PUA RNA-binding domain of the archaeal pseudouridine synthase component Cbf5
The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of the archaeal and eukaryotic subfamily of pseudouridine synthases, including Cbf5 (dyskerin in humans) and similar proteins, are modules that assist in the binding and positioning (guide and/or substrate) of RNA to the pseudouridine synthase complex. Pseudouridine synthases are enzymes that are responsible for post-translational modifications of RNAs by specifically isomerizing uracil residues. In Pyrococcus furiosus H/ACA ribonucleoprotein (RNP) assembly with a single-hairpin H/ACA RNA, the lower stem and the ACA motif of the guide RNA are anchored at the PUA domain of Cbf5. In addition, the N-terminal extension of Cbf5, which is a hot spot for dyskeratosis congenita (a rare genetic form of bone marrow failure) mutation, forms an extra structural layer on the PUA domain.
Feature 1:RNA binding site [nucleic acid binding site]
Evidence:
Comment:many PUA domains have been shown to bind RNA, and although detailed interactions vary, they all seem to share a common surface patch that is associated with binding
Structure:2RFK: PUA domain of an archaeal tRNA pseudouridine synthase B binds RNA, contacts at 4 A
Jiyao W et al.(2023). "The conserved domain database in 2023.",