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:

"
Hect, E3 ligase catalytic domains
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 45: Ubiquitin ligase e3

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 4 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.
2 P33202 (/TAS) P33202 (/TAS)
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).
2 P33202 (/IPI) P33202 (/IPI)
Proteasome regulatory particle binding GO:1904855
Interacting selectively and non-covalently with a proteasome regulatory particle.
2 P33202 (/IPI) P33202 (/IPI)
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 Q10435 (/ISO)

There are 6 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.
2 P33202 (/TAS) P33202 (/TAS)
Protein monoubiquitination GO:0006513
Addition of a single ubiquitin group to a protein.
2 P33202 (/TAS) P33202 (/TAS)
Free ubiquitin chain polymerization GO:0010994
The process of creating free ubiquitin chains, compounds composed of a large number of ubiquitin monomers. These chains are not conjugated to a protein.
2 P33202 (/IMP) P33202 (/IMP)
Negative regulation of telomerase activity GO:0051974
Any process that stops or reduces the activity of the enzyme telomerase, which catalyzes of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
2 P33202 (/IMP) P33202 (/IMP)
Ubiquitin-dependent protein catabolic process GO:0006511
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
1 Q10435 (/ISS)
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 Q10435 (/IC)

There are 5 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
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
3 P33202 (/HDA) P33202 (/HDA) Q10435 (/HDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 P33202 (/HDA) P33202 (/HDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
2 P33202 (/HDA) P33202 (/HDA)
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 Q10435 (/HDA)
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
1 Q10435 (/NAS)
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