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. 2010 Jun 1;107(24):10955–10960. doi: 10.1073/pnas.1000823107

Fig. 2.

Fig. 2.

Alignment of the pheromone biosynthetic reductase from Yponomeuta evonymellus (Yev-pgFAR) and functional FAR proteins from eukaryotic organisms: OnuE, Ostrinia nubilalis (GenBank accession no. FJ807735); Bmo, Bombyx mori (GenBank accession no. BAC79426); Hsa, Homo sapiens (GenBank accession no. AAT42129); Ath, Arabidopsis thaliana (GenBank accession no. NP567936). Sequence alignments were computed in ClustalW (39) and edited in BOXSHADE (http://www.ch.embnet.org/index.html). Identical amino acid residues and conservative substitutions are shaded in black or gray, respectively. The FAR structural elements include a N-teminal Rossmann-fold NAD(P)(+)-binding domain (black box) and the NADH-binding motif (double underline) as well as a Sterile protein domain (thick black line). Yev-pgFAR was isolated using the 1s and 3as oligonucleotide primers (arrows).