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Conserved domains on  [gi|1187585191|ref|XP_020745321|]
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choline-phosphate cytidylyltransferase A isoform X3 [Odocoileus virginianus texanus]

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) ...
 12-161 2.85e-97

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: 284.46  E-value: 2.85e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  12 RPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 91
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  92 PEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 161
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
 
Name Accession Description Interval E-value
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 12-161 2.85e-97

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: 284.46  E-value: 2.85e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  12 RPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 91
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  92 PEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 161
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 2-246 1.97e-95

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 285.30  E-value: 1.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191   2 EEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDE 81
Cdd:PLN02413   16 SATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  82 VVRNAPWTLTPEFLAEHRIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQ 159
Cdd:PLN02413   96 VIPDAPWVITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191 160 RGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGP-----EG 234
Cdd:PLN02413  176 RGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEgchkmGT 255

                         250
                  ....*....|..
gi 1187585191 235 ALKHMLKEGKGR 246
Cdd:PLN02413  256 AIKDRIQERLMR 267
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 17-145 2.51e-35

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: 125.12  E-value: 2.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  17 YADGIFDLFHSGHARALMQAKNLFPNTyLIVGVCSDELTHNFKGfTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLA 96
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1187585191  97 EHRIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FAPTQRTEGISTSDIITR 145
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 15-82 2.85e-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: 88.52  E-value: 2.85e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1187585191  15 RVYADGIFDLFHSGHARALMQAKNLFPntYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEV 82
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 14-146 3.32e-22

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: 90.55  E-value: 3.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  14 VRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTpE 93
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1187585191  94 FLAEHRIDFVAHddipyssaGSDDVY--KHIKEAGMFAPT-------QRTEGISTSDIITRI 146
Cdd:COG0615    78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
 
Name Accession Description Interval E-value
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 12-161 2.85e-97

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: 284.46  E-value: 2.85e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  12 RPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 91
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  92 PEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 161
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 2-246 1.97e-95

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 285.30  E-value: 1.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191   2 EEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDE 81
Cdd:PLN02413   16 SATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  82 VVRNAPWTLTPEFLAEHRIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQ 159
Cdd:PLN02413   96 VIPDAPWVITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191 160 RGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGP-----EG 234
Cdd:PLN02413  176 RGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEgchkmGT 255

                         250
                  ....*....|..
gi 1187585191 235 ALKHMLKEGKGR 246
Cdd:PLN02413  256 AIKDRIQERLMR 267
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-147 3.78e-39

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 141.85  E-value: 3.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191   8 TPCERP--VRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRN 85
Cdd:PTZ00308    4 IPPKKPgtIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1187585191  86 APWTLTPEFLAEHRIDFVAH-DDIPYSSAGsDDVYKHIKEAGMFAPTQRTEGISTSDIITRIV 147
Cdd:PTZ00308   82 YPYTTRLEDLERLECDFVVHgDDISVDLNG-RNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 16-157 1.15e-36

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: 129.30  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  16 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKG--FTVMNENERYDAVQHCRYVDEVVRNAPWTLTPE 93
Cdd:cd02173     5 VYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGsnYPIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1187585191  94 FLAEHRIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRN 157
Cdd:cd02173    83 LIEHFKIDVVVHgkTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 17-145 2.51e-35

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: 125.12  E-value: 2.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  17 YADGIFDLFHSGHARALMQAKNLFPNTyLIVGVCSDELTHNFKGfTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLA 96
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1187585191  97 EHRIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FAPTQRTEGISTSDIITR 145
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 12-146 1.09e-30

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 120.17  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  12 RPVRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLT 91
Cdd:PLN02406   52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1187585191  92 PEFL----AEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRI 146
Cdd:PLN02406  130 EEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRM 188
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 16-168 1.62e-30

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 118.73  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  16 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKG--FTVMNENERYDAVQHCRYVDEVVRNAPWTLTPE 93
Cdd:PTZ00308  195 VYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGsnYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKE 272

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1187585191  94 FLAEHRIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRgyTAKELN 168
Cdd:PTZ00308  273 VIDSLHINVVVGgkFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKK--RAKEIK 347
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 13-146 4.35e-29

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: 108.92  E-value: 4.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  13 PVRVYADGIFDLFHSGHARALMQAKNLFpnTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTP 92
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1187585191  93 EFLAEHRiDFVAHDDIPYSSAGSDDVYKHIKEAGMFA--PTQRTEGISTSDIITRI 146
Cdd:cd02170    79 PLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIevPRKKTEGISSSDIIKRI 133
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 16-173 1.37e-23

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 100.53  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  16 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDEL--THNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPE 93
Cdd:PLN02406  254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  94 FLAEHRIDFVAHDDIPYSS---AGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE--LN 168
Cdd:PLN02406  332 MITTFNISLVVHGTVAENNdflKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRyyES 411


                  ....*
gi 1187585191 169 VSFIN 173
Cdd:PLN02406  412 KSFVS 416
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 15-82 2.85e-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: 88.52  E-value: 2.85e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1187585191  15 RVYADGIFDLFHSGHARALMQAKNLFPntYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEV 82
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 14-146 3.32e-22

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: 90.55  E-value: 3.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  14 VRVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTpE 93
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1187585191  94 FLAEHRIDFVAHddipyssaGSDDVY--KHIKEAGMFAPT-------QRTEGISTSDIITRI 146
Cdd:COG0615    78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 20-142 1.59e-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: 63.66  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  20 GIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHR 99
Cdd:cd02171     8 GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYN 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1187585191 100 ID-FVAHDDIpyssAGSDDVYKHIKEAgMFAPtqRTEGISTSDI 142
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 ...
 11-151 5.08e-10

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: 57.04  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  11 ERPVrVYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVrnapwtL 90
Cdd:cd02172     3 GKTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVV------L 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1187585191  91 TPEFLAEHRIDFVAHD----DIPYSSAGSDDVYKHIKEagmFAPTQRTEG---------ISTSDIITRIVRDYD 151
Cdd:cd02172    74 FDNPTALEIIDALQPNiyvkGGDYENPENDVTGKIAPE---AEAVKAYGGkivftgeivFSSSALINRIFDELD 144
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 16-146 1.65e-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: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187585191  16 VYADGIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFT-VMNENERYDAV---QHCryVDEVVrnaPWTL- 90
Cdd:PRK11316  343 VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKGEGrPVNPLEQRMAVlaaLEA--VDWVV---PFEEd 415

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1187585191  91 TPEFL-AEHRIDFVAH------DDIpyssAGSDDVYKHikeAGMFAPTQRTEGISTSDIITRI 146
Cdd:PRK11316  416 TPQRLiAEILPDLLVKggdykpEEI----AGSKEVWAN---GGEVKVLNFEDGCSTTNIIKKI 471
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
20-92 8.92e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 36.35  E-value: 8.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1187585191  20 GIFDLFHSGHARALMQAKNLfpNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQhcRYVDEVVRNAPWTLTP 92
Cdd:PRK00777    8 GTFDPLHDGHRALLRKAFEL--GKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYEIVK 76
 
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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