TB Genome Annotation Portal

Rv1647 (-)

Amino Acid Sequence

LAGSARTTYPCHVEVGPQDSESGAPDETATAMASPVPRQRSALRWLRTVNRSPGLVSFIHRARRLLPGDPEFGDPLSTAGEGGPRAAARAADRLLRDRDA
ASREVGLSVLQVWQALTEAVSRRPANPEVTLVFTDLVGFSTWSLHAGDDATLTLLRQVARAVESPLLDAGGHIVKRLGDGIMAVFRNPTVALRAVLVAQD
AVKSLEVQGYTPRMRIGIHTGRPQRLAADWLGVDVNIAARVMERATKGGIMISQPTLDLIPQSELDALGVVARRVRKPVFASKPTGIPPDLAIYRIKTVS
ESTAADNFDEMSPDAQ
(Nucleotide sequence available on KEGG)

Additional Information



ESSENTIALITY

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

TnSeqCorr - genes with correlated TnSeq profiles across >100 conditions *new*

Classification Condition Strain Method Reference Notes
Non-Essential Sodium Oleate H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
2 non-insertions in a row out of 11 sites
Non-Essential Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
2 non-insertions in a row out of 11 sites
Non-Essential Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
2 non-insertions in a row out of 11 sites
Non-Essential minimal media + 0.1% glycerol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.000000;
1 non-insertions in a row out of 12 sites
Non-Essential minimal media + 0.01% cholesterol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.000000;
2 non-insertions in a row out of 12 sites
Non-Essential 7H10-glycerol H37RvMA TraSH Sassetti et al. (2003a)
Non-Essential C57BL/6J mice (8 weeks) H37RvMA TraSH Sassetti et al. (2003b) Hybridization Ratio: 0.92
Non-Essential 7H09/7H10 + rich media H37RvMA MotifHMM DeJesus et al. (2017) Fully saturated (14 reps).

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:

      • No bindings to other targets were found.

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



    TBCAP

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

    Rv1647 (-)

    PropertyValueCreatorEvidencePMIDComment
    CitationFunctional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. JU. Linder, LI. Castro et al. FEBS Lett. 2004njamshidiISS|15196937|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    TermEC:4.6.1.1 Adenylate cyclase. - ISSnjamshidiISS|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    JU. Linder, LI. Castro et al. Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. FEBS Lett. 2004
    TermTBRXN:ADNCYC adenylate cyclase - ISSnjamshidiISS|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    JU. Linder, LI. Castro et al. Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. FEBS Lett. 2004
    CitationCharacterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. AR. Shenoy, NP. Sreenath et al. Biochem. J. 2005njamshidiIDA|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    TermEC:4.6.1.1 Adenylate cyclase. - IDAnjamshidiIDA|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    AR. Shenoy, NP. Sreenath et al. Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. Biochem. J. 2005
    TermTBRXN:ADNCYC adenylate cyclase - IDAnjamshidiIDA|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    AR. Shenoy, NP. Sreenath et al. Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. Biochem. J. 2005
    CitationFunctional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. JU. Linder, LI. Castro et al. FEBS Lett. 2004njamshidiIDA|15196937|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    TermEC:4.6.1.1 Adenylate cyclase. - IDAnjamshidiIDA|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    JU. Linder, LI. Castro et al. Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. FEBS Lett. 2004
    TermTBRXN:ADNCYC adenylate cyclase - IDAnjamshidiIDA|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    JU. Linder, LI. Castro et al. Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. FEBS Lett. 2004
    CitationCharacterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. AR. Shenoy, NP. Sreenath et al. Biochem. J. 2005njamshidiISS|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    TermEC:4.6.1.1 Adenylate cyclase. - ISSnjamshidiISS|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    AR. Shenoy, NP. Sreenath et al. Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. Biochem. J. 2005
    TermTBRXN:ADNCYC adenylate cyclase - ISSnjamshidiISS|15500449PMID: 15500449 , also PMID: 15196937 note that ML1399 (M leprae) codes for adenylate cyclase
    AR. Shenoy, NP. Sreenath et al. Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. Biochem. J. 2005
    CitationCharacterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. AR. Shenoy, NP. Sreenath et al. Biochem. J. 2005extern:JZUCKER15500449Assay of protein purified to homogeneity from a heterlogous host
    TermEC:4.6.1.1 Adenylate cyclase. - NRextern:JZUCKERNRAssay of protein purified to homogeneity from a heterlogous host
    AR. Shenoy, NP. Sreenath et al. Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae. Biochem. J. 2005

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