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ileS ileS proS proS cysS cysS leuS leuS glnS glnS metG metG argS argS aspS aspS thrS thrS pheS pheS pheT pheT tyrS tyrS asnS asnS serS serS gltX gltX hisS hisS alaS alaS lysS lysS fmt fmt trpS trpS glyS glyS glyQ glyQ selA selA lysU lysU valS valS
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.
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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:
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. (938 aa)
proSprolyl-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 [...] (572 aa)
cysScysteinyl-tRNA synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
leuSleucyl-tRNA synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
glnSglutamyl-tRNA synthetase; Function experimentally demonstrated in the studied species; enzyme. (554 aa)
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. (677 aa)
argSarginyl-tRNA synthetase; Function experimentally demonstrated in the studied species; enzyme. (577 aa)
aspSaspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (590 aa)
thrSthreonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). (642 aa)
pheSPhenylalanine tRNA synthetase, alpha subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (327 aa)
pheTPhenylalanine tRNA synthetase, beta subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
tyrStyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. (424 aa)
asnSAsparaginyl tRNA synthetase; Function experimentally demonstrated in the studied species; enzyme. (466 aa)
serSseryl-tRNA synthetase, also charges selenocysteinyl-tRNA with serine; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (430 aa)
gltXglutamyl-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). (471 aa)
hisSHistidyl tRNA synthetase; Function experimentally demonstrated in the studied species; enzyme. (424 aa)
alaSalanyl-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; Belongs to the class-II aminoacyl-tRNA synthetase family. (876 aa)
lysSLysine tRNA synthetase, constitutive; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
fmt10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. (315 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
glySGlycine tRNA synthetase, beta subunit; Function experimentally demonstrated in the studied species; enzyme. (689 aa)
glyQGlycine tRNA synthetase, alpha subunit; Function experimentally demonstrated in the studied species; enzyme. (303 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis; Belongs to the SelA family. (463 aa)
lysULysine tRNA synthetase, inducible; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
valSvalyl-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. (951 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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