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Conserved domains on  [gi|374253757|ref|NP_001243362|]
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ethanolamine-phosphate cytidylyltransferase isoform 5 [Homo sapiens]

Protein Classification

ethanolamine-phosphate cytidylyltransferase( domain architecture ID 1005722)

ethanolamine-phosphate cytidylyltransferase catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00308 super family cl31425
ethanolamine-phosphate cytidylyltransferase; Provisional
 14-318 4.69e-123

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 357.56  E-value: 4.69e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  14 QPGpggrrAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD---------------------------------- 59
Cdd:PTZ00308   8 KPG-----TIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDeeimrnkgppvmhqeeryealrackwvdevvegy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  60 --------------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSE 115
Cdd:PTZ00308  83 pyttrledlerlecdfvvhgDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 116 YREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGL 195
Cdd:PTZ00308 163 LFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 196 HFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRR 274
Cdd:PTZ00308 227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAM 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 374253757 275 GIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 318
Cdd:PTZ00308 307 GIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 14-318 4.69e-123

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 357.56  E-value: 4.69e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  14 QPGpggrrAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD---------------------------------- 59
Cdd:PTZ00308   8 KPG-----TIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDeeimrnkgppvmhqeeryealrackwvdevvegy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  60 --------------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSE 115
Cdd:PTZ00308  83 pyttrledlerlecdfvvhgDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 116 YREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGL 195
Cdd:PTZ00308 163 LFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 196 HFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRR 274
Cdd:PTZ00308 227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAM 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 374253757 275 GIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 318
Cdd:PTZ00308 307 GIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 158-310 2.15e-95

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: 279.53  E-value: 2.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 158 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 237
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253757 238 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 310
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 161-230 4.50e-15

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: 68.87  E-value: 4.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  161 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 230
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 160-233 3.42e-13

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: 65.51  E-value: 3.42e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253757 160 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 233
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 163-254 1.17e-12

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: 64.26  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  163 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 242
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 374253757  243 LSHFKVDLVCHG 254
Cdd:pfam01467  77 LKELNPDVLVIG 88
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 14-318 4.69e-123

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 357.56  E-value: 4.69e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  14 QPGpggrrAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD---------------------------------- 59
Cdd:PTZ00308   8 KPG-----TIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDeeimrnkgppvmhqeeryealrackwvdevvegy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  60 --------------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSE 115
Cdd:PTZ00308  83 pyttrledlerlecdfvvhgDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 116 YREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGL 195
Cdd:PTZ00308 163 LFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 196 HFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRR 274
Cdd:PTZ00308 227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAM 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 374253757 275 GIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 318
Cdd:PTZ00308 307 GIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 158-310 2.15e-95

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: 279.53  E-value: 2.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 158 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 237
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253757 238 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 310
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 20-313 5.56e-93

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 283.11  E-value: 5.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  20 RRAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDDDIT------------------------------------ 63
Cdd:PLN02406  51 KKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIankgppvtpmhermimvsgvkwvdevipdapyaite 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  64 ----------------------LTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAH--HSSQEMSSEYREY 119
Cdd:PLN02406 131 efmnklfneynidyiihgddpcLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsiSDSHNHSSLQRQF 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 120 ADSFGKCPG-GRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFD 198
Cdd:PLN02406 211 SHGHSQFEDgGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLLVGIHTD 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 199 QEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGK-TEIIPDRDG-SDPYQEPKRRGI 276
Cdd:PLN02406 289 QTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGeDDPYAVPKSMGI 368

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 374253757 277 FRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKE 313
Cdd:PLN02406 369 FQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 21-109 8.55e-44

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: 147.71  E-value: 8.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  21 RAVRVWCDGCYDMVHYGHSNQLRQARAMG--DYLIVGVHTD--------------------------------------- 59
Cdd:cd02174    1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDeeihkhkgppvmteeeryeavrhckwvdevvegapyvtt 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374253757  60 ---------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 109
Cdd:cd02174   81 pefldkykcdyvahgDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 162-298 3.78e-36

