|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
28-317 |
9.44e-155 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 434.82 E-value: 9.44e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPVEKKL 107
Cdd:PTZ00338 8 MVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYFDICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTH 187
Cdd:PTZ00338 88 EVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVTH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 188 IMKVGKNNFRPPPQVESSVVRLEIKNPRPQVDYNEWDGLLRIVFVRKNRTISAGFKSTTVMDILEKNYKTFLAMNNEMVD 267
Cdd:PTZ00338 168 LMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKVP 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
6RBD_y 268 DTKGSMhdvvKEKIDTVLKETDLGDKRAGKCDQNDFLRLLYAFHQVGIHF 317
Cdd:PTZ00338 248 VSLEPF----KEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
27-282 |
1.15e-101 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 298.90 E-value: 1.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 27 VFKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRgtpVEKK 106
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 107 LEIMLGDFMKTELPYF-------DICISNTPYQISSPLVFKLINQPRPPRV-SILMFQREFALRLLARPGDSLYCRLSAN 178
Cdd:pfam00398 78 LTVIHQDFLKFEFPSLvthihqeFLVVGNLPYNISTPIVKQLLFESRFGIVdMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 179 VQMWANVTHIMKVGKNNFRPPPQVESSVVRLEIKNPR--PQVDYNEWDGLLRIVFVRKNRTISAGFKSTTVMDILEKNYK 256
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSS 237
|
250 260
....*....|....*....|....*.
6RBD_y 257 TFLAMNNEMVDDTKGSMHDVVKEKID 282
Cdd:pfam00398 238 HGINDNALVKKLSPEQTLDIFNELAK 263
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
28-310 |
1.52e-93 |
|
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: 277.96 E-value: 1.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVrgtPVEKKL 107
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYFDI----CISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWA 183
Cdd:TIGR00755 78 EIIEGDALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 184 NVTHIMKVGKNNFRPPPQVESSVVRLEIKNPRPQ-VDYNEWDGLLRIVFVRKNRTISagfksttvmdileKNYKTFLAmn 262
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSpKDFALFEELLKAAFQQRRKTLR-------------NNLKNLLS-- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
6RBD_y 263 nemvddtkgsmhdvvkeKIDTVLKETDL-GDKRAGKCDQNDFLRLLYAF 310
Cdd:TIGR00755 223 -----------------ELVELLEELGIdPDKRVEQLSPEDFLRLANLL 254
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
44-213 |
2.11e-73 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 223.54 E-value: 2.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 44 VAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPvekKLEIMLGDFMKTELPY-- 121
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAAD---NLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 122 FDICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTHIMKVGKNNFRPPPQ 201
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
6RBD_y 202 VESSVVRLEIKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
28-253 |
3.19e-71 |
|
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: 221.54 E-value: 3.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPvekKL 107
Cdd:COG0030 9 LRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYP---NL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYF-----DICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMW 182
Cdd:COG0030 86 TVIEGDALKVDLPALaagepLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6RBD_y 183 ANVTHIMKVGKNNFRPPPQVESSVVRLEiKNPRPQVDYNEWDGLLRIV---FVRKNRTI----SAGFKSTTVMDILEK 253
Cdd:COG0030 166 ADVEILFTVPPEAFYPPPKVDSAVVRLT-PRPEPLVPVADEKLFFRVVkaaFSQRRKTLrnslKSLFSKERLEEALEA 242
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
60-144 |
3.96e-09 |
|
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: 53.59 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 60 VLEVGPGTGNLTVRILEQ-AKNVVAVEMDPRMaAELTKRVRGTPVEKKLEIMLGDFMK---TELPYFDICISNTPYQISS 135
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVA-LELARKAAAALLADNVEVLKGDAEElppEADESFDVIISDPPLHHLV 80
|
....*....
