The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:
"Neutral Protease Domain 2
".
FunFam 5143: Membrane alanine aminopeptidase N
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.
|
3 | O96935 (/IDA) P04825 (/IDA) Q8IEK1 (/IDA) |
|
Metalloexopeptidase activity GO:0008235
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of 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.
|
3 | Q48FU2 (/ISS) Q60AS1 (/ISS) Q87YK7 (/ISS) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q83EI2 (/ISS) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | P04825 (/IPI) |
|
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 | Q5E5B9 (/IDA) |
|
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 | Q5E5B9 (/IMP) |
There are 4 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.
|
7 | Q48FU2 (/ISS) Q60AS1 (/ISS) Q74GE2 (/ISS) Q83EI2 (/ISS) Q87YK7 (/ISS) Q8EDZ0 (/ISS) Q8IEK1 (/ISS) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | O96935 (/IDA) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | P04825 (/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.
|
1 | P04825 (/IGI) |
There are 4 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.
|
3 | O96935 (/IDA) Q5E5B9 (/IDA) Q8IEK1 (/IDA) |
|
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.
|
1 | Q8IEK1 (/IDA) |
|
Microneme GO:0020009
A small, elongated secretory organelle that forms part of the apical complex, located along the main axis of an apicomplexan parasite cell within the extreme apical region and at the periphery under the inner membrane complex. Of the specialized secretory compartments identified in apicomplexans, micronemes discharge their contents first, during initial contact of the parasite's apical pole with the host cell surface. Micronemal proteins function during parasite attachment and penetration into the target cell.
|
1 | Q8IEK1 (/IDA) |
|
Food vacuole GO:0020020
Vacuole within a parasite used for digestion of the host cell cytoplasm. An example of this component is found in the Apicomplexa.
|
1 | Q8IEK1 (/IDA) |