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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 25: ATP-dependent Clp protease subunit

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 32 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).
145 P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P33416 (/IPI) P33416 (/IPI) P33416 (/IPI)
(135 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
124 P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P31539 (/IPI) P63284 (/IPI) P63284 (/IPI) P63284 (/IPI)
(114 more)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
123 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA)
(113 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
116 P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA)
(106 more)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
25 O94641 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P42762 (/IDA) P42762 (/IDA) P9WPC9 (/IDA) P9WPC9 (/IDA)
(15 more)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
24 Q71XF9 (/ISS) Q71XF9 (/ISS) Q71XF9 (/ISS) Q71XF9 (/ISS) Q71XF9 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS)
(14 more)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
21 Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS)
(11 more)
Denatured protein binding GO:0031249
Interacting selectively and non-covalently with denatured proteins.
19 Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS)
(9 more)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
15 Q74G19 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KU18 (/ISS)
(5 more)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
10 P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI) P9WPC9 (/IPI)
Protein folding chaperone 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.
10 P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP) P9WPC9 (/IMP)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
7 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
7 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
7 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
7 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/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.
7 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
5 P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP)
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
5 P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
3 Q586B8 (/ISM) Q586B8 (/ISM) Q586B8 (/ISM)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
3 P42762 (/IDA) P42762 (/IDA) Q9SXJ7 (/IDA)
ATP-dependent peptidase activity GO:0004176
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the hydrolysis of peptide bonds.
2 Q9FI56 (/IDA) Q9FI56 (/IDA)
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
2 Q8IM28 (/ISS) Q8IM28 (/ISS)
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
1 Q587G1 (/ISM)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 O74402 (/ISM)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
1 O74402 (/ISO)
Heat shock protein binding GO:0031072
Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.
1 O94641 (/ISO)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
1 A0A1D8PTP9 (/IGI)
ATPase activity, coupled GO:0042623
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction directly drives some other reaction, for example ion transport across a membrane.
1 O94641 (/ISO)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 Q587G1 (/ISM)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
1 O74402 (/ISS)
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 O94641 (/ISO)
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
1 O94641 (/IPI)

There are 56 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
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.
117 P42730 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP) P63284 (/IMP)
(107 more)
Response to unfolded protein GO:0006986
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 an unfolded protein stimulus.
116 P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA)
(106 more)
DNA mediated transformation GO:0009294
The introduction and uptake of foreign genetic material (DNA or RNA) into a cell, and often the expression of that genetic material.
46 A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS) A0A0J1HLL8 (/ISS)
(36 more)
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.
21 Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS) Q889C2 (/ISS)
(11 more)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
20 Q74G19 (/ISS) Q81TT4 (/ISS) Q81TT4 (/ISS) Q81TT4 (/ISS) Q81TT4 (/ISS) Q81TT4 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS) Q9KN49 (/ISS)
(10 more)
Stress response to copper ion GO:1990169
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 disturbance in organismal or cellular homeostasis caused by a copper ion stimulus.
16 Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA)
(6 more)
Stress response to cadmium ion GO:1990170
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 disturbance in organismal or cellular homeostasis caused by a cadmium ion stimulus.
16 Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA) Q2G0P5 (/IDA)
(6 more)
Protein unfolding GO:0043335
The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.
13 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP)
(3 more)
Cellular heat acclimation GO:0070370
Any process that increases heat tolerance of a cell in response to high temperatures.
9 A0A1D8PTP9 (/IMP) O94641 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
Inheritance of oxidatively modified proteins involved in replicative cell aging GO:0001319
A protein localization process in which progeny cells acquire, or are barred from acquiring, proteins that have been altered by reaction with reactive oxygen species in dividing aging cells.
7 P31539 (/IGI) P31539 (/IGI) P31539 (/IGI) P31539 (/IGI) P31539 (/IGI) P31539 (/IGI) P31539 (/IGI)
Inheritance of oxidatively modified proteins involved in replicative cell aging GO:0001319
A protein localization process in which progeny cells acquire, or are barred from acquiring, proteins that have been altered by reaction with reactive oxygen species in dividing aging cells.
7 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
Cellular response to heat GO:0034605
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 a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
7 A0A1D8PTP9 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) Q6H795 (/IMP)
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
7 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
Stress granule disassembly GO:0035617
The disaggregation of a stress granule into its constituent protein and RNA parts.
7 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA)
Chaperone cofactor-dependent protein refolding 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.
7 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA)
Trehalose metabolism in response to heat stress GO:0070414
The chemical reactions and pathways involving trehalose that occur as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
7 P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP) P31539 (/IMP)
Cellular response to heat GO:0034605
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 a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
6 P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) Q6F2Y7 (/IGI)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
6 O94641 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP)
Mitochondrial genome maintenance GO:0000002
The maintenance of the structure and integrity of the mitochondrial genome; includes replication and segregation of the mitochondrial chromosome.
5 P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) P33416 (/IGI)
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.
