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. 2017 Jan 6;8(1):20. doi: 10.3390/genes8010020

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© 2017 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).

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Domain architecture and catalytic activities of primase-polymerase (PrimPol). The domain architecture of PrimPol is depicted in the top panel. A helix (purple) located at the N-terminus is connected to ModN by a flexible linker and contacts the DNA major groove. ModN (blue) and ModC (orange) comprise the archaeo-eukaryotic primase (AEP) domain and contain motifs Ia, Ib, I, II, and III, required for template binding and catalytic activity. The zinc finger (ZnF) (green) contains three conserved cysteines and a histidine which coordinate a zinc ion and are required for primase, but not polymerase, activity. The replication protein A (RPA) binding domain (RBD) (red) containing RPA binding motif-A (RBM-A) and RBM-B (grey) is located at the C-terminus. A 100 amino acid (aa) scale bar is shown to the right. The catalytic activities of PrimPol are displayed below.