The domain within your query sequence starts at position 41 and ends at position 148; the E-value for the GSHPx domain shown below is 1.3e-46.



PFAM accession number:PF00255
Interpro abstract (IPR000889):

Glutathione peroxidase (GSHPx) ( EC ) is an enzyme that catalyses the reduction of hydroxyperoxides by glutathione [ (PUBMED:7565867) ]. Its main function is to protect against the damaging effect of endogenously formed hydroxyperoxides. In higher vertebrates, several forms of GSHPx are known, including a ubiquitous cytosolic form (GSHPx-1), a gastrointestinal cytosolic form (GSHPx-GI), a plasma secreted form (GSHPx-P), and an epididymal secretory form (GSHPx-EP). In addition to these characterised forms, the sequence of a protein of unknown function [ (PUBMED:2771650) ] has been shown to be evolutionary related to those of GSHPx's.

In filarial nematode parasites, the major soluble cuticular protein (gp29) is a secreted GSHPx, which may provide a mechanism of resistance to the immune reaction of the mammalian host by neutralising the products of the oxidative burst of leukocytes [ (PUBMED:1631065) ]. The structure of bovine seleno-glutathione peroxidase has been determined [ (PUBMED:6852035) ]. The protein belongs to the alpha-beta class, with a three layer(aba) sandwich architecture. The catalyic site of GSHPx contains a conserved residue which is either a cysteine or, in many eukaryotic GSHPx, a selenocysteine [ (PUBMED:2142875) ].

GO process:response to oxidative stress (GO:0006979), oxidation-reduction process (GO:0055114)
GO function:glutathione peroxidase activity (GO:0004602)

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