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
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: pmt:PMT0283 glycyl-tRNA synthetase subunit alpha. (297 aa)    
Predicted Functional Partners:
glyS
TIGRFAM: Glycyl-tRNA synthetase, class IIc, beta subunit; KEGG: pmf:P9303_16721 glycyl-tRNA synthetase beta subunit.
 0.999
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
    0.672
hisZ
ATP phosphoribosyltransferase regulatory subunit; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
  
  
 0.643
hisS
PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain; Anticodon-binding; TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: pmf:P9303_25401 histidyl-tRNA synthetase.
  
  
 0.643
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.
   
    0.630
pheS
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Phenylalanyl-tRNA synthetase alpha chain 1, bacterial; KEGG: pmf:P9303_19341 phenylalanyl-tRNA synthetase subunit alpha; PFAM: Phenylalanyl-tRNA synthetase; Phenylalanyl-tRNA synthetase, class II, N-terminal; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
   
  
 0.597
pheT
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: pmf:P9303_14801 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial.
   
  
 0.584
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.
  
  
 0.534
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.
   
  
 0.520
trmD
tRNA (guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
  
    0.488
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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