Fig. 6
From: Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2
Multiple amino-acid sequence alignment of the serratiopeptidase from S. marcescens AD-W2, PRZN_SERME serralysin from S. marcescens (E-15) with 100% sequence identity, PRZN_SERMA Serralysin from S. marcescens with 98.6% sequence identity, 0A240AD01_SERFI Serralysin from S. ficaria with 92.6% sequence identity, D4E064_SEROD Serralysin from S. odorifera DSM 4582 with 82.8% sequence identity and E0SC28_DICD3 Secreted protease A from Dickeya dadantii with 64.8% sequence identity. The protein sequence from serratiopeptidase was aligned to see the similarities, differences, and conservation of various amino acid residues using multiple sequence alignment. The alignment was carried out by using Clustal W platform in Seaview software