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Conserved domains on  [gi|15224925|ref|NP_181401|]
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phosphorylethanolamine cytidylyltransferase 1 [Arabidopsis thaliana]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 11476749)

nicotinate-nucleotide adenylyltransferase catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 1-421 0e+00

ethanolamine-phosphate cytidylyltransferase


:

Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 756.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925    1 MVWEKEKIVGSCIVGGAAfaVGASFLHLFLKGELPLGlglglSCPWRIL------RKRKPVRVYMDGCFDMMHYGHCNAL 74
Cdd:PLN02406   1 MSISSAKYVASCLIGGLM--LGASVLGLSLAGFGSSL-----PYAWPDLgifkkkKKKKPVRVYMDGCFDMMHYGHANAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   75 RQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITEDFMKKLFDEYQIDYIIHGDDPCV 154
Cdd:PLN02406  74 RQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMNKLFNEYNIDYIIHGDDPCL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  155 LPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDTHSRSSLQRQFSHGHSSPkfEDGASSAGTRVSHF 234
Cdd:PLN02406 154 LPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDSHNHSSLQRQFSHGHSQF--EDGGSGSGTRVSHF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  235 LPTSRRIVQFSNGKGPGPDARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERSLSV 314
Cdd:PLN02406 232 LPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSV 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  315 LACRYVDEVIIGAPWEVSRDTITTFDISLVVHGTVAESDDFRKEEDNPYSVPISMGIFQVLDSPLDITTSTIIRRIVANH 394
Cdd:PLN02406 312 LACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTVAENNDFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANH 391

                        410       420
                 ....*....|....*....|....*..
gi 15224925  395 EAYQKRNAKKEASEKKYYEQKSFVSGD 421
Cdd:PLN02406 392 EAYQKRNEKKAESEKRYYESKSFVSGD 418
 
Name Accession Description Interval E-value
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 1-421 0e+00

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 756.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925    1 MVWEKEKIVGSCIVGGAAfaVGASFLHLFLKGELPLGlglglSCPWRIL------RKRKPVRVYMDGCFDMMHYGHCNAL 74
Cdd:PLN02406   1 MSISSAKYVASCLIGGLM--LGASVLGLSLAGFGSSL-----PYAWPDLgifkkkKKKKPVRVYMDGCFDMMHYGHANAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   75 RQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITEDFMKKLFDEYQIDYIIHGDDPCV 154
Cdd:PLN02406  74 RQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMNKLFNEYNIDYIIHGDDPCL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  155 LPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDTHSRSSLQRQFSHGHSSPkfEDGASSAGTRVSHF 234
Cdd:PLN02406 154 LPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDSHNHSSLQRQFSHGHSQF--EDGGSGSGTRVSHF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  235 LPTSRRIVQFSNGKGPGPDARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERSLSV 314
Cdd:PLN02406 232 LPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSV 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  315 LACRYVDEVIIGAPWEVSRDTITTFDISLVVHGTVAESDDFRKEEDNPYSVPISMGIFQVLDSPLDITTSTIIRRIVANH 394
Cdd:PLN02406 312 LACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTVAENNDFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANH 391

                        410       420
                 ....*....|....*....|....*..
gi 15224925  395 EAYQKRNAKKEASEKKYYEQKSFVSGD 421
Cdd:PLN02406 392 EAYQKRNEKKAESEKRYYESKSFVSGD 418
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 253-405 1.19e-86

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 260.27  E-value: 1.19e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925 253 DARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVS 332
Cdd:cd02173   1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVIT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224925 333 RDTITTFDISLVVHGTVAESDDFRKEEDnPYSVPISMGIFQVLDSPLDITTSTIIRRIVANHEAYQKRNAKKE 405
Cdd:cd02173  81 KELIEHFKIDVVVHGKTEETPDSLDGED-PYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 55-189 5.04e-33

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 120.59  E-value: 5.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  55 VRVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDapyaiTEDFM 134
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILG-----EEWDK 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15224925 135 KKLFDEYQIDYIIHGDDPCVLPDGT-DAYALAKKAGRYKQIKRTEGVSSTDIVGRM 189
Cdd:COG0615  76 FEDIEEIKPDVIVLGDDWKGDFDFLkEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 58-188 1.13e-25

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 101.24  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925    58 YMDGCFDMMHYGHCNALRQARALGDQ-LVVGVVSDEEiIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITEDFMKk 136
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15224925   137 lfdEYQIDYIIHGDDPCV--LPDGTDAYALAKKAGR-----YKQIKRTEGVSSTDIVGR 188
Cdd:pfam01467  79 ---ELNPDVLVIGADSLLdfWYELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 56-121 1.30e-19

