- 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
-
1VS0
-
- 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.