The domain within your query sequence starts at position 77 and ends at position 510; the E-value for the Nucleoporin_N domain shown below is 3.5e-105.

SLPEISTIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAY
FDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANVQTGSGILNDSMCG
GMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINH
SKSSLSFLVPSLLQFTFSEDDPIVQIEIDNSRNILYTRSEKGVIQVYDLGHDGQGMSRVA
SVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIESSESLDCQLLAVTHAGVRLYFSTCPFR
QPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHKALYSKGILLMTASENEDNDILWCVNH
DTFPFQKPMMETQMTTRVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLP
PKKFVLLSAQGSLM

Nucleoporin_N

Nucleoporin_N
PFAM accession number:PF08801
Interpro abstract (IPR014908):

This entry represents the N-terminal domain of nucleoporin 133 (Nup133) and other nucleoporins, including Nup155, Nup15 and Nup170. It forms a seven-bladed beta propeller structure [ (PUBMED:15557116) ].

Nucleoporins are the main components of the nuclear pore complex (NPC) in eukaryotic cells, and mediate bidirectional nucleocytoplasmic transport, especially of mRNA and proteins. RNA undergoing nuclear export first encounters the basket of the nuclear pore and many nucleoporins are accessible on the basket side of the pore [ (PUBMED:10191094) (PUBMED:11684705) ].

The S. Cerevisiae Nup-170, equivalent to the human Nup-155, contains two structural domains: an N-terminal beta-propeller and a C-terminal alpha-helical domain [ (PUBMED:19674973) ].

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