NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|586185321|gb|EWP91157|]
View 

16S rRNA (-2'-O)-methyltransferase [Staphylococcus aureus M1204]

Protein Classification

ribosomal RNA small subunit methyltransferase I( domain architecture ID 10184564)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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-) ...
5-222 3.57e-120

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: 342.44  E-value: 3.57e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   5 YLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSDAG 84
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  85 LPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHR 164
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 586185321 165 VTDTLKTIAKIDATRQVSLGRELTKKFEQIVTDDVTQLQALIQqgDVPLKGEFVILIE 222
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELE--ENKPKGEFVLVVE 216
 
Name Accession Description Interval E-value
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
5-222 3.57e-120

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: 342.44  E-value: 3.57e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   5 YLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSDAG 84
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  85 LPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHR 164
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 586185321 165 VTDTLKTIAKIDATRQVSLGRELTKKFEQIVTDDVTQLQALIQqgDVPLKGEFVILIE 222
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELE--ENKPKGEFVLVVE 216
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
4-223 8.09e-119

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: 339.29  E-value: 8.09e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   4 LYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSDA 83
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  84 GLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPH 163
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERRKRLKELEAEPRTLIFYESPH 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586185321 164 RVTDTLKTIAKID-ATRQVSLGRELTKKFEQIVTDDVTQLQALIQqgDVPLKGEFVILIEG 223
Cdd:COG0313  161 RLAKTLEDLAEVLgPDRRLCVARELTKLFEEIRRGTLAELLAWLP--DLPPKGEFVLVIEG 219
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
2-229 8.55e-70

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


Pssm-ID: 184956  Cd Length: 287  Bit Score: 217.01  E-value: 8.55e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   2 AVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVS 81
Cdd:PRK14994  12 GQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  82 DAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYES 161
Cdd:PRK14994  92 DAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFCYEGFLPAKSKGRRDALKALEAEPRTLIFYES 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586185321 162 PHRVTDTLKTIAKI-DATRQVSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNE 229
Cdd:PRK14994 172 THRLLDSLEDIVAVlGESRYVVLARELTKTWETIHGAPVGELLAWVKEDENRRKGEMVLIVEGHKAQED 240
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
3-276 4.91e-57

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: 184.25  E-value: 4.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321    3 VLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSD 82
Cdd:TIGR00096   1 LLYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIAVSSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   83 AGLPLISDPGYELVVAAREANIkVETVPGPNAGLTALMASGLPSYVYTFL-GFLPRKEKEKSAVLEQRMHENSTLIIYES 161
Cdd:TIGR00096  81 AGPPLISDPGHLLVACREKANI-IVVPLPGAAALTAALCASGPATDRFFFgGFLPKKSKRRQALKAYIAEERTTVFFYES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  162 PHRVTDTLKTIAKIDATRQVSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILI-EGAKANNEISwfdDLSINE 240
Cdd:TIGR00096 160 HHRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDTNNRKGGEVILIiNGHKPQEECS---DLQALA 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 586185321  241 HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYH 276
Cdd:TIGR00096 237 LEILALLQAEVLLKKAAAYIAAEMTLKKNKLLYQFH 272
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
3-202 5.08e-40

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: 138.24  E-value: 5.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321    3 VLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNH-----YDIPTPLKSYHEHNKDKQTAFIIEQLELGLDV 77
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLlpedlYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   78 ALVSdAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLP---SYVYTFLGFLPRKEKEKSAVLEQRMHENS 154
Cdd:pfam00590  81 ARLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPlteGGEVLSVLFLPGLARIELRLLEALLANGD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 586185321  155 TLIIYESPHRVTDTLKTIAKIDA-TRQVSLGRELTKKFEQIVTDDVTQL 202
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYPdTTPVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
5-222 3.57e-120

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: 342.44  E-value: 3.57e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   5 YLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSDAG 84
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  85 LPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHR 164
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 586185321 165 VTDTLKTIAKIDATRQVSLGRELTKKFEQIVTDDVTQLQALIQqgDVPLKGEFVILIE 222
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELE--ENKPKGEFVLVVE 216
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
4-223 8.09e-119

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: 339.29  E-value: 8.09e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   4 LYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSDA 83
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  84 GLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPH 163
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERRKRLKELEAEPRTLIFYESPH 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586185321 164 RVTDTLKTIAKID-ATRQVSLGRELTKKFEQIVTDDVTQLQALIQqgDVPLKGEFVILIEG 223
Cdd:COG0313  161 RLAKTLEDLAEVLgPDRRLCVARELTKLFEEIRRGTLAELLAWLP--DLPPKGEFVLVIEG 219
RsmI_like cd19917
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ...
5-222 1.67e-70

