Fig. 7

Ku70 and Ku80. a Domain model of A. vaga Ku70 A and B ohnologs, with sliding window analysis of nonsynonymous (Ka) difference (solid line) and ratio of nonsynonymous to synonymous differences (Ka/Ks, dashed line) between AvKu70A1 and B1. The alignment on the upper left shows the region where Ka/Ks > 1 near the N-terminus; the alignment to the lower right shows the SAP domains compared to human Ku70. Predicted sumoylation sites are in red, predicted acetylation sites are highlighted in blue. b Domain model of A. vaga Ku80 A and B ohnologs, with sliding window analysis of Ka and Ka/Ks. The alignment in the upper left shows the Q₃E₄Q₈ track at the terminus of the α/β domain present in copy A and not in B. c Crystal structure PDB 1JEY, human Ku70 (yellow) Ku80 (red) heterodimer complexed with DNA (grey). d Three views of the superposition of the predicted structure of A. vaga Ku70A1 (purple) and A. vaga Ku70B1 (green). The N terminal region under putative positive selection and the SAP domain are indicated in red and blue for Ku70 A1 and B1, respectively. First orientation is the same as in (c), second is an elevated view (45° rotation along horizontal axis), third is a top view (90° rotation along horizontal axis). e Superposition of the predicted structures of A. vaga Ku80A1 (blue) and Ku80B1 (copper) in the same orientation as in (c). f Differential expression of A. vaga Ku70 A and B and Ku80 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