Skip to main content
Fig. 2 | BMC Ecology and Evolution

Fig. 2

From: Molecular evolution of hatching enzymes and their paralogous genes in vertebrates

Fig. 2

Comparisons of the primary structure of astacin-superfamily proteases. A Multiple alignments of amino acid sequences in representative astacin proteases. Only the sequences important for distinguishing the astacin proteases, the cysteine residues for disulfide bonds (highlighted with black), and the consensus sequence in the astacin-superfamily (highlighted with gray) are shown. The two Cys residues located at the NH2 terminal region of the protease domain (*) were highly conserved in all C6ast genes, including newly identified sequences. The exon–intron structure (intron phase) in the protease domain was also highly conserved, except for euteleostean HEs that are retrocopied genes. The position of the amino acids in coelacanth C6ast is shown above the alignment. B Schematic diagram of domain structure evolution of C6ast. The shape of the phylogenetic tree is illustrated based on previous studies and the tree shape in Additional file 1: Fig. S1. The black ellipses at the tips of the tree indicate the domain structure of each gene subfamilies (protease: protease domain, CUB: CUB domain, MAM: MAM domain, E: EGF-like domain)

Back to article page