Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes

Additional File 4:

Amino acid sequences of Nox and Duox proteins. Amino acid sequences Nox and Duox proteins of H. sapiens, B. taurus, C. familliaris, R. norvegicus, M. musculus, G. gallus, M. domestica, D. novemcinctus, O. cuniculus, X. tropicalis, D. rerio, T. rubripes, T. nigroviridis, O. latipes, C. intestinalis, S. purpuratus, D. melanogaster, A. gambiae, A. aegypti, A. mellifera, C. elegans, A. thaliana, D. discoideum, P. anserine, A. nidulans, M. grisea, F. graminearum, C. crispus and P. yezoensis are provided.

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Additional File 1:

Supplemental Figure S1. The figure provided shows loop and segment sizes joining transmembrane regions and canonical NADPH-oxidase domains

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Additional File 6:

Amino acid sequences of vertebrate Nox regulatory subunits; p47 phox, NOXO1, p67 phox, NOXA1, p22 phox. Lists of amino acid sequences Nox regulatory subunits of H. sapiens, C. familliaris, R. norvegicus, M. musculus, G. gallus, X. tropicalis, D. rerio, T. rubripes, T. nigroviridis are provided.

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Additional File 11:

Exceptions of amino acid residues conserved in all Nox/Duox proteins. The data provided show exceptions of the 68 residues conserved in all Nox/Duox proteins that are indicated by asterisks in Figure 6.

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Additional File 2:

Supplemental Figure S2. The figure provided shows sequences of EF-hand motifs in Nox5, Duox, plant Nox, and NoxC

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Additional File 8:

Alignment of EF-hand regions of plant Nox, NoxC, Nox5, and Duox. Alignment of EF-hand region of plant Nox, NoxC, Nox5, and Duox are provided. EF-hand motif regions and non-EF-hand "helix-loop-helix (HLH)" structure regions are shown.

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Additional File 9:

Amino acid sequences of ferric reductase (FRE) proteins of fungi and alignment of FRE protein and human Nox2 protein sequences. Amino acid sequences of FRE of A. nidulans, Saccharomyces cerevisiae, Schizosaccharomyces pombe and alignment of FRE and human Nox2 proteins are provided.

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Additional File 12:

Additional methods information. Methods information about gene identification, estimates of substitution rates, generation of point mutations, and Western blot analysis are provided.

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Additional File 5:

Alignment of Nox-domains of Nox and Duox proteins. Amino acid sequences of Nox and Duox orthologs were trimmed to the length corresponding to human Nox2 and aligned. Sixty-eight amino acid residues conserved among all Nox and Duox proteins (shown in Figure 6) are indicated by asterisks below the alignments.

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Additional File 10:

Abbreviation of gene names in Figure 3. Names of the marker genes used in Figures 3 are provided.

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Additional File 3:

Supplemental Figure S3. The figure provided shows substitution rates of vertebrate Nox/Duox and Nox regulatory proteins

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Additional File 7:

Alignment of vertebrate p47 phox, NOXO1, p67phox, NOXA1, and p22phox proteins to estimate substitution rates. Amino acid sequences of p47phox, NOXO1, p67phox, NOXA1 and p22phox were aligned. These alignments were used to estimate evolutionary substitution rates in vertebrate orthologs of Nox regulatory subunits.

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