The domain within your query sequence starts at position 25 and ends at position 106; the E-value for the Sod_Fe_N domain shown below is 1e-34.

KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNATEEKYHEALAKGDVTTQVAL
QPALKFNGGGHINHTIFWTNLS

Sod_Fe_N

Sod_Fe_N
PFAM accession number:PF00081
Interpro abstract (IPR019831):

Superoxide dismutases (SODs) ( EC 1.15.1.1 ) catalyse the conversion of superoxide radicals to molecular oxygen. Their function is to destroy the radicals that are normally produced within cells and are toxic to biological systems. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one [ (PUBMED:3315461) (PUBMED:3345848) (PUBMED:1556751) ]. This family includes both single metal-binding SODs and cambialistic SOD, which can bind either Mn or Fe. Fe/MnSODs are ubiquitous enzymes that are responsible for the majority of SOD activity in prokaryotes, fungi, blue-green algae and mitochondria. Fe/MnSODs are found as homodimers or homotetramers.

The structure of Fe/MnSODs can be divided into two domains, an alpha N-terminal domain and an alpha/beta C-terminal domain, connected by a loop. The structure of the N-terminal domain consists of a two helices in an antiparallel hairpin, with a left-handed twist [ (PUBMED:9537987) ]. The structure of the C-terminal domain is of the alpha/beta type, and consists of a three-stranded antiparallel beta-sheet in the order 213, along with four helices in the arrangement alpha/beta(2)/alpha/beta/alpha(2) [ (PUBMED:9931259) ].

This entry represents the N-terminal domain of Manganese/iron superoxide dismutase.

GO process:superoxide metabolic process (GO:0006801), oxidation-reduction process (GO:0055114)
GO function:superoxide dismutase activity (GO:0004784), metal ion binding (GO:0046872)

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