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. 2017 Jun 6;7:2842. doi: 10.1038/s41598-017-03142-9

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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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Sequence alignment of Sb-PDE with hypothetical proteins from Sphingobium japonicum (accession no. WP_006949123), Altererythrobacter marensis (WP_047806715), Hirschia baltica (WP_015828317) and Sphingobacterium sp. ML3W (WP_051959780). The numbers on the right are the residue numbers for each amino acid sequence. Identical residues and amino acid substitutions with low and high similarities are indicated by asterisks, dots and double dots, respectively. The putative signal peptide of Sb-PDE is in bold. The four conserved motifs in the PHP domain are underlined. The consensus sequence of each motif²⁴ is shown above the alignment; h indicates hydrophobic residues (A, C, F, I, L, M, V, W or Y), s indicates small residues (A, C, S, T, D, N, V, G or P), p indicates polar residues (D, E, H, K, N, Q, R, S or T), o indicates hydroxy residues (S or T), and ‘−’ indicates negatively charged residues (D or E).