Copyright information:Taken from "RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51"Nucleic Acids Research 2006;34(18):5081-5092.Published online 20 Sep 2006PMCID:PMC1636435.Published by Oxford University Press 2006 () Amino acid identities and similarities are indicated by dark blue and gray squares, respectively. Just the C-terminal domains of RAD51AP1 and of RAD51AP2 are shown. Under the sequences are the original residues that were mutated by site-directed mutagenesis. The underlined mutated residues significantly reduce the interaction with RAD51 (see panels B and C). Species abbreviations are as follows: Hs—; Mm—; Gg—. () Interactions in the Y2H system between RAD51 (i.e. pEG960) and both RAD51AP1 (i.e. pOK31, with all of RAD51AP1) and site-specifically mutated RAD51AP1 (in pOK31). Results are the average from three different colonies, with the standard error of the mean. () Interactions in the Y2H system between RAD51 (i.e. pEG960) and both RAD51AP2 (i.e. pDS439; pGBKT7-RAD51AP2-C33) and site-specifically mutated RAD51AP2 (in pDS439). Results are the average from two different colonies, with the standard error of the mean. * Indicate