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
trxBThioredoxin-disulfide reductase; Identified by similarity to SP:P75531; match to protein family HMM PF00070; match to protein family HMM PF07992; match to protein family HMM TIGR01292. (315 aa)    
Predicted Functional Partners:
whiA
Conserved hypothetical protein; Involved in cell division and chromosome segregation.
  
  
 0.932
trx
Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
  
 
 0.917
csd
Aminotransferase, class V; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
  
 
  0.909
gatB
glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatB/GatE family. GatB subfamily.
  
  
 0.800
gatA
glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln) (By similarity).
  
  
 0.790
MG_098
glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, C subunit; MG098 is part of the GatABC aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase complex (MG098-MG099-MG100). The gatC region of this gene resides in the last 100 amino acids of a 500 amino acid protein. The amino terminal 400 amino acids contain 8 transmembrane regions; identified by similarity to EGAD:57274; match to protein family HMM PF02686; match to protein family HMM TIGR00135.
  
    0.787
MG_101
Conserved hypothetical protein; MG101 has some similarity to bacterial regulatory proteins of the gntR family; identified by similarity to EGAD:57268.
       0.781
secG
Hypothetical protein; Involved in protein export. Participates in an early event of protein translocation (By similarity); Belongs to the SecG family.
  
  
 0.772
dacB
Conserved hypothetical protein; Catalyzes the condensation of 2 ATP molecules into cyclic di- AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
  
    0.746
rnr
Ribonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
     
 0.719
Your Current Organism:
Mycoplasma genitalium
NCBI taxonomy Id: 243273
Other names: M. genitalium G37, Mycoplasma genitalium ATCC 33530, Mycoplasma genitalium G37, Mycoplasma genitalium str. G37, Mycoplasma genitalium strain G37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.