CATH Superfamily 2.60.40.1910
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: waiting to be named.
FunFam 4: Aminopeptidase
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 |
---|---|---|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
6 | P37898 (/ISS) P37898 (/ISS) P37898 (/ISS) P37898 (/ISS) P37898 (/ISS) P37898 (/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.
|
5 | A2QIL3 (/IDA) A2QIL3 (/IDA) P32454 (/IDA) P32454 (/IDA) Q59KZ1 (/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).
|
1 | Q9USX1 (/IPI) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in 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 | Q59KZ1 (/IDA) |
Metallopeptidase activity GO:0008237
Catalysis of the hydrolysis of peptide bonds 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 | Q386F5 (/ISM) |
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 | Q9USX1 (/ISM) |
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 |
---|---|---|
Glycogen metabolic process GO:0005977
The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages.
|
6 | P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
6 | P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) P37898 (/IMP) |
Peptide catabolic process GO:0043171
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
4 | A2QIL3 (/IDA) A2QIL3 (/IDA) P32454 (/IDA) P32454 (/IDA) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | A2QIL3 (/IDA) A2QIL3 (/IDA) |
Peptide catabolic process GO:0043171
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
|
2 | P32454 (/IMP) P32454 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q386F5 (/ISM) |
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
|
1 | Q9USX1 (/NAS) |
Protein localization by the NVT pathway GO:0120113
A pathway targeting soluble cytosolic proteins to the vacuole lumen. It uses a selective autophagy receptor protein Nbr1, which is an ortholog of mammalian NBR1, and is remotely related to S. cerevisiae Cvt pathway receptor protein Atg19. Similar to the Cvt pathway, the cargos transported by this pathway are hydrolases, which presumably contribute to the hydrolytic activities in the vacuole lumen. Different from the Cvt pathway, this pathway does not require the macroautophagy machinery, but instead relies on the ESCRT machinery for cargo sequestration. This pathway is observed in the fission yeast S. pombe.
|
1 | Q9USX1 (/IMP) |
There are 11 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 |
---|---|---|
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
8 | P32454 (/HDA) P32454 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
6 | P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) P37898 (/HDA) |
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.
|
5 | P32454 (/IDA) P32454 (/IDA) Q59KZ1 (/IDA) Q5BCU2 (/IDA) Q5BCU2 (/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.
|
2 | P32454 (/HDA) P32454 (/HDA) |
Cell wall-bounded periplasmic space GO:0030287
The region between the plasma membrane and the cell wall in organisms lacking an outer cell membrane such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.
|
2 | P32454 (/IDA) P32454 (/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 | Q9USX1 (/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.
|
1 | Q59KZ1 (/ISM) |
Multivesicular body GO:0005771
A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
|
1 | Q9USX1 (/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 | Q9USX1 (/HDA) |
Fungal-type cell wall GO:0009277
A rigid yet dynamic structure surrounding the plasma membrane that affords protection from stresses and contributes to cell morphogenesis, consisting of extensively cross-linked glycoproteins and carbohydrates. The glycoproteins may be modified with N- or O-linked carbohydrates, or glycosylphosphatidylinositol (GPI) anchors; the polysaccharides are primarily branched glucans, including beta-linked and alpha-linked glucans, and may also include chitin and other carbohydrate polymers, but not cellulose or pectin. Enzymes involved in cell wall biosynthesis are also found in the cell wall. Note that some forms of fungi develop a capsule outside of the cell wall under certain circumstances; this is considered a separate structure.
|
1 | Q59KZ1 (/IDA) |
NVT complex GO:0061957
A protein complex that is capable of contributing to protein localization by the NVT pathway. In fission yeast, the Nvt complex consists of Ape2, Lap2 and Nbr1.
|
1 | Q9USX1 (/IPI) |