{PDOC00295} {PS00697; DNA_LIGASE_A1} {PS00333; DNA_LIGASE_A2} {PS50160; DNA_LIGASE_A3} {BEGIN} *************************************************** * 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 6.5.1.1), the other NAD (EC 6.5.1.2). 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. -Consensus pattern: [EDQH]-{K}-K-{VEDI}-[DN]-G-{GLYN}-R-[GACIVM] [K is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: 33. -Consensus pattern: E-G-[LIVMA]-[LIVM]-[LIVMA]-[KR]-x(5,8)-[YW]-[QNEKTI]- x(2,6)-[KRH]-x(3,5)-K-[LIVMFY]-K -Sequences known to belong to this class detected by the pattern: ALL, except for archebacterial DNA ligases. -Other sequence(s) detected in Swiss-Prot: NONE. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: 1. -Last update: April 2006 / Patterns revised. [ 1] Tomkinson A.E., Totty N.F., Ginsburg M., Lindahl T. "Location of the active site for enzyme-adenylate formation in DNA ligases." Proc. Natl. Acad. Sci. U.S.A. 88:400-404(1991). PubMed=1988940 [ 2] Lindahl T., Barnes D.E. "Mammalian DNA ligases." Annu. Rev. Biochem. 61:251-281(1992). PubMed=1497311; DOI=10.1146/annurev.bi.61.070192.001343 [ 3] Kletzin A. "Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases." Nucleic Acids Res. 20:5389-5396(1992). PubMed=1437556 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}