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HAMP 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)
ATP-binding protein
This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. [1]. 18361456. Crystal structure of a novel non-Pfam protein AF1514 from. Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray. source.. Li Y, Bahti P, Shaw N, Song G, Chen S, Zhang X, Zhang M, Cheng. C, Yin J, Zhu JY, Zhang H, Che D, Xu H, Abbas A, Wang BC, Liu. ZJ;. Proteins 2008;71:2109-13. (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. 200. TRUNCATED at 1650 bytes (from Pfam)
HAMP domain-containing protein
histidine kinase dimerization/phospho-acceptor domain-containing protein
Dimerisation and phospho-acceptor domain of histidine kinases. [1]. 9989504. Structure of CheA, a signal-transducing histidine kinase.. Bilwes AM, Alex LA, Crane BR, Simon MI;. Cell 1999;96:131-141.. [2]. 18361456. Crystal structure of a novel non-Pfam protein AF1514 from. Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray. source.. Li Y, Bahti P, Shaw N, Song G, Chen S, Zhang X, Zhang M, Cheng. C, Yin J, Zhu JY, Zhang H, Che D, Xu H, Abbas A, Wang BC, Liu. ZJ;. Proteins 2008;71:2109-13. (from Pfam)
response regulator
This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain. [1]. 7699720. Response regulators of bacterial signal transduction systems:. selective domain shuffling during evolution.. Pao GM, Saier MH;. J Mol Evol 1995;40:136-154. (from Pfam)
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