The domain within your query sequence starts at position 40 and ends at position 153; the E-value for the GSHPx domain shown below is 8e-45.

IYDYEALSLNGKEHIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQEDLKPFGLVILGF
PCNQFGKQEPGDNLEILPGLKYVRPGKGFLPNFQLFAKGDVNGENEQKIFTFLK

GSHPx

GSHPx
PFAM accession number:PF00255
Interpro abstract (IPR000889):

Glutathione peroxidase (GSHPx) (EC 1.11.1.9) 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