Alignment of the deduced amino acid sequence of the Northern pike Elovl5 with orthologs of other members of the Protacanthopterygii lineage. The amino acid alignment was performed using the BLOSUM62 matrix from BioEdit, and identity/similarity was calculated based on a 60% identity threshold. Identical residues are shaded in grey, and altered residues are shaded in white if they exhibit the same chemical qualities, or black if they do not. Outlined are the HXXHH histidine box, and the endoplasmic reticulum retention signal (ER); the five putative transmembrane domains (I-V) are dash-underlined; the predicted “catalytic site” is indicated by the solid arrow above the sequences; and an asterisk indicates each of the 17 amino acid residues conserved across Elovl proteins .
Carmona-Antoñanzas et al. BMC Evolutionary Biology 2013 13:85 doi:10.1186/1471-2148-13-85