6RBD_y 136 PLVFKLINQ 144
Cdd:cd02440 81 EDLARFLEE 89
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
28-317 |
9.44e-155 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 434.82 E-value: 9.44e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPVEKKL 107
Cdd:PTZ00338 8 MVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYFDICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTH 187
Cdd:PTZ00338 88 EVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVTH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 188 IMKVGKNNFRPPPQVESSVVRLEIKNPRPQVDYNEWDGLLRIVFVRKNRTISAGFKSTTVMDILEKNYKTFLAMNNEMVD 267
Cdd:PTZ00338 168 LMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKVP 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
6RBD_y 268 DTKGSMhdvvKEKIDTVLKETDLGDKRAGKCDQNDFLRLLYAFHQVGIHF 317
Cdd:PTZ00338 248 VSLEPF----KEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
27-282 |
1.15e-101 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 298.90 E-value: 1.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 27 VFKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRgtpVEKK 106
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 107 LEIMLGDFMKTELPYF-------DICISNTPYQISSPLVFKLINQPRPPRV-SILMFQREFALRLLARPGDSLYCRLSAN 178
Cdd:pfam00398 78 LTVIHQDFLKFEFPSLvthihqeFLVVGNLPYNISTPIVKQLLFESRFGIVdMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 179 VQMWANVTHIMKVGKNNFRPPPQVESSVVRLEIKNPR--PQVDYNEWDGLLRIVFVRKNRTISAGFKSTTVMDILEKNYK 256
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSS 237
|
250 260
....*....|....*....|....*.
6RBD_y 257 TFLAMNNEMVDDTKGSMHDVVKEKID 282
Cdd:pfam00398 238 HGINDNALVKKLSPEQTLDIFNELAK 263
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
28-310 |
1.52e-93 |
|
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: 277.96 E-value: 1.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVrgtPVEKKL 107
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYFDI----CISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWA 183
Cdd:TIGR00755 78 EIIEGDALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 184 NVTHIMKVGKNNFRPPPQVESSVVRLEIKNPRPQ-VDYNEWDGLLRIVFVRKNRTISagfksttvmdileKNYKTFLAmn 262
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSpKDFALFEELLKAAFQQRRKTLR-------------NNLKNLLS-- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
6RBD_y 263 nemvddtkgsmhdvvkeKIDTVLKETDL-GDKRAGKCDQNDFLRLLYAF 310
Cdd:TIGR00755 223 -----------------ELVELLEELGIdPDKRVEQLSPEDFLRLANLL 254
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
44-213 |
2.11e-73 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 223.54 E-value: 2.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 44 VAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPvekKLEIMLGDFMKTELPY-- 121
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAAD---NLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 122 FDICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTHIMKVGKNNFRPPPQ 201
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
6RBD_y 202 VESSVVRLEIKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
28-253 |
3.19e-71 |
|
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: 221.54 E-value: 3.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPvekKL 107
Cdd:COG0030 9 LRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYP---NL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYF-----DICISNTPYQISSPLVFKLINQPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMW 182
Cdd:COG0030 86 TVIEGDALKVDLPALaagepLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6RBD_y 183 ANVTHIMKVGKNNFRPPPQVESSVVRLEiKNPRPQVDYNEWDGLLRIV---FVRKNRTI----SAGFKSTTVMDILEK 253
Cdd:COG0030 166 ADVEILFTVPPEAFYPPPKVDSAVVRLT-PRPEPLVPVADEKLFFRVVkaaFSQRRKTLrnslKSLFSKERLEEALEA 242
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
28-253 |
2.00e-67 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 211.68 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 28 FKFNTDLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRvrgTPVEKKL 107
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD---EIAAGNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 108 EIMLGDFMKTELPYFDICISNTPYQISSPLVFKLInqPRPPRVSILMFQREFALRLLARPGDSLYCRLSANVQMWANVTH 187
Cdd:PRK14896 78 EIIEGDALKVDLPEFNKVVSNLPYQISSPITFKLL--KHGFEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6RBD_y 188 IMKVGKNNFRPPPQVESSVVRLEIKNPRPQVDYNE-WDGLLRIVFVRKNRTISAGFKSTTVMDILEK 253
Cdd:PRK14896 156 VEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTLRNALKNSAHISGKED 222
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
48-128 |
7.47e-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: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 48 IVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPVekKLEIMLGDFMKTELP--YFDIC 125
Cdd:COG2226 14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPdgSFDLV 91
|
...
6RBD_y 126 ISN 128
Cdd:COG2226 92 ISS 94
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
60-144 |
3.96e-09 |
|
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: 53.59 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 60 VLEVGPGTGNLTVRILEQ-AKNVVAVEMDPRMaAELTKRVRGTPVEKKLEIMLGDFMK---TELPYFDICISNTPYQISS 135
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVA-LELARKAAAALLADNVEVLKGDAEElppEADESFDVIISDPPLHHLV 80
|
....*....
