STRINGSTRING
STRING protein interaction network
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
recCDNA helicase, ATP-dependent dsDNA/ssDNA exonuclease V subunit, ssDNA endonuclease; 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 [...] (1139 aa)    
Predicted Functional Partners:
recD
DNA helicase, ATP-dependent dsDNA/ssDNA exonuclease V subunit, ssDNA endonuclease; 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 [...]
 
 0.991
recB
ATP-dependent exoDNAse beta subunit; 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 rep [...]
 
 
 0.987
paaG6
Putative enoyl-CoA hydratase paaG; Function:- Could possibly oxidizes fatty acids using specific components (By similarity). Activity:-(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O. Entry name:- SWISSPROT:PAAG_ECOLI InterPro:- IPR001753; EnCoA_hydrtse. Pfam:- PF00378; ECH; 1. Identities = 65/222 (29%) Prediction: Non-secretory protein Signal peptide probability: 0.000 Number of predicted TMHs: 0; Family membership.
       0.773
yeaT
Putative transcriptional regulator, LysR family,; High confidence in function and specificity; Belongs to the LysR transcriptional regulatory family.
       0.613
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
   
 0.522
ada
Methylated-DNA--[protein]-cysteine S-methyltransferase (6-O-methylguanine-DNA methyltransferase) (O-6-methylguanine-DNA-alkyltransferase) InterPro: Methylated-DNA--protein-cysteine methyltransferase; High confidence in function and specificity.
     
 0.448
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.