The domain within your query sequence starts at position 28 and ends at position 176; the E-value for the Catalase domain shown below is 2.33e-3.

TTGGGNPIGDKLNIMTAGSRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEV
THDITRYSKAKVLNEEERKRLCENIAGHLKDAQLFIQKKAVKNFTDVHPDYGARIQALLD
KYNAEKPKNAIHTYTQAGSHMAAKGKANL

Catalase

 Catalase
SMART accession number:SM01060
Description: Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects (PUBMED:11351128). Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria (PUBMED:14745498).
Interpro abstract (IPR011614):

Catalases ( EC 1.11.1.6 ) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [ (PUBMED:11351128) ]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases ( IPR000763 ) that are closely related to plant peroxidases, and non-haem, manganese-containing catalases ( IPR007760 ) that are found in bacteria [ (PUBMED:14745498) ]. Based on a phylogenetic analysis, catalases can be classified into clade 1, 2 and 3. Clade 1 contains small subunit catalases from plants and a subset of bacteria; clade 2 contains large subunit catalases from fungi and a second subset of bacteria; and clade 3 contains small subunit catalases from bacteria, fungi, protists, animals, and plants [ (PUBMED:9287428) (PUBMED:12557185) ].

This entry represent the core-forming domain of mono-functional, haem-containing catalases. It does not cover the region that carries an immune-responsive amphipathic octa-peptide that is found in the C-terminal of some catalases ( IPR010582 ).

GO process:oxidation-reduction process (GO:0055114)
GO function:catalase activity (GO:0004096), heme binding (GO:0020037)
Family alignment:
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There are 26181 Catalase domains in 26155 proteins in SMART's nrdb database.

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