16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Escherichia sp. HH41S]
Protein Classification
16S rRNA (cytidine(1402)-2'-O)-methyltransferase( domain architecture ID 10794106)
16S rRNA (cytidine(1402)-2'-O)-methyltransferase uses assembled 30S subunit as a substrate and catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA; belongs to the tetrapyrrole methylase family
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK14994 | PRK14994 | SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional |
1-287 | 0e+00 | |||||
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional : Pssm-ID: 184956 Cd Length: 287 Bit Score: 584.87 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PRK14994 | PRK14994 | SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional |
1-287 | 0e+00 | |||||
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional Pssm-ID: 184956 Cd Length: 287 Bit Score: 584.87 E-value: 0e+00
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| RsmI | COG0313 | 16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ... |
14-234 | 1.12e-136 | |||||
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; 16S rRNA C1402 (ribose-2'-O) methylase RsmI is part of the Pathway/BioSystem: 16S rRNA modification Pssm-ID: 440082 Cd Length: 219 Bit Score: 384.74 E-value: 1.12e-136
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| RsmI | cd11648 | Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ... |
15-233 | 5.67e-132 | |||||
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase; RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress. Pssm-ID: 381175 Cd Length: 216 Bit Score: 372.49 E-value: 5.67e-132
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| TIGR00096 | TIGR00096 | 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ... |
14-283 | 3.49e-113 | |||||
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is RsmI, one of a pair of genes involved in a unique dimethyl modification of a cytidine in 16S rRNA. See pfam00590 (tetrapyrrole methylase), which demonstrates homology between this family and other members, including several methylases for the tetrapyrrole class of compound, as well as the enzyme diphthine synthase. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 129204 [Multi-domain] Cd Length: 276 Bit Score: 327.55 E-value: 3.49e-113
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
14-213 | 4.67e-33 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 120.14 E-value: 4.67e-33
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| Name | Accession | Description | Interval | E-value | |||||
| PRK14994 | PRK14994 | SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional |
1-287 | 0e+00 | |||||
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional Pssm-ID: 184956 Cd Length: 287 Bit Score: 584.87 E-value: 0e+00
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| RsmI | COG0313 | 16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ... |
14-234 | 1.12e-136 | |||||
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; 16S rRNA C1402 (ribose-2'-O) methylase RsmI is part of the Pathway/BioSystem: 16S rRNA modification Pssm-ID: 440082 Cd Length: 219 Bit Score: 384.74 E-value: 1.12e-136
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| RsmI | cd11648 | Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ... |
15-233 | 5.67e-132 | |||||
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase; RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress. Pssm-ID: 381175 Cd Length: 216 Bit Score: 372.49 E-value: 5.67e-132
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| RsmI_like | cd19917 | tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ... |
15-233 | 2.06e-114 | |||||
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase I (RsmI); RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress. Pssm-ID: 381180 Cd Length: 217 Bit Score: 328.15 E-value: 2.06e-114
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| TIGR00096 | TIGR00096 | 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ... |
14-283 | 3.49e-113 | |||||
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is RsmI, one of a pair of genes involved in a unique dimethyl modification of a cytidine in 16S rRNA. See pfam00590 (tetrapyrrole methylase), which demonstrates homology between this family and other members, including several methylases for the tetrapyrrole class of compound, as well as the enzyme diphthine synthase. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 129204 [Multi-domain] Cd Length: 276 Bit Score: 327.55 E-value: 3.49e-113
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| RsmI_like | cd19918 | uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ... |
15-233 | 3.58e-83 | |||||
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI); RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress. Pssm-ID: 381181 Cd Length: 217 Bit Score: 248.99 E-value: 3.58e-83
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| TP_methylase | cd09815 | S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
17-233 | 9.39e-59 | |||||
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide. Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 186.83 E-value: 9.39e-59
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| RsmI_like | cd11649 | uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ... |
14-232 | 4.87e-42 | |||||
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI); RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress. Pssm-ID: 381176 Cd Length: 229 Bit Score: 144.11 E-value: 4.87e-42
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
14-213 | 4.67e-33 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 120.14 E-value: 4.67e-33
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| Precorrin_2_C20_MT | cd11645 | Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
27-199 | 1.32e-07 | |||||
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme. Pssm-ID: 381172 [Multi-domain] Cd Length: 223 Bit Score: 50.97 E-value: 1.32e-07
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| Precorrin_3B_C17_MT | cd11646 | Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
14-133 | 1.79e-04 | |||||
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone. Pssm-ID: 381173 [Multi-domain] Cd Length: 238 Bit Score: 42.02 E-value: 1.79e-04
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| SUMT | cd11642 | Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
27-186 | 7.46e-04 | |||||
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme. Pssm-ID: 381169 Cd Length: 228 Bit Score: 40.11 E-value: 7.46e-04
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| TP_methylase | cd11724 | uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
13-118 | 1.14e-03 | |||||
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide. Pssm-ID: 381178 [Multi-domain] Cd Length: 243 Bit Score: 39.46 E-value: 1.14e-03
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