CATH Superfamily 1.20.1270.10
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: waiting to be named.
FunFam 5393: Chaperone protein DnaK 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 13 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 |
---|---|---|
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
1 | Q9K0N4 (/IPI) |
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 | P0A6Y8 (/IPI) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | P0A6Y8 (/IDA) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | P0A6Y8 (/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 | P0A6Y8 (/IDA) |
Sigma factor antagonist activity GO:0016989
The function of binding to a sigma factor and stopping, preventing or reducing the rate of its transcriptional activity.
|
1 | P0A6Y8 (/IDA) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
1 | A1A766 (/IPI) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
1 | A1A766 (/TAS) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
1 | P0A6Y8 (/IDA) |
Protein binding involved in protein folding GO:0044183
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) that contributes to the process of protein folding.
|
1 | P0A6Y8 (/IDA) |
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
|
1 | P0A6Y8 (/IDA) |
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
|
1 | P0A6Y8 (/IPI) |
Chaperone binding GO:0051087
Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
|
1 | A1A766 (/TAS) |
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 | O34241 (/ISS) |
Protein complex assembly GO:0006461
The aggregation, arrangement and bonding together of a set of components to form a protein complex.
|
1 | P0A6Y8 (/IDA) |
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 | P0A6Y8 (/IDA) |
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 | P0A6Y8 (/IEP) |
Cellular response to unfolded protein GO:0034620
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
|
1 | P0A6Y8 (/IDA) |
Protein complex disassembly GO:0043241
The disaggregation of a protein complex into its constituent components. Protein complexes may have other associated non-protein prosthetic groups, such as nucleic acids, metal ions or carbohydrate groups.
|
1 | P0A6Y8 (/IDA) |
Interaction with host via substance in symbiont cell outer membrane GO:0044045
An interaction with the host organism mediated by a substance in the symbiont cell outer membrane - a lipid bilayer that forms the outermost layer of the symbiont cell envelope. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
1 | Q9K0N4 (/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 | P0A6Y8 (/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 | P0A6Y8 (/IMP) |
Chaperone cofactor-dependent protein refolding GO:0070389
The process of assisting in the restoration of the biological activity of an unfolded or misfolded protein, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
|
1 | P0A6Y8 (/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 |
---|---|---|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | P0A6Y8 (/IDA) |
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 | P0A6Y8 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P0A6Y8 (/IDA) |
External side of cell outer membrane GO:0031240
The side of the outer membrane that is opposite to the side that faces the periplasm of the cell.
|
1 | Q9K0N4 (/IDA) |
Protein complex GO:0043234
A stable macromolecular complex composed (only) of two or more polypeptide subunits along with any covalently attached molecules (such as lipid anchors or oligosaccharide) or non-protein prosthetic groups (such as nucleotides or metal ions). Prosthetic group in this context refers to a tightly bound cofactor. The component polypeptide subunits may be identical.
|
1 | P0A6Y8 (/IDA) |