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Conserved domains on  [gi|1143076924|ref|NP_001335005|]
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dimethyladenosine transferase isoform 2 [Homo sapiens]

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; ...
 24-263 5.28e-158

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 PTZ00338:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 294  Bit Score: 440.98  E-value: 5.28e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  24 SAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPV 103
Cdd:PTZ00338    4 SKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 104 ASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLA 183
Cdd:PTZ00338   84 ASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 184 RVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHN 263
Cdd:PTZ00338  164 RVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMIN 243
 
Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 24-263 5.28e-158

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 440.98  E-value: 5.28e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  24 SAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPV 103
Cdd:PTZ00338    4 SKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 104 ASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLA 183
Cdd:PTZ00338   84 ASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 184 RVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHN 263
Cdd:PTZ00338  164 RVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMIN 243
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 35-246 2.15e-82

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: 247.91  E-value: 2.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPVASKLQVLVGDV 114
Cdd:TIGR00755   8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 115 LKTDLPFFD----TCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755  85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1143076924 191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSA 246
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNLL 221
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 35-253 1.00e-81

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: 246.96  E-value: 1.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDV 114
Cdd:COG0030    16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAA---YPNLTVIEGDA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 115 LKTDLP-----FFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030    93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKS----SAVQQLLEK 253
Cdd:COG0030   173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSlfskERLEEALEA 242
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-213 1.24e-77

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 232.79  E-value: 1.24e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924   44 IINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDVLKTDLPF-- 121
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  122 FDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650  78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157

                          170
                   ....*....|..
gi 1143076924  202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
27-255 1.32e-75

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 231.10  E-value: 1.32e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  27 GLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtpVASK 106
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 107 LQVLVGDVLKTDLP-------FFDTCVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398  78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143076924 179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-160 1.46e-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: 48.58  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  60 VLEVGPGTGNMTVKLLE-KAKKVVACELDPRLVAELhKRVQGTPVASKLQVLVGDVLktDLPF-----FDTCVANLPYQI 133
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAE--ELPPeadesFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*....
gi 1143076924 134 SSPFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440    79 LVEDLARFLeeARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 24-263 5.28e-158

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 440.98  E-value: 5.28e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  24 SAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPV 103
Cdd:PTZ00338    4 SKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 104 ASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLA 183
Cdd:PTZ00338   84 ASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 184 RVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHN 263
Cdd:PTZ00338  164 RVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMIN 243
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 35-246 2.15e-82

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: 247.91  E-value: 2.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPVASKLQVLVGDV 114
Cdd:TIGR00755   8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 115 LKTDLPFFD----TCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755  85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1143076924 191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSA 246
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNLL 221
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 35-253 1.00e-81

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: 246.96  E-value: 1.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDV 114
Cdd:COG0030    16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAA---YPNLTVIEGDA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 115 LKTDLP-----FFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030    93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKS----SAVQQLLEK 253
Cdd:COG0030   173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSlfskERLEEALEA 242
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
28-246 1.67e-79

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 240.57  E-value: 1.67e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  28 LMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRvqgTPVASKL 107
Cdd:PRK14896    1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD---EIAAGNV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 108 QVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRpfFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDH 187
Cdd:PRK14896   78 EIIEGDALKVDLPEFNKVVSNLPYQISSPITFKLLKHG--FEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEI 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 188 LMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQE-WDGLVRITFVRKNKTLSAAFKSSA 246
Cdd:PRK14896  156 VEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTLRNALKNSA 215
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-213 1.24e-77

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 232.79  E-value: 1.24e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924   44 IINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDVLKTDLPF-- 121
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  122 FDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650  78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157

                          170
                   ....*....|..
gi 1143076924  202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
27-255 1.32e-75

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 231.10  E-value: 1.32e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  27 GLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtpVASK 106
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924 107 LQVLVGDVLKTDLP-------FFDTCVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398  78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143076924 179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 48-129 6.67e-12

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: 61.93  E-value: 6.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVasKLQVLVGDVlkTDLPF----FD 123
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA--EDLPFpdgsFD 89


                  ....*.
gi 1143076924 124 TCVANL 129
Cdd:COG2226    90 LVISSF 95
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-145 1.51e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.03  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  60 VLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPVasKLQVLVGDVlkTDLPF----FDTCVANLPYQIS 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL--NVEFVQGDA--EDLPFpdgsFDLVVSSGVLHHL 76

