Pirin, N-terminal domain (IPR003829)

Short name: Pirin_N_dom

Overlapping homologous superfamilies

Domain relationships



Eukaryotic pirins are highly conserved nuclear proteins that may function as transcriptional regulators with a role in apoptosis [PMID: 21514450, PMID: 11485202]. Prokaryotic homologues have also been identified. Both bacterial and human pirins have been shown to possess quercetinase activity [PMID: 15951572], although this is not universally true for all family members - YhaK (P42624), for example, displays no such enzymatic activity [PMID: 18561187].

Pirin is composed of two structurally similar domains arranged face to face. Although the two domains are similar, the C-terminal domain of pirin differs from the N-terminal domain as it does not contain a metal binding site and its sequence does not contain the conserved metal-coordinating residues [PMID: 14573596].

Pirin is considered a member of the cupin superfamily on the basis of primary sequence and structural similarity. The presence of a metal binding site in the N-terminal beta-barrel of pirin, may be significant in its interaction with Bcl-3 and nuclear factor I (NFI) and role in regulating NF-kappaB transcription factor activity [PMID: 14573596].

This entry represents the Pirin N-terminal domain.

Contributing signatures

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