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Conserved domains on  [gi|489007802|ref|WP_002918373|]
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MULTISPECIES: 23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE [Enterobacteriaceae]

Protein Classification

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE( domain architecture ID 10013754)

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
1-208 5.82e-168

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


:

Pssm-ID: 183025  Cd Length: 209  Bit Score: 459.97  E-value: 5.82e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   1 MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRII 80
Cdd:PRK11188   1 MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGDKGRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  81 ACDLLPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGS 160
Cdd:PRK11188  81 ACDILPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489007802 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRK 208
Cdd:PRK11188 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRK 208
 
Name Accession Description Interval E-value
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
1-208 5.82e-168

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 459.97  E-value: 5.82e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   1 MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRII 80
Cdd:PRK11188   1 MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGDKGRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  81 ACDLLPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGS 160
Cdd:PRK11188  81 ACDILPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489007802 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRK 208
Cdd:PRK11188 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRK 208
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-209 1.80e-143

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 397.90  E-value: 1.80e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   1 MTgKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRII 80
Cdd:COG0293    1 MK-MKRSKSSKRWLQRHLNDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  81 ACDLLPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGS 160
Cdd:COG0293   80 ALDLLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489007802 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP 209
Cdd:COG0293  160 FVVKVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
rrmJ TIGR00438
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ...
 20-207 1.99e-118

cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273078  Cd Length: 188  Bit Score: 334.10  E-value: 1.99e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   20 DKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRIIACDLLPMDPIVGVDFLQGD 99
Cdd:TIGR00438   1 DFYYQKAKKEKYRSRASFKLLQLNQKFKLIKPGDTVLDLGAAPGGWSQVAVEQVGGKGRVIAVDLQPMKPIENVDFIRGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  100 FRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGSFVVKVFQGEGFDEYLREIR 179
Cdd:TIGR00438  81 FTDEEVLNKIRERVGDDKVDVVMSDAAPNISGYWDIDHLRSIDLVELALDIAKEVLKPKGNFVVKVFQGEEIDEYLNELR 160

                         170       180
                  ....*....|....*....|....*...
gi 489007802  180 SLFTKVKVRKPDSSRARSREVYIVATGR 207
Cdd:TIGR00438 161 KLFEKVKVTKPQASRKRSAEVYIVAKRF 188
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 31-207 2.79e-74

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 222.08  E-value: 2.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   31 LRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQigNSGRIIACDLLPM---DPIV--GVDFLQGDFRDELV 105
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQR--GAGKVVGVDLGPMqlwKPRNdpGVTFIQGDIRDPET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  106 LKALLERVGdSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKV 185
Cdd:pfam01728  79 LDLLEELLG-RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFEKV 157

                         170       180
                  ....*....|....*....|..
gi 489007802  186 KVRKPDSSRARSREVYIVATGR 207
Cdd:pfam01728 158 GVFKPPASRPESSEEYLVCLGF 179
capping_2-OMTase_viral cd20754
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
 52-204 9.75e-08

viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.


Pssm-ID: 467730  Cd Length: 179  Bit Score: 50.13  E-value: 9.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  52 GMTVVDLGAAPGGWSQYAvTQIGNSGRIIACDLLPMDPIVG--VDFLQGDFRDELVLKALLERVGDskvqVVMSDMAPNM 129
Cdd:cd20754   17 KMRVIYIGCAPGGWLYYL-RDWFEGTLWVGFDPRDTDPLGYnnVITVNKFFDHEHTKLKFLPNKKD----LLICDIRSDR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489007802 130 CGtpAVDIPRAMYLVELAL--EMSRDVLAPGGSFVVKVFQGEGFDEYlreiRSLFTKVKVRKPDSSrarSREVYIVA 204
Cdd:cd20754   92 SS--HVTKEEDTTESFLTLqeGYIATKLAKVGSICVKVRAPDLKDDG----HFSSGTLFPQPYAAS---SSEMRLFS 159
 
Name Accession Description Interval E-value
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
1-208 5.82e-168

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 459.97  E-value: 5.82e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   1 MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRII 80
Cdd:PRK11188   1 MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGDKGRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  81 ACDLLPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGS 160
Cdd:PRK11188  81 ACDILPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489007802 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRK 208
Cdd:PRK11188 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRK 208
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-209 1.80e-143

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 397.90  E-value: 1.80e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   1 MTgKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRII 80
Cdd:COG0293    1 MK-MKRSKSSKRWLQRHLNDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  81 ACDLLPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGS 160
Cdd:COG0293   80 ALDLLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489007802 161 FVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP 209
Cdd:COG0293  160 FVVKVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
rrmJ TIGR00438
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ...
 20-207 1.99e-118

cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273078  Cd Length: 188  Bit Score: 334.10  E-value: 1.99e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   20 DKYVQQAQKKGLRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQIGNSGRIIACDLLPMDPIVGVDFLQGD 99
Cdd:TIGR00438   1 DFYYQKAKKEKYRSRASFKLLQLNQKFKLIKPGDTVLDLGAAPGGWSQVAVEQVGGKGRVIAVDLQPMKPIENVDFIRGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  100 FRDELVLKALLERVGDSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGSFVVKVFQGEGFDEYLREIR 179
Cdd:TIGR00438  81 FTDEEVLNKIRERVGDDKVDVVMSDAAPNISGYWDIDHLRSIDLVELALDIAKEVLKPKGNFVVKVFQGEEIDEYLNELR 160

                         170       180
                  ....*....|....*....|....*...
gi 489007802  180 SLFTKVKVRKPDSSRARSREVYIVATGR 207
Cdd:TIGR00438 161 KLFEKVKVTKPQASRKRSAEVYIVAKRF 188
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 31-207 2.79e-74

