|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
23-353 |
1.11e-159 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 448.68 E-value: 1.11e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 23 QGGISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFS 102
Cdd:PTZ00338 5 KSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 103 NRLKVIQGDVLKTELPRFDICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYAR 182
Cdd:PTZ00338 85 SKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 183 VSHLLKVGKNNFRPPPKVDSSVVRIEPRRPGPQVNKKEWDGFLRVCFIRKNKTLGSIFKQKSVLSMLEKNFKTLQavlaS 262
Cdd:PTZ00338 165 VTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWC----T 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 263 LQNNGEPALNttsmdlgdqsmgmedddnemddddmemdegegdggetSEFKEKVMNVLKEGGFEEKRSSKLSQQEFLYLL 342
Cdd:PTZ00338 241 MINKKVPVSL-------------------------------------EPFKEFIAEILEDSGMFEKRSVKLDIDDFLKLL 283
|
330
....*....|.
gi 15226591 343 SLFNKSGIHFT 353
Cdd:PTZ00338 284 LAFNKKGIHFV 294
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
25-241 |
3.03e-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: 256.21 E-value: 3.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 25 GISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPfsnR 104
Cdd:COG0030 8 GLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYP---N 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 105 LKVIQGDVLKTELPRF-----DICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQL 179
Cdd:COG0030 85 LTVIEGDALKVDLPALaagepLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQY 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226591 180 YARVSHLLKVGKNNFRPPPKVDSSVVRIEPRR--PGPQVNKKEWDGFLRVCFIRKNKTLGSIFK 241
Cdd:COG0030 165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPepLVPVADEKLFFRVVKAAFSQRRKTLRNSLK 228
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
26-242 |
2.47e-83 |
|
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: 253.31 E-value: 2.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 26 ISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFqgtPFSNRL 105
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 106 KVIQGDVLKTELPRFDI----CVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYA 181
Cdd:TIGR00755 78 EIIEGDALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226591 182 RVSHLLKVGKNNFRPPPKVDSSVVRIEPRRPGPQ-VNKKEWDGFLRVCFIRKNKTLGSIFKQ 242
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSpKDFALFEELLKAAFQQRRKTLRNNLKN 219
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
42-211 |
4.33e-82 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 247.04 E-value: 4.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 42 LVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGtpfSNRLKVIQGDVLKTELPR-- 119
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 120 FDICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYARVSHLLKVGKNNFRPPPK 199
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
gi 15226591 200 VDSSVVRIEPRR 211
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
25-255 |
1.28e-69 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 218.39 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 25 GISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPfsnR 104
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDE---N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 105 LKVIQGDVLKTELP-------RFDICVANIPYQISSPLTFKLLFHPT-SFRCAVIMYQREFAMRLVAQPGDNLYCRLSVN 176
Cdd:pfam00398 78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLFESRfGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 177 TQLYARVSHLLKVGKNNFRPPPKVDSSVVRIEPR--RPGPQVNKKEWDGFLRVCFIRKNKTLGSIFKQKSVLSMLEKNFK 254
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHdpDPHPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSS 237
|
.
gi 15226591 255 T 255
Cdd:pfam00398 238 H 238
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
58-140 |
1.80e-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: 54.74 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 58 ILEIGPGTGNLTKKLLEA-GKEVIAVELDSRMvLELQRRFQGTPFSNRLKVIQGDVLK---TELPRFDICVANIPYQISS 133
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVA-LELARKAAAALLADNVEVLKGDAEElppEADESFDVIISDPPLHHLV 80
|
....*..
