|
Name |
Accession |
Description |
Interval |
E-value |
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
8-254 |
1.08e-111 |
|
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: 322.07 E-value: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 8 KKYGVRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPN 87
Cdd:COG0030 5 RRYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 88 VELRFEDFLKAK--NVPEGA--ICVSNIPYNITGPLMEKIIEWK--FKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQT 161
Cdd:COG0030 85 LTVIEGDALKVDlpALAAGEplKVVGNLPYNISTPILFKLLEARppIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 162 FYEVKKLFDVSRSCFVPNPEVDSTVVDLKRKPVDL----DFEKFKKFVSMIFAKKRKTLKNNLRPFLS------IFE--G 229
Cdd:COG0030 165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPLvpvaDEKLFFRVVKAAFSQRRKTLRNSLKSLFSkerleeALEaaG 244
|
250 260
....*....|....*....|....*
gi 490183090 230 VDLSRRAEQLTVEEIVELYEKWRRA 254
Cdd:COG0030 245 IDPTARAEELSVEEFARLANALKKR 269
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
12-249 |
9.10e-87 |
|
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: 258.31 E-value: 9.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 12 VRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELR 91
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 92 FEDFLK---AKNVPEGAICVSNIPYNITGPLMEKIIE--WKFKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFYEVK 166
Cdd:TIGR00755 81 EGDALKfdlNELAKDLTKVVGNLPYNISSPLIFKLLKekDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 167 KLFDVSRSCFVPNPEVDSTVVDL---KRKPVDLDFEKFKKFVSMIFAKKRKTLKNNLRPFLSI------FEGVDLSRRAE 237
Cdd:TIGR00755 161 IVFKVPPSAFYPPPKVDSAVVRLvplKRKPSPKDFALFEELLKAAFQQRRKTLRNNLKNLLSElvelleELGIDPDKRVE 240
|
250
....*....|..
gi 490183090 238 QLTVEEIVELYE 249
Cdd:TIGR00755 241 QLSPEDFLRLAN 252
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
12-250 |
7.07e-80 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 240.96 E-value: 7.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 12 VRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELR 91
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 92 FEDFLKAkNVPEGAICVSNIPYNITGPLMEKIIEWKFKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFYEVKKLFDV 171
Cdd:PRK14896 81 EGDALKV-DLPEFNKVVSNLPYQISSPITFKLLKHGFEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEIVEKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 172 SRSCFVPNPEVDSTVVDLKRKPVDLDFEK---FKKFVSMIFAKKRKTLKNNLRPFLSIFE------------GVDLSRRA 236
Cdd:PRK14896 160 PPGAFSPKPKVDSAVVRLTPREPKYEVYDedfFDDFVKALFQHRRKTLRNALKNSAHISGkedikavvealpEELLNKRV 239
|
250
....*....|....
gi 490183090 237 EQLTVEEIVELYEK 250
Cdd:PRK14896 240 FQLSPEEIAELANL 253
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
28-193 |
3.67e-73 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 220.85 E-value: 3.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 28 IAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELRFEDFLKAKNVPEGAI- 106
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 107 CVSNIPYNITGPLMEKIIEWK--FKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFYEVKKLFDVSRSCFVPNPEVDS 184
Cdd:smart00650 81 VVGNLPYNISTPILFKLLEEPpaFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160
|
....*....
gi 490183090 185 TVVDLKRKP 193
Cdd:smart00650 161 AVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
13-249 |
1.09e-58 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 187.19 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 13 RLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELRF 92
Cdd:pfam00398 3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 93 EDFLKAkNVPEGAI-------CVSNIPYNITGPLMEKIIE---WKFKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTF 162
Cdd:pfam00398 83 QDFLKF-EFPSLVThihqeflVVGNLPYNISTPIVKQLLFesrFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVLRQAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 163 YEVKKLFDVSRSCFVPNPEVDSTVVDLKRKPVDL----DFEKFKKFVSMIFAKKRKTLKNNLRPFLS-------IFEGVD 231
Cdd:pfam00398 162 TDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPhpvkDLDVYDSVVRKLFNRKRKTLSTSLKSLFPggqlqafSSHGIN 241
|
250
....*....|....*...
gi 490183090 232 LSRRAEQLTVEEIVELYE 249
Cdd:pfam00398 242 DNALVKKLSPEQTLDIFN 259
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
44-125 |
1.30e-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: 45.88 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 44 VVEIGAGAGTLTEELAKT-GARVIAYEIDESLAPILQE--RLSKYPNVELRFEDFLKAKNVPEGA--ICVSNIPYNITGP 118
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKaaAALLADNVEVLKGDAEELPPEADESfdVIISDPPLHHLVE 81
|
....*..
