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; Derived by automated computational analysis using gene prediction method: Protein Homology. (460 aa)    
Predicted Functional Partners:
cysE
Catalyzes the O-acetylation of serine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.992
KOH21423.1
Cysteine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.929
rlmB
23S rRNA methyltransferase; Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
 
 
 0.888
KOH19431.1
Triosephosphate isomerase; Reversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.844
rnc
Ribonuclease III; Cytoplasmic enzyme involved in processing rRNA and some mRNAs; substrates typically have dsRNA regions; forms a homodimer; have N-terminal nuclease and C-terminal RNA-binding domains; requires magnesium as preferred ion for activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.809
thrS
threonine--tRNA ligase; Catalyzes a two-step reaction, first charging a threonine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; catalyzes the formation of threonyl-tRNA(Thr) from threonine and tRNA(Thr); Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.786
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
  
 0.778
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).
 
 
 0.760
truA
tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
  
  
 0.743
leuS
leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase; Derived by automated computational [...]
  
 
 0.738
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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