|
Name |
Accession |
Description |
Interval |
E-value |
| pcm |
PRK00312 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; |
1-208 |
1.63e-130 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
Pssm-ID: 178974 [Multi-domain] Cd Length: 212 Bit Score: 365.30 E-value: 1.63e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 1 MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVL 80
Cdd:PRK00312 4 MESERFARLVLRLRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 81 EIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMT 160
Cdd:PRK00312 84 EIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15832851 161 QLDEGGILVLPVG-EEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:PRK00312 164 QLKEGGILVAPVGgEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGELA 212
|
|
| pimt |
TIGR00080 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ... |
1-208 |
1.54e-124 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]
Pssm-ID: 272896 [Multi-domain] Cd Length: 215 Bit Score: 350.67 E-value: 1.54e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 1 MVSRRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRV 79
Cdd:TIGR00080 2 DLESQKKALIDKLINEGyIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMTELLELKPGMKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 80 LEIGTGSGYQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPT 156
Cdd:TIGR00080 82 LEIGTGSGYQAAVLAEIVGRdglVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15832851 157 ALMTQLDEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:TIGR00080 162 ALIDQLKEGGILVMPVGEYLQVLKRAEKRGGEIIIKDVEPVAFVPLVGGEGF 213
|
|
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
4-202 |
4.62e-107 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 305.83 E-value: 4.62e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 4 RRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEI 82
Cdd:pfam01135 1 NRNEALIENLKNYGvIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 83 GTGSGYQTAILAHLVQHVC---SVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALM 159
Cdd:pfam01135 81 GSGSGYLTACFARMVGEVGrvvSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15832851 160 TQLDEGGILVLPVGEE-HQYLKRVRRRG-GEFIIDTVEAVRFVPL 202
Cdd:pfam01135 161 DQLKEGGRLVIPVGPNgNQVLQQFDKRNdGSVVIKDLEGVRFVPL 205
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
11-205 |
3.64e-106 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 303.16 E-value: 3.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 11 DQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSGYQT 90
Cdd:COG2518 2 QQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 91 AILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDEGGILVL 170
Cdd:COG2518 82 AVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 15832851 171 PVGEE-HQYLKRVRRRGGEFIIDTVEAVRFVPLVKG 205
Cdd:COG2518 162 PVGEGgVQRLVLITRTGDGFERESLFEVRFVPLRGG 197
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
78-172 |
2.25e-05 |
|
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: 42.03 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 78 RVLEIGTGSGYQTAILA-HLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQG-WQARAPFDAIIVTAAPPEIP 155
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....
gi 15832851 156 TALMTQLDE-------GGILVLPV 172
Cdd:cd02440 81 EDLARFLEEarrllkpGGVLVLTL 104
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
63-146 |
8.13e-03 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 35.56 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 63 MVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLqwqaRRRLKNL--DLHNVSTRHGDGWQGWQARA 140
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRL----APRLREKfaAADNLTVIHGDALKFDLPKL 76
|
....*.
