v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | Eukaryotic pirins are highly conserved nuclear proteins that may function as transcriptional regulators with a role in apoptosis [ , ]. Prokaryotic homologues have also been identified. Both bacterial and human pirins have been shown to possess quercetinase activity [], although this is not universally true for all family members - YhaK (), for example, displays no such enzymatic activity [ ].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 [ ].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 β-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 [ ].This entry represents the Pirin N-terminal domain. |
Short Name | Pirin_N_dom |