5 P42730 (/IEP) Q586B8 (/IEP) Q586B8 (/IEP) Q586B8 (/IEP) Q9LF37 (/IEP)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
5 P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
5 Q71XF9 (/ISS) Q71XF9 (/ISS) Q71XF9 (/ISS) Q71XF9 (/ISS) Q71XF9 (/ISS)
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
5 P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) P33416 (/IGI) P33416 (/IGI)
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
5 P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP) P33416 (/IMP)
Chloroplast organization GO:0009658
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the chloroplast.
3 Q9FI56 (/IMP) Q9FI56 (/IMP) Q9LF37 (/IMP)
Protein metabolic process GO:0019538
The chemical reactions and pathways involving a protein. Includes protein modification.
3 Q586B8 (/ISM) Q586B8 (/ISM) Q586B8 (/ISM)
Protein hexamerization GO:0034214
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
3 P42762 (/IDA) P42762 (/IDA) Q9SXJ7 (/IDA)
Response to unfolded protein GO:0006986
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 an unfolded protein stimulus.
2 Q8IIJ8 (/ISS) Q8IIJ8 (/ISS)
Response to cytokinin GO:0009735
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 cytokinin stimulus.
2 Q9FI56 (/IDA) Q9FI56 (/IDA)
Regulation of chlorophyll biosynthetic process GO:0010380
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors.
2 Q9FI56 (/IMP) Q9FI56 (/IMP)
Protein secretion by the type VI secretion system GO:0033103
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
2 Q9I363 (/IGC) Q9I363 (/IGC)
Protein hexamerization GO:0034214
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
2 Q8IIJ8 (/RCA) Q8IIJ8 (/RCA)
Translocation of peptides or proteins into host cell cytoplasm GO:0044053
The directed movement of peptides or proteins produced by a symbiont organism to a location within the host cell cytoplasm.
2 Q8IIJ8 (/IMP) Q8IIJ8 (/IMP)
Protein targeting to chloroplast GO:0045036
The process of directing proteins towards the chloroplast, usually using signals contained within the protein. Imported proteins are synthesized as cytosolic precursors containing N-terminal uptake-targeting sequences that direct each protein to its correct subcompartment and are subsequently cleaved.
2 Q9FI56 (/IMP) Q9FI56 (/IMP)
Protein import into chloroplast stroma GO:0045037
The targeting and import of proteins into the chloroplast stroma. Import depends on ATP hydrolysis catalyzed by stromal chaperones. Chloroplast stromal proteins, such as the S subunit of rubisco, have a N-terminal stromal-import sequence of about 44 amino acids which is cleaved from the protein precursor after import.
2 Q9FI56 (/IMP) Q9FI56 (/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 Q587G1 (/ISM)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q587G1 (/ISM)
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 A0A1D8PTP9 (/IMP)
Response to high light intensity GO:0009644
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 high light intensity stimulus.
1 P42730 (/IEP)
Chloroplast organization GO:0009658
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the chloroplast.
1 Q9SXJ7 (/ISS)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
1 O94641 (/IGI)
Protein refolding GO:0042026
The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
1 O74402 (/ISO)
Response to hydrogen peroxide GO:0042542
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 hydrogen peroxide (H2O2) stimulus.
1 P42730 (/IEP)
Protein unfolding GO:0043335
The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.
1 O94641 (/IDA)
Protein unfolding GO:0043335
The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.
1 O74402 (/ISO)
Single-species biofilm formation on inanimate substrate GO:0044011
A process in which microorganisms of the same species attach to and grow on an inanimate surface such as a rock or pipe, and produce extracellular polymers that facilitate attachment and matrix formation, resulting in an alteration in the phenotype of the organisms with respect to growth rate and gene transcription.
1 A0A1D8PTP9 (/IMP)
Protein import into chloroplast stroma GO:0045037
The targeting and import of proteins into the chloroplast stroma. Import depends on ATP hydrolysis catalyzed by stromal chaperones. Chloroplast stromal proteins, such as the S subunit of rubisco, have a N-terminal stromal-import sequence of about 44 amino acids which is cleaved from the protein precursor after import.
1 Q9SXJ7 (/ISS)
Positive regulation of translation GO:0045727
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
1 P42730 (/IMP)
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
1 Q8DVD0 (/IMP)
Cell motility GO:0048870
Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another.
1 Q1D2Y0 (/IMP)
Chaperone cofactor-dependent protein refolding 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 A0A1D8PTP9 (/IGI)
Chaperone cofactor-dependent protein refolding 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 O94641 (/ISO)
Cellular response to misfolded protein GO:0071218
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 a misfolded protein stimulus.
1 O94641 (/IMP)
Supramolecular fiber organization GO:0097435
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
1 Q1D2Y0 (/IMP)
Positive regulation of response to salt stress GO:1901002
Any process that activates or increases the frequency, rate or extent of response to salt stress.
1 Q6H795 (/IMP)
Positive regulation of response to water deprivation GO:1902584
Any process that activates or increases the frequency, rate or extent of response to water deprivation.
1 Q6H795 (/IMP)

There are 36 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.
