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Conserved domains on  [gi|446733577|ref|WP_000810833|]
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MULTISPECIES: 23S rRNA (adenine(2058)-N(6))-methyltransferase Erm(A) [Bacteria]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 1-239 7.84e-72

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.).


The actual alignment was detected with superfamily member pfam00398:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 263  Bit Score: 220.31  E-value: 7.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    1 MKQKNPKNTQNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKV 80
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   81 IHEDILKFSFPKNTD-----YKIFGNIPYNISTDIVKKIAFDSQA--KYSYLIVERGFAKRLQNT-----QRALGLLLMV 148
Cdd:pfam00398  81 IHQDFLKFEFPSLVThihqeFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLARpgsklYSRLSVLRQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  149 EMDIKILKKVPRAYFHPKPNVDSVLIVLERHKPFILK-KDYKKYRFFVYKWVNREYHVLFTK------NQLRQVLKHANV 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPHPvKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240

                         250       260
                  ....*....|....*....|.
gi 446733577  222 TD---LDKLSNEQFLSVFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
1-239 7.84e-72

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 220.31  E-value: 7.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    1 MKQKNPKNTQNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKV 80
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   81 IHEDILKFSFPKNTD-----YKIFGNIPYNISTDIVKKIAFDSQA--KYSYLIVERGFAKRLQNT-----QRALGLLLMV 148
Cdd:pfam00398  81 IHQDFLKFEFPSLVThihqeFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLARpgsklYSRLSVLRQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  149 EMDIKILKKVPRAYFHPKPNVDSVLIVLERHKPFILK-KDYKKYRFFVYKWVNREYHVLFTK------NQLRQVLKHANV 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPHPvKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240

                         250       260
                  ....*....|....*....|.
gi 446733577  222 TD---LDKLSNEQFLSVFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
rADc smart00650
Ribosomal RNA adenine dimethylases;
18-180 1.67e-67

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 205.82  E-value: 1.67e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    18 HVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHEDILKFSFPKNTDYK 97
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    98 IFGNIPYNISTDIVKKIAFDSQA-KYSYLIVERGFAKRLQN-----TQRALGLLLMVEMDIKILKKVPRAYFHPKPNVDS 171
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAAkpgskDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*....
gi 446733577   172 VLIVLERHK 180
Cdd:smart00650 161 AVVRLERRP 169
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 10-240 2.21e-44

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: 149.89  E-value: 2.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  10 QNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHEDILKFS 89
Cdd:COG0030   17 QNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKVD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  90 FPK---NTDYKIFGNIPYNISTDIVKK-IAFDSQAKYSYLIVERGFAKRL--QNTQRALGLL-LMVE--MDIKILKKVPR 160
Cdd:COG0030   97 LPAlaaGEPLKVVGNLPYNISTPILFKlLEARPPIEDAVLMVQKEVAERLvaKPGSKDYGRLsVLVQyyADVEILFTVPP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577 161 AYFHPKPNVDSVLIVLERHKPFILK-KDYKKYRFFVykwvnreyHVLF---------------TKNQLRQVLKHANVtDL 224
Cdd:COG0030  177 EAFYPPPKVDSAVVRLTPRPEPLVPvADEKLFFRVV--------KAAFsqrrktlrnslkslfSKERLEEALEAAGI-DP 247

                        250       260
                 ....*....|....*....|
gi 446733577 225 DK----LSNEQFLSVFNSYK 240
Cdd:COG0030  248 TAraeeLSVEEFARLANALK 267
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-191 1.30e-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: 124.27  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   10 QNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHEDILKFS 89
Cdd:TIGR00755   9 QNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   90 FPKNTD--YKIFGNIPYNISTDIVKK-IAFDSQAKYSYLIVERGFAKRL-----QNTQRALGLLLMVEMDIKILKKVPRA 161
Cdd:TIGR00755  89 LNELAKdlTKVVGNLPYNISSPLIFKlLKEKDAFKLAVLMVQKEVAERLvakpgSKDYGRLSVLVQYYANVEIVFKVPPS 168

                         170       180       190
                  ....*....|....*....|....*....|
gi 446733577  162 YFHPKPNVDSVLIVLERHKPFILKKDYKKY 191
Cdd:TIGR00755 169 AFYPPPKVDSAVVRLVPLKRKPSPKDFALF 198
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
5-195 8.97e-32

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 116.92  E-value: 8.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   5 NPKNTQNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHED 84
Cdd:PRK14896   4 NKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  85 ILKFSFPKNTdyKIFGNIPYNISTDIVKKIaFDSQAKYSYLIVERGFAKRLQN---TQRALGLLLMVE--MDIKILKKVP 159
Cdd:PRK14896  84 ALKVDLPEFN--KVVSNLPYQISSPITFKL-LKHGFEPAVLMYQKEFAERMVAkpgTKEYGRLSVMVQyyADVEIVEKVP 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446733577 160 RAYFHPKPNVDSVLIVLERHKPFILKKDYKKYRFFV 195
Cdd:PRK14896 161 PGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFV 196
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 33-104 1.15e-05

