|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-226 |
4.08e-121 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 342.88 E-value: 4.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 1 MYTLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYPieKQVQFIQGGA 80
Cdd:PRK00155 3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD--PKVTVVAGGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 81 ERQDSVYNAIQHASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQT 159
Cdd:PRK00155 81 ERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDdGGGIVDTPDRSGLWAAQT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446210456 160 PQGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFLHVQKK 226
Cdd:PRK00155 161 PQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
5-226 |
5.20e-113 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 322.46 E-value: 5.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYPIEKQVQFIQGGAERQD 84
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 85 SVYNAIQHAS-DVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKV-EQGVVVETVERSQLKAVQTPQG 162
Cdd:COG1211 81 SVRNGLEALPdDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVdDDGRVTETVDRSGLWAAQTPQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446210456 163 FSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFLHVQKK 226
Cdd:COG1211 161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
2-217 |
1.15e-105 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 303.68 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 2 YTLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELmQKYPIEKQVQFIQGGAE 81
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL-AKYGLSKVVKIVEGGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 82 RQDSVYNAIQ--HASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQ 158
Cdd:cd02516 80 RQDSVLNGLKalPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDdDGVVVETLDREKLWAAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446210456 159 TPQGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIA 217
Cdd:cd02516 160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
3-221 |
3.05e-93 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 213532 Cd Length: 217 Bit Score: 272.24 E-value: 3.05e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 3 TLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELmqkYPIEKQVQFIQGGAER 82
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKY---LVARAVPKIVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 83 QDSVYNAIQHASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQTPQ 161
Cdd:TIGR00453 78 QDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEaDGFVVETVDREGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 162 GFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFL 221
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
4-221 |
2.65e-85 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Pssm-ID: 460075 Cd Length: 219 Bit Score: 251.99 E-value: 2.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 4 LIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELmqkyPIEKQVQFIQGGAERQ 83
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQL----LGDPSIQLVAGGDTRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 84 DSVYNAIQH-ASDVEYILVHDGARPFVTNKVIQDVLTAAEK-YGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQTP 160
Cdd:pfam01128 77 DSVLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETgTQGAILALPVTDTIKRVEaDGVVAGTPDRSGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446210456 161 QGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFL 221
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-226 |
4.08e-121 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 342.88 E-value: 4.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 1 MYTLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYPieKQVQFIQGGA 80
Cdd:PRK00155 3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD--PKVTVVAGGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 81 ERQDSVYNAIQHASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQT 159
Cdd:PRK00155 81 ERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDdGGGIVDTPDRSGLWAAQT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446210456 160 PQGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFLHVQKK 226
Cdd:PRK00155 161 PQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
5-226 |
5.20e-113 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 322.46 E-value: 5.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYPIEKQVQFIQGGAERQD 84
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 85 SVYNAIQHAS-DVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKV-EQGVVVETVERSQLKAVQTPQG 162
Cdd:COG1211 81 SVRNGLEALPdDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVdDDGRVTETVDRSGLWAAQTPQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446210456 163 FSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFLHVQKK 226
Cdd:COG1211 161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
2-217 |
1.15e-105 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 303.68 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 2 YTLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELmQKYPIEKQVQFIQGGAE 81
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL-AKYGLSKVVKIVEGGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 82 RQDSVYNAIQ--HASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQ 158
