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  Domain Name: GroEL
GroEL_like type I chaperonin. 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. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 7
Total Disease Mutations Found: 2
This domain occurred 7 times on human genes (11 proteins).



  LEUKODYSTROPHY, HYPOMYELINATING, 4
  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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