gi 490183090 119 LMEKIIE 125
Cdd:cd02440 82 DLARFLE 88
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
8-254 |
1.08e-111 |
|
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: 322.07 E-value: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 8 KKYGVRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPN 87
Cdd:COG0030 5 RRYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 88 VELRFEDFLKAK--NVPEGA--ICVSNIPYNITGPLMEKIIEWK--FKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQT 161
Cdd:COG0030 85 LTVIEGDALKVDlpALAAGEplKVVGNLPYNISTPILFKLLEARppIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 162 FYEVKKLFDVSRSCFVPNPEVDSTVVDLKRKPVDL----DFEKFKKFVSMIFAKKRKTLKNNLRPFLS------IFE--G 229
Cdd:COG0030 165 YADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPLvpvaDEKLFFRVVKAAFSQRRKTLRNSLKSLFSkerleeALEaaG 244
|
250 260
....*....|....*....|....*
gi 490183090 230 VDLSRRAEQLTVEEIVELYEKWRRA 254
Cdd:COG0030 245 IDPTARAEELSVEEFARLANALKKR 269
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
12-249 |
9.10e-87 |
|
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: 258.31 E-value: 9.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 12 VRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELR 91
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 92 FEDFLK---AKNVPEGAICVSNIPYNITGPLMEKIIE--WKFKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFYEVK 166
Cdd:TIGR00755 81 EGDALKfdlNELAKDLTKVVGNLPYNISSPLIFKLLKekDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 167 KLFDVSRSCFVPNPEVDSTVVDL---KRKPVDLDFEKFKKFVSMIFAKKRKTLKNNLRPFLSI------FEGVDLSRRAE 237
Cdd:TIGR00755 161 IVFKVPPSAFYPPPKVDSAVVRLvplKRKPSPKDFALFEELLKAAFQQRRKTLRNNLKNLLSElvelleELGIDPDKRVE 240
|
250
....*....|..
gi 490183090 238 QLTVEEIVELYE 249
Cdd:TIGR00755 241 QLSPEDFLRLAN 252
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
12-250 |
7.07e-80 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 240.96 E-value: 7.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 12 VRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELR 91
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 92 FEDFLKAkNVPEGAICVSNIPYNITGPLMEKIIEWKFKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFYEVKKLFDV 171
Cdd:PRK14896 81 EGDALKV-DLPEFNKVVSNLPYQISSPITFKLLKHGFEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEIVEKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 172 SRSCFVPNPEVDSTVVDLKRKPVDLDFEK---FKKFVSMIFAKKRKTLKNNLRPFLSIFE------------GVDLSRRA 236
Cdd:PRK14896 160 PPGAFSPKPKVDSAVVRLTPREPKYEVYDedfFDDFVKALFQHRRKTLRNALKNSAHISGkedikavvealpEELLNKRV 239
|
250
....*....|....
gi 490183090 237 EQLTVEEIVELYEK 250
Cdd:PRK14896 240 FQLSPEEIAELANL 253
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
28-193 |
3.67e-73 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 220.85 E-value: 3.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 28 IAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELRFEDFLKAKNVPEGAI- 106
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 107 CVSNIPYNITGPLMEKIIEWK--FKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFYEVKKLFDVSRSCFVPNPEVDS 184
Cdd:smart00650 81 VVGNLPYNISTPILFKLLEEPpaFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160
|
....*....
gi 490183090 185 TVVDLKRKP 193
Cdd:smart00650 161 AVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
13-249 |
1.09e-58 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 187.19 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 13 RLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYPNVELRF 92
Cdd:pfam00398 3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 93 EDFLKAkNVPEGAI-------CVSNIPYNITGPLMEKIIE---WKFKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTF 162
Cdd:pfam00398 83 QDFLKF-EFPSLVThihqeflVVGNLPYNISTPIVKQLLFesrFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVLRQAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 163 YEVKKLFDVSRSCFVPNPEVDSTVVDLKRKPVDL----DFEKFKKFVSMIFAKKRKTLKNNLRPFLS-------IFEGVD 231
Cdd:pfam00398 162 TDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDPhpvkDLDVYDSVVRKLFNRKRKTLSTSLKSLFPggqlqafSSHGIN 241
|
250
....*....|....*...
