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 () Comparing the cDNA sequence we have determined with the genomic sequence in GenBank, it was determined that RAD51AP2 consists of one very long exon followed by two short exons, the last of which completely encodes the RAD51-interacting domain. () The amino acid sequence of the entire human RAD51AP2 proteins predicted from our cDNA sequence (GenBank accession # DQ860102). Residues similar to a Walker A-type nucleotide-binding motif in human RAD51AP2 are in the light gray box. The long underlined region is missing in the mouse homolog, and the short black boxed residues are the two boundaries among the amino acids encoded by the three exons. The C-terminal 33 amino acids (C33) in the red box are sufficient for RAD51-interaction in the Y2H system.