gi 15226591 134 PLTFKLL 140
Cdd:cd02440 81 EDLARFL 87
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
23-353 |
1.11e-159 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 448.68 E-value: 1.11e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 23 QGGISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFS 102
Cdd:PTZ00338 5 KSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 103 NRLKVIQGDVLKTELPRFDICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYAR 182
Cdd:PTZ00338 85 SKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 183 VSHLLKVGKNNFRPPPKVDSSVVRIEPRRPGPQVNKKEWDGFLRVCFIRKNKTLGSIFKQKSVLSMLEKNFKTLQavlaS 262
Cdd:PTZ00338 165 VTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWC----T 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 263 LQNNGEPALNttsmdlgdqsmgmedddnemddddmemdegegdggetSEFKEKVMNVLKEGGFEEKRSSKLSQQEFLYLL 342
Cdd:PTZ00338 241 MINKKVPVSL-------------------------------------EPFKEFIAEILEDSGMFEKRSVKLDIDDFLKLL 283
|
330
....*....|.
gi 15226591 343 SLFNKSGIHFT 353
Cdd:PTZ00338 284 LAFNKKGIHFV 294
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
25-241 |
3.03e-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: 256.21 E-value: 3.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 25 GISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPfsnR 104
Cdd:COG0030 8 GLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYP---N 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 105 LKVIQGDVLKTELPRF-----DICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQL 179
Cdd:COG0030 85 LTVIEGDALKVDLPALaagepLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQY 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226591 180 YARVSHLLKVGKNNFRPPPKVDSSVVRIEPRR--PGPQVNKKEWDGFLRVCFIRKNKTLGSIFK 241
Cdd:COG0030 165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPepLVPVADEKLFFRVVKAAFSQRRKTLRNSLK 228
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
26-242 |
2.47e-83 |
|
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: 253.31 E-value: 2.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 26 ISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFqgtPFSNRL 105
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 106 KVIQGDVLKTELPRFDI----CVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYA 181
Cdd:TIGR00755 78 EIIEGDALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226591 182 RVSHLLKVGKNNFRPPPKVDSSVVRIEPRRPGPQ-VNKKEWDGFLRVCFIRKNKTLGSIFKQ 242
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSpKDFALFEELLKAAFQQRRKTLRNNLKN 219
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
42-211 |
4.33e-82 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 247.04 E-value: 4.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 42 LVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGtpfSNRLKVIQGDVLKTELPR-- 119
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 120 FDICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYARVSHLLKVGKNNFRPPPK 199
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
gi 15226591 200 VDSSVVRIEPRR 211
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
30-236 |
2.51e-81 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 248.28 E-value: 2.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 30 KSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFqgtPFSNRLKVIQ 109
Cdd:PRK14896 5 KKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDE---IAAGNVEIIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 110 GDVLKTELPRFDICVANIPYQISSPLTFKLLfhPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYARVSHLLKV 189
Cdd:PRK14896 82 GDALKVDLPEFNKVVSNLPYQISSPITFKLL--KHGFEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEIVEKV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15226591 190 GKNNFRPPPKVDSSVVRIEPRRPGPQVNKKE-WDGFLRVCFIRKNKTL 236
Cdd:PRK14896 160 PPGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTL 207
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
25-255 |
1.28e-69 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 218.39 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 25 GISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPfsnR 104
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDE---N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 105 LKVIQGDVLKTELP-------RFDICVANIPYQISSPLTFKLLFHPT-SFRCAVIMYQREFAMRLVAQPGDNLYCRLSVN 176
Cdd:pfam00398 78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLFESRfGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 177 TQLYARVSHLLKVGKNNFRPPPKVDSSVVRIEPR--RPGPQVNKKEWDGFLRVCFIRKNKTLGSIFKQKSVLSMLEKNFK 254
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHdpDPHPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSS 237
|
.
gi 15226591 255 T 255
Cdd:pfam00398 238 H 238
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
37-122 |
7.56e-13 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 66.39 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 37 LKNPL-----------LVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKE---VIAVELDSRMVLELQRRFqgtPfs 102
Cdd:COG3963 17 LRNPRtvgaiapssraLARAMASEVDWSGAGPVVELGPGTGVFTRAILARGVPdarLLAVEINPEFAEHLRRRF---P-- 91
|
90 100
....*....|....*....|..
