Figure 5
From: Gene organization, evolution and expression of the microtubule-associated protein ASAP (MAP9)
ASAP possesses an MIT-like domain. Multiple sequence alignment of selected MIT domain containing proteins [34] with ASAP. The consensus is indicated below the alignment: h, p, + and - indicate hydrophobic, polar, positively and negatively charged residues. Hydrophobic residues are highlighted in blue, polar residues in orange, positive residues in red and negative residues in purple. The secondary structure prediction at the bottom shows that this ASAP region is almost exclusively composed of helix (H). Conserved positions of (+) and (-) amino acids are also indicated in Fig. 2C.