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Conserved domains on  [gi|727225743|ref|WP_033686647|]
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16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Streptococcus mitis]

Protein Classification

16S rRNA (cytidine(1402)-2'-O)-methyltransferase( domain architecture ID 10184564)

16S rRNA (cytidine(1402)-2'-O)-methyltransferase, also called ribosomal RNA small subunit methyltransferase I (RsmI), uses assembled 30S subunit as a substrate to catalyze the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA; belongs to the tetrapyrrole methylase family

EC:  2.1.1.198
Gene Symbol:  rsmI
PubMed:  27711192|16225687
SCOP:  4000056

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
17-232 4.04e-127

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: 360.55  E-value: 4.04e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  17 YLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVSDAG 96
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  97 LPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPHR 176
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727225743 177 VTDTLENMLEVYGDRSVVLVRELTKIYEEYQRGKISELLESISETPLKGECLLIVE 232
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELEENKPKGEFVLVVE 216
 
Name Accession Description Interval E-value
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
17-232 4.04e-127

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: 360.55  E-value: 4.04e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  17 YLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVSDAG 96
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  97 LPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPHR 176
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727225743 177 VTDTLENMLEVYGDRSVVLVRELTKIYEEYQRGKISELLESISETPLKGECLLIVE 232
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELEENKPKGEFVLVVE 216
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
16-233 3.68e-122

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: 348.15  E-value: 3.68e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  16 LYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVSDA 95
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  96 GLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPH 175
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERRKRLKELEAEPRTLIFYESPH 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727225743 176 RVTDTLENMLEVYG-DRSVVLVRELTKIYEEYQRGKISELLESISETPLKGECLLIVEG 233
Cdd:COG0313  161 RLAKTLEDLAEVLGpDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPKGEFVLVIEG 219
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
14-290 2.51e-73

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


Pssm-ID: 184956  Cd Length: 287  Bit Score: 226.64  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  14 GKLYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVS 93
Cdd:PRK14994  12 GQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  94 DAGLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYES 173
Cdd:PRK14994  92 DAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFCYEGFLPAKSKGRRDALKALEAEPRTLIFYES 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743 174 PHRVTDTLENMLEVYG-DRSVVLVRELTKIYEEYQRGKISELLESI--SETPLKGECLLIVEGASQDVEEKDEEDLFLEI 250
Cdd:PRK14994 172 THRLLDSLEDIVAVLGeSRYVVLARELTKTWETIHGAPVGELLAWVkeDENRRKGEMVLIVEGHKAQEDDLPADALRTLA 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 727225743 251 QTRIQQGMKKNQAIkeVAKFYQWNKSQLYAayHDWEENQE 290
Cdd:PRK14994 252 LLQAELPLKKAAAL--AAEIHGVKKNALYK--YALEQQGE 287
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
16-279 1.08e-58

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: 188.88  E-value: 1.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   16 LYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAqVSDA 95
Cdd:TIGR00096   2 LYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIA-VSSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   96 GLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQI-FYESP 174
Cdd:TIGR00096  81 AGPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPATDRFFFGGFLPKKSKRRQALKAYIAEERTTVfFYESH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  175 HRVTDTLENMLEVYGDRSVVLVRELTKIYEEYQRGKISELLESISET---PLKGECLLIVEGASQDVEEKDEEDLFLEIQ 251
Cdd:TIGR00096 161 HRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDtnnRKGGEVILIINGHKPQEECSDLQALALEIL 240
                         250       260
                  ....*....|....*....|....*....
gi 727225743  252 TRIQQGMK-KNQAIKEVAKFYQWNKSQLY 279
Cdd:TIGR00096 241 ALLQAEVLlKKAAAYIAAEMTLKKNKLLY 269
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
15-214 1.63e-27

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: 105.89  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   15 KLYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKH-----FDISSKQISFYEHNAKEKIPDLIGFLKAGQSI 89
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLlpedlYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   90 AQVSdAGLPSISDPGHDLVKAAIEEDIAIVTVPGASAgISALIASGLAPQPH----IFYGFLPRKSGQQKQFFDSKKDYP 165
Cdd:pfam00590  81 ARLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSS-AQAAAARLGIPLTEggevLSVLFLPGLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 727225743  166 ETQIFYESPHRVTDTLENMLEVYGD-RSVVLVRELTKIYEEYQRGKISEL 214
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLELYPDtTPVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
17-232 4.04e-127

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: 360.55  E-value: 4.04e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  17 YLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVSDAG 96
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  97 LPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPHR 176
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727225743 177 VTDTLENMLEVYGDRSVVLVRELTKIYEEYQRGKISELLESISETPLKGECLLIVE 232
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELEENKPKGEFVLVVE 216
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
16-233 3.68e-122

