STRINGSTRING
leuS leuS thrS thrS SFS22963.1 SFS22963.1 argS argS gltX gltX SFS20121.1 SFS20121.1 trpS trpS alaS alaS valS valS SFS20248.1 SFS20248.1 SFS18891.1 SFS18891.1 ileS ileS selA selA SFS16242.1 SFS16242.1 fmt fmt lysS lysS SFS15648.1 SFS15648.1 SFS15557.1 SFS15557.1 pheT pheT pheS pheS ybaK ybaK glyQS glyQS cysS cysS SFS10523.1 SFS10523.1 proS proS aspS-2 aspS-2 hisS hisS fusA fusA metG metG asnS asnS tyrS tyrS gatB gatB gatA gatA gatC gatC aspS aspS
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:
leuSleucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (804 aa)
thrSSer-tRNA(Thr) hydrolase /threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (584 aa)
SFS22963.1Amidase. (524 aa)
argSarginyl-tRNA synthetase. (595 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. (492 aa)
SFS20121.1Predicted hydrolase, HD superfamily. (195 aa)
trpStryptophanyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (363 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. (882 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. (880 aa)
SFS20248.1Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC. (162 aa)
SFS18891.1Ribosomal protection tetracycline resistance protein. (639 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. (1044 aa)
selAL-seryl-tRNA(Sec) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (467 aa)
SFS16242.1seryl-tRNA synthetase. (429 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. (325 aa)
lysSlysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. (649 aa)
SFS15648.1alanyl-tRNA synthetase. (397 aa)
SFS15557.1Translation elongation factor 2 (EF-2/EF-G). (698 aa)
pheTphenylalanyl-tRNA synthetase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (810 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
ybaKCys-tRNA(Pro)/Cys-tRNA(Cys) deacylase; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (155 aa)
glyQSglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (462 aa)
cysScysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (469 aa)
SFS10523.1glutaminyl-tRNA synthetase. (564 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). (479 aa)
aspS-2aspartyl-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)
hisShistidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (421 aa)
fusATranslation elongation factor 2 (EF-2/EF-G); Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. [...] (705 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. (670 aa)
asnSasparaginyl-tRNA synthetase. (463 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. (408 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. (480 aa)
gatAaspartyl/glutamyl-tRNA(Asn/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). (495 aa)
gatCaspartyl/glutamyl-tRNA(Asn/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. (97 aa)
aspSNondiscriminating aspartyl-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 2 subfamily. (443 aa)
Your Current Organism:
Clostridium citroniae
NCBI taxonomy Id: 358743
Other names: CCUG 52203, Clostridium citroniae Warren et al. 2007, DSM 19261, [. citroniae, [Clostridium] citroniae, strain RMA 16102
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