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Conserved domains on  [gi|499232240|ref|WP_010929780|]
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16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Bordetella pertussis]

Protein Classification

16S rRNA (cytidine(1402)-2'-O)-methyltransferase( domain architecture ID 10001055)

16S rRNA (cytidine(1402)-2'-O)-methyltransferase uses assembled 30S subunit as a substrate and catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA

EC:  2.1.1.198
Gene Symbol:  rsmI
SCOP:  4000056

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
31-253 2.54e-113

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: 326.58  E-value: 2.54e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  31 LYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDA 110
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFE 190
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDR---FAFEGFLPRKKKERRKRLKELEAEPRTLIFYE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499232240 191 SPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAADWLAADAHRgqGEFVLIVH 253
Cdd:COG0313  158 SPHRLAKTLEDLAEVLGPDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPK--GEFVLVIE 218
 
Name Accession Description Interval E-value
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
31-253 2.54e-113

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: 326.58  E-value: 2.54e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  31 LYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDA 110
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFE 190
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDR---FAFEGFLPRKKKERRKRLKELEAEPRTLIFYE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499232240 191 SPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAADWLAADAHRgqGEFVLIVH 253
Cdd:COG0313  158 SPHRLAKTLEDLAEVLGPDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPK--GEFVLVIE 218
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
32-253 6.28e-104

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: 302.77  E-value: 6.28e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  32 YVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDAG 111
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 112 APAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFES 191
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDR---FTFLGFLPRKKGKRKKLLEELAEEPRTLIFYES 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499232240 192 PHRLAATLADLREAGGPARlLTVARELTKRFEEIATMPLGEAADWLAADAHRgqGEFVLIVH 253
Cdd:cd11648  158 PHRILKTLEDLAEVGGDRE-VVVARELTKLHEEVIRGTLSELLEELEENKPK--GEFVLVVE 216
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
28-311 3.71e-75

SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional


Pssm-ID: 184956  Cd Length: 287  Bit Score: 232.03  E-value: 3.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  28 AATLYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALV 107
Cdd:PRK14994  11 QGQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 108 SDAGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVV 187
Cdd:PRK14994  91 SDAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDR---FCYEGFLPAKSKGRRDALKALEAEPRTLI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 188 MFESPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAADWLAADAHRGQGEFVLIVhQAPGAQDDEADPAD 267
Cdd:PRK14994 168 FYESTHRLLDSLEDIVAVLGESRYVVLARELTKTWETIHGAPVGELLAWVKEDENRRKGEMVLIV-EGHKAQEDDLPADA 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499232240 268 PRTDALLDAlleSLSVRDAARVAAKVTGLARDVLYARALARKEQ 311
Cdd:PRK14994 247 LRTLALLQA---ELPLKKAAALAAEIHGVKKNALYKYALEQQGE 287
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
31-302 1.94e-47

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: 160.37  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240   31 LYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDA 110
Cdd:TIGR00096   2 LYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIAVSSDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSdenPAFAFAGFLPAKAVARQRwLRQWCALP-APVVMF 189
Cdd:TIGR00096  82 GPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPAT---DRFFFGGFLPKKSKRRQA-LKAYIAEErTTVFFY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  190 ESPHRLAATLADLREAGGPARLLTVARELTKrFEEIATMPLGE-AADWLAADAHRGQGEFVLIVHQAPGAQDDEADPADP 268
Cdd:TIGR00096 158 ESHHRLLTTLTDLNVFLGSERFVGAAELTKK-ESEYWFGTVGQlLPDITEDTNNRKGGEVILIINGHKPQEECSDLQALA 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 499232240  269 RTDALLdaLLESLSVRD-AARVAAKVTGLARDVLY 302
Cdd:TIGR00096 237 LEILAL--LQAEVLLKKaAAYIAAEMTLKKNKLLY 269
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
30-234 7.46e-30

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: 112.44  E-value: 7.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240   30 TLYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLD-AWGVSTPLMAA----HRHNEASAAQAICERLAQGQRV 104
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDlLPEDLYFPMTEdkepLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  105 ALVSdAGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDENPAFAFAGFLPAKAVARQRWLRQWCALPA 184
Cdd:pfam00590  81 ARLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLEALLANGD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 499232240  185 PVVMFESPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAA 234
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
31-253 2.54e-113

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: 326.58  E-value: 2.54e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  31 LYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDA 110
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFE 190
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDR---FAFEGFLPRKKKERRKRLKELEAEPRTLIFYE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499232240 191 SPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAADWLAADAHRgqGEFVLIVH 253
Cdd:COG0313  158 SPHRLAKTLEDLAEVLGPDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPK--GEFVLVIE 218
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
32-253 6.28e-104

