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Conserved domains on  [gi|575501644|ref|NP_001276433|]
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D-ribitol-5-phosphate cytidylyltransferase isoform 4 [Mus musculus]

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; ...
 45-271 6.13e-82

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: 245.90  E-value: 6.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516   81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501644 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 45-271 6.13e-82

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: 245.90  E-value: 6.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516   81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501644 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 48-277 9.30e-59

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: 186.87  E-value: 9.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  48 VLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYG-HKRISLAEAGATRHR 126
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 127 SIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKH 206
Cdd:COG1211   81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501644 207 RASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPALWKVTYKQDLCAAEAMIKG 277
Cdd:COG1211  153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSEDNIKITTPEDLALAEALLRS 221
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
45-277 1.05e-49

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 163.77  E-value: 1.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGATR 124
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGGAER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 125 HRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:PRK00155  83 QDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501644 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCAAEAMIKG 277
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLALAEAILKR 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 46-273 2.86e-44

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: 149.75  E-value: 2.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644   46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRygHKRISLAEAGATRH 125
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVA--RAVPKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  126 RSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAK 205
Cdd:TIGR00453  79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575501644  206 HRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEA 273
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALAEA 215
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 47-275 6.18e-37

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: 130.65  E-value: 6.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644   47 AVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIqryGHKRISLAEAGATRHR 126
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  127 SIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTVISPSADGHLDHSLDRA 204
Cdd:pfam01128  78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501644  205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMI 275
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 45-271 6.13e-82

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: 245.90  E-value: 6.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516   81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575501644 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 48-277 9.30e-59

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: 186.87  E-value: 9.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  48 VLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYG-HKRISLAEAGATRHR 126
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 127 SIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKH 206
Cdd:COG1211   81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501644 207 RASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPALWKVTYKQDLCAAEAMIKG 277
Cdd:COG1211  153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSEDNIKITTPEDLALAEALLRS 221
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
45-277 1.05e-49

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 163.77  E-value: 1.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGATR 124
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGGAER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 125 HRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:PRK00155  83 QDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501644 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCAAEAMIKG 277
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLALAEAILKR 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 46-273 2.86e-44

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: 149.75  E-value: 2.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644   46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRygHKRISLAEAGATRH 125
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVA--RAVPKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  126 RSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAK 205
Cdd:TIGR00453  79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575501644  206 HRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEA 273
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALAEA 215
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 47-275 6.18e-37

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: 130.65  E-value: 6.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644   47 AVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIqryGHKRISLAEAGATRHR 126
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  127 SIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTVISPSADGHLDHSLDRA 204
Cdd:pfam01128  78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575501644  205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMI 275
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 44-275 1.64e-32

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: 123.03  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  44 TVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYghKRISLAEAGAT 123
Cdd:PRK09382   5 DISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI--KFVTLVTGGAT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 124 RHRSIFNGLKALAEdqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVIspsadgHLDHSLDR 203
Cdd:PRK09382  83 RQESVRNALEALDS----------EYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLK------RANETVDR 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575501644 204 AKHRASEMPQAFLFDVIYEAYQQCSDFdlefgTECLQlALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMI 275
Cdd:PRK09382 147 EGLKLIQTPQLSRTKTLKAAADGRGDF-----TDDSS-AAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 46-277 2.32e-24

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 98.02  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRY--GHKRISLAEAGAT 123
Cdd:PRK13385   4 ELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLnvADQRVEVVKGGTE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 124 RHRSIFNGLKALAEDQpdckltkpeVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISpSADGHLDHSLDR 203
Cdd:PRK13385  84 RQESVAAGLDRIGNED---------VILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKR-VKDKQVIETVDR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501644 204 AKHRASEMPQAFLFDVIYEAYQQCSDfDLEFGTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAAEAMIKG 277
Cdd:PRK13385 154 NELWQGQTPQAFELKILQKAHRLASE-QQFLGTDEASLVERSPH-PVKLVQGSYYNIKLTTPEDMPLAKAILQG 225
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 43-275 1.38e-21

