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:

"
GroEL
".

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 156: 60 kDa chaperonin 2

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 9 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).
2 C5A1D5 (/IPI) P0A6F5 (/IPI)
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
1 P0A6F5 (/IDA)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P0A6F5 (/IDA)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
1 P0A6F5 (/IDA)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P0A6F5 (/IDA)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P0A6F5 (/IPI)
Host cell surface binding GO:0046812
Interacting selectively and non-covalently with the surface of a host cell.
1 Q5ZXP3 (/IDA)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 P0A6F5 (/IDA)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 P0A6F5 (/IMP)

There are 10 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.
1 P0A6F5 (/IMP)
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 Q9KLC6 (/ISS)
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
1 O66198 (/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 P0A6F5 (/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 P0A6F5 (/IMP)
Adhesion of symbiont to host cell GO:0044650
The attachment of a symbiont to a host cell via adhesion molecules, general stickiness etc., either directly or indirectly.
1 Q5ZXP3 (/IDA)
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 P0A6F5 (/IDA)
Modification of morphology or physiology of other organism via secreted substance involved in symbiotic interaction GO:0052212
The process in which an organism effects a change in the structure or function of a second organism, mediated by a substance secreted by one of the organisms, where the two organisms are in a symbiotic interaction.
1 O66198 (/IMP)
Parasitism GO:0072519
An interaction between two organisms living together in more or less intimate association in a relationship in which association is disadvantageous or destructive to one of the organisms.
1 O66198 (/IMP)
Regulation of entry of bacterium into host cell GO:2000535
Any process that modulates the frequency, rate or extent of entry of bacterium into host cell.
1 Q5ZXP3 (/IDA)

There are 5 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 P0A6F5 (/IDA)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
1 Q5ZXP3 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 P0A6F5 (/IDA)
Host cell endosome membrane GO:0044175
The lipid bilayer surrounding a host cell endosome.
1 Q5ZXP3 (/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 P0A6F5 (/IDA)
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