Fig. 10

XRCC4. a Domain models of AvXRCC4 A (top) and B (bottom) ohnologs showing the three regions of XRCC4, the total charge of each region, and predicted DNAPKcs phosphorylation sites (blue circles indicate sites conserved between A and B peptides, yellow circles indicate unique sites on each peptide) with sliding window analysis of nonsynonymous difference (Ka, solid line) and ratio of nonsynonymous to synonymous differences (Ka/Ks, dashed line) between copies A1 and B1. b Superposition of the predicted structures of A. vaga XRCC4A1 (blue) and XRCC4B1 (copper) showing the conserved structure of the N-terminal head region, the central helix with Ligase 4 binding regions shown in purple (XRCC4A1) and red (XRCC4B1), and the poorly conserved C terminus with 22 residues present in A1 but not in B1 shown in magenta. c Alignment of the Ligase 4 binding region in A1, B1, and human XRCC4; colons (:) indicate residues involved in binding [116]. d Differential expression of A. vaga XRCC4 A and B ohnologs entering and recovering from desiccation, compared to hydrated controls. Values are log₂ fold change of normalized counts, significance test values are listed in Additional file 1