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:

"
Acid Proteases
".

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.
« Back to all FunFams

FunFam 36: Vacuolar aspartic protease

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 5 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
Aspartic-type endopeptidase activity GO:0004190
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
7 P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA)
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.
7 P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA)
Oligosaccharide binding GO:0070492
Interacting selectively and non-covalently with any oligosaccharide, a molecule with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
7 P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA)
Disordered domain specific binding GO:0097718
Interacting selectively and non-covalently with a disordered domain of a protein.
7 P07267 (/IPI) P07267 (/IPI) P07267 (/IPI) P07267 (/IPI) P07267 (/IPI) P07267 (/IPI) P07267 (/IPI)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
1 Q59U59 (/IDA)

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
Vacuolar protein processing GO:0006624
Protein processing that takes place in the vacuole. Most protein processing in the vacuole represents proteolytic cleavage of precursors to form active enzymes.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP)
Autophagy GO:0006914
The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP)
Cellular response to starvation GO:0009267
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 deprivation of nourishment.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP)
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.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP)
Lysosomal microautophagy GO:0016237
The transfer of cytosolic components into the lysosomal compartment by direct invagination of the lysosomal membrane without prior sequestration into an autophagosome. The engulfing membranes fuse, resulting in the lysosomal delivery of the cargo wrapped in a single membrane derived from the invaginated lysosomal membrane. In S. cerevisiae, the vacuole is the lysosomal compartment.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP)
Protein localization by the Cvt pathway GO:0032258
A cytoplasm to vacuole targeting pathway that uses machinery common with autophagy. The Cvt vesicle is formed when the receptor protein, Atg19, binds to the complexes of the target protein (aminopeptidase or alpha-mannosidase homododecamers), forming the Cvt complex. Atg11 binds to Atg9 and transports the Cvt complex to the pre-autophagosome (PAS). The phagophore membrane expands around the Cvt complex (excluding bulk cytoplasm) forming the Cvt vesicle. This pathway is mostly observed in yeast.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/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.
7 P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP) P07267 (/IMP)

There are 5 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.
7 P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA)
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.
7 P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/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.
7 P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/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).
7 P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA) P07267 (/HDA)
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
7 P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA) P07267 (/IDA)