STRINGSTRING
ABK72876.1 ABK72876.1 ABK76156.1 ABK76156.1 gatA gatA ABK71083.1 ABK71083.1 trpS trpS selA selA gatC gatC gatA-2 gatA-2 gatB gatB gltX gltX ABK72091.1 ABK72091.1 proS proS thrS thrS hisS hisS aspS aspS alaS alaS fmt fmt ileS ileS tyrS tyrS pheT pheT pheS pheS lysX lysX ABK72122.1 ABK72122.1 glyS glyS valS valS argS argS metG metG cysS-2 cysS-2 lysS lysS gltX-2 gltX-2 serS serS 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
Others
textmining
co-expression
protein homology
Your Input:
ABK72876.1Formyl transferase; Identified by match to protein family HMM PF00551; match to protein family HMM PF02911. (322 aa)
ABK76156.1glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF01425. (487 aa)
gatAglutamyl-tRNA(Gln)/aspartyl-tRNA(Asn) amidotransferase, A subunit; Identified by match to protein family HMM PF01425; Belongs to the amidase family. (466 aa)
ABK71083.1Amidase; Identified by match to protein family HMM PF01425; Belongs to the amidase family. (468 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (338 aa)
selAL-seryl-tRNA selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (426 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)
gatA-2glutamyl-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). (494 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. (503 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. (486 aa)
ABK72091.1Identified by match to protein family HMM PF01425; Belongs to the amidase family. (467 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 [...] (585 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). (684 aa)
hisShistidyl-tRNA synthetase; Identified by match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442. (426 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. (598 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. (896 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. (312 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 2 subfamily. (1040 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. (440 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 PF03483; match to protein family HMM PF03484; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (832 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. (356 aa)
lysXlysyl-tRNA synthetase; Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine res [...] (1089 aa)
ABK72122.1glutamyl-tRNA(Gln) amidotransferase subunit A; Identified by match to protein family HMM PF01425; Belongs to the amidase family. (416 aa)
glySglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (461 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. (872 aa)
argSarginyl-tRNA synthetase; Identified by match to protein family HMM PF00750; match to protein family HMM PF03485; match to protein family HMM PF05746; match to protein family HMM TIGR00456. (550 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. (515 aa)
cysS-2cysteinyl-tRNA synthetase; Identified by match to protein family HMM PF01406; match to protein family HMM TIGR00435; Belongs to the class-I aminoacyl-tRNA synthetase family. (477 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. (507 aa)
gltX-2glutamyl-tRNA synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (292 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). (417 aa)
leuSleucyl-tRNA synthetase; Identified by match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family. (953 aa)
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
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