InterPro domain: IPR036974

The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was named after the proteins in which it was first found [ 1 ]. PUA is a highly conserved RNA-binding motif found in a wide range of archaeal, bacterial and eukaryotic proteins, including enzymes that catalyse tRNA and rRNA post-transcriptional modifications, proteins involved in ribosome biogenesis and translation, as well as in enzymes involved in proline biosynthesis [ 2 , 3 , 4 ]. The structures of several PUA-RNA complexes reveal a common RNA recognition surface, but also some versatility in the way in which the motif binds to RNA [ 5 , 5 ]. This domain has an alpha/beta architecture consisting of six beta-strands and two short alpha-helices [ 6 ]. PUA motifs are involved in dyskeratosis congenita and cancer, pointing to links between RNA metabolism and human diseases [ 6 ].

1. Novel predicted RNA-binding domains associated with the translation machinery. J. Mol. Evol. 48, 291-302
2. The structure of the RNA m5C methyltransferase YebU from Escherichia coli reveals a C-terminal RNA-recruiting PUA domain. J. Mol. Biol. 360, 774-87
3. The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation. J. Biol. Chem. 281, 6993-7001
4. Protein universe containing a PUA RNA-binding domain. FEBS J 281, 74-87
5. The PUA domain - a structural and functional overview. FEBS J. 274, 4972-84
6. Crystal structure of an H/ACA box ribonucleoprotein particle. Nature 443, 302-7