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. 2019 Jun 17;85(13):e00552-19. doi: 10.1128/AEM.00552-19

FIG 2.

FIG 2

Multiple-sequence alignments of GH30-7 and GH30-8 xylanases. Amino acid sequences of T. cellulolyticus Xyn30A (NCBI protein accession no. GAM43270), T. cellulolyticus Xyn30B (GAM36763), T. reesei XYN IV (AAP64786), T. reesei XYN VI (EGR45006), Erwinia chrysanthemi EcXynA (AAB53151), and Bacillus subtilis BsXynC (CAA97612) were aligned using the Clustal Omega server (46). The features are shown as follows: a putative N-terminal signal peptide of Xyn30A (highlighted in black), conserved Arg residues in GH30-7 (highlighted in red), putative N-glycosylation sites of Xyn30A (arrows), catalytic Glu residues (highlighted in gray), Phe-201 and Gln-272 of Xyn30A and corresponding residues in GH30-7 (red characters), conserved Arg residues in GH30-8 (red box), and a β2-α2 loop in Xyn30B (blue characters). The signal sequence was predicted using the SignalP 4.1 server in sensitive mode for D-cutoff values (http://www.cbs.dtu.dk/services/SignalP/). N-Glycosylation sites were predicted using the NetNglyc server (http://www.cbs.dtu.dk/services/NetNGlyc/).