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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00809
NAD-dependent DNA ligase signatures


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00809

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).

Bacterial DNA ligases are NAD-dependent. They are proteins of about 75 to 85 Kd whose sequence is well conserved [1]. They also show similarity to yicF, an Escherichia coli hypothetical protein of 63 Kd. We developed two signature patterns for this family of proteins; these signatures are based on conserved regions in the N-terminal half.

Last update:

December 2004 / Patterns and text revised.

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Technical section

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

DNA_LIGASE_N1, PS01055; NAD-dependent DNA ligase signature 1  (PATTERN)

DNA_LIGASE_N2, PS01056; NAD-dependent DNA ligase signature 2  (PATTERN)


References

1AuthorsShark K.B. Conway T.
TitleCloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis.
SourceFEMS Microbiol. Lett. 75:19-26(1992).
PubMed ID1526462

2AuthorsGentry D. Bengra C. Ikehara K. Cashel M.
TitleGuanylate kinase of Escherichia coli K-12.
SourceJ. Biol. Chem. 268:14316-14321(1993).
PubMed ID8390989



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