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Conserved domains on  [gi|6753552|ref|NP_034111|]
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choline-phosphate cytidylyltransferase A [Mus musculus]

Protein Classification

choline-phosphate cytidylyltransferase( domain architecture ID 10114959)

choline-phosphate cytidylyltransferase catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis, the transfer of a cytidylyl group from CTP to phosphocholine to form CDP-choline

EC:  2.7.7.15
Gene Ontology:  GO:0006656|GO:0006657|GO:0031210|GO:0004105
PubMed:  1323039|9370319|26165797|10208837

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 75-224 9.27e-95

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: 279.07  E-value: 9.27e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   75 RPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 154
Cdd:cd02174   1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552  155 PEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 224
Cdd:cd02174  81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
 
Name Accession Description Interval E-value
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 75-224 9.27e-95

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: 279.07  E-value: 9.27e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   75 RPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 154
Cdd:cd02174   1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552  155 PEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 224
Cdd:cd02174  81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 72-309 2.04e-93

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 281.06  E-value: 2.04e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    72 PCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPW 151
Cdd:PLN02413  23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   152 TLTPEFLAEHRIDFVAHDDIPY--SSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 229
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   230 LNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGP-----EGALKHMLK 304
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEgchkmGTAIKDRIQ 262


                 ....*
gi 6753552   305 EGKGR 309
Cdd:PLN02413 263 ERLMR 267
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 80-208 3.72e-34

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: 122.81  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552     80 YADGIFDLFHSGHARALMQAKNLFPNTyLIVGVCSDELTHNFKGfTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLA 159
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753552    160 EHRIDFVAHDDIPYSSA--GSDDVYKHIKDAGM-----FAPTQRTEGISTSDIITR 208
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 78-145 8.66e-22

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: 87.75  E-value: 8.66e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6753552     78 RVYADGIFDLFHSGHARALMQAKNLFPntYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEV 145
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 77-209 4.02e-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: 87.85  E-value: 4.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   77 VRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTpE 156
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6753552  157 FLAEHRIDFVAHddipyssaGSDDVY--KHIKDAGMFAPT-------QRTEGISTSDIITRI 209
Cdd:COG0615  78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
 
Name Accession Description Interval E-value
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 75-224 9.27e-95

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: 279.07  E-value: 9.27e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   75 RPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 154
Cdd:cd02174   1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552  155 PEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 224
Cdd:cd02174  81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 72-309 2.04e-93

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 281.06  E-value: 2.04e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    72 PCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPW 151
Cdd:PLN02413  23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   152 TLTPEFLAEHRIDFVAHDDIPY--SSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 229
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   230 LNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGP-----EGALKHMLK 304
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEgchkmGTAIKDRIQ 262


                 ....*
gi 6753552   305 EGKGR 309
Cdd:PLN02413 263 ERLMR 267
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 71-210 9.51e-39

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 141.46  E-value: 9.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    71 TPCERP--VRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRN 148
Cdd:PTZ00308   4 IPPKKPgtIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6753552   149 APWTLTPEFLAEHRIDFVAH-DDIPYSSAGsDDVYKHIKDAGMFAPTQRTEGISTSDIITRIV 210
Cdd:PTZ00308  82 YPYTTRLEDLERLECDFVVHgDDISVDLNG-RNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 79-220 9.79e-35

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: 125.06  E-value: 9.79e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   79 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKG--FTVMNENERYDAVQHCRYVDEVVRNAPWTLTPE 156
Cdd:cd02173   5 VYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGsnYPIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6753552  157 FLAEHRIDFVAH--DDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRN 220
Cdd:cd02173  83 LIEHFKIDVVVHgkTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 80-208 3.72e-34

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: 122.81  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552     80 YADGIFDLFHSGHARALMQAKNLFPNTyLIVGVCSDELTHNFKGfTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLA 159
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753552    160 EHRIDFVAHDDIPYSSA--GSDDVYKHIKDAGM-----FAPTQRTEGISTSDIITR 208
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 75-209 2.15e-30

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 120.17  E-value: 2.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    75 RPVRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 154
Cdd:PLN02406  52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6753552   155 PEFL----AEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRI 209
Cdd:PLN02406 130 EEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRM 188
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 79-231 1.39e-29

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 116.81  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    79 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKG--FTVMNENERYDAVQHCRYVDEVVRNAPWTLTPE 156
Cdd:PTZ00308 195 VYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGsnYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKE 272

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6753552   157 FLAEHRIDFVAH--DDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRgyTAKELN 231
Cdd:PTZ00308 273 VIDSLHINVVVGgkFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKK--RAKEIK 347
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 76-209 7.99e-28

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: 106.22  E-value: 7.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   76 PVRVYADGIFDLFHSGHARALMQAKNLFpnTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTP 155
Cdd:cd02170   1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753552  156 EFLAEHRiDFVAHDDIPYSSAGSDDVYKHIKDAGMFA--PTQRTEGISTSDIITRI 209
Cdd:cd02170  79 PLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIevPRKKTEGISSSDIIKRI 133
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 79-236 1.78e-23

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 100.53  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    79 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDEL--THNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPE 156
Cdd:PLN02406 254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   157 FLAEHRIDFVAHDDIPYSS---AGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE--LN 231
Cdd:PLN02406 332 MITTFNISLVVHGTVAENNdflKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRyyES 411


                 ....*
gi 6753552   232 VSFIN 236
Cdd:PLN02406 412 KSFVS 416
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 78-145 8.66e-22

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: 87.75  E-value: 8.66e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6753552     78 RVYADGIFDLFHSGHARALMQAKNLFPntYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEV 145
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 77-209 4.02e-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: 87.85  E-value: 4.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   77 VRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTpE 156
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6753552  157 FLAEHRIDFVAHddipyssaGSDDVY--KHIKDAGMFAPT-------QRTEGISTSDIITRI 209
Cdd:COG0615  78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 83-205 1.02e-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: 61.73  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   83 GIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHR 162
Cdd:cd02171   8 GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYN 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6753552  163 ID-FVAHDDIpyssAGSDDVYKHIKDAgMFAPtqRTEGISTSDI 205
Cdd:cd02171  86 VDvFVMGDDW----EGKFDFLKEYCEV-VYLP--RTKGISSTQL 122
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 74-214 1.17e-09

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: 56.27  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552   74 ERPVrVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVrnapwtL 153
Cdd:cd02172   3 GKTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVV------L 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753552  154 TPEFLAEHRIDFVAHD----DIPYSSAGSDdvyKHIKDAGMFAPTQRTEG---------ISTSDIITRIVRDYD 214
Cdd:cd02172  74 FDNPTALEIIDALQPNiyvkGGDYENPEND---VTGKIAPEAEAVKAYGGkivftgeivFSSSALINRIFDELD 144
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 79-209 1.86e-04

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: 43.28  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753552    79 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFT-VMNENERYDAV---QHCryVDEVVrnaPWTL- 153
Cdd:PRK11316 343 VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKGEGrPVNPLEQRMAVlaaLEA--VDWVV---PFEEd 415

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6753552   154 TPEFL-AEHRIDFVAH------DDIpyssAGSDDVYKHikdAGMFAPTQRTEGISTSDIITRI 209
Cdd:PRK11316 416 TPQRLiAEILPDLLVKggdykpEEI----AGSKEVWAN---GGEVKVLNFEDGCSTTNIIKKI 471
 
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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