The domain within your query sequence starts at position 18 and ends at position 159; the E-value for the Ferritin domain shown below is 1.5e-40.

EAAINRQINLELYASYVYLSMSCYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQR
GGRIFLQDIKKPDRDDWESGLNAMECALHLEKSVNQSLLELHKLATDKNDPHLCDFIETY
YLSEQVKSIKELGDHVTNLRKM

Ferritin

Ferritin
PFAM accession number:PF00210
Interpro abstract (IPR008331):

Ferritin is one of the major non-haem iron storage proteins in animals, plants, and microorganisms [(PUBMED:15222465)]. It consists of a mineral core of hydrated ferric oxide, and a multi-subunit protein shell that encloses the former and assures its solubility in an aqueous environment.

In animals the protein is mainly cytoplasmic and there are generally two or more genes that encode closely related subunits - in mammals there are two subunits which are known as H(eavy) and L(ight). In plants ferritin is found in the chloroplast [(PUBMED:2211706)].

This entry represents the main structural domain of ferritin. The domain is also found in other ferritin-like proteins such as members of the DNA protection during starvation (DPS) family [(PUBMED:15365182)] and bacterioferritins [(PUBMED:18946693)].

GO process:cellular iron ion homeostasis (GO:0006879)
GO function:ferric iron binding (GO:0008199)

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