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: 127.68  E-value: 3.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 162 IYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 241
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 242 LLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQI---DSGSnlTTDlIVQRIITN 298
Cdd:cd02174   83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 159-296 8.68e-22

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: 8.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 159 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAV 238
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 239 TAELLsHFKVDLVCHGKTEIIPDrDGSDPYQEPKRRGIFRQI--DSGSNLTTDLIVQRII 296
Cdd:cd02170   77 FKPLE-ELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 150-306 4.98e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 91.16  E-value: 4.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 150 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNypIMNLHERTLSVLACRYVSE 229
Cdd:PLN02413  18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 230 VVIGAPYAVTAELLSHFKVDLVCHgktEIIPDRD----GSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEAR 305
Cdd:PLN02413  96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                 .
gi 374253757 306 N 306
Cdd:PLN02413 173 N 173
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 24-102 1.25e-19

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: 83.49  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD-------------------------------------------- 59
Cdd:cd02170    3 RVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDetvakikrrpilpeeqraevvealkyvdevilghpwsyfkplee 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 374253757  60 ---------DDITLTVDGRDTYEEVKQAGRYREC--KRTQGVSTTDLVGRMLLV 102
Cdd:cd02170   83 lkpdvivlgDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 161-230 4.50e-15

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: 68.87  E-value: 4.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  161 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 230
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 160-233 3.42e-13

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: 65.51  E-value: 3.42e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374253757 160 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 233
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 163-254 1.17e-12

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: 64.26  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757  163 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 242
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 374253757  243 LSHFKVDLVCHG 254
Cdd:pfam01467  77 LKELNPDVLVIG 88
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 8-100 2.07e-12

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 66.51  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757   8 AAGGAEQPGPGGRRAVRVWCDGCYDMVHYGHSNQLRQARAM--GDYLIVGVhTDDDIT--------LT------------ 65
Cdd:PLN02413  13 SSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGC-CNDELThkykgktvMTederyeslrhck 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374253757  66 -VD------------------------------------GRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 100
Cdd:PLN02413  92 wVDevipdapwvitqefldkhridyvahdalpyadasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 23-64 2.20e-12

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: 63.20  E-value: 2.20e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 374253757  23 VRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDDDITL 64
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVAS 42
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 156-263 3.64e-11

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: 60.51  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 156 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNhyKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 235
Cdd:cd02172    1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75

                         90       100
                 ....*....|....*....|....*...
gi 374253757 236 YAVTAELLSHFKVDLVCHGKTEIIPDRD 263
Cdd:cd02172   76 NPTALEIIDALQPNIYVKGGDYENPEND 103
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 24-60 1.46e-10

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: 56.16  E-value: 1.46e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 374253757   24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDD 60
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQ 37
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 158-232 2.98e-08

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: 51.92  E-value: 2.98e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374253757  158 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLHERT--LSVLACryVSEVVI 232
Cdd:TIGR02199  10 GKKIVFTNGCFDILHAGHVSYLQQARALGDR--LVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 26-60 1.57e-07

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: 49.63  E-value: 1.57e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 374253757   26 WCDGCYDMVHYGHSNQLRQARAMGDY-LIVGVHTDD 60
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDE 36
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 159-255 2.36e-07

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: 49.02  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374253757 159 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYAV 238
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76

                         90
                 ....*....|....*..
gi 374253757 239 TAELLSHFKVDLVCHGK 255
Cdd:cd02171   77 KIEDIKKYNVDVFVMGD 93
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 25-60 5.25e-07

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: 50.98  E-value: 5.25e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 374253757  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDD 60
Cdd:PRK11316 343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDA 378
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 29-60 1.27e-06

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: 47.09  E-value: 1.27e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 374253757  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDD 60
Cdd:cd02171    8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDE 39
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 158-223 5.85e-06

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: 47.52  E-value: 5.85e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374253757 158 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLhERTLSVLA 223
Cdd:PRK11316 339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 25-59 9.95e-06

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: 44.71  E-value: 9.95e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 374253757  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD 59
Cdd:cd02172    7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSD 41
 
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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