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Conserved domains on  [gi|1907089536|ref|XP_011242212|]
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D-ribitol-5-phosphate cytidylyltransferase isoform X5 [Mus musculus]

Protein Classification

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; ...
1-172 2.98e-54

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: 178.49  E-value: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   1 MEAMRSIIQRYGHKRISLAEAGATRHRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAG 80
Cdd:cd02516    56 IDLAKELAKYGLSKVVKIVEGGATRQDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  81 AIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPAL 160
Cdd:cd02516   129 PAVPVTDTIKRVDDDGVVVETLDREKLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDN 206
                         170
                  ....*....|..
gi 1907089536 161 WKVTYKQDLCAA 172
Cdd:cd02516   207 IKITTPEDLALA 218
ISPD_C super family cl40022
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
182-315 4.35e-54

D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.


The actual alignment was detected with superfamily member pfam18706:

Pssm-ID: 465843  Cd Length: 169  Bit Score: 176.39  E-value: 4.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536 182 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 259
Cdd:pfam18706   1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089536 260 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQD 315
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQD 136
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
1-172 2.98e-54

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: 178.49  E-value: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   1 MEAMRSIIQRYGHKRISLAEAGATRHRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAG 80
Cdd:cd02516    56 IDLAKELAKYGLSKVVKIVEGGATRQDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  81 AIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPAL 160
Cdd:cd02516   129 PAVPVTDTIKRVDDDGVVVETLDREKLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDN 206
                         170
                  ....*....|..
gi 1907089536 161 WKVTYKQDLCAA 172
Cdd:cd02516   207 IKITTPEDLALA 218
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
182-315 4.35e-54

D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.


Pssm-ID: 465843  Cd Length: 169  Bit Score: 176.39  E-value: 4.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536 182 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 259
Cdd:pfam18706   1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089536 260 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQD 315
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQD 136
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
1-179 1.24e-38

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: 137.95  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   1 MEAMRSIIQRYG-HKRISLAEAGATRHRSIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAA 79
Cdd:COG1211    53 IEYFEELLAKYGiDKPVRVVAGGATRQDSVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  80 GAIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPA 159
Cdd:COG1211   125 IPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSED 202
                         170       180
                  ....*....|....*....|
gi 1907089536 160 LWKVTYKQDLCAAEAMIKEK 179
Cdd:COG1211   203 NIKITTPEDLALAEALLRSR 222
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
13-180 1.90e-30

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 116.39  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  13 HKRISLAEAGATRHRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISP 92
Cdd:PRK00155   70 DPKVTVVAGGAERQDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  93 SADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCA 171
Cdd:PRK00155  141 DDGGGIVDTPDRSGLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLAL 217

                  ....*....
gi 1907089536 172 AEAMIKEKI 180
Cdd:PRK00155  218 AEAILKRRI 226
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
13-174 7.99e-26

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: 103.52  E-value: 7.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  13 HKRISLAEAGATRHRSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISP 92
Cdd:TIGR00453  65 RAVPKIVAGGDTRQDSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  93 SADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAA 172
Cdd:TIGR00453 136 EADGFVVETVDREGLWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALA 213

                  ..
gi 1907089536 173 EA 174
Cdd:TIGR00453 214 EA 215
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
12-178 1.62e-22

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: 94.44  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  12 GHKRISLAEAGATRHRSIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTV 89
Cdd:pfam01128  62 GDPSIQLVAGGDTRQDSVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  90 ISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDL 169
Cdd:pfam01128 133 KRVEADGVVAGTPDRSGLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDL 210

                  ....*....
gi 1907089536 170 CAAEAMIKE 178
Cdd:pfam01128 211 ALAEAILTR 219
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
1-172 2.98e-54

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: 178.49  E-value: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   1 MEAMRSIIQRYGHKRISLAEAGATRHRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAG 80
Cdd:cd02516    56 IDLAKELAKYGLSKVVKIVEGGATRQDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  81 AIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPAL 160
Cdd:cd02516   129 PAVPVTDTIKRVDDDGVVVETLDREKLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDN 206
                         170
                  ....*....|..
gi 1907089536 161 WKVTYKQDLCAA 172
Cdd:cd02516   207 IKITTPEDLALA 218
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
182-315 4.35e-54

D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.


