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Conserved domains on  [gi|496264360|ref|WP_008977745|]
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16S rRNA (guanine(527)-N(7))-methyltransferase RsmG [Longicatena caecimuris]

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

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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, ...
7-220 3.62e-88

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: 259.31  E-value: 3.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   7 KEDFFHVVKSYGITLQDTQLQQFAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSILPSFDVKLKG-TFCDVGAGAGFP 85
Cdd:COG0357    2 AELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKEGaRVLDVGSGAGFP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  86 SIPLKIVYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDYAkeHRESFDIVSARAVANLTMLSELCIPLVKV 165
Cdd:COG0357   82 GIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELA--PREKFDVVTARAVAPLPDLLELALPLLKP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496264360 166 GGMFLALKGANAQEEYALAEKAIRLLgceEKRRDEKVLSDGSKRVNFVFEKVKKT 220
Cdd:COG0357  160 GGRLLALKGPDAEEELAEAPKALKVL---EEVEELTLPGLDAERHLVVIKKIKRT 211
 
Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
7-220 3.62e-88

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: 259.31  E-value: 3.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   7 KEDFFHVVKSYGITLQDTQLQQFAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSILPSFDVKLKG-TFCDVGAGAGFP 85
Cdd:COG0357    2 AELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKEGaRVLDVGSGAGFP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  86 SIPLKIVYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDYAkeHRESFDIVSARAVANLTMLSELCIPLVKV 165
Cdd:COG0357   82 GIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELA--PREKFDVVTARAVAPLPDLLELALPLLKP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496264360 166 GGMFLALKGANAQEEYALAEKAIRLLgceEKRRDEKVLSDGSKRVNFVFEKVKKT 220
Cdd:COG0357  160 GGRLLALKGPDAEEELAEAPKALKVL---EEVEELTLPGLDAERHLVVIKKIKRT 211
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
25-197 7.28e-62

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: 191.73  E-value: 7.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   25 QLQQFAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSILPSFDVK-LKGTFCDVGAGAGFPSIPLKIVYPDLEITIVET 103
Cdd:pfam02527   1 QIEKLKRYLQLLLKWNKRYNLTSITEPNELLERHLLDSLVVLEYLDnDRDHVLDVGSGAGFPGIPLAIARPDKKVTLLES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  104 LGKRITFLEALCHQLKLNNVHCVHARAEDYakEHRESFDIVSARAVANLTMLSELCIPLVKVGGMFLALKGANAQEEYAL 183
Cdd:pfam02527  81 LLKKINFLEEVKSELGLDNVTIVHARAEEY--QPEEQYDVITSRAVASLNELTEWTLPLLKPGGYFLAYKGKQAEDELEE 158
                         170
                  ....*....|....
gi 496264360  184 AEKAIRLLGCEEKR 197
Cdd:pfam02527 159 LDKACQVLGVEVLS 172
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
29-192 3.77e-59

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: 184.77  E-value: 3.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   29 FAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSI--LPSFDVKlkgTFCDVGAGAGFPSIPLKIVYPDLEITIVETLGK 106
Cdd:TIGR00138   1 LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLalLPYLDGK---RVIDIGSGAGFPGIPLAIARPELKLTLLESNHK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  107 RITFLEALCHQLKLNNVHCVHARAEDYakEHRESFDIVSARAVANLTMLSELCIPLVKVGGMFLALKGANAQEEYALAEK 186
Cdd:TIGR00138  78 KVAFLREVKAELGLNNVEIVNGRAEDY--QHEEQFDIITSRALASLNVLLELTLNLLKVGGYFLAYKGKKYLDEIEEAKE 155

                  ....*.
gi 496264360  187 AIRLLG 192
Cdd:TIGR00138 156 KIQVLG 161
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
74-167 1.05e-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: 40.49  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  74 TFCDVGAGAGFPSIPLKIvYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDYAKEHRESFDIVSARAVANLT 153
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79
                         90
                 ....*....|....*....
gi 496264360 154 MLS-----ELCIPLVKVGG 167
Cdd:cd02440   80 VEDlarflEEARRLLKPGG 98
 
Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
7-220 3.62e-88

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: 259.31  E-value: 3.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   7 KEDFFHVVKSYGITLQDTQLQQFAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSILPSFDVKLKG-TFCDVGAGAGFP 85
Cdd:COG0357    2 AELLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKEGaRVLDVGSGAGFP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  86 SIPLKIVYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDYAkeHRESFDIVSARAVANLTMLSELCIPLVKV 165
Cdd:COG0357   82 GIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELA--PREKFDVVTARAVAPLPDLLELALPLLKP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496264360 166 GGMFLALKGANAQEEYALAEKAIRLLgceEKRRDEKVLSDGSKRVNFVFEKVKKT 220
Cdd:COG0357  160 GGRLLALKGPDAEEELAEAPKALKVL---EEVEELTLPGLDAERHLVVIKKIKRT 211
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
25-197 7.28e-62

