Active Site

NAD-dependent DNA ligase, active site (IPR018239)

Short name: DNA_ligase_AS

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 family is predominantly composed of NAD-dependent bacterial DNA ligases. They 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.

This entry contains two signature patterns for this family of proteins; these signatures are based on conserved regions in the N-terminal half. The first of which (DNA_LIGASE_N1) contains the KXDG motif required for adenylation of eukaryotic DNA ligases. The lysine residue being required for the adenylation step of the ligase and the aspartate being required for the de-adenylation step [PMID: 8760897, PMID: 1988940].

GO terms

Biological Process

GO:0006281 DNA repair
GO:0006260 DNA replication

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.
PROSITE patterns
PROSITE patterns