gi 15832851 141 PFDAII 146
Cdd:smart00650 77 QPYKVV 82
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| pcm |
PRK00312 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; |
1-208 |
1.63e-130 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
Pssm-ID: 178974 [Multi-domain] Cd Length: 212 Bit Score: 365.30 E-value: 1.63e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 1 MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVL 80
Cdd:PRK00312 4 MESERFARLVLRLRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 81 EIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMT 160
Cdd:PRK00312 84 EIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15832851 161 QLDEGGILVLPVG-EEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:PRK00312 164 QLKEGGILVAPVGgEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGELA 212
|
|
| pimt |
TIGR00080 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ... |
1-208 |
1.54e-124 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]
Pssm-ID: 272896 [Multi-domain] Cd Length: 215 Bit Score: 350.67 E-value: 1.54e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 1 MVSRRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRV 79
Cdd:TIGR00080 2 DLESQKKALIDKLINEGyIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMTELLELKPGMKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 80 LEIGTGSGYQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPT 156
Cdd:TIGR00080 82 LEIGTGSGYQAAVLAEIVGRdglVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15832851 157 ALMTQLDEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:TIGR00080 162 ALIDQLKEGGILVMPVGEYLQVLKRAEKRGGEIIIKDVEPVAFVPLVGGEGF 213
|
|
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
4-202 |
4.62e-107 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 305.83 E-value: 4.62e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 4 RRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEI 82
Cdd:pfam01135 1 NRNEALIENLKNYGvIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 83 GTGSGYQTAILAHLVQHVC---SVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALM 159
Cdd:pfam01135 81 GSGSGYLTACFARMVGEVGrvvSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15832851 160 TQLDEGGILVLPVGEE-HQYLKRVRRRG-GEFIIDTVEAVRFVPL 202
Cdd:pfam01135 161 DQLKEGGRLVIPVGPNgNQVLQQFDKRNdGSVVIKDLEGVRFVPL 205
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
11-205 |
3.64e-106 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 303.16 E-value: 3.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 11 DQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSGYQT 90
Cdd:COG2518 2 QQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 91 AILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDEGGILVL 170
Cdd:COG2518 82 AVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 15832851 171 PVGEE-HQYLKRVRRRGGEFIIDTVEAVRFVPLVKG 205
Cdd:COG2518 162 PVGEGgVQRLVLITRTGDGFERESLFEVRFVPLRGG 197
|
|
| PRK13942 |
PRK13942 |
protein-L-isoaspartate O-methyltransferase; Provisional |
7-203 |
9.48e-66 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 184409 Cd Length: 212 Bit Score: 201.40 E-value: 9.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 7 QALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTG 85
Cdd:PRK13942 7 RRVIEELIREGyIKSKKVIDALLKVPRHLFVPEYLEEYAYVDTPLEIGYGQTISAIHMVAIMCELLDLKEGMKVLEIGTG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 86 SGYQTAILAHLV---QHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQL 162
Cdd:PRK13942 87 SGYHAAVVAEIVgksGKVVTIERIPELAEKAKKTLKKLGYDNVEVIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15832851 163 DEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLV 203
Cdd:PRK13942 167 KDGGIMVIPVGSYSQELIRVEKDNGKIIKKKLGEVAFVPLI 207
|
|
| PRK13944 |
PRK13944 |
protein-L-isoaspartate O-methyltransferase; Provisional |
9-202 |
5.85e-45 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 140001 Cd Length: 205 Bit Score: 148.42 E-value: 5.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 9 LLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSG 87
Cdd:PRK13944 5 LVEELVREGiIKSERVKKAMLSVPREEFVMPEYRMMAYEDRPLPLFAGATISAPHMVAMMCELIEPRPGMKILEVGTGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 88 YQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHN-VSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLD 163
Cdd:PRK13944 85 YQAAVCAEAIERrgkVYTVEIVKELAIYAAQNIERLGYWGvVEVYHGDGKRGLEKHAPFDAIIVTAAASTIPSALVRQLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15832851 164 EGGILVLPVGEE-HQYLKRVRRRGGEFIIDTVEAVRFVPL 202
Cdd:PRK13944 165 DGGVLVIPVEEGvGQVLYKVVKRGEKVEKRAITYVLFVPL 204
|
|
| PRK13943 |
PRK13943 |
protein-L-isoaspartate O-methyltransferase; Provisional |
13-172 |
1.07e-23 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 237568 [Multi-domain] Cd Length: 322 Bit Score: 96.07 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 13 LRAQGIQDeQVLNALAAVPREKFVDEAFE-QKAWDNIALPIGQGQ----TISQPYMVARMTELLELTPQSRVLEIGTGSG 87
Cdd:PRK13943 14 LKKYGISD-HIAKAFLEVPREEFLTKSYPlSYVYEDIVLVSYDDGeeysTSSQPSLMALFMEWVGLDKGMRVLEIGGGTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 88 YQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDE 164
Cdd:PRK13943 93 YNAAVMSRVVGEkglVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDGYYGVPEFAPYDVIFVTVGVDEVPETWFTQLKE 172
|
....*...