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: 216.44  E-value: 1.67e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   5 YLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPT-PLKSYHEHNKDKQTAFIIEQLELGLDVALVSDA 83
Cdd:cd19917    1 YLVATPIGNTDDITLRALETLKAVDLIICEDTRNASRLLKHVGIIGkTLEVLNEHNTPEDIQELLDKLAGGKNVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  84 GLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPH 163
Cdd:cd19917   81 GTPAFADPGADLVKLCRDAGIPVVPLPGASSLMTALSASGLKSDRFLFYGFLPAEPGERKKALKALEQEPRTLIFMETPY 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321 164 RVTDTLKTIAKI-DATRQVSLGRELTKKFEQIVTDDVTQLQALIQqgDVPlKGEFVILIE 222
Cdd:cd19917  161 RLKKTLEDLAAVfGPNRKVVLARNLTQEEETILTGTLGELLNKIP--ELP-KGEFVLLLY 217
RsmI_like cd19918
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
5-222 2.32e-70

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: 216.25  E-value: 2.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   5 YLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSDAG 84
Cdd:cd19918    1 YIVATPIGNYDDITLRALEVLKEVDVIICEEFKEGSRLLKKLIIEKELLLLNEHNEKEDAAELLDLLAQGKSVALISDCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  85 LPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHR 164
Cdd:cd19918   81 TPVFADPGALLVKLCIQKGIPVVPVPGASSLMAALSVSGFKIDRFLFAGFLPRKKEERRRELKRLKSEKRPIVLMDTPYR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586185321 165 VTDTLKTIAKID-ATRQVSLGRELTKKFEQIVTDDVTQLQALIQQGdvPLKGEFVILIE 222
Cdd:cd19918  161 LKKLLEDLAKVFgPNRRIVLAYNLTLPDEKILRGTLAEILKKVEEK--PLKGEFVLIIH 217
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
2-229 8.55e-70

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


Pssm-ID: 184956  Cd Length: 287  Bit Score: 217.01  E-value: 8.55e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   2 AVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVS 81
Cdd:PRK14994  12 GQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  82 DAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYES 161
Cdd:PRK14994  92 DAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFCYEGFLPAKSKGRRDALKALEAEPRTLIFYES 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586185321 162 PHRVTDTLKTIAKI-DATRQVSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNE 229
Cdd:PRK14994 172 THRLLDSLEDIVAVlGESRYVVLARELTKTWETIHGAPVGELLAWVKEDENRRKGEMVLIVEGHKAQED 240
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
3-276 4.91e-57

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: 184.25  E-value: 4.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321    3 VLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSD 82
Cdd:TIGR00096   1 LLYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIAVSSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   83 AGLPLISDPGYELVVAAREANIkVETVPGPNAGLTALMASGLPSYVYTFL-GFLPRKEKEKSAVLEQRMHENSTLIIYES 161
Cdd:TIGR00096  81 AGPPLISDPGHLLVACREKANI-IVVPLPGAAALTAALCASGPATDRFFFgGFLPKKSKRRQALKAYIAEERTTVFFYES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  162 PHRVTDTLKTIAKIDATRQVSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILI-EGAKANNEISwfdDLSINE 240
Cdd:TIGR00096 160 HHRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDTNNRKGGEVILIiNGHKPQEECS---DLQALA 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 586185321  241 HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYH 276
Cdd:TIGR00096 237 LEILALLQAEVLLKKAAAYIAAEMTLKKNKLLYQFH 272
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
3-202 5.08e-40

