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 11: peptide-N(4)-(N-acetyl-beta- glucosaminyl)asparagi...

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 10 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
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity GO:0000224
Catalysis of the reaction: 4-N-(N-acetyl-D-glucosaminyl)-protein + H2O = N-acetyl-beta-D-glucosaminylamine + peptide L-aspartate. This reaction is the hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the N-acetyl-D-glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and the peptide containing an aspartic residue.
11 O74739 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q55FC8 (/IDA) Q9FGY9 (/IDA) Q9FGY9 (/IDA)
(1 more)
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).
8 Q02890 (/IPI) Q02890 (/IPI) Q02890 (/IPI) Q02890 (/IPI) Q02890 (/IPI) Q02890 (/IPI) Q96IV0 (/IPI) Q9JI78 (/IPI)
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity GO:0000224
Catalysis of the reaction: 4-N-(N-acetyl-D-glucosaminyl)-protein + H2O = N-acetyl-beta-D-glucosaminylamine + peptide L-aspartate. This reaction is the hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the N-acetyl-D-glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and the peptide containing an aspartic residue.
3 Q96IV0 (/IGI) Q9FGY9 (/IGI) Q9FGY9 (/IGI)
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity GO:0000224
Catalysis of the reaction: 4-N-(N-acetyl-D-glucosaminyl)-protein + H2O = N-acetyl-beta-D-glucosaminylamine + peptide L-aspartate. This reaction is the hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the N-acetyl-D-glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and the peptide containing an aspartic residue.
1 Q9JI78 (/ISO)
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity GO:0000224
Catalysis of the reaction: 4-N-(N-acetyl-D-glucosaminyl)-protein + H2O = N-acetyl-beta-D-glucosaminylamine + peptide L-aspartate. This reaction is the hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the N-acetyl-D-glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and the peptide containing an aspartic residue.
1 Q9JI78 (/ISS)
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity GO:0000224
Catalysis of the reaction: 4-N-(N-acetyl-D-glucosaminyl)-protein + H2O = N-acetyl-beta-D-glucosaminylamine + peptide L-aspartate. This reaction is the hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the N-acetyl-D-glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and the peptide containing an aspartic residue.
1 Q96IV0 (/TAS)
Protein disulfide oxidoreductase activity GO:0015035
Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.
1 Q9TW67 (/IDA)
Metal ion binding GO:0046872
Interacting selectively and non-covalently with any metal ion.
1 O74739 (/IDA)
Protein-disulfide reductase activity GO:0047134
Catalysis of the reaction: protein-dithiol + NAD(P)+ = protein-disulfide + NAD(P)H + H+.
1 Q9TW67 (/IDA)
Misfolded protein binding GO:0051787
Interacting selectively and non-covalently with a misfolded protein.
1 O74739 (/IDA)

There are 22 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
Glycoprotein catabolic process GO:0006516
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
8 Q4R6F3 (/ISS) Q4R6F3 (/ISS) Q503I8 (/ISS) Q503I8 (/ISS) Q5WNE3 (/ISS) Q5XI55 (/ISS) Q5ZJM3 (/ISS) Q9TW67 (/ISS)
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
8 Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q96IV0 (/IDA) Q9TW67 (/IDA)
Protein quality control for misfolded or incompletely synthesized proteins GO:0006515
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
6 Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP)
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
6 Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP)
Ubiquitin-dependent glycoprotein ERAD pathway GO:0097466
An ERAD pathway whereby endoplasmic reticulum (ER)-resident glycoproteins are targeted for degradation. Includes differential processing of the glycoprotein sugar chains, retrotranslocation to the cytosol and degradation by the ubiquitin-proteasome pathway. A glycoprotein is a compound in which a carbohydrate component is covalently bound to a protein component.
6 Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP) Q02890 (/IMP)
Glycoprotein catabolic process GO:0006516
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
2 Q96IV0 (/IDA) Q9JI78 (/IDA)
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
2 Q96IV0 (/IGI) Q9TW67 (/IGI)
Response to salicylic acid GO:0009751
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a salicylic acid stimulus.
2 Q9FGY9 (/IEP) Q9FGY9 (/IEP)
Response to microbial phytotoxin GO:0010188
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a microbial phytotoxin stimulus. A microbial phytotoxin is a chemical substance produced by microbes which is toxic to plants.
2 Q9FGY9 (/IEP) Q9FGY9 (/IEP)
Response to ozone GO:0010193
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ozone stimulus.
2 Q9FGY9 (/IEP) Q9FGY9 (/IEP)
Mannoprotein catabolic process GO:0006058
The chemical reactions and pathways resulting in the breakdown of mannoproteins, any protein that contains covalently bound mannose residues.
1 O74739 (/IMP)
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.
1 Q96IV0 (/TAS)
Glycoprotein catabolic process GO:0006516
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
1 Q9JI78 (/ISO)
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
1 Q9JI78 (/ISO)
Protein deglycosylation GO:0006517
The removal of sugar residues from a glycosylated protein.
1 Q55FC8 (/TAS)
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
1 Q9TW67 (/IGI)
Aggregation involved in sorocarp development GO:0031152
The process whose specific outcome is the progression of the aggregate over time, from its formation to the point when a slug is formed. Aggregate development begins in response to starvation and continues by the chemoattractant-mediated movement of cells toward each other. The aggregate is a multicellular structure that gives rise to the slug.
1 Q55FC8 (/IMP)
Protein deglycosylation involved in glycoprotein catabolic process GO:0035977
The removal of sugar residues from a glycosylated protein that contributes to the breakdown of a glycoprotein.
1 O74739 (/IDA)
Sorocarp spore cell differentiation GO:0044671
The process in which a relatively unspecialized cell acquires specialized features of a sorocarp spore cell, a cell of the sorocarp sorus. A sorocarp is the fruiting body characteristic of certain cellular slime moulds (e.g., Dictyosteliida) and consists of both stalk and a sorus (spore mass).
1 Q55FC8 (/IMP)
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
1 Q9TW67 (/IGI)
Negative regulation of collateral sprouting GO:0048671
Any process that stops, prevents, or reduces the frequency, rate or extent of collateral sprouting.
1 Q9TW67 (/IMP)
ER-associated misfolded protein catabolic process GO:0071712
The chemical reactions and pathways resulting in the breakdown of misfolded proteins transported from the endoplasmic reticulum and targeted to cytoplasmic proteasomes for degradation.
1 O74739 (/IDA)

There are 12 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
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
9 Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q55FC8 (/IDA) Q9FGY9 (/IDA) Q9FGY9 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
8 Q4R6F3 (/ISS) Q4R6F3 (/ISS) Q503I8 (/ISS) Q503I8 (/ISS) Q5WNE3 (/ISS) Q5XI55 (/ISS) Q5ZJM3 (/ISS) Q9TW67 (/ISS)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
7 Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q02890 (/IDA) Q55FC8 (/IDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
6 Q02890 (/HDA) Q02890 (/HDA) Q02890 (/HDA) Q02890 (/HDA) Q02890 (/HDA) Q02890 (/HDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
3 Q96IV0 (/IDA) Q9JI78 (/IDA) Q9TW67 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 O74739 (/HDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 Q9JI78 (/ISS)
Nuclear envelope GO:0005635
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
1 O74739 (/HDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 Q9JI78 (/ISO)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 O74739 (/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.
1 Q96IV0 (/TAS)
Collagen-containing extracellular matrix GO:0062023
An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells.
1 Q9JI78 (/HDA)