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:

"
GroEL-like equatorial 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

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 19 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).
382 C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI) C5A1D5 (/IPI)
(372 more)
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
186 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(176 more)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
186 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(176 more)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
181 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(171 more)
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
178 P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI) P0A6F5 (/IPI)
(168 more)
Unfolded protein binding GO:0051082
Interacting selectively and non-covalently with an unfolded protein.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
DNA replication origin binding GO:0003688
Interacting selectively and non-covalently with the DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally.
8 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
Single-stranded DNA binding GO:0003697
Interacting selectively and non-covalently with single-stranded DNA.
8 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
Host cell surface binding GO:0046812
Interacting selectively and non-covalently with the surface of a host cell.
8 P50142 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/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.
8 P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI) P19882 (/IPI)
Mannan binding GO:2001065
Interacting selectively and non-covalently with mannan.
6 P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA)
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
3 P29197 (/IPI) P29197 (/IPI) Q8L7B5 (/IPI)
Copper ion binding GO:0005507
Interacting selectively and non-covalently with copper (Cu) ions.
3 P29197 (/IDA) P29197 (/IDA) Q8L7B5 (/IDA)
Structural constituent of ribosome GO:0003735
The action of a molecule that contributes to the structural integrity of the ribosome.
2 P29197 (/IDA) P29197 (/IDA)
ATPase binding GO:0051117
Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
2 P29185 (/IPI) P29185 (/IPI)
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
1 P50142 (/IPI)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 Q09864 (/ISS)

There are 38 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.
180 P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP) P0A6F5 (/IEP)
(170 more)
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.
178 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(168 more)
Response to radiation GO:0009314
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 electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation.
178 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(168 more)
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.
178 P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP) P0A6F5 (/IMP)
(168 more)
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.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
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.
14 Q9KLC6 (/ISS) Q9KLC6 (/ISS) Q9KLC6 (/ISS) Q9KLC6 (/ISS) Q9KLC6 (/ISS) Q9KLC6 (/ISS) Q9KNR7 (/ISS) Q9KNR7 (/ISS) Q9KNR7 (/ISS) Q9KNR7 (/ISS)
(4 more)
Positive regulation of interleukin-8 secretion GO:2000484
Any process that activates or increases the frequency, rate or extent of interleukin-8 secretion.
12 O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) O68324 (/IGI) Q9AEP7 (/IGI) Q9AEP7 (/IGI) Q9KJ23 (/IGI) Q9KJ23 (/IGI)
(2 more)
'de novo' protein folding GO:0006458
The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
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.
8 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/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.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Protein import into mitochondrial intermembrane space GO:0045041
The import of proteins into the space between the inner and outer mitochondrial membranes.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Protein stabilization GO:0050821
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Chaperone-mediated protein complex assembly GO:0051131
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP)
Protein maturation GO:0051604
Any process leading to the attainment of the full functional capacity of a protein.
8 P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/IMP) P19882 (/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.
5 P50142 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q9KKF0 (/IDA)
Aggregation of unicellular organisms GO:0098630
The clustering together of unicellular organisms in suspension form aggregates.
4 Q9KJ23 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/IDA) Q9KJ23 (/IDA)
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.
3 O66198 (/IMP) O66198 (/IMP) O66198 (/IMP)
Symbiont process GO:0044403
A process carried out by symbiont gene products that enables the interaction between two organisms living together in more or less intimate association. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
3 O66198 (/IMP) O66198 (/IMP) O66198 (/IMP)
Response to cadmium ion GO:0046686
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 cadmium (Cd) ion stimulus.
3 P29197 (/IEP) P29197 (/IEP) Q93ZM7 (/IEP)
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.
3 O66198 (/IMP) O66198 (/IMP) O66198 (/IMP)
Cellular response to temperature stimulus GO:0071502
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 temperature stimulus.
3 Q4X1P0 (/IEP) Q4X1P0 (/IEP) Q4X1P0 (/IEP)
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.
3 Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA)
Group II intron splicing GO:0000373
The splicing of Group II introns. This occurs by a ribozymic mechanism where the intron sequence forms a distinct 3D structure, characteristic of Group II introns and containing splice site consensus sequences, that is involved in catalyzing the splicing reactions, though protein factors are also required in vivo. Splicing occurs by a series of two transesterification reactions (mechanistically similar to those for splicing of nuclear mRNAs) initiated by a bulged adenosine residue within the intron sequence as the initiating nucleophile. The intron is excised as a lariat.
2 P29197 (/IPI) P29197 (/IPI)
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 P29185 (/TAS) P29185 (/TAS)
Mitochondrion organization GO:0007005
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
2 P29197 (/TAS) P29197 (/TAS)
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.
2 P50142 (/IMP) Q9KKF0 (/IMP)
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.
1 Q8L7B5 (/IDA)
Response to acidic pH GO:0010447
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 pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution.
1 Q9KKF0 (/IMP)
Asexual reproduction GO:0019954
The biological process in which new individuals are produced by either a single cell or a group of cells, in the absence of any sexual process.
1 Q54J97 (/IMP)
Protein import into mitochondrial matrix GO:0030150
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
1 Q09864 (/ISO)
Sorocarp morphogenesis GO:0031288
The process in which the sorocarp is generated and organized. An example of this process is found in Dictyostelium discoideum.
1 Q54J97 (/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.
1 O74261 (/IMP)
Hyperosmotic salinity response GO:0042538
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 detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
1 Q9KKF0 (/IMP)
Positive phototaxis GO:0046956
The directed movement of a cell or organism towards a source of light.
1 Q54J97 (/IMP)
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
1 Q09864 (/NAS)
Cellular response to osmotic stress GO:0071470
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 stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
1 Q5B041 (/IEP)
Positive regulation of cellular response to heat GO:1900036
Any process that activates or increases the frequency, rate or extent of cellular response to heat.
1 P50142 (/IDA)
Response to iron ion starvation GO:1990641
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 starvation stimulus, deprivation of iron ion.
1 Q9KKF0 (/IMP)

