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
hisSKEGG: sen:SACE_2032 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. (420 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.
 
  
 0.978
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.
  
 
 0.895
valS
aminoacyl-tRNA synthetase class Ia; 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.
  
 
 0.808
Gobs_3165
PFAM: aldo/keto reductase; KEGG: sgr:SGR_6491 putative oxidoreductase.
       0.806
thrS
TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: sen:SACE_2004 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.801
argS
KEGG: stp:Strop_3653 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase.
 
  
 0.772
pheT
KEGG: stp:Strop_1887 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit.
  
  
 0.753
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.737
ispG
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.
  
  
 0.734
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.
  
 
 0.697
Your Current Organism:
Geodermatophilus obscurus
NCBI taxonomy Id: 526225
Other names: G. obscurus DSM 43160, Geodermatophilus obscurus ATCC 25078, Geodermatophilus obscurus DSM 43160, Geodermatophilus obscurus IFO 13315, Geodermatophilus obscurus JCM 3152, Geodermatophilus obscurus NBRC 13315, Geodermatophilus obscurus NRRL B-3577, Geodermatophilus obscurus VKM Ac-658, Geodermatophilus obscurus str. DSM 43160, Geodermatophilus obscurus strain DSM 43160
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