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
STH2425Putative Fe-S oxidoreductase. (526 aa)    
Predicted Functional Partners:
STH483
Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
  
  
 
0.927
STH2424
Conserved hypothetical protein.
       0.757
argS
arginyl-tRNA synthetase.
   
    0.704
STH2426
Hypothetical protein.
       0.588
STH230
Glutamate synthase large subunit.
     
 0.564
STH3167
Pyruvate flavodoxin dehydrogenase.
  
  
 0.542
STH2433
Conserved hypothetical protein.
 
     0.522
rimO
2-methylthioadenine synthetase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily.
 
  
 0.517
STH3153
Cytochrome C oxidase heme b and copper-binding subunit.
  
  
 0.515
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
       0.506
Your Current Organism:
Symbiobacterium thermophilum
NCBI taxonomy Id: 292459
Other names: S. thermophilum IAM 14863, Symbiobacterium thermophilum IAM 14863, Symbiobacterium thermophilum str. IAM 14863, Symbiobacterium thermophilum strain IAM 14863
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