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Conserved domains on  [gi|1907082877|ref|XP_036012826|]
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ethanolamine-phosphate cytidylyltransferase isoform X4 [Mus musculus]

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
 15-318 5.29e-126

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 364.88  E-value: 5.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  15 KGPGDqriVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD----------------------------------- 59
Cdd:PTZ00308    7 KKPGT---IRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDeeimrnkgppvmhqeeryealrackwvdevvegyp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  60 -------------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSEy 116
Cdd:PTZ00308   84 yttrledlerlecdfvvhgDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 117 reyadsfgkcpggQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLH 196
Cdd:PTZ00308  163 -------------LFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVH 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 197 FDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYQEPKRRG 275
Cdd:PTZ00308  228 EDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMG 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1907082877 276 IFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLE 318
Cdd:PTZ00308  308 IFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 15-318 5.29e-126

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 364.88  E-value: 5.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  15 KGPGDqriVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD----------------------------------- 59
Cdd:PTZ00308    7 KKPGT---IRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDeeimrnkgppvmhqeeryealrackwvdevvegyp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  60 -------------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSEy 116
Cdd:PTZ00308   84 yttrledlerlecdfvvhgDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 117 reyadsfgkcpggQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLH 196
Cdd:PTZ00308  163 -------------LFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVH 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 197 FDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYQEPKRRG 275
Cdd:PTZ00308  228 EDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMG 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1907082877 276 IFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLE 318
Cdd:PTZ00308  308 IFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 158-310 1.98e-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: 1.98e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 158 GETVIYVAGAFDLFHIGHVDFLQEVHKLakRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYS 237
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082877 238 VTAELLNHFKVDLVCHGKTEIVPD-RDGSDPYQEPKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKE 310
Cdd:cd02173    79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 160-254 4.24e-15

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: 70.90  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 160 TVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSVT 239
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKF 76

                          90
                  ....*....|....*
gi 1907082877 240 aELLNHFKVDLVCHG 254
Cdd:COG0615    77 -EDIEEIKPDVIVLG 90
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 161-230 1.24e-14

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: 67.72  E-value: 1.24e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 161 VIYVAGAFDLFHIGHVDFLQEVHKLAkrPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEV 230
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 163-254 3.27e-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: 63.11  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 163 YVAGAFDLFHIGHVDFLQEVHKLAKRPyVIAGLHFDQEVNRYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAEL 242
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 1907082877 243 LNHFKVDLVCHG 254
Cdd:pfam01467  77 LKELNPDVLVIG 88
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 15-318 5.29e-126

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 364.88  E-value: 5.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  15 KGPGDqriVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD----------------------------------- 59
Cdd:PTZ00308    7 KKPGT---IRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDeeimrnkgppvmhqeeryealrackwvdevvegyp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  60 -------------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSEy 116
Cdd:PTZ00308   84 yttrledlerlecdfvvhgDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 117 reyadsfgkcpggQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLH 196
Cdd:PTZ00308  163 -------------LFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVH 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 197 FDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYQEPKRRG 275
Cdd:PTZ00308  228 EDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMG 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1907082877 276 IFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLE 318
Cdd:PTZ00308  308 IFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 158-310 1.98e-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: 1.98e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 158 GETVIYVAGAFDLFHIGHVDFLQEVHKLakRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYS 237
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082877 238 VTAELLNHFKVDLVCHGKTEIVPD-RDGSDPYQEPKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKE 310
Cdd:cd02173    79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 14-313 8.00e-92

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 280.03  E-value: 8.00e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  14 LKGPGDQRIVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDDDIT------------------------------ 63
Cdd:PLN02406   45 FKKKKKKKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIankgppvtpmhermimvsgvkwvdevipda 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  64 ----------------------------LTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAH--HSSQEMS 113
Cdd:PLN02406  125 pyaiteefmnklfneynidyiihgddpcLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsiSDSHNHS 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 114 SEYREYADSFGKCPG-GQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVI 192
Cdd:PLN02406  205 SLQRQFSHGHSQFEDgGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLL 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 193 AGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGK-TEIVPDRDG-SDPYQE 270
Cdd:PLN02406  283 VGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGeDDPYAV 362

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1907082877 271 PKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKE 313
Cdd:PLN02406  363 PKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 21-109 2.01e-43

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: 146.56  E-value: 2.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  21 RIVRVWCDGCYDMVHYGHSNQLRQARAMG--DYLIVGVHTD--------------------------------------- 59
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDeeihkhkgppvmteeeryeavrhckwvdevvegapyvtt 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082877  60 ---------------DDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 109
Cdd:cd02174    81 pefldkykcdyvahgDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 162-298 3.28e-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: 3.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 162 IYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSVTAE 241
Cdd:cd02174     5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 242 LLNHFKVDLVCHGKtEIVPDRDGSDPYQEPKRRGIFYQI---DSGSdlTTDlIVQRIIKN 298
Cdd:cd02174    83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 159-297 1.32e-23

