rRNA (cytidine-2'-O-)-methyltransferase [Helicobacter pylori]
Protein Classification
SAM-dependent methyltransferase( domain architecture ID 148)
SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; belongs to the tetrapyrrole methylase family
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| TP_methylase super family | cl00304 | S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
1-284 | 2.66e-112 | |||||
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. The actual alignment was detected with superfamily member TIGR00096: Pssm-ID: 444820 [Multi-domain] Cd Length: 276 Bit Score: 325.24 E-value: 2.66e-112
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| Name | Accession | Description | Interval | E-value | |||||
| TIGR00096 | TIGR00096 | 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ... |
1-284 | 2.66e-112 | |||||
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: 325.24 E-value: 2.66e-112
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| RsmI | cd11648 | Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ... |
3-236 | 2.58e-86 | |||||
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: 256.93 E-value: 2.58e-86
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| RsmI | COG0313 | 16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ... |
2-236 | 3.25e-83 | |||||
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: 249.15 E-value: 3.25e-83
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| PRK14994 | PRK14994 | SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional |
2-273 | 5.38e-44 | |||||
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional Pssm-ID: 184956 Cd Length: 287 Bit Score: 151.14 E-value: 5.38e-44
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-219 | 1.03e-31 | |||||
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: 116.67 E-value: 1.03e-31
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| Name | Accession | Description | Interval | E-value | |||||
| TIGR00096 | TIGR00096 | 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ... |
1-284 | 2.66e-112 | |||||
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: 325.24 E-value: 2.66e-112
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| RsmI | cd11648 | Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ... |
3-236 | 2.58e-86 | |||||
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: 256.93 E-value: 2.58e-86
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| RsmI | COG0313 | 16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ... |
2-236 | 3.25e-83 | |||||
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: 249.15 E-value: 3.25e-83
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| RsmI_like | cd19918 | uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ... |
3-236 | 7.79e-50 | |||||
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: 163.86 E-value: 7.79e-50
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| RsmI_like | cd19917 | tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ... |
3-236 | 8.51e-48 | |||||
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: 158.66 E-value: 8.51e-48
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| PRK14994 | PRK14994 | SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional |
2-273 | 5.38e-44 | |||||
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional Pssm-ID: 184956 Cd Length: 287 Bit Score: 151.14 E-value: 5.38e-44
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-219 | 1.03e-31 | |||||
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: 116.67 E-value: 1.03e-31
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| RsmI_like | cd11649 | uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ... |
2-205 | 1.65e-26 | |||||
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: 103.66 E-value: 1.65e-26
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| TP_methylase | cd09815 | S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-189 | 9.61e-22 | |||||
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: 90.53 E-value: 9.61e-22
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| DHP5_DphB | cd11647 | diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-147 | 9.37e-04 | |||||
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells. Pssm-ID: 381174 Cd Length: 241 Bit Score: 39.71 E-value: 9.37e-04
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| Precorrin-6Y-MT | cd11644 | Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
10-130 | 9.80e-04 | |||||
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It 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. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B. Pssm-ID: 381171 [Multi-domain] Cd Length: 198 Bit Score: 39.40 E-value: 9.80e-04
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| TP_methylase | cd11724 | uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
2-134 | 8.60e-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: 36.76 E-value: 8.60e-03
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