There are 28 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.
182 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(172 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.
178 P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA)
(168 more)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
178 P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA) P0A6F5 (/HDA)
(168 more)
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.
178 P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA) P0A6F5 (/IDA)
(168 more)
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
14 P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) P37282 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q9KJ23 (/IDA)
(4 more)
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.
13 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P29197 (/IDA) P29197 (/IDA)
(3 more)
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.
9 P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) P19882 (/HDA) Q09864 (/HDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
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.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
8 P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS) P19882 (/TAS)
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
8 P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA) P19882 (/IDA)
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 P29185 (/IDA) P29185 (/IDA) P29197 (/IDA) P29197 (/IDA) Q09864 (/IDA)
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
4 P29197 (/IDA) P29197 (/IDA) Q8L7B5 (/IDA) Q93ZM7 (/IDA)
Host cell endosome membrane GO:0044175
The lipid bilayer surrounding a host cell endosome.
3 Q5ZXP3 (/IDA) Q5ZXP3 (/IDA) Q5ZXP3 (/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 P50142 (/IDA) Q9KKF0 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 P50142 (/IDA) Q9KKF0 (/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.
2 Q8L7B5 (/IDA) Q9KKF0 (/IDA)
Cytosolic ribosome GO:0022626
A ribosome located in the cytosol.
2 P29197 (/IDA) P29197 (/IDA)
Polysomal ribosome GO:0042788
A ribosome bound to mRNA that forms part of a polysome.
2 P29197 (/IDA) P29197 (/IDA)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
1 Q9KKF0 (/IDA)
Mitochondrial intermembrane space GO:0005758
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
1 Q09864 (/IDA)
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
1 Q8L7B5 (/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.
1 Q8L7B5 (/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.
1 Q8L7B5 (/IDA)
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
1 Q09864 (/IDA)
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
1 Q09864 (/ISO)
Post-mRNA release spliceosomal complex GO:0071014
A spliceosomal complex that is formed following the release of the spliced product from the post-spliceosomal complex and contains the excised intron and three snRNPs, including U5.
1 Q09864 (/IDA)