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 222.08  E-value: 2.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   31 LRSRAWFKLDEIQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQigNSGRIIACDLLPM---DPIV--GVDFLQGDFRDELV 105
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQR--GAGKVVGVDLGPMqlwKPRNdpGVTFIQGDIRDPET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  106 LKALLERVGdSKVQVVMSDMAPNMCGTPAVDIPRAMYLVELALEMSRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKV 185
Cdd:pfam01728  79 LDLLEELLG-RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFEKV 157

                         170       180
                  ....*....|....*....|..
gi 489007802  186 KVRKPDSSRARSREVYIVATGR 207
Cdd:pfam01728 158 GVFKPPASRPESSEEYLVCLGF 179
RlmM COG2933
23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; ...
 33-101 8.39e-10

23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; 23S rRNA C2498 (ribose-2'-O)-methylase RlmM is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442177 [Multi-domain]  Cd Length: 356  Bit Score: 57.17  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  33 SRAWFKLDE-------IQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQignSGRIIACDLLPMDPIV----GVDFLQGD-F 100
Cdd:COG2933  186 SRSTLKLEEafhvflpRDEWEERLRPGMRAVDLGAAPGGWTWQLVRR---GMFVTAVDNGPMAPSLmdtgQVEHLREDgF 262


                 .
gi 489007802 101 R 101
Cdd:COG2933  263 K 263
capping_2-OMTase_viral cd20754
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
 52-204 9.75e-08

viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.


Pssm-ID: 467730  Cd Length: 179  Bit Score: 50.13  E-value: 9.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  52 GMTVVDLGAAPGGWSQYAvTQIGNSGRIIACDLLPMDPIVG--VDFLQGDFRDELVLKALLERVGDskvqVVMSDMAPNM 129
Cdd:cd20754   17 KMRVIYIGCAPGGWLYYL-RDWFEGTLWVGFDPRDTDPLGYnnVITVNKFFDHEHTKLKFLPNKKD----LLICDIRSDR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489007802 130 CGtpAVDIPRAMYLVELAL--EMSRDVLAPGGSFVVKVFQGEGFDEYlreiRSLFTKVKVRKPDSSrarSREVYIVA 204
Cdd:cd20754   92 SS--HVTKEEDTTESFLTLqeGYIATKLAKVGSICVKVRAPDLKDDG----HFSSGTLFPQPYAAS---SSEMRLFS 159
PRK11760 PRK11760
putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional
 33-89 1.43e-07

putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional


Pssm-ID: 236971 [Multi-domain]  Cd Length: 357  Bit Score: 50.60  E-value: 1.43e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489007802  33 SRAWFKLDE-------IQQSDKIFKPGMTVVDLGAAPGGWSQYAVTQignSGRIIACDLLPMDP 89
Cdd:PRK11760 186 SRSTLKLEEafhvfipRDEWDERLAPGMRAVDLGAAPGGWTYQLVRR---GMFVTAVDNGPMAQ 246
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-166 4.97e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 46.65  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802  54 TVVDLGAAPGGWSQYAVtqIGNSGRIIACDLLPM-----------DPIVGVDFLQGDFRDELVLKallervgDSKVQVVM 122
Cdd:cd02440    1 RVLDLGCGTGALALALA--SGPGARVTGVDISPValelarkaaaaLLADNVEVLKGDAEELPPEA-------DESFDVII 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489007802 123 SDMApnmcgtpavdIPRAMYLVELALEMSRDVLAPGGSFVVKVF 166
Cdd:cd02440   72 SDPP----------LHHLVEDLARFLEEARRLLKPGGVLVLTLV 105
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 51-86 5.94e-06

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 46.21  E-value: 5.94e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 489007802  51 PGMTVVDLGAAPGGWSQYAVTQIGNSGRIIACDLLP 86
Cdd:PRK14904 250 PGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYP 285
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 50-84 1.74e-04

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 41.53  E-value: 1.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489007802  50 KPGMTVVDLGAAPGGWSqyavTQI----GNSGRIIACDL 84
Cdd:COG0144  248 KPGERVLDLCAAPGGKT----LHLaelmGNKGRVVAVDI 282
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 50-83 7.83e-04

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 39.53  E-value: 7.83e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489007802  50 KPGMTVVDLGAAPGGWSQYAVTQIGNSGRIIACD 83
Cdd:PRK14901 251 QPGEVILDACAAPGGKTTHIAELMGDQGEIWAVD 284
capping_2-OMTase_Flaviviridae cd20761
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
 33-72 1.68e-03

Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Flaviviridae viruses, comprise a family of ss(+)RNA viruses, cap their mRNAs. The 2'OMTase activity is located in the non-structural protein 5 (NS5).


Pssm-ID: 467736  Cd Length: 225  Bit Score: 37.97  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489007802  33 SRAWFKLDEI-QQSDkiFKPGMTVVDLGAAPGGWSQYAVTQ 72
Cdd:cd20761   37 SRGYAKLRWLvERGY--VKPSGKVVDLGCGRGGWSQYAAGL 75
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-159 2.25e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.00  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489007802   55 VVDLGAAPGGWSQYAVTQIGnsGRIIACDLLP-M---------DPIVGVDFLQGDFRDelvlkalLErVGDSKVQVVMSD 124
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPeMlerareraaEAGLNVEFVQGDAED-------LP-FPDGSFDLVVSS 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 489007802  125 MAPNMCGTPavDIPRAMylvelaLEMSRdVLAPGG 159
Cdd:pfam13649  71 GVLHHLPDP--DLEAAL------REIAR-VLKPGG 96
 
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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