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
glySPFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit; COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR006194:IPR002311:IPR008909:IPR015944; KEGG: cyh:Cyan8802_2388 glycyl-tRNA synthetase, beta subunit; 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. (710 aa)    
Predicted Functional Partners:
glyQ
PFAM: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit; COGs: COG0752 Glycyl-tRNA synthetase alpha subunit; InterPro IPR002310:IPR006194; KEGG: syp:SYNPCC7002_A0387 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.
 0.999
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.
  
  
 0.795
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.
 
  
 0.762
leuS
PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR015413:IPR013155:IPR001412; KEGG: cyt:cce_4237 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; tRNA synthetase class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
  
 0.747
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.
  
  
 0.718
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 [...]
   
  
 0.676
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.
  
  
 0.652
atpA
ATP synthase F1 subcomplex alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
    0.529
rplD
LSU ribosomal protein L4P; Forms part of the polypeptide exit tunnel.
   
    0.504
cysH
Phosphoadenylylsulfate reductase (thioredoxin); Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily.
       0.489
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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