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Conserved domains on  [gi|808354889|ref|NP_001293343|]
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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
 2-294 2.11e-116

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 339.07  E-value: 2.11e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889   2 VAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLLLTKN 81
Cdd:PTZ00308  69 LRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889  82 HHTQDehieqhVERARSLSTDnvamSPWTRVSRFIPTTTTILEFAEGRPPKPTDKVVYVTGSFDLFHIGHLAFLEKAKEF 161
Cdd:PTZ00308 149 HLLKS------VDEVQLESSL----FPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKAREL 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 162 GDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDILDQFNVQAVINGfrdnNSSVVNSSL 241
Cdd:PTZ00308 219 GDYLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGG----KFSDLVNEE 294

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808354889 242 ASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKEKKEAD 294
Cdd:PTZ00308 295 GGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIK 347
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-294 2.11e-116

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 339.07  E-value: 2.11e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889   2 VAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLLLTKN 81
Cdd:PTZ00308  69 LRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889  82 HHTQDehieqhVERARSLSTDnvamSPWTRVSRFIPTTTTILEFAEGRPPKPTDKVVYVTGSFDLFHIGHLAFLEKAKEF 161
Cdd:PTZ00308 149 HLLKS------VDEVQLESSL----FPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKAREL 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 162 GDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDILDQFNVQAVINGfrdnNSSVVNSSL 241
Cdd:PTZ00308 219 GDYLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGG----KFSDLVNEE 294

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808354889 242 ASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKEKKEAD 294
Cdd:PTZ00308 295 GGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIK 347
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 135-289 7.19e-86

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


Pssm-ID: 173924  Cd Length: 152  Bit Score: 254.11  E-value: 7.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 135 DKVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITS 214
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354889 215 DILDQFNVQAVINGFRDNNSsvvnSSLASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKE 289
Cdd:cd02173   82 ELIEHFKIDVVVHGKTEETP----DSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 136-216 8.77e-23

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: 91.32  E-value: 8.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTvNQYKGSNhPIMSIHERVLSVLAYKPVNEVVFGAPYEITSD 215
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEF-VASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78


                 .
gi 808354889 216 I 216
Cdd:COG0615   79 I 79
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 137-204 5.68e-19

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


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 78.89  E-value: 5.68e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354889  137 VVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGsnHPIMSIHERVLSVLAYKPVNEV 204
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 139-228 7.43e-18

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


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 78.13  E-value: 7.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889  139 YVTGSFDLFHIGHLAFLEKAKEFGDY-LIVGILSDQTVNQYKgsnHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDIL 217
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77

                          90
                  ....*....|.
gi 808354889  218 DQFNVQAVING 228
Cdd:pfam01467  78 KELNPDVLVIG 88
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 2-294 2.11e-116

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 339.07  E-value: 2.11e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889   2 VAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLLLTKN 81
Cdd:PTZ00308  69 LRACKWVDEVVEGYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889  82 HHTQDehieqhVERARSLSTDnvamSPWTRVSRFIPTTTTILEFAEGRPPKPTDKVVYVTGSFDLFHIGHLAFLEKAKEF 161
Cdd:PTZ00308 149 HLLKS------VDEVQLESSL----FPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKAREL 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 162 GDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDILDQFNVQAVINGfrdnNSSVVNSSL 241
Cdd:PTZ00308 219 GDYLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGG----KFSDLVNEE 294

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808354889 242 ASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKEKKEAD 294
Cdd:PTZ00308 295 GGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIK 347
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 1-292 1.02e-89

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 273.48  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889   1 MVAGIKWVDEVVENAPYATTVETL----DKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRML 76
Cdd:PLN02406 110 MVSGVKWVDEVIPDAPYAITEEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRML 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889  77 LLTKNHHTQDEHIEQHVERARSLSTD---NVAMSPWTRVSRFIPTTTTILEFAEGRPPKPTDKVVYVTGSFDLFHIGHLA 153
Cdd:PLN02406 190 LCVRERSISDSHNHSSLQRQFSHGHSqfeDGGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVE 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 154 FLEKAKEFGDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDILDQFNVQAVINGFRDNN 233
Cdd:PLN02406 270 ILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTVAEN 349

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808354889 234 SSVVNSslaSIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKEKKE 292
Cdd:PLN02406 350 NDFLKG---EDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 135-289 7.19e-86

