The domain within your query sequence starts at position 52 and ends at position 291; the E-value for the Asp-B-Hydro_N domain shown below is 8.6e-96.

NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDD
AKVLLGLKERSPSERTFPPEEEAETHAELEEQAPEGADIQNVEDEVKEQIQSLLQESVHT
DHDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDTASQNHPNDM
EEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQQDTP

Asp-B-Hydro_N

Asp-B-Hydro_N
PFAM accession number:PF05279
Interpro abstract (IPR007943):

This domain is found in members of the junctin, junctate and aspartyl beta-hydroxylase protein families. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin [ (PUBMED:11735129) ]. Aspartyl beta-hydroxylase catalyses the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins [ (PUBMED:11773073) ].

This domain is also found in several eukaryotic triadin proteins. Triadin is a ryanodine receptor and calsequestrin binding protein located in junctional sarcoplasmic reticulum of striated muscles [ (PUBMED:11707337) ].

GO component:membrane (GO:0016020)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Asp-B-Hydro_N