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. 2019 Jun 17;9:8651. doi: 10.1038/s41598-019-44494-8

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© The Author(s) 2019

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 organisation of the six Verticillium nonalfalfae RNAi proteins. (a) VnaAGO1, (b) VnaAGO2, (c) VnaDCL1, (d) VnaDCL2, (e) VnaRdRP1, and (f) VnaRdRP2. In the AGO proteins, the following domains were identified: ArgoN – the N-terminal domain of eukaryotic AGOs; DUF – domain of unknown function; PAZ – Piwi-Argonaute-Zwille domain of unknown function in AGO and DCL proteins; PIWI – the double-stranded RNA-guided catalytic domain of AGOs. The DCL proteins contained the following domains: DEAD – the N-terminal DEAD-like helicase; Hel_C – the C-terminal helicase; D_dimer – the Dicer dimerisation domain; RIBOc – the C-terminal ribonuclease III domain. Both RdRP proteins contained the typical RNA-dependent RNA polymerase domain. For all amino acid sequences, the domains were searched for using the Conserved Domain Database, Pfam, and SMART and visualised with IBS (Illustrator of Biological Sequences⁵⁵; http://ibs.biocuckoo.org/online.php).