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
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[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. (656 aa)    
Predicted Functional Partners:
leuS
COGs: COG0495 Leucyl-tRNA synthetase; InterProIPR015945:IPR013155:IPR001412:IPR014729:IPR 002302:IPR009008:IPR009080; KEGG: glo:Glov_2116 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; Arginyl-tRNA synthetase, class Ic, core; SPTR: B3E3L3 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.
 
0.995
pheS
COGs: COG0016 Phenylalanyl-tRNA synthetase alpha subunit; InterProIPR004529:IPR006195:IPR010978:IPR004188:IPR 002319; KEGG: sfu:Sfum_0428 phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; aminoacyl tRNA synthetase class II domain protein; SPTR: C8QYJ1 Phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA syn [...]
  
 
 0.994
argS
COGs: COG0018 Arginyl-tRNA synthetase; InterProIPR005148:IPR015945:IPR008909:IPR014729:IPR 009080:IPR001412:IPR001278; KEGG: pca:Pcar_0742 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: Q3A6K6 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.
  
 0.981
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.
  
 0.976
asnS
COGs: COG0017 Aspartyl/asparaginyl-tRNA synthetase; InterProIPR004365:IPR004364:IPR016027:IPR012340:IPR 002312:IPR004522:IPR006195; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; PRIAM: Asparagine--tRNA ligase; SPTR: C5TZ48 Asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase.
  
 0.976
glnS
COGs: COG0008 Glutamyl- and glutaminyl-tRNA synthetase; InterProIPR004514:IPR011035:IPR020058:IPR020059:IPR 020060:IPR020061:IPR020056:IPR001412; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; SPTR: B8DLQ7 Glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; TIGRFAM: glutaminyl-tRNA synthetase.
  
 0.976
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.
 
 0.975
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 [...]
  
 0.973
lysS
COGs: COG1190 Lysyl-tRNA synthetase (class II); InterProIPR018149:IPR004365:IPR004364:IPR016027:IPR 006195:IPR012340:IPR002313; KEGG: drt:Dret_2234 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: C8X521 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.
 
 0.946
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.
  
 
 0.938
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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