|
Automatic Ontology |
| ASPECT |
|
| function |
| 3684 Interacting selectively with damaged DNA. | IPR015360 XPC-binding domain | | | 4867 Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide linkages in oligopeptides or polypeptides; a serine residue (and a histidine residue) are at the active center of the enzyme. | IPR000215 Protease inhibitor I4, serpin | | | 5524 Interacting selectively with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | IPR003594 ATP-binding region, ATPase-like | | | 8270 Interacting selectively with zinc (Zn) ions. | IPR006025 Peptidase M, neutral zinc metallopeptidases, zinc-binding site | |
|
| process |
| 43161 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 ubiquitin, and mediated by the proteasome. | IPR015360 XPC-binding domain | | | 6289 In nucleotide excision repair a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). | IPR015360 XPC-binding domain | | | 6508 The hydrolysis of a peptide bond or bonds within a protein. | IPR006025 Peptidase M, neutral zinc metallopeptidases, zinc-binding site | |
|
| kog |
KOG0019 Molecular chaperone (HSP90 family)
Posttranslational modification, protein turnover, chaperones | | |
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