|PROSITE documentation PDOC50890 [for PROSITE entry PS50890]|
The PUA domain, which has been named after PseudoUridine synthase and Archaeosine-specific transglycosylase, is a small, compact domain that consists of 78-83 amino acid residues. The PUA domain is widely conserved in eukaryotic and archaeal RNA modification enzymes and is found in:
The PUA domain can be found alone or in association with other domains, such as the glutamate kinase domain (see <PDOC00701>), the pseudouridine synthase catalytic domain, the phosphoadenosine phosphosulfate (PAPS) reductase domain, the methylase domain, the TGT domain, or the SUI1 domain (see <PDOC00862 >). The PUA domain is supposed to bind to RNA molecules with complex folded structures .
The PUA domain contains highly conserved motifs that center around stretches of hydrophobic residues. The domain also contains two highly conserved positions occupied by small amino acids (primarily glycines) . The resolution of the crystal structure of archaeosine tRNA-guanine transglycosylase from Pyrococcus horikoshii has shown that the PUA domain consists of two α-helices and six β-strands, and folds into a β-sandwich structure similar to the oligonucleotide-binding (OB)-fold (see <PDB:1IQ8>) .
The profile we developed covers the entire PUA domain.Last update:
November 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Aravind L., Koonin E.V.|
|Title||Novel predicted RNA-binding domains associated with the translation machinery.|
|Source||J. Mol. Evol. 48:291-302(1999).|
|2||Authors||Ishitani R., Nureki O., Fukai S., Kijimoto T., Nameki N., Watanabe M., Kondo H., Sekine M., Okada N., Nishimura S., Yokoyama S.|
|Title||Crystal structure of archaeosine tRNA-guanine transglycosylase.|
|Source||J. Mol. Biol. 318:665-677(2002).|