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  Domain Name: chaperonin_type_I_II
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 22
Total Disease Mutations Found: 12
This domain occurred 11 times on human genes (17 proteins).



  BARDET-BIEDL SYNDROME 1, MODIFIER OF
  BARDET-BIEDL SYNDROME 6
  BARDET-BIEDL SYNDROME 6, INCLUDED
  LEUKODYSTROPHY, HYPOMYELINATING, 4
  MCKUSICK-KAUFMAN SYNDROME
  SPASTIC PARAPLEGIA 13


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
ATP/Mg binding site
hinge regions
ring oligomerisation inte
stacking interactions



























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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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