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 32: xyloglucan 6-xylosyltransferase 2

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
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).
6 O22775 (/IPI) O22775 (/IPI) Q9CA75 (/IPI) Q9LF80 (/IPI) Q9LZJ3 (/IPI) Q9LZJ3 (/IPI)
UDP-xylosyltransferase activity GO:0035252
Catalysis of the transfer of a xylosyl group from UDP-xylose to an acceptor molecule.
5 O22775 (/IDA) O22775 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA) Q9M9U0 (/IDA)
Xyloglucan 6-xylosyltransferase activity GO:0033843
Catalysis of the transfer of an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage.
4 O22775 (/IDA) O22775 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
2 O22775 (/IPI) O22775 (/IPI)
Xyloglucan 6-xylosyltransferase activity GO:0033843
Catalysis of the transfer of an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage.
1 Q9CA75 (/IMP)

There are 4 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
Root hair elongation GO:0048767
The process in which the root hair grows longer.
8 Q10MQ0 (/IMP) Q10MQ0 (/IMP) Q10MQ0 (/IMP) Q10MQ0 (/IMP) Q10MQ0 (/IMP) Q10MQ0 (/IMP) Q10MQ0 (/IMP) Q9CA75 (/IMP)
Xyloglucan metabolic process GO:0010411
The chemical reactions and pathways involving xyloglucan, the cross-linking glycan composed of (1->4)-beta-D-glucan backbone substituted at regular intervals with beta-D-xylosyl-(1->6) residues, which is present in the primary cell wall of most higher plants.
5 O22775 (/IDA) O22775 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA) Q9M9U0 (/IDA)
Polysaccharide biosynthetic process GO:0000271
The chemical reactions and pathways resulting in the formation of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
4 O22775 (/IDA) O22775 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA)
Xyloglucan metabolic process GO:0010411
The chemical reactions and pathways involving xyloglucan, the cross-linking glycan composed of (1->4)-beta-D-glucan backbone substituted at regular intervals with beta-D-xylosyl-(1->6) residues, which is present in the primary cell wall of most higher plants.
2 Q9CA75 (/IMP) Q9LF80 (/IMP)

There are 4 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
Endosome GO:0005768
A vacuole to which materials ingested by endocytosis are delivered.
6 O22775 (/IDA) O22775 (/IDA) Q9CA75 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA) Q9M9U0 (/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.
6 O22775 (/IDA) O22775 (/IDA) Q9CA75 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA) Q9M9U0 (/IDA)
Trans-Golgi network GO:0005802
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
6 O22775 (/IDA) O22775 (/IDA) Q9CA75 (/IDA) Q9LZJ3 (/IDA) Q9LZJ3 (/IDA) Q9M9U0 (/IDA)
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
1 Q9CA75 (/IDA)