v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | This superfamily 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 β-barrel domain [ ].Several bacterial hypothetical proteins, such as the N-terminal domain of YggJ [ ].The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was named after the proteins in which it was first found [ ]. 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 [, ]. 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 []. PUA motifs are involved in dyskeratosis congenita and cancer, pointing to links between RNA metabolism and human diseases []. |
Short Name | PUA-like_sf |