Cdd:cd02516 80 RQDSVLNGLKalPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDdDGVVVETLDREKLWAAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446210456 159 TPQGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIA 217
Cdd:cd02516 160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
3-221 |
3.05e-93 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 213532 Cd Length: 217 Bit Score: 272.24 E-value: 3.05e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 3 TLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELmqkYPIEKQVQFIQGGAER 82
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKY---LVARAVPKIVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 83 QDSVYNAIQHASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQTPQ 161
Cdd:TIGR00453 78 QDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEaDGFVVETVDREGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 162 GFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFL 221
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
4-221 |
2.65e-85 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Pssm-ID: 460075 Cd Length: 219 Bit Score: 251.99 E-value: 2.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 4 LIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELmqkyPIEKQVQFIQGGAERQ 83
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQL----LGDPSIQLVAGGDTRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 84 DSVYNAIQH-ASDVEYILVHDGARPFVTNKVIQDVLTAAEK-YGASICAVPVKDTVKKVE-QGVVVETVERSQLKAVQTP 160
Cdd:pfam01128 77 DSVLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETgTQGAILALPVTDTIKRVEaDGVVAGTPDRSGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446210456 161 QGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFL 221
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
2-221 |
2.20e-79 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 237.46 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 2 YTLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYPI-EKQVQFIQGGA 80
Cdd:PRK13385 3 YELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVaDQRVEVVKGGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 81 ERQDSVYNAIQHASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVEQGVVVETVERSQLKAVQTP 160
Cdd:PRK13385 83 ERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQGQTP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446210456 161 QGFSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFL 221
Cdd:PRK13385 163 QAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
5-225 |
6.55e-61 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 191.10 E-value: 6.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYPIEkqVQFIQGGAERQD 84
Cdd:PLN02728 28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDVP--LKFALPGKERQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 85 SVYNAIQHA-SDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVEQGV-VVETVERSQLKAVQTPQG 162
Cdd:PLN02728 106 SVFNGLQEVdANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSfVVKTLDRKRLWEMQTPQV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446210456 163 FSVSLLLEAHRSAKQSCFLGTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFLHVQK 225
Cdd:PLN02728 186 IKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERS 248
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
3-221 |
1.77e-55 |
|
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional
Pssm-ID: 236492 [Multi-domain] Cd Length: 378 Bit Score: 181.20 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 3 TLIIPAAGQGKRMGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEErpyfEELMQK-YPIEKQVQFIQGGAE 81
Cdd:PRK09382 7 SLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDD----IAYMKKaLPEIKFVTLVTGGAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 82 RQDSVYNAIQHASDvEYILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKVEqgvvvETVERSQLKAVQTPQ 161
Cdd:PRK09382 83 RQESVRNALEALDS-EYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRAN-----ETVDREGLKLIQTPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 162 GFSVSLLLEAhrSAKQSCFlgTDDASLVERIGKQVGVVEGSYYNIKVTTPEDLLIAESFL 221
Cdd:PRK09382 157 LSRTKTLKAA--ADGRGDF--TDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-135 |
1.92e-10 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 57.86 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 1 MYTLIIPAAGQGKRMGAgkNKLFLLINEVPIIVHTLRAFeRDKECKSIVMAIneeeRPYFEELMQKYPiEKQVQFI---- 76
Cdd:COG2068 3 KVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAA-LAAGLDPVVVVL----GADAEEVAAALA-GLGVRVVvnpd 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446210456 77 ----QGgaerqDSVYNAIQHAS-DVEYILVHDGARPFVTNKVIQDVLTAAEKYGASIcAVPVKD 135
Cdd:COG2068 75 weegMS-----SSLRAGLAALPaDADAVLVLLGDQPLVTAETLRRLLAAFRESPASI-VAPTYD 132
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
5-135 |
2.06e-10 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 57.20 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMGagKNKLFLLINEVPIIVHTLRAFERDkeCKSIVMAINEEE-RPYFEELmqKYPIEKQVQFIQG-GAer 82
Cdd:pfam12804 2 VILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPA--GDEVVVVANDEEvLAALAGL--GVPVVPDPDPGQGpLA-- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446210456 83 qdSVYNAIQHASDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASIcAVPVKD 135
Cdd:pfam12804 74 --GLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADI-VVPVYD 123
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
5-120 |
3.94e-09 |
|
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.
