|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
27-312 |
2.21e-175 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 486.82 E-value: 2.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGTPLASK 106
Cdd:PTZ00338 7 GMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 107 LQVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVD 186
Cdd:PTZ00338 87 LEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 187 HLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVQNTVI 266
Cdd:PTZ00338 167 HLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKV 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 74222329 267 PEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 247 PVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
35-305 |
1.48e-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: 252.54 E-value: 1.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:TIGR00755 8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 115 LKSDLPFFD----ACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755 85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSavqqlleknyrihcsvqntvIPED 269
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNL--------------------LSEL 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 74222329 270 FsiadkiqQILTSTGFS-DKRARSMDIDDFIRLLHGF 305
Cdd:TIGR00755 225 V-------ELLEELGIDpDKRVEQLSPEDFLRLANLL 254
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
35-301 |
5.16e-82 |
|
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: 248.89 E-value: 5.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:COG0030 16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETF---AAYPNLTVIEGDA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 115 LKSDLP-----FFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030 93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAvqqlleknyrihcsvqntvip 267
Cdd:COG0030 173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSLF--------------------- 231
|
250 260 270
....*....|....*....|....*....|....*
gi 74222329 268 edfsIADKIQQILTSTGFS-DKRARSMDIDDFIRL 301
Cdd:COG0030 232 ----SKERLEEALEAAGIDpTARAEELSVEEFARL 262
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
44-213 |
1.64e-75 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 228.93 E-value: 1.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 44 IVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGtplASKLQVLVGDVLKSDLPF-- 121
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 122 FDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
gi 74222329 202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
27-255 |
6.41e-74 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 228.02 E-value: 6.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQgtpLASK 106
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 107 LQVLVGDVLKSDLP-------FFDACVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398 78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74222329 179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
60-160 |
2.39e-06 |
|
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: 45.50 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 60 VLEVGPGTGNMTVKLLE-KAKKVVACGLDPRLVAELhKRVQGTPLASKLQVLVGDVLK-SDLPF--FDACVANLPYQISS 135
Cdd:cd02440 2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEElPPEADesFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....*..
gi 74222329 136 PFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440 81 EDLARFLeeARRLLKPGGVLVLTLVLA 107
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
27-312 |
2.21e-175 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 486.82 E-value: 2.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGTPLASK 106
Cdd:PTZ00338 7 GMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 107 LQVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVD 186
Cdd:PTZ00338 87 LEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLCRVT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 187 HLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVQNTVI 266
Cdd:PTZ00338 167 HLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMINKKV 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 74222329 267 PEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 247 PVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
35-305 |
1.48e-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: 252.54 E-value: 1.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:TIGR00755 8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 115 LKSDLPFFD----ACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755 85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSavqqlleknyrihcsvqntvIPED 269
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNL--------------------LSEL 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 74222329 270 FsiadkiqQILTSTGFS-DKRARSMDIDDFIRLLHGF 305
Cdd:TIGR00755 225 V-------ELLEELGIDpDKRVEQLSPEDFLRLANLL 254
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
35-301 |
5.16e-82 |
|
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: 248.89 E-value: 5.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVqgtPLASKLQVLVGDV 114
Cdd:COG0030 16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETF---AAYPNLTVIEGDA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 115 LKSDLP-----FFDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030 93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAvqqlleknyrihcsvqntvip 267
Cdd:COG0030 173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSLF--------------------- 231
|
250 260 270
....*....|....*....|....*....|....*
gi 74222329 268 edfsIADKIQQILTSTGFS-DKRARSMDIDDFIRL 301
Cdd:COG0030 232 ----SKERLEEALEAAGIDpTARAEELSVEEFARL 262
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
28-246 |
1.85e-77 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 237.11 E-value: 1.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 28 LMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRvqgTPLASKL 107
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD---EIAAGNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 108 QVLVGDVLKSDLPFFDACVANLPYQISSPFVFKLLLHRpfFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDH 187
Cdd:PRK14896 78 EIIEGDALKVDLPEFNKVVSNLPYQISSPITFKLLKHG--FEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 188 LMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQE-WDGLVRITFVRKNKTLSAAFKSSA 246
Cdd:PRK14896 156 VEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTLRNALKNSA 215
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
44-213 |
1.64e-75 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 228.93 E-value: 1.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 44 IVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGtplASKLQVLVGDVLKSDLPF-- 121
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 122 FDACVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
gi 74222329 202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
27-255 |
6.41e-74 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 228.02 E-value: 6.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 27 GLMFNTGIGQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQgtpLASK 106
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 107 LQVLVGDVLKSDLP-------FFDACVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398 78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74222329 179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
48-129 |
1.18e-10 |
|
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: 58.85 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGTPLasKLQVLVGDVlkSDLPF----FD 123
Cdd:COG2226 14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA--EDLPFpdgsFD 89
|
....*.
gi 74222329 124 ACVANL 129
Cdd:COG2226 90 LVISSF 95
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-145 |
2.03e-07 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 48.33 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 60 VLEVGPGTGNMTVKLLEKAK-KVVACGLDPRLVAELHKRVQGTPLasKLQVLVGDVLksDLPF----FDACVANLPYQIS 134
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAE--DLPFpdgsFDLVVSSGVLHHL 76
|
90
....*....|.
