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:

"
Creatinase/methionine aminopeptidase superfamily
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 9058: Probable Xaa-Pro aminopeptidase P

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 15 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) Q54G06 (/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 O44750 (/IDA) Q8IKT5 (/IDA) Q9NQW7 (/IDA) Q9VJG0 (/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.
4 O54975 (/ISS) Q1JPJ2 (/ISS) Q54G06 (/ISS) Q6P1B1 (/ISS)
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
3 F4JQH3 (/IDA) O54975 (/IDA) Q9NQW7 (/IDA)
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
2 O43895 (/TAS) Q9NQW7 (/TAS)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
2 O44750 (/IPI) Q9NQW7 (/IPI)
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
1 Q6P1B1 (/ISO)
Aminopeptidase activity GO:0004177
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain.
1 Q6P1B1 (/ISS)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
1 O44750 (/IDA)
N-1-naphthylphthalamic acid binding GO:0010013
Interacting selectively and non-covalently with N-1-naphthylphthalamic acid, an auxin transport inhibitor.
1 F4JQH3 (/IDA)
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
1 Q9NQW7 (/IDA)
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
1 Q6P1B1 (/ISO)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
1 Q8IKT5 (/IDA)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
1 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.
1 Q6P1B1 (/ISO)

There are 12 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.
4 O44750 (/IDA) O54975 (/IDA) Q9NQW7 (/IDA) Q9VJG0 (/IDA)
Bradykinin catabolic process GO:0010815
The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
4 O54975 (/ISS) Q1JPJ2 (/ISS) Q54G06 (/ISS) Q6P1B1 (/ISS)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
3 Q6P1B1 (/ISS) Q8IKT5 (/ISS) Q9KVS2 (/ISS)
C-terminal protein lipidation GO:0006501
The covalent attachment of a lipid group to the carboxy terminus of a protein.
1 O43895 (/TAS)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q6P1B1 (/ISO)
Auxin polar transport GO:0009926
The unidirectional movement of auxin in the stem from tip to base along the vector of gravity or basipetally.
1 F4JQH3 (/TAS)
Bradykinin catabolic process GO:0010815
The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
1 Q9NQW7 (/IDA)
Bradykinin catabolic process GO:0010815
The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
1 Q6P1B1 (/ISO)
Negative regulation of transcription from RNA polymerase II promoter in response to iron GO:0034396
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
1 Q07825 (/IGI)
Negative regulation of transcription from RNA polymerase II promoter in response to iron GO:0034396
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
1 Q07825 (/IMP)
Negative regulation of transcription from RNA polymerase II promoter in response to iron GO:0034396
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
1 Q09795 (/ISO)
Hemoglobin catabolic process GO:0042540
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
1 Q8IKT5 (/TAS)

There are 14 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.
8 F4JQH3 (/IDA) O54975 (/IDA) Q07825 (/IDA) Q09795 (/IDA) Q5T6H7 (/IDA) Q8IKT5 (/IDA) Q9NQW7 (/IDA) Q9VJG0 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 O44750 (/IDA) O54975 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 Q6P1B1 (/ISS) Q9NQW7 (/ISS)
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.
2 O43895 (/IDA) Q9NQW7 (/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.
2 B1AVD1 (/ISO) Q6P1B1 (/ISO)
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 O43895 (/TAS)
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 Q09795 (/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 Q6P1B1 (/ISO)
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 F4JQH3 (/IDA)
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 O43895 (/TAS)
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
1 Q8RY11 (/IDA)
Chloroplast stroma GO:0009570
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
1 Q8RY11 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 O43895 (/TAS)
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 Q8IKT5 (/IDA)