Figure 1

Sequence logo representation of the ependymin protein family. Overall comparison among all the 74 ependymin protein sequences used in this study in which the height of a given letter (amino acid residue) represents its frequency of occurrence at that particular site. High variability is observed in the amino (N) and carboxyl (C) terminals. Similarity among ependymins increases noticeably at the domain region (underlined with a solid black bar). Diagnostic cysteines putatively involved in disulfide bonding are indicated by arrowheads above the letter (▼). Asterisks (*) above the letters denote other invariable or almost invariable residues. Empty sites represent regions of the alignment where gaps were introduced in most of the sequences. The approximate posterior mean of the ω ratio (selective pressure) at each codon site calculated under model M3 (discrete) for all the ependymin proteins is shown below the WebLogo. The deeper furrows in the ω plot identify the amino acid sites that are under stronger purifying selection.