gi 15226591 103 nRLKVIQGDV--LKTELPRFDI 122
Cdd:COG3963 92 -RVTVVNGDAedLAELLAEHGI 112
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
44-126 |
1.80e-11 |
|
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: 61.16 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 44 DSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFsnRLKVIQGDVLKTELP--RFD 121
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPdgSFD 89
|
....*
gi 15226591 122 ICVAN 126
Cdd:COG2226 90 LVISS 94
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
58-126 |
3.44e-10 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 56.42 E-value: 3.44e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226591 58 ILEIGPGTGNLTKKLLEA-GKEVIAVELDSRMVLELQRRFQGTPFsnRLKVIQGDVLKTELP--RFDICVAN 126
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPdgSFDLVVSS 70
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
50-129 |
5.17e-10 |
|
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: 59.00 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 50 AGIKSTDVILEIGPGTGN----LTKKLLEAgkEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDV--LKTELP--RFD 121
Cdd:COG4123 33 APVKKGGRVLDLGTGTGVialmLAQRSPGA--RITGVEIQPEAAELARRNVALNGLEDRITVIHGDLkeFAAELPpgSFD 110
|
....*...
gi 15226591 122 ICVANIPY 129
Cdd:COG4123 111 LVVSNPPY 118
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
58-140 |
1.80e-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: 54.74 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 58 ILEIGPGTGNLTKKLLEA-GKEVIAVELDSRMvLELQRRFQGTPFSNRLKVIQGDVLK---TELPRFDICVANIPYQISS 133
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVA-LELARKAAAALLADNVEVLKGDAEElppEADESFDVIISDPPLHHLV 80
|
....*..
gi 15226591 134 PLTFKLL 140
Cdd:cd02440 81 EDLARFL 87
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
58-126 |
3.84e-09 |
|
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: 54.25 E-value: 3.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226591 58 ILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTpfsnRLKVIQGDVLKTELP--RFDICVAN 126
Cdd:COG2227 28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEdgSFDLVICS 94
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
58-126 |
6.96e-09 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 52.52 E-value: 6.96e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226591 58 ILEIGPGTGNLTKKLLEA--GKEVIAVELDSRMVLELQRRFqgtpfsNRLKVIQGDVLKTELPR-FDICVAN 126
Cdd:COG4106 5 VLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEpFDLVVSN 70
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
59-126 |
1.18e-07 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 49.29 E-value: 1.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226591 59 LEIGPGTGNLTKKLLEA--GKEVIAVELDSRMVLELQRRFQGTPFSN--RLKVIQGDVLKTELPRFDICVAN 126
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPGSFDVVVAS 72
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
49-127 |
1.42e-07 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 51.58 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 49 KAGIKSTDVILEIGPGTGNLTKKLLEAG-KEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDVLKTELP-RFDICVAN 126
Cdd:COG4076 30 ERVVKPGDVVLDIGTGSGLLSMLAARAGaKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPeKADVIISE 109
|
.
gi 15226591 127 I 127
Cdd:COG4076 110 M 110
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
59-126 |
1.44e-07 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 48.82 E-value: 1.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 59 LEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGtpfsNRLKVIQGDVLKTELP--RFDICVAN 126
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPR----EGLTFVVGDAEDLPFPdnSFDLVLSS 66
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
41-126 |
1.28e-06 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 48.07 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 41 LLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFsnrlkvIQGDVLKTELP-- 118
Cdd:COG4976 33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRL------LVADLADLAEPdg 106
|
....*...
gi 15226591 119 RFDICVAN 126
Cdd:COG4976 107 RFDLIVAA 114
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
33-111 |
2.41e-06 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 47.39 E-value: 2.41e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226591 33 GQHILKnPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFSNrLKVIQGD 111
Cdd:COG2518 46 GQTISQ-PYIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYDN-VTVRVGD 122
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
31-126 |
6.09e-06 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 46.45 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 31 SKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEA-GKEVIAVELDSRMVLELQRRFQGTPFSNrLKVIQ 109
Cdd:COG0500 3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLGN-VEFLV 81
|
90 100
....*....|....*....|
gi 15226591 110 GDVLKTE---LPRFDICVAN 126
Cdd:COG0500 82 ADLAELDplpAESFDLVVAF 101
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
42-125 |
9.26e-06 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 45.31 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 42 LVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEA-GKEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDVLKTELP-R 119
Cdd:COG2230 39 KLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADgQ 118
|
....*.