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 81.97  E-value: 1.30e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224925    56 RVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEV 121
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 1-421 0e+00

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 756.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925    1 MVWEKEKIVGSCIVGGAAfaVGASFLHLFLKGELPLGlglglSCPWRIL------RKRKPVRVYMDGCFDMMHYGHCNAL 74
Cdd:PLN02406   1 MSISSAKYVASCLIGGLM--LGASVLGLSLAGFGSSL-----PYAWPDLgifkkkKKKKPVRVYMDGCFDMMHYGHANAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   75 RQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITEDFMKKLFDEYQIDYIIHGDDPCV 154
Cdd:PLN02406  74 RQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMNKLFNEYNIDYIIHGDDPCL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  155 LPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDTHSRSSLQRQFSHGHSSPkfEDGASSAGTRVSHF 234
Cdd:PLN02406 154 LPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDSHNHSSLQRQFSHGHSQF--EDGGSGSGTRVSHF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  235 LPTSRRIVQFSNGKGPGPDARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERSLSV 314
Cdd:PLN02406 232 LPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSV 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  315 LACRYVDEVIIGAPWEVSRDTITTFDISLVVHGTVAESDDFRKEEDNPYSVPISMGIFQVLDSPLDITTSTIIRRIVANH 394
Cdd:PLN02406 312 LACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTVAENNDFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANH 391

                        410       420
                 ....*....|....*....|....*..
gi 15224925  395 EAYQKRNAKKEASEKKYYEQKSFVSGD 421
Cdd:PLN02406 392 EAYQKRNEKKAESEKRYYESKSFVSGD 418
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 51-415 3.11e-159

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 452.70  E-value: 3.11e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   51 KRKP--VRVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYA 128
Cdd:PTZ00308   6 PKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  129 ITEDFMKKLfdeyQIDYIIHGDDPCVLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRersisdTHSRSSLq 208
Cdd:PTZ00308  86 TRLEDLERL----ECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTK------SHLLKSV- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  209 rqfshghsSPKFEDGASSAGTRVSHFLPTSRRIVQFSNGKGPGPDARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGI 288
Cdd:PTZ00308 155 --------DEVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  289 HNDQTVSAKRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSRDTITTFDISLVVHGTvaeSDDFRKEED--NPYSVP 366
Cdd:PTZ00308 227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGK---FSDLVNEEGgsDPYEVP 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 15224925  367 ISMGIFQVLDSPLDITTSTIIRRIVANHEAYQKRNAKKEASEKKYYEQK 415
Cdd:PTZ00308 304 KAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEIK 352
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 253-405 1.19e-86

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 260.27  E-value: 1.19e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925 253 DARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVS 332
Cdd:cd02173   1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVIT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224925 333 RDTITTFDISLVVHGTVAESDDFRKEEDnPYSVPISMGIFQVLDSPLDITTSTIIRRIVANHEAYQKRNAKKE 405
Cdd:cd02173  81 KELIEHFKIDVVVHGKTEETPDSLDGED-PYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 53-204 3.75e-82

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 248.64  E-value: 3.75e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  53 KPVRVYMDGCFDMMHYGHCNALRQARALG--DQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAIT 130
Cdd:cd02174   1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224925 131 EDFMKKlfdeYQIDYIIHGDDPCVLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDTHSR 204
Cdd:cd02174  81 PEFLDK----YKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 57-190 7.43e-37

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 131.61  E-value: 7.43e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  57 VYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGP--PVTPLHERMTMVKAVKWVDEVISDAPYAITEDFM 134
Cdd:cd02173   5 VYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSnyPIMNLHERVLSVLACRYVDEVVIGAPYVITKELI 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15224925 135 KKLfdeyQIDYIIHGDDP--CVLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRML 190
Cdd:cd02173  85 EHF----KIDVVVHGKTEetPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRII 138
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 53-207 4.24e-34

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 128.91  E-value: 4.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   53 KPVRVYMDGCFDMMHYGHCNALRQARAL--GDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAIT 130
Cdd:PLN02413  26 RPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWVIT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  131 EDFMkklfDEYQIDYIIHGDDPCVLPDGT--DAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRE---RSISDTHSRS 205
Cdd:PLN02413 106 QEFL----DKHRIDYVAHDALPYADASGAgkDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQyvmRNLARGYSRK 181


                 ..
gi 15224925  206 SL 207
Cdd:PLN02413 182 DL 183
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 54-190 9.91e-34

