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:

"
Histone, subunit A
".

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 121: DNA polymerase II third subunit

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 0 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.

There are 8 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
Replicative cell aging GO:0001302
The process associated with progression of the cell from its inception to the end of its lifespan that occurs as the cell continues cycles of growth and division.
9 P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP)
DNA-dependent DNA replication GO:0006261
A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
9 P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA)
DNA-dependent DNA replication GO:0006261
A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
9 P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP)
Leading strand elongation GO:0006272
The process in which an existing DNA strand is extended continuously in a 5' to 3' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Leading strand elongation proceeds in the same direction as the replication fork.
9 P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI)
Leading strand elongation GO:0006272
The process in which an existing DNA strand is extended continuously in a 5' to 3' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Leading strand elongation proceeds in the same direction as the replication fork.
9 P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/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.
9 P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA)
Heterochromatin organization involved in chromatin silencing GO:0070868
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic heterochromatin and contributes to chromatin silencing.
9 P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI) P27344 (/IGI)
Heterochromatin organization involved in chromatin silencing GO:0070868
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic heterochromatin and contributes to chromatin silencing.
9 P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP) P27344 (/IMP)

There are 1 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
Epsilon DNA polymerase complex GO:0008622
A heterotetrameric DNA polymerase complex that catalyzes processive DNA synthesis in the absence of PCNA, but is further stimulated in the presence of PCNA. The complex contains a large catalytic subunit and three small subunits, and is best characterized in Saccharomyces, in which the subunits are named Pol2p, Dpb2p, Dpb3p, and Dpb4p. Some evidence suggests that DNA polymerase epsilon is the leading strand polymerase; it is also involved in nucleotide-excision repair and mismatch repair.
9 P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA) P27344 (/IDA)