SMART: Pfam domain Nsp1

The domain within your query sequence starts at position 63 and ends at position 179; the E-value for the Nsp1_C domain shown below is 9.4e-35.

SMPSTMTVNSIVTPVMTYGPLESMANNWHYQLQEQEKHYFYQANQFNLWNQALIESGNEI
ALLYNEVERVKIDQSRLEQELDIILFQQKELEQMLTPIEELLKEQNGPLNMMYVNKE

Nsp1_C

PFAM accession number:	PF05064
Interpro abstract (IPR007758):	The NSP1-like protein appears to be an essential component of the nuclear pore complex, for example preribosome nuclear export requires the Nup82p-Nup159p-Nsp1p complex. The C-terminal of Nsp1 is involved in binding Nup82 [ (PUBMED:11689687) ], probably via coiled-coil formation [ (PUBMED:11689687) (PUBMED:17037504) ]. The family is related to the rotavirus nonstructural protein NSP1 which is the least conserved protein in the rotavirus genome. Its function in the replication process is not fully understood.

PFAM accession number:

PF05064

Interpro abstract (IPR007758):

The NSP1-like protein appears to be an essential component of the nuclear pore complex, for example preribosome nuclear export requires the Nup82p-Nup159p-Nsp1p complex. The C-terminal of Nsp1 is involved in binding Nup82 [ (PUBMED:11689687) ], probably via coiled-coil formation [ (PUBMED:11689687) (PUBMED:17037504) ]. The family is related to the rotavirus nonstructural protein NSP1 which is the least conserved protein in the rotavirus genome. Its function in the replication process is not fully understood.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Nsp1_C