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Conserved domains on  [gi|1141152231|ref|WP_076918330|]
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MULTISPECIES: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [unclassified Pseudoalteromonas]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10011283)

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP

EC:  2.7.7.60
Gene Ontology:  GO:0050518|GO:0019288
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
7-229 5.52e-107

D-ribitol-5-phosphate cytidylyltransferase;


:

Pssm-ID: 234670  Cd Length: 227  Bit Score: 307.45  E-value: 5.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLTLA-DPRIVRAIGGKERA 84
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAkDPKVTVVAGGAERQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  85 DSVLNSLLflAANPPAWVLVHDAARPLVDIADIERLIAQCmQADEGGILASKVKDTIKR--GQSHAQQTVPRDDLWQALT 162
Cdd:PRK00155   84 DSVLNGLQ--ALPDDDWVLVHDAARPFLTPDDIDRLIEAA-EETGAAILAVPVKDTIKRsdDGGGIVDTPDRSGLWAAQT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1141152231 163 PQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQKQNN 229
Cdd:PRK00155  161 PQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
7-229 5.52e-107

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 307.45  E-value: 5.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLTLA-DPRIVRAIGGKERA 84
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAkDPKVTVVAGGAERQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  85 DSVLNSLLflAANPPAWVLVHDAARPLVDIADIERLIAQCmQADEGGILASKVKDTIKR--GQSHAQQTVPRDDLWQALT 162
Cdd:PRK00155   84 DSVLNGLQ--ALPDDDWVLVHDAARPFLTPDDIDRLIEAA-EETGAAILAVPVKDTIKRsdDGGGIVDTPDRSGLWAAQT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1141152231 163 PQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQKQNN 229
Cdd:PRK00155  161 PQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 10-227 8.37e-100

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: 289.34  E-value: 8.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  10 IVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLT---LADPRIVRAIGGKERAD 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELLakyGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  86 SVLNSLLFLAAnPPAWVLVHDAARPLVDIADIERLIAQCMQADeGGILASKVKDTIKR--GQSHAQQTVPRDDLWQALTP 163
Cdd:COG1211    81 SVRNGLEALPD-DDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRvdDDGRVTETVDRSGLWAAQTP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141152231 164 QLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQKQ 227
Cdd:COG1211   159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSR 222
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 7-220 2.45e-90

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: 265.16  E-value: 2.45e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLTL--ADPRIVRAIGGKER 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDiDLAKELAKygLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  84 ADSVLNSLLFLAANPPAWVLVHDAARPLVDIADIERLIAQCMQADeGGILASKVKDTIKR--GQSHAQQTVPRDDLWQAL 161
Cdd:cd02516    81 QDSVLNGLKALPDADPDIVLIHDAARPFVSPELIDRLIDALKEYG-AAIPAVPVTDTIKRvdDDGVVVETLDREKLWAAQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1141152231 162 TPQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLA 220
Cdd:cd02516   160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 8-224 1.72e-78

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: 234.87  E-value: 1.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   8 AAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETDPYFDDLTLADPR-IVRAIGGKERADS 86
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAvPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  87 VLNSLLFLAANPpaWVLVHDAARPLVDIADIERLIAQcMQADEGGILASKVKDTIKRGQSHAQ--QTVPRDDLWQALTPQ 164
Cdd:TIGR00453  81 VRNGLKALKDAE--FVLVHDAARPFVPKELLDRLLEA-LRKAGAAILALPVADTLKRVEADGFvvETVDREGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231 165 LFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLL 224
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 9-224 1.19e-72

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: 220.40  E-value: 1.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   9 AIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLtLADPRIVRAIGGKERADSV 87
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQL-LGDPSIQLVAGGDTRQDSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  88 LNSLLFLAANPpAWVLVHDAARPLVDIADIERLIAQCMQADEGGILASKVKDTIKRGQSHAQ--QTVPRDDLWQALTPQL 165
Cdd:pfam01128  80 LNGLKALAGTA-KFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVvaGTPDRSGLWAAQTPQG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1141152231 166 FKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLL 224
Cdd:pfam01128 159 FRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
7-229 5.52e-107