gi 490183090 232 LSRRAEQLTVEEIVELYE 249
Cdd:pfam00398 242 DNALVKKLSPEQTLDIFN 259
|
|
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
9-221 |
3.03e-49 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 164.02 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 9 KYGVRLKKHLGQVFLSDDRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQER---LSKY 85
Cdd:PTZ00338 5 KSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRfqnSPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 86 PNVELRFEDFLKAkNVPEGAICVSNIPYNITGPLMEKIIEWK--FKRAIVMIQKEVGERILAKPGKKTYGYLSVVVQTFY 163
Cdd:PTZ00338 85 SKLEVIEGDALKT-EFPYFDVCVANVPYQISSPLVFKLLAHRplFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLC 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 164 EVKKLFDVSRSCFVPNPEVDSTVVDL--KRKPVDLDFEKFKKFVSMIFAKKRKTLKNNLR 221
Cdd:PTZ00338 164 RVTHLMKVSKNSFNPPPKVESSVVRIepKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFK 223
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
29-178 |
5.48e-11 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 60.22 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 29 AKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTG---ARVIAYEIDESLAPILQERlskYPNVEL------RFEDFLKAK 99
Cdd:COG3963 34 ARAMASEVDWSGAGPVVELGPGTGVFTRAILARGvpdARLLAVEINPEFAEHLRRR---FPRVTVvngdaeDLAELLAEH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 100 NVPE-GAIcVSNIPYNItgplmekiiewkfkraivmIQKEVGERILA------KPGKK----TYGYLSVVVQTFYEvkKL 168
Cdd:COG3963 111 GIGKvDAV-VSGLPLLS-------------------FPPELRRAILDaafrvlAPGGVfvqfTYSPRSPVPRKLLR--RG 168
|
170
....*....|
gi 490183090 169 FDVSRSCFVP 178
Cdd:COG3963 169 FEAVRSGFVW 178
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
31-105 |
1.11e-08 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 53.55 E-value: 1.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490183090 31 RIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSK--YPNVELRFEDFlkAKNVPEGA 105
Cdd:COG2518 57 RMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAAlgYDNVTVRVGDG--ALGWPEHA 131
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
26-91 |
2.68e-08 |
|
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: 51.53 E-value: 2.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490183090 26 DRIA------KRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYP-NVELR 91
Cdd:COG2226 2 DRVAarydgrEALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFV 74
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
25-96 |
7.17e-07 |
|
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: 47.32 E-value: 7.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490183090 25 DDRIAKRIvkAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYpNVELRFEDFL 96
Cdd:COG2227 11 DRRLAALL--ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL-NVDFVQGDLE 79
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
44-125 |
1.30e-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: 45.88 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 44 VVEIGAGAGTLTEELAKT-GARVIAYEIDESLAPILQE--RLSKYPNVELRFEDFLKAKNVPEGA--ICVSNIPYNITGP 118
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKaaAALLADNVEVLKGDAEELPPEADESfdVIISDPPLHHLVE 81
|
....*..
gi 490183090 119 LMEKIIE 125
Cdd:cd02440 82 DLARFLE 88
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
8-106 |
2.74e-06 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 47.08 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 8 KKYGVRLKKHLGQVF------LSDD-RIAKR------------IVKAAELTPEDVVVEIGAGAGTLTEELAK----TGaR 64
Cdd:COG2519 40 KPEGSVVTTSKGKEFlvlrptLYDYvLSMKRgtqiiypkdagyIIARLDIFPGARVLEAGTGSGALTLALARavgpEG-K 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490183090 65 VIAYEIDESLAPILQERLSKY---PNVELRFEDFlkAKNVPEGAI 106
Cdd:COG2519 119 VYSYERREDFAEIARKNLERFglpDNVELKLGDI--REGIDEGDV 161
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
26-95 |
7.85e-06 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 44.92 E-value: 7.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490183090 26 DRIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAK-TGARVIAYEIDESLAPILQERLSKY---PNVELRFEDF 95
Cdd:COG2230 37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAglaDRVEVRLADY 110
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
40-89 |
1.39e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 45.03 E-value: 1.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490183090 40 PEDVVVEIGAGAGTLTEELAKTGAR-VIAYEIDESLAPILQERLSKYPNVE 89
Cdd:COG4076 35 PGDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLSD 85
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
44-97 |
