The alignment of amino acid sequences of AtMIPS1 and others.

<p>The following MIPSs are shown: ScMIPS, <i>Saccharomyces cerevisiae</i>; SpMIPS, <i>Spirodela polyrrhiza</i>; OsMIPS, <i>Oryza sativa</i>; and PcMIPS, <i>Porteresia coarctata</i>. The completely conserved residues are indicated with “*<i>”</i> and those that are essentially conserved are shown with “<b>. <i>“</i></b> or “<b>: “</b>, and the amino acids are colored red, hydrophobic; green, hydrophilic; purple, positively charged; and blue, negatively charged. Elements of secondary structure with reference to the crystal structure of ScMIPS [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0115502#pone.0115502.ref061" target="_blank">61</a>] are shown as cylinders for helices, and arrows for b-strands. These elements are also colored domain by domain: red, the central domain (Met1-Val60, Gly104-Val133 and Glu439-Lys511); cyan, the NAD-binding domain (Pro61-Phe103 and Asn134-Ser310); and magenta, the catalytic domain (Gly311-Asp423). Amino acids that interacted with NAD in ScMIPS are indicated with “# “and those that interacted with 2-deoxy-glucitol-6-phosphate (analog of glucose-6-phosphate, an inhibitor of MIPS) are shown with “! “. A putative myristoylation site conserved in PcMIPS and AtMIPS1 is marked with “+ “. The region of PcMIPS (Trp174-Ser210) reportedly involved in salt tolerance [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0115502#pone.0115502.ref043" target="_blank">43</a>] is enclosed with black rectangles. Accession numbers of sequences: ScMIPS, 1JKI (Protein Data Bank); SpMIPS, Z11693; OsMIPS, AB012107; PcMIPS, SAF412340; and AtMIPS1, NM_120143.