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
".

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 18: 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 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
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).
5 P00729 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI)
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).
4 P38109 (/ISA) P38109 (/ISA) P38109 (/ISA) P38109 (/ISA)
Serine hydrolase activity GO:0017171
Catalysis of the hydrolysis of a substrate 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).
4 P38109 (/HDA) P38109 (/HDA) P38109 (/HDA) P38109 (/HDA)
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 O13849 (/IDA) P00729 (/IDA)
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 P00729 (/IMP) Q96VC4 (/IMP)
Carboxypeptidase activity GO:0004180
Catalysis of the hydrolysis of the terminal or penultimate peptide bond at the C-terminal end of a peptide or polypeptide.
1 Q96VC4 (/IDA)
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).
1 Q38CD7 (/ISM)
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).
1 P00729 (/IPI)

There are 8 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
Macroautophagy GO:0016236
The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded.
5 P00729 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI)
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
5 P00729 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI)
Phytochelatin biosynthetic process GO:0046938
The chemical reactions and pathways resulting in the formation of phytochelatins, any of a group of peptides that bind metals (Cd, Zn, Cu, Pb, Hg) in thiolate coordination complexes. The structure is of the type (gamma-glutamyl-cysteinyl)n-glycine, where n is 2 to 11.
4 P38109 (/IGI) P38109 (/IGI) P38109 (/IGI) P38109 (/IGI)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q38CD7 (/ISM)
Protein catabolic process in the vacuole GO:0007039
The chemical reactions and pathways resulting in the breakdown of a protein in the vacuole, usually by the action of vacuolar proteases.
1 P00729 (/TAS)
Response to drug GO:0042493
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
1 Q38CD7 (/IMP)
Phytochelatin biosynthetic process GO:0046938
The chemical reactions and pathways resulting in the formation of phytochelatins, any of a group of peptides that bind metals (Cd, Zn, Cu, Pb, Hg) in thiolate coordination complexes. The structure is of the type (gamma-glutamyl-cysteinyl)n-glycine, where n is 2 to 11.
1 P00729 (/IDA)
Phytochelatin biosynthetic process GO:0046938
The chemical reactions and pathways resulting in the formation of phytochelatins, any of a group of peptides that bind metals (Cd, Zn, Cu, Pb, Hg) in thiolate coordination complexes. The structure is of the type (gamma-glutamyl-cysteinyl)n-glycine, where n is 2 to 11.
1 P00729 (/IMP)

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
Fungal-type vacuole GO:0000324
A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
6 O13849 (/HDA) P00729 (/HDA) P38109 (/HDA) P38109 (/HDA) P38109 (/HDA) P38109 (/HDA)
Fungal-type vacuole lumen GO:0000328
The volume enclosed within the vacuolar membrane of a vacuole, the shape of which correlates with cell cycle phase. An example of this structure is found in Saccharomyces cerevisiae.
6 P00729 (/IDA) P38109 (/IDA) P38109 (/IDA) P38109 (/IDA) P38109 (/IDA) Q2TYA1 (/IDA)
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
2 P00729 (/IDA) Q96VC4 (/IDA)
Fungal-type vacuole GO:0000324
A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
1 P00729 (/IDA)
Fungal-type vacuole lumen GO:0000328
The volume enclosed within the vacuolar membrane of a vacuole, the shape of which correlates with cell cycle phase. An example of this structure is found in Saccharomyces cerevisiae.
1 Q96VC4 (/TAS)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P00729 (/HDA)
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
1 P00729 (/HDA)