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:
"Nucleic acid-binding proteins
".
FunFam 331: Nucleoporin NUP116/NSP116
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 |
---|---|---|
Structural constituent of nuclear pore GO:0017056
The action of a molecule that contributes to the structural integrity of the nuclear pore complex, a protein-lined channel in the nuclear envelope that allows the transfer of macromolecules.
|
2 | Q8IKA0 (/ISS) Q8IKA0 (/ISS) |
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 import into nucleus GO:0006606
The directed movement of a protein from the cytoplasm to the nucleus.
|
2 | Q8IKA0 (/ISS) Q8IKA0 (/ISS) |
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 |
---|---|---|
Nuclear pore central transport channel GO:0044613
The central substructure of the nuclear pore complex (NPC), through which nucleocytoplasmic transport of RNAs, proteins and small molecules occurs. The central transport channel is filled with FG-nucleoporins, which form a selective barrier and provide a series of binding sites for transporter proteins. Characterized S. cerevisiae FG-nucleoporins include Nup159p, Nup145Np, Nup116p, Nup100p, Nsp1p, Nup57p, Nup49p, Nup42p, Nup53p, Nup59p/Asm4p, Nup60p and Nup1. Characterized vertebrate FG-nucleoporins include Nup214, Nup98, Nup62, Nup54, Nup58/45, NLP1, and Nup153.
|
2 | Q8IKA0 (/ISS) Q8IKA0 (/ISS) |