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:
"XPA C-terminal domain
".
FunFam 3: Dna repair rad14 protein
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 |
|---|---|---|
|
Damaged DNA binding GO:0003684
Interacting selectively and non-covalently with damaged DNA.
|
5 | P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) |
|
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).
|
5 | P28519 (/IPI) P28519 (/IPI) P28519 (/IPI) P28519 (/IPI) P28519 (/IPI) |
|
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
5 | P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) |
|
Damaged DNA binding GO:0003684
Interacting selectively and non-covalently with damaged DNA.
|
1 | O59753 (/ISO) |
There are 5 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 |
|---|---|---|
|
Nucleotide-excision repair, DNA damage recognition GO:0000715
The identification of lesions in DNA, such as pyrimidine-dimers, intrastrand cross-links, and bulky adducts. The wide range of substrate specificity suggests the repair complex recognizes distortions in the DNA helix.
|
5 | P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) |
|
Nucleotide-excision repair, DNA damage recognition GO:0000715
The identification of lesions in DNA, such as pyrimidine-dimers, intrastrand cross-links, and bulky adducts. The wide range of substrate specificity suggests the repair complex recognizes distortions in the DNA helix.
|
1 | O59753 (/ISO) |
|
Nucleotide-excision repair GO:0006289
A DNA repair process in which 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).
|
1 | O59753 (/IGI) |
|
UV-damage excision repair GO:0070914
A DNA repair process that is initiated by an endonuclease that introduces a single-strand incision immediately 5' of a UV-induced damage site. UV-damage excision repair acts on both cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone 6-4 photoproducts (6-4PPs).
|
1 | O59753 (/IMP) |
|
Nucleotide-excision repair involved in interstrand cross-link repair GO:1901255
Any nucleotide-excision repair that is involved in interstrand cross-link repair.
|
1 | O59753 (/IMP) |
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 |
|---|---|---|
|
Nucleotide-excision repair factor 1 complex GO:0000110
One of several protein complexes involved in nucleotide-excision repair; possesses DNA damage recognition and endodeoxynuclease activities. In S. cerevisiae, it is composed of Rad1p, Rad10p, and Rad14p; in human the subunits are ERCC4/XPF, ERCC1 and XPA, respectively.
|
5 | P28519 (/IPI) P28519 (/IPI) P28519 (/IPI) P28519 (/IPI) P28519 (/IPI) |
|
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.
|
5 | P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) P28519 (/IDA) |
|
Nucleotide-excision repair complex GO:0000109
Any complex formed of proteins that act in nucleotide-excision repair.
|
1 | O59753 (/ISO) |
