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Sigma-54 interaction domain
GAF domain-containing protein
The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes [1,2]. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain [3]. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 9433123. The GAF domain: an evolutionary link between diverse phototransducing proteins. Aravind L, Ponting CP;. Trends Biochem Sci 1997;22:458-459. [2]. 20004158. Cyclic nucleotide binding GAF domains from phosphodiesterases: structural and mechanistic insights. Heikaus CC, Pandit J, Klevit RE;. Structure. 2009;17:1551-1557. [3]. 11032796. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. Ho YS, Burden LM, Hurley JH;. EMBO J. 2000;19:5288-5299. (from Pfam)
AAA family ATPase
This Pfam entry includes some of the AAA proteins not detected by the Pfam:PF00004 model. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)
This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Discovery and naming of the GAF domain. [1]. 9433123. The GAF domain: an evolutionary link between diverse phototransducing proteins. Aravind L, Ponting CP;. Trends Biochem Sci 1997;22:458-459. [2]. 20004158. Cyclic nucleotide binding GAF domains from phosphodiesterases: structural and mechanistic insights. Heikaus CC, Pandit J, Klevit RE;. Structure. 2009;17:. TRUNCATED at 1650 bytes (from Pfam)
sigma 54-interacting transcriptional regulator
AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)
nitric oxide reductase transcription regulator
nitric oxide reductase transcription regulator similar to the Escherichia coli anaerobic nitric oxide reductase transcription regulator NorR, which is required for the expression of anaerobic nitric oxide reductase
nitric oxide reductase transcriptional regulator NorR
Required for the expression of anaerobic nitric oxide (NO) reductase; acts as a transcriptional activator for the norVW operon
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