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
ileSIsoleucyl-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. (955 aa)    
Predicted Functional Partners:
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 [...]
  
 0.989
pheT
phenylalanyl-tRNA synthetase beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterProIPR002547:IPR005146:IPR005147:IPR005121:IPR 004532; KEGG: npu:Npun_F1087 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/B4 tRNA-binding domain; tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SMART: B3/B4 tRNA-bindi [...]
  
 
 0.987
leuS
PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR015413:IPR013155:IPR002302; KEGG: cyj:Cyan7822_5283 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); PRIAM: Valine--tRNA ligase., Leucine--tRNA ligase; SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial.
 
0.941
gltX
glutamyl-tRNA synthetase, glutamate--tRNA(Gln) ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.925
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.907
AFZ12661.1
KEGG: ava:Ava_0784 hypothetical protein; SPTR: Alr4119 protein.
  
 0.889
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.
 
 
0.860
argS
arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR008909:IPR005148:IPR015945; KEGG: npu:Npun_R4006 arginyl-tRNA synthetase; PFAM: Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; DALR anticodon binding; PRIAM: Arginine--tRNA ligase; SMART: DALR anticodon binding; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic.
  
 0.859
AFZ12975.1
DALR anticodon binding domain protein; PFAM: Arginyl tRNA synthetase N terminal domain; InterPro IPR008909; KEGG: cyc:PCC7424_0116 DALR anticodon binding domain protein; PFAM: DALR anticodon binding; SMART: DALR anticodon binding; SPTR: Putative Arginyl tRNA synthetase, anticodon binding.
  
 0.854
lysS
PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; COGs: COG1190 Lysyl-tRNA synthetase (class II); HAMAP: Lysyl-tRNA synthetase, class II; InterPro IPR002313:IPR004365:IPR004364; KEGG: ter:Tery_2366 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; PRIAM: Lysine--tRNA ligase; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 0.840
Your Current Organism:
Crinalium epipsammum
NCBI taxonomy Id: 1173022
Other names: C. epipsammum PCC 9333, Crinalium epipsammum PCC 9333, Crinalium sp. PCC 9333
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.