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
".
FunFam 220: ATP-dependent protease ATPase subunit HslU
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 7 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 |
---|---|---|
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
99 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(89 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).
|
99 |
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
(89 more) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
99 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(89 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
99 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(89 more) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
99 |
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
(89 more) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
99 |
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
P0A6H5 (/IPI)
(89 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.
|
4 | Q9KNQ7 (/ISS) Q9KNQ7 (/ISS) Q9KNQ7 (/ISS) Q9KNQ7 (/ISS) |
There are 9 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.
|
99 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(89 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.
|
99 |
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
P0A6H5 (/IEP)
(89 more) |
Protein hexamerization GO:0034214
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
|
99 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(89 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.
|
99 |
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
P0A6H5 (/IMP)
(89 more) |
Mitochondrial DNA replication GO:0006264
The process in which new strands of DNA are synthesized in the mitochondrion.
|
6 | Q382V8 (/IMP) Q382V8 (/IMP) Q57VB1 (/IMP) Q57VB1 (/IMP) Q57VB1 (/IMP) Q57VB1 (/IMP) |
Mitochondrial DNA replication GO:0006264
The process in which new strands of DNA are synthesized in the mitochondrion.
|
5 | Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QI03 (/ISO) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
4 | Q9KNQ7 (/ISS) Q9KNQ7 (/ISS) Q9KNQ7 (/ISS) Q9KNQ7 (/ISS) |
Rolling circle DNA replication GO:0070581
A DNA-dependent DNA replication process in which a single-stranded DNA molecule is synthesized from a circular duplex template. Replication typically does not cease when one circumference has been replicated, but continues around the circumference several more times, producing a long single strand comprising multimers of the replicon.
|
4 | Q57VB1 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) |
Rolling circle DNA replication GO:0070581
A DNA-dependent DNA replication process in which a single-stranded DNA molecule is synthesized from a circular duplex template. Replication typically does not cease when one circumference has been replicated, but continues around the circumference several more times, producing a long single strand comprising multimers of the replicon.
|
4 | Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) |
There are 11 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 |
---|---|---|
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.
|
105 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(95 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.
|
99 |
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
P0A6H5 (/IDA)
(89 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
99 |
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
P0A6H5 (/HDA)
(89 more) |
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
|
6 | Q382V8 (/IDA) Q382V8 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) |
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.
|
5 | Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QI03 (/ISO) |
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
|
5 | Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QI03 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
4 | Q57VB1 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) Q57VB1 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
4 | Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/ISO) Q4QFH5 (/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.
|
4 | Q57VB1 (/RCA) Q57VB1 (/RCA) Q57VB1 (/RCA) Q57VB1 (/RCA) |
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.
|
2 | Q382V8 (/IDA) Q382V8 (/IDA) |
Kinetoplast GO:0020023
A sub-structure within the large single mitochondrion of kinetoplastid parasites and which is closely associated with the flagellar pocket and basal body of the flagellum.
|
2 | Q382V8 (/IDA) Q382V8 (/IDA) |