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Conserved domains on  [gi|489336237|ref|WP_003243457|]
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MULTISPECIES: 16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Bacillus]

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

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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-) ...
18-233 4.32e-121

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: 345.52  E-value: 4.32e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  18 YLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDAG 97
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  98 LPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPHR 177
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489336237 178 LKETLSAMAEILGDREIAVTRELTKKYEEFIRGTISEVIGWANEDQIRGEFCLVVE 233
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-) ...
18-233 4.32e-121

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: 345.52  E-value: 4.32e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  18 YLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDAG 97
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  98 LPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPHR 177
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489336237 178 LKETLSAMAEILGDREIAVTRELTKKYEEFIRGTISEVIGWANEDQIRGEFCLVVE 233
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELEENKPKGEFVLVVE 216
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
17-234 5.62e-116

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: 332.36  E-value: 5.62e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  17 LYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDA 96
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  97 GLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPH 176
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERRKRLKELEAEPRTLIFYESPH 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336237 177 RLKETLSAMAEILG-DREIAVTRELTKKYEEFIRGTISEVIGWANEDQIRGEFCLVVEG 234
Cdd:COG0313  161 RLAKTLEDLAEVLGpDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPKGEFVLVIEG 219
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
15-239 1.68e-63

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


Pssm-ID: 184956  Cd Length: 287  Bit Score: 201.60  E-value: 1.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  15 GILYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVS 94
Cdd:PRK14994  12 GQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  95 DAGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEA 174
Cdd:PRK14994  92 DAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFCYEGFLPAKSKGRRDALKALEAEPRTLIFYES 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489336237 175 PHRLKETLSAMAEILG-DREIAVTRELTKKYEEFIRGTISEVIGWANEDQIR--GEFCLVVEGSNNEE 239
Cdd:PRK14994 172 THRLLDSLEDIVAVLGeSRYVVLARELTKTWETIHGAPVGELLAWVKEDENRrkGEMVLIVEGHKAQE 239
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
16-285 1.24e-54

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: 178.48  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   16 ILYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSD 95
Cdd:TIGR00096   1 LLYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIAVSSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   96 AGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAP 175
Cdd:TIGR00096  81 AGPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPATDRFFFGGFLPKKSKRRQALKAYIAEERTTVFFYESH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  176 HRLKETLSAMAEILGDREIAVTRELTKKYEEFIRGTISEVIGWANED---QIRGEFCLVVEGSNNeevdEEEQWWETLTA 252
Cdd:TIGR00096 161 HRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDtnnRKGGEVILIINGHKP----QEECSDLQALA 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 489336237  253 KEHVEHYISKGATSKEAIKKAAVDRNVPKREVY 285
Cdd:TIGR00096 237 LEILALLQAEVLLKKAAAYIAAEMTLKKNKLLY 269
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
17-215 1.52e-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: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   17 LYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCH-----VYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIA 91
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDllpedLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   92 LVSdAGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFF---FYGFLNRQKKEKKKELEALKKRQET 168
Cdd:pfam00590  82 RLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGevlSVLFLPGLARIELRLLEALLANGDT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 489336237  169 IIFYEAPHRLKETLSAMAEILGD-REIAVTRELTKKYEEFIRGTISEV 215
Cdd:pfam00590 161 VVLLYGPRRLAELAELLLELYPDtTPVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
RsmI cd11648
Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-) ...
18-233 4.32e-121

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: 345.52  E-value: 4.32e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  18 YLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDAG 97
Cdd:cd11648    1 YLVATPIGNLEDITLRALEVLKEVDLIACEDTRHTRKLLNHYGIKKPLISYHEHNEKKRAEKIIELLKEGKSVALVSDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  98 LPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPHR 177
Cdd:cd11648   81 TPGISDPGYRLVRAAIEAGIEVVPIPGPSAVITALSASGLPTDRFTFLGFLPRKKGKRKKLLEELAEEPRTLIFYESPHR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489336237 178 LKETLSAMAEILGDREIAVTRELTKKYEEFIRGTISEVIGWANEDQIRGEFCLVVE 233
Cdd:cd11648  161 ILKTLEDLAEVGGDREVVVARELTKLHEEVIRGTLSELLEELEENKPKGEFVLVVE 216
RsmI COG0313
16S rRNA C1402 (ribose-2'-O) methylase RsmI [Translation, ribosomal structure and biogenesis]; ...
17-234 5.62e-116

