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:
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Coexpression
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[Homology]
Score
alaSalanyl-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. (895 aa)    
Predicted Functional Partners:
AJI79050.1
RNAse H-fold protein YqgF; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF HJR family.
  
  
 0.927
pheT
phenylalanyl-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.
 
 
 0.885
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.838
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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
 
  
 0.821
mltG
Conserved hypothetical protein, YceG family; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
  
    0.817
aroE
PFAM: Shikimate dehydrogenase substrate binding domain; Shikimate / quinate 5-dehydrogenase; TIGRFAM: shikimate-5-dehydrogenase, fungal AROM-type; shikimate dehydrogenase.
  
    0.765
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.
  
 
 0.742
lepB
PFAM: Peptidase S24-like; Signal peptidase, peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family.
   
  
 0.736
lepB2
PFAM: Peptidase S24-like; Signal peptidase, peptidase S26; TIGRFAM: signal peptidase I, bacterial type; Belongs to the peptidase S26 family.
   
  
 0.736
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.
  
 
 0.711
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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.