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Conserved domains on  [gi|1841703223|gb|QJT41634|]
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ErmG [Cloning vector pMT406]

Protein Classification

rRNA adenine N(6)-methyltransferase family protein( domain architecture ID 10652749)

rRNA adenine N(6)-methyltransferase family protein similar to rRNA adenine N(6)-methyltransferase, also called 23S rRNA (adenine(2085)-N(6))-dimethyltransferase, that produces a dimethylation of the adenine residue at position 2085 in 23S rRNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rADc smart00650
Ribosomal RNA adenine dimethylases;
18-180 1.91e-68

Ribosomal RNA adenine dimethylases;


:

Pssm-ID: 128898  Cd Length: 169  Bit Score: 208.13  E-value: 1.91e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   18 HIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFTFPSHNPYK 97
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   98 IFGSIPYNISTNIIRKIVFESSA-TISYLIVEYGFAKMLL-----DTNRSLALLLMAEVDISILAKIPRYYFHPKPKVDS 171
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*....
gi 1841703223  172 TLIVLKRKP 180
Cdd:smart00650 161 AVVRLERRP 169
 
Name Accession Description Interval E-value
rADc smart00650
Ribosomal RNA adenine dimethylases;
18-180 1.91e-68

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 208.13  E-value: 1.91e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   18 HIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFTFPSHNPYK 97
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   98 IFGSIPYNISTNIIRKIVFESSA-TISYLIVEYGFAKMLL-----DTNRSLALLLMAEVDISILAKIPRYYFHPKPKVDS 171
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*....
gi 1841703223  172 TLIVLKRKP 180
Cdd:smart00650 161 AVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
1-239 2.05e-61

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 193.74  E-value: 2.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   1 MNKVNIKDSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQI 80
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  81 VNDDILKFTFPS-----HNPYKIFGSIPYNISTNIIRKIVFESSATI--SYLIVEYGFAKMLLDTN-----RSLALLLMA 148
Cdd:pfam00398  81 IHQDFLKFEFPSlvthiHQEFLVVGNLPYNISTPIVKQLLFESRFGIvdMLLMLQKEFARRLLARPgsklySRLSVLRQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRK-PAKMAFKERKKYETFVMKWVNKEYEKLFTK------NQFNKALKHARI 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHdPDPHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240

                         250       260
                  ....*....|....*....|.
gi 1841703223 222 YD---INNISFEQFVSLFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 9-240 1.75e-47

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 157.98  E-value: 1.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:COG0030    16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  89 TFPSH---NPYKIFGSIPYNISTNIIRKIvFESSATISYLIV-----------------EYGfakmlldtnrSLALLLMA 148
Cdd:COG0030    96 DLPALaagEPLKVVGNLPYNISTPILFKL-LEARPPIEDAVLmvqkevaerlvakpgskDYG----------RLSVLVQY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRKPA-KMAFKERKKYETFV--------------MKwvnkeyeKLFTKNQFN 213
Cdd:COG0030   165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEpLVPVADEKLFFRVVkaafsqrrktlrnsLK-------SLFSKERLE 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1841703223 214 KALKHARIyDIN----NISFEQFVSLFNSYK 240
Cdd:COG0030   238 EALEAAGI-DPTaraeELSVEEFARLANALK 267
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
9-219 1.36e-34

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 124.24  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:PRK14896    8 GQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGDALKV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  89 TFPSHNpyKIFGSIPYNISTNIIRKIV---FESSAtisyLIVEYGFAK-MLLDTNRS----LALLLMAEVDISILAKIPR 160
Cdd:PRK14896   88 DLPEFN--KVVSNLPYQISSPITFKLLkhgFEPAV----LMYQKEFAErMVAKPGTKeygrLSVMVQYYADVEIVEKVPP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1841703223 161 YYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFVmkwvnkeyEKLFTknQFNKALKHA 219
Cdd:PRK14896  162 GAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFV--------KALFQ--HRRKTLRNA 210
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-195 5.88e-34

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 122.72  E-value: 5.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  10 QNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFT 89
Cdd:TIGR00755   9 QNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  90 FPS--HNPYKIFGSIPYNISTNIIRKivfessatisyLIVE-YGFAKMLLDTNRSLALLLMAEV---------------- 150
Cdd:TIGR00755  89 LNElaKDLTKVVGNLPYNISSPLIFK-----------LLKEkDAFKLAVLMVQKEVAERLVAKPgskdygrlsvlvqyya 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1841703223 151 DISILAKIPRYYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFV 195
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELL 202
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 33-96 8.45e-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: 46.27  E-value: 8.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841703223  33 NIFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKLLNY--PNYQIVNDDILKFTFPSHNPY 96
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPEADESF 67
 
Name Accession Description Interval E-value
rADc smart00650
Ribosomal RNA adenine dimethylases;
18-180 1.91e-68

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 208.13  E-value: 1.91e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   18 HIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFTFPSHNPYK 97
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   98 IFGSIPYNISTNIIRKIVFESSA-TISYLIVEYGFAKMLL-----DTNRSLALLLMAEVDISILAKIPRYYFHPKPKVDS 171
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*....
gi 1841703223  172 TLIVLKRKP 180
Cdd:smart00650 161 AVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
1-239 2.05e-61

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 193.74  E-value: 2.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   1 MNKVNIKDSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQI 80
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  81 VNDDILKFTFPS-----HNPYKIFGSIPYNISTNIIRKIVFESSATI--SYLIVEYGFAKMLLDTN-----RSLALLLMA 148
Cdd:pfam00398  81 IHQDFLKFEFPSlvthiHQEFLVVGNLPYNISTPIVKQLLFESRFGIvdMLLMLQKEFARRLLARPgsklySRLSVLRQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRK-PAKMAFKERKKYETFVMKWVNKEYEKLFTK------NQFNKALKHARI 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHdPDPHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240

