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. 2021 Jan 8;12:144. doi: 10.1038/s41467-020-20418-3

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© The Author(s) 2021

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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Fig. 5 — a BiG-SCAPE analysis network of frs and 2716 NRPS BGCs, obtained from a global BiG-SLiCE query against all non-fragmented NRPS from the BiG-FAM database (distance of d < 1400) at distance cutoff 0.5. The frs BGCs from C. vaccinii and “Ca. B. crenata” (red) do not cluster with any other BGC. b Alignment of frs and their 4 closest BGCs from the BiG-SCAPE analysis in Fig. 5a. Color intensity denotes the degree of homology to the respective protein of the frs BGC. Red: frsD (NRPS), blue: frsB (MbtH-like protein), yellow: frsC (dehydrogenase), green: frsH (hydroxylase). None of the listed BGCs contains homologues to frsC or frsH. Alignment adapted from Corason⁴⁵. c Phylogenetic tree of C_starter domains. Taxonomy of clades is indicated. The scale bar represents 20 substitutions per 100 amino acids. d Phylogenetic tree of NRPS TE domains. The observed mode of peptide release is indicated. The scale bar represents 50 substitutions per 100 amino acids.