The domain within your query sequence starts at position 52 and ends at position 307; the E-value for the Asp-B-Hydro_N domain shown below is 7e-104.
NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDD AKVLLGLKERSPSERTFPPEEEAETHAELEEQAPEGADIQNVEDEVKEQIQSLLQESVHT DHDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDTASQNHPNDM EEMTNEQENSDPSEAVTDAGVLLPHAEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSII SEEINVASVEEQQDTP
Asp-B-Hydro_N |
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PFAM accession number: | PF05279 |
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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