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: 302.77  E-value: 6.28e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  32 YVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDAG 111
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 112 APAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFES 191
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDR---FTFLGFLPRKKGKRKKLLEELAEEPRTLIFYES 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499232240 192 PHRLAATLADLREAGGPARlLTVARELTKRFEEIATMPLGEAADWLAADAHRgqGEFVLIVH 253
Cdd:cd11648  158 PHRILKTLEDLAEVGGDRE-VVVARELTKLHEEVIRGTLSELLEELEENKPK--GEFVLVVE 216
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
28-311 3.71e-75

SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional


Pssm-ID: 184956  Cd Length: 287  Bit Score: 232.03  E-value: 3.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  28 AATLYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALV 107
Cdd:PRK14994  11 QGQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 108 SDAGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVV 187
Cdd:PRK14994  91 SDAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDR---FCYEGFLPAKSKGRRDALKALEAEPRTLI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 188 MFESPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAADWLAADAHRGQGEFVLIVhQAPGAQDDEADPAD 267
Cdd:PRK14994 168 FYESTHRLLDSLEDIVAVLGESRYVVLARELTKTWETIHGAPVGELLAWVKEDENRRKGEMVLIV-EGHKAQEDDLPADA 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499232240 268 PRTDALLDAlleSLSVRDAARVAAKVTGLARDVLYARALARKEQ 311
Cdd:PRK14994 247 LRTLALLQA---ELPLKKAAALAAEIHGVKKNALYKYALEQQGE 287
RsmI_like cd19918
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
32-253 4.89e-71

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: 218.94  E-value: 4.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  32 YVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDAG 111
Cdd:cd19918    1 YIVATPIGNYDDITLRALEVLKEVDVIICEEFKEGSRLLKKLIIEKELLLLNEHNEKEDAAELLDLLAQGKSVALISDCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 112 APAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFES 191
Cdd:cd19918   81 TPVFADPGALLVKLCIQKGIPVVPVPGASSLMAALSVSGFKIDR---FLFAGFLPRKKEERRRELKRLKSEKRPIVLMDT 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499232240 192 PHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAadWLAADAHRGQGEFVLIVH 253
Cdd:cd19918  158 PYRLKKLLEDLAKVFGPNRRIVLAYNLTLPDEKILRGTLAEI--LKKVEEKPLKGEFVLIIH 217
RsmI_like cd19917
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ...
32-252 4.34e-64

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: 201.42  E-value: 4.34e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  32 YVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWG-VSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDA 110
Cdd:cd19917    1 YLVATPIGNTDDITLRALETLKAVDLIICEDTRNASRLLKHVGiIGKTLEVLNEHNTPEDIQELLDKLAGGKNVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpaFAFAGFLPAKAVARQRWLRQWCALPAPVVMFE 190
Cdd:cd19917   81 GTPAFADPGADLVKLCRDAGIPVVPLPGASSLMTALSASGLKSDR---FLFYGFLPAEPGERKKALKALEQEPRTLIFME 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499232240 191 SPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEaadWLAADAHRGQGEFVLIV 252
Cdd:cd19917  158 TPYRLKKTLEDLAAVFGPNRKVVLARNLTQEEETILTGTLGE---LLNKIPELPKGEFVLLL 216
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
31-302 1.94e-47

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: 160.37  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240   31 LYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDA 110
Cdd:TIGR00096   2 LYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIAVSSDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSdenPAFAFAGFLPAKAVARQRwLRQWCALP-APVVMF 189
Cdd:TIGR00096  82 GPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPAT---DRFFFGGFLPKKSKRRQA-LKAYIAEErTTVFFY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  190 ESPHRLAATLADLREAGGPARLLTVARELTKrFEEIATMPLGE-AADWLAADAHRGQGEFVLIVHQAPGAQDDEADPADP 268
Cdd:TIGR00096 158 ESHHRLLTTLTDLNVFLGSERFVGAAELTKK-ESEYWFGTVGQlLPDITEDTNNRKGGEVILIINGHKPQEECSDLQALA 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 499232240  269 RTDALLdaLLESLSVRD-AARVAAKVTGLARDVLY 302
Cdd:TIGR00096 237 LEILAL--LQAEVLLKKaAAYIAAEMTLKKNKLLY 269
RsmI_like cd11649
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
31-232 5.53e-38

