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:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
glySCOGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR015944:IPR002311:IPR008909:IPR006194; KEGG: sat:SYN_01537 glycyl-tRNA synthetase subunit beta; PFAM: glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain protein; PRIAM: Glycine--tRNA ligase; SPTR: Glycyl-tRNA synthetase beta subunit; TIGRFAM: glycyl-tRNA synthetase, beta subunit; IMG reference gene:2505284773; PFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit. (692 aa)    
Predicted Functional Partners:
glyQ
COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR002310:IPR006194; KEGG: sat:SYN_01536 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit; PRIAM: Glycine--tRNA ligase; SPTR: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; IMG reference gene:2505284772; PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit.
 0.999
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.
 
  
 0.754
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.
  
  
 0.735
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR001412:IPR015413:IPR013155; KEGG: ddf:DEFDS_0790 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; IMG reference gene:2505285153; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
  
 0.694
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.
  
  
 0.680
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.
  
  
 0.663
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 [...]
   
  
 0.621
thrS
COGs: COG0441 Threonyl-tRNA synthetase; InterProIPR018158:IPR002320:IPR006195:IPR004095:IPR 012947:IPR002314:IPR004154; KEGG: dak:DaAHT2_1245 threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Threonyl/alanyl tRNA synthetase SAD; TGS domain-containing protein; Anticodon-binding domain protein; SPTR: Threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; IMG reference gene:2505284914; PFAM: Anticodon binding domain; Threonyl and Alanyl tRNA synthetase second additional domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: threonyl-tRNA synt [...]
  
  
 0.566
rplD
Ribosomal protein L4/L1e; Forms part of the polypeptide exit tunnel.
   
    0.555
rplA
Ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
   
    0.548
Your Current Organism:
Thermodesulfatator indicus
NCBI taxonomy Id: 667014
Other names: T. indicus DSM 15286, Thermodesulfatator indicus CIR29812, Thermodesulfatator indicus DSM 15286, Thermodesulfatator indicus str. DSM 15286, Thermodesulfatator indicus strain DSM 15286, Thermodesulfobacterium sp. CIR29812
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.