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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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. (1057 aa)    
Predicted Functional Partners:
argS
Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.996
leuS
PFAM: tRNA synthetases class I (I, L, M and V); tRNA synthetases class I (M); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, archaeal and cytosolic family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR004493:IPR015413:IPR013155; KEGG: mem:Memar_2008 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, archaeal/eukaryotic cytosolic.
  
 0.995
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.
 
0.992
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).
 
 0.991
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; InterPro IPR002313:IPR004365:IPR004364; KEGG: mem:Memar_2341 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 0.985
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).
 
 0.977
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).
 
 0.975
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.
 
0.972
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.
 
 
 0.969
pheT
Phenylalanyl-tRNA synthetase beta chain; PFAM: tRNA synthetases class II core domain (F); tRNA synthetase B5 domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase beta chain; InterPro IPR004531:IPR005146:IPR005147; KEGG: mem:Memar_0644 phenylalanyl-tRNA synthetase subunit beta; PFAM: tRNA synthetase, B5; B3/B4 tRNA-binding domain; SPTR: Phenylalanyl-tRNA synthetase beta chain; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archae/euk cytosolic.
 
 
 0.948
Your Current Organism:
Methanofollis liminatans
NCBI taxonomy Id: 28892
Other names: M. liminatans DSM 4140, Methanofollis liminatans DSM 4140, Methanofollis liminatans GKZPZ, Methanofollis liminatans str. DSM 4140, Methanofollis liminatans strain DSM 4140, Methanogenium liminatans (DSM 4140), Methanogenium liminatans DSM 4140
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