The domain within your query sequence starts at position 22 and ends at position 753; the E-value for the LRIF1 domain shown below is 1.7e-292.

ISGCMYQVVPTIGSDGKKLLQLLPISKSSGNLIPVVQSPVMSHGLKANTEKPVQVTFQTQ
ISSSSTSASVQLPVFQPANTTKCFFTGAIDTTGKDRVTSVRTGNFTPPVSNIQNHGVKIH
KLTRQTFTIPPSTQNDSSHFIFNTPSLLPNVNSSILPSGNHLKIPAHAEVKSVLASSLPP
LVQQKILGTATTSTSGTVEASQIPTVVYVHPVNSVKFVVTKKTQTIYPKPVTFNTLQIPP
NVATETQLKGGQHPQAAPVNSIFQEYLQPGIPCIIPVKSSNNVATKVLNTFVGRKNLGDN
TIDTPLLNTNSSGRTHSVSEPIKDNALIMFNGKVWLNEKGTCGLPSKIDQQNSVSSDIPL
KDSSQLVSSSIVTEISREILNSVLVKSKSFQLKTKSLSNSQLASMANLRAEKNEKVERPS
FSVTNPHTMNQSTHCLKQSKTVFINPVFPDGFRTGQNAPRKGNLVQNIEKICSSVDAATV
TSQQCVFRDQESQTQYEMASIVKKEIQEKGNNKKYSQGSHTNIKASCLKNDAEFKKLFGL
TKDLRVCLTRIPDHLSSGKSFNSFNSLMKSSSYKDANIVVKKEEKKQSFSKKRKAETMKM
GNTKKIKIENADDTVMSIMNGTDVASSQPLSSILPTSDISQHNIVTSHSTTREDKRTEAE
HCSHEKQEKGTLSSSTSFEQSTFLNKNFMEDIFPVTPPELEETIRDEKIRRLKQILREKE
AALEELRKKMYQ

LRIF1

LRIF1
PFAM accession number:PF15741
Interpro abstract (IPR026191):

Ligand-dependent nuclear receptor-interacting factor 1 (LRIF1) was initially identified as a protein that interacts with retinoic acid receptors and other nuclear receptors [ (PUBMED:17455211) ]. The protein has been shown to repress the ligand-induced transcriptional activity of retinoic acid receptor alpha. Its repression activity is mediated at least in part through direct recruitment of histone deacetylases [ (PUBMED:17455211) ].

GO process:regulation of transcription, DNA-templated (GO:0006355)
GO function:retinoic acid receptor binding (GO:0042974)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry LRIF1