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: 94.28  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 159 ETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSV 238
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082877 239 TaELLNHFKVDLVCHGKTEIVPDrDGSDPYQEPKRRGIFYQIDSGSD--LTTDLIVQRIIK 297
Cdd:cd02170    77 F-KPLEELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVPRKKTegISSSDIIKRILE 135
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 150-306 1.38e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 92.70  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 150 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKNypIMNLHERTLSVLACRYVSE 229
Cdd:PLN02413   18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 230 VVIGAPYSVTAELLNHFKVDLVCHgktEIVPDRD----GSDPYQEPKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEAR 305
Cdd:PLN02413   96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                  .
gi 1907082877 306 N 306
Cdd:PLN02413  173 N 173
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 24-102 2.39e-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: 82.72  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD-------------------------------------------- 59
Cdd:cd02170     3 RVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDetvakikrrpilpeeqraevvealkyvdevilghpwsyfkplee 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907082877  60 ---------DDITLTVDGRDTYEEVKQAGRYREC--KRTQGVSTTDLVGRMLLV 102
Cdd:cd02170    83 lkpdvivlgDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 160-254 4.24e-15

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: 70.90  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 160 TVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSVT 239
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKF 76

                          90
                  ....*....|....*
gi 1907082877 240 aELLNHFKVDLVCHG 254
Cdd:COG0615    77 -EDIEEIKPDVIVLG 90
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 161-230 1.24e-14

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: 67.72  E-value: 1.24e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 161 VIYVAGAFDLFHIGHVDFLQEVHKLAkrPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEV 230
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 23-64 2.79e-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: 2.79e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907082877  23 VRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDDDITL 64
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVAS 42
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 163-254 3.27e-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: 63.11  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 163 YVAGAFDLFHIGHVDFLQEVHKLAKRPyVIAGLHFDQEVNRYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAEL 242
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 1907082877 243 LNHFKVDLVCHG 254
Cdd:pfam01467  77 LKELNPDVLVIG 88
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 156-263 4.89e-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: 62.82  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 156 QPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNryKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 235
Cdd:cd02172     1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75

                          90       100
                  ....*....|....*....|....*...
gi 1907082877 236 YSVTAELLNHFKVDLVCHGKTEIVPDRD 263
Cdd:cd02172    76 NPTALEIIDALQPNIYVKGGDYENPEND 103
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 8-100 9.59e-12

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 64.58  E-value: 9.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877   8 AASAAGLKGPGDQRIVRVWCDGCYDMVHYGHSNQLRQARAM--GDYLIVGVhTDDDIT--------LT------------ 65
Cdd:PLN02413   13 SSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGC-CNDELThkykgktvMTederyeslrhck 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082877  66 -VD------------------------------------GRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 100
Cdd:PLN02413   92 wVDevipdapwvitqefldkhridyvahdalpyadasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 24-60 1.44e-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: 1.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907082877  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 9.05e-10

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: 56.16  E-value: 9.05e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082877 158 GETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNRYKGKNYPIMNLHERT--LSVLACryVSEVVI 232
Cdd:TIGR02199  10 GKKIVFTNGCFDILHAGHVSYLQQARALGDR--LVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 26-60 1.41e-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: 1.41e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907082877  26 WCDGCYDMVHYGHSNQLRQARAMGDY-LIVGVHTDD 60
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDE 36
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 158-223 2.88e-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: 51.75  E-value: 2.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082877 158 GETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNRYKGKNYPIMNLhERTLSVLA 223
Cdd:PRK11316  339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 25-60 4.42e-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: 4.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907082877  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDD 60
Cdd:PRK11316  343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDA 378
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 159-255 7.16e-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: 47.86  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082877 159 ETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSV 238
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76

                          90
                  ....*....|....*..
gi 1907082877 239 TAELLNHFKVDLVCHGK 255
Cdd:cd02171    77 KIEDIKKYNVDVFVMGD 93
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 29-60 2.07e-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: 46.32  E-value: 2.07e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907082877  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDD 60
Cdd:cd02171     8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDE 39
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 25-59 9.10e-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: 9.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907082877  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTD 59
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSD 41
PRK07143 PRK07143
hypothetical protein; Provisional
 145-217 6.61e-03

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 37.67  E-value: 6.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082877 145 KIIQFAsgKEPQPGETVIYVAGAFDLFHIGHvdflQEVHKLAKRP-YVIAGLHFDQEVNRYKGKNYPIMNLHER 217
Cdd:PRK07143    3 KVYTFP--LKNFKFEKPTFVLGGFESFHLGH----LELFKKAKESnDEIVIVIFKNPENLPKNTNKKFSDLNSR 70
 
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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