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:

"
Metalloproteases ("zincins"), catalytic domain
".

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 4972: CAAX prenyl protease 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 7 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
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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 P47154 (/IDA) Q80W54 (/IDA) Q9XVE5 (/IDA)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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 Q54FH7 (/ISS) Q8RX88 (/ISS)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
1 Q8RX88 (/IDA)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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 Q80W54 (/IMP)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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 Q10071 (/ISO)
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 O75844 (/IPI)
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.
1 O75844 (/TAS)

There are 14 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.
1 Q8RX88 (/IDA)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 O75844 (/TAS)
Nuclear envelope organization GO:0006998
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear envelope.
1 Q80W54 (/IGI)
Nuclear envelope organization GO:0006998
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear envelope.
1 Q80W54 (/IMP)
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
1 P47154 (/IDA)
Prenylated protein catabolic process GO:0030327
The chemical reactions and pathways resulting in the breakdown of prenylated proteins.
1 Q80W54 (/IDA)
Peptide mating pheromone maturation involved in conjugation with cellular fusion GO:0071432
The formation of a mature peptide mating pheromone by proteolysis and/or modification of a peptide precursor, occurring in the context of conjugation with cellular fusion.
1 P47154 (/IDA)
Peptide mating pheromone maturation involved in conjugation with cellular fusion GO:0071432
The formation of a mature peptide mating pheromone by proteolysis and/or modification of a peptide precursor, occurring in the context of conjugation with cellular fusion.
1 P47154 (/IGI)
Peptide mating pheromone maturation involved in conjugation with cellular fusion GO:0071432
The formation of a mature peptide mating pheromone by proteolysis and/or modification of a peptide precursor, occurring in the context of conjugation with cellular fusion.
1 P47154 (/IMP)
CAAX-box protein processing GO:0071586
The second process in a series of specific posttranslational modifications to the CAAX box region of CAAX box proteins, in which the last three amino acids of the protein (AAX) are removed by proteolysis.
1 Q9XVE5 (/IDA)
CAAX-box protein processing GO:0071586
The second process in a series of specific posttranslational modifications to the CAAX box region of CAAX box proteins, in which the last three amino acids of the protein (AAX) are removed by proteolysis.
1 P47154 (/IGI)
CAAX-box protein processing GO:0071586
The second process in a series of specific posttranslational modifications to the CAAX box region of CAAX box proteins, in which the last three amino acids of the protein (AAX) are removed by proteolysis.
1 P47154 (/IMP)
CAAX-box protein processing GO:0071586
The second process in a series of specific posttranslational modifications to the CAAX box region of CAAX box proteins, in which the last three amino acids of the protein (AAX) are removed by proteolysis.
1 Q10071 (/ISO)
CAAX-box protein maturation GO:0080120
A series of specific posttranslational modifications to the CAAX box region of CAAX box proteins. CAAX box proteins are eukaryotic proteins that contain a CAAX motif where the C is a cysteine, the two A residues are aliphatic amino acids and the X can be one of several amino acids. The CAAX-box proteins undergo three sequential, enzymatic, post-translational modifications essential to their targeting: First, the proteins are prenylated by one of two prenyltransferases called farnesyltransferase and geranylgeranyltransferase-I. Prenylation results in the covalent attachment of either farnesyl or geranylgeranyl isoprenoid groups to the cysteine in the CAAX box motif. Prenylation is followed by proteolytic removal of the last three amino acids of the protein (AAX). Finally, the newly exposed carboxylate group of the isoprenylcysteine is methylated by an ER-associated prenyl-dependent carboxylmethyltransferase.
1 Q8RX88 (/IDA)

There are 10 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
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
3 O75844 (/IDA) Q80W54 (/IDA) Q9XVE5 (/IDA)
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
2 Q10071 (/IDA) Q8RX88 (/IDA)
Nuclear inner membrane GO:0005637
The inner, i.e. lumen-facing, lipid bilayer of the nuclear envelope.
1 P47154 (/IMP)
Vacuole GO:0005773
A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.
1 Q8RX88 (/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 A0A1D8PL01 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 Q80W54 (/ISO)
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
1 P47154 (/IDA)
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
1 Q10071 (/ISO)
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 O75844 (/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 Q80W54 (/ISO)
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