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ileS ileS rluA rluA gluQ gluQ tilS tilS arfB arfB proS proS tsaA tsaA queA queA tgt tgt thiI thiI ybaK ybaK mnmH mnmH cysS cysS leuS leuS glnS glnS serS serS smtA smtA asnS asnS pth pth hemA hemA tyrS tyrS pheT pheT pheS pheS thrS thrS yeaK yeaK aspS aspS cmoB cmoB argS argS metG metG dusC dusC rbn rbn truA truA mnmC mnmC gtrA gtrA gltX gltX hisS hisS rlmN rlmN trmJ trmJ trmN trmN yfiP yfiP trmD trmD alaS alaS truD truD truC truC tcdA tcdA lysS lysS trmI trmI cca cca truB truB dusB dusB fmt fmt trpS trpS glyS glyS glyQ glyQ selA selA trmL trmL yicC yicC trmH trmH rnpA rnpA dtd dtd trmA trmA rluF rluF dusA dusA lysU lysU epmA epmA miaA miaA valS valS kptA kptA yjtD yjtD
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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). (938 aa)
rluADual-specificity RNA pseudouridine synthase RluA; 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)
gluQglutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis. (308 aa)
tilStRNA(Ile)-lysidine synthetase; 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. This enzyme is essential for viability. (432 aa)
arfBAlternative stalled-ribosome rescue factor B; Rescues stalled ribosomes. Can hydrolyze peptidyl-tRNA on ribosomes stalled by both non-stop mRNAs and mRNAs that contain rare codon clusters or ribosomes stalled in the middle of mRNA. First identified as a complementary ribosome rescue system when the stalled ribosome cannot be rescued by the SsrA(tmRNA)- SmpB quality control system or the alternative ribosome-rescue factor A (arfA). (140 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)
tsaAtRNA-Thr(GGU) m(6)t(6)A37 methyltransferase, SAM-dependent; S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU) that read codons starting with adenosine. The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability. Binds to tRNA. (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); Belongs to the QueA family. (356 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)
thiItRNA s(4)U8 sulfurtransferase; 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. Belongs to the ThiI family. (482 aa)
ybaKCys-tRNA(Pro)/Cys-tRNA(Cys) deacylase; Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. May compensate for the lack of Cys-tRNA(Pro) editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and displays weak deacylase activity in vitro against Gly-tRNA(Gly), as well as, at higher concentrations, some other correctly charged tRNAs. Unlike some of its orthologs it is not able to remove the amino acid moiety from incorrectly charged Ala- tRNA(Pro); Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (159 aa)
mnmHtRNA 2-selenouridine synthase; 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. (364 aa)
cysSCysteine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
leuSLeucine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
glnSGlutamine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (554 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)
smtAPutative S-adenosyl-L-methionine-dependent methyltransferase; Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs. Four tRNAs (tRNA(Ala1), tRNA(Ser1), tRNA(Pro3) and tRNA(Thr4)) are fully modified with mcmo5U in stationary-phase E.coli. Also present at low frequency in tRNA(Leu3) and tRNA(Val1). (261 aa)
asnSAsparagine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (466 aa)
pthpeptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death. (194 aa)
hemAGlutamyl tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. (418 aa)
tyrStyrosyl-tRNA synthetase; Catalyzes the attachment of L-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). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine. (424 aa)
pheTPhenylalanine tRNA synthetase, beta-subunit; Protein involved in tRNA aminoacylation for protein translation. (795 aa)
pheSPhenylalanine tRNA synthetase, alpha-subunit; Protein involved in tRNA aminoacylation for protein translation. (327 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). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isost [...] (642 aa)
yeaKaminoacyl-tRNA editing domain protein. (167 aa)
aspSaspartyl-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). Also mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate ; Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (590 aa)
cmoBtRNA (cmo5U34)-carboxymethyltransferase, carboxy-SAM-dependent; 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. Can also catalyze the SAM-dependent methylation of ho5U, with much lower efficiency. (323 aa)
argSArginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (577 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. (677 aa)
dusCtRNA-dihydrouridine synthase C; 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. DusC specifically modifies U16 in tRNAs. (315 aa)
rbnRNase BN, tRNA processing enzyme; Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities, depending on the nature of the substrate and of the added divalent cation, and on its 3'-terminal structure. Can process the 3' termini of both CCA-less and CCA-containing tRNA precursors. CCA-less tRNAs are cleaved endonucleolytically after the discriminator base, whereas residues following the CCA sequence can be removed exonucleolytically or endonucleolytically in CCA-containing molecules. Does not remove the CCA sequence. May also be involved in the degradation [...] (305 aa)
