Fig. 1From: Bioinformatic and literature assessment of toxicity and allergenicity of a CRISPR-Cas9 engineered gene drive to control Anopheles gambiae the mosquito vector of human malariaSequence alignment between hCas9 and VapC. The domains within the hCas9 protein are illustrated in colour in the top box graphic [43], with all numbers corresponding to amino acids in hCas9, and regions of alignment to VapC (green box graphic) indicated by the dotted lines. From N- to C-terminus of hCas9, domains are “3 × FLAG” (coloured brown): FLAG epitopes in three tandem repeats positioned at the N-terminus of hCas9; “NLS” (purple): Nuclear localization signal; “RuvC-I” (red): RuvC domain I; “Arg” (silver): Arginine-rich domain; “Alpha-helical lobe” (orange); “RuvC-II” (red): RuvC domain II; “HNH” (blue): NHN nuclease domain; “RuvC-III” (red): RuvC domain III; “Topo” (dark grey): topo-homology domain; “CTD” (yellow): C-terminal domain [43]. Red triangles indicate catalytic residues in the RuvC-III domain [43]. Amino acid sequence alignments between hCas9 and VapC are shown below box graphics, with blue- and red- coloured amino acids from NHN and RuvC-III domains of hCas9, respectively, and VapC amino acids shown in green below [43]. Identical amino acids between both proteins are indicated by asterisksBack to article page