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aspS aspS yecO yecO yecP yecP argS argS metG metG yohI yohI elaC elaC truA truA mnmC mnmC gltX gltX ypfI ypfI hisS hisS yfgB yfgB trmJ trmJ yfhC yfhC rnc rnc yfiC yfiC yfiP yfiP trmD trmD alaS alaS ygbO ygbO yqcB yqcB ygdL ygdL lysS lysS ygfZ ygfZ yggH yggH cca cca gcp gcp truB truB yhdG yhdG yrdC yrdC fmt fmt yheL yheL yheM yheM yheN yheN trpS trpS yhhP yhhP glyS glyS glyQ glyQ selA selA yibK yibK rph rph spoU spoU STM3768 STM3768 rnpA rnpA trmE trmE gidA gidA yihZ yihZ trmA trmA yjbC yjbC yjbN yjbN yjeA yjeA yjeS yjeS yjeE yjeE miaA miaA STM4446 STM4446 miaE miaE valS valS trpS2 trpS2 STM4549 STM4549 lasT lasT ileS ileS rluA rluA yadB yadB mesJ mesJ proS proS yaeB yaeB queA queA tgt tgt thiI thiI ybaK ybaK ybbB ybbB cysS cysS leuS leuS miaB miaB glnS glnS yliG yliG serS serS smtA smtA asnS asnS yccK yccK STM1109 STM1109 yceA yceA rne rne trmU trmU yeaK yeaK thrS thrS pheS pheS pheT pheT rnt rnt tyrS tyrS STM1548 STM1548 ydaO ydaO rnd rnd yeaZ yeaZ
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query proteins and first shell of interactors
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proteins of unknown 3D structure
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aspSAspartate 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. (590 aa)
yecOPutative SAM-dependent methyltransferase; Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM); Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family. (247 aa)
yecPPutative enzyme; Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L- methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5- carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoB family. (323 aa)
argSarginyl-tRNA synthetase. (SW:SYR_SALTY). (577 aa)
metGMethionine 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. (677 aa)
yohIPutative nitrogen regulation protein; 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. Specifically modifies U16 in tRNAs. Belongs to the Dus family. DusC subfamily. (312 aa)
elaCPutative metal-dependent hydrolase; Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities. (305 aa)
truAPseudouridylate synthase I; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (270 aa)
mnmCPutative peptidase; Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34; In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family. (686 aa)
gltXGlutamate tRNA synthetase, catalytic subunit; 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). (471 aa)
ypfIPutative acetyltransferase; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). (672 aa)
hisShistidyl-tRNA synthetase. (SW:SYH_SALTY). (424 aa)
yfgBPutative Fe-S-cluster redox enzyme; 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. (388 aa)
trmJPutative rRNA methylase; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. (243 aa)
yfhCPutative cytosine/adenosine deaminase; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family. (183 aa)
rncRNase III, ds RNA; Digests double-stranded RNA. Involved in the processing of ribosomal RNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Removes small helical intervening sequences (IVSs) from all 7 of the 23S rRNA transcripts. Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. (226 aa)
yfiCPutative transferase; Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC). (245 aa)
yfiPPutative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC75636.1); Blastp hit to AAC75636.1 (240 aa), 88% identity in aa 9 - 234. (226 aa)
trmDtRNA (guanine-7-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (255 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; Belongs to the class-II aminoacyl-tRNA synthetase family. (876 aa)
ygbOPutative hydrogenase subunit; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. (349 aa)
yqcBPutative synthase; Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs; Belongs to the pseudouridine synthase RluA family. (260 aa)
ygdLSimilar to E. coli putative enzyme (AAC75854.1); Blastp hit to AAC75854.1 (268 aa), 93% identity in aa 1 - 267. (268 aa)
lysSSimilar to E. coli lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA (AAC75928.1); Blastp hit to AAC75928.1 (505 aa), 95% identity in aa 1 - 505; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
ygfZPutative aminomethyltransferase; Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication; Belongs to the tRNA-modifying YgfZ family. (326 aa)
yggHPutative S-adenosylmethionine-dependent methyltransferase; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family. (239 aa)
ccatRNA nucleotidyl transferase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. (413 aa)
gcpPutative O-sialoglycoprotein endopeptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family. (337 aa)
truBtRNA pseudouridine 5S synthase; 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. (314 aa)
yhdGPutative TIM-barrel enzyme; 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. DusB subfamily. (321 aa)
yrdCPutative translation factor; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. (190 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. (315 aa)
yheLPutative oxidation of intracellular sulfur; Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. (95 aa)
yheMPutative oxidation of intracellular sulfur; Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. (118 aa)
yheNPutative ACR involved in intracellular sulfur reduction; Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE. (128 aa)
trpSTryptophan tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
yhhPSmall ubiquitous protein required for normal growth; Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthes [...] (81 aa)
glySSimilar to E. coli glycine tRNA synthetase, beta subunit (AAC76583.1); Blastp hit to AAC76583.1 (689 aa), 92% identity in aa 1 - 689. (689 aa)
glyQSimilar to E. coli glycine tRNA synthetase, alpha subunit (AAC76584.1); Blastp hit to AAC76584.1 (303 aa), 99% identity in aa 1 - 303. (303 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis; Belongs to the SelA family. (463 aa)
yibKPutative tRNA/rRNA methyltransferase; 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. (157 aa)
rphRNase PH; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates. (238 aa)
spoUPutative tRNA/rRNA methyltransferase; Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. (229 aa)
STM3768Putative selenocysteine synthase (L-seryl-tRNA(Ser) selenium transferase). (369 aa)
rnpARNase P; 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. (119 aa)
trmEGTPase for tRNA modification and thiophene and furan oxidation; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family. (454 aa)