gi 74222329 135 SPFVFKLLLHR 145
Cdd:pfam13649 77 PDPDLEAALRE 87
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
60-160 |
2.39e-06 |
|
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: 45.50 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 60 VLEVGPGTGNMTVKLLE-KAKKVVACGLDPRLVAELhKRVQGTPLASKLQVLVGDVLK-SDLPF--FDACVANLPYQISS 135
Cdd:cd02440 2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEElPPEADesFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....*..
gi 74222329 136 PFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440 81 EDLARFLeeARRLLKPGGVLVLTLVLA 107
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-129 |
2.46e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 42.27 E-value: 2.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74222329 61 LEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGtplaSKLQVLVGDVlkSDLPF----FDACVANL 129
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPR----EGLTFVVGDA--EDLPFpdnsFDLVLSSE 67
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
45-128 |
3.07e-05 |
|
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: 42.70 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 45 VNSIIDKAALRPTDVvLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQgtplASKLQVLVGDVLksDLPF--- 121
Cdd:COG2227 14 LAALLARLLPAGGRV-LDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA----ELNVDFVQGDLE--DLPLedg 86
|
....*...
gi 74222329 122 -FDACVAN 128
Cdd:COG2227 87 sFDLVICS 94
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
48-127 |
5.03e-05 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 42.99 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACGLDPRLVAELHKRVQGTPLASKLQVLVGDVLksDLPF---FD 123
Cdd:COG2230 43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYR--DLPAdgqFD 120
|
....
gi 74222329 124 ACVA 127
Cdd:COG2230 121 AIVS 124
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
35-93 |
7.93e-05 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 42.77 E-value: 7.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 74222329 35 GQHILKnPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAE 93
Cdd:COG2518 46 GQTISQ-PYIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAER 103
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
46-131 |
8.05e-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: 42.54 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 46 NSIIDKAALR--PTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGTPLasKLQVLVGDVLKSDLPFFD 123
Cdd:TIGR00537 7 DSLLLEANLRelKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV--GLDVVMTDLFKGVRGKFD 84
|
....*...
gi 74222329 124 ACVANLPY 131
Cdd:TIGR00537 85 VILFNPPY 92
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
35-128 |
8.19e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 42.98 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 35 GQHILKNPLIVNSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACGLDPRLVAELHKRVQGTPLaSKLQVLVGD 113
Cdd:COG0500 5 YYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIALARARAAKAGL-GNVEFLVAD 83
|
90
....*....|....*...
gi 74222329 114 VLKSD---LPFFDACVAN 128
Cdd:COG0500 84 LAELDplpAESFDLVVAF 101
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
48-131 |
9.66e-05 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 42.58 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACGLDPRLV--AELHKRVQGTPlASKLQVLVGDVLKsdlPF---- 121
Cdd:PRK14968 15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVecAKCNAKLNNIR-NNGVEVIRSDLFE---PFrgdk 90
|
90
....*....|
gi 74222329 122 FDACVANLPY 131
Cdd:PRK14968 91 FDVILFNPPY 100
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
51-120 |
1.18e-04 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 42.72 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74222329 51 KAALRPTDVVLEVGPGTGNMTVKLLEK-AKKVVACGLDPRLVAELHKRVQGTPLASKLQVLVGDVLKSDLP 120
Cdd:COG4076 30 ERVVKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP 100
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
56-128 |
4.94e-04 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 38.65 E-value: 4.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74222329 56 PTDVVLEVGPGTGNMTVKLLEKAKKVVACGLD--PRLVAELHKRVQGtplaskLQVLVGDVLksDLPF---FDACVAN 128
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDlsPEMLARARARLPN------VRFVVADLR--DLDPpepFDLVVSN 70
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
60-127 |
5.50e-04 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 40.59 E-value: 5.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74222329 60 VLEVGPGTGNMTVKLLEKAKKVVACGLDPRLVAELHKRVQGTPLASKLQVLVGDvLKSDLPFFDACVA 127
Cdd:PRK07580 67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD-LESLLGRFDTVVC 133
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
39-97 |
5.66e-04 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 40.19 E-value: 5.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74222329 39 LKNPLIVNSII-----------DKAALRPTDVVLEVGPGTGNMTVKLLE---KAKKVVACGLDPRLVAELHKR 97
Cdd:COG3963 17 LRNPRTVGAIApssralaramaSEVDWSGAGPVVELGPGTGVFTRAILArgvPDARLLAVEINPEFAEHLRRR 89
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
52-131 |
1.73e-03 |
|
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: 38.97 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74222329 52 AALRPTDVVLEVGPGTGNMTVKLLEK--AKKVVACGLDPRLVAELHKRVQGTPLASKLQVLVGDV--LKSDLP--FFDAC 125
Cdd:COG4123 33 APVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLkeFAAELPpgSFDLV 112
|
....*.
gi 74222329 126 VANLPY 131
Cdd:COG4123 113 VSNPPY 118
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