3.3 Superimpositions and sequence comparison
The ESPript 3.0 computed the structure elements, α-amylase is highly conservd, and no amino acid mutations have been found in the homologous sequence regions and active sites (Figure 2A-left). CYP6AE76 has high sequence identities in Six substrate recognition sites (SRS) 1, SRS3, SRS4 and SRS5, and SRS2 with SRS6 shows the lowest identity. In addition, both two sequences had mutations at the WxxR site, but no mutations were found at the ExxRxxP and Heme-binding sites (Figure 2A-right). Superimpositions of each model with the template using UCSF ChimeraX v1.1 software showed a very low RMSD value of 0.130 Å for α-amylase 1 from C. pinicolalis andC. punctiferalis (Figure 2B). Similarly, a low RMSD value of 0.224 Å was observed between the superimposed CYP6AE76 3D structures ofC. pinicolalis and C. punctiferalis , respectively (Figure 2B). In addition, it can be seen from the 3D diagram that although the amino acid sequence is partially different, it does not affect the overall structural change.