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Conserved domains on  [gi|193209647|ref|NP_001041226|]
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ethanolamine-phosphate cytidylyltransferase [Caenorhabditis elegans]

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
 19-284 1.97e-65

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 211.18  E-value: 1.97e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  19 RVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTLN 98
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  99 QLDCD-IIAIPDISHLTTVETArYEEIRGSERAKQYVISEHVTDQEIAGRLMLVTKKHHMETdsildfksailpfaldpl 177
Cdd:PTZ00308  93 RLECDfVVHGDDISVDLNGRNS-YQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLLKS------------------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 178 SNEPVISVSLFKQNYTFAPVVIGRK---------PKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVN 248
Cdd:PTZ00308 154 VDEVQLESSLFPYTPTSHCLTTSRKivqfsnnrsPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVN 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 193209647 249 EEKGTIFPVMNLLERTLNISSLKIVDEVFVGVP-AVT 284
Cdd:PTZ00308 234 EQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPfDVT 270
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 19-284 1.97e-65

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 211.18  E-value: 1.97e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  19 RVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTLN 98
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  99 QLDCD-IIAIPDISHLTTVETArYEEIRGSERAKQYVISEHVTDQEIAGRLMLVTKKHHMETdsildfksailpfaldpl 177
Cdd:PTZ00308  93 RLECDfVVHGDDISVDLNGRNS-YQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLLKS------------------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 178 SNEPVISVSLFKQNYTFAPVVIGRK---------PKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVN 248
Cdd:PTZ00308 154 VDEVQLESSLFPYTPTSHCLTTSRKivqfsnnrsPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVN 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 193209647 249 EEKGTIFPVMNLLERTLNISSLKIVDEVFVGVP-AVT 284
Cdd:PTZ00308 234 EQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPfDVT 270
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 207-341 1.03e-33

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: 121.98  E-value: 1.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 207 DKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVGVPAVTNS 286
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193209647 287 KF-----VNLIRASKIAVYSETH--PRRFADCTYHRIIEEVTPDYDATCEEILERITSRKIA 341
Cdd:cd02173   82 ELiehfkIDVVVHGKTEETPDSLdgEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLA 143
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 21-144 8.71e-22

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: 89.69  E-value: 8.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647   21 YTDGCFDFVHFANARLLWPAKQYG-KKLIVGIHSDDELDNNGiLPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTLNQ 99
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFdEDLIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 193209647  100 LDCDIIAIPDISHLTTVEtaRYEEIRGSERAKQYVISEHVTDQEI 144
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWY--ELDEILGNVKLVVVVRPVFFIPLKP 122
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 208-293 3.06e-21

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: 88.24  E-value: 3.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGdDDVNEEKGtIFPVMNLLERTLNISSLKIVDEVFVGvpaVTNSK 287
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVAT-DEFVASKG-RKPIIPEEQRKEIVEALKYVDEVILG---EEWDK 75


                 ....*.
gi 193209647 288 FVNLIR 293
Cdd:COG0615   76 FEDIEE 81
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 209-276 1.89e-16

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: 73.11  E-value: 1.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193209647  209 VVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGtiFPVMNLLERTLNISSLKIVDEV 276
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 19-284 1.97e-65

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 211.18  E-value: 1.97e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  19 RVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTLN 98
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  99 QLDCD-IIAIPDISHLTTVETArYEEIRGSERAKQYVISEHVTDQEIAGRLMLVTKKHHMETdsildfksailpfaldpl 177
Cdd:PTZ00308  93 RLECDfVVHGDDISVDLNGRNS-YQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLLKS------------------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 178 SNEPVISVSLFKQNYTFAPVVIGRK---------PKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVN 248
Cdd:PTZ00308 154 VDEVQLESSLFPYTPTSHCLTTSRKivqfsnnrsPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVN 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 193209647 249 EEKGTIFPVMNLLERTLNISSLKIVDEVFVGVP-AVT 284
Cdd:PTZ00308 234 EQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPfDVT 270
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 14-281 2.28e-47

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 165.63  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  14 EKKKARVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPF--- 90
Cdd:PLN02406  50 KKKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYait 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  91 QPEMSTL-NQLDCDIIAIPDISHLTTVETARYEEIRGSERAKQYVISEHVTDQEIAGRLMLVTKK-----HHMETDSILD 164
Cdd:PLN02406 130 EEFMNKLfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRErsisdSHNHSSLQRQ 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 165 FKSAILPFALDPLSNEPVISVSLfKQNYTFAPVVIGRKPKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGD 244
Cdd:PLN02406 210 FSHGHSQFEDGGSGSGTRVSHFL-PTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTD 288

