STRINGSTRING
ADU66787.1 ADU66787.1 hisZ hisZ ADU64984.1 ADU64984.1 serS serS ADU65202.1 ADU65202.1 gatB gatB trmFO trmFO fmt fmt rph rph metG metG ADU65311.1 ADU65311.1 alaS alaS rlmN rlmN rnpA rnpA aspS aspS hisS hisS queA queA leuS leuS gltX gltX ADU65677.1 ADU65677.1 ADU65730.1 ADU65730.1 valS valS asnS asnS tyrS tyrS ADU65883.1 ADU65883.1 ADU65897.1 ADU65897.1 truA truA pth pth lysS lysS glyS glyS glyQ glyQ ileS ileS cysS cysS truB truB gatC gatC gatA gatA proS proS ADU66758.1 ADU66758.1 miaA miaA ADU66799.1 ADU66799.1 ADU66842.1 ADU66842.1 gluQ gluQ argS argS ADU66975.1 ADU66975.1 hemA hemA tgt tgt ADU67127.1 ADU67127.1 thrS thrS pheS pheS pheT pheT ADU67268.1 ADU67268.1 trmD trmD
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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
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a 3D structure is known or predicted
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ADU66787.1PFAM: Methyltransferase type 11; KEGG: alv:Alvin_1115 methyltransferase type 11. (248 aa)
hisZHistidine--tRNA ligase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. (386 aa)
ADU64984.1KEGG: sno:Snov_3767 hypothetical protein. (297 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). (430 aa)
ADU65202.1Dihydrouridine 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. (324 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. (479 aa)
trmFOGid protein; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. (438 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. (312 aa)
rphRibonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (244 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. (629 aa)
ADU65311.1PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: swo:Swol_2044 YbaK/EbsC family protein. (307 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. (893 aa)
rlmNRadical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. (342 aa)
rnpARibonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. (117 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. (592 aa)
hisSTIGRFAM: histidyl-tRNA synthetase; KEGG: dap:Dacet_1436 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein. (418 aa)
queAS-adenosylmethionine/tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). (339 aa)
leuSKEGG: dba:Dbac_0057 leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (822 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. (480 aa)
ADU65677.1PFAM: protein of unknown function DUF752; KEGG: sun:SUN_0204 hypothetical protein. (270 aa)
ADU65730.1KEGG: tcx:Tcr_1023 tRNA 2-selenouridine synthase; TIGRFAM: tRNA 2-selenouridine synthase; SMART: Rhodanese domain protein. (380 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)
asnSKEGG: pca:Pcar_0586 asparaginyl-tRNA synthetase; TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type. (448 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. (404 aa)
ADU65883.1PFAM: methyltransferase; KEGG: fnu:FN1606 3-deoxy-D-manno-octulosonic-acid transferase. (216 aa)
ADU65897.1PFAM: formyl transferase domain protein; KEGG: ppd:Ppro_0055 methionyl-tRNA formyltransferase. (310 aa)
truAtRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (263 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)
lysSKEGG: ddf:DEFDS_1155 lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; PFAM: 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. (498 aa)
glySTIGRFAM: glycyl-tRNA synthetase, beta subunit; KEGG: gem:GM21_0656 glycyl-tRNA synthetase subunit beta; PFAM: glycyl-tRNA synthetase beta subunit. (693 aa)
glyQTIGRFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: ddf:DEFDS_0639 glycyl-tRNA synthetase subunit alpha; PFAM: glycyl-tRNA synthetase alpha subunit. (293 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. (925 aa)
cysSTIGRFAM: cysteinyl-tRNA synthetase; KEGG: ddf:DEFDS_0838 cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase class Ia; Cysteinyl-tRNA synthetase class Ia DALR; Belongs to the class-I aminoacyl-tRNA synthetase family. (465 aa)
truBtRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. (293 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. (95 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). (480 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 [...] (572 aa)
ADU66758.1KEGG: amt:Amet_0949 hypothetical protein. (327 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. (312 aa)
ADU66799.1KEGG: tgr:Tgr7_2730 YbaK/EbsC protein; TIGRFAM: ybaK/ebsC protein; PFAM: YbaK/prolyl-tRNA synthetase associated region; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (158 aa)
ADU66842.1TIGRFAM: tryptophanyl-tRNA synthetase; KEGG: cth:Cthe_0686 tryptophanyl-tRNA synthetase; PFAM: aminoacyl-tRNA synthetase class Ib. (327 aa)
gluQGlutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (318 aa)
argSTIGRFAM: arginyl-tRNA synthetase; KEGG: gem:GM21_1940 arginyl-tRNA synthetase. (556 aa)
ADU66975.1tRNA/rRNA methyltransferase (SpoU); Could methylate the ribose at the nucleotide 34 wobble position in tRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily. (158 aa)
hemAglutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (419 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 [...] (368 aa)
ADU67127.1PFAM: domain of unknown function DUF1732; YicC-like domain-containing protein; KEGG: dal:Dalk_1930 YicC domain protein. (297 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). (657 aa)
pheSKEGG: pca:Pcar_1422 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. (377 aa)
pheTKEGG: mxa:MXAN_3595 phenylalanyl-tRNA synthetase subunit beta; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (793 aa)
ADU67268.1KEGG: bav:BAV0365 hypothetical protein. (261 aa)
trmDtRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (436 aa)
Your Current Organism:
Desulfurispirillum indicum
NCBI taxonomy Id: 653733
Other names: D. indicum S5, Desulfurispirillum indicum S5, Desulfurispirillum indicum str. S5, Desulfurispirillum indicum strain S5, bacterium S5, dissimilatory selenate-respiring bacterium S5
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