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 122.78  E-value: 9.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  54 PVRVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYaiteDF 133
Cdd:cd02170   1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPW----SY 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15224925 134 MKKLFDEYQiDYIIHGDDPCVLPDGTDAYALAKKAGRYKQI--KRTEGVSSTDIVGRML 190
Cdd:cd02170  77 FKPLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 55-189 5.04e-33

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 120.59  E-value: 5.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  55 VRVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDapyaiTEDFM 134
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILG-----EEWDK 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15224925 135 KKLFDEYQIDYIIHGDDPCVLPDGT-DAYALAKKAGRYKQIKRTEGVSSTDIVGRM 189
Cdd:COG0615  76 FEDIEEIKPDVIVLGDDWKGDFDFLkEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 257-404 2.71e-32

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 119.59  E-value: 2.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925 257 IYIDGAFDLFHAGHVEILRRARELG--DFLLVGIHNDQTVSAKRGahRPIMNLHERSLSVLACRYVDEVIIGAPWEVSRD 334
Cdd:cd02174   5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224925 335 TITTFDISLVVHGtvaesDD--FRKEEDNPYSVPISMGIFQVLDSPLDITTSTIIRRIVANHEAYQKRNAKK 404
Cdd:cd02174  83 FLDKYKCDYVAHG-----DDiyLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQR 149
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 58-188 1.13e-25

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 101.24  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925    58 YMDGCFDMMHYGHCNALRQARALGDQ-LVVGVVSDEEiIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITEDFMKk 136
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15224925   137 lfdEYQIDYIIHGDDPCV--LPDGTDAYALAKKAGR-----YKQIKRTEGVSSTDIVGR 188
Cdd:pfam01467  79 ---ELNPDVLVIGADSLLdfWYELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 255-390 3.41e-25

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 99.79  E-value: 3.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925 255 RIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRgaHRPIMNLHERSLSVLACRYVDEVIIGAPWEVsRD 334
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKG--RKPIIPEEQRKEIVEALKYVDEVILGEEWDK-FE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15224925 335 TITTFDISLVVHGtvaeSD---DFRKEEDNPYSVPISMGIFqVLDSPLDITTSTIIRRI 390
Cdd:COG0615  78 DIEEIKPDVIVLG----DDwkgDFDFLKEELEKRGIGCEVV-YLPRTEGISSTKIKKRI 131
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 257-390 2.40e-21

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 89.27  E-value: 2.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925 257 IYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGahRPIMNLHERSLSVLACRYVDEVIIGAPWEVsRDTI 336
Cdd:cd02170   4 VYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWSY-FKPL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15224925 337 TTFDISLVVHGTVAESDDFRKEEdnpYSVPISMGIFQVL---DSPLdITTSTIIRRI 390
Cdd:cd02170  81 EELKPDVIVLGDDQKNGVDEEEV---YEELKKRGKVIEVprkKTEG-ISSSDIIKRI 133
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 245-409 9.64e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 91.93  E-value: 9.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  245 SNGKGPGPDARII--YIDGAFDLFHAGHVEILRRAREL--GDFLLVGIHNDQTVSAKRGahRPIMNLHERSLSVLACRYV 320
Cdd:PLN02413  16 SATPSSSPSDRPVrvYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKG--KTVMTEDERYESLRHCKWV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  321 DEVIIGAPWEVSRDTITTFDISLVVHGTVAESDDFRKEEDnPYSVPISMGIFQVLDSPLDITTSTIIRRIVANHEAYQKR 400
Cdd:PLN02413  94 DEVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGKD-VYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                 ....*....
gi 15224925  401 NAKKEASEK 409
Cdd:PLN02413 173 NLARGYSRK 181
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 56-121 1.30e-19

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 81.97  E-value: 1.30e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224925    56 RVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEV 121
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 258-390 3.30e-18

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 80.44  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   258 YIDGAFDLFHAGHVEILRRARELGD-FLLVGIHNDQTVSAKrgaHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSRDTI 336
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDeDLIVGVPSDEPPHKL---KRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15224925   337 TTFDISLVVHGTVAESDDFRKEEDNPYSVPISMGIFQVLDSPLDIT---TSTIIRRI 390
Cdd:pfam01467  78 KELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTngiSSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 256-323 9.72e-18

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 76.96  E-value: 9.72e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224925   256 IIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGahRPIMNLHERSLSVLACRYVDEV 323
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 255-325 2.89e-15

rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in E. coli, and separate proteins in some other genome. Domain I (TIGR02198) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131254 [Multi-domain]  Cd Length: 144  Bit Score: 72.34  E-value: 2.89e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224925   255 RIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERS--LSVLACryVDEVII 325
Cdd:TIGR02199  12 KIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 56-189 6.22e-15

