• Version:
  • 11.0 (preview - - version 10.5 still available here)
STRINGSTRING
Mettu_2609 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2609" - PFAM: RecF/RecN/SMC protein, N-terminal in Methylobacter tundripaludum
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_2609PFAM- RecF/RecN/SMC protein, N-terminal; KEGG- mxa-MXAN_0959 nuclease SbcCD subunit C (1260 aa)    
Predicted Functional Partners:
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)
  0.997
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
  0.937
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)
   
  0.758
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)
   
  0.701
Mettu_2713
PFAM- Ankyrin repeat; KEGG- sdy-SDY_P106 hypothetical protein (938 aa)
   
  0.682
Mettu_1189
KEGG- eba-p1B285 hypothetical protein (293 aa)
      
  0.680
Mettu_4224
Protein-glutamate methylesterase; PFAM- Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase; MCP methyltransferase, CheR-type; KEGG- mag-amb3654 hypothetical protein; SMART- MCP methyltransferase, CheR-type (976 aa)
   
  0.670
Mettu_0457
TIGRFAM- CRISPR-associated protein Crm2; KEGG- dae-Dtox_2979 CRISPR-associated protein, Crm2 family (634 aa)
        
      0.648
Mettu_4044
PFAM- Mechanosensitive ion channel MscS; KEGG- nhl-Nhal_3600 MscS mechanosensitive ion channel (1136 aa)
   
  0.607
Mettu_2611
ADP-ribosyl-(Dinitrogen reductase) hydrolase; TIGRFAM- ADP-ribosyl-dinitrogen reductase hydrolase; KEGG- rru-Rru_A1008 ADP-ribosyl-(dinitrogen reductase) hydrolase; PFAM- ADP-ribosylation/Crystallin J1 (294 aa)
              0.586
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
Server load: low (9%) [HD]
STRING is part of the ELIXIR infrastructure: it is one of ELIXIR's Core Data Resources.  Learn more >