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
asnSCOGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR006195:IPR002312:IPR016027:IPR004522:IPR 004365:IPR004364; KEGG: tai:Taci_1677 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: D1B7A0 Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. (434 aa)    
Predicted Functional Partners:
gatB
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 0.999
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.
  
 0.993
gatA
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
  
 0.988
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).
  
 0.973
Apau_1528
COGs: COG0749 DNA polymerase I - 3'-5' exonuclease and polymerase domains; InterProIPR002298:IPR020046:IPR020047:IPR001098:IPR 018320:IPR002421:IPR008918:IPR020045:IPR019760; KEGG: tai:Taci_1079 DNA polymerase I; PFAM: DNA-directed DNA polymerase; 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; PRIAM: DNA-directed DNA polymerase; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2; DNA-directed DNA polymerase; SPTR: D1B5M0 DNA polymerase I; TIGRFAM: DNA polymerase I; PFAM: 5'-3' exonuclease, C-terminal SAM fold; 5'-3' exonucleas [...]
  
 0.961
gatC
glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
   
 0.958
argS
COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR001278:IPR005148:IPR015945:IPR008909:IPR 009080:IPR014729:IPR001412; KEGG: tai:Taci_0648 arginyl-tRNA synthetase; PFAM: Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; DALR anticodon binding domain protein; PRIAM: Arginine--tRNA ligase; SPTR: D1B9D1 Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase.
   
 0.946
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterProIPR002302:IPR015945:IPR002300:IPR013155:IPR 009008:IPR009080:IPR014729:IPR001412; KEGG: tai:Taci_0698 leucyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ia; Arginyl-tRNA synthetase, class Ic, core; tRNA synthetase valyl/leucyl anticodon-binding; SPTR: D1B9I1 Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family.
  
 0.946
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.
  
 0.939
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
  
 
 0.909
Your Current Organism:
Aminomonas paucivorans
NCBI taxonomy Id: 584708
Other names: A. paucivorans DSM 12260, Aminomonas paucivorans DSM 12260, Aminomonas paucivorans str. DSM 12260, Aminomonas paucivorans strain DSM 12260
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