truAtRNA pseudouridine(38-40) synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (270 aa)
mnmCtRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC; 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. (668 aa)
gtrACPS-53 (KpLE1) prophage; Involved in O antigen modification. Involved in the translocation of bactoprenol-linked glucose across the cytoplasmic membrane (By similarity); Belongs to the GtrA family. (120 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). (471 aa)
hisSHistidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. (424 aa)
rlmNDual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; 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. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. (384 aa)
trmJtRNA mC32,mU32 2'-O-methyltransferase, SAM-dependent; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA. (246 aa)
trmNtRNA1(Val) (adenine(37)-N6)-methyltransferase; Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC); Belongs to the methyltransferase superfamily. tRNA (adenine-N(6)-)-methyltransferase family. (245 aa)
yfiPDTW domain protein. (232 aa)
trmDtRNA m(1)G37 methyltransferase, SAM-dependent; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (255 aa)
alaSalanyl-tRNA synthetase; Catalyzes the attachment of L-alanine to tRNA(Ala) in a two- step reaction: L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser. These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step. Attaches Ala to transfer-me [...] (876 aa)
truDtRNA(Glu) pseudouridine(13) synthase; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. (349 aa)
truCtRNA(Ile1,Asp) pseudouridine(65) synthase; Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs; Belongs to the pseudouridine synthase RluA family. (260 aa)
tcdAtRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine. TcdA is also part of a sulfur transfer pathway; is able to accept sulfur from CsdA directly in vitro, but CsdE might act as the sulfur donor in vivo; Belongs to the HesA/MoeB/ThiF family. (268 aa)
lysSLysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
trmItRNA m(7)G46 methyltransferase, SAM-dependent; 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)
ccaFused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; 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 highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...] (412 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. (314 aa)
dusBtRNA-dihydrouridine synthase B; 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)
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. Belongs to the Fmt family. (315 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Amino acylates tRNA(Trp) with both L- and D-tryptophan, although D-tryptophan is a poor substrate ; Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
glySGlycine tRNA synthetase, beta subunit; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-II aminoacyl-tRNA synthetase family. (689 aa)
glyQGlycine tRNA synthetase, alpha subunit; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-II aminoacyl-tRNA synthetase family. (303 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule; Belongs to the SelA family. (463 aa)
trmLtRNA Leu mC34,mU34 2'-O-methyltransferase, SAM-dependent; 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. Recognition of the target requires a pyridine at position 34 and N(6)-(isopentenyl)-2-methylthioadenosine at position 37. (157 aa)
yicCUPF0701 protein YicC; Ribonuclease PH (defective);enzyme; Degradation of RNA; RNase PH; Protein involved in RNA catabolic process. (287 aa)
trmHtRNA mG18-2'-O-methyltransferase, SAM-dependent; Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. (229 aa)
rnpAProtein C5 component of RNase 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)
dtdD-tyr-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-t [...] (145 aa)
trmAtRNA m(5)U54 methyltransferase, SAM-dependent; 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). (366 aa)
rluF23S rRNA pseudouridine(2604) 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). Can, to a small extent, also react with uracil-2605. Belongs to the pseudouridine synthase RsuA family. (290 aa)
dusAtRNA-dihydrouridine synthase A; 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. (345 aa)
lysULysine tRNA synthetase, inducible; Also can synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
epmAElongation Factor P Lys34 lysyltransferase; 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'. The substrate (R)-beta-lysine is 100-fold more efficient than either (S)-beta-lysine or L-alpha-lysine. Cannot ligate lysine to any tRNA. (325 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)
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. (951 aa)
kptARNA 2'-phosphotransferase; Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''- cyclic phosphate (APPR>P). May function as an ADP-ribosylase. (184 aa)
yjtDPutative methyltransferase; Protein involved in RNA modification; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. (228 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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