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


Pssm-ID: 173924  Cd Length: 152  Bit Score: 254.11  E-value: 7.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 135 DKVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITS 214
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354889 215 DILDQFNVQAVINGFRDNNSsvvnSSLASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKE 289
Cdd:cd02173   82 ELIEHFKIDVVVHGKTEETP----DSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 1-88 7.47e-48

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: 156.96  E-value: 7.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889   1 MVAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLLLTK 80
Cdd:cd02174   61 AVRHCKWVDEVVEGAPYVTTPEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYR 140


                 ....*...
gi 808354889  81 NHHTQDEH 88
Cdd:cd02174  141 DYHRRNLQ 148
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 136-275 1.63e-25

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: 98.52  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSnhPIMSIHERVLSVLAYKPVNEVVFGAPYEITsD 215
Cdd:cd02170    2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSYF-K 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354889 216 ILDQFNVQAVINGFrDNNSSVVNSSLasidpFAEAKRRGIYHEVDSGSD--MTTDLIIDRII 275
Cdd:cd02170   79 PLEELKPDVIVLGD-DQKNGVDEEEV-----YEELKKRGKVIEVPRKKTegISSSDIIKRIL 134
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 138-275 1.11e-24

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: 96.87  E-value: 1.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 138 VYVTGSFDLFHIGHLAFLEKAKEFG--DYLIVGILSDQTVNQYKGsnHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSD 215
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808354889 216 ILDQFNVQAVINGfrDNNSSVVNSSlasiDPFAEAKRRGIYHEV---DSGSdmTTDlIIDRII 275
Cdd:cd02174   83 FLDKYKCDYVAHG--DDIYLDADGE----DCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRIL 136
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 136-216 8.77e-23

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: 91.32  E-value: 8.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTvNQYKGSNhPIMSIHERVLSVLAYKPVNEVVFGAPYEITSD 215
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEF-VASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78


                 .
gi 808354889 216 I 216
Cdd:COG0615   79 I 79
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 130-270 2.06e-19

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 87.15  E-value: 2.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 130 PPKPTDKVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSnhPIMSIHERVLSVLAYKPVNEVVFGAP 209
Cdd:PTZ00308   6 PKKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGYP 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354889 210 YEITSDILDQFNVQAVINGfrDNNSSVVNSSlasiDPFAEAKRRGIYHEVDSGSDM-TTDLI 270
Cdd:PTZ00308  84 YTTRLEDLERLECDFVVHG--DDISVDLNGR----NSYQEIIDAGKFKVVKRTEGIsTTDLV 139
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 137-204 5.68e-19

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


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 78.89  E-value: 5.68e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354889  137 VVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGsnHPIMSIHERVLSVLAYKPVNEV 204
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 130-285 4.99e-18

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 82.30  E-value: 4.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 130 PPKPTDKV--VYVTGSFDLFHIGHLAFLEKAKEF--GDYLIVGILSDQTVNQYKGSNhpIMSIHERVLSVLAYKPVNEVV 205
Cdd:PLN02413  20 SSSPSDRPvrVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDEVI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 206 FGAPYEITSDILDQFNVQAVINgfrdNNSSVVNSSLASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRN 285
Cdd:PLN02413  98 PDAPWVITQEFLDKHRIDYVAH----DALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRN 173
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 139-228 7.43e-18

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


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 78.13  E-value: 7.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889  139 YVTGSFDLFHIGHLAFLEKAKEFGDY-LIVGILSDQTVNQYKgsnHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDIL 217
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77

                          90
                  ....*....|.
gi 808354889  218 DQFNVQAVING 228
Cdd:pfam01467  78 KELNPDVLVIG 88
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 138-275 4.17e-17

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 80.88  E-value: 4.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 138 VYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSnhPIMSIHERVLSVLAYKPVNEVVFGAPYEITSD-- 215
Cdd:PLN02406  56 VYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEEfm 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354889 216 --ILDQFNVQAVINGfrDNNSSVVNSSlasiDPFAEAKRRGIYHEVDSGSDMTTDLIIDRII 275
Cdd:PLN02406 134 nkLFNEYNIDYIIHG--DDPCLLPDGT----DAYALAKKAGRYKQIKRTEGVSSTDIVGRML 189
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 6-76 2.50e-14

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 71.90  E-value: 2.50e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354889   6 KWVDEVVENAPYATTVETLDKYDCDFCVHgdDITLTAD----GKDTYQEVKDHQRYRECKRTCGVSTTDLVGRML 76
Cdd:PLN02413  91 KWVDEVIPDAPWVITQEFLDKHRIDYVAH--DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-78 1.93e-13

