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. 2016 Jul 18;6:29927. doi: 10.1038/srep29927

Figure 1. Protein sequence alignment of SexpgFAR I and SexpgFAR II with B. mori (BmopgFAR) (GenBank accession no. BAC79426), O. scapularis (OscpgFAR) (ACJ06520) B. anynana (BanpgFAR) (AGD98719) and H. assulta (HaspgFAR) (JF709977).

Figure 1

The sequence alignments were computed in Clustal W and edited in BioEdit (v.7.2.5). The amino acids shaded in black or grey indicate identical residues or conserved substitutions. The FAR protein structure includes an N-terminal Rossmann fold (NAD(P)(+)-binding domain) (dashed line), the NADPH-binding motif (dotted line), and the sterile domain (thick dark line).