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: 191.73  E-value: 7.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   25 QLQQFAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSILPSFDVK-LKGTFCDVGAGAGFPSIPLKIVYPDLEITIVET 103
Cdd:pfam02527   1 QIEKLKRYLQLLLKWNKRYNLTSITEPNELLERHLLDSLVVLEYLDnDRDHVLDVGSGAGFPGIPLAIARPDKKVTLLES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  104 LGKRITFLEALCHQLKLNNVHCVHARAEDYakEHRESFDIVSARAVANLTMLSELCIPLVKVGGMFLALKGANAQEEYAL 183
Cdd:pfam02527  81 LLKKINFLEEVKSELGLDNVTIVHARAEEY--QPEEQYDVITSRAVASLNELTEWTLPLLKPGGYFLAYKGKQAEDELEE 158
                         170
                  ....*....|....
gi 496264360  184 AEKAIRLLGCEEKR 197
Cdd:pfam02527 159 LDKACQVLGVEVLS 172
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
29-192 3.77e-59

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: 184.77  E-value: 3.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   29 FAMYAAMLLEWNQKMNLTAITDMDEIYEKHFLDSI--LPSFDVKlkgTFCDVGAGAGFPSIPLKIVYPDLEITIVETLGK 106
Cdd:TIGR00138   1 LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLalLPYLDGK---RVIDIGSGAGFPGIPLAIARPELKLTLLESNHK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  107 RITFLEALCHQLKLNNVHCVHARAEDYakEHRESFDIVSARAVANLTMLSELCIPLVKVGGMFLALKGANAQEEYALAEK 186
Cdd:TIGR00138  78 KVAFLREVKAELGLNNVEIVNGRAEDY--QHEEQFDIITSRALASLNVLLELTLNLLKVGGYFLAYKGKKYLDEIEEAKE 155

                  ....*.
gi 496264360  187 AIRLLG 192
Cdd:TIGR00138 156 KIQVLG 161
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
74-167 1.05e-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: 40.49  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  74 TFCDVGAGAGFPSIPLKIvYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDYAKEHRESFDIVSARAVANLT 153
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79
                         90
                 ....*....|....*....
gi 496264360 154 MLS-----ELCIPLVKVGG 167
Cdd:cd02440   80 VEDlarflEEARRLLKPGG 98
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
64-145 1.53e-04

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: 41.04  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360   64 LPSFDVKLKGTFCDVGAGAGFPSIPLKIVYPDLEITIVETLGKRITFLEAlchQLKLNNVHCVHARAED-YAKEHRESFD 142
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARE---NLAANGLENGEVVASDvYSGVEDGKFD 100

                  ....
gi 496264360  143 -IVS 145
Cdd:pfam05175 101 lIIS 104
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
64-145 2.38e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 37.86  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  64 LPSFDVKLKGTFCDVGAGAGFPSIPLKIVYPDLEITIVEtlgkrITF--LEALCHQLKLNNVHCVHARAED-YAKEHRES 140
Cdd:COG2813   42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVD-----VNAraVELARANAAANGLENVEVLWSDgLSGVPDGS 116

                 ....*.
gi 496264360 141 FD-IVS 145
Cdd:COG2813  117 FDlILS 122
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
77-149 3.10e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.19  E-value: 3.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496264360   77 DVGAGAGFPSIPLKIVYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDYAKEHRESFDIVSARAV 149
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNV 74
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
55-149 4.82e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 36.82  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  55 YEKHFLDSILPSFDVKLK--------GTFCDVGAGAGFPSIPLkivypdleitiVETLGKR----------ITFLEALCH 116
Cdd:COG0500    2 WDSYYSDELLPGLAALLAllerlpkgGRVLDLGCGTGRNLLAL-----------AARFGGRvigidlspeaIALARARAA 70
                         90       100       110
                 ....*....|....*....|....*....|...
gi 496264360 117 QLKLNNVHCVHARAEDYAKEHRESFDIVSARAV 149
Cdd:COG0500   71 KAGLGNVEFLVADLAELDPLPAESFDLVVAFGV 103
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
74-171 5.73e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 37.45  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264360  74 TFCDVGAGAGfpSIPLKI--VYPDLEITIVETLGKRITFLEALCHQLKLNNVHCVHARAEDyAKEHRESFDIV----SAR 147
Cdd:COG2242  250 VLWDIGAGSG--SVSIEAarLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPE-ALADLPDPDAVfiggSGG 326
                         90       100
                 ....*....|....*....|....
gi 496264360 148 avaNLTMLSELCIPLVKVGGMFLA 171
Cdd:COG2242  327 ---NLPEILEACWARLRPGGRLVA 347
 
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.
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