Figure 3

Meg protein secondary structure has changed over the maize-specific gene family expansion. The secondary structures of Meg proteins were predicted using different algorithms on the Network sequence analysis server (NPS@, Network Protein Sequence Analysis, http://npsa-pbil.ibcp.fr). The α-helix, β-strand and disordered loop regions are denoted by the longest, the second longest and the second shortest bars, respectively. The shortest bars represent residues with ambiguous states. The symbols of positively selected amino acids are shown above the corresponding bars. Gaps were introduced according to the amino acid sequence alignment in order to align secondary structural elements for visualization. The figure illustrates amino acid sequences of Meg genes whose coding sequences are intact.