Pathways & interactions
PUA-like domain (IPR015947)
Short name: PUA-like_domain
- PUA-like domain (IPR015947)
- ASCH domain (IPR007374)
- ATP-sulfurylase PUA-like domain (IPR025980)
- EVE domain (IPR002740)
- PUA domain (IPR002478)
- Pheromone response, PrgU-like domain (IPR018589)
- tRNA pseudouridine synthase II, TruB, subfamily 1, C-terminal (IPR015240)
- tRNA pseudouridine synthase II, TruB, subfamily 2, C-terminal (IPR015225)
This entry represents domains with a PUA-like structure, consisting of a pseudo-barrel composed of mixed folded sheets of five strands. This structural motif is found in:
- PUA-containing proteins.
- The N-terminal of ATP sulphurylases, which contains extra structures, some similar to the PK beta-barrel domain [PMID: 11157739].
- Several bacterial hypothetical proteins, such as the N-terminal domain of YggJ [PMID: 14517985].
The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was named after the proteins in which it was first found [PMID: 10093218]. 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 [PMID: 16793063, PMID: 16407303]. 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 [PMID: 17803682]. PUA motifs are involved in dyskeratosis congenita and cancer, pointing to links between RNA metabolism and human diseases [PMID: 16943774].