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
cysScysteinyl-tRNA synthetase; Identified by match to protein family HMM TIGR00435; Belongs to the class-I aminoacyl-tRNA synthetase family. (458 aa)    
Predicted Functional Partners:
cysE
Serine O-acetyltransferase; Identified by match to protein family HMM TIGR01172.
 
  
 0.992
cysK
Cysteine synthase A; Identified by match to protein family HMM TIGR01136; match to protein family HMM TIGR01139; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 
 0.924
tpiA
Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.
 
 
  
 0.837
radA
DNA repair protein RadA; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
       0.794
ispD
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
       0.794
ispF
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
       0.794
serS
seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec).
 
 
 0.764
leuS
leucyl-tRNA synthetase; Identified by similarity to SP:P36430; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.746
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).
 
  
 0.681
pheT
phenylalanyl-tRNA synthetase, beta subunit; Identified by similarity to SP:P17922; match to protein family HMM PF01588; match to protein family HMM PF03483; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.643
Your Current Organism:
Dehalococcoides mccartyi
NCBI taxonomy Id: 243164
Other names: D. mccartyi 195, Dehalococcoides ethenogenes 195, Dehalococcoides mccartyi 195, Dehalococcoides mccartyi str. 195, Dehalococcoides mccartyi strain 195
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