IPR000700
PAS-associated, C-terminal
InterPro entry
Short name | PAS-assoc_C |
Overlapping homologous superfamilies |
Description
The PAS (Per, Arnt, Sim) domain
[2, 1] is an approximately 300 amino-acid segment of sequence similarity which is conserved between the Drosophila protein period clock (PER), the Ah receptor nuclear translocator (ARNT) and the Drosophila single-minded (SIM). It is composed of two or more imperfect repeats (PAS-1, PAS-2). In addition, some proteins have another similar region of 40-45 amino acids situated carboxy-terminal to any PAS repeat and which contributes to the PAS structural domain: the PAC motif. The PAS family can be divided in two groups; the proteins that have the PAS motif followed by a PAC motif, and those that do not. It appears that these domains are directly linked, and that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs
[3]. Within the bHLH/PAS proteins, the PAS domain is involved in protein dimerization with another protein of the family. It has also been associated with light reception, light regulation and circadian rhythm regulators (clock).
In bacteria, the PAS domain is usually associated with the input domain of a histidine kinase, or a sensor protein that regulates a histidine kinase.
References
1.PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Zhulin IB, Taylor BL, Dixon R. Trends Biochem. Sci. 22, 331-3, (1997). View articlePMID: 9301332
2.PAS: a multifunctional domain family comes to light. Ponting CP, Aravind L. Curr. Biol. 7, R674-7, (1997). View articlePMID: 9382818
3.The PAS fold. A redefinition of the PAS domain based upon structural prediction. Hefti MH, Francoijs KJ, de Vries SC, Dixon R, Vervoort J. Eur. J. Biochem. 271, 1198-208, (2004). View articlePMID: 15009198
Cross References
Contributing Member Database Entry
- PROSITE profiles:PS50113
Representative structure
1xj3: bjFixLH in unliganded ferrous form