The domain within your query sequence starts at position 434 and ends at position 593; the E-value for the RHD_DNA_bind domain shown below is 4.9e-25.

LKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYSEKPINLQMFIGTADDRYLRP
HAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRK
GETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECS

RHD_DNA_bind

RHD_DNA_bind
PFAM accession number:PF00554
Interpro abstract (IPR011539):

The Rel homology domain (RHD) is found in a family of eukaryotic transcription factors, which includes NF-kappaB, Dorsal, Relish, NFAT, among others. The RHD is composed of two structural domains: the N-terminal DNA binding domain that is similar to that found in P53, the C-terminal domain has an immunoglobulin-like fold (See ) that functions as a dimerisation domain. This entry represents the N-terminal DNA binding domain [(PUBMED:17869269)].

Some of these transcription factors appear to form multi-protein DNA-bound complexes [(PUBMED:9794820)]. Phosphorylation of the RHD appears to play a role in the regulation of some of these transcription factors, acting to modulate the expression of their target genes [(PUBMED:15516339)]. The RHD is composed of two immunoglobulin-like beta-barrel subdomains that grip the DNA in the major groove. The N-terminal specificity domain resembles the core domain of the p53 transcription factor, and contains a recognition loop that interacts with DNA bases; the C-terminal dimerisation domain contains the site for interaction with I-kappaB [(PUBMED:7830764)].

GO process:regulation of transcription, DNA-templated (GO:0006355)
GO function:DNA binding (GO:0003677), DNA binding transcription factor activity (GO:0003700)

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