The domain within your query sequence starts at position 550 and ends at position 1325; the E-value for the Enamelin domain shown below is < 1e-12.

FIGANPAANKPSIGTNPAANKPSIGTNPAANKPFVRNNVGANKPFVGTNPSSNQPFLRSN
QASNKPFMRSNQASNKPFVGTNVASVGPKQVTVSHNMKTQNPKEKSLGQKERTVTPTKDA
SNPWRSAKQYGINNPNYNLPRSEGSMVGPNFNSFDQQENSYFSKGASKRVPSPNIQIQSQ
NLPKGIALEPRRTPFQSETKKPELKHGTHQPAYPKKIPSPTRKHFPAERNTWNRQKILPP
LKEDYGRQDENLRHPSYGSRGNIFYHEYTNPYHNEKSQYIKSNPWDKSSPSTMMRPENPQ
YTMTSLDQKETEQYNEEDPIDPNEDESFPGQSRWGDEEMNFKGNPTVRQYEGEHYASTLA
KEYLPYSLSNPPKPSEDFPYSEFYPWNPQETFPIYNPGPTIAPPVDPRSYYVNNAIGQEE
STLFPSWTSWDHRNQAERQKESEPYFNRNVWDQSINLHKSNIPNHPYSTTSPARFPKDPT
WFEGENLNYDLQITSLSPPEREQLAFPDFLPQSYPTGQNEAHLFHQSQRGSCCIGGSTGH
KDNVLALQDYTSSYGLPPRKNQETSPVHTESSYIKYARPNVSPASILPSQRNISENKLTA
ESPNPSPFGDGVPTVRKNTPYSGKNQLETGIVAFSEASSSQPKNTPCLKSDLGGDRRDVL
KQFFEGSQLSERTAGLTPEQLVIGIPDKGSGPDSIQSEVQGKEGEMQQQRPPTIMKLPCF
GSNSKFHSSTTGPPINNRRPTLLNGALSTPTESPNTLVGLATREQLKSINVDKLNA

Enamelin

Enamelin
PFAM accession number:PF15362
Interpro abstract (IPR015673):

Enamelin is a secreted structural protein that acts to create dental enamel matrix. Enamelin protein is proteolytically cleaved into several products, which are identified by their molecular weights and appear to have different functions in different enamel compartments. It is not currently known how enamelin interacts with other proteins of the enamel matrix [(PUBMED:14656895)].

Enamelin mutations have been found to cause certain forms of amelogenesis imperfecta, a condition in which enamel is malformed [(PUBMED:11037750)].

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