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
glyQPFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; TIGRFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Glycyl-tRNA synthetase, class IIc, alpha subunit; KEGG: cni:Calni_0744 glycyl-tRNA synthetase alpha chain. (281 aa)    
Predicted Functional Partners:
glyS
TIGRFAM: Glycyl-tRNA synthetase, class IIc, beta subunit; HAMAP: Glycyl-tRNA synthetase beta subunit; KEGG: ddf:DEFDS_0236 glycyl-tRNA synthetase subunit beta.
 0.999
purM
TIGRFAM: Phosphoribosylformylglycinamidine cyclo-ligase; KEGG: dol:Dole_0293 phosphoribosylformylglycinamidine cyclo-ligase; PFAM: AIR synthase related protein, C-terminal; AIR synthase related protein.
  
    0.805
AEH23366.1
TIGRFAM: Translation elongation factor, selenocysteine-specific; Small GTP-binding protein; KEGG: dal:Dalk_1105 selenocysteine-specific translation elongation factor; PFAM: Protein synthesis factor, GTP-binding; Translation elongation factor EFTu/EF1A, domain 2; Translation elongation factor SelB, winged helix, type 2; Translation elongation factor SelB, winged helix, type 3.
       0.759
hisS
PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: has:Halsa_1638 histidyl-tRNA synthetase.
  
  
 0.717
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.
   
  
 0.677
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
    0.657
pheS
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain; KEGG: dte:Dester_0632 phenylalanyl-tRNA synthetase alpha chain; PFAM: Phenylalanyl-tRNA synthetase alpha chain; Phenylalanyl-tRNA synthetase, class II, N-terminal; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
   
  
 0.643
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.
  
  
 0.632
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.
   
  
 0.604
atpH
ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
   
    0.585
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.