                         250       260
                  ....*....|....*....|.
gi 1841703223 222 YD---INNISFEQFVSLFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 9-240 1.75e-47

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 157.98  E-value: 1.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:COG0030    16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  89 TFPSH---NPYKIFGSIPYNISTNIIRKIvFESSATISYLIV-----------------EYGfakmlldtnrSLALLLMA 148
Cdd:COG0030    96 DLPALaagEPLKVVGNLPYNISTPILFKL-LEARPPIEDAVLmvqkevaerlvakpgskDYG----------RLSVLVQY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRKPA-KMAFKERKKYETFV--------------MKwvnkeyeKLFTKNQFN 213
Cdd:COG0030   165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEpLVPVADEKLFFRVVkaafsqrrktlrnsLK-------SLFSKERLE 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1841703223 214 KALKHARIyDIN----NISFEQFVSLFNSYK 240
Cdd:COG0030   238 EALEAAGI-DPTaraeELSVEEFARLANALK 267
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
9-219 1.36e-34

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 124.24  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:PRK14896    8 GQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGDALKV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  89 TFPSHNpyKIFGSIPYNISTNIIRKIV---FESSAtisyLIVEYGFAK-MLLDTNRS----LALLLMAEVDISILAKIPR 160
Cdd:PRK14896   88 DLPEFN--KVVSNLPYQISSPITFKLLkhgFEPAV----LMYQKEFAErMVAKPGTKeygrLSVMVQYYADVEIVEKVPP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1841703223 161 YYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFVmkwvnkeyEKLFTknQFNKALKHA 219
Cdd:PRK14896  162 GAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFV--------KALFQ--HRRKTLRNA 210
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-195 5.88e-34

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 122.72  E-value: 5.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  10 QNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFT 89
Cdd:TIGR00755   9 QNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  90 FPS--HNPYKIFGSIPYNISTNIIRKivfessatisyLIVE-YGFAKMLLDTNRSLALLLMAEV---------------- 150
Cdd:TIGR00755  89 LNElaKDLTKVVGNLPYNISSPLIFK-----------LLKEkDAFKLAVLMVQKEVAERLVAKPgskdygrlsvlvqyya 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1841703223 151 DISILAKIPRYYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFV 195
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELL 202
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 19-174 1.75e-08

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 53.85  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  19 IEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLN---YPNYQIVNDDILKFTFPSHNp 95
Cdd:PTZ00338   25 LDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNsplASKLEVIEGDALKTEFPYFD- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  96 yKIFGSIPYNISTNIIRKIV-----FESsatiSYLIVEYGFA-KMLLDTNRSLALLLMAEVD----ISILAKIPRYYFHP 165
Cdd:PTZ00338  104 -VCVANVPYQISSPLVFKLLahrplFRC----AVLMFQKEFAlRLLAQPGDELYCRLSVNTQllcrVTHLMKVSKNSFNP 178


                  ....*....
gi 1841703223 166 KPKVDSTLI 174
Cdd:PTZ00338  179 PPKVESSVV 187
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 33-96 8.45e-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: 46.27  E-value: 8.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841703223  33 NIFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKLLNY--PNYQIVNDDILKFTFPSHNPY 96
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPEADESF 67
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 28-96 1.13e-04

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 41.61  E-value: 1.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841703223  28 LDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKL--LNYPNYQIVNDDiLKFTFPSHNPY 96
Cdd:COG2518    64 LKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLaaLGYDNVTVRVGD-GALGWPEHAPF 133
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-92 1.26e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.85  E-value: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841703223  34 IFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKLL-NYPNYQIVNDDILKFTFPS 92
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAeAGLNVEFVQGDAEDLPFPD 61
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-93 1.76e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 40.39  E-value: 1.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841703223  28 LDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRnKLLNYPNYQIVNDDILKFTFPSH 93
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR-ERAAELNVDFVQGDLEDLPLEDG 86
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 8-96 7.16e-04

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.51  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223   8 DSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKL--LNYPNYQIVNDD 84
Cdd:COG0500     4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAakAGLGNVEFLVAD 83

                          90
                  ....*....|..
gi 1841703223  85 ILKFTFPSHNPY 96
Cdd:COG0500    84 LAELDPLPAESF 95
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-93 1.22e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.26  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1841703223  36 EIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNdDILKFTFPSH 93
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVG-DAEDLPFPDN 58
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 26-183 5.91e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 37.05  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  26 ISLDEKDNIFEIGAGKGHFTAGLVKRCN--FVTAIEIDSKLCE-----VTRNKLLNypNYQIVNDDILKFTFPSH----- 93
Cdd:COG4123    33 APVKKGGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAElarrnVALNGLED--RITVIHGDLKEFAAELPpgsfd 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703223  94 ----NPykifgsiPYN------ISTNIIRKIV-FESSATISYLIveyGFAKMLLDTNRSLALLLMAEVDISILAKIPRYY 162
Cdd:COG4123   111 lvvsNP-------PYFkagsgrKSPDEARAIArHEDALTLEDLI---RAAARLLKPGGRFALIHPAERLAEILAALRKYG 180

                         170       180
                  ....*....|....*....|....*..
gi 1841703223 163 FHPK------PKVDstlivlkrKPAKM 183
Cdd:COG4123   181 LGPKrlrpvhPRPG--------KPAKR 199
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-91 8.91e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 35.74  E-value: 8.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841703223  20 EKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYP-NYQIVNDDILKFTFP 91
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFP 84
 
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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