Domain

NAD-dependent DNA ligase, adenylation (IPR013839)

Short name: DNAligase_adenylation

Domain relationships

None.

Description

DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalyzing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination. There are two forms of DNA ligase: one requires ATP (EC:6.5.1.1), the other NAD (EC:6.5.1.2).

This entry represents the N-terminal adenylation domain of NAD-dependent DNA ligases. These are proteins of about 75 to 85 Kd whose sequence is well conserved [PMID: 1526462, PMID: 8390989]. They also show similarity to yicF, an Escherichia coli hypothetical protein of 63 Kd. Despite a complete lack of detectable sequence similarity, the fold of the central core of this adenyaltion domain shares homology with the equivalent region of ATP-dependent DNA ligases [PMID: 10368271, PMID: 10698952].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003911 DNA ligase (NAD+) activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
CDD
Pfam