|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-232 |
3.18e-123 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 348.66 E-value: 3.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLANHPQITVVDGGDERA 86
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRNGLWHALTP 166
Cdd:PRK00155 84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832855 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
10-229 |
8.83e-116 |
|
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: 329.80 E-value: 8.83e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 10 AVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLanHPQITVVDGGDERADS 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 89 VLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQ 167
Cdd:pfam01128 79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832855 168 FFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
9-227 |
2.98e-105 |
|
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: 303.05 E-value: 2.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 9 CAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADS 88
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 89 VLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQF 168
Cdd:TIGR00453 81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15832855 169 FPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
11-229 |
2.57e-101 |
|
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: 293.19 E-value: 2.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 11 VVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQL--PLANHPQITVVDGGDERAD 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 88 SVLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRtGGILAAPVRDTMKRAEPGkNAIAHTVDRNGLWHALTP 166
Cdd:COG1211 81 SVRNGLEAlPDDDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832855 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211 159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-223 |
2.36e-89 |
|
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: 262.84 E-value: 2.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQ--LPLANHPQITVVDGGDER 85
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 86 ADSVLAGLKA--AGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHA 163
Cdd:cd02516 81 QDSVLNGLKAlpDADPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 164 LTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-232 |
3.18e-123 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 348.66 E-value: 3.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLANHPQITVVDGGDERA 86
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRNGLWHALTP 166
Cdd:PRK00155 84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832855 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
10-229 |
8.83e-116 |
|
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: 329.80 E-value: 8.83e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 10 AVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLanHPQITVVDGGDERADS 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 89 VLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQ 167
Cdd:pfam01128 79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832855 168 FFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
9-227 |
2.98e-105 |
|
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: 303.05 E-value: 2.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 9 CAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADS 88
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 89 VLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQF 168
Cdd:TIGR00453 81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15832855 169 FPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
11-229 |
2.57e-101 |
|
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: 293.19 E-value: 2.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 11 VVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQL--PLANHPQITVVDGGDERAD 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 88 SVLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRtGGILAAPVRDTMKRAEPGkNAIAHTVDRNGLWHALTP 166
Cdd:COG1211 81 SVRNGLEAlPDDDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832855 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211 159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-223 |
2.36e-89 |
|
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: 262.84 E-value: 2.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQ--LPLANHPQITVVDGGDER 85
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 86 ADSVLAGLKA--AGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHA 163
Cdd:cd02516 81 QDSVLNGLKAlpDADPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 164 LTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
3-229 |
1.48e-54 |
|
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: 179.27 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 3 TTHLDVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGG 82
Cdd:PRK09382 1 TLMSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 83 DERADSVLAGLKAAgDAQWVLVHDAARPCLHQDDLARLL-ALSETSrtgGILAA-PVRDTMKRAEPgknaiahTVDRNGL 160
Cdd:PRK09382 81 ATRQESVRNALEAL-DSEYVLIHDAARPFVPKELIDRLIeALDKAD---CVLPAlPVADTLKRANE-------TVDREGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832855 161 WHALTPQFFPRELlhdcLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:PRK09382 150 KLIQTPQLSRTKT----LKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSP 214
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
14-223 |
1.71e-41 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 141.16 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 14 AAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIA-----ISPGDSRFAQLPLANHpQITVVDGGDERADS 88
Cdd:PRK13385 9 AAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQ-RVEVVKGGTERQES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 89 VLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSRtGGILAAPVRDTMKRAEPGKNAiaHTVDRNGLWHALTPQF 168
