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Conserved domains on  [gi|1473385972|ref|WP_117849605|]
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MULTISPECIES: 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG [Clostridia]

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, ...
 7-227 6.90e-100

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: 289.36  E-value: 6.90e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972   7 LFEKGLEELGIALSQDQKKQFITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNFDqnklaGKSVIDIGTGA 86
Cdd:COG0357     4 LLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKE-----GARVLDVGSGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  87 GFPGIPLKIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYAkqkeHREKYDFCVSRAVANLSTLSEYCI 166
Cdd:COG0357    79 GFPGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELA----PREKFDVVTARAVAPLPDLLELAL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473385972 167 PFVKEGGSFISYKSGKIDEELTQAENAVKILggkvQDVVKFPLMDTDMDRSFVVIKKVKPT 227
Cdd:COG0357   155 PLLKPGGRLLALKGPDAEEELAEAPKALKVL----EEVEELTLPGLDAERHLVVIKKIKRT 211
 
Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 7-227 6.90e-100

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: 289.36  E-value: 6.90e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972   7 LFEKGLEELGIALSQDQKKQFITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNFDqnklaGKSVIDIGTGA 86
Cdd:COG0357     4 LLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKE-----GARVLDVGSGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  87 GFPGIPLKIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYAkqkeHREKYDFCVSRAVANLSTLSEYCI 166
Cdd:COG0357    79 GFPGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELA----PREKFDVVTARAVAPLPDLLELAL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473385972 167 PFVKEGGSFISYKSGKIDEELTQAENAVKILggkvQDVVKFPLMDTDMDRSFVVIKKVKPT 227
Cdd:COG0357   155 PLLKPGGRLLALKGPDAEEELAEAPKALKVL----EEVEELTLPGLDAERHLVVIKKIKRT 211
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 23-207 3.49e-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: 192.88  E-value: 3.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  23 QKKQFITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNFDQNKlagksVIDIGTGAGFPGIPLKIAFPELKI 102
Cdd:pfam02527   1 QIEKLKRYLQLLLKWNKRYNLTSITEPNELLERHLLDSLVVLEYLDNDRDH-----VLDVGSGAGFPGIPLAIARPDKKV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972 103 TLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYakqkEHREKYDFCVSRAVANLSTLSEYCIPFVKEGGSFISYKSGK 182
Cdd:pfam02527  76 TLLESLLKKINFLEEVKSELGLDNVTIVHARAEEY----QPEEQYDVITSRAVASLNELTEWTLPLLKPGGYFLAYKGKQ 151

                         170       180
                  ....*....|....*....|....*
gi 1473385972 183 IDEELTQAENAVKILGGKVQDVVKF 207
Cdd:pfam02527 152 AEDELEELDKACQVLGVEVLSVPSL 176
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 27-222 6.84e-62

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: 192.09  E-value: 6.84e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  27 FITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNfdqnklaGKSVIDIGTGAGFPGIPLKIAFPELKITLLD 106
Cdd:TIGR00138   1 LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLALLPYLD-------GKRVIDIGSGAGFPGIPLAIARPELKLTLLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972 107 SLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYakqkEHREKYDFCVSRAVANLSTLSEYCIPFVKEGGSFISYKSGKIDEE 186
Cdd:TIGR00138  74 SNHKKVAFLREVKAELGLNNVEIVNGRAEDY----QHEEQFDIITSRALASLNVLLELTLNLLKVGGYFLAYKGKKYLDE 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1473385972 187 LTQAENAVKILGGKVQDVVKFplmdTDMDRSFVVIK 222
Cdd:TIGR00138 150 IEEAKEKIQVLGVEPLEVPPL----TGPDRHLVVLK 181
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 79-155 1.34e-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: 40.11  E-value: 1.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473385972  79 VIDIGTGAGFPGIPLkIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYakQKEHREKYDFCVSRAV 155
Cdd:cd02440     2 VLDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL--PPEADESFDVIISDPP 75
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
77-134 2.96e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 37.67  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1473385972  77 KSVIDIGTGAGFPGIPLKIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRA 134
Cdd:PRK08287   33 KHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIPGEA 90
 
Name Accession Description Interval E-value
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 7-227 6.90e-100

