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
Daci_4000TIGRFAM: transcriptional regulator, Rrf2 family; iron-sulfur cluster assembly transcription factor IscR; PFAM: protein of unknown function UPF0074; KEGG: ajs:Ajs_2145 transcriptional regulator, BadM/Rrf2 family. (178 aa)    
Predicted Functional Partners:
Daci_3998
FeS cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
 
  
 0.975
iscS
Cysteine desulfurase IscS; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
  
 0.971
hscB
Co-chaperone Hsc20; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.
 
  
 0.957
Daci_3997
TIGRFAM: iron-sulfur cluster assembly accessory protein; iron-sulfur cluster assembly protein IscA; PFAM: HesB/YadR/YfhF-family protein; KEGG: ajs:Ajs_2142 iron-sulfur cluster assembly protein IscA; Belongs to the HesB/IscA family.
  
  
 0.890
Daci_3994
TIGRFAM: ferredoxin, 2Fe-2S type, ISC system; PFAM: ferredoxin; KEGG: ajs:Ajs_2139 ferredoxin, 2Fe-2S type, ISC system.
  
  
 0.660
uvrB
Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...]
       0.506
Daci_1079
PFAM: globin; oxidoreductase FAD/NAD(P)-binding domain protein; Oxidoreductase FAD-binding domain protein; KEGG: pmy:Pmen_3580 globin; Belongs to the globin family.
     
 0.491
Daci_2352
PFAM: ferredoxin; KEGG: pla:Plav_2520 ferredoxin.
  
  
 0.480
Daci_0354
TIGRFAM: cell shape determining protein, MreB/Mrl family; PFAM: cell shape determining protein MreB/Mrl; KEGG: ajs:Ajs_0239 cell shape determining protein, MreB/Mrl family.
  
    0.461
dnaQ
DNA polymerase III, epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease.
 
    0.460
Your Current Organism:
Delftia acidovorans
NCBI taxonomy Id: 398578
Other names: D. acidovorans SPH-1, Delftia acidovorans SPH-1, Delftia acidovorans str. SPH-1, Delftia acidovorans strain SPH-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.