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. 2019 Aug 14;15(8):e1008086. doi: 10.1371/journal.pgen.1008086

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© 2019 Grognet et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 1 — (A) Domain architecture of P. anserina putative DNA methyltransferase PaRid. The catalytic domains contain 10 conserved motifs (I—X) and a target recognition domain (TRD) located between the motifs VIII and IX. The amino acid length is indicated. (B) Domain architecture of DNA methyltransferase proteins (DMT). The functional domain analysis was performed using InterProScan and visualized using IBS. Mus musculus: MusmuDnmt1: NP_001300940.1, MusmuDnmt2: NP_034197.3, MusmuDnmt3A: NP_031898.1; Ascobolus immersus, AscimMasc1 (AAC49849.1), AscimMasc3; Aspergillus nidulans AspniDmtA: XP_664242.1, Neurospora crassa NeucrRid: AAM27408.1, NeucrDim2: XP_959891.1; Podospora anserina PaDim2: Pa_5_9100; PaRid: Pa_1_19440; Trichoderma reesei TrireDim2 XP_006964860.1; TrireRid: AEM66210.1. Cytosine-specific DNA methyltransferase domains: PF00145, PR00105, PS51679, PS00095, PS00094; protein-DNA interaction domains: bromo-associated homology (BAH) domain PS51038, Replication foci targeting sequence (RFTS) PF12047, Zinc finger motif (CXXC) PS51058, PWWP domain (PF00855). Because its sequence is too divergent, PaDnmt5 (Pa_4_2960) was not included.