The domain within your query sequence starts at position 434 and ends at position 497; the E-value for the Catalase-rel domain shown below is 5.8e-21.
SANEDNVTQVRTFYTKVLNEEERKRLCENIAGHLKDAQLFIQKKAVKNFTDVHPDYGARI QALL
Catalase-rel |
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PFAM accession number: | PF06628 |
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Interpro abstract (IPR010582): | 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) ]. This entry represents a small conserved region within catalase enzymes that carries the immune-responsive amphipathic octa-peptide that is recognised by T cells [ (PUBMED:15585332) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Catalase-rel