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: 43.19  E-value: 1.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446733577  33 KIIEIGSGKGHFTKELVEMS-QRVNAIEIDEGLCHATKKAVE--PFQNIKVIHEDILKFSFPKNTDY-KIFGNIPY 104
Cdd:cd02440    1 RVLDLGCGTGALALALASGPgARVTGVDISPVALELARKAAAalLADNVEVLKGDAEELPPEADESFdVIISDPPL 76
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
1-239 7.84e-72

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 220.31  E-value: 7.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    1 MKQKNPKNTQNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKV 80
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   81 IHEDILKFSFPKNTD-----YKIFGNIPYNISTDIVKKIAFDSQA--KYSYLIVERGFAKRLQNT-----QRALGLLLMV 148
Cdd:pfam00398  81 IHQDFLKFEFPSLVThihqeFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLARpgsklYSRLSVLRQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  149 EMDIKILKKVPRAYFHPKPNVDSVLIVLERHKPFILK-KDYKKYRFFVYKWVNREYHVLFTK------NQLRQVLKHANV 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPHPvKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240

                         250       260
                  ....*....|....*....|.
gi 446733577  222 TD---LDKLSNEQFLSVFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
rADc smart00650
Ribosomal RNA adenine dimethylases;
18-180 1.67e-67

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 205.82  E-value: 1.67e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    18 HVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHEDILKFSFPKNTDYK 97
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577    98 IFGNIPYNISTDIVKKIAFDSQA-KYSYLIVERGFAKRLQN-----TQRALGLLLMVEMDIKILKKVPRAYFHPKPNVDS 171
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAAkpgskDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*....
gi 446733577   172 VLIVLERHK 180
Cdd:smart00650 161 AVVRLERRP 169
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 10-240 2.21e-44

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: 149.89  E-value: 2.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  10 QNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHEDILKFS 89
Cdd:COG0030   17 QNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKVD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  90 FPK---NTDYKIFGNIPYNISTDIVKK-IAFDSQAKYSYLIVERGFAKRL--QNTQRALGLL-LMVE--MDIKILKKVPR 160
Cdd:COG0030   97 LPAlaaGEPLKVVGNLPYNISTPILFKlLEARPPIEDAVLMVQKEVAERLvaKPGSKDYGRLsVLVQyyADVEILFTVPP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577 161 AYFHPKPNVDSVLIVLERHKPFILK-KDYKKYRFFVykwvnreyHVLF---------------TKNQLRQVLKHANVtDL 224
Cdd:COG0030  177 EAFYPPPKVDSAVVRLTPRPEPLVPvADEKLFFRVV--------KAAFsqrrktlrnslkslfSKERLEEALEAAGI-DP 247

                        250       260
                 ....*....|....*....|
gi 446733577 225 DK----LSNEQFLSVFNSYK 240
Cdd:COG0030  248 TAraeeLSVEEFARLANALK 267
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-191 1.30e-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: 124.27  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   10 QNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHEDILKFS 89
Cdd:TIGR00755   9 QNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   90 FPKNTD--YKIFGNIPYNISTDIVKK-IAFDSQAKYSYLIVERGFAKRL-----QNTQRALGLLLMVEMDIKILKKVPRA 161
Cdd:TIGR00755  89 LNELAKdlTKVVGNLPYNISSPLIFKlLKEKDAFKLAVLMVQKEVAERLvakpgSKDYGRLSVLVQYYANVEIVFKVPPS 168

                         170       180       190
                  ....*....|....*....|....*....|
gi 446733577  162 YFHPKPNVDSVLIVLERHKPFILKKDYKKY 191
Cdd:TIGR00755 169 AFYPPPKVDSAVVRLVPLKRKPSPKDFALF 198
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
5-195 8.97e-32

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 116.92  E-value: 8.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   5 NPKNTQNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPFQNIKVIHED 84
Cdd:PRK14896   4 NKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  85 ILKFSFPKNTdyKIFGNIPYNISTDIVKKIaFDSQAKYSYLIVERGFAKRLQN---TQRALGLLLMVE--MDIKILKKVP 159
Cdd:PRK14896  84 ALKVDLPEFN--KVVSNLPYQISSPITFKL-LKHGFEPAVLMYQKEFAERMVAkpgTKEYGRLSVMVQyyADVEIVEKVP 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446733577 160 RAYFHPKPNVDSVLIVLERHKPFILKKDYKKYRFFV 195
Cdd:PRK14896 161 PGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFV 196
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 5-242 1.04e-15

