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gatA1 gatA1 pheS pheS pheT pheT trpS trpS fmt fmt hisS hisS ileS ileS glyQ glyQ glyS glyS cysS cysS aspS aspS proS proS gatC gatC gatA2 gatA2 gatB gatB valS valS argS argS serS serS metS metS thrS thrS tyrS tyrS alaS2 alaS2 trpS-2 trpS-2 Arad_3833 Arad_3833 gltX1 gltX1 lysS lysS leuS leuS Arad_7518 Arad_7518 gatA1-2 gatA1-2 gatA1-3 gatA1-3 metS-2 metS-2
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:
gatA1glutamyl-tRNA amidotransferase subunit A protein. (463 aa)
pheSphenylalanyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (360 aa)
pheTphenylalanyl-tRNA synthetase; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (807 aa)
trpStryptophanyl-tRNA synthetase protein; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (354 aa)
fmtmethionyl-tRNA 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)
hisShistidyl-tRNA synthetase protein. (504 aa)
ileSisoleucyl-tRNA synthetase protein; 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). (960 aa)
glyQglycyl-tRNA synthetase. (319 aa)
glySglycyl-tRNA synthetase. (742 aa)
cysScysteinyl-tRNA synthetase protein; Belongs to the class-I aminoacyl-tRNA synthetase family. (463 aa)
aspSaspartyl-tRNA synthetase protein; 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. (596 aa)
proSprolyl-tRNA synthetase protein; 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); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily. (475 aa)
gatCglutamyl-tRNA amidotransferase subunit C protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. (95 aa)
gatA2glutamyl-tRNA amidotransferase subunit A protein; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (490 aa)
gatBglutamyl-tRNA amidotransferase subunit B protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (474 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. (947 aa)
argSarginyl-tRNA synthetase. (586 aa)
serSseryl-tRNA synthetase (serine-tRNA ligase) protein; 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). (427 aa)
metSmethionyl-tRNA synthetase protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. (517 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). (662 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. (410 aa)
alaS2alanyl-tRNA synthetase protein; 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. (886 aa)
trpS-2tryptophanyl-tRNA synthetase protein; Belongs to the class-I aminoacyl-tRNA synthetase family. (339 aa)
Arad_3833tRNA synthetase class II (G H P and S). (294 aa)
gltX1glutamyl-tRNA synthetase protein; 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. (485 aa)
lysSlysyl-tRNA synthetase protein; Belongs to the class-II aminoacyl-tRNA synthetase family. (498 aa)
leuSleucyl-tRNA synthetase protein; Belongs to the class-I aminoacyl-tRNA synthetase family. (876 aa)
Arad_7518Amidase family protein; Belongs to the amidase family. (456 aa)
gatA1-2glutamyl-tRNA amidotransferase subunit A protein. (476 aa)
gatA1-3glutamyl-tRNA amidotransferase subunit A protein. (475 aa)
metS-2methionyl-tRNA synthetase protein; Belongs to the class-I aminoacyl-tRNA synthetase family. (521 aa)
Your Current Organism:
Agrobacterium radiobacter
NCBI taxonomy Id: 311403
Other names: A. radiobacter K84, Agrobacterium radiobacter K84, Agrobacterium radiobacter str. K84, Agrobacterium radiobacter strain K84, Agrobacterium rhizogenes K84, Agrobacterium tumefaciens K84, Rhizobium radiobacter K84
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