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Mettu_2674 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2674" - TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial 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
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Mettu_2674TIGRFAM- 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)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
  0.969
Mettu_2713
PFAM- Ankyrin repeat; KEGG- sdy-SDY_P106 hypothetical protein (938 aa)
   
  0.902
Mettu_3281
SMART- 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)
 
  0.873
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)
     
  0.872
Mettu_1083
KEGG- pmy-Pmen_0549 sporulation domain-containing protein; PFAM- Sporulation/cell division region, bacteria; SMART- ATPase, AAA+ type, core (628 aa)
   
  0.849
Mettu_4364
AAA ATPase central domain protein; KEGG- mca-MCA1782 recombination factor protein RarA; PFAM- ATPase, AAA-type, core; SMART- ATPase, AAA+ type, core (435 aa)
   
  0.821
recG
ATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3’- to 5’- polarity. Unwinds branched duplex DNA (Y-DNA) (699 aa)
   
  0.817
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)
   
  0.804
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)
   
  0.803
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)
   
  0.799
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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