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 |
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PFAM accession number: | PF15362 |
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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