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Daci_0184 Daci_0184 gatB gatB gatA gatA gatC gatC argS argS fmt fmt glyQ glyQ glyS glyS Daci_1444 Daci_1444 metG metG serS serS Daci_2093 Daci_2093 valS valS glnS glnS cysS cysS selA selA alaS alaS pheT pheT pheS pheS thrS thrS gltX gltX hisS hisS lysS lysS ileS ileS trpS trpS Daci_5442 Daci_5442 aspS aspS proS proS tyrS tyrS leuS leuS
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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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empty nodes:
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
Your Input:
Daci_0184PFAM: Amidase; KEGG: rrs:RoseRS_3083 amidase. (480 aa)
gatBglutamyl-tRNA(Gln) amidotransferase, B subunit; 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. (481 aa)
gatAglutamyl-tRNA(Gln) amidotransferase, A subunit; 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). (498 aa)
gatCglutamyl-tRNA(Gln) amidotransferase, C subunit; 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. (99 aa)
argSKEGG: aav:Aave_0414 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. (565 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. (327 aa)
glyQKEGG: ajs:Ajs_0527 glycine--tRNA ligase; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit. (312 aa)
glySglycyl-tRNA synthetase, beta subunit; KEGG: aav:Aave_4177 glycine--tRNA ligase; TIGRFAM: glycyl-tRNA synthetase, beta subunit. (704 aa)
Daci_1444PFAM: Amidase; KEGG: bpe:BP1874 putative amidase. (456 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. (717 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). (438 aa)
Daci_2093PFAM: Amidase; KEGG: pfl:PFL_1361 amidase family protein. (477 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. (970 aa)
glnSKEGG: aav:Aave_2300 glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase class Ic. (628 aa)
cysSKEGG: ajs:Ajs_1623 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase class Ia DALR; tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
selAL-seryl-tRNA(Sec) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (484 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. (874 aa)
pheTKEGG: ajs:Ajs_2395 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (815 aa)
pheSTIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; aminoacyl tRNA synthetase class II domain protein; KEGG: aav:Aave_2855 phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (350 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). (643 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (468 aa)
hisSKEGG: ajs:Ajs_1171 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. (431 aa)
lysSTIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; KEGG: aav:Aave_1204 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (519 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. (951 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (430 aa)
Daci_5442PFAM: Amidase; KEGG: vei:Veis_0140 amidase. (493 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. (600 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 [...] (581 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. (410 aa)
leuSTIGRFAM: leucyl-tRNA synthetase; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (911 aa)
Your Current Organism:
Delftia acidovorans
NCBI taxonomy Id: 398578
Other names: D. acidovorans SPH-1, Delftia acidovorans SPH-1, Delftia acidovorans str. SPH-1, Delftia acidovorans strain SPH-1
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