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
recRRecombination protein recR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. (198 aa)    
Predicted Functional Partners:
recO
DNA repair protein recO; Involved in DNA repair and RecF pathway recombination.
 
 
 0.987
CCH86013.1
Conserved protein of unknown function; Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
  
  
 0.982
recF
DNA replication and repair protein recF; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP; Belongs to the RecF family.
 
  
 0.891
recA
Recombinase A (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; Belongs to the RecA family.
 
   
 0.781
ruvB
Holliday junction DNA helicase ruvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
   
 0.776
dnaA
Chromosomal replication initiator protein dnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family.
 
  
 0.773
pcrA
ATP-dependent DNA helicase pcrA; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 
   
 0.748
ruvA
Holliday junction ATP-dependent DNA helicase ruvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
 
   
 0.730
dnaG-2
DNA primase (modular protein); RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Belongs to the DnaG primase family.
      
 0.707
dnaX
DNA polymerase III, subunits gamma and tau; 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.
  
 0.693
Your Current Organism:
Modestobacter marinus
NCBI taxonomy Id: 477641
Other names: CGMCC 4.5581, DSM 45201, M. marinus, Modestobacter marinus Xiao et al. 2011, Modestobacter sp. 42H12-1, strain 42H12-1
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