|
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
|
|
|