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 76.41  E-value: 6.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   56 RVYM-DGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGP--PVTPLHERMTMVKAVKWVDEVIS---DAPY-- 127
Cdd:PRK11316 341 KIVMtNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPVNPLEQRMAVLAALEAVDWVVPfeeDTPQrl 420

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224925  128 --AITEDFMKKLFDeYQIDYIIHGDdpCVLPDGtdayalakkaGRYKQIKRTEGVSSTDIVGRM 189
Cdd:PRK11316 421 iaEILPDLLVKGGD-YKPEEIAGSK--EVWANG----------GEVKVLNFEDGCSTTNIIKKI 471
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 254-359 8.18e-15

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 70.59  E-value: 8.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925 254 ARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKrgAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSR 333
Cdd:cd02171   1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGK--GKKAVIPYEQRAEILESIRYVDLVIPETNWEQKI 78

                        90       100
                ....*....|....*....|....*..
gi 15224925 334 DTITTFDISLVVHGTVAESD-DFRKEE 359
Cdd:cd02171  79 EDIKKYNVDVFVMGDDWEGKfDFLKEY 105
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 53-185 3.20e-13

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 66.35  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  53 KPVRVYmdGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITED 132
Cdd:cd02171   2 KVVITY--GTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIE 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15224925 133 FMKKlfdeYQIDYIIHGDdpcvlpDGTDAYALAKKAGRYKQIKRTEGVSSTDI 185
Cdd:cd02171  80 DIKK----YNVDVFVMGD------DWEGKFDFLKEYCEVVYLPRTKGISSTQL 122
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 53-151 4.86e-13

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 66.29  E-value: 4.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  53 KPVrVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEV-ISDAPYAITe 131
Cdd:cd02172   4 KTV-VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVvLFDNPTALE- 81

                        90       100
                ....*....|....*....|....*..
gi 15224925 132 dfmkkLFDEYQ-------IDYIIHGDD 151
Cdd:cd02172  82 -----IIDALQpniyvkgGDYENPEND 103
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 255-325 2.25e-12

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 64.36  E-value: 2.25e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224925 255 RIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVsaKRGAHRPIMNLHERSLSVLACRYVDEVII 325
Cdd:cd02172   5 TVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYV--NKGPGRPIFPEDLRAEVLAALGFVDYVVL 73
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 255-324 1.83e-11

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 65.62  E-value: 1.83e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224925  255 RIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERS--LSVLACryVDEVI 324
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMavLAALEA--VDWVV 410
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
61-147 1.58e-09

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 56.38  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   61 GCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKavKWVDEVISDAPYAItedfmKKLFDE 140
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYEI-----VKIDDP 80

                         90
                 ....*....|...
gi 15224925  141 Y------QIDYII 147
Cdd:PRK00777  81 YgpaledDFDAIV 93
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
261-345 3.14e-08

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 52.53  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  261 GAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRgaHRPIMNLHERSLSVLacRYVDEVIIGAPWEVSR------D 334
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYK--KHKVRPYEVRLKNLK--KFLKAVEYDREYEIVKiddpygP 83

                         90
                 ....*....|..
gi 15224925  335 TITT-FDIsLVV 345
Cdd:PRK00777  84 ALEDdFDA-IVV 94
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 61-153 9.73e-06

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 45.12  E-value: 9.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925  61 GCFDMMHYGHCNALRQARALG-DQLVVGVVSDEEIIANKGPPvTPLHERMTMVKA--------VKWVDEVISDAPyaiTE 131
Cdd:cd02039   6 GRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKRNKDP-FSLHERVEMLKEilkdrlkvVPVDFPEVKILL---AV 81

                        90       100
                ....*....|....*....|..
gi 15224925 132 DFMKKLFDEYQIDYIIHGDDPC 153
Cdd:cd02039  82 VFILKILLKVGPDKVVVGEDFA 103
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
56-152 5.34e-05

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 44.81  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224925   56 RVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVtPLHERmtmvkavkwvdevisdapYAITEDFMK 135
Cdd:PRK01170   2 ITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPI-PYEDR------------------KRKLENFIK 62

                         90
                 ....*....|....*..
gi 15224925  136 KLFDEYQIDYIihgDDP 152
Cdd:PRK01170  63 KFTNKFRIRPI---DDR 76
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
256-304 1.57e-03

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 40.19  E-value: 1.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 15224925  256 IIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVsaKRGAHRPI 304
Cdd:PRK01170   2 ITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYV--RKNKVYPI 48
 
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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