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:

"
Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
".

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 21: Polypeptide N-acetylgalactosaminyltransferase

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 8 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
Polypeptide N-acetylgalactosaminyltransferase activity GO:0004653
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis.
8 P34678 (/IDA) Q6WV20 (/IDA) Q8I136 (/IDA) Q8MVS5 (/IDA) Q8MVS5 (/IDA) Q8N4A0 (/IDA) Q95ZJ1 (/IDA) Q9Y117 (/IDA)
Polypeptide N-acetylgalactosaminyltransferase activity GO:0004653
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis.
2 O08832 (/ISS) Q8MRC9 (/ISS)
Polypeptide N-acetylgalactosaminyltransferase activity GO:0004653
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis.
1 O08832 (/ISO)
Acetylgalactosaminyltransferase activity GO:0008376
Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an oligosaccharide.
1 Q9Y117 (/IDA)
Transferase activity, transferring glycosyl groups GO:0016757
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
1 Q9Y117 (/IDA)
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
1 Q8N4A0 (/IDA)
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
1 O08832 (/ISO)
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
1 O08832 (/ISS)

There are 17 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
Oligosaccharide biosynthetic process GO:0009312
The chemical reactions and pathways resulting in the formation of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
4 Q6WV20 (/IDA) Q8MVS5 (/IDA) Q8MVS5 (/IDA) Q9Y117 (/IDA)
Protein O-linked glycosylation via threonine GO:0018243
The glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine.
4 P34678 (/IDA) Q8I136 (/IDA) Q8N4A0 (/IDA) Q95ZJ1 (/IDA)
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
2 Q8MRC9 (/IDA) Q9Y117 (/IDA)
Open tracheal system development GO:0007424
The process whose specific outcome is the progression of an open tracheal system over time, from its formation to the mature structure. An open tracheal system is a respiratory system, a branched network of epithelial tubes that supplies oxygen to target tissues via spiracles. An example of this is found in Drosophila melanogaster.
2 Q8MVS5 (/IMP) Q8MVS5 (/IMP)
O-glycan processing GO:0016266
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form a core O-glycan structure.
2 Q8IXK2 (/TAS) Q8N4A0 (/TAS)
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
1 Q9Y117 (/IMP)
Protein O-linked glycosylation GO:0006493
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
1 Q8MRC9 (/ISS)
O-glycan processing GO:0016266
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form a core O-glycan structure.
1 Q9Y117 (/IDA)
Protein O-linked glycosylation via serine GO:0018242
The glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine.
1 Q8N4A0 (/IDA)
Protein O-linked glycosylation via serine GO:0018242
The glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine.
1 O08832 (/ISO)
Protein O-linked glycosylation via serine GO:0018242
The glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine.
1 O08832 (/ISS)
Protein O-linked glycosylation via threonine GO:0018243
The glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine.
1 O08832 (/ISO)
Protein O-linked glycosylation via threonine GO:0018243
The glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine.
1 O08832 (/ISS)
Cell-substrate adhesion GO:0031589
The attachment of a cell to the underlying substrate via adhesion molecules.
1 Q9Y117 (/IMP)
Multicellular organism reproduction GO:0032504
The biological process in which new individuals are produced by one or two multicellular organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
1 Q8MRC9 (/IEP)
Regulation of cell adhesion mediated by integrin GO:0033628
Any process that modulates the frequency, rate, or extent of cell adhesion mediated by integrin.
1 Q9Y117 (/IMP)
Extracellular matrix constituent secretion GO:0070278
The controlled release of molecules that form the extracellular matrix, including carbohydrates and glycoproteins by a cell.
1 Q9Y117 (/IMP)

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
Golgi stack GO:0005795
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
4 Q6WV20 (/NAS) Q8MVS5 (/NAS) Q8MVS5 (/NAS) Q9Y117 (/NAS)
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
2 Q8IXK2 (/TAS) Q8N4A0 (/TAS)
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.
2 Q8MRC9 (/IDA) Q9Y117 (/IDA)
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 Q8MRC9 (/ISS)
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 Q8MRC9 (/HDA)
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.
1 Q8MRC9 (/ISM)
Golgi cisterna GO:0031985
Any of the thin, flattened membrane-bounded compartments that form the central portion of the Golgi complex.
1 Q8MRC9 (/IDA)
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
1 Q8N4A0 (/IDA)
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
1 O08832 (/ISO)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
1 Q8N4A0 (/HDA)
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