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Conserved domains on  [gi|532524975|ref|NP_001269132|]
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ethanolamine-phosphate cytidylyltransferase isoform 4 [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
 2-294 2.49e-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: 2.49e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975   2 VQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKA 81
Cdd:PTZ00308  69 LRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  82 HH----SSQEMSSEYREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEK 157
Cdd:PTZ00308 149 HLlksvDEVQLESSLFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQK 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 158 VHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIP 236
Cdd:PTZ00308 215 ARELGD--YLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVN 292

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532524975 237 DRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 294
Cdd:PTZ00308 293 EEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-294 2.49e-126

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 364.88  E-value: 2.49e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975   2 VQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKA 81
Cdd:PTZ00308  69 LRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  82 HH----SSQEMSSEYREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEK 157
Cdd:PTZ00308 149 HLlksvDEVQLESSLFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQK 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 158 VHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIP 236
Cdd:PTZ00308 215 ARELGD--YLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVN 292

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532524975 237 DRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 294
Cdd:PTZ00308 293 EEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 134-286 1.60e-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: 278.76  E-value: 1.60e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 134 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 213
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532524975 214 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 286
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 137-206 4.01e-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: 4.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  137 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 206
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 136-209 3.78e-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: 65.13  E-value: 3.78e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532524975 136 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 209
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 139-230 1.22e-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: 63.88  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  139 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 218
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 532524975  219 LSHFKVDLVCHG 230
Cdd:pfam01467  77 LKELNPDVLVIG 88
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-294 2.49e-126

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 364.88  E-value: 2.49e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975   2 VQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKA 81
Cdd:PTZ00308  69 LRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  82 HH----SSQEMSSEYREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEK 157
Cdd:PTZ00308 149 HLlksvDEVQLESSLFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQK 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 158 VHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIP 236
Cdd:PTZ00308 215 ARELGD--YLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVN 292

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532524975 237 DRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 294
Cdd:PTZ00308 293 EEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 1-289 1.55e-96

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 291.20  E-value: 1.55e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975   1 MVQAIKWVDEVVPAAPYVTTLETL----DKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 76
Cdd:PLN02406 110 MVSGVKWVDEVIPDAPYAITEEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRML 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  77 LVTKAH--HSSQEMSSEYREYADSFGKCPG-GRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVD 153
Cdd:PLN02406 190 LCVRERsiSDSHNHSSLQRQFSHGHSQFEDgGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVE 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 154 FLEKVHRLAErpYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGK-T 232
Cdd:PLN02406 270 ILRLARALGD--FLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvA 347

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532524975 233 EIIPDRDG-SDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKE 289
Cdd:PLN02406 348 ENNDFLKGeDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 134-286 1.60e-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: 278.76  E-value: 1.60e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 134 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 213
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532524975 214 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 286
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 1-85 2.72e-49

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: 161.20  E-value: 2.72e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975   1 MVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTK 80
Cdd:cd02174   61 AVRHCKWVDEVVEGAPYVTTPEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYR 140


                 ....*
gi 532524975  81 AHHSS 85
Cdd:cd02174  141 DYHRR 145
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 138-274 1.56e-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: 128.07  E-value: 1.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 138 IYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 217
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 218 LLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQI---DSGSnlTTDlIVQRIITN 274
Cdd:cd02174   83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 132-272 5.04e-25

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 102.94  E-value: 5.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 132 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAP 211
Cdd:PTZ00308   8 KPGTIRVWVDGCFDMLHFGHANALRQARALGDE--LFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGYP 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532524975 212 YAVTAELLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRII 272
Cdd:PTZ00308  84 YTTRLEDLERLECDFVVHGD-DISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 135-272 1.23e-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: 88.50  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 135 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAV 214
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 215 TAELLsHFKVDLVCHGKTEIIPDrDGSDPYQEPKRRGIFRQI--DSGSNLTTDLIVQRII 272
Cdd:cd02170   77 FKPLE-ELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 126-282 3.10e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 91.55  E-value: 3.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 126 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNypIMNLHERTLSVLACRYVSE 205
Cdd:PLN02413  18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 206 VVIGAPYAVTAELLSHFKVDLVCHgktEIIPDRD----GSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEAR 281
Cdd:PLN02413  96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                 .
gi 532524975 282 N 282
Cdd:PLN02413 173 N 173
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-78 1.72e-20

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: 85.42  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975   1 MVQAIKWVDEVVPAAPYVTTLETLDKYNcDFCVHGNDITLTVDGRDTYEEVKQAGRYREC--KRTQGVSTTDLVGRMLLV 78
Cdd:cd02170   58 VVEALKYVDEVILGHPWSYFKPLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 6-76 3.32e-18

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 83.07  E-value: 3.32e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532524975   6 KWVDEVVPAAPYVTTLETLDKYNCDFCVHgnDITLTVD----GRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 76
Cdd:PLN02413  91 KWVDEVIPDAPWVITQEFLDKHRIDYVAH--DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 138-273 7.89e-17

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 80.50  E-value: 7.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 138 IYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 217
Cdd:PLN02406  56 VYMDGCFDMMHYGHANALRQARALGDE--LVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEE 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532524975 218 ----LLSHFKVDLVCHGKTE-IIPdrDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIIT 273
Cdd:PLN02406 132 fmnkLFNEYNIDYIIHGDDPcLLP--DGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLL 190
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 137-206 4.01e-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: 4.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  137 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 206
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 136-209 3.78e-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: 65.13  E-value: 3.78e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532524975 136 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 209
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 139-230 1.22e-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: 63.88  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975  139 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 218
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 532524975  219 LSHFKVDLVCHG 230
Cdd:pfam01467  77 LKELNPDVLVIG 88
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 1-74 2.22e-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: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975    1 MVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVG 73
Cdd:pfam01467  54 MLELAKWVDEVIVVAPWELTRELLKELNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRE 133


                  .
gi 532524975   74 R 74
Cdd:pfam01467 134 R 134
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 132-239 2.77e-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: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 132 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNhyKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 211
Cdd:cd02172    1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75

                         90       100
                 ....*....|....*....|....*...
gi 532524975 212 YAVTAELLSHFKVDLVCHGKTEIIPDRD 239
Cdd:cd02172   76 NPTALEIIDALQPNIYVKGGDYENPEND 103
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 2-76 7.54e-11

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: 59.58  E-value: 7.54e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532524975   2 VQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHG--NDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 76
Cdd:cd02173   62 VLACRYVDEVVIGAPYVITKELIEHFKIDVVVHGktEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRII 138
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 134-208 2.14e-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: 52.31  E-value: 2.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532524975  134 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLHERT--LSVLACryVSEVVI 208
Cdd:TIGR02199  10 GKKIVFTNGCFDILHAGHVSYLQQARALGDR--LVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 135-231 4.62e-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: 48.25  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532524975 135 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYAV 214
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76

                         90
                 ....*....|....*..
gi 532524975 215 TAELLSHFKVDLVCHGK 231
Cdd:cd02171   77 KIEDIKKYNVDVFVMGD 93
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 134-199 3.80e-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: 47.90  E-value: 3.80e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532524975 134 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLhERTLSVLA 199
Cdd:PRK11316 339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-71 1.47e-03

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: 38.23  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532524975   1 MVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKqagrYREckRTQGVSTTDL 71
Cdd:cd02171   58 ILESIRYVDLVIPETNWEQKIEDIKKYNVDVFVMGDDWEGKFDFLKEYCEVV----YLP--RTKGISSTQL 122
 
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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