{PDOC51398}
{PS51398; PAW}
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* PAW domain profile *
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The PAW  domain  (present  in  PNGases  and other worm proteins) is found as a
single copy  at the C-terminus of metazoan peptide:N-glycanase (PNGase) and in
multiple copies  in  hypothetical  Caenorhabditis  elegans proteins peptide:N-
glycanases (PNGases)  [1].  The  C-terminal  PAW domain of PNGase binds to the
mannose moieties of N-linked oligosaccharide chains [2].

The PAW  domain  is a slightly elongated molecule and displays a beta-sandwich
architecture, which  is  composed  of  two  layers,  containing nine and eight
antiparallel beta-strands,  respectively,  and  three additional short helices
(see <PDB:2G9G>) [2].

Some proteins known to contain a PAW domain are listed below:

 - Animal   peptide:N-glycanase   (PNGase)   (EC   3.5.1.52),   catalyzes  the
   deglycosylation of several misfolded N-linked glycoproteins by cleaving the
   bulky glycan chain before the proteins are degraded by the proteasome.
 - Caenorhabditis elegans putative uncharacterized protein C17B7.5.

The profile we developed covers the entire PAW domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 2008 / First entry.

[ 1] Doerks T., Copley R.R., Schultz J., Ponting C.P., Bork P.
     "Systematic identification of novel protein domain families associated
     with nuclear functions."
     Genome Res. 12:47-56(2002).
     PubMed=11779830; DOI=10.1101/
[ 2] Zhou X., Zhao G., Truglio J.J., Wang L., Li G., Lennarz W.J.,
     Schindelin H.
     "Structural and biochemical studies of the C-terminal domain of mouse
     peptide-N-glycanase identify it as a mannose-binding module."
     Proc. Natl. Acad. Sci. U.S.A. 103:17214-17219(2006).
     PubMed=17088551; DOI=10.1073/pnas.0602954103

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