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: 348.15  E-value: 3.68e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  16 LYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVSDA 95
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  96 GLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPH 175
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERRKRLKELEAEPRTLIFYESPH 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727225743 176 RVTDTLENMLEVYG-DRSVVLVRELTKIYEEYQRGKISELLESISETPLKGECLLIVEG 233
Cdd:COG0313  161 RLAKTLEDLAEVLGpDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPKGEFVLVIEG 219
RsmI_like cd19917
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ...
17-232 1.82e-83

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: 249.95  E-value: 1.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  17 YLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSK-QISFYEHNAKEKIPDLIGFLKAGQSIAQVSDA 95
Cdd:cd19917    1 YLVATPIGNTDDITLRALETLKAVDLIICEDTRNASRLLKHVGIIGKtLEVLNEHNTPEDIQELLDKLAGGKNVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  96 GLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPH 175
Cdd:cd19917   81 GTPAFADPGADLVKLCRDAGIPVVPLPGASSLMTALSASGLKSDRFLFYGFLPAEPGERKKALKALEQEPRTLIFMETPY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 727225743 176 RVTDTLENMLEVYG-DRSVVLVRELTKIYEEYQRGKISELLESISETPlKGECLLIVE 232
Cdd:cd19917  161 RLKKTLEDLAAVFGpNRKVVLARNLTQEEETILTGTLGELLNKIPELP-KGEFVLLLY 217
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
14-290 2.51e-73

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


Pssm-ID: 184956  Cd Length: 287  Bit Score: 226.64  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  14 GKLYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVS 93
Cdd:PRK14994  12 GQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  94 DAGLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYES 173
Cdd:PRK14994  92 DAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFCYEGFLPAKSKGRRDALKALEAEPRTLIFYES 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743 174 PHRVTDTLENMLEVYG-DRSVVLVRELTKIYEEYQRGKISELLESI--SETPLKGECLLIVEGASQDVEEKDEEDLFLEI 250
Cdd:PRK14994 172 THRLLDSLEDIVAVLGeSRYVVLARELTKTWETIHGAPVGELLAWVkeDENRRKGEMVLIVEGHKAQEDDLPADALRTLA 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 727225743 251 QTRIQQGMKKNQAIkeVAKFYQWNKSQLYAayHDWEENQE 290
Cdd:PRK14994 252 LLQAELPLKKAAAL--AAEIHGVKKNALYK--YALEQQGE 287
RsmI_like cd19918
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
17-232 3.53e-73

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: 223.95  E-value: 3.53e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  17 YLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAQVSDAG 96
Cdd:cd19918    1 YIVATPIGNYDDITLRALEVLKEVDVIICEEFKEGSRLLKKLIIEKELLLLNEHNEKEDAAELLDLLAQGKSVALISDCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  97 LPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQIFYESPHR 176
Cdd:cd19918   81 TPVFADPGALLVKLCIQKGIPVVPVPGASSLMAALSVSGFKIDRFLFAGFLPRKKEERRRELKRLKSEKRPIVLMDTPYR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 727225743 177 VTDTLENMLEVYG-DRSVVLVRELTKIYEEYQRGKISELLESISETPLKGECLLIVE 232
Cdd:cd19918  161 LKKLLEDLAKVFGpNRRIVLAYNLTLPDEKILRGTLAEILKKVEEKPLKGEFVLIIH 217
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
16-279 1.08e-58

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: 188.88  E-value: 1.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   16 LYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYEHNAKEKIPDLIGFLKAGQSIAqVSDA 95
Cdd:TIGR00096   2 LYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIA-VSSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   96 GLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFFDSKKDYPETQI-FYESP 174
Cdd:TIGR00096  81 AGPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPATDRFFFGGFLPKKSKRRQALKAYIAEERTTVfFYESH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  175 HRVTDTLENMLEVYGDRSVVLVRELTKIYEEYQRGKISELLESISET---PLKGECLLIVEGASQDVEEKDEEDLFLEIQ 251
Cdd:TIGR00096 161 HRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDtnnRKGGEVILIINGHKPQEECSDLQALALEIL 240
                         250       260
                  ....*....|....*....|....*....
gi 727225743  252 TRIQQGMK-KNQAIKEVAKFYQWNKSQLY 279
Cdd:TIGR00096 241 ALLQAEVLlKKAAAYIAAEMTLKKNKLLY 269
RsmI_like cd11649
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
16-187 2.64e-32

