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
hisSTIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: txy:Thexy_1458 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding. (417 aa)    
Predicted Functional Partners:
aspS
aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.981
fmt
Methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
  
 0.796
hisI
TIGRFAM: Phosphoribosyl-ATP pyrophosphohydrolase; HAMAP: Histidine biosynthesis bifunctional protein hisIE; KEGG: txy:Thexy_0452 phosphoribosyl-ATP pyrophosphatase; PFAM: Phosphoribosyl-AMP cyclohydrolase; Phosphoribosyl-ATP pyrophosphohydrolase; In the N-terminal section; belongs to the PRA-CH family.
  
  
 0.788
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
  
 0.763
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).
  
 
 0.750
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.
 
 
 0.728
ribBA
GTP cyclohydrolase-2; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
     
 0.698
cysS
KEGG: txy:Thexy_0313 cysteinyl-tRNA synthetase; TIGRFAM: Cysteinyl-tRNA synthetase, class Ia; PFAM: Cysteinyl-tRNA synthetase, class Ia, N-terminal; Cysteinyl-tRNA synthetase, class Ia, DALR; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.694
metG
Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
 
 
 0.661
pheT
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: txy:Thexy_1029 phenylalanyl-tRNA synthetase beta chain.
 
  
 0.660
Your Current Organism:
Thermoanaerobacterium saccharolyticum
NCBI taxonomy Id: 1094508
Other names: T. saccharolyticum JW/SL-YS485, Thermoanaerobacterium saccharolyticum JW/SL-YS485, Thermoanaerobacterium saccharolyticum str. JW/SL-YS485, Thermoanaerobacterium saccharolyticum strain JW/SL-YS485, Thermoanaerobacterium sp. (strain JW/SL YS485)
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