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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
metGmethionyl-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. (512 aa)    
Predicted Functional Partners:
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302: IPR001412: IPR015413: IPR013155; KEGG: cth:Cthe_1237 leucyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); tRNA synthetase valyl/leucyl anticodon-binding; SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.982
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 [...]
  
 0.974
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.
 
0.972
AEE95728.1
Hydrolase, TatD family; COGs: COG0084 Mg-dependent DNase; InterPro IPR018228: IPR015991: IPR012278: IPR001130; KEGG: cdf:CD3539 putative deoxyribonuclease; PFAM: TatD-related deoxyribonuclease; SPTR: Putative uncharacterized protein; TIGRFAM: hydrolase, TatD family; PFAM: TatD related DNase; TIGRFAM: hydrolase, TatD family.
 
 0.969
lysS
COGs: COG1190 Lysyl-tRNA synthetase (class II); InterPro IPR018149: IPR006195: IPR002313: IPR004365: IPR 004364; KEGG: ate:Athe_0659 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.931
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
     
 0.924
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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.923
gltX-2
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).
 
 0.919
AEE95476.1
Homocysteine S-methyltransferase; COGs: COG0646 Methionine synthase I (cobalamin-dependent) methyltransferase domain; InterPro IPR003726: IPR003171; KEGG: csc:Csac_1165 bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; PFAM: homocysteine S-methyltransferase; methylenetetrahydrofolate reductase; SPTR: Methylenetetrahydrofolate reductase; PFAM: Methylenetetrahydrofolate reductase; Homocysteine S-methyltransferase.
  
 
 0.917
argS
COGs: COG0018 Arginyl-tRNA synthetase; InterPro IPR001412: IPR015945: IPR001278: IPR005148: IPR 008909; KEGG: amt:Amet_1714 arginyl-tRNA synthetase; PFAM: Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; DALR anticodon binding domain protein; PRIAM: Arginine--tRNA ligase; SPTR: Arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase.
  
 0.898
Your Current Organism:
Mahella australiensis
NCBI taxonomy Id: 697281
Other names: M. australiensis 50-1 BON, Mahella australiensis 50-1 BON, Mahella australiensis DSM 15567, Mahella australiensis str. 50-1 BON, Mahella australiensis strain 50-1 BON
Server load: low (24%) [HD]