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Conserved domains on  [gi|27151491|sp|Q9D0D4|]
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RecName: Full=Probable dimethyladenosine transferase; AltName: Full=DIM1 dimethyladenosine transferase 1 homolog; AltName: Full=DIM1 dimethyladenosine transferase 1-like; AltName: Full=Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase; AltName: Full=Probable 18S rRNA dimethylase; AltName: Full=Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase

Protein Classification

rRNA adenine N(6)-methyltransferase family protein( domain architecture ID 10794378)

rRNA adenine N(6)-methyltransferase family protein is a class I SAM-dependent methyltransferase, similar to Schizosaccharomyces pombe dimethyladenosine transferase that specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008173
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 27-312 1.58e-176

dimethyladenosine transferase-like protein; Provisional


:

Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 489.51  E-value: 1.58e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPLASK 106
Cdd:PTZ00338   7 GMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  107 LQVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVD 186
Cdd:PTZ00338  87 LEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  187 HLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVQNTVI 266
Cdd:PTZ00338 167 HLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKV 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 27151491  267 PEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 247 PVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
 
Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 27-312 1.58e-176

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 489.51  E-value: 1.58e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPLASK 106
Cdd:PTZ00338   7 GMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  107 LQVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVD 186
Cdd:PTZ00338  87 LEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  187 HLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVQNTVI 266
Cdd:PTZ00338 167 HLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKV 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 27151491  267 PEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 247 PVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 35-305 3.15e-85

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: 256.77  E-value: 3.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:TIGR00755   8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   115 LKSDLPFFD----ACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755  85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSavqqlleknyrihcsvqntvIPED 269
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNL--------------------LSEL 224

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 27151491   270 FsiadkiqQILTSTGFS-DKRARSMDIDDFIRLLHGF 305
Cdd:TIGR00755 225 V-------ELLEELGIDpDKRVEQLSPEDFLRLANLL 254
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 35-301 1.58e-84

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: 255.44  E-value: 1.58e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:COG0030  16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETF---AAYPNLTVIEGDA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491 115 LKSDLP-----FFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030  93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAvqqlleknyrihcsvqntvip 267
Cdd:COG0030 173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSLF--------------------- 231

                       250       260       270
                ....*....|....*....|....*....|....*
gi 27151491 268 edfsIADKIQQILTSTGFS-DKRARSMDIDDFIRL 301
Cdd:COG0030 232 ----SKERLEEALEAAGIDpTARAEELSVEEFARL 262
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-213 1.62e-77

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 233.94  E-value: 1.62e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491     44 IVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtplASKLQVLVGDVLKSDLPF-- 121
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    122 FDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650  78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157

                          170
                   ....*....|..
gi 27151491    202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
27-255 2.17e-75

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 231.87  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtpLASK 106
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   107 LQVLVGDVLKSDLP-------FFDACVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398  78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27151491   179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-160 4.58e-08

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: 50.51  E-value: 4.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  60 VLEVGPGTGNMTVKLLE-KAKKVVACELDPRLVAELhKRVQGTPLASKLQVLVGDVLK-SDLPF--FDACVANLPYQISS 135
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEElPPEADesFDVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|....*..
gi 27151491 136 PFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440  81 EDLARFLeeARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 27-312 1.58e-176

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 489.51  E-value: 1.58e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPLASK 106
Cdd:PTZ00338   7 GMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  107 LQVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVD 186
Cdd:PTZ00338  87 LEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  187 HLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVQNTVI 266
Cdd:PTZ00338 167 HLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKV 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 27151491  267 PEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 247 PVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 35-305 3.15e-85

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: 256.77  E-value: 3.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:TIGR00755   8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   115 LKSDLPFFD----ACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755  85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSavqqlleknyrihcsvqntvIPED 269
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNL--------------------LSEL 224

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 27151491   270 FsiadkiqQILTSTGFS-DKRARSMDIDDFIRLLHGF 305
Cdd:TIGR00755 225 V-------ELLEELGIDpDKRVEQLSPEDFLRLANLL 254
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 35-301 1.58e-84

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: 255.44  E-value: 1.58e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:COG0030  16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETF---AAYPNLTVIEGDA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491 115 LKSDLP-----FFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030  93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAvqqlleknyrihcsvqntvip 267
Cdd:COG0030 173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSLF--------------------- 231

                       250       260       270
                ....*....|....*....|....*....|....*
gi 27151491 268 edfsIADKIQQILTSTGFS-DKRARSMDIDDFIRL 301
Cdd:COG0030 232 ----SKERLEEALEAAGIDpTARAEELSVEEFARL 262
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
28-246 3.63e-79

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 241.34  E-value: 3.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   28 LMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRvqgTPLASKL 107
Cdd:PRK14896   1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD---EIAAGNV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  108 QVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRpfFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDH 187
Cdd:PRK14896  78 EIIEGDALKVDLPEFNKVVSNLPYQISSPITFKLLKHG--FEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  188 LMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQE-WDGLVRITFVRKNKTLSAAFKSSA 246
Cdd:PRK14896 156 VEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTLRNALKNSA 215
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-213 1.62e-77

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 233.94  E-value: 1.62e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491     44 IVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtplASKLQVLVGDVLKSDLPF-- 121
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    122 FDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650  78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157

                          170
                   ....*....|..
gi 27151491    202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
27-255 2.17e-75

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 231.87  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtpLASK 106
Cdd:pfam00398   1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   107 LQVLVGDVLKSDLP-------FFDACVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398  78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27151491   179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 48-129 8.03e-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: 8.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPLasKLQVLVGDVlkSDLPF----FD 123
Cdd:COG2226  14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA--EDLPFpdgsFD 89


