The domain within your query sequence starts at position 61 and ends at position 277; the E-value for the PhyH domain shown below is 1.4e-51.

YEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSK
IQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHY
FPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYD
PNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKA

PhyH

 PhyH
PFAM accession number:PF05721
Interpro abstract (IPR008775):

This family is made up of several eukaryotic phytanoyl-CoA dioxygenase (PhyH) proteins as well as a number of bacterial deoxygenases. PhyH is a peroxisomal enzyme catalysing the first step of phytanic acid alpha-oxidation. PhyH deficiency causes Refsum's disease (RD) which is an inherited neurological syndrome biochemically characterised by the accumulation of phytanic acid in plasma and tissues [ (PUBMED:10767344) ].

The bacterial deoxygenase 2-aminoethylphosphonate dioxygenase (PhnY) hydroxyles 2-aminoethylphosphonic acid to form (2-amino-1-hydroxyethyl)phosphonic acid, which is then oxidatively converted to inorganic phosphate and glycine by 2-amino-1-hydroxyethylphosphonate dioxygenase (PhnZ) [ (PUBMED:22564006) ].

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