Alignment of Ls AChE1a and Ls AChE1b proteins with other AChE from other species.
2015-05-04T03:28:31Z (GMT) by
<p>Alignment of AChE1a and AChE1b proteins from <i>Lepeophtheirus salmonis</i> (abbreviated to LS_ace1-A and LS_ace1-B) with AChE proteins from other species: <i>Cimex lectularius</i> AChE1; JN563927.1 (Cim__lec_ace1), and <i>Torpedo californica</i> AChE; CAA27169.1 (Tor_cal). By convention, numbering is that of <i>T</i>. <i>californica</i>. The three amino acids composing the catalytic triad (S200, E327 and H440) are indicated by arrows. The 14 conserved aromatic residues lining the active gorge are represented by circles. Out of these 14, 11 residues were present in both <i>L</i>. <i>salmonis</i> AChE1a and AChE1b (shown by filled circles), whereas the other 3 non conserved residues (shown by open circles) were absent in both the proteins of salmon louse. The choline binding site (W at 84) is underlined. Three interchain disulphide bridges are drawn between conserved C residues (shown by arrows). The solid box represents the canonical *FGESAG* motif, characteristic of the active site of cholinesterases. The dotted box represents the typical sequence insertion/deletion domain that easily distinguishes AChE1 and AChE2 proteins.</p>