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:
"Phox-like domain
".
FunFam 73: Vacuolar morphogenesis protein
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 |
---|---|---|
SNAP receptor activity GO:0005484
Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
|
2 | P32912 (/IDA) P32912 (/IDA) |
SNAP receptor activity GO:0005484
Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
|
2 | P32912 (/ISS) P32912 (/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).
|
2 | P32912 (/IPI) P32912 (/IPI) |
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
|
2 | P32912 (/IDA) P32912 (/IDA) |
Phosphatidylinositol-3-phosphate binding GO:0032266
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
|
2 | P32912 (/IMP) P32912 (/IMP) |
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 |
---|---|---|
Vesicle fusion GO:0006906
Fusion of the membrane of a transport vesicle with its target membrane.
|
2 | P32912 (/IDA) P32912 (/IDA) |
Macroautophagy GO:0016236
The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded.
|
2 | P32912 (/IMP) P32912 (/IMP) |
Protein localization by the Cvt pathway GO:0032258
A cytoplasm to vacuole targeting pathway that uses machinery common with autophagy. The Cvt vesicle is formed when the receptor protein, Atg19, binds to the complexes of the target protein (aminopeptidase or alpha-mannosidase homododecamers), forming the Cvt complex. Atg11 binds to Atg9 and transports the Cvt complex to the pre-autophagosome (PAS). The phagophore membrane expands around the Cvt complex (excluding bulk cytoplasm) forming the Cvt vesicle. This pathway is mostly observed in yeast.
|
2 | P32912 (/IMP) P32912 (/IMP) |
Piecemeal microautophagy of the nucleus GO:0034727
Degradation of a cell nucleus by lysosomal microautophagy.
|
2 | P32912 (/IMP) P32912 (/IMP) |
Vacuole fusion, non-autophagic GO:0042144
The fusion of two vacuole membranes to form a single vacuole.
|
2 | P32912 (/IDA) P32912 (/IDA) |
Vacuole fusion, non-autophagic GO:0042144
The fusion of two vacuole membranes to form a single vacuole.
|
2 | P32912 (/IMP) P32912 (/IMP) |
Autophagosome-lysosome fusion GO:0061909
The process in which autophagosomes, double-membraned vesicles containing cytoplasmic material, fuse with a vacuole (yeast) or lysosome (e.g. mammals and insects). In the case of yeast, inner membrane-bounded structures (autophagic bodies) appear in the vacuole. Fusion provides an acidic environment and digestive function to the interior of the autophagosome.
|
2 | P32912 (/IMP) P32912 (/IMP) |
There are 6 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.
|
2 | P32912 (/HDA) P32912 (/HDA) |
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.
|
2 | P32912 (/IDA) P32912 (/IDA) |
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.
|
2 | P32912 (/IMP) P32912 (/IMP) |
Phagophore assembly site GO:0000407
Punctate structures proximal to the endoplasmic reticulum which are the sites where the Atg machinery assembles upon autophagy induction.
|
2 | P32912 (/IDA) P32912 (/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.
|
2 | P32912 (/IMP) P32912 (/IMP) |
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.
|
2 | P32912 (/IPI) P32912 (/IPI) |