STRINGSTRING
aspS aspS trpS trpS valS valS lysS lysS tyrS tyrS ileS ileS glnS glnS asnS asnS metG metG hisS hisS cysS cysS alaS alaS leuS leuS proS proS glyS glyS glyQ glyQ serS serS thrS thrS pheS pheS pheT pheT argS argS gltX gltX
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
Your Input:
aspSAspartate--tRNA ligase; 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. (560 aa)
trpSTryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
valSValine--tRNA ligase; 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. (881 aa)
lysSLysine--tRNA ligase; Protein synthesis; Belongs to the class-II aminoacyl-tRNA synthetase family. (493 aa)
tyrSTyrosine--tRNA ligase; 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. (496 aa)
ileSIsoleucine--tRNA ligase; 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. (940 aa)
glnSGlutamine--tRNA ligase; Protein synthesis. (549 aa)
asnSAsparagine--tRNA ligase; Protein synthesis. (466 aa)
metGMethionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (550 aa)
hisSHistidine--tRNA ligase; Protein synthesis. (432 aa)
cysSCysteine--tRNA ligase; Protein synthesis; Belongs to the class-I aminoacyl-tRNA synthetase family. (463 aa)
alaSAlanine--tRNA ligase; 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. (873 aa)
leuSLeucine--tRNA ligase; Protein synthesis; Belongs to the class-I aminoacyl-tRNA synthetase family. (864 aa)
proSProline--tRNA ligase; 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 [...] (561 aa)
glySGlycine--tRNA ligase beta subunit; Protein synthesis. (694 aa)
glyQGlycine--tRNA ligase alpha subunit; Protein synthesis. (302 aa)
serSSerine--tRNA ligase; 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). (429 aa)
thrSThreonine--tRNA ligase; 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). (636 aa)
pheSPhenylalanine--tRNA ligase alpha subunit; Protein synthesis; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (333 aa)
pheTPhenylalanine--tRNA ligase beta subunit; Protein synthesis; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (803 aa)
argSArginine--tRNA ligase; Protein synthesis. (576 aa)
gltXGlutamate--tRNA ligase; 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. (473 aa)
Your Current Organism:
Wigglesworthia glossinidia endosymbiont of Glossina brevipalpis
NCBI taxonomy Id: 36870
Other names: Glossina brevipalpis P-endosymbiont, W. glossinidia endosymbiont of Glossina brevipalpis, Wigglesworthia brevipalpis, Wigglesworthia glossinidia brevipalpis
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