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Conserved domains on  [gi|56686170|dbj|BAD79392|]
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dimethyladenosine transferase [Synechococcus elongatus PCC 6301]

Protein Classification

ribosomal RNA small subunit methyltransferase A( domain architecture ID 10000482)

ribosomal RNA small subunit methyltransferase A specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle

CATH:  2.20.25.110
Gene Ontology:  GO:1904047|GO:0052908|GO:0031167
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
3-263 9.01e-103

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: 300.50  E-value: 9.01e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:COG0030  11 PKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  83 DILQLDWTAAIADRPRfanpsKVVANIPYNITGPILQSLLGtiaqpRRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:COG0030  91 DALKVDLPALAAGEPL-----KVVGNLPYNISTPILFKLLE-----ARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170 163 RVQYLASCERVCAVppksfspppkVQSTVICLKPRPWPQV-CNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEAAF 241
Cdd:COG0030 161 LVQYYADVEILFTVppeafypppkVDSAVVRLTPRPEPLVpVADEKLFFRVVKAAFSQRRKTLRNSLKSLFSKERLEEAL 240
                       250       260
                ....*....|....*....|..
gi 56686170 242 AAHQIAPEARAETLSIDQWIGL 263
Cdd:COG0030 241 EAAGIDPTARAEELSVEEFARL 262
 
Name Accession Description Interval E-value
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
3-263 9.01e-103

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: 300.50  E-value: 9.01e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:COG0030  11 PKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  83 DILQLDWTAAIADRPRfanpsKVVANIPYNITGPILQSLLGtiaqpRRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:COG0030  91 DALKVDLPALAAGEPL-----KVVGNLPYNISTPILFKLLE-----ARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170 163 RVQYLASCERVCAVppksfspppkVQSTVICLKPRPWPQV-CNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEAAF 241
Cdd:COG0030 161 LVQYYADVEILFTVppeafypppkVDSAVVRLTPRPEPLVpVADEKLFFRVVKAAFSQRRKTLRNSLKSLFSKERLEEAL 240
                       250       260
                ....*....|....*....|..
gi 56686170 242 AAHQIAPEARAETLSIDQWIGL 263
Cdd:COG0030 241 EAAGIDPTARAEELSVEEFARL 262
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
3-263 4.49e-81

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: 244.83  E-value: 4.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:TIGR00755   3 PRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    83 DILQLDWTAAIADRPrfanpsKVVANIPYNITGPILQSLLGTiaqprRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:TIGR00755  83 DALKFDLNELAKDLT------KVVGNLPYNISSPLIFKLLKE-----KDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   163 RVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPRPWPQVCNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSeqIEAAFA 242
Cdd:TIGR00755 152 LVQYYANVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELLKAAFQQRRKTLRNNLKNLLSE--LVELLE 229
                         250       260
                  ....*....|....*....|.
gi 56686170   243 AHQIAPEARAETLSIDQWIGL 263
Cdd:TIGR00755 230 ELGIDPDKRVEQLSPEDFLRL 250
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
1-269 5.22e-61

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 193.58  E-value: 5.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    1 MPARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLL 80
Cdd:PRK14896   1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   81 EGDILQLDWtaaiadrPRFanpSKVVANIPYNITGPILQSLLgtiaqprRPAFERLVLLVQQEVADRLCATPGQRAYGAL 160
Cdd:PRK14896  81 EGDALKVDL-------PEF---NKVVSNLPYQISSPITFKLL-------KHGFEPAVLMYQKEFAERMVAKPGTKEYGRL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  161 SVRVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPRPWPQVCNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEAA 240
Cdd:PRK14896 144 SVMVQYYADVEIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVKALFQHRRKTLRNALKNSAHISGKEDI 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 56686170  241 FAAHQIAPE----ARAETLSIDQWIGLCTDLGD 269
Cdd:PRK14896 224 KAVVEALPEellnKRVFQLSPEEIAELANLLYE 256
rADc smart00650
Ribosomal RNA adenine dimethylases;
17-198 1.31e-52

