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Mettu_4215 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_4215" - Exodeoxyribonuclease I in Methylobacter tundripaludum
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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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_4215Exodeoxyribonuclease I (501 aa)    
Predicted Functional Partners:
Mettu_4247
Single-stranded DNA-binding protein ; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism (164 aa)
     
 
  0.879
recB
Helicase/nuclease RecBCD subunit RecB ; 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 [...] (1185 aa)
       
 
  0.852
Mettu_1482
Single-stranded DNA-binding protein ; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism (144 aa)
     
      0.817
recD
Helicase/nuclease RecBCD 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 [...] (562 aa)
       
 
  0.785
recC
Helicase/nuclease RecBCD subunit RecC ; 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 [...] (1077 aa)
           
  0.773
recA
Recombinase A ; 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)
       
 
  0.727
recF
DNA replication and repair protein RecF ; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP (358 aa)
     
   
  0.694
Mettu_1042
Single-stranded-DNA-specific exonuclease RecJ (581 aa)
     
 
  0.693
recO
Recombination protein O ; Involved in DNA repair and RecF pathway recombination (249 aa)
     
 
  0.687
ruvB
Holliday junction ATP-dependent DNA helicase RuvB ; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (344 aa)
     
 
  0.685
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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