|
Name |
Accession |
Description |
Interval |
E-value |
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
18-180 |
1.91e-68 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 208.13 E-value: 1.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 18 HIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFTFPSHNPYK 97
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 98 IFGSIPYNISTNIIRKIVFESSA-TISYLIVEYGFAKMLL-----DTNRSLALLLMAEVDISILAKIPRYYFHPKPKVDS 171
Cdd:smart00650 81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160
|
....*....
gi 1841703296 172 TLIVLKRKP 180
Cdd:smart00650 161 AVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
1-239 |
2.05e-61 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 193.74 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 1 MNKVNIKDSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQI 80
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 81 VNDDILKFTFPS-----HNPYKIFGSIPYNISTNIIRKIVFESSATI--SYLIVEYGFAKMLLDTN-----RSLALLLMA 148
Cdd:pfam00398 81 IHQDFLKFEFPSlvthiHQEFLVVGNLPYNISTPIVKQLLFESRFGIvdMLLMLQKEFARRLLARPgsklySRLSVLRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRK-PAKMAFKERKKYETFVMKWVNKEYEKLFTK------NQFNKALKHARI 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHdPDPHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240
|
250 260
....*....|....*....|.
gi 1841703296 222 YD---INNISFEQFVSLFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
9-240 |
1.75e-47 |
|
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: 157.98 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:COG0030 16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 89 TFPSH---NPYKIFGSIPYNISTNIIRKIvFESSATISYLIV-----------------EYGfakmlldtnrSLALLLMA 148
Cdd:COG0030 96 DLPALaagEPLKVVGNLPYNISTPILFKL-LEARPPIEDAVLmvqkevaerlvakpgskDYG----------RLSVLVQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRKPA-KMAFKERKKYETFV--------------MKwvnkeyeKLFTKNQFN 213
Cdd:COG0030 165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEpLVPVADEKLFFRVVkaafsqrrktlrnsLK-------SLFSKERLE 237
|
250 260 270
....*....|....*....|....*....|.
gi 1841703296 214 KALKHARIyDIN----NISFEQFVSLFNSYK 240
Cdd:COG0030 238 EALEAAGI-DPTaraeELSVEEFARLANALK 267
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
9-219 |
1.36e-34 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 124.24 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:PRK14896 8 GQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGDALKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 89 TFPSHNpyKIFGSIPYNISTNIIRKIV---FESSAtisyLIVEYGFAK-MLLDTNRS----LALLLMAEVDISILAKIPR 160
Cdd:PRK14896 88 DLPEFN--KVVSNLPYQISSPITFKLLkhgFEPAV----LMYQKEFAErMVAKPGTKeygrLSVMVQYYADVEIVEKVPP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1841703296 161 YYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFVmkwvnkeyEKLFTknQFNKALKHA 219
Cdd:PRK14896 162 GAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFV--------KALFQ--HRRKTLRNA 210
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
10-195 |
5.88e-34 |
|
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: 122.72 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 10 QNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFT 89
Cdd:TIGR00755 9 QNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 90 FPS--HNPYKIFGSIPYNISTNIIRKivfessatisyLIVE-YGFAKMLLDTNRSLALLLMAEV---------------- 150
Cdd:TIGR00755 89 LNElaKDLTKVVGNLPYNISSPLIFK-----------LLKEkDAFKLAVLMVQKEVAERLVAKPgskdygrlsvlvqyya 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1841703296 151 DISILAKIPRYYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFV 195
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELL 202
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
33-96 |
8.45e-07 |
|
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: 46.27 E-value: 8.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841703296 33 NIFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKLLNY--PNYQIVNDDILKFTFPSHNPY 96
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPEADESF 67
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
18-180 |
1.91e-68 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 208.13 E-value: 1.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 18 HIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFTFPSHNPYK 97
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 98 IFGSIPYNISTNIIRKIVFESSA-TISYLIVEYGFAKMLL-----DTNRSLALLLMAEVDISILAKIPRYYFHPKPKVDS 171
Cdd:smart00650 81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160
|
....*....
gi 1841703296 172 TLIVLKRKP 180
Cdd:smart00650 161 AVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
1-239 |
2.05e-61 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 193.74 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 1 MNKVNIKDSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQI 80
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 81 VNDDILKFTFPS-----HNPYKIFGSIPYNISTNIIRKIVFESSATI--SYLIVEYGFAKMLLDTN-----RSLALLLMA 148
Cdd:pfam00398 81 IHQDFLKFEFPSlvthiHQEFLVVGNLPYNISTPIVKQLLFESRFGIvdMLLMLQKEFARRLLARPgsklySRLSVLRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRK-PAKMAFKERKKYETFVMKWVNKEYEKLFTK------NQFNKALKHARI 221
Cdd:pfam00398 161 FTDVKLVAKVPPSIFSPPPKVDSALVRLERHdPDPHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGI 240
|
250 260
....*....|....*....|.
gi 1841703296 222 YD---INNISFEQFVSLFNSY 239
Cdd:pfam00398 241 NDnalVKKLSPEQTLDIFNEL 261
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
9-240 |
1.75e-47 |
|
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: 157.98 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:COG0030 16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDALKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 89 TFPSH---NPYKIFGSIPYNISTNIIRKIvFESSATISYLIV-----------------EYGfakmlldtnrSLALLLMA 148
Cdd:COG0030 96 DLPALaagEPLKVVGNLPYNISTPILFKL-LEARPPIEDAVLmvqkevaerlvakpgskDYG----------RLSVLVQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 149 EVDISILAKIPRYYFHPKPKVDSTLIVLKRKPA-KMAFKERKKYETFV--------------MKwvnkeyeKLFTKNQFN 213
Cdd:COG0030 165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEpLVPVADEKLFFRVVkaafsqrrktlrnsLK-------SLFSKERLE 237
|
250 260 270
....*....|....*....|....*....|.
