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:
"alpha/beta hydrolase
".
FunFam 130: Carboxypeptidase
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 3 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 |
|---|---|---|
|
Serine-type carboxypeptidase activity GO:0004185
Catalysis of the hydrolysis of a peptide bond not more than three residues from the C-terminus of 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).
|
3 | P16675 (/ISS) P16675 (/ISS) Q6AYS3 (/ISS) |
|
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).
|
3 | P16675 (/IPI) P16675 (/IPI) Q6AYS3 (/IPI) |
|
Serine-type carboxypeptidase activity GO:0004185
Catalysis of the hydrolysis of a peptide bond not more than three residues from the C-terminus of 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 | P16675 (/ISO) P16675 (/ISO) |
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.
|
3 | P16675 (/ISS) P16675 (/ISS) Q6AYS3 (/ISS) |
|
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
|
3 | P16675 (/ISS) P16675 (/ISS) Q6AYS3 (/ISS) |
|
Negative regulation of chaperone-mediated autophagy GO:1904715
Any process that stops, prevents or reduces the frequency, rate or extent of chaperone-mediated autophagy.
|
3 | P16675 (/ISS) P16675 (/ISS) Q6AYS3 (/ISS) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | P16675 (/ISO) P16675 (/ISO) |
|
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
|
2 | P16675 (/IMP) P16675 (/IMP) |
|
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
|
2 | P16675 (/ISO) P16675 (/ISO) |
|
Negative regulation of chaperone-mediated autophagy GO:1904715
Any process that stops, prevents or reduces the frequency, rate or extent of chaperone-mediated autophagy.
|
2 | P16675 (/IMP) P16675 (/IMP) |
|
Negative regulation of chaperone-mediated autophagy GO:1904715
Any process that stops, prevents or reduces the frequency, rate or extent of chaperone-mediated autophagy.
|
2 | P16675 (/ISO) P16675 (/ISO) |
|
Negative regulation of chaperone-mediated autophagy GO:1904715
Any process that stops, prevents or reduces the frequency, rate or extent of chaperone-mediated autophagy.
|
1 | Q6AYS3 (/NAS) |
There are 7 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 |
|---|---|---|
|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | P16675 (/ISO) P16675 (/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.
|
2 | P16675 (/HDA) P16675 (/HDA) |
|
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
2 | P16675 (/ISO) P16675 (/ISO) |
|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | X6R5C5 (/IDA) |
|
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
|
1 | Q6AYS3 (/IDA) |
|
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
1 | X6R5C5 (/IDA) |
|
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
|
1 | O76725 (/HDA) |
