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lysS lysS gltX gltX selA selA Sdel_1928 Sdel_1928 serS serS Sdel_1755 Sdel_1755 alaS alaS glyQ glyQ trmD trmD Sdel_1632 Sdel_1632 leuS leuS trmL trmL glyS glyS Sdel_1454 Sdel_1454 valS valS hemA hemA proS proS Sdel_1304 Sdel_1304 hisS hisS tgt tgt truD truD gatB gatB truA truA cysS cysS trmA trmA Sdel_0896 Sdel_0896 Sdel_0681 Sdel_0681 Sdel_0680 Sdel_0680 metG metG aspS aspS tyrS tyrS trmB trmB pheT pheT pheS pheS gatC gatC Sdel_0536 Sdel_0536 fmt fmt gatA gatA ileS ileS argS argS Sdel_0261 Sdel_0261 pth pth miaA miaA thrS thrS rlmN rlmN
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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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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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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)
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)
selAL-seryl-tRNA selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (445 aa)
Sdel_1928PFAM: tRNA synthetase class II (G H P and S); KEGG: cco:CCC13826_2132 ATP phosphoribosyltransferase regulatory subunit. (284 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_1755KEGG: cco:CCC13826_0775 tryptophanyl-tRNA synthetase; TIGRFAM: tryptophanyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ib. (321 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)
glyQKEGG: nis:NIS_1511 glycyl-tRNA synthetase subunit alpha; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit. (285 aa)
trmDtRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (230 aa)
Sdel_1632PFAM: pseudouridylate synthase TruB domain protein; KEGG: cff:CFF8240_0715 tRNA pseudouridine synthase B; Belongs to the pseudouridine synthase TruB family. (275 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)
trmLtRNA/rRNA methyltransferase (SpoU); Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. (156 aa)
glySKEGG: nis:NIS_0732 glycyl-tRNA synthetase subunit beta; TIGRFAM: glycyl-tRNA synthetase, beta subunit; PFAM: glycyl-tRNA synthetase beta subunit. (683 aa)
Sdel_1454S-adenosylmethionine/tRNA-ribosyltransferase-iso merase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). (308 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)
hemAglutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (433 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)
Sdel_1304TIGRFAM: tRNA 2-selenouridine synthase; SMART: Rhodanese domain protein; KEGG: cco:CCC13826_0142 tRNA 2-selenouridine synthase; Belongs to the SelU family. (342 aa)
hisSKEGG: tdn:Suden_1130 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S). (402 aa)
tgtQueuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] (373 aa)
truDtRNA pseudouridine synthase D TruD; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. (361 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)
truAtRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (247 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)
trmAtRNA (uracil-5-)-methyltransferase; Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). (367 aa)
Sdel_0896TIGRFAM: ybaK/ebsC protein; PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: wsu:WS1648 hypothetical protein; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (158 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)
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)
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)
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)
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)
trmBtRNA (guanine-N(7)-)-methyltransferase; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. (392 aa)
pheTTIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: ccv:CCV52592_0517 phenylalanyl-tRNA synthetase subunit beta. (779 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)
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)
Sdel_0536Dihydrouridine synthase DuS; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. (312 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)
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)
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)
argSKEGG: nis:NIS_1495 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. (528 aa)
Sdel_0261PFAM: Radical SAM domain protein; protein of unknown function DUF752; SMART: Elongator protein 3/MiaB/NifB; KEGG: glo:Glov_3168 conserved hypothetical radical SAM protein. (564 aa)
pthpeptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family. (191 aa)
miaAtRNA delta(2)-isopentenylpyrophosphate transferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (298 aa)
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)
rlmNRadical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (358 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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