STRINGSTRING
alaS alaS serS serS fmt fmt tyrS tyrS valS valS hisS hisS aspS aspS Gura_2250 Gura_2250 gltX gltX argS argS pheT pheT pheS pheS thrS thrS proS proS asnS asnS leuS leuS metG metG lysS lysS glyS glyS glyQ glyQ Gura_3697 Gura_3697 selA selA glnS glnS cysS cysS ileS ileS gatB gatB gatA gatA gatC gatC
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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:
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. (876 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). (422 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. (313 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. (403 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. (886 aa)
hisSTIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. (415 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. (593 aa)
Gura_2250TIGRFAM: tryptophanyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase, class Ib. (327 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). (467 aa)
argSTIGRFAM: arginyl-tRNA synthetase. (561 aa)
pheTTIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (801 aa)
pheSTIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase, class IIc; aminoacyl tRNA synthetase, class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (338 aa)
thrSthreonyl-tRNA synthetase / Ser-tRNA(Thr) hydrolase; 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). (645 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)
asnSTIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type. (461 aa)
leuSTIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (824 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. (509 aa)
lysSTIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family. (494 aa)
glySglycyl-tRNA synthetase beta chain. (688 aa)
glyQPFAM: glycyl-tRNA synthetase, alpha subunit. (291 aa)
Gura_3697PFAM: formyl transferase domain protein. (308 aa)
selAL-seryl-tRNA(Sec) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (462 aa)
glnSTIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase, class Ic. (568 aa)
cysSTIGRFAM: cysteinyl-tRNA synthetase; PFAM: cysteinyl-tRNA synthetase, class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family. (494 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. (924 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. (479 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). (485 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. (95 aa)
Your Current Organism:
Geobacter uraniireducens
NCBI taxonomy Id: 351605
Other names: G. uraniireducens Rf4, Geobacter uraniireducens Rf4, Geobacter uraniireducens str. Rf4, Geobacter uraniireducens strain Rf4, Geobacter uraniumreducens JCM 13001
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