Pssm-ID: 465843  Cd Length: 169  Bit Score: 176.39  E-value: 4.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536 182 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 259
Cdd:pfam18706   1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089536 260 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQD 315
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQD 136
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
1-179 1.24e-38

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: 137.95  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   1 MEAMRSIIQRYG-HKRISLAEAGATRHRSIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAA 79
Cdd:COG1211    53 IEYFEELLAKYGiDKPVRVVAGGATRQDSVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  80 GAIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPA 159
Cdd:COG1211   125 IPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSED 202
                         170       180
                  ....*....|....*....|
gi 1907089536 160 LWKVTYKQDLCAAEAMIKEK 179
Cdd:COG1211   203 NIKITTPEDLALAEALLRSR 222
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
13-180 1.90e-30

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 116.39  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  13 HKRISLAEAGATRHRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISP 92
Cdd:PRK00155   70 DPKVTVVAGGAERQDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  93 SADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCA 171
Cdd:PRK00155  141 DDGGGIVDTPDRSGLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLAL 217

                  ....*....
gi 1907089536 172 AEAMIKEKI 180
Cdd:PRK00155  218 AEAILKRRI 226
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
13-174 7.99e-26

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: 103.52  E-value: 7.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  13 HKRISLAEAGATRHRSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISP 92
Cdd:TIGR00453  65 RAVPKIVAGGDTRQDSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  93 SADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAA 172
Cdd:TIGR00453 136 EADGFVVETVDREGLWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALA 213

                  ..
gi 1907089536 173 EA 174
Cdd:TIGR00453 214 EA 215
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
12-178 1.62e-22

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: 94.44  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  12 GHKRISLAEAGATRHRSIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTV 89
Cdd:pfam01128  62 GDPSIQLVAGGDTRQDSVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  90 ISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDL 169
Cdd:pfam01128 133 KRVEADGVVAGTPDRSGLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDL 210

                  ....*....
gi 1907089536 170 CAAEAMIKE 178
Cdd:pfam01128 211 ALAEAILTR 219
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
1-176 4.95e-17

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: 81.82  E-value: 4.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   1 MEAMRSIIQRYghKRISLAEAGATRHRSIFNGLKALAEdqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAG 80
Cdd:PRK09382   61 IAYMKKALPEI--KFVTLVTGGATRQESVRNALEALDS----------EYVLIHDAARPFVPKELIDRLIEALDKADCVL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  81 AIRPLVSTVIspsadgHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFdlefgTECLQlALKYCHRKAKLVEGPPAL 160
Cdd:PRK09382  129 PALPVADTLK------RANETVDREGLKLIQTPQLSRTKTLKAAADGRGDF-----TDDSS-AAEAAGGKVALVEGSEDL 196
                         170
                  ....*....|....*.
gi 1907089536 161 WKVTYKQDLCAAEAMI 176
Cdd:PRK09382  197 HKLTYKEDLKMADLLL 212
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
5-183 2.57e-15

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 74.52  E-value: 2.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536   5 RSIIQRY--GHKRISLAEAGATRHRSIFNGLKALAEDQpdckltkpeVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAI 82
Cdd:PRK13385   62 QDLMKQLnvADQRVEVVKGGTERQESVAAGLDRIGNED---------VILVHDGARPFLTQDIIDRLLEGVAKYGAAICA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  83 RPLVSTVISpSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDfDLEFGTECLQLALKYCHrKAKLVEGPPALWK 162
Cdd:PRK13385  133 VEVKDTVKR-VKDKQVIETVDRNELWQGQTPQAFELKILQKAHRLASE-QQFLGTDEASLVERSPH-PVKLVQGSYYNIK 209
                         170       180
                  ....*....|....*....|.
gi 1907089536 163 VTYKQDLCAAEAMIKEKISQE 183
Cdd:PRK13385  210 LTTPEDMPLAKAILQGDIADD 230
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
13-184 3.02e-10

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 60.13  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  13 HKRISLAEAGATRHRSIFNGLKALaedQPDCKLtkpevVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISP 92
Cdd:PLN02728   91 DVPLKFALPGKERQDSVFNGLQEV---DANSEL-----VCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089536  93 SADGHLDHSLDRAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQL--ALKychRKAKLVEGPPALWKVTYKQDLC 170
Cdd:PLN02728  163 NSDSFVVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEV-TDDVSIveALK---HPVFITEGSYTNIKVTTPDDML 238
                         170
                  ....*....|....
gi 1907089536 171 AAEAMIKEKISQEI 184
Cdd:PLN02728  239 VAERILNERSDAEV 252
 
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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