The domain within your query sequence starts at position 82 and ends at position 377; the E-value for the BNR_2 domain shown below is 1.8e-52.



PFAM accession number:PF13088
Interpro abstract (IPR011040):

Sialidases (neuraminidases) hydrolyse the non-reducing, terminal sialic acid linkage in various natural substrates, such as glycoproteins, glycolipids, gangliosides, and polysaccharides [ (PUBMED:12374200) ]. In mammals, sialidases occur in the lysosome, the cytosol, and associated with the plasma membrane. Sialidases have also been implicated in the pathogenesis of many diseases. For example, in viruses neuraminidases enable the transport of the virus through mucin, the eruption of the virus from the infected host cell, and the prevention of self-aggregation of virus particles through the destruction of the host cell receptor recognised by the virus [ (PUBMED:14561719) ]. Eukaryotic, bacterial and viral sialidases share highly conserved regions of beta-sheet motifs. Bacterial sialidases often possess domains in addition to the catalytic sialidase domain, for instance the sialidase from Micromonospora viridifaciens contains three domains, of which the catalytic domain described here is the N-terminal domain [ (PUBMED:8591030) ]. Similarly, leech sialidase is a multidomain protein, where the catalytic domain is the C-terminal domain [ (PUBMED:9878409) ]. In several paramyxoviruses, sialidase forms part of the multi-functional haemagglutinin-sialidase glycoprotein found on the viral envelope [ (PUBMED:14729348) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry BNR_2