DNA binding HTH domain, Psq-type (IPR007889)

Short name: HTH_Psq

Overlapping homologous superfamilies

Domain relationships



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 [PMID: 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 [PMID: 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 [PMID: 11726497].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003677 DNA binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles