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Figure 4 | BMC Evolutionary Biology

Figure 4

From: Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes

Figure 4

Hypothetical function of T. rubripes C17orf39 protein as a Nox organizer protein. (A) Schematic domain structures of C17orf39 and NOXO1. Names of orthologs that possess domains are shown to the left of structures. T. rubripes C17orf39 was located in scaffold 141 (Sc 141). Abbreviations of species names and most domains are shown in Figure 3; "basic" indicates a lysine/arginine-rich polybasic region. (B) Alignments of the PRR and basic regions of C17orf39. Letters in solid boxes indicate conserved the proline residues in the PRR and lysines and arginines in the basic region. (C) Comparison of bis-SH3 domain among T. rubripes C17orf39, human NOXO1, and human p47phox. (D) Comparison of PRR and C-tail regions among T. rubripes C17orf39, human NOXO1, and human p47phox. Letters in solid boxes indicate the evolutionally conserved residues that have been identified in Figure 3 (C, D). An arrow head indicates a residue corresponding to a phosphorylation site of human p47phox. Identical residues are shown by asterisks (B-D).

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