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 169.23  E-value: 1.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     17 ILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEGDILQLDWTAaiadr 96
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPK----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     97 prfANPSKVVANIPYNITGPILQSLLGTiaqprRPAFERLVLLVQQEVADRLCATPGQRAYGALSVRVQYLASCERVCAV 176
Cdd:smart00650  76 ---LQPYKVVGNLPYNISTPILFKLLEE-----PPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKV 147
                          170       180
                   ....*....|....*....|..
gi 56686170    177 PPKSFSPPPKVQSTVICLKPRP 198
Cdd:smart00650 148 PPSAFRPPPKVDSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
3-260 3.50e-51

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 168.70  E-value: 3.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:pfam00398   4 FRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIHQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    83 DILQLDwTAAIADRPRFanPSKVVANIPYNITGPILQSLLgtiaQPRRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:pfam00398  84 DFLKFE-FPSLVTHIHQ--EFLVVGNLPYNISTPIVKQLL----FESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   163 RVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPR---PWPQVcnNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEa 239
Cdd:pfam00398 157 LRQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHdpdPHPVK--DLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQ- 233
                         250       260
                  ....*....|....*....|.
gi 56686170   240 AFAAHQIAPEARAETLSIDQW 260
Cdd:pfam00398 234 AFSSHGINDNALVKKLSPEQT 254
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
32-127 2.63e-04

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: 39.72  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  32 RVLEIGPGRGALTQRLLAAVDGLV-AVELDRDLIGQLQQRF--GQAENFCLLEGDILQLDWTAaiadrprFANPSKVVAN 108
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVtGVDISPVALELARKAAaaLLADNVEVLKGDAEELPPEA-------DESFDVIISD 73
                        90
                ....*....|....*....
gi 56686170 109 IPYNITGPILQSLLGTIAQ 127
Cdd:cd02440  74 PPLHHLVEDLARFLEEARR 92
 
Name Accession Description Interval E-value
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
3-263 9.01e-103

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: 300.50  E-value: 9.01e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:COG0030  11 PKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  83 DILQLDWTAAIADRPRfanpsKVVANIPYNITGPILQSLLGtiaqpRRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:COG0030  91 DALKVDLPALAAGEPL-----KVVGNLPYNISTPILFKLLE-----ARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170 163 RVQYLASCERVCAVppksfspppkVQSTVICLKPRPWPQV-CNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEAAF 241
Cdd:COG0030 161 LVQYYADVEILFTVppeafypppkVDSAVVRLTPRPEPLVpVADEKLFFRVVKAAFSQRRKTLRNSLKSLFSKERLEEAL 240
                       250       260
                ....*....|....*....|..
gi 56686170 242 AAHQIAPEARAETLSIDQWIGL 263
Cdd:COG0030 241 EAAGIDPTARAEELSVEEFARL 262
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
3-263 4.49e-81

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: 244.83  E-value: 4.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:TIGR00755   3 PRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    83 DILQLDWTAAIADRPrfanpsKVVANIPYNITGPILQSLLGTiaqprRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:TIGR00755  83 DALKFDLNELAKDLT------KVVGNLPYNISSPLIFKLLKE-----KDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   163 RVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPRPWPQVCNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSeqIEAAFA 242
Cdd:TIGR00755 152 LVQYYANVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELLKAAFQQRRKTLRNNLKNLLSE--LVELLE 229
                         250       260
                  ....*....|....*....|.
gi 56686170   243 AHQIAPEARAETLSIDQWIGL 263
Cdd:TIGR00755 230 ELGIDPDKRVEQLSPEDFLRL 250
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
1-269 5.22e-61

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 193.58  E-value: 5.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    1 MPARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLL 80
Cdd:PRK14896   1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   81 EGDILQLDWtaaiadrPRFanpSKVVANIPYNITGPILQSLLgtiaqprRPAFERLVLLVQQEVADRLCATPGQRAYGAL 160
Cdd:PRK14896  81 EGDALKVDL-------PEF---NKVVSNLPYQISSPITFKLL-------KHGFEPAVLMYQKEFAERMVAKPGTKEYGRL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  161 SVRVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPRPWPQVCNNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEAA 240
Cdd:PRK14896 144 SVMVQYYADVEIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVKALFQHRRKTLRNALKNSAHISGKEDI 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 56686170  241 FAAHQIAPE----ARAETLSIDQWIGLCTDLGD 269
Cdd:PRK14896 224 KAVVEALPEellnKRVFQLSPEEIAELANLLYE 256
rADc smart00650
Ribosomal RNA adenine dimethylases;
17-198 1.31e-52

