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
alaSalanine--tRNA ligase; 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. (903 aa)    
Predicted Functional Partners:
AOS92777.1
Holliday junction DNA helicase RuvA; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF HJR family.
 
  
 0.979
pheT
phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
 
 0.964
AOS92025.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.955
APD84296.1
DUF3298 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.955
aspS
aspartate--tRNA ligase; 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.
  
 0.924
mltG
Aminodeoxychorismate lyase; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family.
  
    0.919
thrS
threonine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.894
leuS
leucine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.881
AOS92776.1
Shikimate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the shikimate dehydrogenase family.
       0.869
ileS
isoleucine--tRNA ligase; 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.
  
 
 0.850
Your Current Organism:
Mycobacterium chimaera
NCBI taxonomy Id: 222805
Other names: CCUG 50989, CIP 107892, DSM 44623, JCM 14737, M. chimaera, Mycobacterium chimaera Tortoli et al. 2004, NCTC 13781, personal::FI-01069, strain FI-01069
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.