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NAD-binding protein
This domain is found in a wide variety of proteins. These protein include potassium channels Swiss:P31069, phosphoesterases Swiss:Q59027, and various other transporters. This domain binds to NAD. Domain called KTN in figure 2.. [1]. 9478130. A novel family of predicted phosphoesterases includes Drosophila. prune protein and bacterial RecJ exonuclease.. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:17-19.. [2]. 8412700. NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA. and sequence similarity between TrkA and domains of a family of. dehydrogenases suggest a role for NAD+ in bacterial transport.. Schlosser A, Hamann A, Bossemeyer D, Schneider E, Bakker EP;. Mol Microbiol 1993;9:533-543.. Called TRKA-N domain. See alignment in figure 8a.. [3]. 11292341. Regulatory potential, phyletic distribution and evolution of. ancient, intracellular small-molecule-binding domains.. Anantharaman V, Koonin EV, Aravind L;. J Mol Biol 2001;307:1271-1292. (from Pfam)
cation:proton antiporter
Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family. [1]. 9537504. Comparative molecular analysis of Na+/H+ exchangers: a unified. model for Na+/H+ antiport?. Dibrov P, Fliegel L;. FEBS Lett 1998;424:1-5.. [2]. 9278382. Na+/H+ exchangers of mammalian cells.. Orlowski J, Grinstein S;. J Biol Chem 1997;272:22373-22376.. [3]. 9507001. Identification of a mitochondrial Na+/H+ exchanger.. Numata M, Petrecca K, Lake N, Orlowski J;. J Biol Chem 1998;273:6951-6959. (from Pfam)
cation:proton antiporter similar to Escherichia coli inner membrane protein YbaL and Yersinia RosB, which mediates resistance to cationic antimicrobial peptides
monovalent cation:proton antiporter-2 (CPA2) family protein
YbaL family putative K(+) efflux transporter
YbaL is a homolog of Kef, a potassium/proton antiporter that performs potassium efflux.
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