| 词条 | Cache domain |
| 释义 |
| Symbol = Cache_1 | Name = Cache domain | image = | width = | caption = crystal structure of mcp_n and cache domains of methyl-accepting chemotaxis protein from vibrio cholerae | Pfam = PF02743 | Pfam_clan = CL0165 | InterPro = IPR004010 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}{{Infobox protein family | Symbol = Cache_2 | Name = Cache domain (type 2) | image = | width = | caption = crystal structure of methyl-accepting chemotaxis protein from vibrio parahaemolyticus rimd 2210633 | Pfam = PF08269 | Pfam_clan = CL0165 | InterPro = IPR013163 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, the cache domain is an extracellular protein domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2+ channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source.[1] The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.[2] References1. ^{{cite journal |vauthors=Anantharaman V, Aravind L | title = Cache - a signaling domain common to animal Ca(2+)-channel subunits and a class of prokaryotic chemotaxis receptors | journal = Trends Biochem. Sci. | volume = 25 | issue = 11 | pages = 535–7 |date=November 2000 | pmid = 11084361 | doi = 10.1016/s0968-0004(00)01672-8| url = }} {{InterPro content|IPR004010}}{{InterPro content|IPR013163}}2. ^{{cite journal |vauthors=Anantharaman V, Koonin EV, Aravind L | title = Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains | journal = J. Mol. Biol. | volume = 307 | issue = 5 | pages = 1271–92 |date=April 2001 | pmid = 11292341 | doi = 10.1006/jmbi.2001.4508 | url = }} 1 : Protein domains |
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