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 193209647 245 DDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVGVP 281
Cdd:PLN02406 289 QTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAP 325
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 207-341 1.03e-33

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: 121.98  E-value: 1.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 207 DKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVGVPAVTNS 286
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193209647 287 KF-----VNLIRASKIAVYSETH--PRRFADCTYHRIIEEVTPDYDATCEEILERITSRKIA 341
Cdd:cd02173   82 ELiehfkIDVVVHGKTEETPDSLdgEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLA 143
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 16-157 4.15e-31

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: 114.97  E-value: 4.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  16 KKARVYTDGCFDFVHFANARLLWPAKQYGK--KLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPE 93
Cdd:cd02174    1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPndYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193209647  94 MSTLNQLDCDIIAIPDISHLTTVETARYEEIRGSERAKQYVISEHVTDQEIAGRLMLVTKKHHM 157
Cdd:cd02174   81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHR 144
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 21-144 8.71e-22

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: 89.69  E-value: 8.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647   21 YTDGCFDFVHFANARLLWPAKQYG-KKLIVGIHSDDELDNNGiLPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTLNQ 99
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFdEDLIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 193209647  100 LDCDIIAIPDISHLTTVEtaRYEEIRGSERAKQYVISEHVTDQEI 144
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWY--ELDEILGNVKLVVVVRPVFFIPLKP 122
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 208-293 3.06e-21

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: 88.24  E-value: 3.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGdDDVNEEKGtIFPVMNLLERTLNISSLKIVDEVFVGvpaVTNSK 287
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVAT-DEFVASKG-RKPIIPEEQRKEIVEALKYVDEVILG---EEWDK 75


                 ....*.
gi 193209647 288 FVNLIR 293
Cdd:COG0615   76 FEDIEE 81
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 210-290 5.89e-18

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: 79.53  E-value: 5.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 210 VYVSGAFDLFHAGHLSFLEAAKDLG--DYLIVGIVGDDDVNEEKGTifPVMNLLERTLNISSLKIVDEVFVGVPAVTNSK 287
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82


                 ...
gi 193209647 288 FVN 290
Cdd:cd02174   83 FLD 85
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 209-276 1.89e-16

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: 73.11  E-value: 1.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193209647  209 VVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGtiFPVMNLLERTLNISSLKIVDEV 276
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 208-281 2.83e-16

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: 74.63  E-value: 2.83e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGT-IFPVMnllERTLNISSLKIVDEVFVGVP 281
Cdd:cd02170    2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRpILPEE---QRAEVVEALKYVDEVILGHP 73
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 19-125 4.30e-16

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: 74.25  E-value: 4.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  19 RVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPEMsTLN 98
Cdd:cd02170    3 RVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK-PLE 81

                         90       100
                 ....*....|....*....|....*..
gi 193209647  99 QLDCDIIAIPDISHLTTVETARYEEIR 125
Cdd:cd02170   82 ELKPDVIVLGDDQKNGVDEEEVYEELK 108
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 210-290 2.27e-14

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 73.95  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 210 VYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTifPVMNLLERTLNISSLKIVDEVFVGVPAVTNSKFV 289
Cdd:PLN02406  56 VYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFM 133


                 .
gi 193209647 290 N 290
Cdd:PLN02406 134 N 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 19-85 5.24e-14

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: 68.21  E-value: 5.24e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193209647  19 RVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAF 85
Cdd:COG0615    2 RVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVI 68
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 208-300 1.41e-13

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: 67.33  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFV---GVPavt 284
Cdd:TIGR02199  12 KIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVVIfdeDTP--- 88

                          90
                  ....*....|....*.
gi 193209647  285 nskfVNLIRASKIAVY 300
Cdd:TIGR02199  89 ----EELIGELKPDIL 100
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 201-289 9.46e-13

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 68.27  E-value: 9.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 201 RKPKVTDkvVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTifPVMNLLERTLNISSLKIVDEVFVGV 280
Cdd:PTZ00308   7 KKPGTIR--VWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGY 82


                 ....*....
gi 193209647 281 PAVTNSKFV 289
Cdd:PTZ00308  83 PYTTRLEDL 91
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 208-314 3.06e-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: 63.59  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNeeKGTIFPVMNLLERTLNISSLKIVDEVFVgvpaVTNSK 287
Cdd:cd02172    5 TVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL----FDNPT 78

                         90       100
                 ....*....|....*....|....*..
gi 193209647 288 FVNLIRASKIAVYSETHPRRFADCTYH 314
Cdd:cd02172   79 ALEIIDALQPNIYVKGGDYENPENDVT 105
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 208-323 1.65e-11