gi 15832851 165 GGILVLPV 172
Cdd:PRK13943 173 GGRVIVPI 180
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
62-147 |
3.63e-08 |
|
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: 52.08 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 62 YMVARmtelLELTPQSRVLEIGTGSGYQTAILAHLVQ---HVCSVERIKGLQWQARRRLKNLDLH-NVSTRHGDGWQGWQ 137
Cdd:COG2519 82 YIIAR----LDIFPGARVLEAGTGSGALTLALARAVGpegKVYSYERREDFAEIARKNLERFGLPdNVELKLGDIREGID 157
|
90
....*....|
gi 15832851 138 ARaPFDAIIV 147
Cdd:COG2519 158 EG-DVDAVFL 166
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
65-150 |
9.96e-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: 49.22 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 65 ARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLhNVSTRHGDGWQGWQARAPFDA 144
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGSFDL 90
|
....*.
gi 15832851 145 IIVTAA 150
Cdd:COG2226 91 VISSFV 96
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
60-170 |
5.98e-07 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 47.99 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 60 QPYMVARMTELLELTPQSRVLEIGTGSGYQTAILA-HLVQHVC----SVERIKglqwQARRRLKNLDLHNVSTRHGDgWQ 134
Cdd:COG0500 11 LPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAaRFGGRVIgidlSPEAIA----LARARAAKAGLGNVEFLVAD-LA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15832851 135 GWQAR--APFDAIIVTAA----PPEIPTALM----TQLDEGGILVL 170
Cdd:COG0500 86 ELDPLpaESFDLVVAFGVlhhlPPEEREALLrelaRALKPGGVLLL 131
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
60-193 |
2.61e-06 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 45.69 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 60 QPYMVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHvcsveRIKGL---QWQ---ARRRLKNLDLHN-VSTRHGDg 132
Cdd:COG2230 36 QEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGV-----RVTGVtlsPEQleyARERAAEAGLADrVEVRLAD- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832851 133 WQGWQARAPFDAIIVTAappeiptalMTQLdeggilvlpVGEEH--QYLKRVRRR---GGEFIIDT 193
Cdd:COG2230 110 YRDLPADGQFDAIVSIG---------MFEH---------VGPENypAYFAKVARLlkpGGRLLLHT 157
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
75-170 |
5.05e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 43.66 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 75 PQSRVLEIGTGSGYQTAILAhlvqhvcsvERIKGLQW-----------QARRRLKNLDLHnvstrHGDGWQgWQARAPFD 143
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLA---------ERFPGARVtgvdlspemlaRARARLPNVRFV-----VADLRD-LDPPEPFD 65
|
90 100 110
....*....|....*....|....*....|...
gi 15832851 144 AIIVTAA------PPEIPTALMTQLDEGGILVL 170
Cdd:COG4106 66 LVVSNAAlhwlpdHAALLARLAAALAPGGVLAV 98
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
79-158 |
6.21e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 43.32 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 79 VLEIGTGSGYQTAILAHLVQ-HVCSVERIKGLQWQARRRLKNLDLhNVSTRHGDGWQGWQARAPFDAIIVTAA-----PP 152
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlpDP 79
|
....*.
gi 15832851 153 EIPTAL 158
Cdd:pfam13649 80 DLEAAL 85
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
65-170 |
9.31e-06 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 43.47 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 65 ARMTELLE--LTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLdlhNVSTRHGDGWQGWQARAPF 142
Cdd:COG2227 12 RRLAALLArlLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLPLEDGSF 88
|
90 100 110
....*....|....*....|....*....|....
gi 15832851 143 DAIIVTAA------PPEIPTALMTQLDEGGILVL 170
Cdd:COG2227 89 DLVICSEVlehlpdPAALLRELARLLKPGGLLLL 122
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
63-164 |
1.36e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 44.76 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 63 MVARMTELLELTPQSRVLEIGTGSGyqtAI---LAHLVQ--HVCSVERIKG-LQWqARRRLKNLDLHN-VSTRHGDGWQG 135
Cdd:COG2890 100 LVELALALLPAGAPPRVLDLGTGSG---AIalaLAKERPdaRVTAVDISPDaLAV-ARRNAERLGLEDrVRFLQGDLFEP 175
|
90 100
....*....|....*....|....*....
