Sequence analysis of the PDIR non-catalytic domain.

<p>(A) Occurrence of the domain in protein disulfide isomerases and other proteins. Human ERp57 is shown for comparison. Catalytic motifs are shown in catalytically-active thioredoxin-like domains. (B) Rooted phylogenetic tree of proteins shown in panel (A). Sequences labeled WUBG_02370 and RNA methyltransferase are proteins from parasitic nematodes <i>Wuchereria bancrofti</i> (EJW86719) and <i>Brugia malayi</i> (XP_001896925); mosquito PDIR is from <i>Aedes aegypti</i> (XP_001659136). The N-terminal catalytic domain of ERp57 was used for the phylogenetic tree. The figure was generated with ClustalW <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062021#pone.0062021-Thompson1" target="_blank">[29]</a> and TreeViewPPC <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062021#pone.0062021-Page1" target="_blank">[30]</a>. (C) Sequence alignment of the non-catalytic domain from PDIR proteins from human (NP_006801), rabbit (XP_002716857), rattlesnake (AFJ50881), chicken (XP_422097), zebrafish (XP_001107048), frog (XP_001086600), fly (XP_609645), and sea urchin (XP_001200801) and the related sequence from <i>Brugia malayi</i> RNA methyltransferase (XP_001896925). The consensus sequence is shown below; the secondary structure elements are above the sequence.