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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
plu4265tRNA-synt_1g domain-containing protein; Unnamed protein product; Similar to methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (497 aa)    
Predicted Functional Partners:
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.
 
 
0.937
metE
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
     
 0.906
plu1413
Formyl_trans_N domain-containing protein; Unnamed protein product; Some similarities with methionyl-tRNA formyltransferase.
     
 0.904
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.
     
 0.904
plu0523
Unnamed protein product; Similar to cystathionine gamma-lyase.
   
 
 0.903
plu4830
ANK_REP_REGION domain-containing protein; Truncated gene. Similar to the N-terminal region of transposase, IS30 family.
     
 0.902
leuS
leucine-tRNA synthetase (leucine--tRNA ligase) (LEURS); Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.866
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
  
 0.827
argS
Arginyl-tRNA synthetase (Arginine-tRNA ligase).
 
 0.827
ileS
Isoleucine 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 1 subfamily.
  
 0.805
Your Current Organism:
Photorhabdus laumondii
NCBI taxonomy Id: 243265
Other names: P. laumondii subsp. laumondii TTO1, Photorhabdus laumondii subsp. laumondii TTO1, Photorhabdus luminescens subsp. laumondii TTO1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.