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: 332.36  E-value: 5.62e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  17 LYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDA 96
Cdd:COG0313    1 LYLVPTPIGNLEDITLRALEVLKEVDLIAAEDTRTTRKLLKHLGIKKPLISLHEHNEAERAPELLERLKAGKDVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  97 GLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPH 176
Cdd:COG0313   81 GTPGISDPGARLVRAAHEAGIPVVPLPGPSAVLTALSASGLPGDRFAFEGFLPRKKKERRKRLKELEAEPRTLIFYESPH 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336237 177 RLKETLSAMAEILG-DREIAVTRELTKKYEEFIRGTISEVIGWANEDQIRGEFCLVVEG 234
Cdd:COG0313  161 RLAKTLEDLAEVLGpDRRLCVARELTKLFEEIRRGTLAELLAWLPDLPPKGEFVLVIEG 219
RsmI_like cd19917
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ...
18-233 1.60e-71

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: 219.52  E-value: 1.60e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  18 YLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLC-HVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDA 96
Cdd:cd19917    1 YLVATPIGNTDDITLRALETLKAVDLIICEDTRNASRLLkHVGIIGKTLEVLNEHNTPEDIQELLDKLAGGKNVALVSDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  97 GLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPH 176
Cdd:cd19917   81 GTPAFADPGADLVKLCRDAGIPVVPLPGASSLMTALSASGLKSDRFLFYGFLPAEPGERKKALKALEQEPRTLIFMETPY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489336237 177 RLKETLSAMAEILG-DREIAVTRELTKKYEEFIRGTISEVIGWAnEDQIRGEFCLVVE 233
Cdd:cd19917  161 RLKKTLEDLAAVFGpNRKVVLARNLTQEEETILTGTLGELLNKI-PELPKGEFVLLLY 217
RsmI_like cd19918
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
18-233 4.49e-67

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: 208.16  E-value: 4.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  18 YLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSDAG 97
Cdd:cd19918    1 YIVATPIGNYDDITLRALEVLKEVDVIICEEFKEGSRLLKKLIIEKELLLLNEHNEKEDAAELLDLLAQGKSVALISDCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  98 LPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAPHR 177
Cdd:cd19918   81 TPVFADPGALLVKLCIQKGIPVVPVPGASSLMAALSVSGFKIDRFLFAGFLPRKKEERRRELKRLKSEKRPIVLMDTPYR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489336237 178 LKETLSAMAEILG-DREIAVTRELTKKYEEFIRGTISEVIGWANEDQIRGEFCLVVE 233
Cdd:cd19918  161 LKKLLEDLAKVFGpNRRIVLAYNLTLPDEKILRGTLAEILKKVEEKPLKGEFVLIIH 217
PRK14994 PRK14994
SAM-dependent 16S ribosomal RNA C1402 ribose 2'-O-methyltransferase; Provisional
15-239 1.68e-63

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


Pssm-ID: 184956  Cd Length: 287  Bit Score: 201.60  E-value: 1.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  15 GILYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVS 94
Cdd:PRK14994  12 GQLYIVPTPIGNLADITQRALEVLQAVDLIAAEDTRHTGLLLQHFAINARLFALHDHNEQQKAETLLAKLQEGQNIALVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  95 DAGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEA 174
Cdd:PRK14994  92 DAGTPLINDPGYHLVRTCREAGIRVVPLPGPCAAITALSAAGLPSDRFCYEGFLPAKSKGRRDALKALEAEPRTLIFYES 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489336237 175 PHRLKETLSAMAEILG-DREIAVTRELTKKYEEFIRGTISEVIGWANEDQIR--GEFCLVVEGSNNEE 239
Cdd:PRK14994 172 THRLLDSLEDIVAVLGeSRYVVLARELTKTWETIHGAPVGELLAWVKEDENRrkGEMVLIVEGHKAQE 239
TIGR00096 TIGR00096
16S rRNA (cytidine(1402)-2'-O)-methyltransferase; This protein, previously known as YraL, is ...
16-285 1.24e-54