6RBD_y 136 PLVFKLINQ 144
Cdd:cd02440 81 EDLARFLEE 89
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-168 |
2.65e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 50.64 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 60 VLEVGPGTGNLTVRILEQAK-NVVAVEMDPRMAAELTKRVRGTPVekKLEIMLGDFMKTELP--YFDICISNtpyqissp 136
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPdgSFDLVVSS-------- 70
|
90 100 110
....*....|....*....|....*....|..
6RBD_y 137 LVFKLINQPRPPRVsilmFQRefALRLLaRPG 168
Cdd:pfam13649 71 GVLHHLPDPDLEAA----LRE--IARVL-KPG 95
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
51-127 |
4.45e-08 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 52.73 E-value: 4.45e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6RBD_y 51 KAQIRPSDVVLEVGPGTGNLTVRILEQ-AKNVVAVEMDPRMAAELTKRVRGTPVEKKLEIMLGDFMKTELP-YFDICIS 127
Cdd:COG4076 30 ERVVKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPeKADVIIS 108
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
50-131 |
6.29e-08 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 51.82 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 50 DKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRmAAELTKR-VRGTPV-EKKLEIMLGDFMKTELPY-FDICI 126
Cdd:PRK14968 17 ENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPY-AVECAKCnAKLNNIrNNGVEVIRSDLFEPFRGDkFDVIL 95
|
....*
6RBD_y 127 SNTPY 131
Cdd:PRK14968 96 FNPPY 100
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
26-131 |
2.35e-07 |
|
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: 50.91 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 26 SVFKFNTD---LGQHilknplvaqgivdkAQIRPSDVVLEVGPGTGNLTVrILEQ---AKNVVAVEMDPRMAAELTKRVR 99
Cdd:COG4123 18 CGYRFGTDavlLAAF--------------APVKKGGRVLDLGTGTGVIAL-MLAQrspGARITGVEIQPEAAELARRNVA 82
|
90 100 110
....*....|....*....|....*....|....*.
6RBD_y 100 GTPVEKKLEIMLGDF--MKTELP--YFDICISNTPY 131
Cdd:COG4123 83 LNGLEDRITVIHGDLkeFAAELPpgSFDLVVSNPPY 118
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-128 |
6.16e-07 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 46.89 E-value: 6.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 61 LEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRgtpvEKKLEIMLGDFMKTELP--YFDICISN 128
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP----REGLTFVVGDAEDLPFPdnSFDLVLSS 66
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
39-97 |
1.23e-06 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 48.28 E-value: 1.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6RBD_y 39 LKNPLV-----------AQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQ---AKNVVAVEMDPRMAAELTKR 97
Cdd:COG3963 17 LRNPRTvgaiapssralARAMASEVDWSGAGPVVELGPGTGVFTRAILARgvpDARLLAVEINPEFAEHLRRR 89
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
48-127 |
2.29e-06 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 46.85 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 48 IVDKAQIRPSDVVLEVGPGTGNLTVRILEQAK-NVVAVEMDPRMAAELTKRVRGTPVEKKLEIMLGDFMKTELP-YFDIC 125
Cdd:COG2230 43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADgQFDAI 122
|
..
6RBD_y 126 IS 127
Cdd:COG2230 123 VS 124
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
55-131 |
2.92e-06 |
|
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 129628 [Multi-domain] Cd Length: 179 Bit Score: 46.77 E-value: 2.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6RBD_y 55 RPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPrMAAELTKRvRGTPVEKKLEIMLGDFMKTELPYFDICISNTPY 131
Cdd:TIGR00537 18 LKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINP-FAVKELRE-NAKLNNVGLDVVMTDLFKGVRGKFDVILFNPPY 92
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
51-128 |
3.66e-06 |
|
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: 45.39 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 51 KAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAELTKRVRGTPVekklEIMLGDFMKTELP--YFDICISN 128
Cdd:COG2227 19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLPLEdgSFDLVICS 94
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
56-128 |
4.72e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 44.43 E-value: 4.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
6RBD_y 56 PSDVVLEVGPGTGNLTVRILEQAKN--VVAVEMDPRMAAELTKRVRGtpvekkLEIMLGDFMKTELPY-FDICISN 128
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFPGarVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEpFDLVVSN 70
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
35-93 |
1.20e-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: 1.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 35 GQHILKnP-LVAQgIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAE 93
Cdd:COG2518 46 GQTISQ-PyIVAR-MLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAER 103
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-128 |
1.22e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 37.73 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6RBD_y 61 LEVGPGTGNLTVRILEQAKN--VVAVEMDPRM---AAELTKRVRGTPVEkKLEIMLGDFMKTELPYFDICISN 128
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGleYTGLDISPAAleaARERLAALGLLNAV-RVELFQLDLGELDPGSFDVVVAS 72
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
43-128 |
1.24e-03 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 39.21 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 43 LVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAAeltkRVRGTPVEKKLEimLGDFMKTELPY- 121
Cdd:COG4976 33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLA----KAREKGVYDRLL--VADLADLAEPDg 106
|
....*...
