Figure 2.

Sequence alignment of six secreted phospholipase A₂ from different sources: human synovial (UniProtKB AC: P14555), bovine pancreatic (UniProtKB AC: P00593), B. asper (UniProtKB AC: P20474), E. carinatus (UniProtKB AC: Q7T3S7), N. atra (UniProtKB AC: P00598) and N. sputatrix (UniProtKB AC: Q92085). Overall, highly conserved residues can be found in the active site, Ca²⁺ binding loop and disulfide bonds. Amino acids residues that have an identity threshold above 40% are colored according to the ClustalX color scheme: hydrophobic (blue), positive charge (red), negative charge (magenta), polar (green), cysteines (pink), glycines (orange), prolines (yellow), aromatic (cyan), and unconserved (white). The numbering shown is that from Renetseder et al.³⁴ Green triangles indicate the locations of the residues involved in the calcium-binding, while yellow stars indicate those involved in the active site.