2.91e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 41.78 E-value: 2.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490183090 44 VVEIGAGAGTLTEELAK-TGARVIAYEIDESLAPILQERLSKY-PNVELRFEDFLK 97
Cdd:pfam13649 1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAgLNVEFVQGDAED 56
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
40-95 |
3.02e-05 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 41.73 E-value: 3.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490183090 40 PEDVVVEIGAGAGTLTEELAK--TGARVIAYEIDESLAPILQERLskyPNVELRFEDF 95
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAErfPGARVTGVDLSPEMLARARARL---PNVRFVVADL 55
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
27-73 |
4.63e-05 |
|
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: 44.01 E-value: 4.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490183090 27 RIAKRIVKAAELTPEDVVVEIGAGAGTLTEELAKTGARVIAYEIDES 73
Cdd:COG2265 220 ALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPE 266
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
44-111 |
7.39e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 42.60 E-value: 7.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490183090 44 VVEIGAGAGTLTEELAK-TGARVIAYEIDESLAPILQERLSKY--PNVELRFEDFLKAKNVPEG---AICVSNI 111
Cdd:COG0500 30 VLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKAglGNVEFLVADLAELDPLPAEsfdLVVAFGV 103
|
|
| MDR_enoyl_red |
cd08244 |
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ... |
23-67 |
1.35e-03 |
|
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176206 [Multi-domain] Cd Length: 324 Bit Score: 39.27 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490183090 23 LSDDRIAKRIVKAAELTPEDVVVEIGA--GAGTLTEELAKT-GARVIA 67
Cdd:cd08244 125 VHDGRTALGLLDLATLTPGDVVLVTAAagGLGSLLVQLAKAaGATVVG 172
|
|
| CobL |
COG2242 |
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ... |
28-90 |
1.82e-03 |
|
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441843 [Multi-domain] Cd Length: 403 Bit Score: 38.99 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490183090 28 IAKRIVKAA-----ELTPEDVVVEIGAGAGTLTEELAKT--GARVIAYEIDESLAPILQERLSKY--PNVEL 90
Cdd:COG2242 230 ITKREVRALtlaklALRPGDVLWDIGAGSGSVSIEAARLapGGRVYAIERDPERAALIRANARRFgvPNVEV 301
|
|
| Methyltransf_33 |
pfam10017 |
Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family ... |
36-98 |
2.10e-03 |
|
Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family are expressed from part of the ergothioneine biosynthetic gene cluster. EGTD is the histidine methyltransferase that transfers three methyl groups to the alpha-amino moiety of histidine, in the first stage of the production of this histidine betaine derivative that carries a thiol group attached to the C2 atom of an imidazole ring.
Pssm-ID: 462944 Cd Length: 304 Bit Score: 38.61 E-value: 2.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490183090 36 AELTPEDVVVEIGAGAGT----LTEELAKTGARVIAYEID---ESLAPILQERLSKYPNVELR-----FEDFLKA 98
Cdd:pfam10017 57 AALIPAAVLVELGSGSSRktrlLLDALPAAGKPVTYVPIDisaEALEESAAALAADYPGLTVHglvgdYEDGLAR 131
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
45-86 |
2.25e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 36.49 E-value: 2.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490183090 45 VEIGAGAGTLTEELAKTGARVIAYEIDESLAPILQERLSKYP 86
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG 42
|
|
| PRK07402 |
PRK07402 |
precorrin-6Y C5,15-methyltransferase subunit CbiT; |
32-89 |
3.43e-03 |
|
precorrin-6Y C5,15-methyltransferase subunit CbiT;
Pssm-ID: 180961 Cd Length: 196 Bit Score: 37.67 E-value: 3.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490183090 32 IVKAAELTPEDVVVEIGAGAGTLTEELAK--TGARVIAYEIDESLAPILQERLSKY--PNVE 89
Cdd:PRK07402 32 LISQLRLEPDSVLWDIGAGTGTIPVEAGLlcPKGRVIAIERDEEVVNLIRRNCDRFgvKNVE 93
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
45-95 |
3.48e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 36.19 E-value: 3.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490183090 45 VEIGAGAGTLTEELAK--TGARVIAYEIDESLAPILQERLSKYPNVELRFEDF 95
Cdd:pfam08242 1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAALGLLNAVRVEL 53
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
15-112 |
5.11e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 37.19 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490183090 15 KKHLGQvFLSDDRIAKRIVKAAEL---TPEDVVVEIGAGAGTLTEELAKTGA-RVIAYEIDESLAPILQERLSKY-PNVE 89
Cdd:COG2263 18 KVELEQ-YPTPAELAAELLHLAYLrgdIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLgVRVD 96
|
90 100
....*....|....*....|...
gi 490183090 90 LRFEDFLKAKNVPEGAICVSNIP 112
Cdd:COG2263 97 FIRADVTRIPLGGSVDTVVMNPP 119
|
|
|