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Mettu_2681 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2681" - SNF2-related protein in Methylobacter tundripaludum
Nodes:
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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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empty nodes:
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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Gene Fusion
Cooccurence
Coexpression
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[Homology]
Score
Mettu_2681SNF2-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)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
  0.891
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)
   
  0.803
Mettu_2713
PFAM- Ankyrin repeat; KEGG- sdy-SDY_P106 hypothetical protein (938 aa)
 
  0.789
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)
     
  0.759
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)
 
 
 
  0.759
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1364 aa)
     
  0.756
Mettu_1953
Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] (366 aa)
   
  0.755
dinB
DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3’-5’ exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (367 aa)
   
  0.752
rpoZ
DNA-directed RNA polymerase subunit omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta’ subunit thereby facilitating its interaction with the beta and alpha subunits (81 aa)
   
    0.747
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)
     
  0.746
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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