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. 2020 Oct 21;10(10):200197. doi: 10.1098/rsob.200197

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© 2020 The Authors.

Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 1. — Molecular characterization of Se-Duox. (a) Functional domain analysis of Se-Duox. Domains were predicted using HMMER (https://www.ebi.ac.uk) and Pfam (http://pfam.xfam.org). Predicted domains include ‘Pox’ for peroxidase, ‘EF’ for calcium-binding EF hand, ‘Ferric-reduct’ for ferric chelate reductase, ‘FAD’ for FAD-binding domain and ‘NAD’ for NAD-binding domain. (b) Phylogenetic analysis of Se-Duox with other insect dual oxidases based on their amino acid sequences. The tree was generated by the neighbour-joining method using MEGA 6.0. Bootstrapping values were obtained with 1000 repetitions to support branch and clustering. Amino acid sequences were retrieved from GenBank. Accession numbers of genes are shown in electronic supplementary material, table S2.