In all organisms, regulation of gene expression must be adjusted to meet cellular requirements, which frequently involves helix–turn–helix (HTH) domain proteins. One example for HTH-mediated gene regulation is found in the arms race between bacteria and their viruses, bacteriophages (phages). When bacteria are infected by phages, they use adaptive CRISPR–Cas defence systems for protection; in turn, phages rapidly produce anti-CRISPR (Acr) proteins to inactive CRISPR–Cas. Acr proteins are frequently co-encoded in operons with HTH-containing anti-CRISPR-associated (Aca) proteins, which we and others have demonstrated to transcriptionally auto-repress acr–aca operons by promoter binding.1–4 This Aca-mediated repression after an initial burst of Acr production likely reduces fitness costs from excessive expression. However, it is unclear how a single HTH regulator can adjust anti-CRISPR production to cope with the increasing number of phage genome copies and accumulating acr–aca mRNAs. Here, we show that the HTH domain of the regulator Aca2 not only represses Acr synthesis transcriptionally through DNA binding, but also inhibits translation of mRNAs by binding conserved RNA stem-loops and blocking ribosome access.5 The cryogenic electron microscopy structure of the ~40-kDa Aca2–RNA complex demonstrates how the remarkably versatile HTH domain specifically discriminates RNA from DNA binding sites. These combined regulatory modes are widespread in the Aca2 family and facilitate CRISPR–Cas inhibition in the face of rapid phage DNA replication without toxic acr overexpression. Given the ubiquity of HTH-domain proteins, it is anticipated that many more elicit regulatory control by dual DNA and RNA binding.