The domain within your query sequence starts at position 261 and ends at position 528; the E-value for the Ofd1_CTDD domain shown below is 7.2e-51.

QDHEILYEWINPAYLEMDYQMQIQEEFEERSEILLKEFLKPEKFAEVCEALEKGDVEWKS
HGPPNKRFYEKAEENNLPDVLKECMGLFRSEALFLLLSNLTGLKLHFLAPSEDDETEEKG
EGETASAAAGTEEGTSRRPSGPENNQVAAGSHSQENGEQADPEAQEEEAKKESSVPMCQG
ELRRWKTGHYTLVHDNTKTEFALDLFLYCGCEGWEPEYGGFTSYIAKGEDEELLIVNPEN
NSLALVYRDRETLRFVKHINHRSLEQSK

Ofd1_CTDD

Ofd1_CTDD
PFAM accession number:PF10637
Interpro abstract (IPR019601):

This entry represents the C-terminal degradation domain of oxoglutarate and iron-dependent oxygenase (Ofd1), the domain being conserved from yeasts to humans.

Ofd1 is a prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygenase that accelerates the degradation of Sre1N (the N-terminal transcription factor domain of Sre1) in the presence of oxygen [ (PUBMED:19158663) ]. Yeast Sre1 is the orthologue of mammalian sterol regulatory element binding protein (SREBP), and it responds to changes in oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. However, unlike the prolyl 4-hydroxylases that regulate mammalian hypoxia-inducible factor, Ofd1 uses multiple domains to regulate Sre1N degradation by oxygen; the Ofd1 N-terminal dioxygenase domain is required for oxygen sensing and this Ofd1 C-terminal domain accelerates Sre1N degradation in yeasts [ (PUBMED:18418381) ].

GO process:oxidation-reduction process (GO:0055114)
GO function:2-oxoglutarate-dependent dioxygenase activity (GO:0016706), L-ascorbic acid binding (GO:0031418), iron ion binding (GO:0005506)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ofd1_CTDD