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:
"Zinc/RING finger domain, C3HC4 (zinc finger)
".
FunFam 648: RING finger domain protein, putative
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 2 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 |
|---|---|---|
|
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | Q1MTR5 (/ISM) |
|
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.
|
1 | Q1MTR5 (/ISM) |
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 modification by small protein conjugation or removal GO:0070647
A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein.
|
1 | Q1MTR5 (/IC) |
There are 3 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 |
|---|---|---|
|
Fungal-type vacuole GO:0000324
A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
|
1 | Q1MTR5 (/HDA) |
|
Cell division site GO:0032153
The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
|
1 | Q1MTR5 (/HDA) |
|
Cell tip GO:0051286
The region at the end of the longest axis of a cylindrical or elongated cell.
|
1 | Q1MTR5 (/HDA) |
