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
glyQSGlycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (516 aa)    
Predicted Functional Partners:
leuS
Leucyl-tRNA synthetase catalyses the attachment of leucine to its cognate transfer RNA molecule in a highly specific two-step reaction. Belongs to the class I of the aminoacyl-tRNA synthetases. It is a monomer and adopts a Rossmann fold. Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.793
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.
 
 
 0.783
proB2
Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
 
 
    0.781
serS
Seryl-tRNA synthetase, class IIa; Seryl-tRNA synthetase is responsible for the attachment of serine to the 3' OH group of ribose of its cognate transfer RNA molecule (tRNA(Ser)) in a highly specific two-step reaction. It is a homodimer; Belongs to the class-IIa aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity.
   
  
 0.750
AsnS
AsparaginyltRNA synthetase catalyse the attachment of the aminoacid asparagine to the 3'-hydroxyl of the tRNA. It is an homodimer; Belongs to the class-II aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.738
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 1 subfamily.
 
  
 0.701
cdd
Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family.
  
    0.698
ppa
Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
  
  
 0.687
argS
Arginyl-tRNA synthetase also called Arginine-tRNA ligase is a monomeric enzyme that catalyzes the transfer of arginine to specific tRNA molecule as the first step in protein biosynthesis; Belongs to the class-I aminoacyl-tRNA synthetase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.668
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.
  
 
 0.665
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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