gi 15832851 136 WQARAPFDAIIvtAAPPEIPTALMTQLDE 164
Cdd:COG2890 176 LPGDGRFDLIV--SNPPYIPEDEIALLPP 202
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
61-171 |
2.15e-05 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 43.89 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 61 PYMVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLqwQARRRLKNLDLHNVSTRHGDGWQgWQ--- 137
Cdd:pfam00398 16 PKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRL--AKLLQKKLSLDENLTVIHQDFLK-FEfps 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15832851 138 --ARAPFDAIIVTAAPPEIPTALMTQL-------DEGGILVLP 171
Cdd:pfam00398 93 lvTHIHQEFLVVGNLPYNISTPIVKQLlfesrfgIVDMLLMLQ 135
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
78-172 |
2.25e-05 |
|
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: 42.03 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 78 RVLEIGTGSGYQTAILA-HLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQG-WQARAPFDAIIVTAAPPEIP 155
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....
gi 15832851 156 TALMTQLDE-------GGILVLPV 172
Cdd:cd02440 81 EDLARFLEEarrllkpGGVLVLTL 104
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
68-163 |
4.18e-04 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 40.15 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 68 TELL--------ELTPQSRVLEIGTGSGyqtAI---LAHLVQH--VCSVERIKG-LQWqARRRLKNLDLHNVSTRHGDGW 133
Cdd:PRK09328 93 TEELvewalealLLKEPLRVLDLGTGSG---AIalaLAKERPDaeVTAVDISPEaLAV-ARRNAKHGLGARVEFLQGDWF 168
|
90 100 110
....*....|....*....|....*....|
gi 15832851 134 QGwQARAPFDAIIvtAAPPEIPTALMTQLD 163
Cdd:PRK09328 169 EP-LPGGRFDLIV--SNPPYIPEADIHLLQ 195
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
64-131 |
1.84e-03 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 38.34 E-value: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832851 64 VARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDlhNVSTRHGD 131
Cdd:PRK14896 18 VDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAG--NVEIIEGD 83
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
53-170 |
3.03e-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: 37.09 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 53 GQGQTIsqpYMVARMTElleltPQsRVLEIGTGSGYQTAILAHLVQ---HVCSVERIKGLQWQARRRLKNLDL-HNVSTR 128
Cdd:COG4122 3 EQGRLL---YLLARLLG-----AK-RILEIGTGTGYSTLWLARALPddgRLTTIEIDPERAAIARENFARAGLaDRIRLI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15832851 129 HGDgwqgwqAR--------APFDAIIVTAAPPEIPTAL---MTQLDEGGILVL 170
Cdd:COG4122 74 LGD------ALevlprladGPFDLVFIDADKSNYPDYLelaLPLLRPGGLIVA 120
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
78-201 |
3.21e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 36.63 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 78 RVLEIGTGSGYQTAILAHLVQ---HVCSVERIKGLQWQARRRLKNLDLHNVSTRHGD--GWQGWQARAPFDaIIVTAApp 152
Cdd:pfam13847 6 RVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDieELPELLEDDKFD-VVISNC-- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15832851 153 eiptALMTQLDEGGILvlpvgeehQYLKRVRRRGGEFIIDTVEAVRFVP 201
Cdd:pfam13847 83 ----VLNHIPDPDKVL--------QEILRVLKPGGRLIISDPDSLAELP 119
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
63-146 |
8.13e-03 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 35.56 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832851 63 MVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLqwqaRRRLKNL--DLHNVSTRHGDGWQGWQARA 140
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRL----APRLREKfaAADNLTVIHGDALKFDLPKL 76
|
....*.
gi 15832851 141 PFDAII 146
Cdd:smart00650 77 QPYKVV 82
|
|
|