127 O94641 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA)
(117 more)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
118 P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA) P63284 (/IDA)
(108 more)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
116 P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA) P63284 (/HDA)
(106 more)
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
21 P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA)
(11 more)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
21 P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA) P9WPC9 (/HDA)
(11 more)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
11 O94641 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) Q586B8 (/IDA) Q586B8 (/IDA)
(1 more)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
8 O94641 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA)
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
8 P42762 (/IDA) P42762 (/IDA) Q75GT3 (/IDA) Q8VYJ7 (/IDA) Q9FI56 (/IDA) Q9FI56 (/IDA) Q9LF37 (/IDA) Q9SXJ7 (/IDA)
Chloroplast stroma GO:0009570
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
8 P42730 (/IDA) P42762 (/IDA) P42762 (/IDA) Q8VYJ7 (/IDA) Q9FI56 (/IDA) Q9FI56 (/IDA) Q9LF37 (/IDA) Q9SXJ7 (/IDA)
Apicoplast GO:0020011
The plastid organelle found in apicomplexans.
8 Q8IB03 (/IDA) Q8IB03 (/IDA) Q8IB03 (/IDA) Q8IB03 (/IDA) Q8IB03 (/IDA) Q8IB03 (/IDA) Q8IM28 (/IDA) Q8IM28 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
7 P31539 (/HDA) P31539 (/HDA) P31539 (/HDA) P31539 (/HDA) P31539 (/HDA) P31539 (/HDA) P31539 (/HDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
7 Q0E3C8 (/IDA) Q0E3C8 (/IDA) Q587G1 (/IDA) Q8VYJ7 (/IDA) Q9FI56 (/IDA) Q9FI56 (/IDA) Q9SXJ7 (/IDA)
Chloroplast envelope GO:0009941
The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
7 P42730 (/IDA) P42762 (/IDA) P42762 (/IDA) Q8VYJ7 (/IDA) Q9FI56 (/IDA) Q9FI56 (/IDA) Q9SXJ7 (/IDA)
Nuclear periphery GO:0034399
The portion of the nuclear lumen proximal to the inner nuclear membrane.
7 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA)
TRC complex GO:0072380
An ER membrane insertion complex that contains subunits that recognize two types of transmembrane domain signals. In budding yeast the complex contains Get4p, Get5p, Sgt2p, and at least two heat shock proteins (HSPs).
7 P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA) P31539 (/IDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
5 P33416 (/HDA) P33416 (/HDA) P33416 (/HDA) P33416 (/HDA) P33416 (/HDA)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
5 P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA) P33416 (/IDA)
Plastid stroma GO:0009532
The proteinaceous ground substance of plastids.
4 Q9FI56 (/IDA) Q9FI56 (/IDA) Q9LF37 (/IDA) Q9SXJ7 (/IDA)
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
3 Q586B8 (/IDA) Q586B8 (/IDA) Q586B8 (/IDA)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
3 Q586B8 (/IDA) Q586B8 (/IDA) Q586B8 (/IDA)
Plastid GO:0009536
Any member of a family of organelles found in the cytoplasm of plants and some protists, which are membrane-bounded and contain DNA. Plant plastids develop from a common type, the proplastid.
3 Q9FI56 (/IDA) Q9FI56 (/IDA) Q9SXJ7 (/IDA)
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
2 Q9FI56 (/IDA) Q9FI56 (/IDA)
Chloroplast thylakoid membrane GO:0009535
The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.
2 Q9FI56 (/IDA) Q9FI56 (/IDA)
Chloroplast inner membrane GO:0009706
The inner, i.e. lumen-facing, lipid bilayer of the chloroplast envelope; also faces the chloroplast stroma.
2 Q9FI56 (/IDA) Q9FI56 (/IDA)
Symbiont-containing vacuole GO:0020003
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
2 Q8IIJ8 (/IDA) Q8IIJ8 (/IDA)
Symbiont-containing vacuole membrane GO:0020005
The lipid bilayer surrounding a symbiont-containing vacuole, derived from both the host and symbiont.
2 Q8IIJ8 (/IDA) Q8IIJ8 (/IDA)
Apical complex GO:0020007
A group of cytoskeletal structures and associated membrane-bounded organelles found at the anterior end of adult obligate intracellular protozoan parasites in the phylum Apicomplexa. The apical complex is involved in attachment to and penetration of the host cell, and in parasite proliferation.
2 Q8IIJ8 (/IDA) Q8IIJ8 (/IDA)
Tic complex GO:0031897
The translocon of the inner envelope of chloroplasts, which facilitates the import of proteins across the chloroplast inner membrane.
2 Q9FI56 (/TAS) Q9FI56 (/TAS)
PTEX complex GO:0097619
A protein complex that acts as a protein trafficking machinery and is responsible for the export of proteins across the parasitophorous (symbiont-containing) vacuolar membrane and into the human host cell. The PTEX complex is located in the vacuole membrane. It is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a parasite protein termed PTEX150, and exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components.
2 Q8IIJ8 (/IDA) Q8IIJ8 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 O94641 (/HDA)
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
1 O94641 (/HDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
1 E9ACE5 (/ISO)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
1 Q587G1 (/RCA)
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
1 O74402 (/ISO)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
1 A0A1D8PTP9 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 Q9SXJ7 (/IDA)