STRINGSTRING
thrS thrS argS argS ileS ileS gatA gatA fmt fmt lysS lysS gatC gatC pheS pheS pheT pheT tyrS tyrS aspS aspS metG metG Sdel_0680 Sdel_0680 Sdel_0681 Sdel_0681 cysS cysS gatB gatB hisS hisS proS proS valS valS glyS glyS leuS leuS glyQ glyQ alaS alaS Sdel_1755 Sdel_1755 serS serS Sdel_1928 Sdel_1928 selA selA gltX gltX
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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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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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thrSTIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: cha:CHAB381_0611 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (605 aa)
argSKEGG: nis:NIS_1495 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. (528 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. (918 aa)
gatAglutamyl-tRNA(Gln) amidotransferase, A subunit; 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). (452 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. (319 aa)
lysSTIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; KEGG: nis:NIS_1177 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (506 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. (96 aa)
pheSKEGG: cff:CFF8240_1254 phenylalanyl-tRNA synthetase subunit alpha; TIGRFAM: 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. (330 aa)
pheTTIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: ccv:CCV52592_0517 phenylalanyl-tRNA synthetase subunit beta. (779 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. (402 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. (582 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. (642 aa)
Sdel_0680PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; KEGG: abu:Abu_1214 glutamylglutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (380 aa)
Sdel_0681TIGRFAM: glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; Asn/Gln amidotransferase; KEGG: sun:SUN_1139 glutaminyl-tRNA synthetase. (748 aa)
cysSKEGG: abu:Abu_0245 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase class Ia; tRNA synthetase class I (M); Belongs to the class-I aminoacyl-tRNA synthetase family. (466 aa)
gatBglutamyl-tRNA(Gln) amidotransferase, B 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 GatB/GatE family. GatB subfamily. (476 aa)
hisSKEGG: tdn:Suden_1130 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S). (402 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 [...] (567 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. (876 aa)
glySKEGG: nis:NIS_0732 glycyl-tRNA synthetase subunit beta; TIGRFAM: glycyl-tRNA synthetase, beta subunit; PFAM: glycyl-tRNA synthetase beta subunit. (683 aa)
leuSTIGRFAM: leucyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ia; tRNA synthetase class I (M); KEGG: abu:Abu_0402 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (815 aa)
glyQKEGG: nis:NIS_1511 glycyl-tRNA synthetase subunit alpha; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit. (285 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. (846 aa)
Sdel_1755KEGG: cco:CCC13826_0775 tryptophanyl-tRNA synthetase; TIGRFAM: tryptophanyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ib. (321 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). (414 aa)
Sdel_1928PFAM: tRNA synthetase class II (G H P and S); KEGG: cco:CCC13826_2132 ATP phosphoribosyltransferase regulatory subunit. (284 aa)
selAL-seryl-tRNA selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (445 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. (463 aa)
Your Current Organism:
Sulfurospirillum deleyianum
NCBI taxonomy Id: 525898
Other names: S. deleyianum DSM 6946, Sulfurospirillum deleyianum DSM 6946, Sulfurospirillum deleyianum str. DSM 6946, Sulfurospirillum deleyianum strain DSM 6946
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