close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
APA96456.1Peroxiredoxin; Belongs to the AhpC/TSA family; Contains 1 thioredoxin domain; KEGG: asd:AS9A_3616 peroxiredoxin Q/BCP. (157 aa)    
Predicted Functional Partners:
APA96007.1
Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.
  
  
 0.692
APA96457.1
Hypothetical protein.
       0.679
APA98515.1
Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.
  
  
 0.671
dinG
Probable helicase involved in DNA repair and perhaps also replication; Belongs to the helicase family. DinG subfamily; Contains 1 helicase ATP-binding domain; KEGG: ncy:NOCYR_1167 ATP-dependent DNA helicase DinG.
      
 0.643
trxA-2
Protein disulfide-isomerase A4; Belongs to the protein disulfide isomerase family; Contains 3 thioredoxin domains.
  
 
 0.626
trxB-2
Component of the thioredoxin-thioredoxin reductase system which may be involved in biosynthesis of penicillins and cephalosporins and may be important in determining the thiol- disulfide redox balance. Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family; KEGG: nfa:nfa56620 thioredoxin reductase (NADPH).
 
  
 0.505
trxA
Thioredoxin-1; Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Stimulates complex formation between sigma factor SigR and its cognate anti- sigma factor RsrA probably by reducing RsrA; Belongs to the thioredoxin family; Contains 1 thioredoxin domain.
  
 
 0.489
APA96866.1
Hypothetical protein.
  
 
 0.456
APB01200.1
Uncharacterized protein; Contains 1 thioredoxin domain.
  
 
 0.452
APB00036.1
Peroxiredoxin; Together with AhpD, DltA and Lpd constitutes an NADH- dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. Does not however seem to play a role in detoxification of isoniazid (By similarity); Belongs to the AhpC/TSA family; Contains 1 thioredoxin domain; KEGG: mtu:Rv2428 peroxiredoxin (alkyl hydroperoxide reductase subunit C).
 
 
0.431
Your Current Organism:
Nocardia seriolae
NCBI taxonomy Id: 37332
Other names: ATCC 43993, CCUG 46828, CIP 104778, DSM 44129, IFO 15557, JCM 3360, N. seriolae, NBRC 15557
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.