The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"Glutaredoxin
".
FunFam 84: Protein disulfide-isomerase A4
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 |
---|---|---|
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
10 | F1SAD9 (/ISS) G3IDT6 (/ISS) G3RY30 (/ISS) H2QVK7 (/ISS) H9G279 (/ISS) H9G279 (/ISS) M3W9X1 (/ISS) P08003 (/ISS) P13667 (/ISS) P13667 (/ISS) |
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).
|
3 | P13667 (/IPI) P13667 (/IPI) P38659 (/IPI) |
RNA binding GO:0003723
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
|
2 | P13667 (/HDA) P13667 (/HDA) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
2 | P13667 (/IDA) P13667 (/IDA) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
1 | P38659 (/IDA) |
Protein disulfide isomerase activity GO:0003756
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
|
1 | P08003 (/ISO) |
Peptide disulfide oxidoreductase activity GO:0015037
Catalysis of the reaction: a peptide with reduced sulfide groups = a peptide with oxidized disulfide bonds.
|
1 | P08003 (/ISO) |
There are 6 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 |
---|---|---|
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
|
10 | F1SAD9 (/ISS) G3IDT6 (/ISS) G3RY30 (/ISS) H2QVK7 (/ISS) H9G279 (/ISS) H9G279 (/ISS) M3W9X1 (/ISS) P08003 (/ISS) P13667 (/ISS) P13667 (/ISS) |
Protein secretion GO:0009306
The controlled release of proteins from a cell.
|
2 | P13667 (/TAS) P13667 (/TAS) |
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
|
1 | P38659 (/IDA) |
Chaperone-mediated protein folding GO:0061077
The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
|
1 | P08003 (/ISO) |
Positive regulation of protein folding GO:1903334
Any process that activates or increases the frequency, rate or extent of protein folding.
|
1 | P38659 (/IDA) |
Positive regulation of protein folding GO:1903334
Any process that activates or increases the frequency, rate or extent of protein folding.
|
1 | P08003 (/ISO) |
There are 9 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 |
---|---|---|
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
3 | P08003 (/IDA) P13667 (/IDA) P13667 (/IDA) |
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 | P13667 (/IDA) P13667 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | P13667 (/TAS) P13667 (/TAS) |
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.
|
1 | P08003 (/ISO) |
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 | P08003 (/IDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
1 | P38659 (/IDA) |
Smooth endoplasmic reticulum GO:0005790
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
|
1 | P08003 (/ISO) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
1 | P08003 (/ISO) |
Endoplasmic reticulum chaperone complex GO:0034663
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
|
1 | P08003 (/IDA) |