Cache domain
{{Infobox protein family
| 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.{{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}} The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.{{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 }}