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 307.45  E-value: 5.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLTLA-DPRIVRAIGGKERA 84
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAkDPKVTVVAGGAERQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  85 DSVLNSLLflAANPPAWVLVHDAARPLVDIADIERLIAQCmQADEGGILASKVKDTIKR--GQSHAQQTVPRDDLWQALT 162
Cdd:PRK00155   84 DSVLNGLQ--ALPDDDWVLVHDAARPFLTPDDIDRLIEAA-EETGAAILAVPVKDTIKRsdDGGGIVDTPDRSGLWAAQT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1141152231 163 PQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQKQNN 229
Cdd:PRK00155  161 PQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 10-227 8.37e-100

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: 289.34  E-value: 8.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  10 IVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLT---LADPRIVRAIGGKERAD 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELLakyGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  86 SVLNSLLFLAAnPPAWVLVHDAARPLVDIADIERLIAQCMQADeGGILASKVKDTIKR--GQSHAQQTVPRDDLWQALTP 163
Cdd:COG1211    81 SVRNGLEALPD-DDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRvdDDGRVTETVDRSGLWAAQTP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141152231 164 QLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQKQ 227
Cdd:COG1211   159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSR 222
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 7-220 2.45e-90

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: 265.16  E-value: 2.45e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLTL--ADPRIVRAIGGKER 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDiDLAKELAKygLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  84 ADSVLNSLLFLAANPPAWVLVHDAARPLVDIADIERLIAQCMQADeGGILASKVKDTIKR--GQSHAQQTVPRDDLWQAL 161
Cdd:cd02516    81 QDSVLNGLKALPDADPDIVLIHDAARPFVSPELIDRLIDALKEYG-AAIPAVPVTDTIKRvdDDGVVVETLDREKLWAAQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1141152231 162 TPQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLA 220
Cdd:cd02516   160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 8-224 1.72e-78

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: 234.87  E-value: 1.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   8 AAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETDPYFDDLTLADPR-IVRAIGGKERADS 86
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAvPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  87 VLNSLLFLAANPpaWVLVHDAARPLVDIADIERLIAQcMQADEGGILASKVKDTIKRGQSHAQ--QTVPRDDLWQALTPQ 164
Cdd:TIGR00453  81 VRNGLKALKDAE--FVLVHDAARPFVPKELLDRLLEA-LRKAGAAILALPVADTLKRVEADGFvvETVDREGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231 165 LFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLL 224
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 9-224 1.19e-72

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: 220.40  E-value: 1.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   9 AIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLtLADPRIVRAIGGKERADSV 87
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQL-LGDPSIQLVAGGDTRQDSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  88 LNSLLFLAANPpAWVLVHDAARPLVDIADIERLIAQCMQADEGGILASKVKDTIKRGQSHAQ--QTVPRDDLWQALTPQL 165
Cdd:pfam01128  80 LNGLKALAGTA-KFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVvaGTPDRSGLWAAQTPQG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1141152231 166 FKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLL 224
Cdd:pfam01128 159 FRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 6-224 1.62e-51

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: 171.18  E-value: 1.62e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   6 TIAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETD-PYFDDLTLADPRIVRAIGGKERA 84
Cdd:PRK09382    5 DISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDiAYMKKALPEIKFVTLVTGGATRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  85 DSVLNSLLFLAAnppAWVLVHDAARPLVDIADIERLIAQCMQADegGIL-ASKVKDTIKRGQShaqqTVPRDDLWQALTP 163
Cdd:PRK09382   85 ESVRNALEALDS---EYVLIHDAARPFVPKELIDRLIEALDKAD--CVLpALPVADTLKRANE----TVDREGLKLIQTP 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1141152231 164 QLFKYDelktALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLL 224
Cdd:PRK09382  156 QLSRTK----TLKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 3-232 5.75e-48

