16S rRNA (guanine(527)-N(7))-methyltransferase RsmG specifically methylates the N7 position of guanine in position 527 of 16S rRNA; requires the intact 30S subunit for methylation
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
2-221
2.17e-96
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification
:
Pssm-ID: 440126 Cd Length: 211 Bit Score: 280.50 E-value: 2.17e-96
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
2-221
2.17e-96
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440126 Cd Length: 211 Bit Score: 280.50 E-value: 2.17e-96
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
21-213
2.69e-63
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited division proteins these are probably involved in the regulation of cell devision. GidB has been shown to be a methyltransferase G specific to the rRNA small subunit. Previously identified as a glucose-inhibited division protein B that appears to be present and in a single copy in all complete eubacterial genomes so far sequenced. GidB specifically methylates the N7 position of a guanosine in 16S rRNA.
Pssm-ID: 396880 Cd Length: 184 Bit Score: 195.58 E-value: 2.69e-63
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
28-215
5.81e-55
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272928 Cd Length: 181 Bit Score: 173.98 E-value: 5.81e-55
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
72-172
2.85e-04
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 39.34 E-value: 2.85e-04
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
2-221
2.17e-96
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440126 Cd Length: 211 Bit Score: 280.50 E-value: 2.17e-96
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
21-213
2.69e-63
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited division proteins these are probably involved in the regulation of cell devision. GidB has been shown to be a methyltransferase G specific to the rRNA small subunit. Previously identified as a glucose-inhibited division protein B that appears to be present and in a single copy in all complete eubacterial genomes so far sequenced. GidB specifically methylates the N7 position of a guanosine in 16S rRNA.
Pssm-ID: 396880 Cd Length: 184 Bit Score: 195.58 E-value: 2.69e-63
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
28-215
5.81e-55
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272928 Cd Length: 181 Bit Score: 173.98 E-value: 5.81e-55
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
72-172
2.85e-04
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 39.34 E-value: 2.85e-04
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.
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