ligD



Type
protein_coding
Name
ligD
Locus Name

Rv0938

Product

ATP dependent DNA ligase LigD (ATP dependent polydeoxyribonucleotide synthase) (thermostable DNA ligase) (ATP dependent polynucleotide ligase) (sealase) (DNA repair enzyme) (DNA joinase)

Functional Category

Information pathways

Location
1046136..1048415 (+ strand)
Gene Length
2279 bp
Nucleotides
TGGGTTCGGCGTCGGAGCAACGGGTGACGCTGACCAACGCCGACAAGGTGCTCTATCCCGCCACCGGGACCACAAAGTCCGATATCTTCGACTACTACGCCGGTGTTGCCGAAGTCATGCTCGGCCACATCGCGGGACGGCCGGCGACGCGCAAGCGCTGGCCTAACGGCGTCGACCAACCCGCGTTCTTCGAAAAGCAGTTGGCGTTGTCGGCGCCGCCTTGGCTGTCACGTGCAACGGTGGCGCACCGGTCCGGGACGACGACCTATCCGATCATCGATAGCGCAACCGGGCTGGCCTGGATCGCCCAACAGGCGGCGCTGGAGGTGCACGTGCCGCAGTGGCGGTTTGTCGCCGAGCCCGGATCAGGTGAGTTAAATCCGGGCCCGGCAACGCGTTTGGTGTTCGACCTGGACCCGGGCGAAGGCGTGATGATGGCCCAGCTGGCCGAGGTGGCGCGCGCGGTTCGTGATCTTCTCGCCGATATCGGGTTGGTCACCTTCCCGGTCACCAGCGGCAGCAAGGGATTGCATCTGTACACACCGCTGGATGAGCCGGTGAGCAGCAGGGGAGCCACGGTGTTGGCCAAGCGCGTCGCGCAGCGATTGGAGCAGGCGATGCCCGCGTTGGTCACCTCGACCATGACCAAAAGCCTGCGGGCCGGGAAGGTGTTTGTGGACTGGAGCCAGAACAGCGGCTCGAAGACCACCATCGCGCCGTACTCACTACGTGGCCGGACGCATCCGACCGTCGCGGCGCCACGCACCTGGGCGGAGCTCGACGACCCCGCACTGCGTCAGCTCTCCTACGACGAGGTGCTGACCCGGATTGCCCGCGACGGCGATCTGCTCGAGCGGCTGGATGCCGACGCTCCGGTAGCGGACCGGTTGACCCGATACCGCCGCATGCGCGACGCATCGAAAACTCCCGAGCCGATTCCCACGGCGAAACCCGTTACCGGAGACGGCAATACGTTCGTCATCCAGGAGCATCACGCGCGTCGGCCGCACTACGATTTCCGGCTGGAATGCGACGGCGTGCTGGTCTCGTGGGCGGTACCGAAAAACCTGCCCGACAACACATCGGTTAACCATCTAGCGATACACACCGAGGACCACCCGCTGGAATACGCCACGTTCGAGGGCGCGATTCCCAGCGGGGAGTACGGCGCCGGCAAGGTGATCATCTGGGACTCCGGCACTTACGACACCGAGAAGTTCCACGATGACCCGCACACGGGGGAGGTCATCGTGAATCTGCACGGCGGCCGGATCTCTGGGCGTTATGCGCTGATTCGGACCAACGGCGATCGGTGGCTGGCGCACCGCCTAAAGAATCAGAAAGACCAGAAGGTGTTCGAGTTCGACAATCTGGCCCCAATGCTTGCCACGCACGGCACGGTGGCCGGTCTAAAGGCCAGCCAGTGGGCGTTCGAAGGCAAGTGGGACGGCTACCGGTTGCTGGTTGAGGCTGACCACGGCGCCGTGCGGCTGCGGTCCCGCAGCGGGCGCGATGTCACCGCCGAGTATCCGCAATTGCGGGCATTGGCGGAGGATCTCGCCGATCACCACGTGGTGCTGGACGGCGAGGCCGTCGTACTTGACTCCTCTGGTGTGCCCAGCTTCAGCCAGATGCAGAATCGGGGCCGCGACACCCGTGTCGAGTTCTGGGCGTTCGACCTGCTCTACCTCGACGGCCGCGCGCTGCTAGGCACCCGCTACCAAGACCGGCGTAAGCTGCTCGAAACCCTAGCTAACGCAACCAGTCTCACCGTTCCCGAGCTGCTGCCCGGTGACGGCGCCCAAGCGTTTGCGTGCTCGCGCAAGCACGGCTGGGAGGGCGTGATCGCCAAGAGGCGTGACTCGCGCTATCAGCCGGGCCGGCGCTGCGCGTCGTGGGTCAAGGACAAGCACTGGAACACCCAGGAAGTCGTCATTGGTGGCTGGCGCGCCGGGGAAGGCGGGCGCAGCAGTGGCGTCGGGTCGCTGCTCATGGGCATCCCCGGTCCAGGTGGGCTGCAGTTCGCCGGGCGGGTCGGTACCGGCCTCAGCGAACGCGAACTGGCCAACCTCAAGGAGATGCTGGCGCCGCTGCATACCGACGAGTCCCCCTTCGACGTACCACTGCCCGCGCGTGACGCCAAGGGCATCACATATGTCAAGCCGGCGCTGGTTGCAGAGGTGCGCTACAGCGAGTGGACTCCGGAGGGCCGGCTGCGTCAATCAAGCTGGCGTGGGCTGCGGCCGGACAAGAAACCCAGTGAGGTGGTGCGCGAATGA
Drug Resistance

