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lpg0607 lpg0607 serS serS tyrS tyrS metG_1 metG_1 hisS hisS aspS aspS thrS thrS trpS trpS leuS leuS cysS cysS glnS glnS ileS ileS valS valS proS proS alaS alaS alaS-2 alaS-2 glyS glyS glyQ glyQ gltX gltX argS argS asnS asnS csaA csaA pheS pheS pheT pheT lysU lysU
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:
lpg0607Lysyl tRNA synthetase. (317 aa)
serSSeryl 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). (426 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 2 subfamily. (423 aa)
metG_1Methionyl 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. (693 aa)
hisSHistidyl tRNA synthetase. (426 aa)
aspSAspartyl 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (593 aa)
thrSThreonyl tRNA synthase; 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). (646 aa)
trpSTryptophanyl tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (405 aa)
leuSLeucyl tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (823 aa)
cysScysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (456 aa)
glnSglutaminyl-tRNA synthetase. (551 aa)
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. (931 aa)
valSValyl tRNA synthase; 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. (921 aa)
proSprolyl-tRNA synthase; 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 deacy [...] (589 aa)
alaSAlanyl tRNA synthetase. (257 aa)
alaS-2Alanyl 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. (860 aa)
glySGlycyl tRNA synthetase, beta subunit. (688 aa)
glyQGlycyl tRNA synthetase, alpha subunit. (307 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (494 aa)
argSArginyl tRNA synthetase. (589 aa)
asnSAsparaginyl tRNA synthetase. (478 aa)
csaAChaperonin CsaA. (111 aa)
pheSPhenylalanyl tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (342 aa)
pheTPhenylalanyl tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (793 aa)
lysULysine tRNA synthetase, heat inducible; Belongs to the class-II aminoacyl-tRNA synthetase family. (496 aa)
Your Current Organism:
Legionella pneumophila Philadelphia
NCBI taxonomy Id: 272624
Other names: L. pneumophila subsp. pneumophila str. Philadelphia 1, Legionella pneumophila subsp. pneumophila str. Philadelphia 1, Legionella pneumophila subsp. pneumophila str. Philadelphia-1, Legionella pneumophila subsp. pneumophila strain Philadelphia 1
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