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: 66.16  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889   1 MVAGIKWVDEVVENAPYaTTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYREC--KRTCGVSTTDLVGRMLLL 78
Cdd:cd02170   58 VVEALKYVDEVILGHPW-SYFKPLEELKPDVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 136-228 8.15e-12

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: 61.35  E-value: 8.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQtVNQYKGSNhPIMSIHERVLSVLAYKPVNEVVFGAPYEITSD 215
Cdd:cd02171    2 KVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDE-FNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQKIE 79

                         90
                 ....*....|...
gi 808354889 216 ILDQFNVQAVING 228
Cdd:cd02171   80 DIKKYNVDVFVMG 92
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
136-213 1.74e-11

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 61.00  E-value: 1.74e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354889 136 KVVyVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKgsNHPIMSIHERVLSVLAYkpVNEVVFGAPYEIT 213
Cdd:PRK00777   3 KVA-VGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYK--KHKVRPYEVRLKNLKKF--LKAVEYDREYEIV 75
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 136-205 4.87e-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: 59.74  E-value: 4.87e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNqyKGSNHPIMSIHERVLSVLAYKPVNEVV 205
Cdd:cd02172    5 TVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVV 72
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 136-197 2.67e-10

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: 60.61  E-value: 2.67e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSNHPIMSIHER--VLSVLA 197
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRmaVLAALE 404
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 1-74 5.45e-09

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: 53.48  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889    1 MVAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDD--ITLTADGKDTYQEVKDHQRYR-----ECKRTCGVSTTDLVG 73
Cdd:pfam01467  54 MLELAKWVDEVIVVAPWELTRELLKELNPDVLVIGADslLDFWYELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRE 133


                  .
gi 808354889   74 R 74
Cdd:pfam01467 134 R 134
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 6-82 6.94e-09

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: 6.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808354889   6 KWVDEVVENAPYATTVETLDKYDCDFCVHG--DDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLlltKNH 82
Cdd:cd02173   66 RYVDEVVIGAPYVITKELIEHFKIDVVVHGktEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRII---KNR 141
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 137-237 1.82e-06

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


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 46.66  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354889 137 VVYVTGSFDLFHIGHLAFLEKAKE-FGDYLIVGILSDQTVNQYKGSnhpIMSIHERVLSVLAY-KPVNEVVfgaPYEItS 214
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEeALDEVIIIIVSNPPKKKRNKD---PFSLHERVEMLKEIlKDRLKVV---PVDF-P 73

                         90       100
                 ....*....|....*....|...
gi 808354889 215 DILDQFNVQAVINGFRDNNSSVV 237
Cdd:cd02039   74 EVKILLAVVFILKILLKVGPDKV 96
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
136-185 1.32e-05

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 45.96  E-value: 1.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 808354889 136 KVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNqyKGSNHPI 185
Cdd:PRK01170   1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVR--KNKVYPI 48
PRK07143 PRK07143
hypothetical protein; Provisional
 130-194 7.29e-05

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 43.45  E-value: 7.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808354889 130 PPKPTDKV--VYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDqTVNQYKGSNHPIMSIHERVLS 194
Cdd:PRK07143   8 PLKNFKFEkpTFVLGGFESFHLGHLELFKKAKESNDEIVIVIFKN-PENLPKNTNKKFSDLNSRLQT 73
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 137-198 2.55e-03

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 37.64  E-value: 2.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808354889 137 VVYVTGSFDLFHIGHLAFLEKAKEFG-DYLIVGILSDQTVNQYKGSNHpIMSIHERVLSVLAY 198
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLKNKSLKEL-IEPYEERIANLHEF 62
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 147-173 2.89e-03

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 37.48  E-value: 2.89e-03
                         10        20
                 ....*....|....*....|....*..
gi 808354889 147 FHIGHLAFLEKAKEFGDYLIVGILSDQ 173
Cdd:COG1056   14 FHLGHLAVIKWALEEVDELIIGIGSAQ 40
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 136-192 8.94e-03

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 36.13  E-value: 8.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 808354889 136 KVVYvTGSFDLFHIGHLAFLEKAKEFGDYLIVGILsdqtVNQYKgsnHPIMSIHERV 192
Cdd:COG0669    3 IAVY-PGSFDPITNGHLDIIERAAKLFDEVIVAVA----VNPSK---KPLFSLEERV 51
 
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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