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:
"ABC transporter type 1, transmembrane domain
".
FunFam 311: ABC transporter ATP-binding protein
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 1 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 |
|---|---|---|
|
Lipopolysaccharide floppase activity GO:0015437
Enables the transfer of a lipopolysaccharide from the cytosolic to the exoplasmic leaftlet of a membrane, using energy from the hydrolysis of ATP.
|
3 | Q0P9C4 (/IDA) Q0P9C4 (/IDA) Q0P9C4 (/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 |
|---|---|---|
|
Oligosaccharide transport GO:0015772
The directed movement of oligosaccharides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Oligosaccharides are molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
|
3 | Q0P9C4 (/IDA) Q0P9C4 (/IDA) Q0P9C4 (/IDA) |
|
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.
|
3 | Q0P9C4 (/IDA) Q0P9C4 (/IDA) Q0P9C4 (/IDA) |
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.
