The domain within your query sequence starts at position 556 and ends at position 713; the E-value for the Asp_Arg_Hydrox domain shown below is 3.8e-64.

SLERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTC
ALLEKFSETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANET
RTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPE

Asp_Arg_Hydrox

Asp_Arg_Hydrox
PFAM accession number:PF05118
Interpro abstract (IPR007803):

Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase (P3H) hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. PH3 folds into two domains, an N-terminal domain containing 10 beta strands and a C-terminal helical domain. The N-terminal domain contains the distorted jelly roll beta sheet core [(PUBMED:11737217)]. A similar domain is also found in aspartyl/asparaginyl beta-hydroxylase, which hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins [(PUBMED:8041771)].

GO process:peptidyl-amino acid modification (GO:0018193)

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