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
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[Homology]
Score
pheTphenylalanyl-tRNA synthetase beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (840 aa)    
Predicted Functional Partners:
pheS
phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
 
 0.999
leuS
PFAM: Leucyl-tRNA synthetase, Domain 2; tRNA synthetases class I (M); Anticodon-binding domain of tRNA; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.976
AJI78091.1
PFAM: IMP dehydrogenase / GMP reductase domain; TIGRFAM: IMP dehydrogenase family protein.
  
 
 0.965
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
  
 0.960
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.
  
 
 0.952
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.
  
  
 0.947
thrS
threonyl-tRNA synthetase; PFAM: Anticodon binding domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.945
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.
 
  
 0.934
pyrD1
Dihydroorotate oxidase A; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
  
  
 0.932
pyrD2
Dihydroorotate oxidase A; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
  
  
 0.932
Your Current Organism:
Corynebacterium singulare
NCBI taxonomy Id: 161899
Other names: C. singulare, CCUG 37330, CIP 105491, DSM 44357, IBS B52218, IFO 16162, JCM 10385, NBRC 16162
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