The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
GroES chaperonin
".

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 1980: 10 kDa chaperonin

Please note: GO 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.

There are 3 GO terms relating to "molecular function"

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.
GO Term Annotations Evidence
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
1 P0A6F9 (/IPI)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P0A6F9 (/IDA)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P0A6F9 (/IPI)

There are 6 GO terms relating to "biological process"

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.
GO Term Annotations Evidence
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
2 Q9KLC7 (/ISS) Q9KNR6 (/ISS)
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
1 P0A6F9 (/IDA)
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
1 P0A6F9 (/IMP)
Response to heat GO:0009408
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
1 P0A6F9 (/IEP)
Virion assembly GO:0019068
A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.
1 P0A6F9 (/IMP)
Chaperone mediated protein folding requiring cofactor GO:0051085
The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
1 P0A6F9 (/IDA)

There are 2 GO terms relating to "cellular component"

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.
GO Term Annotations Evidence
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 P0A6F9 (/IDA)
GroEL-GroES complex GO:1990220
Bacterial chaperonin complex consisting of a heptameric 10kDa chaperonin subunit GroES and a tetradecameric (2x7) 60kDa chaperonin subunit GroEL. The 60kDa subunit possesses ATPase activity while the holo-enzyme is responsible for the correct folding of proteins.
1 P0A6F9 (/IDA)