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:
"Peptidase M1, alanyl aminopeptidase, C-terminal domain
".
FunFam 1: 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 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 |
|---|---|---|
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
19 |
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
P04825 (/IDA)
(9 more) |
|
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).
|
19 |
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
(9 more) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
19 |
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
P04825 (/IPI)
(9 more) |
|
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 2 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.
|
19 |
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
P04825 (/IMP)
(9 more) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q8EDZ0 (/ISS) |
There are 1 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.
|
1 | Q5E5B9 (/IDA) |
