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Figure 3 | BMC Evolutionary Biology

Figure 3

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

Figure 3

Identification of highly conserved residues of Nox organizer proteins. Species names were abbreviated as follows: v-, vertebrate; Hs, H. sapiens; Cf, C. familliaris; Rn, R. norvegicus; Mm, M. musculus; Gg, G. gallus; Xt, X. tropicalis, Dr, D. rerio; Tr, T. rubripes; Tn, T. nigroviridis; Ol, O. latipes; Ci, C. intestinalis; Sp, S. purpuratus. (A) Schematic domain structures of Nox organizer are shown; PX, Phox homology; SH3, the Src homology 3; AIR, autoinhibitory region; PRR, proline-rich region; C-tail, C-terminal tail region. Orthologs that possess these domains are shown below the domains. Amino acid residues indicate conserved amino acids in all Nox-organizers. Residue numbers correspond to those of the human p47phox protein sequence. Letters in solid boxes indicate the residues that have been previously proven by mutational analyses to be essential for the human Nox2 activation [24, 68, 126]. (B) Molecular taxonomy was created comparing by the sequence spanning the PX and bis-SH3 domains. (C) Alignment of amino acid sequences of the AIR. Letters in solid boxes indicate residues previously shown to be essential for human Nox2 activation, determined by mutational analyses [20] and also key residues responsible for interactions with the bis-SH3 domain, shown by X-ray crystallography [21]. (D) Alignment of amino acid sequences of the PRR and C-tail regions. Letters in solid boxes indicate the residues that have been shown by mutational analyses to be important for binding to p67phox [18, 72]. An arrow head indicates a residue corresponding to a phosphorylation site of human p47phox [19].

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