%) -Figure . It was also the sole domain enriched in phenylalanine, as measured in Table . The second popular domain contained 15 residues and leaned towards the C-terminal region for 6 non-selective sequences (~6%, Figure ). Likewise, the last ACP-NS domain was 20-residue long and was located in the C-terminal region of 4 sequences (~4%, Figure ). Both domains were headed with polar amino acids. With regards to the nature of the residues, we discerned that both ACP-S and ACP-NS peptides alternated between hydrophobic residues (in green), charged residues (mainly positive, in purple) and occasionally, they presented polar amino acids (in orange), clustered into short domains of 2-4mers. Such alternates are characteristic of amphipathic membrane-active peptides. ) and nonselective peptides (D-F) using the MEME suite (). Hydrophobic residues, charged residues and polar residues are depicted in green, purple and orange, respectively.