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:

"
Tetratricopeptide repeat 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 49: Alpha-soluble NSF attachment protein-like

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 5 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
Soluble NSF attachment protein activity GO:0005483
Interacting selectively and non-covalently with both N-ethylmaleimide-sensitive fusion protein (NSF) and a cis-SNARE complex (i.e. a SNARE complex in which all proteins are associated with the same membrane) and increasing the ATPase activity of NSF, thereby allowing ATP hydrolysis by NSF to disassemble the cis-SNARE complex.
7 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) Q54NP6 (/IDA)
ATPase activator activity GO:0001671
Binds to and increases the ATP hydrolysis activity of an ATPase.
6 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA)
Soluble NSF attachment protein activity GO:0005483
Interacting selectively and non-covalently with both N-ethylmaleimide-sensitive fusion protein (NSF) and a cis-SNARE complex (i.e. a SNARE complex in which all proteins are associated with the same membrane) and increasing the ATPase activity of NSF, thereby allowing ATP hydrolysis by NSF to disassemble the cis-SNARE complex.
6 P32602 (/IPI) P32602 (/IPI) P32602 (/IPI) P32602 (/IPI) P32602 (/IPI) P32602 (/IPI)
Soluble NSF attachment protein activity GO:0005483
Interacting selectively and non-covalently with both N-ethylmaleimide-sensitive fusion protein (NSF) and a cis-SNARE complex (i.e. a SNARE complex in which all proteins are associated with the same membrane) and increasing the ATPase activity of NSF, thereby allowing ATP hydrolysis by NSF to disassemble the cis-SNARE complex.
1 Q9P4X4 (/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 Q54NP6 (/IPI)

There are 7 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
Autophagy GO:0006914
The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.
6 P32602 (/IMP) P32602 (/IMP) P32602 (/IMP) P32602 (/IMP) P32602 (/IMP) P32602 (/IMP)
SNARE complex disassembly GO:0035494
The disaggregation of the SNARE protein complex into its constituent components. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
6 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA)
Vacuole fusion, non-autophagic GO:0042144
The fusion of two vacuole membranes to form a single vacuole.
6 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA)
Vesicle fusion with Golgi apparatus GO:0048280
The joining of the lipid bilayer membrane around a vesicle to the lipid bilayer membrane around the Golgi.
6 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA)
Intracellular protein transport GO:0006886
The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
1 Q9P4X4 (/IC)
Endoplasmic reticulum to Golgi vesicle-mediated transport GO:0006888
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
1 Q9P4X4 (/ISO)
Vacuole fusion, non-autophagic GO:0042144
The fusion of two vacuole membranes to form a single vacuole.
1 Q9P4X4 (/ISO)

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
Fungal-type vacuole membrane GO:0000329
The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
6 P32602 (/HDA) P32602 (/HDA) P32602 (/HDA) P32602 (/HDA) P32602 (/HDA) P32602 (/HDA)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
6 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA)
Extrinsic component of membrane GO:0019898
The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
6 P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA) P32602 (/IDA)
SNARE complex GO:0031201
A protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25.
6 P32602 (/IPI) P32602 (/IPI) P32602 (/IPI) P32602 (/IPI) P32602 (/IPI) P32602 (/IPI)
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.
3 Q9SPE6 (/IDA) Q9SPE6 (/IDA) Q9SPE6 (/IDA)
Vacuolar membrane GO:0005774
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
3 Q9SPE6 (/IDA) Q9SPE6 (/IDA) Q9SPE6 (/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.
3 Q9SPE6 (/IDA) Q9SPE6 (/IDA) Q9SPE6 (/IDA)
Plasmodesma GO:0009506
A fine cytoplasmic channel, found in all higher plants, that connects the cytoplasm of one cell to that of an adjacent cell.
3 Q9SPE6 (/IDA) Q9SPE6 (/IDA) Q9SPE6 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
3 Q9SPE6 (/IDA) Q9SPE6 (/IDA) Q9SPE6 (/IDA)
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
1 Q54NP6 (/HDA)
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