{PDOC51472}
{PS51472; RRM_NUP35}
{BEGIN}
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* RNA-recognition motif (RRM) Nup35-type domain profile *
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The nuclear pore complex (NPC) mediates the transport of macromolecules across
the nuclear envelope (NE). The NPC is composed of a relatively small number of
proteins (~30),  termed  nucleoporins  or  Nups.  The  vertebrate nuclear pore
protein Nup35,  the  ortholog of Saccharomyces cerevisiae Nup53p, is suggested
to interact  with  the  NE membrane and to be required for nuclear morphology.
The highly  conserved  region  between  vertebrate  Nup35  and yeast Nup53p is
predicted to contain an RNA-recognition motif (RRM) domain (see <PDOC00030>).

The sequences  of  the  RRM  Nup-35-type  domain  are  highly conserved in all
eucaryotes. The  RRM Nup35-type domain adopts the characteristic BetaAlphaBeta
BetaAlphaBeta topology  of  the  secondary  structure  elements,  with a four-
stranded antiparallel   beta-sheet  packed  against  two  alpha  helices  (see
<PDB:1WWH>). The RRM Nup35-type domain forms a homodimer and contains atypical
rinonucleoprotein (RNP)   motifs,  which  lack  the  conserved  residues  that
typically bind  RNA in canonical RRM domains. The dimer interface involves the
beta-sheet surface,  with  its atypical RNP motifs, which is generally used to
bind RNA in typical RRM domains [1].

The profile we developed covers the entire RRM Nup35-type domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2009 / First entry.

[ 1] Handa N., Kukimoto-Niino M., Akasaka R., Kishishita S., Murayama K.,
     Terada T., Inoue M., Kigawa T., Kose S., Imamoto N., Tanaka A.,
     Hayashizaki Y., Shirouzu M., Yokoyama S.
     "The crystal structure of mouse Nup35 reveals atypical RNP motifs and
     novel homodimerization of the RRM domain."
     J. Mol. Biol. 363:114-124(2006).
     PubMed=16962612; DOI=10.1016/j.jmb.2006.07.089

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