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. 2016 Jan 8;6:1489. doi: 10.3389/fmicb.2015.01489

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Copyright © 2016 Lachnit, Thomas and Steinberg.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A–C) Comparison between the Asterionellopis glacialis (“Agla”) RNA virus and the D. pulchra RNA virus. (A) The genomes of both viruses encode two polyproteins, one replication associated and one structural polyprotein. (B) Protein domain analysis using SMART (Simple Modular Architecture Research Tool) and sequence alignment of the replication associated polyprotein shows a similar structural organization consisting of RNA helicase or replication associated protein AAA, transmembrane proteins (blue boxes) and RdRP. Low complex regions are shown in pink. (C) Protein domain analysis and sequence alignment of the structural polyprotein shows four structural protein domains Rhv, DicistroVP4, Calici coat, and CRPV capsid. The Calici coat domain overlaps with the second Rhv domain of the Agla RNA virus. Sequences of conserved protein domains are highlighted in boxes.