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Fig. 7 | BMC Evolutionary Biology

Fig. 7

From: Phylogenetic analyses reveal molecular signatures associated with functional divergence among Subtilisin like Serine Proteases are linked to lifestyle transitions in Hypocreales

Fig. 7

Functional divergence in Subtilisin (S08.005) protein sequences. a Subtilisin structure of a member (fx|XP5977|Fusarium oxysporum) of the “Nectriaceae” clade is shown. The amino acid residues that experienced site-specific rate shift (RVS) and/or type II divergence and fell into the catalytic triad/active sites/substrate binding sites of the enzyme are highlighted. The catalytic triad is shown by a triangle (brown colour). Predicted active sites are shown in yellow colour; substrate binding sites are shown in blue colour. Amino acids highlighted in brown colour experienced type-II divergence and was present in an active site and a binding site. b Subtilisin structure of a member (bb|XP2612|Beauveria bassiana) of the “Cordycipitaceae/Clavicipitaceae” clade is shown. The amino acids residues that experienced site-specific rate shift (RVS) and/or type II divergence and fell into the catalytic triad/active sites/substrate binding sites of the enzyme are highlighted. Predicted catalytic triad is shown by a triangle (red in colour); Active sites in cyan colour, Substrate binding sites in magenta colour. Amino acid highlighted in red experienced both RVS and type-II divergence and was present in one of the active sites. c Subtilisin structure of a member (pl|XP5939|Purpureocillium lilacinum) of the “Ophiocordycipitaceae” clade is shown. The amino acids residues that experienced site-specific rate shift (RVS) and/or type II divergence and fell into the catalytic triad/active sites/substrate binding sites of the enzyme are highlighted. Predicted catalytic triad is shown by a triangle (black in colour); Active sites in yellow colour, Substrate binding sites in magenta colour. Amino acid highlighted in black experienced type-II divergence and was present in one of the active sites

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