CATH Superfamily 3.40.1380.40
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: waiting to be named.
FunFam 1: Undecaprenyl-diphosphooligosaccharide--protein gly...
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 3 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 |
|---|---|---|
|
Transferase activity, transferring glycosyl groups GO:0016757
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
|
4 | B9KDD4 (/IDA) Q0P9C8 (/IDA) Q0P9C8 (/IDA) Q0P9C8 (/IDA) |
|
Transferase activity, transferring glycosyl groups GO:0016757
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
|
2 | Q5HTX9 (/IMP) Q5HTX9 (/IMP) |
|
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
1 | B9KDD4 (/IDA) |
There are 2 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 via asparagine GO:0018279
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
|
4 | B9KDD4 (/IDA) Q0P9C8 (/IDA) Q0P9C8 (/IDA) Q0P9C8 (/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 | Q5HTX9 (/IMP) Q5HTX9 (/IMP) |
There are 0 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.
