To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC50890 [for PROSITE entry PS50890]

PUA domain profile


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

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)


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

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.


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