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 74.65  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   5 NPKNTQNFITSKKHVKEILKYT----------NINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVE- 73
Cdd:PTZ00338   1 TGGSKSGMVFNKKFGQHILKNPlvldkivekaAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  74 --PFQNIKVIHEDILKFSFPKNTdyKIFGNIPYNISTDIV-KKIAFDSQAKYSYLIVERGFAKRLQ-------------N 137
Cdd:PTZ00338  81 spLASKLEVIEGDALKTEFPYFD--VCVANVPYQISSPLVfKLLAHRPLFRCAVLMFQKEFALRLLaqpgdelycrlsvN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577 138 TQralgLLLMVemdiKILKKVPRAYFHPKPNVDSVLIVLE-RHKPFILkkDYKKY----RF-FVYKwvNREYHVLFTKNQ 211
Cdd:PTZ00338 159 TQ----LLCRV----THLMKVSKNSFNPPPKVESSVVRIEpKNPPPDV--DFEEWdgllRIcFSRK--NKTLSAIFKTKS 226

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446733577 212 LRQVLKHaNVTDLDKLSNEQFLSVFNSYKLF 242
Cdd:PTZ00338 227 VLQTLEH-NYKSWCTMINKKVPVSLEPFKEF 256
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 29-93 9.19e-06

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 45.13  E-value: 9.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446733577  29 NKQDKIIEIGSGKGHFTkelVEMSQR---VN--AIEIDE-GLCHATKKAVE-PFQNIKVIHEDILKF--SFPKN 93
Cdd:COG0220   31 NDAPLVLEIGFGKGEFL---VELAAAnpdINfiGIEVHEpGVAKALKKAEEeGLTNVRLLRGDAVELleLFPDG 101
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 33-104 1.15e-05

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: 43.19  E-value: 1.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446733577  33 KIIEIGSGKGHFTKELVEMS-QRVNAIEIDEGLCHATKKAVE--PFQNIKVIHEDILKFSFPKNTDY-KIFGNIPY 104
Cdd:cd02440    1 RVLDLGCGTGALALALASGPgARVTGVDISPVALELARKAAAalLADNVEVLKGDAEELPPEADESFdVIISDPPL 76
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 33-94 3.49e-05

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: 42.31  E-value: 3.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446733577  33 KIIEIGSGKGHFTKELVEMSQRVNAIEIDEG-LCHATKKAVEpfQNIKVIHEDILKFSFPKNT 94
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGADVTGVDISPEaLEIARERAAE--LNVDFVQGDLEDLPLEDGS 87
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-94 3.91e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 41.40  E-value: 3.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446733577   34 IIEIGSGKGHFTKELVEMSQ-RVNAIEIDEG-LCHATKKAVEPFQNIKVIHEDILKFSFPKNT 94
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEmLERARERAAEAGLNVEFVQGDAEDLPFPDGS 63
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 29-93 2.01e-04

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 40.91  E-value: 2.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446733577  29 NKQDKIIEIGSGKGHFtkeLVEMSQR---VN--AIEI-DEGLCHATKKAVE-PFQNIKVIHEDILKF---SFPKN 93
Cdd:PRK00121  39 NDAPIHLEIGFGKGEF---LVEMAKAnpdINfiGIEVhEPGVGKALKKIEEeGLTNLRLLCGDAVEVlldMFPDG 110
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
14-114 2.43e-04

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 40.96  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  14 TSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVE-MS--QRVNAIEIDEGLCHATKKAvepFQNIKVIHED------ 84
Cdd:COG3963   29 SSRALARAMASEVDWSGAGPVVELGPGTGVFTRAILArGVpdARLLAVEINPEFAEHLRRR---FPRVTVVNGDaedlae 105

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446733577  85 ILKFSFPKNTDYKIFGnIPY-NISTDIVKKI 114
Cdd:COG3963  106 LLAEHGIGKVDAVVSG-LPLlSFPPELRRAI 135
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 35-94 3.27e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.80  E-value: 3.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   35 IEIGSGKGHFTKELVEMSQRVNAIEIDEGLCHATKKAVEPfQNIKVIHEDILKFSFPKNT 94
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPR-EGLTFVVGDAEDLPFPDNS 59
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 25-115 1.52e-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: 38.59  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577  25 YTNINKQDKIIEIGSGKGhftkeLV--EMSQRVN-----AIEIDEGLCHATKKAVE--PFQN-IKVIHEDILKFSFPKNT 94
Cdd:COG4123   32 FAPVKKGGRVLDLGTGTG-----VIalMLAQRSPgaritGVEIQPEAAELARRNVAlnGLEDrITVIHGDLKEFAAELPP 106

                         90       100       110
                 ....*....|....*....|....*....|
gi 446733577  95 ---DYkIFGNIPYN------ISTDIVKKIA 115
Cdd:COG4123  107 gsfDL-VVSNPPYFkagsgrKSPDEARAIA 135
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 34-103 5.05e-03

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 36.88  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446733577   34 IIEIGSGKGHFtkeLVEMSQR---VN--AIEI-----DEGLCHATKKAVepfQNIKVIHEDILKF---SFPKNTDYKIFG 100
Cdd:pfam02390   5 FLEIGCGMGGF---LVAMAKAnpdKNfiGIEIrvpgvAKALKKIDALGL---QNLRILCGNALDVlpnYFPPGSLQKIFI 78


                  ...
gi 446733577  101 NIP 103
Cdd:pfam02390  79 NFP 81
 
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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