The constitutive transport element (CTE) of the simian type D retroviruses overcomes nuclear retention and allows nuclear export of unspliced viral RNAs by recruiting TAP, a host factor which is thought to be required for export of cellular mRNAs. In this report, we show that the first 372 amino acid residues of TAP, comprising a stretch of leucine‐rich repeats, are both necessary and sufficient for binding to the CTE RNA and promoting its export to the cytoplasm. Moreover, like the full‐length protein, this domain migrates to the cytoplasm upon nuclear co‐injection with the CTE RNA. Together, these results indicate that the CTE‐binding domain includes the signals for nuclear export. We also describe a derivative of TAP that bears a triple amino acid substitution within the CTE‐binding domain and substantially reduces the export of mRNAs from the nucleus. This provides further evidence for a role for TAP in this process. Thus, the CTE‐binding domain of TAP defines a novel RNA‐binding motif which has dual functions, both recognizing the CTE RNA and interacting with other components of the nuclear transport machinery.