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Mettu_3281 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3281" - SMART: DNA topoisomerase, type IA, DNA-binding in Methylobacter tundripaludum
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
Mettu_3281SMART- DNA topoisomerase, type IA, DNA-binding; DNA topoisomerase, type IA, domain 2; Toprim domain, subgroup; TIGRFAM- DNA topoisomerase III, bacterial-type; KEGG- wch-wcw_0920 DNA topoisomerase III; PFAM- DNA topoisomerase, type IA, central; Toprim domain (789 aa)    
Predicted Functional Partners:
Mettu_2674
TIGRFAM- DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type, N-terminal; PFAM- RQC domain; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; DNA/RNA helicase, C-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG- mca-MCA1868 ATP-dependent DNA helicase RecQ; SMART- DEAD-like helicase, N-terminal; DNA/RNA helicase, C-terminal; Helicase/RNase D C-terminal, HRDC domain (712 aa)
 
  0.873
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
  0.817
Mettu_3480
Pyruvate-flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (1212 aa)
     
 
  0.747
recA
Protein RecA; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (345 aa)
   
  0.725
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1397 aa)
     
 
  0.713
rpoA
DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (337 aa)
     
 
  0.702
recD
RecBCD enzyme subunit RecD; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3’ direction. Cuts ssDNA a few nucleotides 3’ to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3’-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holo [...] (562 aa)
   
 
  0.664
Mettu_2681
SNF2-related protein; KEGG- hch-HCH_06999 SNF2 family DNA/RNA helicase; PFAM- SNF2-related; Zinc finger, SWIM-type; DNA/RNA helicase, C-terminal; SMART- DEAD-like helicase, N-terminal; DNA/RNA helicase, C-terminal (1083 aa)
   
 
  0.655
rapA
RNA polymerase-associated protein RapA; Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair (938 aa)
   
 
  0.652
Mettu_1247
Flagella basal body P-ring formation protein FlgA; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P-ring assembly (232 aa)
       
      0.599
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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