NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907089525|ref|XP_011242209|]
View 

D-ribitol-5-phosphate cytidylyltransferase isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 8.89e-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: 252.44  E-value: 8.89e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516    81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516   154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
ISPD_C super family cl40022
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
 281-414 6.91e-55

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: 181.01  E-value: 6.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 281 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 358
Cdd:pfam18706   1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089525 359 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQD 414
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; ...
 45-271 8.89e-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: 252.44  E-value: 8.89e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516    81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516   154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 48-278 1.80e-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: 194.96  E-value: 1.80e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  48 VLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYG-HKRISLAEAGATRHR 126
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 127 SIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKH 206
Cdd:COG1211    81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089525 207 RASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPALWKVTYKQDLCAAEAMIKEK 278
Cdd:COG1211   153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSEDNIKITTPEDLALAEALLRSR 222
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
 281-414 6.91e-55

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: 181.01  E-value: 6.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 281 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 358
Cdd:pfam18706   1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089525 359 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQD 414
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQD 136
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
45-279 1.22e-49

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 169.54  E-value: 1.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGATR 124
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 125 HRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:PRK00155   83 QDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCAAEAMIKEKI 279
Cdd:PRK00155  154 GLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLALAEAILKRRI 226
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 46-273 2.00e-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: 155.14  E-value: 2.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRygHKRISLAEAGATRH 125
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVA--RAVPKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 126 RSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAK 205
Cdd:TIGR00453  79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089525 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 ...
 47-277 7.58e-38

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: 137.97  E-value: 7.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  47 AVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIqryGHKRISLAEAGATRHR 126
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 127 SIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTVISPSADGHLDHSLDRA 204
Cdd:pfam01128  78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMIKE 277
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 45-271 8.89e-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: 252.44  E-value: 8.89e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516    81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516   154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 48-278 1.80e-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: 194.96  E-value: 1.80e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  48 VLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYG-HKRISLAEAGATRHR 126
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 127 SIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKH 206
Cdd:COG1211    81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089525 207 RASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPALWKVTYKQDLCAAEAMIKEK 278
Cdd:COG1211   153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSEDNIKITTPEDLALAEALLRSR 222
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
 281-414 6.91e-55

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: 181.01  E-value: 6.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 281 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 358
Cdd:pfam18706   1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089525 359 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQD 414
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQD 136
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
45-279 1.22e-49

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 169.54  E-value: 1.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGATR 124
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 125 HRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:PRK00155   83 QDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCAAEAMIKEKI 279
Cdd:PRK00155  154 GLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLALAEAILKRRI 226
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 46-273 2.00e-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: 155.14  E-value: 2.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRygHKRISLAEAGATRH 125
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVA--RAVPKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 126 RSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAK 205
Cdd:TIGR00453  79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089525 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 ...
 47-277 7.58e-38

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: 137.97  E-value: 7.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  47 AVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIqryGHKRISLAEAGATRHR 126
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 127 SIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTVISPSADGHLDHSLDRA 204
Cdd:pfam01128  78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907089525 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMIKE 277
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 44-275 4.01e-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: 126.50  E-value: 4.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  44 TVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYghKRISLAEAGAT 123
Cdd:PRK09382    5 DISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI--KFVTLVTGGAT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 124 RHRSIFNGLKALAEdqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVIspsadgHLDHSLDR 203
Cdd:PRK09382   83 RQESVRNALEALDS----------EYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLK------RANETVDR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089525 204 AKHRASEMPQAFLFDVIYEAYQQCSDFdlefgTECLQlALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMI 275
Cdd:PRK09382  147 EGLKLIQTPQLSRTKTLKAAADGRGDF-----TDDSS-AAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 46-282 1.02e-22

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 96.48  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRY--GHKRISLAEAGAT 123
Cdd:PRK13385    4 ELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLnvADQRVEVVKGGTE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 124 RHRSIFNGLKALAEDQpdckltkpeVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISpSADGHLDHSLDR 203
Cdd:PRK13385   84 RQESVAAGLDRIGNED---------VILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKR-VKDKQVIETVDR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089525 204 AKHRASEMPQAFLFDVIYEAYQQCSDfDLEFGTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAAEAMIKEKISQE 282
Cdd:PRK13385  154 NELWQGQTPQAFELKILQKAHRLASE-QQFLGTDEASLVERSPH-PVKLVQGSYYNIKLTTPEDMPLAKAILQGDIADD 230
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 43-283 4.07e-22