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: 134.48  E-value: 5.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  31 LYVIATPIGNLGDLG---LRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAH-----RHNEASAAQAICERLAQGQ 102
Cdd:cd11649    1 LYLIPTPLGEESPDEvlpPEVLEIIRSLDHFIVENEKTARRFLKKLGPPKPIDELTffelnKHTREEDLEELLKPLLEGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 103 RVALVSDAGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDenpAFAFAGFLPAKAVARQRWLRQWCAL 182
Cdd:cd11649   81 DIGLISEAGCPGVADPGAELVALAHRLGIKVVPLVGPSSILLALMASGLNGQ---NFAFHGYLPIDKEERKKKLKELEKR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499232240 183 PAP-----VVMfESPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGE 232
Cdd:cd11649  158 SRKegqtqIFI-ETPYRNNALLEDLLKTLQPDTRLCVACDLTGPSEFIKTKTIAE 211
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
30-234 7.46e-30

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: 112.44  E-value: 7.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240   30 TLYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLD-AWGVSTPLMAA----HRHNEASAAQAICERLAQGQRV 104
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDlLPEDLYFPMTEdkepLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  105 ALVSdAGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDENPAFAFAGFLPAKAVARQRWLRQWCALPA 184
Cdd:pfam00590  81 ARLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLEALLANGD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 499232240  185 PVVMFESPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAA 234
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
34-252 1.97e-24

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: 98.23  E-value: 1.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  34 IATPIGNLGDLGLRAWQALVRADVIAAEDTRASR---TLLDAWGVSTPLMAAHRHN-EASAAQAICERLAQGQRVALVSd 109
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLlslVLRAILKDGKRIYDLHDPNvEEEMAELLLEEARQGKDVAFLS- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240 110 AGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDEnpAFAFAGFLPAKAVARQRWLRQWCALPAPVVMF 189
Cdd:cd09815   80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGE--SFLFVTASDLLENPRLLVLKALAKERRHLVLF 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499232240 190 ESPHRLAATLADL-REAGGPARLLTVARELTKRFEEIATMPLGEaadWLAADAHRGQGEFVLIV 252
Cdd:cd09815  158 LDGHRFLKALERLlKELGEDDTPVVLVANAGSEGEVIRTGTVKE---LRAERTERGKPLTTILV 218
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
46-145 8.67e-06

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


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 45.86  E-value: 8.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  46 LRAWQALVRADVIAAEDTRAS-----RTLLDAWGVSTPLMAAH---RHNEA-------SAAQAICERLAQGQRVALVSdA 110
Cdd:COG2243   20 LKAVRALREADVIAYPAKGAGkaslaREIVAPYLPPARIVELVfpmTTDYEalvaawdEAAARIAEELEAGRDVAFLT-E 98
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499232240 111 GAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAA 145
Cdd:COG2243   99 GDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAA 133
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
31-145 6.38e-05

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: 43.70  E-value: 6.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  31 LYVIATPIGNLGDLGLRAWQALVRADVIAA-EDTR-------ASRTLLDAWGVSTPLMAAHRHN--------------EA 88
Cdd:cd11724    2 LYLVGVGPGDPDLITLRALKAIKKADVVFApPDLRkrfaeylAGKEVLDDPHGLFTYYGKKCSPleeaekeceelekqRA 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499232240  89 SAAQAICERLAQGQRVALVsDAGAPAVSDPGARIVRAVREAgYAVVpVPGPSAVIAA 145
Cdd:cd11724   82 EIVQKIREALAQGKNVALL-DSGDPTIYGPWIWYLEEFADL-NPEV-IPGVSSFNAA 135
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
46-145 2.63e-04

Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) 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. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 41.34  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  46 LRAWQALVRADVIAAEDTRASRTLLDAWGVSTPL------------M----AAHRHNEASAAQAICERLAQGQRVALVSd 109
Cdd:cd11645   13 LKAVRILKEADVIFVPVSKGGEGSAALIIAAALLipdkeiiplefpMtkdrEELEEAWDEAAEEIAEELKEGKDVAFLT- 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499232240 110 agapaVSDPG-----ARIVRAVREAGYAVVPVPGPSAVIAA 145
Cdd:cd11645   92 -----LGDPSlystfSYLLERLRAPGVEVEIIPGITSFSAA 127
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
31-145 3.50e-03

Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. 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. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.


Pssm-ID: 381173 [Multi-domain]  Cd Length: 238  Bit Score: 38.16  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232240  31 LYVIATPIGNLGDLGLRAWQALVRADVIAAEDT---RASRTLLDAWGVSTPLMAahrhnEASAAQAICERLAQGQRVALV 107
Cdd:cd11646    1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTyldLIEDLLPGKEVISSGMGE-----EVERAREALELALEGKRVALV 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499232240 108 S--DAGAPAVSDPGARIVRAvREAGYAVVPVPGPSAVIAA 145
Cdd:cd11646   76 SsgDPGIYGMAGLVLELLDE-RWDDIEVEVVPGITAALAA 114
 
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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