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
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Textmining
[Homology]
Score
hisShistidyl-tRNA synthetase; histidine--tRNA ligase; HisRS; HisS; COG family: histidyl-tRNA synthetase; PFAM_ID: tRNA-synt_2b; PFAM_ID: HGTP_anticodon. (466 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.
 
  
 0.971
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.
 
 
 0.882
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).
  
 
 0.786
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.
  
 
 0.773
argS
arginyl-tRNA synthetase; arginine--tRNA ligase; ArgRS; ArgS; COG family: arginyl-tRNA synthetase; PFAM_ID: tRNA-synt_1d.
  
  
 0.728
BL0016
Narrowly conserved hypothetical protein.
  
    0.721
pheT
phenylalanine--tRNA ligase beta chain; PheRS; PheT; COG family: emap domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.718
guaA
GMP synthase glutamine amidotransferase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.678
aroB
Bifunctional shikimate kinase-3-dehydroquinate synthase protein; AroB; COG family: 3-dehydroquinate synthetase; PFAM_ID: SKI; PFAM_ID: DHQ_synthase; In the N-terminal section; belongs to the shikimate kinase family.
  
  
 0.634
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.
  
 
 0.623
Your Current Organism:
Bifidobacterium longum
NCBI taxonomy Id: 206672
Other names: B. longum NCC2705, Bifidobacterium longum NCC2705, Bifidobacterium longum str. NCC2705
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.