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:
"2-enoyl-CoA Hydratase; Chain A, domain 1
".
FunFam 1: ATP-dependent Clp protease proteolytic 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 14 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 |
---|---|---|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
202 |
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
(192 more) |
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).
|
168 |
M0RAD5 (/IPI)
O88696 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
(158 more) |
ATP-dependent peptidase activity GO:0004176
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the hydrolysis of peptide bonds.
|
165 |
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
(155 more) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of 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).
|
165 |
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
(155 more) |
ATPase binding GO:0051117
Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
|
165 |
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
P0A6G7 (/IPI)
(155 more) |
ATP-dependent peptidase activity GO:0004176
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the hydrolysis of peptide bonds.
|
12 |
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
P80244 (/IMP)
(2 more) |
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 | O88696 (/ISS) Q2KHU4 (/ISS) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
2 | Q9FN42 (/IDA) Q9FN42 (/IDA) |
Cobalt ion binding GO:0050897
Interacting selectively and non-covalently with a cobalt (Co) ion.
|
2 | Q9FN42 (/IDA) Q9FN42 (/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).
|
1 | Q16740 (/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).
|
1 | O88696 (/ISO) |
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.
|
1 | Q16740 (/TAS) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | M0RAD5 (/IDA) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | O88696 (/ISO) |
There are 20 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 |
---|---|---|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
165 |
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
(155 more) |
Protein quality control for misfolded or incompletely synthesized proteins GO:0006515
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
|
165 |
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
(155 more) |
Response to temperature stimulus GO:0009266
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 temperature stimulus.
|
165 |
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
P0A6G7 (/EXP)
(155 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.
|
165 |
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
(155 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.
|
165 |
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
P0A6G7 (/IEP)
(155 more) |
Proteasomal protein catabolic process GO:0010498
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome.
|
165 |
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
P0A6G7 (/IMP)
(155 more) |
Positive regulation of single-species biofilm formation GO:1900192
Any process that activates or increases the frequency, rate or extent of single-species biofilm formation.
|
16 |
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
I4K5Z9 (/IMP)
(6 more) |
Single-species biofilm formation GO:0044010
A process in which planktonically growing microorganisms of the same species grow at a liquid-air interface or on a solid substrate under the flow of a liquid and produce extracellular polymers that facilitate matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
|
11 |
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
(1 more) |
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.
|
11 |
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
(1 more) |
Cellular response to antibiotic GO:0071236
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 antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
|
11 |
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
(1 more) |
Bacterial-type flagellum-dependent swarming motility GO:0071978
Bacterial-type flagellum-dependent cell motility in which the action of numerous flagella results in the smooth movement of a group of cells along a solid surface. Swarming motility is observed in groups of bacteria.
|
11 |
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
Q9I2U1 (/IMP)
(1 more) |
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.
|
2 | Q94B60 (/IMP) Q94B60 (/IMP) |
Regulation of timing of transition from vegetative to reproductive phase GO:0048510
The process controlling the point in time during development when a vegetative meristem will change its identity to become an inflorescence or floral meristem, and/or the rate at which the change occurs.
|
2 | Q94B60 (/IMP) Q94B60 (/IMP) |
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
2 | O88696 (/ISS) Q2KHU4 (/ISS) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9VKY3 (/ISS) |
Protein quality control for misfolded or incompletely synthesized proteins GO:0006515
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
|
1 | O88696 (/ISA) |
Protein homooligomerization GO:0051260
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | M0RAD5 (/IDA) |
Protein homooligomerization GO:0051260
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | O88696 (/ISO) |
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
1 | Q16740 (/IDA) |
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
1 | O88696 (/ISO) |
There are 21 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.
|
165 |
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
(155 more) |
HslUV protease complex GO:0009376
A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer.
|
165 |
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
P0A6G7 (/IDA)
(155 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
165 |
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
P0A6G7 (/HDA)
(155 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.
|
7 | M0R208 (/IDA) M0R208 (/IDA) M0RAD5 (/IDA) O88696 (/IDA) Q16740 (/IDA) Q9FN42 (/IDA) Q9FN42 (/IDA) |
Plastid stroma GO:0009532
The proteinaceous ground substance of plastids.
|
6 | Q94B60 (/IDA) Q94B60 (/IDA) Q9FN42 (/IDA) Q9FN42 (/IDA) Q9SXJ6 (/IDA) Q9SXJ6 (/IDA) |
Chloroplastic endopeptidase Clp complex GO:0009840
A Clp endopeptidase complex located in the chloroplast.
|
6 | Q94B60 (/IDA) Q94B60 (/IDA) Q9FN42 (/IDA) Q9FN42 (/IDA) Q9SXJ6 (/IDA) Q9SXJ6 (/IDA) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
4 | Q94B60 (/IDA) Q94B60 (/IDA) Q9SXJ6 (/IDA) Q9SXJ6 (/IDA) |
Chloroplast thylakoid membrane GO:0009535
The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.
|
4 | Q94B60 (/IDA) Q94B60 (/IDA) Q9FN42 (/IDA) Q9FN42 (/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.
|
4 | Q94B60 (/IDA) Q94B60 (/IDA) Q9SXJ6 (/IDA) Q9SXJ6 (/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.
|
4 | Q94B60 (/IDA) Q94B60 (/IDA) Q9SXJ6 (/IDA) Q9SXJ6 (/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.
|
2 | O88696 (/ISS) Q2KHU4 (/ISS) |
Endopeptidase Clp complex GO:0009368
A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form.
|
2 | O88696 (/ISS) Q2KHU4 (/ISS) |
Chloroplast thylakoid GO:0009534
Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana.
|
2 | Q9SXJ6 (/IDA) Q9SXJ6 (/IDA) |
Thylakoid GO:0009579
A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation.
|
2 | Q94B60 (/IDA) Q94B60 (/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.
|
1 | O88696 (/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 | O88696 (/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 | Q9VKY3 (/ISS) |
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 | Q16740 (/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.
|
1 | O88696 (/ISO) |
Endopeptidase Clp complex GO:0009368
A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form.
|
1 | Q16740 (/IDA) |
Endopeptidase Clp complex GO:0009368
A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form.
|
1 | O88696 (/ISO) |