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
leuSTIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (901 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.
  
0.991
pheT
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: ajs:Ajs_2395 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.980
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 1 subfamily.
 
0.963
lptE
Rare lipoprotein B; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane; Belongs to the LptE lipoprotein family.
  
  
 0.947
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.942
argS
TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: ajs:Ajs_0343 arginyl-tRNA synthetase.
 
 0.912
gluQ
Glutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
 
 0.900
AEB84135.1
SMART: DNA topoisomerase, type IA, DNA-binding; DNA topoisomerase, type IA, domain 2; Toprim domain; TIGRFAM: DNA topoisomerase III, bacterial-type; KEGG: mpt:Mpe_A2342 DNA topoisomerase III; PFAM: DNA topoisomerase, type IA, central; Toprim domain; DNA topoisomerase, type IA, zn finger.
   
 
 0.898
AEB84262.1
SMART: DNA topoisomerase, type IA, DNA-binding; DNA topoisomerase, type IA, domain 2; Toprim domain; TIGRFAM: DNA topoisomerase III, bacterial-type; KEGG: mpt:Mpe_A2342 DNA topoisomerase III; PFAM: DNA topoisomerase, type IA, central; Toprim domain; DNA topoisomerase, type IA, zn finger.
   
 
 0.898
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 [...]
 
 0.897
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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