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Conserved domains on  [gi|465143603|gb|EMP15660|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Fusobacterium nucleatum CC53]

Protein Classification

IspD/TarI family cytidylyltransferase( domain architecture ID 10118526)

IspD/TarI family cytidylyltransferase such as 2-C-methyl-d-erythritol 4-phosphate cytidylyltransferase (IspD) that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-d-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP, and ribitol-5-phosphate cytidylyltransferase (TarI) that catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate

EC:  2.7.7.-
Gene Ontology:  GO:0070567
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
12-230 7.59e-94

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: 274.02  E-value: 7.59e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  12 VTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYcqDKNLFSKVKYIVEGGS 91
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  92 ERQYSIYNAIKKIE--DTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIM 169
Cdd:cd02516   79 TRQDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465143603 170 VHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFL 230
Cdd:cd02516  158 AQTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
12-230 7.59e-94

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: 274.02  E-value: 7.59e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  12 VTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYcqDKNLFSKVKYIVEGGS 91
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  92 ERQYSIYNAIKKIE--DTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIM 169
Cdd:cd02516   79 TRQDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465143603 170 VHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFL 230
Cdd:cd02516  158 AQTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
15-231 7.29e-88

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: 258.91  E-value: 7.29e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCqDKNLFSKVKYIVEGGSERQ 94
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELL-AKYGIDKPVRVVAGGATRQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  95 YSIYNAIKKI-EDTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIMVHTP 173
Cdd:COG1211   80 DSVRNGLEALpDDDDWVLVHDAARPLVSPELIDRVIEAAR-EYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTP 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 465143603 174 QTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFLK 231
Cdd:COG1211  159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAE 216
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
11-229 3.32e-83

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 247.35  E-value: 3.32e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  11 KVTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCQDKNlfSKVKyIVEGG 90
Cdd:PRK00155   3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD--PKVT-VVAGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  91 SERQYSIYNAIKKIEDTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIMV 170
Cdd:PRK00155  80 AERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAE-ETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 465143603 171 HTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKF 229
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLAL 217
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
15-231 1.88e-75

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: 227.17  E-value: 1.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCQDKNLFSkvkyIVEGGSERQ 94
Cdd:TIGR00453   3 VIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK----IVAGGDTRQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   95 YSIYNAIKKIEDTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIMVHTPQ 174
Cdd:TIGR00453  79 DSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALR-KAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTPQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 465143603  175 TFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFLK 231
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAE 214
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
15-227 6.42e-59

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: 185.35  E-value: 6.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKenlnfmvkycQDKNLFSKVK-----YIVEG 89
Cdd:pfam01128   2 VIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSP----------DDTPEFRQLLgdpsiQLVAG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   90 GSERQYSIYNAIKKIEDTD-IVIIQDAARPFLKDKYIEESIKILDNDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLI 168
Cdd:pfam01128  72 GDTRQDSVLNGLKALAGTAkFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLW 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 465143603  169 MVHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDL 227
Cdd:pfam01128 152 AAQTPQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDL 210
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
12-230 7.59e-94

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: 274.02  E-value: 7.59e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  12 VTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYcqDKNLFSKVKYIVEGGS 91
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  92 ERQYSIYNAIKKIE--DTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIM 169
Cdd:cd02516   79 TRQDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465143603 170 VHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFL 230
Cdd:cd02516  158 AQTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
15-231 7.29e-88

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: 258.91  E-value: 7.29e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCqDKNLFSKVKYIVEGGSERQ 94
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELL-AKYGIDKPVRVVAGGATRQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  95 YSIYNAIKKI-EDTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIMVHTP 173
Cdd:COG1211   80 DSVRNGLEALpDDDDWVLVHDAARPLVSPELIDRVIEAAR-EYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTP 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 465143603 174 QTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFLK 231
Cdd:COG1211  159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAE 216
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
11-229 3.32e-83

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 247.35  E-value: 3.32e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  11 KVTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCQDKNlfSKVKyIVEGG 90
Cdd:PRK00155   3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD--PKVT-VVAGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  91 SERQYSIYNAIKKIEDTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIMV 170
Cdd:PRK00155  80 AERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAE-ETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 465143603 171 HTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKF 229
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLAL 217
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
15-231 1.88e-75

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: 227.17  E-value: 1.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCQDKNLFSkvkyIVEGGSERQ 94
Cdd:TIGR00453   3 VIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK----IVAGGDTRQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   95 YSIYNAIKKIEDTDIVIIQDAARPFLKDKYIEESIKILDnDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLIMVHTPQ 174
Cdd:TIGR00453  79 DSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALR-KAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTPQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 465143603  175 TFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFLK 231
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAE 214
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
15-227 6.42e-59

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: 185.35  E-value: 6.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKenlnfmvkycQDKNLFSKVK-----YIVEG 89
Cdd:pfam01128   2 VIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSP----------DDTPEFRQLLgdpsiQLVAG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   90 GSERQYSIYNAIKKIEDTD-IVIIQDAARPFLKDKYIEESIKILDNDCDGAVIGVKCKDTVKIIDENGIVVETPNRNNLI 168
Cdd:pfam01128  72 GDTRQDSVLNGLKALAGTAkFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLW 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 465143603  169 MVHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDL 227
Cdd:pfam01128 152 AAQTPQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDL 210
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
15-231 1.40e-49