Check for drug resistance association at TBDREAMDB

Mutations

Check for mutants available at TARGET


Function
With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs DNA double-strand breaks (DSB) with reduced fidelity. Recognizes, processes and reseals DSBs, including repairs on incompatible DSB which require 3'-resection, gap filling and ligation. Anneals the 3' overhanging strands from opposing breaks to form a gapped intermediate, which then can be extended in trans by using the termini as primers for extension of the annealed break. Binds to the recessed 5'-phosphate moiety of the downstream DNA strand forming a stable synaptic complex even when the 3'-protruding ends of the template DNA strands are not complementary. Has numerous activites; gap filling copies the template strand, and prefers a 5'-phosphate in the gap and rNTPS (PubMed:17174332, PubMed:17947582), DNA-directed DNA or RNA polymerase on 5'-overhangs, terminal transferase (extending ssDNA or blunt dsDNA in a non-templated fashion, preferentially with rNTPs), DNA-dependent RNA primase (synthesizes short RNAs on unprimed closed ssDNA) and 3'- to 5'-exonuclease on ssDNA (PubMed:15499016). Isolated Pol domain (and presumably the holoenzyme) is able to form complexes between 2 noncompatible protruding 3'-ends DNA ends via microhomologous DNA strands, in a end-bridging function to which it adds a templated nucleotide (PubMed:17947582). Minimal primer length is 2 nucleotides (PubMed:21255731). {ECO:0000269|PubMed:15499016, ECO:0000269|PubMed:17174332, ECO:0000269|PubMed:17947582, ECO:0000269|PubMed:21255731}.; FUNCTION: The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool is limiting.; FUNCTION: In conjunction with endogenous or Mycobacterium phage Omega Ku (AC Q853W0) can reconstitute NHEJ in Saccharomyces cerevisiae.
Family

LigD polymerase family; LigD 3'-phosphoesterase family; ATP-dependent DNA ligase family