Cdd:PRK13385 88 VAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYG-AAICAVEVKDTVKRVKDKQVI--ETVDRNELWQGQTPQA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15832855 169 FPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:PRK13385 165 FELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
7-228 |
2.13e-36 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 128.70 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 7 DVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISP--------------GDSRFAqLPlan 72
Cdd:PLN02728 24 SVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPsyrdvfeeavenidVPLKFA-LP--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 73 hpqitvvdgGDERADSVLAGLKAA-GDAQWVLVHDAARPCLHQDDLARLLalSETSRTGG-ILAAPVRDTMKRAEPGkNA 150
Cdd:PLN02728 100 ---------GKERQDSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVL--KDAAVHGAaVLGVPVKATIKEANSD-SF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832855 151 IAHTVDRNGLWHALTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGfHP-QLVEGRADNIKVTRPEDLALAEFYLT 228
Cdd:PLN02728 168 VVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALK-HPvFITEGSYTNIKVTTPDDMLVAERILN 245
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
8-139 |
8.55e-13 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 64.80 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 8 VCAVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHpRVKRVVIAISPGDSRFAqlPLANHPQITVV---DGGDE 84
Cdd:COG2068 4 VAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLGADAEEVA--AALAGLGVRVVvnpDWEEG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15832855 85 RADSVLAGLKAA-GDAQWVLVHDAARPCLHQDDLARLLALSEtsRTGGILAAPVRD 139
Cdd:COG2068 79 MSSSLRAGLAALpADADAVLVLLGDQPLVTAETLRRLLAAFR--ESPASIVAPTYD 132
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
8-137 |
6.79e-11 |
|
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: 59.50 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 8 VCAVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHPRVKrvVIAISPGDSRFAQLPLANHPQITVVDGGDER-- 85
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSR--VIVVLGAEADAVRAALAGLPVVVVINPDWEEgm 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15832855 86 ADSVLAGLKAA-GDAQWVLVHDAARPCLHQDDLARLLALSetSRTGGILAAPV 137
Cdd:cd04182 77 SSSLAAGLEALpADADAVLILLADQPLVTAETLRALIDAF--REDGAGIVAPV 127
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
10-174 |
4.02e-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: 56.82 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 10 AVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHprVKRVVIaISPGDSRFAQLPLANHPQITVVDGGDERADSV 89
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRPA--GDEVVV-VANDEEVLAALAGLGVPVVPDPDPGQGPLAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 90 LAGLKAAGDAQWVLVHDAARPCLHQDDLARLLAlsetsrtggilaapvrdtmkRAEPGKNAIAHTVDRNGLWHALtpqFF 169
Cdd:pfam12804 76 LAALRAAPGADAVLVLACDMPFLTPELLRRLLA--------------------AAEESGADIVVPVYDGGRGHPL---LY 132
|
....*
gi 15832855 170 PRELL 174
Cdd:pfam12804 133 RRRLL 137
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
10-123 |
1.11e-08 |
|
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: 53.11 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 10 AVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHpRVKRVVIAISPGDSRFAQLpLANHPQITVVDGGDER---A 86
Cdd:TIGR03310 2 AIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHEADELVAL-LANHSNITLVHNPQYAegqS 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 15832855 87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLAL 123
Cdd:TIGR03310 78 SSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEA 114
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
10-59 |
6.79e-07 |
|
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: 48.61 E-value: 6.79e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15832855 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNQTILEHSVYALLAHPrVKRVVIAIS 59
Cdd:COG1208 2 AVILAGGLGTRLRplTDtRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG 53
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
10-80 |
1.98e-06 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 47.16 E-value: 1.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832855 10 AVVPAAGFGRRMQ---TECPKQYLSIGNQTILEHSVYALLAHpRVKRVVIAISPGDSRFAQLPLANHPQITVVD 80
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAELIEEALARPGPDVTFVY 74
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
10-60 |
2.08e-06 |
|
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: 47.19 E-value: 2.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15832855 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNQTILEHSVYALLAHPrVKRVVIAISP 60
Cdd:cd04181 1 AVILAAGKGTRLRplTDtRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGY 53
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
10-56 |
2.67e-05 |
|
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: 43.76 E-value: 2.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15832855 10 AVVPAAGFGRRMQT---ECPKQYLSIGNQTILEHSVYALLAHpRVKRVVI 56
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVI 49
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-130 |
2.79e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 38.38 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832855 7 DVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLA-HPRvkRVVIAISPGDSRFAQLPLANHPQITVVD----G 81
Cdd:PRK14352 4 PTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGlAPQ--HLVVVVGHDRERVAPAVAELAPEVDIAVqdeqP 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15832855 82 GDERAdsVLAGLKAAGD--AQWVLVHDAARPCLHQDDLARLLALSETSRTG 130
Cdd:PRK14352 82 GTGHA--VQCALEALPAdfDGTVVVTAGDVPLLDGETLADLVATHTAEGNA 130
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
10-56 |
5.23e-03 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 36.78 E-value: 5.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15832855 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNQTILEHSVyALLAHPRVKRVVI 56
Cdd:cd06422 2 AMILAAGLGTRMRplTDtRPKPLVPVAGKPLIDHAL-DRLAAAGIRRIVV 50
|
|
| |
