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ileS ileS proS proS cysS cysS leuS leuS glnS glnS serS serS asnS asnS thrS thrS pheS pheS pheT pheT tyrS tyrS aspS aspS argS argS metG metG gltX gltX hisS hisS alaS alaS lysS lysS fmt fmt trpS trpS glyS glyS glyQ glyQ selA selA STM4446 STM4446 valS valS trpS2 trpS2
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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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colored nodes:
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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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
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textmining
co-expression
protein homology
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ileSIsoleucine 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. (944 aa)
proSProline 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 de [...] (572 aa)
cysSSimilar to E. coli cysteine tRNA synthetase (AAC73628.1); Blastp hit to AAC73628.1 (461 aa), 94% identity in aa 1 - 461; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
leuSSimilar to E. coli leucine tRNA synthetase (AAC73743.1); Blastp hit to AAC73743.1 (860 aa), 95% identity in aa 1 - 860; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
glnSSimilar to E. coli glutamine tRNA synthetase (AAC73774.1); Blastp hit to AAC73774.1 (554 aa), 96% identity in aa 1 - 554. (555 aa)
serSSerine tRNA synthetase; 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)
asnSSimilar to E. coli asparagine tRNA synthetase (AAC74016.1); Blastp hit to AAC74016.1 (466 aa), 94% identity in aa 1 - 466. (466 aa)
thrSThreonine 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)
pheSSimilar to E. coli phenylalanine tRNA synthetase, alpha-subunit (AAC74784.1); Blastp hit to AAC74784.1 (327 aa), 97% identity in aa 1 - 327. (327 aa)
pheTPhenylalanine tRNA synthetase, beta-subunit; phenylalanyl-tRNA synthetase beta chain. (SW:SYFB_SALTY); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
tyrSTyrosine 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)
aspSAspartate 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)
argSarginyl-tRNA synthetase. (SW:SYR_SALTY). (577 aa)
metGMethionine 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)
gltXGlutamate tRNA synthetase, catalytic subunit; 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. (SW:SYH_SALTY). (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)
lysSSimilar to E. coli lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA (AAC75928.1); Blastp hit to AAC75928.1 (505 aa), 95% identity in aa 1 - 505; 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. (315 aa)
trpSTryptophan tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
glySSimilar to E. coli glycine tRNA synthetase, beta subunit (AAC76583.1); Blastp hit to AAC76583.1 (689 aa), 92% identity in aa 1 - 689. (689 aa)
glyQSimilar to E. coli glycine tRNA synthetase, alpha subunit (AAC76584.1); Blastp hit to AAC76584.1 (303 aa), 99% identity in aa 1 - 303. (303 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis; Belongs to the SelA family. (463 aa)
STM4446Putative selenocysteine synthase; [L-seryl-tRNA(Ser) selenium transferase]. (372 aa)
valSValine 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)
trpS2Putative tryptophanyl-tRNA synthetase; Similar to E. coli tryptophan tRNA synthetase (AAC76409.1); Blastp hit to AAC76409.1 (334 aa), 26% identity in aa 2 - 329; Belongs to the class-I aminoacyl-tRNA synthetase family. (337 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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