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:
"Rhomboid-like
".
FunFam 9: Rhomboid domain containing 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 6 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 |
---|---|---|
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
3 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8BHC7 (/ISS) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
3 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8BHC7 (/ISS) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | Q8BHC7 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | Q8BHC7 (/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 | Q8BHC7 (/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 | Q8BHC7 (/IDA) |
There are 26 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 |
---|---|---|
Positive regulation of protein processing GO:0010954
Any process that increases the rate, frequency or extent of protein maturation by peptide bond cleavage.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Membrane protein intracellular domain proteolysis GO:0031293
The proteolytic cleavage of a transmembrane protein leading to the release of an intracellular domain.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Cellular response to unfolded protein GO:0034620
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Cellular response to UV GO:0034644
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
ERAD pathway GO:0036503
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Post-translational protein modification GO:0043687
The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Spermatid differentiation GO:0048515
The process whose specific outcome is the progression of a spermatid over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Membrane protein proteolysis GO:0033619
The proteolytic cleavage of a transmembrane protein leading to the release of its intracellular or ecto-domains.
|
3 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8BHC7 (/ISS) |
Positive regulation of protein catabolic process GO:0045732
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
3 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8BHC7 (/ISS) |
Positive regulation of secretion GO:0051047
Any process that activates or increases the frequency, rate or extent of the controlled release of a substance from a cell or a tissue.
|
3 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8BHC7 (/ISS) |
Cellular response to unfolded protein GO:0034620
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
|
2 | Q8TEB9 (/IEP) Q8TEB9 (/IEP) |
Membrane protein proteolysis involved in retrograde protein transport, ER to cytosol GO:1904211
Any membrane protein proteolysis that is involved in retrograde protein transport, ER to cytosol.
|
2 | Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Positive regulation of protein processing GO:0010954
Any process that increases the rate, frequency or extent of protein maturation by peptide bond cleavage.
|
1 | Q8BHC7 (/IDA) |
Membrane protein intracellular domain proteolysis GO:0031293
The proteolytic cleavage of a transmembrane protein leading to the release of an intracellular domain.
|
1 | Q8BHC7 (/IDA) |
Membrane protein proteolysis GO:0033619
The proteolytic cleavage of a transmembrane protein leading to the release of its intracellular or ecto-domains.
|
1 | Q8BHC7 (/ISO) |
Cellular response to unfolded protein GO:0034620
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
|
1 | Q8BHC7 (/IDA) |
Cellular response to UV GO:0034644
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
|
1 | Q8BHC7 (/IDA) |
ERAD pathway GO:0036503
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
1 | Q8BHC7 (/IDA) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
1 | Q8BHC7 (/IMP) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
1 | Q8BHC7 (/ISO) |
Post-translational protein modification GO:0043687
The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
|
1 | Q8BHC7 (/IDA) |
Positive regulation of protein catabolic process GO:0045732
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
1 | Q8BHC7 (/ISO) |
Spermatid differentiation GO:0048515
The process whose specific outcome is the progression of a spermatid over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
|
1 | Q8BHC7 (/IMP) |
Positive regulation of secretion GO:0051047
Any process that activates or increases the frequency, rate or extent of the controlled release of a substance from a cell or a tissue.
|
1 | Q8BHC7 (/ISO) |
Membrane protein proteolysis involved in retrograde protein transport, ER to cytosol GO:1904211
Any membrane protein proteolysis that is involved in retrograde protein transport, ER to cytosol.
|
1 | Q8BHC7 (/IDA) |
There are 8 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 |
---|---|---|
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).
|
4 | A0A024R455 (/IDA) A0A024R455 (/IDA) Q8TEB9 (/IDA) Q8TEB9 (/IDA) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
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.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
Endoplasmic reticulum quality control compartment GO:0044322
A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins.
|
4 | Q4V8F3 (/ISS) Q5RBS4 (/ISS) Q8TEB9 (/ISS) Q8TEB9 (/ISS) |
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).
|
1 | Q8BHC7 (/ISO) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | Q8BHC7 (/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 | Q8BHC7 (/IDA) |
Endoplasmic reticulum quality control compartment GO:0044322
A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins.
|
1 | Q8BHC7 (/IDA) |