Figure 2 | Scientific Reports

Figure 2

From: A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

Figure 2

Multiple amino acid sequence alignment analysis. The proteases used were AprA, IbaP from I. baltica (GenBank No. WP_006955586.1), IxiP from I. xiamenensis (GenBank No. WP_008487188.1), AagP from A. agri (GenBank No. WP_008985417.1), PspP6 from P. sp. 2–10 (GenBank No. ABS01328.1), AprI from P. piscicida (GenBank No. BAA18912.2), PspP28 from P. sp. A28 (GenBank No. BAG31346.1), StmPr2 from S. maltophilia (GenBank No. AEL88836.1), KerSMF from S. maltophilia (GenBank No. AGK29593.1), AprV2 from Dichelobacter nodosus (PDB No. 3LPA_A) and Pro-TK-SP from Thermococcus kodakaraensis (PDB No. 3AFG_A). Strictly conserved residues are highlighted by black background and conservatively substituted residues are boxed. The vertical arrow shows the cleavage site of the signal peptide. The horizontal arrows show the N-terminal residues. The conserved catalytic residues are indicated by black circles and the PPC truncation site of AprA is indicated by black triangle. The residues in Ca-I and Ca-II binding sites of Pro-TK-SP were indicated by black and white pentagrams, respectively. The black circles indicated the residues of Ca-I binding site in AprV2, whereas white and black diamonds showed the residues of Ca-II and Ca-III binding site in AprV2, respectively. The figure was produced using ESPript 3.0.

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