gidAAssociated with glucose-inhibited division; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34; Belongs to the MnmG family. (629 aa)
yihZD-Tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. (145 aa)
trmAtRNA (uracil-5-)-methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNAs. (366 aa)
yjbCPutative pseudouridine synthase; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35 in the anticodon of tRNA(Tyr); Belongs to the pseudouridine synthase RsuA family. (289 aa)
yjbNPutative TIM-barrel enzyme; 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. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (332 aa)
yjeAPutative pyruvate oxidase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta- lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF- P 'Lys-34' (Probable). Can also use L-alpha-lysine as a substrate, but probably with lower efficiency. Cannot aminoacylate tRNA(Lys) with lysine. (325 aa)
yjeSPutative Fe-S protein; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr); Belongs to the QueG family. (384 aa)
yjeEPutative nucleotide-binding protein; Similar to E. coli orf, hypothetical protein (AAC77125.1); Blastp hit to AAC77125.1 (153 aa), 93% identity in aa 1 - 152. (153 aa)
miaADelta(2)-isopentenylpyrophosphate tRNA-adenosine 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. (316 aa)
STM4446Putative selenocysteine synthase; [L-seryl-tRNA(Ser) selenium transferase]. (372 aa)
miaEHydroxylase for synthesis of 2-methylthio-cis-ribozeatin in tRNA; Production of the modified nucleoside 2-methylthio-cis- ribozeatin (MS[2]IO[6]A) found in some tRNAs. Catalyzes the oxygen- dependent transformation of MS[2]I[6]A into MS[2]IO[6]A. (270 aa)
valSValine 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. (951 aa)
trpS2Putative tryptophanyl-tRNA synthetase; Similar to E. coli tryptophan tRNA synthetase (AAC76409.1); Blastp hit to AAC76409.1 (334 aa), 26% identity in aa 2 - 329; Belongs to the class-I aminoacyl-tRNA synthetase family. (337 aa)
STM4549Putative cytoplasmic protein. (152 aa)
lasTPutative tRNA/tRNA methyltransferase; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. (228 aa)
ileSIsoleucine 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. (944 aa)
rluA23S rRNA pseudouridylate 746 synthase; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs. (219 aa)
yadBPutative glutamyl t-RNA synthetase; 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. (313 aa)
mesJCell cycle protein; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (430 aa)
proSProline 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 de [...] (572 aa)
yaeBPutative regulator; Similar to E. coli orf, hypothetical protein (AAC73306.1); Blastp hit to AAC73306.1 (235 aa), 89% identity in aa 1 - 235. (235 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). (354 aa)
tgttRNA-guanine transglycosylase; 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 the [...] (375 aa)
thiISulfur transfer protein (from cys to ThiS and from IscS to U8-tRNA); Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (482 aa)
ybaKPutative cytoplasmic protein; Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. (159 aa)
ybbBPutative ATPase; Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain (Probable); Belongs to the SelU family. (364 aa)
cysSSimilar to E. coli cysteine tRNA synthetase (AAC73628.1); Blastp hit to AAC73628.1 (461 aa), 94% identity in aa 1 - 461; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
leuSSimilar to E. coli leucine tRNA synthetase (AAC73743.1); Blastp hit to AAC73743.1 (860 aa), 95% identity in aa 1 - 860; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
miaBMethylthiolation of isopentenylated A37 derivatives in rRNA; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
glnSSimilar to E. coli glutamine tRNA synthetase (AAC73774.1); Blastp hit to AAC73774.1 (554 aa), 96% identity in aa 1 - 554. (555 aa)
yliGPutative Fe-S oxidoreductases family 1; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (441 aa)
serSSerine 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)
smtAS-adenosylmethionine-dependent methyltransferase; Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs; Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoM family. (267 aa)
asnSSimilar to E. coli asparagine tRNA synthetase (AAC74016.1); Blastp hit to AAC74016.1 (466 aa), 94% identity in aa 1 - 466. (466 aa)
yccKPutative sulfite reductase, gamma subunit; Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Could accept sulfur from TusD (By similarity). (109 aa)
STM1109Putative periplasmic protein; Similar to E. coli orf, hypothetical protein (AAC75328.1); Blastp hit to AAC75328.1 (311 aa), 27% identity in aa 7 - 147, 27% identity in aa 155 - 277. (312 aa)
yceAPutative enzyme related to sulfur transferases; Similar to E. coli orf, hypothetical protein (AAC74139.1); Blastp hit to AAC74139.1 (350 aa), 88% identity in aa 1 - 350; Belongs to the UPF0176 family. (350 aa)
rneRNase E; Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Belongs to the RNase E/G family. RNase E subfamily. (1067 aa)
trmUtRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs; Belongs to the MnmA/TRMU family. (383 aa)
yeaKPutative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74857.1); Blastp hit to AAC74857.1 (167 aa), 87% identity in aa 1 - 165. (172 aa)
thrSThreonine 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). Also edits incorrectly charged L-seryl-tRNA(Thr). (642 aa)
pheSSimilar to E. coli phenylalanine tRNA synthetase, alpha-subunit (AAC74784.1); Blastp hit to AAC74784.1 (327 aa), 97% identity in aa 1 - 327. (327 aa)
pheTPhenylalanine tRNA synthetase, beta-subunit; phenylalanyl-tRNA synthetase beta chain. (SW:SYFB_SALTY); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
rntRNase T; Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis. (215 aa)
tyrSTyrosine 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 1 subfamily. (424 aa)
STM1548Putative S-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). (346 aa)
ydaOPutative ATPase; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. Belongs to the TtcA family. (311 aa)
rndRNase D; Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides; Belongs to the RNase D family. (375 aa)
yeaZPutative molecular chaperone; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity). Neither binds polyphosphates nor a wide range of nucleotides on its own. Does n [...] (231 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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