The domain within your query sequence starts at position 173 and ends at position 290; the E-value for the AhpC-TSA domain shown below is 4.7e-10.

VIAGPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQEFEII
FVSADRSEESFKQYFSEMPWLAVPYTDEARRSRLNRLYGIQGIPTLIVLDPQGEVITR

AhpC-TSA

AhpC-TSA
PFAM accession number:PF00578
Interpro abstract (IPR000866):

Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerisation states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism, in which an active-site cysteine (the peroxidatic cysteine) is oxidised to a sulphenic acid by the peroxide substrate. The recycling of the sulphenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity [(PUBMED:12517450)].

Alkyl hydroperoxide reductase (AhpC) is responsible for directly reducing organic hyperoxides in its reduced dithiol form. Thiol specific antioxidant (TSA) is a physiologically important antioxidant which constitutes an enzymatic defence against sulphur-containing radicals. This family contains AhpC and TSA, as well as related proteins.

GO process:oxidation-reduction process (GO:0055114)
GO function:antioxidant activity (GO:0016209), oxidoreductase activity (GO:0016491)

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