Pssm-ID: 274516 Cd Length: 188 Bit Score: 54.27 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMgaGKNKLFLLINEVPIIVHTLRAFERdKECKSIVMAINEEERPYFEELMQKYPI---------EKQVQF 75
Cdd:TIGR03310 3 IILAAGLSSRM--GQNKLLLPYKGKTILEHVVDNALR-LFFDEVILVLGHEADELVALLANHSNItlvhnpqyaEGQSSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446210456 76 IQGGAERQDSvynaiqhaSDVEYILVHDgaRPFVTNKVIQDVLTA 120
Cdd:TIGR03310 80 IKLGLELPVQ--------SDGYLFLLGD--QPFVTPDIIQLLLEA 114
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
8-221 |
1.17e-08 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 52.97 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 8 AAGQGKRMGAGKnKLFLLINEVPIIVHTLRAFErDKECKSIVMAINEEErPYFEELMQkypiEKQVQFIQGGAErqDSVY 87
Cdd:COG2266 2 AGGKGTRLGGGE-KPLLEICGKPMIDRVIDALE-ESCIDKIYVAVSPNT-PKTREYLK----ERGVEVIETPGE--GYVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 88 NAIQHASDVE-YILVHDGARPFVTNKVIQDVLTAAEKYGASICAVPVKDTVKKvEQGVVVETVERSQLKAVqtPQGFSVs 166
Cdd:COG2266 73 DLNEALESISgPVLVVPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPAALKR-ELGVSPDTTFEIDGELV--PTGINI- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446210456 167 llLEAHRSAKQSCFLGTDDASLVerigkqvgvvegsyYNikVTTPEDLLIAESFL 221
Cdd:COG2266 149 --VDGSDGEQEETNLVLDDPRLA--------------LN--VNTPEDLKLAEKLL 185
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
5-130 |
5.62e-08 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 51.02 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMGAgkNKLFLLINEVPIIVHTLRAFeRDKECKSIVMAINEEErpyfEELMQKYPIEKQVQFIQGGAERQ- 83
Cdd:cd04182 4 IILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAA-LAAGLSRVIVVLGAEA----DAVRAALAGLPVVVVINPDWEEGm 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446210456 84 -DSVYNAIQHAS-DVEYILVHDGARPFVTNKVIQDVLTAAEKYGASICA 130
Cdd:cd04182 77 sSSLAAGLEALPaDADAVLILLADQPLVTAETLRALIDAFREDGAGIVA 125
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
2-133 |
2.20e-05 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 43.33 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 2 YTLIIPAAGQGKRMGAgkNKLFLLINEVPIIVHTLRAFErdKECKSIVMAINEEERPYFeelmqkypiEKQVQFIQ---- 77
Cdd:cd02503 1 ITGVILAGGKSRRMGG--DKALLELGGKPLLEHVLERLK--PLVDEVVISANRDQERYA---------LLGVPVIPdepp 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446210456 78 -----GGaerqdsVYNAIQHASdVEYILVHDGARPFVTNKVIQDVLTAAEKyGASICaVPV 133
Cdd:cd02503 68 gkgplAG------ILAALRAAP-ADWVLVLACDMPFLPPELLERLLAAAEE-GADAV-VPK 119
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
4-150 |
1.47e-04 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 41.47 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 4 LIIPAAGQGKR---MGAGKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEERPYFEELMQKYpIEKQVQFIQ--- 77
Cdd:cd04183 1 IIIPMAGLGSRfkkAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLKL-LAPNATVVEldg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 78 ---GGAErqdSVYNAIQHASDVEYILVHDGarPFVTNKVIQDVLTAAEKYGASICAVPVKDT------VKKVEQGVVVET 148
Cdd:cd04183 80 etlGAAC---TVLLAADLIDNDDPLLIFNC--DQIVESDLLAFLAAFRERDLDGGVLTFFSShprwsyVKLDENGRVIET 154
|
..
