NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1777026778|ref|WP_154169703|]
View 

MULTISPECIES: 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG [Vibrio]

Protein Classification

16S rRNA (guanine(527)-N(7))-methyltransferase RsmG( domain architecture ID 10001247)

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

CATH:  3.40.50.150
EC:  2.1.1.170
Gene Ontology:  GO:0070043

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 4-210 1.68e-98

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: 284.35  E-value: 1.68e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778   4 LRSKLDALIAQTDLVVSDQQREQLVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYL--QGQRFIDVGTGPGL 81
Cdd:COG0357     1 LAELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLpkEGARVLDVGSGAGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  82 PGIPLAIMNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLpCAK 161
Cdd:COG0357    81 PGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELAPREKFDVVTARAVAPLPDLLELALPL-LKP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1777026778 162 QGVFLALKGQRPQEELNSLPE-WCSVIDIKALKVPELEGERHLVILSRKG 210
Cdd:COG0357   160 GGRLLALKGPDAEEELAEAPKaLKVLEEVEELTLPGLDAERHLVVIKKIK 209
 
Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 4-210 1.68e-98

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: 284.35  E-value: 1.68e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778   4 LRSKLDALIAQTDLVVSDQQREQLVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYL--QGQRFIDVGTGPGL 81
Cdd:COG0357     1 LAELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLpkEGARVLDVGSGAGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  82 PGIPLAIMNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLpCAK 161
Cdd:COG0357    81 PGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELAPREKFDVVTARAVAPLPDLLELALPL-LKP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1777026778 162 QGVFLALKGQRPQEELNSLPE-WCSVIDIKALKVPELEGERHLVILSRKG 210
Cdd:COG0357   160 GGRLLALKGPDAEEELAEAPKaLKVLEEVEELTLPGLDAERHLVVIKKIK 209
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 23-204 7.95e-76

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: 226.01  E-value: 7.95e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  23 QREQLVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYLQGQR--FIDVGTGPGLPGIPLAIMNPDRQFVLLDS 100
Cdd:pfam02527   1 QIEKLKRYLQLLLKWNKRYNLTSITEPNELLERHLLDSLVVLEYLDNDRdhVLDVGSGAGFPGIPLAIARPDKKVTLLES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778 101 LGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLPcAKQGVFLALKGQRPQEELNSL 180
Cdd:pfam02527  81 LLKKINFLEEVKSELGLDNVTIVHARAEEYQPEEQYDVITSRAVASLNELTEWTLPLL-KPGGYFLAYKGKQAEDELEEL 159

                         170       180
                  ....*....|....*....|....*
gi 1777026778 181 PEWCSVIDIKALKVPEL-EGERHLV 204
Cdd:pfam02527 160 DKACQVLGVEVLSVPSLgAGDRHLV 184
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 27-206 2.34e-67

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: 204.41  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  27 LVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYLQGQRFIDVGTGPGLPGIPLAIMNPDRQFVLLDSLGKRIR 106
Cdd:TIGR00138   1 LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLALLPYLDGKRVIDIGSGAGFPGIPLAIARPELKLTLLESNHKKVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778 107 FIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLPcAKQGVFLALKGQRPQEELNSLPEWCSV 186
Cdd:TIGR00138  81 FLREVKAELGLNNVEIVNGRAEDYQHEEQFDIITSRALASLNVLLELTLNLL-KVGGYFLAYKGKKYLDEIEEAKEKIQV 159

                         170       180
                  ....*....|....*....|.
gi 1777026778 187 IDIKALKVPELEG-ERHLVIL 206
Cdd:TIGR00138 160 LGVEPLEVPPLTGpDRHLVVL 180
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-143 8.53e-06

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: 43.19  E-value: 8.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777026778  71 RFIDVGTGPGLPGIPLAImNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHG--FDGVLSRA 143
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADesFDVIISDP 74
 
Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 4-210 1.68e-98

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: 284.35  E-value: 1.68e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778   4 LRSKLDALIAQTDLVVSDQQREQLVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYL--QGQRFIDVGTGPGL 81
Cdd:COG0357     1 LAELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLpkEGARVLDVGSGAGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  82 PGIPLAIMNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLpCAK 161
Cdd:COG0357    81 PGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELAPREKFDVVTARAVAPLPDLLELALPL-LKP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1777026778 162 QGVFLALKGQRPQEELNSLPE-WCSVIDIKALKVPELEGERHLVILSRKG 210
Cdd:COG0357   160 GGRLLALKGPDAEEELAEAPKaLKVLEEVEELTLPGLDAERHLVVIKKIK 209
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 23-204 7.95e-76

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: 226.01  E-value: 7.95e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  23 QREQLVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYLQGQR--FIDVGTGPGLPGIPLAIMNPDRQFVLLDS 100
Cdd:pfam02527   1 QIEKLKRYLQLLLKWNKRYNLTSITEPNELLERHLLDSLVVLEYLDNDRdhVLDVGSGAGFPGIPLAIARPDKKVTLLES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778 101 LGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLPcAKQGVFLALKGQRPQEELNSL 180
Cdd:pfam02527  81 LLKKINFLEEVKSELGLDNVTIVHARAEEYQPEEQYDVITSRAVASLNELTEWTLPLL-KPGGYFLAYKGKQAEDELEEL 159

                         170       180
                  ....*....|....*....|....*
gi 1777026778 181 PEWCSVIDIKALKVPEL-EGERHLV 204
Cdd:pfam02527 160 DKACQVLGVEVLSVPSLgAGDRHLV 184
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 27-206 2.34e-67

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: 204.41  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  27 LVGYVELLNKWNKAYNLTSVRDPQEMLVKHILDSIVVSPYLQGQRFIDVGTGPGLPGIPLAIMNPDRQFVLLDSLGKRIR 106
Cdd:TIGR00138   1 LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLALLPYLDGKRVIDIGSGAGFPGIPLAIARPELKLTLLESNHKKVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778 107 FIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLSRAFASMLDMVEWCHHLPcAKQGVFLALKGQRPQEELNSLPEWCSV 186
Cdd:TIGR00138  81 FLREVKAELGLNNVEIVNGRAEDYQHEEQFDIITSRALASLNVLLELTLNLL-KVGGYFLAYKGKKYLDEIEEAKEKIQV 159

                         170       180
                  ....*....|....*....|.
gi 1777026778 187 IDIKALKVPELEG-ERHLVIL 206
Cdd:TIGR00138 160 LGVEPLEVPPLTGpDRHLVVL 180
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-143 8.53e-06

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: 43.19  E-value: 8.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777026778  71 RFIDVGTGPGLPGIPLAImNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHG--FDGVLSRA 143
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADesFDVIISDP 74
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
68-143 1.06e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777026778  68 QGQRFIDVGTGPGLPGIPLAIMNPDRQFVLLDSLGKRIRFIKQvlhelRIDNVTALQSRVEEFKPEHGFDGVLSRA 143
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARA-----RLPNVRFVVADLRDLDPPEPFDLVVSNA 71
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 69-141 3.63e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 36.80  E-value: 3.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777026778  69 GQRFIDVGTGPGLPGIPLAIMNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFKPEHGFDGVLS 141
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIIS 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 69-144 6.56e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 35.86  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777026778  69 GQRFIDVGTGPGLPGIPLA-IMNPDRQFVLLDSLGKRIRFIKQVLHELRIDNVTALQSRVEEFK---PEHGFDGVLSRAF 144
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPellEDDKFDVVISNCV 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH