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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
aspSaspartyl-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. (594 aa)    
Predicted Functional Partners:
gatB
glutamyl-tRNA(Gln) amidotransferase, B 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 GatB/GatE family. GatB subfamily.
 
 0.990
aspS-2
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 2 subfamily.
  
0.934
hisS
COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR015807:IPR004516:IPR006195:IPR002314:IPR 004154; KEGG: tde:TDE1442 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase.
  
  
 0.916
ADK81528.1
COGs: COG0519 GMP synthase PP-ATPase domain/subunit; InterProIPR000991:IPR001962:IPR001674:IPR017926:IPR 004739; KEGG: aae:aq_236 GMP synthase; PFAM: GMP synthase domain protein; glutamine amidotransferase class-I; asparagine synthase; SPTR: GMP synthase; TIGRFAM: GMP synthase, large subunit; GMP synthase, small subunit; PFAM: GMP synthase C terminal domain; Glutamine amidotransferase class-I; Asparagine synthase; TIGRFAM: GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit.
  
  
 0.906
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.
  
  
 0.898
alaS
alanyl-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.
  
 0.871
ADK81136.1
Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876; KEGG: tde:TDE1487 hypothetical protein; PFAM: protein of unknown function DUF28; SPTR: UPF0082 protein TDE_1487; PFAM: Domain of unknown function DUF28; TIGRFAM: conserved hypothetical protein TIGR01033.
  
 0.863
gatA
glutamyl-tRNA(Gln) amidotransferase, A subunit; 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).
 
 0.859
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.
  
 
 0.822
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR002300:IPR013155:IPR001412; KEGG: gwc:GWCH70_2764 leucyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ia; tRNA synthetase valyl/leucyl anticodon-binding; SPTR: Leucine--tRNA ligase; 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.
 
  
 0.809
Your Current Organism:
Sediminispirochaeta smaragdinae
NCBI taxonomy Id: 573413
Other names: S. smaragdinae DSM 11293, Sediminispirochaeta smaragdinae DSM 11293, Spirochaeta smaragdinae DSM 11293
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