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional


Pssm-ID: 184017  Cd Length: 230  Bit Score: 161.96  E-value: 1.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  15 ILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCQDKNLFSKVKYIVEGGSERQ 94
Cdd:PRK13385   6 IFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKGGTERQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  95 YSIYNAIKKIEDTDIVIIQDAARPFLKDKYIEESIKILDNdcDGAVI-GVKCKDTVKIIdENGIVVETPNRNNLIMVHTP 173
Cdd:PRK13385  86 ESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAK--YGAAIcAVEVKDTVKRV-KDKQVIETVDRNELWQGQTP 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 465143603 174 QTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFLK 231
Cdd:PRK13385 163 QAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAK 220
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
10-230 1.22e-43

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: 150.38  E-value: 1.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  10 KKVTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTNKENLNFMVKYCQDKNLFSkvkyIVEG 89
Cdd:PRK09382   4 SDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVT----LVTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  90 GSERQYSIYNAIKKIeDTDIVIIQDAARPFLKDKYIEESIKILDNDcDGAVIGVKCKDTVKIIDengivvETPNRNNLIM 169
Cdd:PRK09382  80 GATRQESVRNALEAL-DSEYVLIHDAARPFVPKELIDRLIEALDKA-DCVLPALPVADTLKRAN------ETVDREGLKL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465143603 170 VHTPQTFKFEILKKAHQMAEEknilATDDASLVEMISGKVKIIYGDYDNIKITVQEDLKFL 230
Cdd:PRK09382 152 IQTPQLSRTKTLKAAADGRGD----FTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMA 208
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
3-227 2.05e-41

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 141.41  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   3 SSNSKIKKK-VTFILAAAGQGKRMNLNSPKQFLDYKGEPLFYSSLKIAFDNKYIDDIIIVTN----------KENLNFMV 71
Cdd:PLN02728  15 ETSAVVKEKsVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDpsyrdvfeeaVENIDVPL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603  72 KYCQDknlfskvkyivegGSERQYSIYNAIKKI-EDTDIVIIQDAARPFLKDKYIEESIKilDNDCDGA-VIGVKCKDTV 149
Cdd:PLN02728  95 KFALP-------------GKERQDSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVLK--DAAVHGAaVLGVPVKATI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 465143603 150 KIIDENGIVVETPNRNNLIMVHTPQTFKFEILKKAHQMAEEKNILATDDASLVEMISGKVKIIYGDYDNIKITVQEDL 227
Cdd:PLN02728 160 KEANSDSFVVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDM 237
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
9-62 6.11e-06

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 45.15  E-value: 6.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 465143603   9 KKKVTFILAAAGQGKRMnlNSPKQFLDYKGEPLFYSSLKIAFDNKyIDDIIIVT 62
Cdd:COG2068    1 MSKVAAIILAAGASSRM--GRPKLLLPLGGKPLLERAVEAALAAG-LDPVVVVL 51
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
15-164 1.99e-03

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 38.39  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   15 ILAAAGQGKRM----NLNSPKQFLDYKGEPLFYSSLKIAFdNKYIDDIIIVTNKENLnFMVK-YCQDKNLFS-KVKYIVE 88
Cdd:pfam00483   3 IILAGGSGTRLwpltRTLAKPLVPVGGKYPLIDYPLSRLA-NAGIREIIVILTQEHR-FMLNeLLGDGSKFGvQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465143603   89 G-GSERQYSIYNAIKKIEDTDI--------VIIQDAARPFLKdKYIEesikiLDNDCDGAVIGVKCKDT----VKIIDEN 155
Cdd:pfam00483  81 PeGKGTAPAVALAADFLGDEKSdvlvlggdHIYRMDLEQAVK-FHIE-----KAADATVTFGIVPVEPPtgygVVEFDDN 154
                         170
                  ....*....|..
gi 465143603  156 GIV---VETPNR 164
Cdd:pfam00483 155 GRVirfVEKPKL 166
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
15-63 3.29e-03

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: 36.79  E-value: 3.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 465143603   15 ILAAaGQGKRMnlNSPKQFLDYKGEPLFYSSLKIAfdNKYIDDIIIVTN 63
Cdd:pfam12804   3 ILAG-GRSSRM--GGDKALLPLGGKPLLERVLERL--RPAGDEVVVVAN 46
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
12-41 5.55e-03

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: 36.77  E-value: 5.55e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 465143603  12 VTFILAAAGQGKRMnlNSPKQFLDYKGEPL 41
Cdd:cd04182    1 IAAIILAAGRSSRM--GGNKLLLPLDGKPL 28
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
15-62 8.52e-03

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 36.37  E-value: 8.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 465143603  15 ILAAaGQGKRMN---LNSPKQFLDYKGEPLFYSSLKiAFDNKYIDDIIIVT 62
Cdd:COG1213    4 ILAA-GRGSRLGpltDDIPKCLVEIGGKTLLERQLE-ALAAAGIKDIVVVT 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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