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 158.36  E-value: 5.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   3 NKQTIAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALsetDPYFDDLTLA-----DPRIVRA 77
Cdd:PLN02728   21 KEKSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVC---DPSYRDVFEEaveniDVPLKFA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  78 IGGKERADSVLNSLLFLAANPpAWVLVHDAARPLVDIADIERLIAQCmQADEGGILASKVKDTIKR--GQSHAQQTVPRD 155
Cdd:PLN02728   98 LPGKERQDSVFNGLQEVDANS-ELVCIHDSARPLVTSADIEKVLKDA-AVHGAAVLGVPVKATIKEanSDSFVVKTLDRK 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1141152231 156 DLWQALTPQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQKQNNESA 232
Cdd:PLN02728  176 RLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERSDAEV 252
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 8-225 1.04e-38

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 133.84  E-value: 1.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   8 AAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVA-----LSETDPYFDDLTLADPRIVRAIGGKE 82
Cdd:PRK13385    4 ELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQRVEVVKGGTE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231  83 RADSVLNSLLflAANPPAWVLVHDAARPLVDIADIERLIAQCMQaDEGGILASKVKDTIKRGQSH-AQQTVPRDDLWQAL 161
Cdd:PRK13385   84 RQESVAAGLD--RIGNEDVILVHDGARPFLTQDIIDRLLEGVAK-YGAAICAVEVKDTVKRVKDKqVIETVDRNELWQGQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141152231 162 TPQLFKYDELKTALQSALNSGATITDEASAMEWANKPVKLVAGRSDNIKITTPEDLDLAGFLLQ 225
Cdd:PRK13385  161 TPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ 224
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 7-144 1.41e-11

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: 61.04  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQHttPKQYISLAGKTILEHTLAKLSQLPqLNSIVVALSETDpyfDDLTLADPRIVRAIGGKERA-- 84
Cdd:cd04182     1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAG-LSRVIVVLGAEA---DAVRAALAGLPVVVVINPDWee 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1141152231  85 ---DSVLNSLLFLAANPPAWVLVHdAARPLVDIADIERLIAqCMQADEGGILASKVKDtiKRG 144
Cdd:cd04182    75 gmsSSLAAGLEALPADADAVLILL-ADQPLVTAETLRALID-AFREDGAGIVAPVYQG--RRG 133
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
7-144 1.90e-09

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 55.55  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   7 IAAIVPAAGVGSRMQhtTPKQYISLAGKTILEHTLAKLSQLPqLNSIVVAL-SETDPYFDDLTLADPRIV---RAIGGKe 82
Cdd:COG2068     4 VAAIILAAGASSRMG--RPKLLLPLGGKPLLERAVEAALAAG-LDPVVVVLgADAEEVAAALAGLGVRVVvnpDWEEGM- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1141152231  83 rADSVLNSLLFLAANPPAWVLVH-DaaRPLVDIADIERLIAQCmQADEGGILASKVKDtiKRG 144
Cdd:COG2068    80 -SSSLRAGLAALPADADAVLVLLgD--QPLVTAETLRRLLAAF-RESPASIVAPTYDG--RRG 136
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 8-144 9.65e-08

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 50.42  E-value: 9.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   8 AAIVPAAGVGSRMQhtTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVALSETDPYFDDltLADPRIVRAIGGKERADSV 87
Cdd:TIGR03310   1 DAIILAAGLSSRMG--QNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVAL--LANHSNITLVHNPQYAEGQ 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1141152231  88 LNSLLFLAANPPAW--VLVHDAARPLVDIADIERLIAqCMQADEGGILASKVKDtiKRG 144
Cdd:TIGR03310  77 SSSIKLGLELPVQSdgYLFLLGDQPFVTPDIIQLLLE-AFALKNDEIVVPLYKG--KRG 132
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 9-135 1.54e-07

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: 49.50  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   9 AIVPAAGVGSRMQhtTPKQYISLAGKTILEHTLAKLSqlPQLNSIVVAlSETDPYFDDLTLADPRIVR-AIGGKERADSV 87
Cdd:pfam12804   1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLR--PAGDEVVVV-ANDEEVLAALAGLGVPVVPdPDPGQGPLAGL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1141152231  88 LNSLLFLAANPPAWVLVHDAarPLVDIADIERLIAQCMQADEGGILAS 135
Cdd:pfam12804  76 LAALRAAPGADAVLVLACDM--PFLTPELLRRLLAAAEESGADIVVPV 121
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 9-55 3.47e-07

