Protein Family Models

This region is found in many but not all ATP-dependent DNA ligase enzymes (EC:6.5.1.1). It is thought to be involved in DNA binding and in catalysis. In human DNA ligase I (Swiss:P18858), and in Saccharomyces cerevisiae (Swiss:P04819), this region was necessary for catalysis, and separated from the amino terminus by targeting elements. In vaccinia virus (Swiss:P16272) this region was not essential for catalysis, but deletion decreases the affinity for nicked DNA and decreased the rate of strand joining at a step subsequent to enzyme-adenylate formation [1]. [1]. 9016621. Domain structure of vaccinia DNA ligase.. Sekiguchi J, Shuman S;. Nucleic Acids Res 1997;25:727-734. (from Pfam)

Date:

2024-08-14

This region is found in many but not all ATP-dependent DNA ligase enzymes (EC:6.5.1.1). It is thought to constitute part of the catalytic core of ATP dependent DNA ligase [1]. [1]. 9016621. Domain structure of vaccinia DNA ligase.. Sekiguchi J, Shuman S;. Nucleic Acids Res 1997;25:727-734. (from Pfam)

Date:

2024-08-14

This domain belongs to a more diverse superfamily, including Pfam:PF01331 and Pfam:PF01653 [3]. [1]. 8653795. Crystal structure of an ATP-dependent DNA ligase from. bacteriophage T7.. Subramanya HS, Doherty AJ, Ashford SR, Wigley DB;. Cell 1996;85:607-615.. [2]. 9363683. Mammalian DNA ligases.. Tomkinson AE, Levin DS;. Bioessays 1997;19:893-901.. [3]. 10222208. Gleaning non-trivial structural, functional and evolutionary. information about proteins by iterative database searches.. Aravind L, Koonin EV;. J Mol Biol 1999;287:1023-1040. (from Pfam)

Date:

2024-08-14

ATP-dependent DNA ligase catalyzes the ATP-dependent formation of a phosphodiester at the site of a single-strand break in duplex DNA

Date:

2017-03-02

All proteins in this family with known functions are ATP-dependent DNA ligases. Functions include DNA repair, DNA replication, and DNA recombination (or any process requiring ligation of two single-stranded DNA sections). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Date:

2024-05-30