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:
"Nucleoside Triphosphate Pyrophosphohydrolase
".
FunFam 35: Uridine diphosphate glucose pyrophosphatase
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 6 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).
|
1 | O95848 (/IPI) |
|
UDP-sugar diphosphatase activity GO:0008768
Catalysis of the reaction: UDP-sugar + H2O = UMP + sugar 1-phosphate.
|
1 | Q9D142 (/IDA) |
|
UDP-sugar diphosphatase activity GO:0008768
Catalysis of the reaction: UDP-sugar + H2O = UMP + sugar 1-phosphate.
|
1 | O95848 (/TAS) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | O95848 (/IPI) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | Q9D142 (/ISO) |
|
ADP-ribose diphosphatase activity GO:0047631
Catalysis of the reaction: ADP-ribose + H2O = AMP + D-ribose 5-phosphate.
|
1 | Q9D142 (/IDA) |
There are 1 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.
|
1 | O95848 (/TAS) |
There are 1 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.
|
1 | O95848 (/TAS) |
