tRNA-(ms[2]io[6]A)-hydroxylase catalyzes the oxygen-dependent transformation of 2-methylthio-N-6-isopentenyl adenosine (ms[2]i[6]A) into ms[2]io[6]A, a modified nucleoside found in some tRNAs
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
16-260
7.16e-96
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) [Translation, ribosomal structure and biogenesis]; tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) is part of the Pathway/BioSystem: tRNA modification
:
Pssm-ID: 443544 Cd Length: 198 Bit Score: 279.71 E-value: 7.16e-96
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
16-260
7.16e-96
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) [Translation, ribosomal structure and biogenesis]; tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443544 Cd Length: 198 Bit Score: 279.71 E-value: 7.16e-96
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO ...
18-260
1.38e-92
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO(6)A)-hydroxylase (MiaE) proteins. The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present at position 37 (3' of the anticodon) of tRNAs that read codons beginning with U except tRNA(I,V Ser) in Escherichia coli. Salmonella typhimurium 2-methylthio-cis-ribozeatin (ms2io6A) is found in tRNA, probably in the corresponding species that have ms2i6A in E. coli. The miaE gene is absent in E. coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.
Pssm-ID: 114868 Cd Length: 199 Bit Score: 271.27 E-value: 1.38e-92
MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain; MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.
Pssm-ID: 153119 Cd Length: 180 Bit Score: 203.18 E-value: 5.93e-66
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
16-260
7.16e-96
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) [Translation, ribosomal structure and biogenesis]; tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443544 Cd Length: 198 Bit Score: 279.71 E-value: 7.16e-96
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO ...
18-260
1.38e-92
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO(6)A)-hydroxylase (MiaE) proteins. The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present at position 37 (3' of the anticodon) of tRNAs that read codons beginning with U except tRNA(I,V Ser) in Escherichia coli. Salmonella typhimurium 2-methylthio-cis-ribozeatin (ms2io6A) is found in tRNA, probably in the corresponding species that have ms2i6A in E. coli. The miaE gene is absent in E. coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.
Pssm-ID: 114868 Cd Length: 199 Bit Score: 271.27 E-value: 1.38e-92
MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain; MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.
Pssm-ID: 153119 Cd Length: 180 Bit Score: 203.18 E-value: 5.93e-66
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
130-225
6.55e-03
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).
Pssm-ID: 153097 Cd Length: 130 Bit Score: 35.93 E-value: 6.55e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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