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 169.23  E-value: 1.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     17 ILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEGDILQLDWTAaiadr 96
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPK----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     97 prfANPSKVVANIPYNITGPILQSLLGTiaqprRPAFERLVLLVQQEVADRLCATPGQRAYGALSVRVQYLASCERVCAV 176
Cdd:smart00650  76 ---LQPYKVVGNLPYNISTPILFKLLEE-----PPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKV 147
                          170       180
                   ....*....|....*....|..
gi 56686170    177 PPKSFSPPPKVQSTVICLKPRP 198
Cdd:smart00650 148 PPSAFRPPPKVDSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
3-260 3.50e-51

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 168.70  E-value: 3.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170     3 ARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEG 82
Cdd:pfam00398   4 FRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIHQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    83 DILQLDwTAAIADRPRFanPSKVVANIPYNITGPILQSLLgtiaQPRRPAFERLVLLVQQEVADRLCATPGQRAYGALSV 162
Cdd:pfam00398  84 DFLKFE-FPSLVTHIHQ--EFLVVGNLPYNISTPIVKQLL----FESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   163 RVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPR---PWPQVcnNPGRLEKLLNQGFSAKRKMLRNNLKSLYSSEQIEa 239
Cdd:pfam00398 157 LRQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHdpdPHPVK--DLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQ- 233
                         250       260
                  ....*....|....*....|.
gi 56686170   240 AFAAHQIAPEARAETLSIDQW 260
Cdd:pfam00398 234 AFSSHGINDNALVKKLSPEQT 254
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
1-230 4.60e-50

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 166.72  E-value: 4.60e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170    1 MPARKRFGQHWLRSEAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRF---GQAENF 77
Cdd:PTZ00338   8 MVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFqnsPLASKL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   78 CLLEGDILQldwtaaiADRPRFanpSKVVANIPYNITGPILQSLLGtiaqpRRPAFERLVLLVQQEVADRLCATPGQRAY 157
Cdd:PTZ00338  88 EVIEGDALK-------TEFPYF---DVCVANVPYQISSPLVFKLLA-----HRPLFRCAVLMFQKEFALRLLAQPGDELY 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56686170  158 GALSVRVQYLASCERVCAVPPKSFSPPPKVQSTVICLKPRPWPQVCNNpGRLEKLLNQGFSAKRKMLRNNLKS 230
Cdd:PTZ00338 153 CRLSVNTQLLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDF-EEWDGLLRICFSRKNKTLSAIFKT 224
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
19-99 3.36e-08

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 52.52  E-value: 3.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  19 DRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDG---LVAVELDRDLIGQLQQRFGQAEnfcLLEGDILQLDWTAAIAD 95
Cdd:COG3963  35 RAMASEVDWSGAGPVVELGPGTGVFTRAILARGVPdarLLAVEINPEFAEHLRRRFPRVT---VVNGDAEDLAELLAEHG 111

                ....
gi 56686170  96 RPRF 99
Cdd:COG3963 112 IGKV 115
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
19-88 1.68e-07

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: 49.61  E-value: 1.68e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56686170  19 DRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAE-NFCLLEGDILQLD 88
Cdd:COG2226  12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLP 82
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
14-97 9.73e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.54  E-value: 9.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  14 SEAILDRIVAAAELRPSDRVLEIGPGRGALTqRLLAAVDGL--VAVELDRDLIGQLQQRFGQAENFCLLEgdILQLDWTA 91
Cdd:COG2230  36 QEAKLDLILRKLGLKPGMRVLDIGCGWGGLA-LYLARRYGVrvTGVTLSPEQLEYARERAAEAGLADRVE--VRLADYRD 112

                ....*.
gi 56686170  92 AIADRP 97
Cdd:COG2230 113 LPADGQ 118
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
21-84 9.77e-06

