TB Genome Annotation Portal

Rv0938 (ligD)

Amino Acid Sequence

MGSASEQRVTLTNADKVLYPATGTTKSDIFDYYAGVAEVMLGHIAGRPATRKRWPNGVDQPAFFEKQLALSAPPWLSRATVAHRSGTTTYPIIDSATGLA
WIAQQAALEVHVPQWRFVAEPGSGELNPGPATRLVFDLDPGEGVMMAQLAEVARAVRDLLADIGLVTFPVTSGSKGLHLYTPLDEPVSSRGATVLAKRVA
QRLEQAMPALVTSTMTKSLRAGKVFVDWSQNSGSKTTIAPYSLRGRTHPTVAAPRTWAELDDPALRQLSYDEVLTRIARDGDLLERLDADAPVADRLTRY
RRMRDASKTPEPIPTAKPVTGDGNTFVIQEHHARRPHYDFRLECDGVLVSWAVPKNLPDNTSVNHLAIHTEDHPLEYATFEGAIPSGEYGAGKVIIWDSG
TYDTEKFHDDPHTGEVIVNLHGGRISGRYALIRTNGDRWLAHRLKNQKDQKVFEFDNLAPMLATHGTVAGLKASQWAFEGKWDGYRLLVEADHGAVRLRS
RSGRDVTAEYPQLRALAEDLADHHVVLDGEAVVLDSSGVPSFSQMQNRGRDTRVEFWAFDLLYLDGRALLGTRYQDRRKLLETLANATSLTVPELLPGDG
AQAFACSRKHGWEGVIAKRRDSRYQPGRRCASWVKDKHWNTQEVVIGGWRAGEGGRSSGVGSLLMGIPGPGGLQFAGRVGTGLSERELANLKEMLAPLHT
DESPFDVPLPARDAKGITYVKPALVAEVRYSEWTPEGRLRQSSWRGLRPDKKPSEVVRE
(Nucleotide sequence available on KEGG)

Additional Information




Analysis of Positive Selection in Clinical Isolates *new*

Moldova (2,057)global set (5,195)
under significant positive selection?NONO
omega peak height (95%CI lower bound)1.68 (0.25)1.35 (0.5)
codons under selection
omega plots
genetic variants*linklink
statistics at each codonlinklink
* example format for variants: "D27 (GAC): D27H (CAC,11)" means "Asp27 (native codon GAC) mutated to His (codon CAC) in 11 isolates"


ESSENTIALITY

MtbTnDB - interactive tool for exploring a database of published TnSeq datasets for Mtb

TnSeqCorr - genes with correlated TnSeq profiles across ~100 conditions

Rv0938/ligD, gene len: 2279 bp, num TA sites: 43
conditiondatasetcallmediummethodnotes
in-vitroDeJesus 2017 mBionon-essential7H9HMMfully saturated, 14 TnSeq libraries combined
in-vitroSassetti 2003 Mol Microno data 7H9TRASHessential if hybridization ratio<0.2
in-vivo (mice)Sassetti 2003 PNASno data BL6 miceTRASHessential if hybridization ratio<0.4, min over 4 timepoints (1-8 weeks)
in-vitro (glycerol)Griffin 2011 PPathessentialM9 minimal+glycerolGumbel2 replicates; Padj<0.05
in-vitro (cholesterol)Griffin 2011 PPathuncertainM9 minimal+cholesterolGumbel3 replicates; Padj<0.05
differentially essential in cholesterol Griffin 2011 PPathNO (LFC=0.23)cholesterol vs glycerolresampling-SRYES if Padj<0.05, else not significant; LFC<0 means less insertions/more essential in cholesterol
in-vitroSmith 2022 eLifenon-essential7H9HMM6 replicates (raw data in Subramaniam 2017, PMID 31752678)
in-vivo (mice)Smith 2022 eLifenon-essentialBL6 miceHMM6 replicates (raw data in Subramaniam 2017, PMID 31752678)
differentially essential in miceSmith 2022 eLifeNO (LFC=0.077)in-vivo vs in-vitroZINBYES if Padj<0.05, else not significant; LFC<0 means less insertions/more essential in mice
in-vitro (minimal)Minato 2019 mSysnon-essentialminimal mediumHMM
in-vitro (YM rich medium)Minato 2019 mSysnon-essentialYM rich mediumHMM7H9 supplemented with ~20 metabolites (amino acids, cofactors)
differentially essential in YM rich mediumMinato 2019 mSysNO (LFC=-0.55)YM rich vs minimal mediumresampling

