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:
"Cyclophilin-like
".
FunFam 19: Peptidyl-prolyl cis-trans isomerase
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 |
---|---|---|
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
13 |
P15425 (/TAS)
P15425 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
(3 more) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
11 |
P15425 (/ISS)
P15425 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
P35176 (/ISS)
(1 more) |
Cyclosporin A binding GO:0016018
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
|
11 |
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
(1 more) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
9 | O94273 (/IDA) P23285 (/IDA) P23285 (/IDA) P23285 (/IDA) P23285 (/IDA) P23285 (/IDA) P23285 (/IDA) P23285 (/IDA) P23285 (/IDA) |
Peptidyl-prolyl cis-trans isomerase activity GO:0003755
Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
|
4 | Q57U26 (/ISM) Q57U26 (/ISM) Q57U26 (/ISM) Q57U26 (/ISM) |
Cyclosporin A binding GO:0016018
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
|
2 | P15425 (/IMP) P15425 (/IMP) |
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 |
---|---|---|
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.
|
11 |
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
Q8IIK8 (/TAS)
(1 more) |
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.
|
4 | Q57U26 (/ISM) Q57U26 (/ISM) Q57U26 (/ISM) Q57U26 (/ISM) |
'de novo' protein folding GO:0006458
The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.
|
2 | P15425 (/TAS) P15425 (/TAS) |
N-glycan processing GO:0006491
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
|
2 | P15425 (/IMP) P15425 (/IMP) |
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
|
2 | P15425 (/IMP) P15425 (/IMP) |
Phototransduction GO:0007602
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
|
2 | P15425 (/IMP) P15425 (/IMP) |
Phototransduction GO:0007602
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
|
2 | P15425 (/IPI) P15425 (/IPI) |
Phototransduction GO:0007602
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
|
2 | P15425 (/TAS) P15425 (/TAS) |
Phototransduction, visible light GO:0007603
The sequence of reactions within a cell required to convert absorbed photons from visible light into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm.
|
2 | P15425 (/IMP) P15425 (/IMP) |
Rhodopsin biosynthetic process GO:0016063
The chemical reactions and pathways resulting in the formation of rhodopsin, a brilliant purplish-red, light-sensitive visual pigment found in the rod cells of the retinas.
|
2 | P15425 (/IMP) P15425 (/IMP) |
Rhodopsin biosynthetic process GO:0016063
The chemical reactions and pathways resulting in the formation of rhodopsin, a brilliant purplish-red, light-sensitive visual pigment found in the rod cells of the retinas.
|
2 | P15425 (/NAS) P15425 (/NAS) |
Rhodopsin biosynthetic process GO:0016063
The chemical reactions and pathways resulting in the formation of rhodopsin, a brilliant purplish-red, light-sensitive visual pigment found in the rod cells of the retinas.
|
2 | P15425 (/TAS) P15425 (/TAS) |
Intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress GO:0070059
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
2 | P15425 (/IMP) P15425 (/IMP) |
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 | O94273 (/IC) |
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 |
---|---|---|
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).
|
11 |
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
Q8IIK8 (/RCA)
(1 more) |
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).
|
10 | O94273 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
9 | P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) P35176 (/HDA) |
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).
|
9 | P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) P35176 (/IDA) |
Fungal-type vacuole GO:0000324
A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
|
8 | P23285 (/HDA) P23285 (/HDA) P23285 (/HDA) P23285 (/HDA) P23285 (/HDA) P23285 (/HDA) P23285 (/HDA) P23285 (/HDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | P15425 (/IDA) P15425 (/IDA) |
Integral component of membrane GO:0016021
The component of a 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.
|
2 | P15425 (/IDA) P15425 (/IDA) |
Cytoplasmic vesicle GO:0031410
A vesicle found in the cytoplasm of a cell.
|
2 | P15425 (/IDA) P15425 (/IDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | O94273 (/ISO) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
1 | O94273 (/HDA) |