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
AHY46513.1Glutathione S-transferase, N-terminal domain; COG:COG0695: Glutaredoxin and related proteins [Posttranslational modification protein turnover chaperones]; Pfam:PF13417:Glutathione S-transferase, N-terminal domain; PRINTS:PR00160:Glutaredoxin subgroup; ProSitePatterns:PS00195:Glutaredoxin active site; ProSiteProfiles:PS51354:Glutaredoxin; SUPERFAMILY:SSF52833:Thioredoxin-like fold. (88 aa)    
Predicted Functional Partners:
AHY47573.1
Ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
  
 0.855
msrA
msrA: peptide-methionine (S)-S-oxide 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.
  
 
 0.617
AHY46980.1
Heavy metal translocating P-type ATPase; TIGRFAM:TIGR01525:Cation-transporting P-type ATPase, subfamily IB; COG:COG2217: Cation transport ATPase [Inorganic ion transport and metabolism]; Pfam:PF00122:P-type ATPase, A domain; PRINTS:PR00119:Cation-transporting P-type ATPase; ProSitePatterns:PS01047:Heavy-metal-associated, conserved site; ProSiteProfiles:PS50846:Heavy metal-associated domain, HMA; SUPERFAMILY:SSF56784:HAD-like domain; ATPase-IB_hvy.
   
 
 0.532
AHY45357.1
TIGRFAM:TIGR01292:Thioredoxin reductase; COG:COG0492: Thioredoxin reductase [Posttranslational modification protein turnover chaperones]; Pfam:PF07992:Pyridine nucleotide-disulphide oxidoreductase, FAD/NAD(P)-binding domain; PRINTS:PR00469:Pyridine nucleotide-disulphide oxidoreductase, class-II; ProSitePatterns:PS00573:Pyridine nucleotide-disulphide oxidoreductase, class-II, active site; SUPERFAMILY:SSF51905:No Description;KEGG: 00240; TRX_reduct.
   
 
 0.515
AHY47700.1
TIGRFAM:TIGR00049:FeS cluster insertion protein; COG:COG0316: Uncharacterized conserved protein [Function unknown]; Pfam:PF01521:FeS cluster biogenesis; ProSitePatterns:PS01152:FeS cluster insertion, C-terminal, conserved site; SUPERFAMILY:SSF89360:FeS cluster biogenesis; Belongs to the HesB/IscA family.
  
  
 0.472
AHY45802.1
TIGRFAM:TIGR01068:Thioredoxin; COG:COG3118: Thioredoxin domain-containing protein [Posttranslational modification protein turnover chaperones]; Pfam:PF00085:Thioredoxin domain; PIRSF:PIRSF000077:Thioredoxin; PRINTS:PR00421:Thioredoxin; ProSiteProfiles:PS51352:Thioredoxin-like fold; SUPERFAMILY:SSF52833:Thioredoxin-like fold; Belongs to the thioredoxin family.
  
  
 0.467
sodA
Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.
  
  
 0.465
Your Current Organism:
Rubrobacter radiotolerans
NCBI taxonomy Id: 42256
Other names: ATCC 51242, Arthrobacter radiotolerans, CIP 106991, DSM 46359, DSM 5868, IAM 12072, IFO 14777, JCM 2153, NBRC 14777, R. radiotolerans, strain P-1
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