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:

"
5' to 3' exonuclease, C-terminal subdomain
".

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 5: UvrABC system protein C

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 1 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
Excinuclease ABC activity GO:0009381
Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind.
6 Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS)

There are 3 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
Response to radiation GO:0009314
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation.
110 P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP) P0A8G0 (/IMP)
(100 more)
DNA repair GO:0006281
The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
6 Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS)
SOS response GO:0009432
An error-prone process for repairing damaged microbial DNA.
2 Q9A4F3 (/EXP) Q9A4F3 (/EXP)

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
Excinuclease repair complex GO:0009380
Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
110 P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA) P0A8G0 (/IDA)
(100 more)
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
10 P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
10 P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA) P9WFC5 (/HDA)
Excinuclease repair complex GO:0009380
Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
6 Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS) Q9KSP2 (/ISS)
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