PUA-like superfamily
IPR015947
Definition
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 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 [[cite:PMID:16793063], [cite: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.
20 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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