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: 49.54  E-value: 3.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1141152231   9 AIVPAAGVGSRMQH---TTPKQYISLAGKTILEHTLAKLSQLpQLNSIVV 55
Cdd:cd02523     1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVI 49
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 9-47 1.65e-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: 47.19  E-value: 1.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1141152231   9 AIVPAAGVGSRMQ---HTTPKQYISLAGKTILEHTLAKLSQL 47
Cdd:cd04181     1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARA 42
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 9-46 3.03e-06

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: 46.68  E-value: 3.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1141152231   9 AIVPAAGVGSRMQ---HTTPKQYISLAGKTILEHTLAKLSQ 46
Cdd:COG1208     2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAA 42
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
9-44 6.95e-06

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 45.62  E-value: 6.95e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1141152231   9 AIVPAAGVGSRMQHTT---PKQYISLAGKTILEHTLAKL 44
Cdd:COG1213     2 AVILAAGRGSRLGPLTddiPKCLVEIGGKTLLERQLEAL 40
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 9-44 9.97e-06

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: 45.25  E-value: 9.97e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1141152231   9 AIVPAAGVGSRMQ---HTTPKQYISLAGKTILEHTLAKL 44
Cdd:cd04189     3 GLILAGGKGTRLRpltYTRPKQLIPVAGKPIIQYAIEDL 41
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-55 1.82e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 44.93  E-value: 1.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1141152231   8 AAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVV 55
Cdd:PRK14352    6 AVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVV 53
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
9-44 3.91e-05

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 43.54  E-value: 3.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1141152231   9 AIVPAAGVGSRMQ---HTTPKQYISLAGKTILEHTLAKL 44
Cdd:COG1209     3 GIILAGGSGTRLRpltLTVSKQLLPVYDKPMIYYPLSTL 41
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 9-55 6.29e-05

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 42.56  E-value: 6.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1141152231   9 AIVPAAGVGSRMQ---HTTPKQYISLAGKTILEHTLAKLSQLPqLNSIVV 55
Cdd:cd06422     2 AMILAAGLGTRMRpltDTRPKPLVPVAGKPLIDHALDRLAAAG-IRRIVV 50
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-56 1.65e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.16  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1141152231   1 MTNKqTIAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVA 56
Cdd:PRK14353    1 MTDR-TCLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV 55
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-55 1.74e-04

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 41.94  E-value: 1.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1141152231   5 QTIAAIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLpQLNSIVV 55
Cdd:COG1207     1 SPLAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVV 50
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 7-67 1.96e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 40.64  E-value: 1.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1141152231   7 IAAIVPAAGVGSRMQhtTPKQYISLAGKTILEHTLAKLSqlPQLNSIVVALSETDPYFDDL 67
Cdd:cd02503     1 ITGVILAGGKSRRMG--GDKALLELGGKPLLEHVLERLK--PLVDEVVISANRDQERYALL 57
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 9-56 3.12e-04

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 40.58  E-value: 3.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1141152231   9 AIVPAAGVGSRMQHTTPKQYISLAGKTILEHTLAKLSQLPQLNSIVVA 56
Cdd:cd02540     1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVV 48
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-123 8.97e-04

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.02  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141152231   1 MTNKqtIAAIVPAAGVGSRMQhtTPKQYISLAGKTILEHTLAKLSqlPQLNSIVVALSETDPY--FDDLTLADPRIVR-A 77
Cdd:COG0746     1 MTMP--ITGVILAGGRSRRMG--QDKALLPLGGRPLLERVLERLR--PQVDEVVIVANRPERYaaLGVPVVPDDPPGAgP 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1141152231  78 IGGkeradsvLNSLLFLAANPpaWVLVH--DAarPLVDIADIERLIAQ 123
Cdd:COG0746    75 LAG-------ILAALEAAPAE--WVLVLacDM--PFLPPDLVRRLLEA 111
 
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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