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 95.18  E-value: 4.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  43 GTVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGA 122
Cdd:PLN02728   23 KSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENI-DVPLKFALPGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 123 TRHRSIFNGLKALaedQPDCKLtkpevVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLD 202
Cdd:PLN02728  102 ERQDSVFNGLQEV---DANSEL-----VCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLD 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 203 RAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQL--ALKychRKAKLVEGPPALWKVTYKQDLCAAEAMIKEKIS 280
Cdd:PLN02728  174 RKRLWEMQTPQVIKPELLRRGFELVEREGLEV-TDDVSIveALK---HPVFITEGSYTNIKVTTPDDMLVAERILNERSD 249


                  ...
gi 1907089525 281 QEI 283
Cdd:PLN02728  250 AEV 252
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 46-181 4.07e-06

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: 46.80  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  46 AAVLpAGGCGERMGvrTPKQFCRVLERPLISYTLQAMERVCwiKDIVVtVTGEnmEAMRSIIQRYGHKRISLAEAGATRH 125
Cdd:pfam12804   1 AVIL-AGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAG--DEVVV-VAND--EEVLAALAGLGVPVVPDPDPGQGPL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089525 126 RSIFNGLKALAEDQPdckltkpeVVIIH-DAvrPFVEEDILLRVVLAAKEHGAAGAI 181
Cdd:pfam12804  73 AGLLAALRAAPGADA--------VLVLAcDM--PFLTPELLRRLLAAAEESGADIVV 119
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 45-183 7.35e-06

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: 46.40  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  45 VAAVLPAGGCGERMGvrTPKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTGENMEAMRSIIQRYGHKRISL--AEAG- 121
Cdd:cd04182     1 IAAIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAG-LSRVIV-VLGAEADAVRAALAGLPVVVVINpdWEEGm 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907089525 122 ATrhrSIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGaAGAIRP 183
Cdd:cd04182    77 SS---SLAAGLEALPAD--------ADAVLILLADQPLVTAETLRALIDAFREDG-AGIVAP 126
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 47-193 9.70e-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: 9.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  47 AVLPAGGCGERMG---VRTPKQFCRVLERPLISYTLQAMERVcWIKDIVVtVTGENMEAmrsIIQRYG-----HKRISLA 118
Cdd:cd04181     1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARA-GIDEIIL-VVGYLGEQ---IEEYFGdgskfGVNIEYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525 119 E-------AGAtrhrsIFNGLKALAEDqpdckltkpEVVIIH-DAVrpfVEEDiLLRVVLAAKEHGAAGAIrpLVSTVIS 190
Cdd:cd04181    76 VqeeplgtAGA-----VRNAEDFLGDD---------DFLVVNgDVL---TDLD-LSELLRFHREKGADATI--AVKEVED 135


                  ...
gi 1907089525 191 PSA 193
Cdd:cd04181   136 PSR 138
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 47-95 3.30e-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: 45.14  E-value: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907089525  47 AVLPAGGCGERMG---VRTPKQFCRVLERPLISYTLQAMERvCWIKDIVVTV 95
Cdd:COG1208     2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINV 52
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 51-115 6.82e-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: 6.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907089525  51 AGGCGERMGvRTPKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTGENMEAMRSIIQRYGHKRI 115
Cdd:COG2266     2 AGGKGTRLG-GGEKPLLEICGKPMIDRVIDALEESC-IDKIYV-AVSPNTPKTREYLKERGVEVI 63
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
47-97 8.25e-04

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 40.99  E-value: 8.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907089525  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 ...
 47-120 4.08e-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: 38.70  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089525  47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMeRVCWIKDIVVtVTGENMEAMRSII---QRYG--------H 112
Cdd:cd04189     3 GLILAGGKGTRLRPLTytrPKQLIPVAGKPIIQYAIEDL-REAGIEDIGI-VVGPTGEEIKEALgdgSRFGvrityilqE 80


                  ....*...
gi 1907089525 113 KRISLAEA 120
Cdd:cd04189    81 EPLGLAHA 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH