|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
10-238 |
3.61e-97 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 282.79 E-value: 3.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 10 QTKLWAVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLP-LNGYVLAIGTQD-TFAQTLAFQNIDKAHFCMGGA 87
Cdd:PRK00155 1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 88 ERVHSVLNALNHLltfaDENDWVLVHDAARPCVTIECLNALVEQAIEsNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLL 167
Cdd:PRK00155 81 ERQDSVLNGLQAL----PDDDWVLVHDAARPFLTPDDIDRLIEAAEE-TGAAILAVPVKDTIKRSDDGGGIVDTPDRSGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518597504 168 WQAQTPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQSQS 238
Cdd:PRK00155 156 WAAQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRI 226
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
16-238 |
2.41e-89 |
|
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: 263.14 E-value: 2.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 16 VIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPL-NGYVLAIGTQD--TFAQTLAFQNIDK-AHFCMGGAERVH 91
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVPPDDieYFEELLAKYGIDKpVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 92 SVLNALNHLltfADENDWVLVHDAARPCVTIECLNALVEqAIESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQAQ 171
Cdd:COG1211 81 SVRNGLEAL---PDDDDWVLVHDAARPLVSPELIDRVIE-AAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518597504 172 TPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQSQS 238
Cdd:COG1211 157 TPQGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRE 223
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
14-230 |
1.81e-83 |
|
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: 247.82 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 14 WAVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPL-NGYVLAI--GTQDTFAQTLAFQNIDKAHFCMGGAERV 90
Cdd:cd02516 2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVppDDIDLAKELAKYGLSKVVKIVEGGATRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 91 HSVLNALNHLLtfADENDWVLVHDAARPCVTIECLNALVEqAIESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQA 170
Cdd:cd02516 82 DSVLNGLKALP--DADPDIVLIHDAARPFVSPELIDRLID-ALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 171 QTPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELA 230
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
14-234 |
2.25e-74 |
|
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: 224.86 E-value: 2.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 14 WAVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLP-LNGYVLAIGTQDTFAQTLAFQNIDKAHFCMGGAERVHS 92
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPaIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 93 VLNALnhllTFADENDWVLVHDAARPCVTIECLNALVEQAiESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQAQT 172
Cdd:TIGR00453 81 VRNGL----KALKDAEFVLVHDAARPFVPKELLDRLLEAL-RKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518597504 173 PQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLIL 234
Cdd:TIGR00453 156 PQAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
15-236 |
9.31e-60 |
|
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: 187.66 E-value: 9.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 15 AVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPLNGYVLAIGTQDTFAQTLAFQNIDKAHFCMGGAERVHSVL 94
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQLVAGGDTRQDSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 95 NALNHLltfADENDWVLVHDAARPCVTIECLNALVEQAIESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQAQTPQ 174
Cdd:pfam01128 81 NGLKAL---AGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518597504 175 IAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQS 236
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
10-238 |
3.61e-97 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 282.79 E-value: 3.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 10 QTKLWAVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLP-LNGYVLAIGTQD-TFAQTLAFQNIDKAHFCMGGA 87
Cdd:PRK00155 1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 88 ERVHSVLNALNHLltfaDENDWVLVHDAARPCVTIECLNALVEQAIEsNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLL 167
Cdd:PRK00155 81 ERQDSVLNGLQAL----PDDDWVLVHDAARPFLTPDDIDRLIEAAEE-TGAAILAVPVKDTIKRSDDGGGIVDTPDRSGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518597504 168 WQAQTPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQSQS 238
Cdd:PRK00155 156 WAAQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRI 226
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
16-238 |
2.41e-89 |
|
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: 263.14 E-value: 2.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 16 VIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPL-NGYVLAIGTQD--TFAQTLAFQNIDK-AHFCMGGAERVH 91
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVPPDDieYFEELLAKYGIDKpVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 92 SVLNALNHLltfADENDWVLVHDAARPCVTIECLNALVEqAIESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQAQ 171
Cdd:COG1211 81 SVRNGLEAL---PDDDDWVLVHDAARPLVSPELIDRVIE-AAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518597504 172 TPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQSQS 238
Cdd:COG1211 157 TPQGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRE 223
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
14-230 |
1.81e-83 |
|
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: 247.82 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 14 WAVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPL-NGYVLAI--GTQDTFAQTLAFQNIDKAHFCMGGAERV 90
Cdd:cd02516 2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVppDDIDLAKELAKYGLSKVVKIVEGGATRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 91 HSVLNALNHLLtfADENDWVLVHDAARPCVTIECLNALVEqAIESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQA 170
