Rv1647 - conserved hypothetical protein


Protein Domains

Gene Information
LocusRv1647
Symbol
Gene Nameconserved hypothetical protein
Location1856774 - 1857724 (+)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:951 bp
Protein:317 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number2985
Related GenesMAP1357 MAV_3122 Mkms_3019 ML1399 Mmcs_2975 MSMEG_3780 MT1685 MUL_1633 Mvan_3321 nfa53340
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv1647
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
TermTBRXN:ADNCYC adenylate cyclase - ISSactivenjamshidi2012-10-05
PMID: 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
TermEC:4.6.1.1 Adenylate cyclase. - ISSactivenjamshidi2012-10-05
PMID: 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 - ISSactivenjamshidi2012-10-05
PMID: 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
TermEC:4.6.1.1 Adenylate cyclase. - ISSactivenjamshidi2012-10-05
PMID: 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 - IDAactivenjamshidi2012-10-05
PMID: 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
TermEC:4.6.1.1 Adenylate cyclase. - IDAactivenjamshidi2012-10-05
PMID: 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 - IDAactivenjamshidi2012-10-05
PMID: 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
TermEC:4.6.1.1 Adenylate cyclase. - IDAactivenjamshidi2012-10-05
PMID: 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
TermEC:4.6.1.1 Adenylate cyclase. - NRactiveextern:JZUCKER2012-03-06
Assay 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