The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"P-loop containing nucleotide triphosphate hydrolases
".
FunFam 5: ATP-dependent Clp protease ATP-binding subunit Clp...
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 8 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).
|
191 |
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
(181 more) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
181 |
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
(171 more) |
ATP-dependent peptidase activity GO:0004176
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the hydrolysis of peptide bonds.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 more) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 more) |
ATPase activity GO:0016887
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 more) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
181 |
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
(171 more) |
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
|
181 |
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
P0A6H1 (/IPI)
(171 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.
|
12 |
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
Q9KQS7 (/ISS)
(2 more) |
There are 7 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 denaturation GO:0030164
Structural change in proteins which destroys the native, active configuration without rupture of peptide bonds.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 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.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 more) |
Cell division GO:0051301
The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
|
181 |
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
P0A6H1 (/IGI)
(171 more) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
49 |
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
Q81LB9 (/ISS)
(39 more) |
Protein catabolic process GO:0030163
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
14 |
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
P50866 (/IMP)
(4 more) |
Negative regulation of protein polymerization GO:0032272
Any process that stops, prevents, or reduces the frequency, rate or extent of the process of creating protein polymers.
|
10 | P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) P9WPB9 (/IDA) |
Cell division GO:0051301
The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
|
10 | P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) P9WPB9 (/IMP) |
There are 3 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.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 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.
|
181 |
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
P0A6H1 (/IDA)
(171 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.
|
10 | P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) P9WPB9 (/HDA) |