gi 15226591 120 FDICVA 125
Cdd:COG2230 119 FDAIVS 124
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
41-129 |
1.16e-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: 45.23 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 41 LLVDSIVQKAGikstDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRrfQGTPFSNRLKVIQGDVLKTELPRF 120
Cdd:TIGR00537 10 LLEANLRELKP----DDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRE--NAKLNNVGLDVVMTDLFKGVRGKF 83
|
....*....
gi 15226591 121 DICVANIPY 129
Cdd:TIGR00537 84 DVILFNPPY 92
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
41-129 |
2.41e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 45.53 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 41 LLVDSIVQKAGIKSTDVILEIGPGTGN----LTKKLLEAgkEVIAVELDSRmVLELQRR-FQGTPFSNRLKVIQGDVLK- 114
Cdd:COG2890 99 ELVELALALLPAGAPPRVLDLGTGSGAialaLAKERPDA--RVTAVDISPD-ALAVARRnAERLGLEDRVRFLQGDLFEp 175
|
90
....*....|....*.
gi 15226591 115 -TELPRFDICVANIPY 129
Cdd:COG2890 176 lPGDGRFDLIVSNPPY 191
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
41-129 |
4.11e-05 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 43.73 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 41 LLVDSIVQKAGikstDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFSNR-LKVIQGDVLKTELPR 119
Cdd:PRK14968 14 LLAENAVDKKG----DRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPFRGD 89
|
90
....*....|.
gi 15226591 120 -FDICVANIPY 129
Cdd:PRK14968 90 kFDVILFNPPY 100
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
39-133 |
7.52e-05 |
|
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 42.63 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 39 NPLLVDSIVQKAGIKSTDVILEigP--GTGNLtkkLLEA---GKEVIAVELDSRMVLELQR---RFQGTPFsnrlKVIQG 110
Cdd:COG1041 11 DPRLARALVNLAGAKEGDTVLD--PfcGTGTI---LIEAgllGRRVIGSDIDPKMVEGAREnleHYGYEDA----DVIRG 81
|
90 100
....*....|....*....|....*
gi 15226591 111 DVLKTELP--RFDICVANIPYQISS 133
Cdd:COG1041 82 DARDLPLAdeSVDAIVTDPPYGRSS 106
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
41-129 |
2.03e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 39.37 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226591 41 LLVDSIVQKAGIKSTDVILEIGPGTGNLT---KKLLEaGKEVIAVELDSRmVLELQRRFQGTPFSNRLKVIQGDVLKT-E 116
Cdd:PRK09328 95 ELVEWALEALLLKEPLRVLDLGTGSGAIAlalAKERP-DAEVTAVDISPE-ALAVARRNAKHGLGARVEFLQGDWFEPlP 172
|
90
....*....|...
gi 15226591 117 LPRFDICVANIPY 129
Cdd:PRK09328 173 GGRFDLIVSNPPY 185
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
58-125 |
2.83e-03 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 38.66 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226591 58 ILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDvLKTELPRFDICVA 125
Cdd:PRK07580 67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD-LESLLGRFDTVVC 133
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
46-112 |
3.45e-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: 38.60 E-value: 3.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226591 46 IVQKAGIKSTDVILEIGPGTGNLTKKLLEA-GKE--VIAVELDSRMvLELQRR-FQGTPFSNRLKVIQGDV 112
Cdd:COG2519 83 IIARLDIFPGARVLEAGTGSGALTLALARAvGPEgkVYSYERREDF-AEIARKnLERFGLPDNVELKLGDI 152
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
58-123 |
8.55e-03 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 36.70 E-value: 8.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226591 58 ILEIGPGTGNLTKKLLEA---GKEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDVLKTeLPR-----FDIC 123
Cdd:COG4122 20 ILEIGTGTGYSTLWLARAlpdDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEV-LPRladgpFDLV 92
|
|
| |