gi 1841703296 214 KALKHARIyDIN----NISFEQFVSLFNSYK 240
Cdd:COG0030 238 EALEAAGI-DPTaraeELSVEEFARLANALK 267
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
9-219 |
1.36e-34 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 124.24 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 9 SQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKF 88
Cdd:PRK14896 8 GQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEIIEGDALKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 89 TFPSHNpyKIFGSIPYNISTNIIRKIV---FESSAtisyLIVEYGFAK-MLLDTNRS----LALLLMAEVDISILAKIPR 160
Cdd:PRK14896 88 DLPEFN--KVVSNLPYQISSPITFKLLkhgFEPAV----LMYQKEFAErMVAKPGTKeygrLSVMVQYYADVEIVEKVPP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1841703296 161 YYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFVmkwvnkeyEKLFTknQFNKALKHA 219
Cdd:PRK14896 162 GAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFV--------KALFQ--HRRKTLRNA 210
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
10-195 |
5.88e-34 |
|
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: 122.72 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 10 QNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFT 89
Cdd:TIGR00755 9 QNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 90 FPS--HNPYKIFGSIPYNISTNIIRKivfessatisyLIVE-YGFAKMLLDTNRSLALLLMAEV---------------- 150
Cdd:TIGR00755 89 LNElaKDLTKVVGNLPYNISSPLIFK-----------LLKEkDAFKLAVLMVQKEVAERLVAKPgskdygrlsvlvqyya 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1841703296 151 DISILAKIPRYYFHPKPKVDSTLIVLKRKPAKMAFKERKKYETFV 195
Cdd:TIGR00755 158 NVEIVFKVPPSAFYPPPKVDSAVVRLVPLKRKPSPKDFALFEELL 202
|
|
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
19-174 |
1.75e-08 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 53.85 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 19 IEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLN---YPNYQIVNDDILKFTFPSHNp 95
Cdd:PTZ00338 25 LDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNsplASKLEVIEGDALKTEFPYFD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 96 yKIFGSIPYNISTNIIRKIV-----FESsatiSYLIVEYGFA-KMLLDTNRSLALLLMAEVD----ISILAKIPRYYFHP 165
Cdd:PTZ00338 104 -VCVANVPYQISSPLVFKLLahrplFRC----AVLMFQKEFAlRLLAQPGDELYCRLSVNTQllcrVTHLMKVSKNSFNP 178
|
....*....
gi 1841703296 166 KPKVDSTLI 174
Cdd:PTZ00338 179 PPKVESSVV 187
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
33-96 |
8.45e-07 |
|
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: 46.27 E-value: 8.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841703296 33 NIFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKLLNY--PNYQIVNDDILKFTFPSHNPY 96
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPEADESF 67
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
28-96 |
1.13e-04 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 41.61 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841703296 28 LDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKL--LNYPNYQIVNDDiLKFTFPSHNPY 96
Cdd:COG2518 64 LKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLaaLGYDNVTVRVGD-GALGWPEHAPF 133
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
34-92 |
1.26e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 39.85 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841703296 34 IFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKLL-NYPNYQIVNDDILKFTFPS 92
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAeAGLNVEFVQGDAEDLPFPD 61
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
28-93 |
1.76e-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: 40.39 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841703296 28 LDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRnKLLNYPNYQIVNDDILKFTFPSH 93
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR-ERAAELNVDFVQGDLEDLPLEDG 86
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
8-96 |
7.16e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 39.51 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 8 DSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNF-VTAIEIDSKLCEVTRNKL--LNYPNYQIVNDD 84
Cdd:COG0500 4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAakAGLGNVEFLVAD 83
|
90
....*....|..
gi 1841703296 85 ILKFTFPSHNPY 96
Cdd:COG0500 84 LAELDPLPAESF 95
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
36-93 |
1.22e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 37.26 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1841703296 36 EIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNdDILKFTFPSH 93
Cdd:pfam08241 2 DVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVG-DAEDLPFPDN 58
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
26-183 |
5.91e-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: 37.05 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 26 ISLDEKDNIFEIGAGKGHFTAGLVKRCN--FVTAIEIDSKLCE-----VTRNKLLNypNYQIVNDDILKFTFPSH----- 93
Cdd:COG4123 33 APVKKGGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAElarrnVALNGLED--RITVIHGDLKEFAAELPpgsfd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841703296 94 ----NPykifgsiPYN------ISTNIIRKIV-FESSATISYLIveyGFAKMLLDTNRSLALLLMAEVDISILAKIPRYY 162
Cdd:COG4123 111 lvvsNP-------PYFkagsgrKSPDEARAIArHEDALTLEDLI---RAAARLLKPGGRFALIHPAERLAEILAALRKYG 180
|
170 180
....*....|....*....|....*..
gi 1841703296 163 FHPK------PKVDstlivlkrKPAKM 183
Cdd:COG4123 181 LGPKrlrpvhPRPG--------KPAKR 199
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
20-91 |
8.91e-03 |
|
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: 35.74 E-value: 8.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841703296 20 EKIMNCISLDEKDNIFEIGAGKGHFTAGLVKRCNFVTAIEIDSKLCEVTRNKLLNYP-NYQIVNDDILKFTFP 91
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFP 84
|
|
|