Sequence analysis of the protein sequence of mycosin-1. (A) Sequence alignment of mycosin-1 with the B. amyloliquifaciens subtilisin BPN protein. The conserved amino acid residues are indicated in bold. The catalytic residues (D-90, H-131, and S-332, mycosin-1 numbering) are in open boxes; the oxyanion hole (N-237) is in a closed box. The mycosin-1 signal peptide cleavage site (A-21/I-22) is shaded. The arrows below the BPN sequence bracket the propeptide sequence; arrows above mycosin-1 indicate the predicted propeptide. Overlines (numbered 1–5) above the mycosin-1 sequence indicate hydrophobic regions and correspond to domains 1–5 shown in (B). (B) Hydrophobicity plot of mycosin-1.