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
Rmag_0682KEGG: tcx:Tcr_1759 thioredoxin, putative. (160 aa)    
Predicted Functional Partners:
msrA
Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
   
 0.860
Rmag_0098
PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein; KEGG: tcx:Tcr_1387 alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen.
  
 0.838
dsbD
Protein-disulfide reductase; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily.
 
 
 0.822
Rmag_0034
Cytochrome-c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.790
pdxB
4-phosphoerythronate dehydrogenase; Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate.
  
    0.774
ung
Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
       0.773
Rmag_0290
NADPH-glutathione reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: tcx:Tcr_0140 glutathione reductase.
   
 0.772
Rmag_0963
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: tcx:Tcr_1003 dihydrolipoamide dehydrogenase.
   
 0.772
Rmag_0310
PFAM: peptidylprolyl isomerase, FKBP-type; peptidyl-prolyl cis-trans isomerase, cyclophilin type; KEGG: tde:TDE2391 peptidyl-prolyl cis-trans isomerase.
   
 0.723
Rmag_0523
Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
  
 
 0.650
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
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