PROSITE documentation PDOC50890 [for PROSITE entry PS50890]

PUA domain profile




Description

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:

  • Archaeal and eukaryotic pseudouridine synthases.
  • Archaeosine tRNA-guanine transglycosylases.
  • A family of predicted ATPases that may be involved in RNA modification.
  • A family of predicted archaeal and bacterial rRNA methylases.
  • A conserved family of putative novel eukaryotic translation factors.
  • Glutamate 5-kinases (EC 2.7.2.11).

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 [1].

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) [1]. 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>) [2].

The profile we developed covers the entire PUA domain.

Last update:

November 2002 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PUA, PS50890; PUA domain profile  (MATRIX)


References

1AuthorsAravind L., Koonin E.V.
TitleNovel predicted RNA-binding domains associated with the translation machinery.
SourceJ. Mol. Evol. 48:291-302(1999).
PubMed ID10093218

2AuthorsIshitani R., Nureki O., Fukai S., Kijimoto T., Nameki N., Watanabe M., Kondo H., Sekine M., Okada N., Nishimura S., Yokoyama S.
TitleCrystal structure of archaeosine tRNA-guanine transglycosylase.
SourceJ. Mol. Biol. 318:665-677(2002).
PubMed ID12054814
DOI10.1016/S0022-2836(02)00090-6



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)