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
hisShistidyl-tRNA synthetase; Similar to Mycobacterium tuberculosis histidyl-tRNA synthetase HisS or Rv2580c or MT2657 or MTCY227.21 SWALL:SYH_MYCTU (SWALL:Q50641) (423 aa) fasta scores: E(): 1.6e-112, 70.4% id in 419 aa, and to Bacillus subtilis histidyl-tRNA synthetase HisS SWALL:SYH_BACSU (SWALL:O32039) (424 aa) fasta scores: E(): 3.8e-61, 45.63% id in 412 aa. (423 aa)    
Predicted Functional Partners:
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.
  
  
 0.839
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
  
 
 0.798
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
 
 
 0.780
hisG
ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
  
 
 0.778
DIP1361
Conserved hypothetical protein; Similar to Streptomyces coelicolor possible hydrolase SC9C5.33c SWALL:Q9KXP1 (EMBL:AL357523) (235 aa) fasta scores: E(): 6.5e-25, 40.35% id in 223 aa, and to Escherichia coli hypothetical protein YcbL or B0927 SWALL:YCBL_ECOLI (SWALL:P75849) (215 aa) fasta scores: E(): 3.7e-23, 36.79% id in 212 aa.
  
    0.764
tpx
Thiol peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Tpx subfamily.
       0.761
pheT
Similar to Mycobacterium tuberculosis phenylalanyl-tRNA synthetase beta chain PheT or Rv1650 or MT1688 or MTCY06H11.15 SWALL:SYFB_MYCTU (SWALL:P94985) (831 aa) fasta scores: E(): 4.2e-156, 49.64% id in 844 aa, and to Bacillus subtilis phenylalanyl-tRNA synthetase beta chain PheT SWALL:SYFB_BACSU (SWALL:P17922) (804 aa) fasta scores: E(): 1.8e-53, 30.69% id in 847 aa.
  
  
 0.674
argS
arginyl-tRNA synthetase; Similar to Mycobacterium tuberculosis arginyl-tRNA synthetase ArgS or Rv1292 or MT1331 or MTCY373.12 SW:SYR_MYCTU (Q10609) (550 aa) fasta scores: E(): 4.5e-144, 65.63% id in 550 aa, and to Bacillus subtilis arginyl-tRNA synthetase ArgS SW:SYR_BACSU (P46906) (556 aa) fasta scores: E(): 1.7e-82, 42.75% id in 545 aa.
  
  
 0.672
DIP1363
Putative isomerase; Similar to Mycobacterium tuberculosis probable peptidyl-prolyl cis-trans isomerase B PpiB or Ppi or Rv2582 or MT2659 or MTCY227.19c SWALL:PPIB_MYCTU (SWALL:Q50639) (308 aa) fasta scores: E(): 5.5e-37, 46.23% id in 292 aa, and to Streptomyces coelicolor putative peptidyl-prolyl cis-trans isomerase SC9C5.34 SWALL:Q9KXP0 (EMBL:AL357523) (277 aa) fasta scores: E(): 3.5e-26, 37.5% id in 288 aa.
       0.635
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
 
 0.628
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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