STRINGSTRING
serS serS gltX gltX alaS alaS trpS trpS fmt fmt hisS hisS argS argS tyrS tyrS gltX-2 gltX-2 ileS ileS gatA gatA glyS glyS valS valS lysS lysS pheS pheS pheT pheT cysS cysS aspS aspS proS proS gatB gatB gatC gatC metG metG selA selA thrS thrS glyQ glyQ leuS leuS NAMH_1683 NAMH_1683
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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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
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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). (416 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)
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. (853 aa)
trpStryptophanyl-tRNA synthetase; Identified by match to protein family HMM PF00579; match to protein family HMM TIGR00233; Belongs to the class-I aminoacyl-tRNA synthetase family. (323 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. (294 aa)
hisShistidyl-tRNA synthetase; Identified by match to protein family HMM PF00587; match to protein family HMM TIGR00442. (386 aa)
argSarginyl-tRNA synthetase; Identified by match to protein family HMM PF00750; match to protein family HMM PF01406; match to protein family HMM PF03485; match to protein family HMM PF05746; match to protein family HMM PF09334; match to protein family HMM TIGR00456. (532 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. (417 aa)
gltX-2glutamyl-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. (434 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. (911 aa)
gatAglutamyl-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). (451 aa)
glySglycyl-tRNA synthetase, beta subunit; Identified by match to protein family HMM PF02092; match to protein family HMM PF05746; match to protein family HMM TIGR00211. (657 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. (858 aa)
lysSlysyl-tRNA synthetase; Identified by match to protein family HMM PF00152; match to protein family HMM PF01336; match to protein family HMM TIGR00499; Belongs to the class-II aminoacyl-tRNA synthetase family. (502 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; Identified by match to protein family HMM PF01409; match to protein family HMM PF02912; match to protein family HMM TIGR00468; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (328 aa)
pheTphenylalanyl-tRNA synthetase, beta subunit; Identified by match to protein family HMM PF01588; match to protein family HMM PF03147; match to protein family HMM PF03484; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (749 aa)
cysScysteinyl-tRNA synthetase; Identified by match to protein family HMM PF01406; match to protein family HMM PF09190; match to protein family HMM PF09334; match to protein family HMM TIGR00435; Belongs to the class-I aminoacyl-tRNA synthetase family. (464 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. (588 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 [...] (574 aa)
gatBaspartyl/glutamyl-tRNA(Asn/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. (474 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. (93 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. (635 aa)
selAL-seryl-tRNA selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (448 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). (611 aa)
glyQglycyl-tRNA synthetase, alpha subunit; Identified by match to protein family HMM PF02091; match to protein family HMM TIGR00388. (280 aa)
leuSleucyl-tRNA synthetase; Identified by match to protein family HMM PF00133; match to protein family HMM PF09334; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family. (819 aa)
NAMH_1683tRNA synthetase, class II; Identified by match to protein family HMM PF00587. (271 aa)
Your Current Organism:
Nautilia profundicola
NCBI taxonomy Id: 598659
Other names: N. profundicola AmH, Nautilia profundicola AmH, Nautilia profundicola str. AmH, Nautilia profundicola strain AmH, Nautilia sp. AmH, epsilon proteobacterium AmH
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