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_2749PFAM: cytochrome c class I; KEGG: aav:Aave_1504 cytochrome c, class I. (102 aa)    
Predicted Functional Partners:
Daci_1565
PFAM: cytochrome c class I; KEGG: ajs:Ajs_3583 cytochrome c, class I.
  
  
 
0.910
Daci_0055
PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; KEGG: ajs:Ajs_0035 oxidoreductase, molybdopterin binding.
   
 
 0.684
Daci_2499
Gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I; KEGG: rme:Rmet_2155 cytochrome c, class I.
 
  
 0.652
Daci_2750
KEGG: aav:Aave_1505 hypothetical protein.
       0.640
Daci_5007
TIGRFAM: 40-residue YVTN family beta-propeller repeat protein; KEGG: ajs:Ajs_1184 hypothetical protein.
  
  
 0.625
Daci_2239
PFAM: Rieske [2Fe-2S] domain protein; KEGG: ajs:Ajs_1035 Rieske (2Fe-2S) domain protein.
  
     0.512
Daci_3134
PFAM: oxidoreductase molybdopterin binding; KEGG: dar:Daro_2592 oxidoreductase, molybdopterin binding.
   
 
 0.405
msrP
Oxidoreductase molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce b [...]
   
 
 0.405
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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