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
ADI31489.1PFAM: t-RNA-binding domain protein; KEGG: nam:NAMH_1243 methionyl-tRNA synthetase. (112 aa)    
Predicted Functional Partners:
ADI31687.1
Transcriptional regulator, MarR family; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; KEGG: hypothetical protein; K01889 phenylalanyl-tRNA synthetase alpha chain; PFAM: phenylalanyl-tRNA synthetase class IIc; regulatory protein DeoR; regulatory protein MarR.
  
 
 0.999
ADI32039.1
KEGG: sat:SYN_00558 methionyl-tRNA synthetase; TIGRFAM: methionyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.956
ADI31490.1
PFAM: Thiamine biosynthesis protein-like; Queuosine synthesis-like; KEGG: bpn:BPEN_246 thiamine biosynthesis protein ThiI.
  
  
 0.692
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.673
leuS
leucyl-tRNA synthetase; KEGG: similar to CG33123 CG33123-PA; K01869 leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.646
tyrS
tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 4 subfamily.
  
  
 0.634
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
  
  
 0.582
ADI32750.1
DNA-directed RNA polymerase subunit B; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
  
 0.579
thrS
KEGG: dvl:Dvul_0707 threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; PFAM: Threonyl-tRNA synthetase editing domain protein; Anticodon-binding domain protein; tRNA synthetase class II (G H P and S); Belongs to the class-II aminoacyl-tRNA synthetase family.
  
  
 0.577
ADI31695.1
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: similar to Probable phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain) (PheRS); K01890 phenylalanyl-tRNA synthetase beta chain; PFAM: tRNA synthetase B5; B3/4 domain protein.
 
  
 0.541
Your Current Organism:
Staphylothermus hellenicus
NCBI taxonomy Id: 591019
Other names: S. hellenicus DSM 12710, Staphylothermus hellenicus BK20S6-10-b1, Staphylothermus hellenicus DSM 12710, Staphylothermus hellenicus P8, Staphylothermus hellenicus str. DSM 12710, Staphylothermus hellenicus strain DSM 12710, Staphylothermus sp. P8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.