The domain within your query sequence starts at position 229 and ends at position 535; the E-value for the Oxysterol_BP domain shown below is 7.8e-70.

HLISQLKLGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVISFVEY
YLTAFHEGRKGTLAKKPYNPIIGETFHCSWEVPKDRVKSKWTSPHPPISAHEHPMADDPS
KSYKLRFVAEQVSHHPPISCFYCECKEKRLCVNTHVWTKSKFMGMSVGVSMIGEGVLRLL
DHGEEYVFTLPSAYARSILTVPWVELGGKVNISCAKTGYSATVTFHTKPFYGGKVHRVTA
EVKHNPTNTIVCKAHGEWNGTLEFTYSNGETKVIDTTTLPVYPKKLRPLEKQGPMESRNL
WQEVTHY

Oxysterol_BP

Oxysterol_BP
PFAM accession number:PF01237
Interpro abstract (IPR000648):

A number of eukaryotic proteins that seem to be involved with sterol synthesis and/or its regulation have been found [(PUBMED:8017104)] to be evolutionary related. These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds a variety of oxysterols (oxygenated derivatives of cholesterol); yeast OSH1, a protein of 859 residues that also plays a role in ergosterol synthesis; yeast proteins HES1 and KES1, highly related proteins of 434 residues that seem to play a role in ergosterol synthesis; and yeast hypothetical proteins YHR001w, YHR073w and YKR003w.

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