STRINGSTRING
aspS aspS gatA gatA gatB gatB serS serS tyrS tyrS metS metS valS valS lysU lysU hisS hisS glnS glnS thrS thrS pheS pheS pheT pheT argS argS aspS-2 aspS-2 hisS-2 hisS-2 selA selA alaS alaS glyS glyS glyQ glyQ fmt fmt trpS trpS ileS ileS CBH22145.1 CBH22145.1 leuS leuS proS proS cysS cysS gltX gltX asnS asnS aspC aspC
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
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aspSaspartyl-tRNA synthetase; 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. (700 aa)
gatAGlutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT 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). (491 aa)
gatBAspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT 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. (468 aa)
serSseryl-tRNA synthetase, also charges selenocysteinyl-tRNA with serine; 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). (425 aa)
tyrSTyrosyl-tRNA synthetase 1 (Tyrosine--tRNA ligase 1) (TyrRS 1); 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)
metSmethionyl-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. (651 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. (884 aa)
lysULysine tRNA synthetase, inducible; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. (506 aa)
hisSHistidyl-tRNA synthetase (Histidine--tRNA ligase) (HisRS). (430 aa)
glnSglutamyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (559 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). (637 aa)
pheSPhenylalanine tRNA synthetase, alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
pheTPhenylalanine tRNA synthetase, beta subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (788 aa)
argSArginyl-tRNA synthetase 2 (Arginine--tRNA ligase 2) (ArgRS 2). (566 aa)
aspS-2aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (586 aa)
hisS-2Histidyl tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (420 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (472 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)
glySGlycine tRNA synthetase, beta subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (687 aa)
glyQGlycine tRNA synthetase, alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (294 aa)
fmt10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. (313 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (339 aa)
ileSIsoleucyl-tRNA synthetase 2 (Isoleucine--tRNA ligase 2) (IleRS 2); 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 [...] (1034 aa)
CBH22145.1Alanyl-tRNA synthetase related protein. (402 aa)
leuSleucyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (800 aa)
proSProlyl-tRNA synthetase 2 (Proline--tRNA ligase 2) (ProRS 2); 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). Can inadvertently accommodate and process cysteine. Misacylated Cys-tRNA(Pro) is not edited by ProRS; this function may be provided by ProX; Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily. (481 aa)
cysScysteinyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. (466 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). (495 aa)
asnSAsparaginyl tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (464 aa)
aspCaspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily. (429 aa)
Your Current Organism:
Acetoanaerobium sticklandii
NCBI taxonomy Id: 1511
Other names: A. sticklandii, ATCC 12662, BCRC 14485, CCRC 14485, CCRC:14485, CCUG 9281, Clostridium sticklandii, DSM 519, NCIMB 10654, strain StadtmanHF
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