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:
"DNA helicase RuvA subunit, C-terminal domain
".
FunFam 95: Uncharacterized protein, isoform F
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 |
|---|---|---|
|
Ubiquitin-protein transferase activity GO:0004842
Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
|
4 | M9PB55 (/ISS) M9PCD7 (/ISS) M9PCS0 (/ISS) Q8IPJ3 (/ISS) |
|
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
4 | M9PB55 (/ISM) M9PCD7 (/ISM) M9PCS0 (/ISM) Q8IPJ3 (/ISM) |
|
K48-linked polyubiquitin modification-dependent protein binding GO:0036435
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 48 in the target protein.
|
4 | M9PB55 (/IDA) M9PCD7 (/IDA) M9PCS0 (/IDA) Q8IPJ3 (/IDA) |
|
Ubiquitin protein ligase activity GO:0061630
Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
|
4 | M9PB55 (/IDA) M9PCD7 (/IDA) M9PCS0 (/IDA) Q8IPJ3 (/IDA) |
|
K63-linked polyubiquitin modification-dependent protein binding GO:0070530
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 63 in the target protein.
|
4 | M9PB55 (/IDA) M9PCD7 (/IDA) M9PCS0 (/IDA) Q8IPJ3 (/IDA) |
|
Linear polyubiquitin binding GO:1990450
Interacting selectively and non-covalently with a linear polymer of ubiquitin. Linear ubiquitin polymers are formed by linking the amino-terminal methionine (M1) of one ubiquitin molecule to the carboxy-terminal glycine (G76) of the next.
|
4 | M9PB55 (/IDA) M9PCD7 (/IDA) M9PCS0 (/IDA) Q8IPJ3 (/IDA) |
There are 3 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 polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
4 | M9PB55 (/ISS) M9PCD7 (/ISS) M9PCS0 (/ISS) Q8IPJ3 (/ISS) |
|
Heat acclimation GO:0010286
Any process that increases heat tolerance of an organism in response to high temperatures.
|
4 | M9PB55 (/IMP) M9PCD7 (/IMP) M9PCS0 (/IMP) Q8IPJ3 (/IMP) |
|
Protein linear polyubiquitination GO:0097039
A protein ubiquitination process in which a linear polymer of ubiquitin, formed by the amino-terminal methionine (M1) of one ubiquitin molecule and by the carboxy-terminal glycine (G76) of the next, is added to a protein.
|
4 | M9PB55 (/IDA) M9PCD7 (/IDA) M9PCS0 (/IDA) Q8IPJ3 (/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.
