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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
thrSthreonyl-tRNA synthetase; Identified by similarity to SP:P00955; match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM PF07973; match to protein family HMM TIGR00418; Belongs to the class-II aminoacyl-tRNA synthetase family. (615 aa)    
Predicted Functional Partners:
infC
Translation initiation factor IF-3; Identified by match to protein family HMM PF00707; match to protein family HMM PF05198; match to protein family HMM TIGR00168; Belongs to the IF-3 family.
  
 0.982
rplT
Ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
 
 
 0.946
pheT
phenylalanyl-tRNA synthetase, beta subunit; Identified by similarity to SP:P07395; match to protein family HMM PF01588; match to protein family HMM PF03147; match to protein family HMM PF03483; match to protein family HMM PF03484; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
 
 0.920
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
  
 
 0.867
rsfS
Iojap-related protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
  
 0.865
leuS
leucyl-tRNA synthetase; Identified by similarity to SP:P56457; match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.853
rpmA
Ribosomal protein L27; Identified by match to protein family HMM PF01016; match to protein family HMM TIGR00062; Belongs to the bacterial ribosomal protein bL27 family.
  
 
 0.841
rpsA
Ribosomal protein S1; Identified by similarity to SP:P02349; match to protein family HMM PF00575.
  
   0.806
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.
  
 
 0.800
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.
 
 
 0.796
Your Current Organism:
Anaplasma phagocytophilum
NCBI taxonomy Id: 212042
Other names: A. phagocytophilum str. HZ, Anaplasma phagocytophilum HZ, Anaplasma phagocytophilum str. HZ
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.