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CATH Superfamily 3.30.260.10

TCP-1-like chaperonin intermediate domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
TCP-1-like chaperonin intermediate domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: 60 kDa chaperonin

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Chaperonin ATPase. [EC: 5.6.1.7]
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
  • Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts.
  • Molecular masses of subunits ranges from 10-90 kDa.
  • They are a subclass of molecular chaperones that are related to EC 5.6.1.5.
  • Formerly EC 3.6.4.9.
 17 A0A024R3X4 A0A024R3X4 A0A482IDN3 A0A482IDN3 A0A482IDN3 P10809 P10809 P18687 P31081 P63038
(7 more...)