gi 446210456 149 VE 150
Cdd:cd04183 155 AE 156
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
2-132 |
2.40e-04 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 41.28 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 2 YTLIIPAAGQGKRMGaGKNKLFLLINEVPIIVHTLRAFeRDKECKSIVMAINEEERpyFEELMQKYPIEKQVqfIQGGAE 81
Cdd:PRK14489 6 IAGVILAGGLSRRMN-GRDKALILLGGKPLIERVVDRL-RPQFARIHLNINRDPAR--YQDLFPGLPVYPDI--LPGFQG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446210456 82 RQDSVYNAIQHAsDVEYILVHDGARPFVTNKVIQDVLTAAEKYGASiCAVP 132
Cdd:PRK14489 80 PLSGILAGLEHA-DSEYLFVVACDTPFLPENLVKRLSKALAIEGAD-IAVP 128
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
5-150 |
2.53e-04 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 40.64 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMG---AGKNKLFLLINEVPIIVHTLRAFERDKeCKSIVMAINEEERPYFEELMQKYPIEKQVQFIQ---- 77
Cdd:cd04181 2 VILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVqeep 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 78 ---GGAerqdsVYNAIQHASDvEYILVHDGarpfvtnkviqDVLT-----------AAEKYGASICAVPVKDT-----VK 138
Cdd:cd04181 81 lgtAGA-----VRNAEDFLGD-DDFLVVNG-----------DVLTdldlsellrfhREKGADATIAVKEVEDPsrygvVE 143
|
170
....*....|..
gi 446210456 139 KVEQGVVVETVE 150
Cdd:cd04181 144 LDDDGRVTRFVE 155
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-41 |
3.21e-04 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 40.61 E-value: 3.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMG---AGKNKLFLLINEVPIIVHTLRAFER 41
Cdd:COG1213 3 VILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAA 42
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
5-53 |
3.93e-04 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 40.17 E-value: 3.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446210456 5 IIPAAGQGKRMGaGKNKLFLLINEVPIIVHTLRAFErdKECKSIVmaIN 53
Cdd:PRK00317 7 VILAGGRSRRMG-GVDKGLQELNGKPLIQHVIERLA--PQVDEIV--IN 50
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
3-57 |
1.27e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 38.25 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446210456 3 TLIIPAAGQGKRMGAgkNKLFLLINEVPIIVHTLRAFERDkeCKSIVMAINEEER 57
Cdd:COG0746 6 TGVILAGGRSRRMGQ--DKALLPLGGRPLLERVLERLRPQ--VDEVVIVANRPER 56
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
5-76 |
1.67e-03 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 38.37 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446210456 5 IIPAAGQGKRMGA-GKN--KLFLLINEVPIIVHTLRAFerdKECK----SIVMAINEEerpYFEELMQKYPiekQVQFI 76
Cdd:cd02523 2 IILAAGRGSRLRPlTEDrpKCLLEINGKPLLERQIETL---KEAGiddiVIVTGYKKE---QIEELLKKYP---NIKFV 71
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
5-135 |
4.00e-03 |
|
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.
Pssm-ID: 396773 Cd Length: 217 Bit Score: 37.32 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210456 5 IIPAAGQGKRMgagKNKLFLLINEVPIIVHTLRAFERDKECKSIVMAINEEErpyFEELMQKYPIekQVQFIQGGAER-Q 83
Cdd:pfam02348 3 IIPARLGSKRL---PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEE---IADVAKEFGA--GVVMTSGSLSSgT 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446210456 84 DSVYNAIQ--HASDVEYILVHDGARPFVTNKVIQDV---LTAAEKYGASICAVPVKD 135
Cdd:pfam02348 75 DRFYEVVKafLNDHDDIIVNIQGDNPLLQPEVILKAietLLNNGEPYMSTLVVPVGS 131
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-67 |
7.76e-03 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 36.28 E-value: 7.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446210456 5 IIPAAGQGKRMG---AGKNKLFLLINEVPIIVHTLRAFERDKeCKSIVMAINeeerpYFEELMQKY 67
Cdd:COG1208 3 VILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG-----YLAEQIEEY 62
|
|
| |
