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:
"Glutaredoxin
".
FunFam 42: protein disulfide-isomerase A2
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 13 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 |
---|---|---|
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
6 | A3KPF5 (/ISS) Q54EN4 (/ISS) Q66GQ3 (/ISS) Q66GQ3 (/ISS) Q9FF55 (/ISS) Q9FF55 (/ISS) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
2 | D3Z6P0 (/TAS) Q13087 (/TAS) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
2 | P54399 (/ISS) P54399 (/ISS) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
1 | Q17770 (/IDA) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
1 | Q10057 (/ISO) |
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
|
1 | Q17770 (/IDA) |
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 | Q13087 (/IPI) |
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
|
1 | Q1HGL1 (/IDA) |
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
|
1 | Q10057 (/ISO) |
Disulfide oxidoreductase activity GO:0015036
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
|
1 | Q13087 (/TAS) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | Q13087 (/IDA) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | D3Z6P0 (/ISO) |
Isomerase activity GO:0016853
Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
|
1 | Q1HGL1 (/IDA) |
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 |
---|---|---|
Response to oxidative stress GO:0006979
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
|
2 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
Nematode larval development GO:0002119
The process whose specific outcome is the progression of the nematode larva over time, from its formation to the mature structure. Nematode larval development begins with the newly hatched first-stage larva (L1) and ends with the end of the last larval stage (for example the fourth larval stage (L4) in C. elegans). Each stage of nematode larval development is characterized by proliferation of specific cell lineages and an increase in body size without alteration of the basic body plan. Nematode larval stages are separated by molts in which each stage-specific exoskeleton, or cuticle, is shed and replaced anew.
|
1 | A0A1S0S010 (/IMP) |
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
|
1 | Q54EN4 (/ISS) |
Protein folding GO:0006457
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
|
1 | Q13087 (/TAS) |
Protein retention in ER lumen GO:0006621
The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
|
1 | Q13087 (/TAS) |
Response to bacterium GO:0009617
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium.
|
1 | Q54EN4 (/HEP) |
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline GO:0018401
The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase.
|
1 | Q17770 (/IDA) |
Sexual reproduction GO:0019953
A reproduction process that creates a new organism by combining the genetic material of two gametes, which may come from two organisms or from a single organism, in the case of self-fertilizing hermaphrodites, e.g. C. elegans, or self-fertilization in plants. It occurs both in eukaryotes and prokaryotes: in multicellular eukaryotic organisms, an individual is created anew; in prokaryotes, the initial cell has additional or transformed genetic material. In a process called genetic recombination, genetic material (DNA) originating from two gametes join up so that homologous sequences are aligned with each other, and this is followed by exchange of genetic information. After the new recombinant chromosome is formed, it is passed on to progeny.
|
1 | Q54EN4 (/IEP) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
1 | Q17770 (/HEP) |
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
1 | Q10057 (/IC) |
Protein folding in endoplasmic reticulum GO:0034975
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
|
1 | Q13087 (/TAS) |
Macromolecule modification GO:0043412
The covalent alteration of one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule, resulting in a change in its properties.
|
1 | Q17770 (/IDA) |
Oxidation-reduction process GO:0055114
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
|
1 | Q17770 (/IDA) |
Protein deglutathionylation GO:0080058
The protein modification process in which a glutathione molecule is removed from a protein amino acid by breaking a disulfide linkage.
|
1 | Q17770 (/IDA) |
There are 20 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).
|
8 | A3KPF5 (/IDA) P54399 (/IDA) P54399 (/IDA) Q17770 (/IDA) Q66GQ3 (/IDA) Q66GQ3 (/IDA) Q9FF55 (/IDA) Q9FF55 (/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).
|
3 | P54399 (/HDA) P54399 (/HDA) Q10057 (/HDA) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
|
2 | P54399 (/IDA) P54399 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
|
2 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
2 | Q9FF55 (/IDA) Q9FF55 (/IDA) |
Endomembrane system GO:0012505
A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
|
2 | P54399 (/HDA) P54399 (/HDA) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Fusome GO:0045169
A large intracellular spectrin-rich structure that has been found in insect germline cells and mammalian hematopoietic cells. The fusome is an elongated, branched structure, formed from the spherical spectrosome organelle.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Cell pole GO:0060187
Either of two different areas at opposite ends of an axis of a cell.
|
2 | P54399 (/IDA) P54399 (/IDA) |
Spindle envelope GO:0070732
An organelle envelope that surrounds the chromosomes and the central part of the spindle apparatus during mitosis and meiosis; observed in many invertebrates. The spindle envelope consists of membrane layers, called parafusorial membranes, derived from endoplasmic reticulum membrane; in male meiosis it forms during prometaphase and persists until early in the ensuing interphase.
|
2 | P54399 (/IDA) P54399 (/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).
|
1 | Q13087 (/TAS) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | Q10057 (/ISO) |
Procollagen-proline 4-dioxygenase complex GO:0016222
A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase.
|
1 | Q17770 (/IDA) |
Extracellular matrix GO:0031012
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
|
1 | Q54EN4 (/HDA) |
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
|
1 | Q54EN4 (/HDA) |