Figure 3.

Alignment of AsMASPa and AsMASPb amino acid sequences with mammalian MASP, C1r, and C1s. Multiple alignment of the amino acid sequences was performed using Clustal W software. Gaps introduced to increase identity are shown by dashes. The completely conserved residues among these eight sequences are indicated by ∗ below the sequences. The amino acid numbers of the rightmost residues of AsMASPa are shown for each lane. The N-termini of each domain are marked by/above the sequences. Three residues at the catalytic site of serine proteases ⁵²⁷H, ⁵⁷⁹D, and ⁶⁹⁰S, two cysteine residues involved in histidine loop formation (⁵¹²C and ⁵²⁸C), and the residue at the S1 specificity crevice (⁶⁸⁴D) are marked by +, #, and $, respectively. The arrow pointing downward indicates a processing site of mammalian MASP, C1r, and C1s. The line connecting ⁴⁵⁶C and ⁵⁹⁹C indicates a disulfide bond between two subunit chains.