GO
InterPro

UniProt
P9WNV3
GenBank
Rv0938
EnsemblBacteria
Rv0938
Mycobrowser
Rv0938


1VS0
Summary
Name
Multifunctional non-homologous end joining DNA repair protein LigD (NHEJ DNA repair protein D) (Mt-Lig) (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase/primase); 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase) (PE); DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP])]
Family
LigD polymerase family; LigD 3'-phosphoesterase family; ATP-dependent DNA ligase family
Protein Sequence
MGSASEQRVTLTNADKVLYPATGTTKSDIFDYYAGVAEVMLGHIAGRPATRKRWPNGVDQPAFFEKQLALSAPPWLSRATVAHRSGTTTYPIIDSATGLAWIAQQAALEVHVPQWRFVAEPGSGELNPGPATRLVFDLDPGEGVMMAQLAEVARAVRDLLADIGLVTFPVTSGSKGLHLYTPLDEPVSSRGATVLAKRVAQRLEQAMPALVTSTMTKSLRAGKVFVDWSQNSGSKTTIAPYSLRGRTHPTVAAPRTWAELDDPALRQLSYDEVLTRIARDGDLLERLDADAPVADRLTRYRRMRDASKTPEPIPTAKPVTGDGNTFVIQEHHARRPHYDFRLECDGVLVSWAVPKNLPDNTSVNHLAIHTEDHPLEYATFEGAIPSGEYGAGKVIIWDSGTYDTEKFHDDPHTGEVIVNLHGGRISGRYALIRTNGDRWLAHRLKNQKDQKVFEFDNLAPMLATHGTVAGLKASQWAFEGKWDGYRLLVEADHGAVRLRSRSGRDVTAEYPQLRALAEDLADHHVVLDGEAVVLDSSGVPSFSQMQNRGRDTRVEFWAFDLLYLDGRALLGTRYQDRRKLLETLANATSLTVPELLPGDGAQAFACSRKHGWEGVIAKRRDSRYQPGRRCASWVKDKHWNTQEVVIGGWRAGEGGRSSGVGSLLMGIPGPGGLQFAGRVGTGLSERELANLKEMLAPLHTDESPFDVPLPARDAKGITYVKPALVAEVRYSEWTPEGRLRQSSWRGLRPDKKPSEVVRE
Mass
83,572 Da
Length
759 Aa

Rv0938 doesn't seem to be a targeted by any drug.


Rv0938 doesn't seem to be involved in any pathway.


Molecular basis for DNA double-strand break annealing and primer extension by an NHEJ DNA polymerase.
Cell Rep. 2013 Nov 27;5(4):1108-20. doi: 10.1016/j.celrep.2013.10.016. Epub 2013 Nov 14.
Structure of a preternary complex involving a prokaryotic NHEJ DNA polymerase.
Mol Cell. 2011 Jan 21;41(2):221-31. doi: 10.1016/j.molcel.2010.12.026.
Structure of a NHEJ polymerase-mediated DNA synaptic complex.
Science. 2007 Oct 19;318(5849):456-9. doi: 10.1126/science.1145112.
Structure and function of a mycobacterial NHEJ DNA repair polymerase.
J Mol Biol. 2007 Feb 16;366(2):391-405. doi: 10.1016/j.jmb.2006.10.046. Epub 2006 Oct 20.
Crystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D.
J Biol Chem. 2006 May 12;281(19):13412-23. doi: 10.1074/jbc.M513550200. Epub 2006 Feb 13.
A Sir2-like protein participates in mycobacterial NHEJ.
PLoS One. 2011;6(5):e20045. doi: 10.1371/journal.pone.0020045. Epub 2011 May 26.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
Mycobacteriophage exploit NHEJ to facilitate genome circularization.
Mol Cell. 2006 Sep 1;23(5):743-8. doi: 10.1016/j.molcel.2006.07.009.
Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase C.
Nat Struct Mol Biol. 2005 Apr;12(4):304-12. doi: 10.1038/nsmb915. Epub 2005 Mar 20.
Domain structure of a NHEJ DNA repair ligase from Mycobacterium tuberculosis.
J Mol Biol. 2005 Aug 19;351(3):531-44. doi: 10.1016/j.jmb.2005.06.038.
Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine.
Science. 2004 Oct 22;306(5696):683-5. doi: 10.1126/science.1099824.
Biochemical and genetic analysis of the four DNA ligases of mycobacteria.
J Biol Chem. 2004 May 14;279(20):20594-606. doi: 10.1074/jbc.M401841200. Epub 2004 Feb 25.
Identification of a DNA nonhomologous end-joining complex in bacteria.
Science. 2002 Sep 6;297(5587):1686-9. doi: 10.1126/science.1074584.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.