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leuS leuS proS proS CV_0748 CV_0748 lysS lysS metG metG thrS thrS pheS pheS pheT pheT serS serS alaS alaS glyQ glyQ glyS glyS trpS1 trpS1 glnS glnS cysS cysS gltX gltX argS argS valS valS fmt2 fmt2 tyrS tyrS hisS hisS ileS ileS trpS2 trpS2 aspS aspS fmt fmt gatB gatB gatA gatA gatC gatC
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:
leuSleucyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Blastx/COG0495; Belongs to the class-I aminoacyl-tRNA synthetase family. (872 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 [...] (568 aa)
CV_0748Probable transformylase; Identified by sequence similarity; putative; ORF located using Blastx/COG0223. (305 aa)
lysSlysyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG1190; Belongs to the class-II aminoacyl-tRNA synthetase family. (502 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. (689 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). (633 aa)
pheSphenylalanyl-tRNA synthetase alpha chain; Identified by sequence similarity; putative; ORF located using Blastx/COG0016; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (328 aa)
pheTphenylalanyl-tRNA synthetase beta chain; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0073; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (785 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). (427 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. (877 aa)
glyQglycyl-tRNA synthetase, alpha chain; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0752. (306 aa)
glySglycyl-tRNA synthetase, beta chain; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0751. (686 aa)
trpS1tryptophanyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Blastx; Belongs to the class-I aminoacyl-tRNA synthetase family. (398 aa)
glnSglutaminyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Blastx/COG0008. (560 aa)
cysScysteinyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Glimmer/Blastx/COG0215; Belongs to the class-I aminoacyl-tRNA synthetase family. (459 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. (461 aa)
argSarginyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0018. (572 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. (939 aa)
fmt2methionyl-tRNA formyltransferase; Identified by sequence similarity; putative; ORF located using Blastx/COG0223. (286 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)
hisShistidyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Blastx/COG0124. (423 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. (925 aa)
trpS2tryptophanyl-tRNA synthetase; Identified by sequence similarity; putative; ORF located using Blastx; Belongs to the class-I aminoacyl-tRNA synthetase family. (340 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. (597 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. (307 aa)
gatBGlu-tRNA(Gln) amidotransferase, subunit B; 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. (475 aa)
gatAGlu-tRNA(Gln) amidotransferase, subunit A; 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). (483 aa)
gatCGlu-tRNA(Gln) amidotransferase subunit C; 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)
Your Current Organism:
Chromobacterium violaceum
NCBI taxonomy Id: 243365
Other names: C. violaceum ATCC 12472, Chromobacterium violaceum ATCC 12472, Chromobacterium violaceum ATCC12472, Chromobacterium violaceum str. ATCC 12472
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