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Mettu_2187 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2187" - DNA polymerase I in Methylobacter tundripaludum
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query proteins and first shell of interactors
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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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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_2187DNA polymerase I (930 aa)    
Predicted Functional Partners:
Mettu_1953
DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA (366 aa)
   
  0.999
Mettu_3850
DNA-directed DNA polymerase (1164 aa)
   
  0.994
Mettu_0829
DNA polymerase III, delta prime subunit (352 aa)
 
  0.994
sbcD
Nuclease SbcCD subunit D ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity (413 aa)
   
  0.994
Mettu_3842
Nuclease SbcCD subunit C ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity (1147 aa)
     
  0.987
Mettu_2609
Nuclease SbcCD subunit C ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity (1260 aa)
     
  0.987
Mettu_2113
DNA sulfur modification protein DndD (678 aa)
     
  0.987
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)
   
  0.987
Mettu_3680
Ribonucleotide reductase, alpha subunit (254 aa)
   
  0.985
Mettu_3679
Ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent (716 aa)
   
  0.985
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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