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PAS domain-containing protein
This domain is found in many signalling proteins in which it functions as a sensor domain. It recognises FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). (from Pfam)
The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [4]. The PAS fold appears in archaea, eubacteria and eukarya. [1]. 9301332. PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Zhulin IB, Taylor BL, Dixon R;. Trends Biochem Sci 1997;22:331-333. [2]. 7756254. 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Borgstahl GE, Williams DR, Getzoff ED;. Biochemistry 1995;34:6278-6287. [3]. 9382818. PAS: a multifunctional domain family comes to light. Ponting CP, Aravind L;. Curr Biol 1997;7:674-677. [4]. 15009198. The PAS fold: a redefination of the PAS domain based upon structural prediction. Hefti MH, Francoijs KJ, de Vries SC, Dixon R, Vervoort J;. Eur J Biochem 2004;271:1198-1208. (from Pfam)
methyl-accepting chemotaxis protein
This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs. [1]. 1601874. Sequence and characterization of Bacillus subtilis CheW. Hanlon DW, Marquez-Magana LM, Carpenter PB, Chamberlin MJ, Ordal GW;. J Biol Chem 1992;267:12055-12060. (from Pfam)
The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [4]. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 9301332. PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Zhulin IB, Taylor BL, Dixon R;. Trends Biochem Sci 1997;22:331-333. [2]. 7756254. 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Borgstahl GE, Williams DR, Getzoff ED;. Biochemistry 1995;34:6278-6287. [3]. 9382818. PAS: a multifunctional domain family comes to light. Ponting CP, Aravind L;. Curr Biol 1997;7:674-677. [4]. 15009198. The PAS fold: a redefination of the PAS domain based upon structural prediction. Hefti MH, Francoijs KJ, de Vries SC, Dixon R, Vervoort J;. Eur J Biochem 2004;271:1198-1208. (from Pfam)
PAS domain-containing methyl-accepting chemotaxis protein
PAS domain-containing methyl-accepting chemotaxis protein is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior
PAS domain S-box protein
The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator.
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