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


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 65.24  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVfvgVPavtnsk 287
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVLAALEAVDWV---VP------ 411

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 193209647 288 fvnliraskiavysethprrFADCTYHRIIEEVTPD 323
Cdd:PRK11316 412 --------------------FEEDTPQRLIAEILPD 427
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 208-276 2.69e-11

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: 60.58  E-value: 2.69e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGiVGDDDVNEEKGTIfPVMNLLERTLNISSLKIVDEV 276
Cdd:cd02171    2 KVVITYGTFDLLHIGHLNLLERAKALGDKLIVA-VSTDEFNAGKGKK-AVIPYEQRAEILESIRYVDLV 68
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 10-106 7.57e-11

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 62.27  E-value: 7.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  10 TPDGEKKKARVYTDGCFDFVHFANARLLWPAKQY--GKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFED 87
Cdd:PLN02413  20 SSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPD 99

                         90
                 ....*....|....*....
gi 193209647  88 APFQPEMSTLNQLDCDIIA 106
Cdd:PLN02413 100 APWVITQEFLDKHRIDYVA 118
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 19-84 4.45e-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: 55.01  E-value: 4.45e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193209647   19 RVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEA 84
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 210-290 5.65e-10

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 59.57  E-value: 5.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647 210 VYVSGAFDLFHAGHLSFLEAAKDL--GDYLIVGIVGDDDVNEEKGTIfpVMNLLERTLNISSLKIVDEVFVGVPAVTNSK 287
Cdd:PLN02413  30 VYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDEVIPDAPWVITQE 107


                 ...
gi 193209647 288 FVN 290
Cdd:PLN02413 108 FLD 110
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 214-304 8.88e-10

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: 56.17  E-value: 8.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  214 GAFDLFHAGHLSFLEAAKDLGDY-LIVGIVGDDDVNEEKGTIFPVMnllERTLNISSLKIVDEVFVGVPAVTNSKFVNLI 292
Cdd:pfam01467   4 GTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLKRPLFSAE---ERLEMLELAKWVDEVIVVAPWELTRELLKEL 80

                          90
                  ....*....|..
gi 193209647  293 RASKIAVYSETH 304
Cdd:pfam01467  81 NPDVLVIGADSL 92
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 20-106 1.00e-08

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: 53.80  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  20 VYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELD--NNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTL 97
Cdd:cd02173    5 VYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNeyKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITKELI 84


                 ....*....
gi 193209647  98 NQLDCDIIA 106
Cdd:cd02173   85 EHFKIDVVV 93
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-106 3.08e-08

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 54.79  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647   3 KAIVQGLTPDGEKKKAR-VYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNN--GILPIFTDEERYRLISAIR 79
Cdd:PTZ00308 177 RKIVQFSNNRSPKPGDRiVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQkgSNYPIMNLNERVLGVLSCR 256

                         90       100
                 ....*....|....*....|....*..
gi 193209647  80 WVDEAFEDAPFQPEMSTLNQLDCDIIA 106
Cdd:PTZ00308 257 YVDEVVIGAPFDVTKEVIDSLHINVVV 283
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 5-91 1.70e-07

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 52.76  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647   5 IVQGLTPDGEKKKAR-VYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGIL--PIFTDEERYRLISAIRWV 81
Cdd:PLN02406 238 IVQFSNGKGPGPDARiVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAhrPIMNLHERSLSVLACRYV 317

                         90
                 ....*....|
gi 193209647  82 DEAFEDAPFQ 91
Cdd:PLN02406 318 DEVIIGAPWE 327
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 20-109 1.84e-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: 49.41  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193209647  20 VYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVDEAFEDAPFQPEMSTLNQ 99
Cdd:cd02171    4 VITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKK 83

                         90
                 ....*....|
gi 193209647 100 LDCDIIAIPD 109
Cdd:cd02171   84 YNVDVFVMGD 93
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 14-82 3.33e-07

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: 48.95  E-value: 3.33e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193209647  14 EKKKARVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDDELDNNGILPIFTDEERYRLISAIRWVD 82
Cdd:cd02172    1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVD 69
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
208-252 7.18e-04

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 39.43  E-value: 7.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 193209647 208 KVVyVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKG 252
Cdd:PRK00777   3 KVA-VGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKK 46
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
208-256 1.99e-03

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 39.80  E-value: 1.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 193209647 208 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFP 256
Cdd:PRK01170   1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPIP 49
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 13-55 8.59e-03

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: 37.89  E-value: 8.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 193209647  13 GEKKkarVYTDGCFDFVHFANARLLWPAKQYGKKLIVGIHSDD 55
Cdd:PRK11316 339 GEKI---VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDA 378
 
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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