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 90.95  E-value: 1.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  43 GTVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGA 122
Cdd:PLN02728  23 KSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENI-DVPLKFALPGK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 123 TRHRSIFNGLKALaedQPDCKLtkpevVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLD 202
Cdd:PLN02728 102 ERQDSVFNGLQEV---DANSEL-----VCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLD 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575501644 203 RAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQL--ALKychRKAKLVEGPPALWKVTYKQDLCAAEAMI 275
Cdd:PLN02728 174 RKRLWEMQTPQVIKPELLRRGFELVEREGLEV-TDDVSIveALK---HPVFITEGSYTNIKVTTPDDMLVAERIL 244
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 47-193 4.31e-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: 46.42  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  47 AVLPAGGCGERMG---VRTPKQFCRVLERPLISYTLQAMERVcWIKDIVVtVTGENMEAmrsIIQRYG-----HKRISLA 118
Cdd:cd04181    1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARA-GIDEIIL-VVGYLGEQ---IEEYFGdgskfGVNIEYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644 119 E-------AGAtrhrsIFNGLKALAEDqpdckltkpEVVIIH-DAVrpfVEEDiLLRVVLAAKEHGAAGAIrpLVSTVIS 190
Cdd:cd04181   76 VqeeplgtAGA-----VRNAEDFLGDD---------DFLVVNgDVL---TDLD-LSELLRFHREKGADATI--AVKEVED 135


                 ...
gi 575501644 191 PSA 193
Cdd:cd04181  136 PSR 138
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 47-95 2.34e-05

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: 44.76  E-value: 2.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 575501644  47 AVLPAGGCGERMG---VRTPKQFCRVLERPLISYTLQAMERvCWIKDIVVTV 95
Cdd:COG1208    2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINV 52
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 45-183 5.51e-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: 5.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  45 VAAVLPAGGCGERMGvrTPKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTGENMEAMRSIIQRYGHKRISLAEA---- 120
Cdd:cd04182    1 IAAIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAG-LSRVIV-VLGAEADAVRAALAGLPVVVVINPDWeegm 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575501644 121 GAtrhrSIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGaAGAIRP 183
Cdd:cd04182   77 SS----SLAAGLEALPAD--------ADAVLILLADQPLVTAETLRALIDAFREDG-AGIVAP 126
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 47-181 8.63e-05

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: 42.18  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644   47 AVLPAGGCGERMGvrTPKQFCRVLERPLISYTLQAMERVCwiKDIVVtVTGEnmEAMRSIIQRYGHKRISLAEAGATRHR 126
Cdd:pfam12804   1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAG--DEVVV-VAND--EEVLAALAGLGVPVVPDPDPGQGPLA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 575501644  127 SIFNGLKALAEDQPdckltkpeVVIIH-DAvrPFVEEDILLRVVLAAKEHGAAGAI 181
Cdd:pfam12804  74 GLLAALRAAPGADA--------VLVLAcDM--PFLTPELLRRLLAAAEESGADIVV 119
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 51-115 3.68e-04

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: 40.64  E-value: 3.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575501644  51 AGGCGERMGvRTPKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTGENMEAMRSIIQRYGHKRI 115
Cdd:COG2266    2 AGGKGTRLG-GGEKPLLEICGKPMIDRVIDALEESC-IDKIYV-AVSPNTPKTREYLKERGVEVI 63
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
47-97 3.74e-04

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 40.99  E-value: 3.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 575501644  47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTG 97
Cdd:COG1213    2 AVILAAGRGSRLGPLTddiPKCLVEIGGKTLLERQLEALAAAG-IKDIVV-VTG 53
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 47-107 2.73e-03

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 38.32  E-value: 2.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575501644  47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMeRVCWIKDIVVtVTGENMEAMRSII 107
Cdd:cd04189    3 GLILAGGKGTRLRPLTytrPKQLIPVAGKPIIQYAIEDL-REAGIEDIGI-VVGPTGEEIKEAL 64
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 47-113 4.16e-03

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 37.64  E-value: 4.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575501644  47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMERVCwIKDIVVTVTGENMEAMRSIIQRYGHK 113
Cdd:cd04198    3 AVILAGGGGSRLYPLTdniPKALLPVANKPMIWYPLDWLEKAG-FEDVIVVVPEEEQAEISTYLRSFPLN 71
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 47-97 7.11e-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: 37.21  E-value: 7.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 575501644  47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMERvCWIKDIVVtVTG 97
Cdd:cd02523    1 AIILAAGRGSRLRPLTedrPKCLLEINGKPLLERQIETLKE-AGIDDIVI-VTG 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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