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:
"Creatinase/prolidase N-terminal domain
".
FunFam 1: Putative xaa-Pro 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 12 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 |
|---|---|---|
|
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
|
4 | O54975 (/ISS) Q1JPJ2 (/ISS) Q6P1B1 (/ISS) Q6P1B1 (/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.
|
4 | O54975 (/ISS) Q1JPJ2 (/ISS) Q6P1B1 (/ISS) Q6P1B1 (/ISS) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
2 | O54975 (/IDA) Q9NQW7 (/IDA) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
2 | Q6P1B1 (/ISS) Q6P1B1 (/ISS) |
|
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
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.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q9NQW7 (/TAS) |
|
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
|
1 | Q9NQW7 (/IDA) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
1 | Q9NQW7 (/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 | Q9NQW7 (/IDA) |
There are 6 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 |
|---|---|---|
|
Bradykinin catabolic process GO:0010815
The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
|
4 | O54975 (/ISS) Q1JPJ2 (/ISS) Q6P1B1 (/ISS) Q6P1B1 (/ISS) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | O54975 (/IDA) Q9NQW7 (/IDA) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | Q6P1B1 (/ISS) Q6P1B1 (/ISS) |
|
Bradykinin catabolic process GO:0010815
The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
Bradykinin catabolic process GO:0010815
The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
|
1 | Q9NQW7 (/IDA) |
There are 6 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 |
|---|---|---|
|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
5 | O54975 (/IDA) Q5T6H2 (/IDA) Q5T6H2 (/IDA) Q5T6H2 (/IDA) Q9NQW7 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
3 | Q6P1B1 (/ISS) Q6P1B1 (/ISS) Q9NQW7 (/ISS) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
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 | Q6P1B1 (/ISO) Q6P1B1 (/ISO) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | O54975 (/IDA) |
|
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
1 | Q9NQW7 (/HDA) |
