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 2 subfamily. (1060 aa)    
Predicted Functional Partners:
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.
 
0.999
argS
KEGG: mth:MTH1447 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.983
gltX
glutamyl-tRNA synthetase; 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).
 
 0.982
pheT
Phenylalanyl-tRNA synthetase beta chain; SMART: B3/B4 tRNA-binding domain; tRNA synthetase, B5; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archae/euk cytosolic; KEGG: mmg:MTBMA_c11660 phenylalanyl-tRNA synthetase, beta chain; HAMAP: Phenylalanyl-tRNA synthetase beta chain 2, bacterial/archaeal; PFAM: tRNA synthetase, B5; B3/B4 tRNA-binding domain.
  
 
 0.965
leuS
TIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic; KEGG: mst:Msp_0171 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
0.963
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).
 
 0.954
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 2 subfamily.
 
 
0.953
purL
Phosphoribosylformylglycinamidine synthase 2; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist i [...]
  
  
 0.950
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).
 
 0.936
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.
 
 
 0.925
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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