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. 2021 Jun 16;12:696604. doi: 10.3389/fmicb.2021.696604

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Copyright © 2021 Shao, Shen, Wang and Qiu.

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) and the copyright owner(s) 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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Domains of HBoV1 NS proteins. HBoV1 NS1 (GenBank: AFR53039) and AAV5 Rep78 (GenBank: AAD13755) are aligned. N-terminal origin DNA binding domain (OBD; in red) and helicase domain (in purple) are diagramed. The regions positioned between the OBD and helicase domains (shown in green) are predicted to be the oligomerization signal. The C-terminal region (shown in yellow) is predicted to serve potentially transcriptional activation function. Dashed lines in the OBD indicate residues that are structured as endonuclease core/DNA binding loop (Tewary et al., 2013), and dashed rectangles in the helicase domain indicate Walker boxes (Koonin, 1993). Oligo. indicates a putative oligomerization signal. NS2, NS3, NS4, and NS1-70 proteins are diagramed in colored blocks with thin lines indicating excised aa sequences due to ligation of the neighboring exons of their mRNAs.