Cdd:cd02516 82 DSVLNGLKALP--DADPDIVLIHDAARPFVSPELIDRLID-ALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 171 QTPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELA 230
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
14-234 |
2.25e-74 |
|
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: 224.86 E-value: 2.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 14 WAVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLP-LNGYVLAIGTQDTFAQTLAFQNIDKAHFCMGGAERVHS 92
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPaIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 93 VLNALnhllTFADENDWVLVHDAARPCVTIECLNALVEQAiESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQAQT 172
Cdd:TIGR00453 81 VRNGL----KALKDAEFVLVHDAARPFVPKELLDRLLEAL-RKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518597504 173 PQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLIL 234
Cdd:TIGR00453 156 PQAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
15-236 |
9.31e-60 |
|
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: 187.66 E-value: 9.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 15 AVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPLNGYVLAIGTQDTFAQTLAFQNIDKAHFCMGGAERVHSVL 94
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQLVAGGDTRQDSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 95 NALNHLltfADENDWVLVHDAARPCVTIECLNALVEQAIESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQAQTPQ 174
Cdd:pfam01128 81 NGLKAL---AGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518597504 175 IAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQS 236
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
15-230 |
1.44e-44 |
|
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: 153.08 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 15 AVIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPLNG-YVLAIGTQDTFAQTLAFQNIDKAHFCMGGAERVHSV 93
Cdd:PRK09382 8 LVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKeIVVVIHPDDIAYMKKALPEIKFVTLVTGGATRQESV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 94 LNALNHLltfadENDWVLVHDAARPCVTIECLNALVEqAIESNHSAILAIPVRDTLKQVksgnqiDKTVSRDLLWQAQTP 173
Cdd:PRK09382 88 RNALEAL-----DSEYVLIHDAARPFVPKELIDRLIE-ALDKADCVLPALPVADTLKRA------NETVDREGLKLIQTP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518597504 174 QIAKIGKLKKAieyaLENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELA 230
Cdd:PRK09382 156 QLSRTKTLKAA----ADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMA 208
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
16-238 |
3.34e-41 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 141.02 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 16 VIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRISQLPLNGYVLAI---GTQDTFAQtlAFQNIDK-AHFCMGGAERVH 91
Cdd:PLN02728 28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVcdpSYRDVFEE--AVENIDVpLKFALPGKERQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 92 SVLNALNHLltfaDEN-DWVLVHDAARPCVTIECLNALVEQAiESNHSAILAIPVRDTLKQVKSGNQIDKTVSRDLLWQA 170
Cdd:PLN02728 106 SVFNGLQEV----DANsELVCIHDSARPLVTSADIEKVLKDA-AVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEM 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518597504 171 QTPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQSQS 238
Cdd:PLN02728 181 QTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERS 248
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
16-236 |
1.52e-31 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 115.35 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 16 VIPAAGSGSRFSKTELKQYQYIQNTTVLEHTVRRIsqLPLNGYV-LAIGTQDTF---AQTLAFQ-NI--DKAHFCMGGAE 88
Cdd:PRK13385 6 IFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPF--LADNRCSkIIIVTQAQErkhVQDLMKQlNVadQRVEVVKGGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 89 RVHSVLNALNHlltfADENDWVLVHDAARPCVTIECLNALVEqAIESNHSAILAIPVRDTLKQVKSgNQIDKTVSRDLLW 168
Cdd:PRK13385 84 RQESVAAGLDR----IGNEDVILVHDGARPFLTQDIIDRLLE-GVAKYGAAICAVEVKDTVKRVKD-KQVIETVDRNELW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518597504 169 QAQTPQIAKIGKLKKAIEYALENNIAITDEASALEYMGETVQVVMGRSDNIKITYPDDLELARLILQS 236
Cdd:PRK13385 158 QGQTPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQG 225
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
11-142 |
1.91e-05 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 44.00 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 11 TKLWAVIPAAGSGSRFSktELKQYQYIQNTTVLEHTVRRISQLPLNGYVLAIGTQ-DTFAQTLAFQNIdKAHFC------ 83
Cdd:COG2068 2 SKVAAIILAAGASSRMG--RPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADaEEVAAALAGLGV-RVVVNpdweeg 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518597504 84 MGgaervHSVLNALNHLltfADENDWVLVHDAARPCVTIECLNALVEQAIESNHSAILA 142
Cdd:COG2068 79 MS-----SSLRAGLAAL---PADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAP 129
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
15-142 |
4.12e-05 |
|
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: 42.93 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 15 AVIPAAGSGSRFSktELKQYQYIQNTTVLEHTVRRISQLPLNGYVLAIG-TQDTFAQTLA---FQNIDKAHFCMGGAerv 90
Cdd:cd04182 3 AIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGaEADAVRAALAglpVVVVINPDWEEGMS--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 518597504 91 HSVLNALNHLLtfaDENDWVLVHDAARPCVTIECLNALVEQAIESNHSAILA 142
Cdd:cd04182 78 SSLAAGLEALP---ADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAP 126
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
15-147 |
6.05e-04 |
|
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: 39.10 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518597504 15 AVIPAAGSGSRF--SKTELKqyqyIQNTTVLEHTVRRISqlPLNGYVLAIGTQDTFAQTLAFQNI-----DKAHFCMGGa 87
Cdd:pfam12804 1 AVILAGGRSSRMggDKALLP----LGGKPLLERVLERLR--PAGDEVVVVANDEEVLAALAGLGVpvvpdPDPGQGPLA- 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518597504 88 ervhSVLNALNHlltfADENDWVLVhdAA--RPCVTIECLNALVEQAIESNHSAilAIPVRD 147
Cdd:pfam12804 74 ----GLLAALRA----APGADAVLV--LAcdMPFLTPELLRRLLAAAEESGADI--VVPVYD 123
|
|
| |