                          90
                  ....*....|.
gi 1143076924 135 SPFVFKLLLHR 145
Cdd:pfam13649  77 PDPDLEAALRE 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-160 1.46e-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: 48.58  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  60 VLEVGPGTGNMTVKLLE-KAKKVVACELDPRLVAELhKRVQGTPVASKLQVLVGDVLktDLPF-----FDTCVANLPYQI 133
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAE--ELPPeadesFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*....
gi 1143076924 134 SSPFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440    79 LVEDLARFLeeARRLLKPGGVLVLTLVLA 107
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 45-128 1.95e-07

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: 48.86  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  45 INSIIDKAALRPTDVvLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVasklQVLVGDVlkTDLPF--- 121
Cdd:COG2227    14 LAALLARLLPAGGRV-LDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDL--EDLPLedg 86


                  ....*...
gi 1143076924 122 -FDTCVAN 128
Cdd:COG2227    87 sFDLVICS 94
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-129 2.23e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.96  E-value: 2.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143076924  61 LEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvaSKLQVLVGDVlkTDLPF----FDTCVANL 129
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPR----EGLTFVVGDA--EDLPFpdnsFDLVLSSE 67
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 35-93 4.31e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 46.23  E-value: 4.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1143076924  35 GQHILKnPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAE 93
Cdd:COG2518    46 GQTISQ-PYIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAER 103
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
51-127 4.58e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 46.57  E-value: 4.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143076924  51 KAALRPTDVVLEVGPGTGNMTVKLLEK-AKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLPF-FDTCVA 127
Cdd:COG4076    30 ERVVKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEkADVIIS 108
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 46-131 7.33e-06

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 45.23  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  46 NSIIDKAALR--PTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVasKLQVLVGDVLKTDLPFFD 123
Cdd:TIGR00537   7 DSLLLEANLRelKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV--GLDVVMTDLFKGVRGKFD 84


                  ....*...
gi 1143076924 124 TCVANLPY 131
Cdd:TIGR00537  85 VILFNPPY 92
PRK14968 PRK14968
putative methyltransferase; Provisional
 48-131 8.26e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.27  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLV--AELHKRVQGTPvASKLQVLVGDVLKtdlPF---- 121
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVecAKCNAKLNNIR-NNGVEVIRSDLFE---PFrgdk 90

                          90
                  ....*....|
gi 1143076924 122 FDTCVANLPY 131
Cdd:PRK14968   91 FDVILFNPPY 100
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
39-97 9.51e-06

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 45.20  E-value: 9.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143076924  39 LKNPLIINSII-----------DKAALRPTDVVLEVGPGTGNMTVKLLE---KAKKVVACELDPRLVAELHKR 97
Cdd:COG3963    17 LRNPRTVGAIApssralaramaSEVDWSGAGPVVELGPGTGVFTRAILArgvPDARLLAVEINPEFAEHLRRR 89
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 48-127 1.53e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.15  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLP-FFDTC 125
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADgQFDAI 122


                  ..
gi 1143076924 126 VA 127
Cdd:COG2230   123 VS 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 35-123 2.88e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPvASKLQVLVGD 113
Cdd:COG0500     5 YYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIALARARAAKAG-LGNVEFLVAD 83

                          90
                  ....*....|...
gi 1143076924 114 VLKTD---LPFFD 123
Cdd:COG0500    84 LAELDplpAESFD 96
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 52-131 7.46e-05

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: 42.82  E-value: 7.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  52 AALRPTDVVLEVGPGTGNMTVKLLEK--AKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLPF----FDTC 125
Cdd:COG4123    33 APVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELppgsFDLV 112


                  ....*.
gi 1143076924 126 VANLPY 131
Cdd:COG4123   113 VSNPPY 118
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 60-127 1.70e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.75  E-value: 1.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143076924  60 VLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDvLKTDLPFFDTCVA 127
Cdd:PRK07580   67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD-LESLLGRFDTVVC 133
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-128 1.95e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143076924  56 PTDVVLEVGPGTGNMTVKLLEKAK--KVVACELDPRLVAELHKRVQGtpvaskLQVLVGDVLKTDLPF-FDTCVAN 128
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEpFDLVVSN 70
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-128 1.18e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 1.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143076924  61 LEVGPGTGNMTVKLLEKAK--KVVACELDPRLV--AELHKRVQGTPVASKLQVLVGDVLKTDLPFFDTCVAN 128
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALeaARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS 72
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
43-123 3.53e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.67  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143076924  43 LIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRvqgtpvASKLQVLVGDVlkTDLPFF 122
Cdd:COG4976    33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK------GVYDRLLVADL--ADLAEP 104


                  .
gi 1143076924 123 D 123
Cdd:COG4976   105 D 105
 
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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