                ....*.
gi 27151491 124 ACVANL 129
Cdd:COG2226  90 LVISSF 95
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-145 5.07e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.95  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    60 VLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPLasKLQVLVGDVLksDLPF----FDACVANLPYQIS 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAE--DLPFpdgsFDLVVSSGVLHHL 76

                          90
                  ....*....|.
gi 27151491   135 SPFVFKLLLHR 145
Cdd:pfam13649  77 PDPDLEAALRE 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-160 4.58e-08

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: 50.51  E-value: 4.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  60 VLEVGPGTGNMTVKLLE-KAKKVVACELDPRLVAELhKRVQGTPLASKLQVLVGDVLK-SDLPF--FDACVANLPYQISS 135
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEElPPEADesFDVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|....*..
gi 27151491 136 PFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440  81 EDLARFLeeARRLLKPGGVLVLTLVLA 107
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 35-93 4.76e-07

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 49.32  E-value: 4.76e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27151491  35 GQHILKnPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAE 93
Cdd:COG2518  46 GQTISQ-PYIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAER 103
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 45-128 7.68e-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: 47.32  E-value: 7.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  45 VNSIIDKAALRPTDVvLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtplASKLQVLVGDVLksDLPF--- 121
Cdd:COG2227  14 LAALLARLLPAGGRV-LDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA----ELNVDFVQGDLE--DLPLedg 86


                ....*...
gi 27151491 122 -FDACVAN 128
Cdd:COG2227  87 sFDLVICS 94
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-129 1.30e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 45.73  E-value: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27151491    61 LEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtplaSKLQVLVGDVlkSDLPF----FDACVANL 129
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPR----EGLTFVVGDA--EDLPFpdnsFDLVLSSE 67
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
51-120 3.41e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 47.34  E-value: 3.41e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27151491  51 KAALRPTDVVLEVGPGTGNMTVKLLEK-AKKVVACELDPRLVAELHKRVQGTPLASKLQVLVGDVLKSDLP 120
Cdd:COG4076  30 ERVVKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 48-127 5.00e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.69  E-value: 5.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPLASKLQVLVGDVLksDLPF---FD 123
Cdd:COG2230  43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYR--DLPAdgqFD 120


                ....
gi 27151491 124 ACVA 127
Cdd:COG2230 121 AIVS 124
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
39-97 6.01e-06

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 45.97  E-value: 6.01e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27151491  39 LKNPLIVNSII-----------DKAALRPTDVVLEVGPGTGNMTVKLLE---KAKKVVACELDPRLVAELHKR 97
Cdd:COG3963  17 LRNPRTVGAIApssralaramaSEVDWSGAGPVVELGPGTGVFTRAILArgvPDARLLAVEINPEFAEHLRRR 89
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 35-128 9.84e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.68  E-value: 9.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPLaSKLQVLVGD 113
Cdd:COG0500   5 YYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIALARARAAKAGL-GNVEFLVAD 83

                        90
                ....*....|....*...
gi 27151491 114 VLKSD---LPFFDACVAN 128
Cdd:COG0500  84 LAELDplpAESFDLVVAF 101
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 52-131 1.48e-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: 45.52  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  52 AALRPTDVVLEVGPGTGNMTVKLLEK--AKKVVACELDPRLVAELHKRVQGTPLASKLQVLVGDV--LKSDLP--FFDAC 125
Cdd:COG4123  33 APVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLkeFAAELPpgSFDLV 112


                ....*.
gi 27151491 126 VANLPY 131
Cdd:COG4123 113 VSNPPY 118
PRK14968 PRK14968
putative methyltransferase; Provisional
 48-131 1.52e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491   48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLV--AELHKRVQGTPlASKLQVLVGDVLKsdlPF---- 121
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVecAKCNAKLNNIR-NNGVEVIRSDLFE---PFrgdk 90

                         90
                 ....*....|
gi 27151491  122 FDACVANLPY 131
Cdd:PRK14968  91 FDVILFNPPY 100
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 46-131 3.11e-05

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: 43.69  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491    46 NSIIDKAALR--PTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPLasKLQVLVGDVLKSDLPFFD 123
Cdd:TIGR00537   7 DSLLLEANLRelKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV--GLDVVMTDLFKGVRGKFD 84


                  ....*...
gi 27151491   124 ACVANLPY 131
Cdd:TIGR00537  85 VILFNPPY 92
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-128 4.28e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 41.73  E-value: 4.28e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27151491  56 PTDVVLEVGPGTGNMTVKLLEKAK--KVVACELDPRLVAELHKRVQGtplaskLQVLVGDVLksDLPF---FDACVAN 128
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARARARLPN------VRFVVADLR--DLDPpepFDLVVSN 70
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 60-127 2.18e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.75  E-value: 2.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27151491   60 VLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPLASKLQVLVGDvLKSDLPFFDACVA 127
Cdd:PRK07580  67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD-LESLLGRFDTVVC 133
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-128 1.95e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.96  E-value: 1.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27151491    61 LEVGPGTGNMTVKLLEKAK--KVVACELDPRLVAELHKRVQGTPL--ASKLQVLVGDVLKSDLPFFDACVAN 128
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALEAARERLAALGLlnAVRVELFQLDLGELDPGSFDVVVAS 72
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
43-131 3.41e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.67  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27151491  43 LIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRvqgtplASKLQVLVGDVlkSDLPF- 121
Cdd:COG4976  33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK------GVYDRLLVADL--ADLAEp 104

                        90
                ....*....|....*
gi 27151491 122 ---FDACVAN--LPY 131
Cdd:COG4976 105 dgrFDLIVAAdvLTY 119
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 41-92 8.39e-03

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 37.46  E-value: 8.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 27151491  41 NPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVA 92
Cdd:COG2265 218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269
 
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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