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:
"Tandem AAA-ATPase domain
".
FunFam 99: Rad5p
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 |
|---|---|---|
|
Four-way junction DNA binding GO:0000400
Interacting selectively and non-covalently with DNA containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
Y-form DNA binding GO:0000403
Interacting selectively and non-covalently with segment of DNA shaped like a Y. This shape occurs when DNA contains a region of paired double-stranded DNA on one end and a region of unpaired DNA strands on the opposite end.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
DNA-dependent ATPase activity GO:0008094
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of single- or double-stranded DNA, and it drives another reaction.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
Four-way junction helicase activity GO:0009378
Catalysis of the reaction: ATP + H2O = ADP + phosphate, where this reaction drives the unwinding of the DNA helix of DNA containing four-way junctions, including Holliday junctions.
|
2 | P32849 (/IDA) P32849 (/IDA) |
There are 10 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 | P32849 (/IDA) P32849 (/IDA) |
|
Postreplication repair GO:0006301
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
Double-strand break repair GO:0006302
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
|
2 | P32849 (/IGI) P32849 (/IGI) |
|
Double-strand break repair GO:0006302
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
|
2 | P32849 (/IMP) P32849 (/IMP) |
|
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 | P32849 (/IDA) P32849 (/IDA) |
|
Error-free postreplication DNA repair GO:0042275
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate.
|
2 | P32849 (/IMP) P32849 (/IMP) |
|
Error-prone translesion synthesis GO:0042276
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
Error-prone translesion synthesis GO:0042276
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
|
2 | P32849 (/IMP) P32849 (/IMP) |
|
Error-free translesion synthesis GO:0070987
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
Error-free translesion synthesis GO:0070987
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
|
2 | P32849 (/IMP) P32849 (/IMP) |
There are 4 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 |
|---|---|---|
|
Chromosome, telomeric region GO:0000781
The terminal region of a linear chromosome that includes the telomeric DNA repeats and associated proteins.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
Nuclear chromatin GO:0000790
The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome in the nucleus.
|
2 | P32849 (/IDA) P32849 (/IDA) |
|
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.
|
2 | P32849 (/HDA) P32849 (/HDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P32849 (/HDA) P32849 (/HDA) |