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 45.92  E-value: 9.77e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  21 IVAAAELRPSDRVLEIGPGRGALTQRLLAAV--DG-LVAVELDRDLIGQLQQ---RFGQAENFCLLEGDI 84
Cdd:COG2519  83 IIARLDIFPGARVLEAGTGSGALTLALARAVgpEGkVYSYERREDFAEIARKnleRFGLPDNVELKLGDI 152
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
15-95 1.02e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.99  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  15 EAILDRIVAAAELRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAEnfcLLEGDILQLDWTAAIA 94
Cdd:COG4976  32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDR---LLVADLADLAEPDGRF 108

                .
gi 56686170  95 D 95
Cdd:COG4976 109 D 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
29-88 1.06e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.06e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56686170  29 PSDRVLEIGPGRGALTQRLLAAVDG--LVAVELDRDLIGQLQQRFGQAEnfcLLEGDILQLD 88
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGarVTGVDLSPEMLARARARLPNVR---FVVADLRDLD 59
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
20-83 1.13e-05

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 45.08  E-value: 1.13e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56686170  20 RIVAAAELRPSDRVLEIGPGRG---ALTQRLLAAVdglVAVELDRDLIGQLQQRFGQA--ENFCLLEGD 83
Cdd:COG2518  57 RMLEALDLKPGDRVLEIGTGSGyqaAVLARLAGRV---YSVERDPELAERARERLAALgyDNVTVRVGD 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
33-88 2.22e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.47  E-value: 2.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 56686170    33 VLEIGPGRGALTQRLLAAVDG-LVAVELDRDLIGQLQQRFGQAE-NFCLLEGDILQLD 88
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLP 58
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
32-127 2.63e-04

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: 39.72  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  32 RVLEIGPGRGALTQRLLAAVDGLV-AVELDRDLIGQLQQRF--GQAENFCLLEGDILQLDWTAaiadrprFANPSKVVAN 108
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVtGVDISPVALELARKAAaaLLADNVEVLKGDAEELPPEA-------DESFDVIISD 73
                        90
                ....*....|....*....
gi 56686170 109 IPYNITGPILQSLLGTIAQ 127
Cdd:cd02440  74 PPLHHLVEDLARFLEEARR 92
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
23-111 3.49e-04

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: 40.90  E-value: 3.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170  23 AAAELRPSDRVLEIGPGRGA----LTQRLLAAVdgLVAVELDRDLIGQLQQRFGQ---AENFCLLEGDILQLdwtAAIAD 95
Cdd:COG4123  31 AFAPVKKGGRVLDLGTGTGVialmLAQRSPGAR--ITGVEIQPEAAELARRNVALnglEDRITVIHGDLKEF---AAELP 105
                        90
                ....*....|....*.
gi 56686170  96 RPRFANpskVVANIPY 111
Cdd:COG4123 106 PGSFDL---VVSNPPY 118
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
18-95 5.41e-04

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 39.23  E-value: 5.41e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56686170  18 LDRIVAAAeLRPSDRVLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRfGQAENFCLLEGDILQLDWTAAIAD 95
Cdd:COG2227  14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER-AAELNVDFVQGDLEDLPLEDGSFD 89
PRK08317 PRK08317
hypothetical protein; Provisional
19-109 1.42e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.15  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56686170   19 DRIVAAAELRPSDRVLEIGPGRGALTQRLLAAV--DG-LVAVELDRDLIGQLQQRFGQAE-NFCLLEGDILQLDW----- 89
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRVgpEGrVVGIDRSEAMLALAKERAAGLGpNVEFVRGDADGLPFpdgsf 88
                         90       100
                 ....*....|....*....|..
gi 56686170   90 TAAIADR--PRFANPSKVVANI 109
Cdd:PRK08317  89 DAVRSDRvlQHLEDPARALAEI 110
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
20-91 4.36e-03

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 37.29  E-value: 4.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56686170    20 RIVAAAELRPSDR----VLEIGPGRGALTQRLLAAVDGLVAVELDRDLIGQLQQRFGQAENFCLLEGDILQLDWTA 91
Cdd:pfam05401  30 RLAAILELCLGDGdaadALEIGCAAGAFTEMLAILCERLTVVDLMPEAIAKAQERTGKWSDIIWHECDICQFDLNA 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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