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![[Figure 2]](wa5073fig2mag.jpg)
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Figure 2
Multiple sequence alignment of Cwp8433–497 and the highest unique BLAST results. All are cysteine proteases that possess a putative lectin-like domain. The alignment was performed using ClustalW2 (Larkin et al., 2007  ) and rendered with ALINE (Bond & Schüttelkopf, 2009). Strictly conserved residues are shown in yellow, medium to well conserved residues are in orange and slightly conserved residues are in blue. The secondary structure of Cwp84, as predicted by DSSP (Kabsch & Sander, 1983), is also shown coloured according to Fig. 1. 310-Helices and β-bridges are displayed in the same way as α-;helices and β-strands, but are not numbered. Active-site residues (Gln110, Cys116 and His262) are indicated with pink stars, the propeptide cleavage site (Lys91-Ser92) is indicated with a black arrow and the occluding loop and PBL regions are indicated with blue and red triangular brackets, respectively. Sequences are taken from the following NCBI GenBank references: Cwp84, NC_009089; Eubacterium CAG:202, CDC03302; Ruminococcus bromii, YP_007780613; Eubacterium CAG:581, CDF12829; Clostridium hiranonis, WP_006441026; Peptostreptococcus stomatis, WP_007788460; P. anaerobius, WP_002842957; Anaerococcus hydrogenalis, WP_004816163; Methanosarcina mazei, NP_632235. The proteins from C. hiranonis, P. stomatis and P. anaerobius possess three putative Pfam 04122 repeats and thus are likely to be S-layer proteins performing similar functions to Cwp84. |
![[Figure 2]](wa5073fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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