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. 2017 Jun 16;7:3700. doi: 10.1038/s41598-017-03927-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Domain architecture of CBM containing polypeptides identified in P. Polymyxa A18 genome. The numbering above the polypeptides shows the amino acid positions of the module boundaries as determined by HMM scan search. CBMs are color coded according to the previous knowledge on their binding affinity and categorized on the basis of (a) cellulose binding, (b) hemicellulose binding and (c) starch binding. Black and yellow boxes represent a potential signal sequence and the catalytic domain, respectively.