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; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit; COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR002311:IPR015944; KEGG: tjr:TherJR_2403 glycyl-tRNA synthetase, beta subunit; PFAM: Glycyl-tRNA synthetase, class IIc, beta subunit, N-terminal; SPTR: Glycyl-tRNA synthetase beta subunit; TIGRFAM: Glycyl-tRNA synthetase, class IIc, beta subunit. (700 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; HAMAP: Glycyl-tRNA synthetase, class IIc, alpha subunit; InterPro IPR002310; KEGG: dbr:Deba_1978 glycyl-tRNA synthetase, subunit alpha; PFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; SPTR: Glycyl-tRNA synthetase alpha subunit; TIGRFAM: Glycyl-tRNA synthetase, class IIc, 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.
 
  
 0.799
leuS
PFAM: tRNA synthetases class I (I, L, M and V); tRNA synthetases class I (M); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302:IPR015413:IPR013155; KEGG: gtn:GTNG_2742 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial.
   
  
 0.793
AFM12824.1
tRNA synthetase class II (G H P and S); COGs: COG3705 ATP phosphoribosyltransferase involved in histidine biosynthesis; InterPro IPR002314; KEGG: bpr:GBP346_A2287 ATP phosphoribosyltransferase regulatory subunit; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; SPTR: Histidyl-tRNA synthetase 2.
       0.777
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.
  
  
 0.743
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 [...]
  
  
 0.720
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.
  
  
 0.678
aspS
aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.661
pheT
phenylalanyl-tRNA synthetase beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterPro IPR004532:IPR002547:IPR005146:IPR005147:IPR005121; KEGG: lil:LA_4035 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/B4 tRNA-binding domain; tRNA-binding region; tRNA synthetase, B5; Phenylalanyl-tRNA syntheta [...]
  
  
 0.647
thrS
Ser-tRNA(Thr) hydrolase, threonyl-tRNA synthetase; 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 synthetase; COGs: COG0441 Threonyl-tRNA synthetase; InterPro IPR012947:IPR002314:IPR004154:IPR002320; KEGG: tra:Trad_1638 threonyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Threonyl/alanyl tRNA synthetase, SAD; Anticodon-binding; SPTR: Threonyl-tRNA synthetase; TIGRFAM: Threonyl-tRNA synthetase, class IIa; Belongs to [...]
  
  
 0.608
Your Current Organism:
Turneriella parva
NCBI taxonomy Id: 869212
Other names: T. parva DSM 21527, Turneriella parva DSM 21527, Turneriella parva H, Turneriella parva NCTC 11395, Turneriella parva str. DSM 21527, Turneriella parva strain DSM 21527
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