Multiple sequence alignment of FeCH sequences.

<p>The FeCH sequences were taken from the NCBI protein database together with the <i>S. venezuelensis</i> sequence (this study); <i>Homo sapiens</i> (CAB65962), <i>Drosophila melanogaster</i> (AAC26225), <i>Saccharomyces cerevisiae</i> (EDV10759), <i>Brugia malayi</i> 1 (ADI33748), <i>Brugia malayi</i> 2 (ADI33749), <i>Acanthocheilonema viteae</i> (ADI33750), <i>Dirofilaria immitis</i> (ADI33752), <i>Onchocerca volvulus</i> (ADI33751), <i>Escherichia coli</i> (AP_001124), and <i>Bacillus subtilis</i> (NP_388894). The sequences were computationally aligned by the ClustalX program <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0058458#pone.0058458-Larkin1" target="_blank">[55]</a>. The catalytic core and the C-terminal extension are boxed by red and green dotted lines, respectively. A histidine residue reported to be critical for metal substrate binding (H263, human sequence numbering) is indicated by an inverted triangle. A cluster of three acidic residues are marked with asterisks. Two residues at the active site that were reported to be identical in all known FeCH sequences (Y276 and W310) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0058458#pone.0058458-Medlock1" target="_blank">[56]</a> are indicated by number (#) marks.