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) ...
10-254
3.21e-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: 280.09 E-value: 3.21e-96
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
10-254
3.21e-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: 280.09 E-value: 3.21e-96
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO ...
12-254
1.12e-94
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: 276.66 E-value: 1.12e-94
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: 207.41 E-value: 9.15e-68
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
10-254
3.21e-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: 280.09 E-value: 3.21e-96
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO ...
12-254
1.12e-94
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: 276.66 E-value: 1.12e-94
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: 207.41 E-value: 9.15e-68
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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