Rv0938 - ATP dependent DNA ligase


Protein Domains

Gene Information
LocusRv0938
Symbol
Gene NameATP dependent DNA ligase
Location1046136 - 1048415 (+)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:2280 bp
Protein:760 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number25679
Related GenesMAP0880 MAV_1056 Mkms_4438 Mmcs_4352 MSMEG_5570 MT0965 MUL_4434 Mvan_4915 nfa6770 SAV2946
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv0938
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
authors,C. Gong,P. Bongiorno,A. Martins,NC. Stephanou,H. Zhu,S. Shuman,MS. Glickman 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
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
authors,RS. Pitcher,LM. Tonkin,AJ. Green,AJ. Doherty Domain structure of a NHEJ DNA repair ligase from Mycobacterium tuberculosis. J. Mol. Biol. 2005
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
KM. Sinha, NC. Stephanou et al. Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair. J. Biol. Chem. 2007
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
authors,D. Akey,A. Martins,J. Aniukwu,MS. Glickman,S. Shuman,JM. Berger Crystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D. J. Biol. Chem. 2006
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
authors,C. Gong,P. Bongiorno,A. Martins,NC. Stephanou,H. Zhu,S. Shuman,MS. Glickman 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
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
authors,RS. Pitcher,LM. Tonkin,AJ. Green,AJ. Doherty Domain structure of a NHEJ DNA repair ligase from Mycobacterium tuberculosis. J. Mol. Biol. 2005
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
KM. Sinha, NC. Stephanou et al. Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair. J. Biol. Chem. 2007
InteractionPhysicalInteraction Rv0937cactiveaparna.vchalam2012-10-05
Yeast two-hybrid (Physical interaction)
authors,RS. Pitcher,LM. Tonkin,JM. Daley,PL. Palmbos,AJ. Green,TL. Velting,A. Brzostek,M. Korycka-Machala,S. Cresawn,J. Dziadek,GF. Hatfull,TE. Wilson,AJ. Doherty Mycobacteriophage exploit NHEJ to facilitate genome circularization. Mol. Cell 2006
InteractionRegulatedBy Rv0491activeyamir.moreno2012-10-05
E.coli orthology based inference. Orthologous pair regulator-target found in E.coli.
G. Balázsi, AP. Heath et al. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 2008
InteractionRegulatedBy Rv0491activeyamir.moreno2012-10-05
E.coli orthology based inference. Orthologous pair regulator-target found in E.coli.
authors,M. Madan Babu,SA. Teichmann,L. Aravind Evolutionary dynamics of prokaryotic transcriptional regulatory networks. J. Mol. Biol. 2006
OtherTBPWY:Non-homologous end-joiningactivevmizrahi2012-03-05
Crystal structure and nonhomologous end-joining function of the ligase component of LigD determined
OtherTBPWY:Non-homologous end-joiningactivevmizrahi2012-03-05
Crystal structures of the primase/polymerisation domain (PolDom) of LigD have been determined alone and complexed with nucleotides
OtherTBPWY:Non-homologous end-joiningactivevmizrahi2012-03-05
Catalyses DSB repair via non-homologous end-joining (NHEJ) with Ku. Biochemically characterised.
SymbolligDactivevmizrahi2012-03-05
Catalyses DSB repair via non-homologous end-joining (NHEJ) with Ku. Biochemically characterised.