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PROSITE documentation PDOC00295 [for PROSITE entry PS50160]

ATP-dependent DNA ligase signatures and profile


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, the other NAD (EC

Eukaryotic, archaebacterial, virus and phage DNA ligases are ATP-dependent. During the first step of the joining reaction, the ligase interacts with ATP to form a covalent enzyme-adenylate intermediate. A conserved lysine residue is the site of adenylation [1,2].

Apart from the active site region, the only conserved region common to all ATP-dependent DNA ligases is found [3] in the C-terminal section and contains a conserved glutamate as well as four positions with conserved basic residues.

We developed signature patterns for both conserved regions.

Last update:

April 2006 / Patterns revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

DNA_LIGASE_A3, PS50160; ATP-dependent DNA ligase family profile  (MATRIX)

DNA_LIGASE_A1, PS00697; ATP-dependent DNA ligase AMP-binding site  (PATTERN)

DNA_LIGASE_A2, PS00333; ATP-dependent DNA ligase signature 2  (PATTERN)


1AuthorsTomkinson A.E. Totty N.F. Ginsburg M. Lindahl T.
TitleLocation of the active site for enzyme-adenylate formation in DNA ligases.
SourceProc. Natl. Acad. Sci. U.S.A. 88:400-404(1991).
PubMed ID1988940

2AuthorsLindahl T. Barnes D.E.
TitleMammalian DNA ligases.
SourceAnnu. Rev. Biochem. 61:251-281(1992).
PubMed ID1497311

3AuthorsKletzin A.
TitleMolecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.
SourceNucleic Acids Res. 20:5389-5396(1992).
PubMed ID1437556

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