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
mfdTranscription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily. (1147 aa)    
Predicted Functional Partners:
rpoC
DNA-directed RNA polymerase, beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 
 0.959
uvrA
Excinuclease ABC, A subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
 
 
 
 0.947
rpoB
DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 
 0.946
rpoA
DNA-directed RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 
 
 0.936
rpoZ
DNA-directed RNA polymerase, omega subunit; 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.
    
 
 0.921
Deba_1624
InterPro IPR005834; KEGG: ppr:PBPRA2135 hypothetical protein; PFAM: Haloacid dehalogenase domain protein hydrolase; SPTR: A6FCM0 Putative uncharacterized protein; PFAM: haloacid dehalogenase-like hydrolase.
       0.786
pth
peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
  
  
 0.715
tilS
tRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family.
 
  
 0.706
prfB
LigA; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
   
  
 0.684
Deba_2230
COGs: COG1186 Protein chain release factor B; InterPro IPR000352; KEGG: ank:AnaeK_3493 class I peptide chain release factor; PFAM: Class I peptide chain release factor; SPTR: B4UBN2 Class I peptide chain release factor; PFAM: RF-1 domain.
   
  
 0.684
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.