The domain within your query sequence starts at position 166 and ends at position 251; the E-value for the Nup35_RRM domain shown below is 8.2e-30.

SEDHLDDTWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALS
KDGRIFGESIMIGVKPCIDKNVMENS

Nup35_RRM

Nup35_RRM
PFAM accession number:PF05172
Interpro abstract (IPR007846):

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.

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. 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 [ (PUBMED:16962612) ].

This entry represents the RRM Nup35-type domain.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Nup35_RRM