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: 138.24  E-value: 5.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321    3 VLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNH-----YDIPTPLKSYHEHNKDKQTAFIIEQLELGLDV 77
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLlpedlYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   78 ALVSdAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLP---SYVYTFLGFLPRKEKEKSAVLEQRMHENS 154
Cdd:pfam00590  81 ARLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPlteGGEVLSVLFLPGLARIELRLLEALLANGD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 586185321  155 TLIIYESPHRVTDTLKTIAKIDA-TRQVSLGRELTKKFEQIVTDDVTQL 202
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYPdTTPVAVVERAGTPDEKVVRGTLGEL 208
RsmI_like cd11649
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
4-196 1.70e-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: 1.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   4 LYLVGTPIGNLAD---ITYRAVDVLKRVDMIACEDTRVT----SKLCNHYDIPT-PLKSYHEHNKDKQTAFIIEQLELGL 75
Cdd:cd11649    1 LYLIPTPLGEESPdevLPPEVLEIIRSLDHFIVENEKTArrflKKLGPPKPIDElTFFELNKHTREEDLEELLKPLLEGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  76 DVALVSDAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSYVYTFLGFLPRKEKEKSAV---LEQRMH- 151
Cdd:cd11649   81 DIGLISEAGCPGVADPGAELVALAHRLGIKVVPLVGPSSILLALMASGLNGQNFAFHGYLPIDKEERKKKlkeLEKRSRk 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 586185321 152 ENSTLIIYESPHRVTDTLKTIAKI-DATRQVSLGRELTKKFEQIVT 196
Cdd:cd11649  161 EGQTQIFIETPYRNNALLEDLLKTlQPDTRLCVACDLTGPSEFIKT 206
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
7-222 2.19e-25

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: 100.16  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   7 VGTPIGNLADITYRAVDVLKRVDMIACEDTRV----TSKLCNHYDIPTPLKSYHEHNKDKQTAFIIEQLELGLDVALVSd 82
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSkllsLVLRAILKDGKRIYDLHDPNVEEEMAELLLEEARQGKDVAFLS- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  83 AGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLPSY----VYTFLGFLPRKEKEKSAVLEQrmhENSTLII 158
Cdd:cd09815   80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGesflFVTASDLLENPRLLVLKALAK---ERRHLVL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586185321 159 YESPHRVTDTLKTIAKIDATRQ--VSLGRELTKKFEQIVTDDVTQLQALIQqgdVPLKGEFVILIE 222
Cdd:cd09815  157 FLDGHRFLKALERLLKELGEDDtpVVLVANAGSEGEVIRTGTVKELRAERT---ERGKPLTTILVG 219
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
17-198 3.87e-06

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: 46.73  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  17 ITYRAVDVLKRVDMIAC-----EDTRVTSKLCNHYDIP---------------TPLKSYHEHNKDKqtafIIEQLELGLD 76
Cdd:cd11645   11 LTLKAVRILKEADVIFVpvskgGEGSAALIIAAALLIPdkeiiplefpmtkdrEELEEAWDEAAEE----IAEELKEGKD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  77 VALVS--DaglPLI-SDPGYeLVVAAREANIKVETVPGPNAgLTALMA-SGLPsyvytfLGflprKEKEKSAV------- 145
Cdd:cd11645   87 VAFLTlgD---PSLySTFSY-LLERLRAPGVEVEIIPGITS-FSAAAArLGIP------LA----EGDESLAIlpatyde 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 586185321 146 --LEQRMHENSTLIIYESPHRVTDTLKTIAKIDATRQVSLGRELTKKFEQIVTDD 198
Cdd:cd11645  152 eeLEKALENFDTVVLMKVGRNLEEIKELLEELGLLDKAVYVERCGMEGERIYTDL 206
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
1-125 1.38e-04

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 42.12  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   1 MAVLYLVGTPIGNLADITYRAVDVLKRVDMI-------------ACEDTRVTS--KLCNHydiptplksyHEHNKDKQTA 65
Cdd:PRK06136   2 MGKVYLVGAGPGDPDLITLKGVRLLEQADVVlyddlvspeilayAKPDAELIYvgKRAGR----------HSTKQEEINR 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321  66 FIIEQLELGLDVALVSdAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALMASGLP 125
Cdd:PRK06136  72 LLVDYARKGKVVVRLK-GGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIP 130
OphMA_like cd19916
tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin ...
4-111 9.19e-04

tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA; OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A.


Pssm-ID: 381179  Cd Length: 237  Bit Score: 39.77  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586185321   4 LYLVGTPIGNLADITYRAVDVLKRVDMI-ACEDTRVT----SKLC-NHYDiptpLKSYHEHNKDKQ------TAFIIEQL 71
Cdd:cd19916    3 LVVVGTGIKGIGHLTLEAESAIEQADKVfYLVADPLTeewlRELNpNAED----LYDLYGEGKPRLdtyremAERILEAV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 586185321  72 ELGLDVALVSdAGLPLI-SDPGYELVVAAREANIKVETVPG 111
Cdd:cd19916   79 RAGKPVCAAF-YGHPGVfVSPSHLAIRIARREGYRARMLPG 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH