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:
"Aminopeptidase i, Domain 2
".
FunFam 1: Aspartyl aminopeptidase 1
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 6 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 |
---|---|---|
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
8 | O36014 (/IDA) P14904 (/IDA) P14904 (/IDA) P14904 (/IDA) P14904 (/IDA) Q9LST0 (/IDA) Q9LST0 (/IDA) Q9LZ26 (/IDA) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
6 | P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) |
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).
|
5 | P14904 (/IPI) P14904 (/IPI) P14904 (/IPI) P14904 (/IPI) Q54M70 (/IPI) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
5 | P14904 (/IPI) P14904 (/IPI) P14904 (/IPI) P14904 (/IPI) Q19087 (/IPI) |
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q54M70 (/ISS) |
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
1 | A0A1D8PJE0 (/ISS) |
There are 5 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.
|
10 | O36014 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) Q9LST0 (/IDA) Q9LST0 (/IDA) Q9LZ26 (/IDA) |
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.
|
4 | P14904 (/IMP) P14904 (/IMP) P14904 (/IMP) P14904 (/IMP) |
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
|
3 | O36014 (/IDA) Q9LST0 (/IDA) Q9LST0 (/IDA) |
Response to cadmium ion GO:0046686
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 cadmium (Cd) ion stimulus.
|
2 | Q9LST0 (/IEP) Q9LST0 (/IEP) |
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 | A0A1D8PJE0 (/ISS) |
There are 12 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 |
---|---|---|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
10 | P14904 (/HDA) P14904 (/HDA) P14904 (/HDA) P14904 (/HDA) P38821 (/HDA) P38821 (/HDA) P38821 (/HDA) P38821 (/HDA) P38821 (/HDA) P38821 (/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 | P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/IDA) P38821 (/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.
|
5 | A0A1D8PJE0 (/IDA) P14904 (/IDA) P14904 (/IDA) P14904 (/IDA) P14904 (/IDA) |
Cvt complex GO:0034270
A protein complex that is involved in the Cvt pathway. In budding yeast, the Cvt complex consists of multimers of preApe1p.
|
4 | P14904 (/IDA) P14904 (/IDA) P14904 (/IDA) P14904 (/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 | C8V7I0 (/IDA) C8VJ09 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q57V45 (/IDA) Q57V45 (/IDA) |
Vacuole GO:0005773
A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.
|
2 | Q9LST0 (/IDA) Q9LST0 (/IDA) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
2 | Q9LST0 (/IDA) Q9LST0 (/IDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | Q9LST0 (/IDA) Q9LST0 (/IDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | O36014 (/HDA) |
Chloroplast stroma GO:0009570
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
|
1 | Q9LZ26 (/IDA) |
Motile cilium GO:0031514
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
|
1 | E9AE98 (/ISO) |