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: waiting to be named.

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 27: Probable mannosyl-oligosaccharide glucosidase

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 4 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
Mannosyl-oligosaccharide glucosidase activity GO:0004573
Catalysis of the exohydrolysis of the non-reducing terminal glucose residue in the mannosyl-oligosaccharide Glc(3)Man(9)GlcNAc(2).
4 A0A1D8PMH9 (/IDA) A0A1D8PMH9 (/IDA) P53008 (/IDA) P53008 (/IDA)
Mannosyl-oligosaccharide glucosidase activity GO:0004573
Catalysis of the exohydrolysis of the non-reducing terminal glucose residue in the mannosyl-oligosaccharide Glc(3)Man(9)GlcNAc(2).
2 P53008 (/IMP) P53008 (/IMP)
Mannosyl-oligosaccharide glucosidase activity GO:0004573
Catalysis of the exohydrolysis of the non-reducing terminal glucose residue in the mannosyl-oligosaccharide Glc(3)Man(9)GlcNAc(2).
2 A0A1D8PMH9 (/ISA) A0A1D8PMH9 (/ISA)
Mannosyl-oligosaccharide glucosidase activity GO:0004573
Catalysis of the exohydrolysis of the non-reducing terminal glucose residue in the mannosyl-oligosaccharide Glc(3)Man(9)GlcNAc(2).
1 O14255 (/ISO)

There are 12 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 N-linked glycosylation GO:0006487
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
2 A0A1D8PMH9 (/IDA) A0A1D8PMH9 (/IDA)
Protein N-linked glycosylation GO:0006487
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
2 P53008 (/IMP) P53008 (/IMP)
Fungal-type cell wall biogenesis GO:0009272
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin.
2 P53008 (/IMP) P53008 (/IMP)
Filamentous growth GO:0030447
The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.
2 A0A1D8PMH9 (/IMP) A0A1D8PMH9 (/IMP)
Filamentous growth of a population of unicellular organisms GO:0044182
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape.
2 A0A1D8PMH9 (/IMP) A0A1D8PMH9 (/IMP)
Fungal-type cell wall polysaccharide biosynthetic process GO:0051278
The chemical reactions and pathways resulting in the formation of the polysaccharides which make up the fungal-type cell wall.
2 A0A1D8PMH9 (/IMP) A0A1D8PMH9 (/IMP)
Induction by symbiont of host immune response GO:0052559
Any process in which an organism activates the immune response of the host organism; the immune response is any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat. The host is defined as the larger of the organisms involved in a symbiotic interaction.
2 A0A1D8PMH9 (/IMP) A0A1D8PMH9 (/IMP)
Fungal-type cell wall beta-glucan biosynthetic process GO:0070880
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of fungal cells.
2 P53008 (/IGI) P53008 (/IGI)
Protein N-linked glycosylation GO:0006487
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
1 O14255 (/ISO)
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.
1 Q4WDB9 (/IMP)
Fungal-type cell wall biogenesis GO:0009272
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin.
1 O14255 (/ISO)
Post-translational protein modification GO:0043687
The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
1 Q4WDB9 (/IMP)

There are 5 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 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.
2 P53008 (/HDA) P53008 (/HDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
2 P53008 (/IDA) P53008 (/IDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
2 A0A1D8PMH9 (/ISA) A0A1D8PMH9 (/ISA)
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 O14255 (/HDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
1 O14255 (/ISO)
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