Rv0937c - conserved hypothetical protein


Protein Domains

Gene Information
LocusRv0937c
Symbol
Gene Nameconserved hypothetical protein
Location1045199 - 1046020 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:822 bp
Protein:274 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number24893
Related GenesMAP0875c MAV_1050 Mkms_4447 Mmcs_4361 MSMEG_5580 MT0964 MUL_4436 Mvan_4917 nfa34910
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv0937c
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionPhysicalInteraction Rv0938activeaparna.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 Rv0938activeaparna.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 Rv0938activeaparna.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 Rv0938activeaparna.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 Rv0938activeaparna.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 Rv0938activeaparna.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 Rv0938activeaparna.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 Rv0938activeaparna.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
OtherTBPWY:Non-homologous end-joiningactivevmizrahi2012-03-05
LigD consists of a C-terminal ATP-dependent ligase domain fused to upstream polymerase and phosphoesterase modules. Catalyses DSB repair via non-homologous end-joining (NHEJ) with DNA ligase D (LigD)
Symbolkuactivevmizrahi2012-03-05
LigD consists of a C-terminal ATP-dependent ligase domain fused to upstream polymerase and phosphoesterase modules. Catalyses DSB repair via non-homologous end-joining (NHEJ) with DNA ligase D (LigD)