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: 119.07  E-value: 2.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  16 LYLVATPIG-NLDDMTF--RAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQ--ISFY---EHNAKEKIPDLIGFLKAGQ 87
Cdd:cd11649    1 LYLIPTPLGeESPDEVLppEVLEIIRSLDHFIVENEKTARRFLKKLGPPKPIdeLTFFelnKHTREEDLEELLKPLLEGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  88 SIAQVSDAGLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHIFYGFLPRKSGQQKQFF-----DSKK 162
Cdd:cd11649   81 DIGLISEAGCPGVADPGAELVALAHRLGIKVVPLVGPSSILLALMASGLNGQNFAFHGYLPIDKEERKKKLkelekRSRK 160
                        170       180
                 ....*....|....*....|....*
gi 727225743 163 DyPETQIFYESPHRVTDTLENMLEV 187
Cdd:cd11649  161 E-GQTQIFIETPYRNNALLEDLLKT 184
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
15-214 1.63e-27

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: 105.89  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   15 KLYLVATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKH-----FDISSKQISFYEHNAKEKIPDLIGFLKAGQSI 89
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLlpedlYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743   90 AQVSdAGLPSISDPGHDLVKAAIEEDIAIVTVPGASAgISALIASGLAPQPH----IFYGFLPRKSGQQKQFFDSKKDYP 165
Cdd:pfam00590  81 ARLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSS-AQAAAARLGIPLTEggevLSVLFLPGLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 727225743  166 ETQIFYESPHRVTDTLENMLEVYGD-RSVVLVRELTKIYEEYQRGKISEL 214
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLELYPDtTPVAVVERAGTPDEKVVRGTLGEL 208
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
19-232 1.90e-26

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: 103.24  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  19 VATPIGNLDDMTFRAIQTLKEVDWIAAEDTRNTGLLLKHFDISSKQISFYE---HNAKEKIPD-LIGFLKAGQSIAQVSd 94
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGKRIYDlhdPNVEEEMAElLLEEARQGKDVAFLS- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  95 AGLPSISDPGHDLVKAAIEEDIAIVTVPGASAGISALIASGLAPQPHI-FYGFLPRKSGQQKQFFDSKKDYPETQIFYES 173
Cdd:cd09815   80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGESFlFVTASDLLENPRLLVLKALAKERRHLVLFLD 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727225743 174 PHRVTDTLENMLEVYG--DRSVVLVRELTKIYEEYQRGKISELLESISEtPLKGECLLIVE 232
Cdd:cd09815  160 GHRFLKALERLLKELGedDTPVVLVANAGSEGEVIRTGTVKELRAERTE-RGKPLTTILVG 219
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
15-231 8.52e-06

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: 46.01  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  15 KLYLVATPIGNLDDMTFRAIQTLKEVDWIAA-EDTRntglllKHF--DISSKQISF-----YEHNAKEKIPDLIG----- 81
Cdd:cd11724    1 KLYLVGVGPGDPDLITLRALKAIKKADVVFApPDLR------KRFaeYLAGKEVLDdphglFTYYGKKCSPLEEAekece 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  82 ---------------FLKAGQSIAqVSDAGLPSISDPGHDLVKAAieEDIAIVTVPGASA--GISALIASGLAPQPHIfy 144
Cdd:cd11724   75 elekqraeivqkireALAQGKNVA-LLDSGDPTIYGPWIWYLEEF--ADLNPEVIPGVSSfnAANAALKRSLTGGGDS-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743 145 GFL----PRKSGQQKQFFDSKKDYPETQIFYESPHRVTDTLENMLEVY-GDRSVVLVRELTkiYEEYQ---RGKISELLE 216
Cdd:cd11724  150 RSViltaPFALKENEDLLEDLAATGDTLVIFMMRLDLDELVEKLKKHYpPDTPVAIVYHAG--YSEKEkviRGTLDDILE 227
                        250
                 ....*....|....*
gi 727225743 217 SISETPLKGECLLIV 231
Cdd:cd11724  228 KLGGEKEPFLGLIYV 242
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
27-134 4.83e-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: 40.57  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727225743  27 DDMTFRAIQTLKEVDWIAAEDTRNTGLLL-----KHFDISSKQI---------------SFYEHNAKEkipdLIGFLKAG 86
Cdd:cd11645    9 ELLTLKAVRILKEADVIFVPVSKGGEGSAaliiaAALLIPDKEIiplefpmtkdreeleEAWDEAAEE----IAEELKEG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727225743  87 QSIAQVsdaglpSISDPG-----HDLVKAAIEEDIAIVTVPgasaGISALIAS 134
Cdd:cd11645   85 KDVAFL------TLGDPSlystfSYLLERLRAPGVEVEIIP----GITSFSAA 127
 
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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