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: 178.48  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   16 ILYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIALVSD 95
Cdd:TIGR00096   1 LLYVVTTPIGNLEDITRRALELLACVDLFAEEDTRTSKLLLHLGIIATPKAFHIDNEFQEKQNLLAAKLEIGNNIAVSSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   96 AGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFLNRQKKEKKKELEALKKRQETIIFYEAP 175
Cdd:TIGR00096  81 AGPPLISDPGHLLVACREKANIIVVPLPGAAALTAALCASGPATDRFFFGGFLPKKSKRRQALKAYIAEERTTVFFYESH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  176 HRLKETLSAMAEILGDREIAVTRELTKKYEEFIRGTISEVIGWANED---QIRGEFCLVVEGSNNeevdEEEQWWETLTA 252
Cdd:TIGR00096 161 HRLLTTLTDLNVFLGSERFVGAAELTKKESEYWFGTVGQLLPDITEDtnnRKGGEVILIINGHKP----QEECSDLQALA 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 489336237  253 KEHVEHYISKGATSKEAIKKAAVDRNVPKREVY 285
Cdd:TIGR00096 237 LEILALLQAEVLLKKAAAYIAAEMTLKKNKLLY 269
RsmI_like cd11649
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ...
17-222 9.28e-33

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: 120.23  E-value: 9.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  17 LYLVPTPIG-NLEDMTF--RAIDTLKSVDAIAAEDTRQT----KKLCHVYEI-ETPLVSYHEHNKESSGHKIIEWLKSGK 88
Cdd:cd11649    1 LYLIPTPLGeESPDEVLppEVLEIIRSLDHFIVENEKTArrflKKLGPPKPIdELTFFELNKHTREEDLEELLKPLLEGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  89 NIALVSDAGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFFFYGFL-----NRQKKEKKKELEALK 163
Cdd:cd11649   81 DIGLISEAGCPGVADPGAELVALAHRLGIKVVPLVGPSSILLALMASGLNGQNFAFHGYLpidkeERKKKLKELEKRSRK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237 164 KRQeTIIFYEAPHRLKETLSAMAEIL-GDREIAVTRELTKKYEEFIRGTISEvigWANED 222
Cdd:cd11649  161 EGQ-TQIFIETPYRNNALLEDLLKTLqPDTRLCVACDLTGPSEFIKTKTIAE---WKKKK 216
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
17-215 1.52e-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: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   17 LYLVPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCH-----VYEIETPLVSYHEHNKESSGHKIIEWLKSGKNIA 91
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDllpedLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237   92 LVSdAGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFF---FYGFLNRQKKEKKKELEALKKRQET 168
Cdd:pfam00590  82 RLV-SGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGevlSVLFLPGLARIELRLLEALLANGDT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 489336237  169 IIFYEAPHRLKETLSAMAEILGD-REIAVTRELTKKYEEFIRGTISEV 215
Cdd:pfam00590 161 VVLLYGPRRLAELAELLLELYPDtTPVAVVERAGTPDEKVVRGTLGEL 208
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
20-221 2.25e-20

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: 87.06  E-value: 2.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  20 VPTPIGNLEDMTFRAIDTLKSVDAIAAEDTRQTKKLCHVYEIETP----LVSYHEHNKESSGHKIIEWLKSGKNIALVSd 95
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDgkriYDLHDPNVEEEMAELLLEEARQGKDVAFLS- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336237  96 AGLPTISDPGAEIVKDFTDIGGYVVPLPGANAALTALIASGIVPQPFF-FYGFLNRQKKEKKKELEALKKRQETIIFYEA 174
Cdd:cd09815   80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGESFlFVTASDLLENPRLLVLKALAKERRHLVLFLD 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489336237 175 PHRLKETLSAMAEILG--DREIAVTRELTKKYEEFIRGTISEVIGWANE 221
Cdd:cd09815  160 GHRFLKALERLLKELGedDTPVVLVANAGSEGEVIRTGTVKELRAERTE 208
 
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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