PROSITE documentation PDOC50890

{PDOC50890}
{PS50890; PUA}
{BEGIN}
**********************
* 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 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  alpha-helices  and  six beta-strands, and folds into a beta-
sandwich structure  similar  to  the  oligonucleotide-binding  (OB)-fold  (see
<PDB:1IQ8>) [2].

The profile we developed covers the entire PUA domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2002 / First entry.

[ 1] Aravind L., Koonin E.V.
     "Novel predicted RNA-binding domains associated with the translation
     machinery."
     J. Mol. Evol. 48:291-302(1999).
     PubMed=10093218
[ 2] Ishitani R., Nureki O., Fukai S., Kijimoto T., Nameki N., Watanabe M.,
     Kondo H., Sekine M., Okada N., Nishimura S., Yokoyama S.
     "Crystal structure of archaeosine tRNA-guanine transglycosylase."
     J. Mol. Biol. 318:665-677(2002).
     PubMed=12054814; DOI=10.1016/S0022-2836(02)00090-6

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}