The domain within your query sequence starts at position 14 and ends at position 66; the E-value for the CENP-B_N domain shown below is 5.3e-27.

KRKRVVLTLKEKIDICTRLERGESRKALMQEYNVGMSTLYDIKAHKAQLLRFF

CENP-B_N

CENP-B_N
PFAM accession number:PF04218
Interpro abstract (IPR007889):

The psq-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50 amino acids present in eukaryotic proteins of the Pipsqueak family. This family is named after the Drosophila pipsqueak protein, containing a DNA-binding domain that consists of four tandem repeats of the psq motif [(PUBMED:9774480)]. Proteins of the Pipsqueak family occur in vertebrates, insects, nematodes, and fungi.

Three subgroups of the family have been described: BTB, E93 and CENP-B. Pipsqueak and the other proteins of the BTB group (Broad-Complex, Tramtrack, Bric a brac) contain a BTB protein-protein interaction domain in the N-terminal part, and the psq-type HTH domain(s) occur in the C-terminal part. Many BTB proteins are transcriptional regulators and the psq-type HTH domain binds DNA. The Drosophila cell death regulating protein E93 and human orthologs form the second subgroup and can contain the psq-type HTH at varying positions. The human centromere protein B (CENP-B) and the other members of the CENP-B group contain a psq-type DNA-binding domain in the N-terminal part and often a dimerisation domain in the C-terminal part. The CENP-B group includes fungal transposases that, however, lack the N-terminal extremity of the psq-type HTH domain [(PUBMED:11976954)].

The structure of human CENP-B shows that the N-terminal part of the DNA binding domain is composed of three alpha-helices. The second and third helices connected via a turn comprise the helix-turn-helix motif. Helix 3 is termed the recognition helix as it binds the DNA major groove, like in other HTHs [(PUBMED:11726497)].

GO function:DNA binding (GO:0003677)

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