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: 289.36  E-value: 6.90e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972   7 LFEKGLEELGIALSQDQKKQFITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNFDqnklaGKSVIDIGTGA 86
Cdd:COG0357     4 LLEEGLAELGLELSEEQLEQLEAYLELLLKWNKKINLTAIRDPEELWERHILDSLALLPLLPKE-----GARVLDVGSGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  87 GFPGIPLKIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYAkqkeHREKYDFCVSRAVANLSTLSEYCI 166
Cdd:COG0357    79 GFPGIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVVHGRAEELA----PREKFDVVTARAVAPLPDLLELAL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473385972 167 PFVKEGGSFISYKSGKIDEELTQAENAVKILggkvQDVVKFPLMDTDMDRSFVVIKKVKPT 227
Cdd:COG0357   155 PLLKPGGRLLALKGPDAEEELAEAPKALKVL----EEVEELTLPGLDAERHLVVIKKIKRT 211
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 23-207 3.49e-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: 192.88  E-value: 3.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  23 QKKQFITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNFDQNKlagksVIDIGTGAGFPGIPLKIAFPELKI 102
Cdd:pfam02527   1 QIEKLKRYLQLLLKWNKRYNLTSITEPNELLERHLLDSLVVLEYLDNDRDH-----VLDVGSGAGFPGIPLAIARPDKKV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972 103 TLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYakqkEHREKYDFCVSRAVANLSTLSEYCIPFVKEGGSFISYKSGK 182
Cdd:pfam02527  76 TLLESLLKKINFLEEVKSELGLDNVTIVHARAEEY----QPEEQYDVITSRAVASLNELTEWTLPLLKPGGYFLAYKGKQ 151

                         170       180
                  ....*....|....*....|....*
gi 1473385972 183 IDEELTQAENAVKILGGKVQDVVKF 207
Cdd:pfam02527 152 AEDELEELDKACQVLGVEVLSVPSL 176
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 27-222 6.84e-62

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: 192.09  E-value: 6.84e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  27 FITYYEYLVEKNKVMNLTAITEYEEVILKHFLDSLSIVKVSNfdqnklaGKSVIDIGTGAGFPGIPLKIAFPELKITLLD 106
Cdd:TIGR00138   1 LLAYLELLQKWNQRFNLTSIKTPEEIWQRHILDSLALLPYLD-------GKRVIDIGSGAGFPGIPLAIARPELKLTLLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972 107 SLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYakqkEHREKYDFCVSRAVANLSTLSEYCIPFVKEGGSFISYKSGKIDEE 186
Cdd:TIGR00138  74 SNHKKVAFLREVKAELGLNNVEIVNGRAEDY----QHEEQFDIITSRALASLNVLLELTLNLLKVGGYFLAYKGKKYLDE 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1473385972 187 LTQAENAVKILGGKVQDVVKFplmdTDMDRSFVVIK 222
Cdd:TIGR00138 150 IEEAKEKIQVLGVEPLEVPPL----TGPDRHLVVLK 181
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 58-152 1.10e-05

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: 44.50  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  58 LDSLSIVKVSNFDQNkLAGKsVIDIGTGAGFPGIPLKIAFPELKITLLDsLNKR-VNFLNEVIEMLGLKNVTAVHGRAed 136
Cdd:pfam05175  16 LDIGSRLLLEHLPKD-LSGK-VLDLGCGAGVLGAALAKESPDAELTMVD-INARaLESARENLAANGLENGEVVASDV-- 90

                          90
                  ....*....|....*.
gi 1473385972 137 YAKQKEhrEKYDFCVS 152
Cdd:pfam05175  91 YSGVED--GKFDLIIS 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 75-177 5.93e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.02  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  75 AGKSVIDIGTGAGFPGIPL-KIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDyAKQKEHREKYDFCVSR 153
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEE-LPELLEDDKFDVVISN 81

                          90       100
                  ....*....|....*....|....*...
gi 1473385972 154 AVANLSTLSEYCI----PFVKEGGSFIS 177
Cdd:pfam13847  82 CVLNHIPDPDKVLqeilRVLKPGGRLII 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 79-155 1.34e-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: 40.11  E-value: 1.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473385972  79 VIDIGTGAGFPGIPLkIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRAEDYakQKEHREKYDFCVSRAV 155
Cdd:cd02440     2 VLDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL--PPEADESFDVIISDPP 75
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 75-152 1.71e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 38.59  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473385972  75 AGKSVIDIGTGAGFpgIPLKIA--FPELKITLLDsLNKR-VNFLNEVIEMLGLKN-VTAVHGRAEDYAKQKEhREKYDFC 150
Cdd:COG4123    37 KGGRVLDLGTGTGV--IALMLAqrSPGARITGVE-IQPEaAELARRNVALNGLEDrITVIHGDLKEFAAELP-PGSFDLV 112


                  ..
gi 1473385972 151 VS 152
Cdd:COG4123   113 VS 114
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 52-126 2.37e-03

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 37.70  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1473385972  52 VILKHFLDSLSIvkvSNFDQNKLAGKSVIDIGTGAGFPGIPLKIAFPELKITLLDsLNKRVNFLNEVIEMLGLKN 126
Cdd:pfam10294  26 VVLSKYLEMKIF---KELGANNLSGLNVLELGSGTGLVGIAVALLLPGASVTITD-LEEALELLKKNIELNALSS 96
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
77-134 2.96e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 37.67  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1473385972  77 KSVIDIGTGAGFPGIPLKIAFPELKITLLDSLNKRVNFLNEVIEMLGLKNVTAVHGRA 134
Cdd:PRK08287   33 KHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIPGEA 90
 
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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