TnSeq Data No data currently available.
  • No TnSeq data currently available for this Target.
RNASeq Data No data currently available.
  • No RNA-Seq data currently available for this Target.
Metabolomic Profiles No data currently available.
  • No Metabolomic data currently available for this Target.
Proteomic Data No data currently available.
  • No Proteomic data currently available for this Target.

Regulatory Relationships from Systems Biology
  • BioCyc

    Gene interactions based on ChIPSeq and Transcription Factor Over-Expression (TFOE) (Systems Biology)

    NOTE: Green edges represent the connected genes being classified as differentially essential as a result of the middle gene being knocked out. These interactions are inferred based on RNASeq.

    Interactions based on ChIPSeq data

  • Interactions based on ChIPSeq data (Minch et al. 2014)

    • Binds To:

      • No bindings to other targets were found.
    • Bound By:

    Interactions based on TFOE data (Rustad et al. 2014)



    TBCAP

    Tubculosis Community Annotation Project (
    Slayden et al., 2013)

    Rv0938 (ligD)

    PropertyValueCreatorEvidencePMIDComment
    CitationMycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair. KM. Sinha, NC. Stephanou et al. J. Biol. Chem. 2007aparna.vchalamIDA17376770Yeast two-hybrid (Physical interaction)
    InteractionPhysicalInteraction Rv0937caparna.vchalamIDAYeast 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
    CitationDomain structure of a NHEJ DNA repair ligase from Mycobacterium tuberculosis. authors,RS. Pitcher,LM. Tonkin,AJ. Green,AJ. Doherty J. Mol. Biol. 2005aparna.vchalamIDA16023671Yeast two-hybrid (Physical interaction)
    InteractionPhysicalInteraction Rv0937caparna.vchalamIDAYeast 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
    CitationMechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase C. authors,C. Gong,P. Bongiorno,A. Martins,NC. Stephanou,H. Zhu,S. Shuman,MS. Glickman Nat. Struct. Mol. Biol. 2005aparna.vchalamIDA15778718Yeast two-hybrid (Physical interaction)
    InteractionPhysicalInteraction Rv0937caparna.vchalamIDAYeast 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 Rv0937caparna.vchalamIDAYeast 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
    InteractionPhysicalInteraction Rv0937caparna.vchalamIDAYeast 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 Rv0937caparna.vchalamIDAYeast 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 Rv0937caparna.vchalamIDAYeast 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
    CitationCrystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D. authors,D. Akey,A. Martins,J. Aniukwu,MS. Glickman,S. Shuman,JM. Berger J. Biol. Chem. 2006aparna.vchalamIDA16476729Yeast two-hybrid (Physical interaction)
    InteractionPhysicalInteraction Rv0937caparna.vchalamIDAYeast 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
    InteractionRegulatedBy Rv0491yamir.morenoISOE.coli orthology based inference. Orthologous pair regulator-target found in E.coli.
    G. Balzsi, AP. Heath et al. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 2008
    InteractionRegulatedBy Rv0491yamir.morenoISOE.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
    SymbolligDvmizrahiCatalyses DSB repair via non-homologous end-joining (NHEJ) with Ku. Biochemically characterised.
    OtherTBPWY:Non-homologous end-joiningvmizrahiCatalyses DSB repair via non-homologous end-joining (NHEJ) with Ku. Biochemically characterised.
    OtherTBPWY:Non-homologous end-joiningvmizrahiCrystal structures of the primase/polymerisation domain (PolDom) of LigD have been determined alone and complexed with nucleotides
    OtherTBPWY:Non-homologous end-joiningvmizrahiCrystal structure and nonhomologous end-joining function of the ligase component of LigD determined

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