The domain within your query sequence starts at position 453 and ends at position 500; the E-value for the P4Hc domain shown below is 1e-22.

VGIWNVPYMANVYLIQGKTLRSEMNERNYFVRDKLDPDMALCRNARDM

The domain was found using the schnipsel database

P4Hc

Prolyl 4-hydroxylase alpha subunit homologues.
P4Hc
SMART accession number:SM00702
Description: Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.
Interpro abstract (IPR006620):

Mammalian prolyl 4-hydroxylase alpha catalyses the posttranslational formation of 4- hydroxyproline in -xaa-pro-gly-sequences in collagens and other proteins. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor [(PUBMED:11276424)].

GO process:oxidation-reduction process (GO:0055114)
GO function:iron ion binding (GO:0005506), L-ascorbic acid binding (GO:0031418), oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen (GO:0016705)
Family alignment:
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There are 28654 P4Hc domains in 28559 proteins in SMART's nrdb database.

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