6RBD_y 122 -FDICISN 128
Cdd:COG4976 107 rFDLIVAA 114
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
33-129 |
1.55e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 39.13 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 33 DLGQHILKNPLVAQGIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAK-NVVAVEMDPRMAAELTKRVRGTPVeKKLEIML 111
Cdd:COG0500 3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIALARARAAKAGL-GNVEFLV 81
|
90 100
....*....|....*....|.
6RBD_y 112 GDFMKTE---LPYFDICISNT 129
Cdd:COG0500 82 ADLAELDplpAESFDLVVAFG 102
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
41-92 |
2.63e-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: 39.00 E-value: 2.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
6RBD_y 41 NPLVAQGIVDKA----QIRPSDVVLEVGPGTGNLTVRILEQAKNVVAVEMDPRMAA 92
Cdd:COG2265 214 NPEQAEALYAAAlewlDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
53-132 |
2.63e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 38.76 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 53 QIRPSDVVLEVGPGTGNLTVRILEQAKN---VVAVEMDPRMAAELTKRVRGTpvEKKLEIMLGDfmKTELP----YFDIC 125
Cdd:PRK08317 16 AVQPGDRVLDVGCGPGNDARELARRVGPegrVVGIDRSEAMLALAKERAAGL--GPNVEFVRGD--ADGLPfpdgSFDAV 91
|
....*..
6RBD_y 126 ISNTPYQ 132
Cdd:PRK08317 92 RSDRVLQ 98
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
48-114 |
5.90e-03 |
|
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: 37.45 E-value: 5.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 48 IVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKN---VVAVEMDPRMAAELTKRVRGTPVEKKLEIMLGDF 114
Cdd:COG2519 83 IIARLDIFPGARVLEAGTGSGALTLALARAVGPegkVYSYERREDFAEIARKNLERFGLPDNVELKLGDI 152
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
43-131 |
7.12e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 37.45 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 43 LVAQgIVDKAQIRPSDVVLEVGPGTGNLTVRILEQAKN--VVAVEMDPRmAAELTKRVRGTPVEKKLEIMLGDFMkTELP 120
Cdd:PRK09328 96 LVEW-ALEALLLKEPLRVLDLGTGSGAIALALAKERPDaeVTAVDISPE-ALAVARRNAKHGLGARVEFLQGDWF-EPLP 172
|
90
....*....|...
6RBD_y 121 Y--FDICISNTPY 131
Cdd:PRK09328 173 GgrFDLIVSNPPY 185
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
49-94 |
7.54e-03 |
|
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 37.43 E-value: 7.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
6RBD_y 49 VDKAQIRPSDVVLEVGPGT-GNLTVRILEQ--AKNVVAVEMDP---RMAAEL 94
Cdd:COG1063 154 VERAGVKPGDTVLVIGAGPiGLLAALAARLagAARVIVVDRNPerlELAREL 205
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
43-131 |
9.33e-03 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 37.05 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RBD_y 43 LVAQgIVDKAQIRPSDVVLEVGPGTGNLTV---RILEQAKnVVAVEMDPRmAAELTKR-VRGTPVEKKLEIMLGDFMK-- 116
Cdd:COG2890 100 LVEL-ALALLPAGAPPRVLDLGTGSGAIALalaKERPDAR-VTAVDISPD-ALAVARRnAERLGLEDRVRFLQGDLFEpl 176
|
90
....*....|....*
6RBD_y 117 TELPYFDICISNTPY 131
Cdd:COG2890 177 PGDGRFDLIVSNPPY 191
|
|
| |
