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:
"Zn peptidases
".
FunFam 34806: probable leucine aminopeptidase 2
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 9 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 | P37302 (/IDA) Q2U1F3 (/IDA) Q8J2N2 (/IDA) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | P37302 (/IMP) |
|
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
|
1 | Q81JU2 (/ISS) |
|
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
1 | P81715 (/TAS) |
|
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 | Q306T3 (/IPI) |
|
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
|
1 | Q9KLD3 (/ISS) |
|
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 | P81715 (/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 | P83913 (/ISS) |
|
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | P81715 (/TAS) |
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.
|
3 | P81715 (/IDA) Q2U1F3 (/IDA) Q9HZQ8 (/IDA) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
3 | P83913 (/ISS) Q81JU2 (/ISS) Q9KLD3 (/ISS) |
|
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 | P37302 (/IDA) |
|
Protein secretion by the type II secretion system GO:0015628
The process in which proteins are secreted across the outer membrane of Gram-negative bacteria by the type II secretion system. Proteins using this pathway are first translocated across the cytoplasmic membrane via the Sec or Tat pathways.
|
1 | Q9HZQ8 (/IDA) |
|
Protein transport by the Sec complex GO:0043952
The process in which unfolded proteins are transported across the cytoplasmic membrane in Gram-positive and Gram-negative bacteria by the Sec complex, in a process involving proteolytic cleavage of an N-terminal signal peptide.
|
1 | Q9HZQ8 (/IDA) |
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 |
|---|---|---|
|
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.
|
3 | C8V659 (/IDA) P96264 (/IDA) Q2U1F3 (/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.
|
1 | P37302 (/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 | P81715 (/TAS) |
|
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
1 | P96264 (/IDA) |
