{PDOC51281}
{PS51281; TAP_C}
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* TAP C-terminal (TAP-C) domain profile *
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The NXF  family  of  shuttling  transport receptors for nuclear export of mRNA
includes:

 - vertebrate mRNA export factor TAP or nuclear RNA export factor 1 (NXF1).
 - Caenorhabditis elegans nuclear RNA export factor 1 (nxf-1).
 - yeast mRNA export factor MEX67.

Members of  the  NXF  family  have a modular structure. A nuclear localization
sequence and  a  noncanonical  RNA  recognition  motif (RRM) (see <PDOC00030>)
followed by  four  LRR  repeats  are  located  in  its N-terminal half. The C-
terminal half  contains  a  NTF2 domain (see <PDOC50177>) followed by a second
domain. This  most  C-terminal  TAP-C  domain  is  important for binding to FG
repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to
mediate nuclear shuttling [1,2].

The Tap-C  domain is made of four alpha helices packed against each other (see
<PDB:1GO5>). The  arrangement of helices 1, 2 and 3 is similar to that seen in
a UBA  fold.  and is joined to the next module by flexible 12-residue Pro-rich
linker [1,2].

The profile we developed covers the entire TAP-C domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2006 / First entry.

[ 1] Suyama M., Doerks T., Braun I.C., Sattler M., Izaurralde E., Bork P.
     "Prediction of structural domains of TAP reveals details of its
     interaction with p15 and nucleoporins."
     EMBO Rep. 1:53-58(2000).
     PubMed=11256625; DOI=10.1038/sj.embor.embor627
[ 2] Grant R.P., Hurt E., Neuhaus D., Stewart M.
     "Structure of the C-terminal FG-nucleoporin binding domain of
     Tap/NXF1."
     Nat. Struct. Biol. 9:247-251(2002).
     PubMed=11875519; DOI=10.1038/nsb773

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