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Conserved domains on  [gi|442627729|ref|NP_609613|]
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phosphoethanolamine cytidylyltransferase, isoform E [Drosophila melanogaster]

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
 16-359 4.33e-174

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 488.53  E-value: 4.33e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  16 KQRKDVRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVT 95
Cdd:PTZ00308   7 KKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  96 TLDVLDQNNCDFCVHGDDITMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLVGRMLLLTRNHFRQGSAEYDIEKEAkSP 175
Cdd:PTZ00308  87 RLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLLKSVDEVQLESSL-FP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 176 WTGCSQFLPTTQKIIQFSDGKSPNPGDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSNYPIMNL 255
Cdd:PTZ00308 166 YTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 256 HERVLSVLACKFVNEVVIGAPYCVTEELLEHFKIDVVCHGRTPIAL-ENGKIDPYAVPKTRAIFELIDSGNEMTTERIVE 334
Cdd:PTZ00308 246 NERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLVnEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVD 325

                        330       340
                 ....*....|....*....|....*
gi 442627729 335 RIISHRLEYERRNQAKEKKEIEAFE 359
Cdd:PTZ00308 326 RVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 16-359 4.33e-174

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 488.53  E-value: 4.33e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  16 KQRKDVRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVT 95
Cdd:PTZ00308   7 KKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  96 TLDVLDQNNCDFCVHGDDITMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLVGRMLLLTRNHFRQGSAEYDIEKEAkSP 175
Cdd:PTZ00308  87 RLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLLKSVDEVQLESSL-FP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 176 WTGCSQFLPTTQKIIQFSDGKSPNPGDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSNYPIMNL 255
Cdd:PTZ00308 166 YTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 256 HERVLSVLACKFVNEVVIGAPYCVTEELLEHFKIDVVCHGRTPIAL-ENGKIDPYAVPKTRAIFELIDSGNEMTTERIVE 334
Cdd:PTZ00308 246 NERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLVnEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVD 325

                        330       340
                 ....*....|....*....|....*
gi 442627729 335 RIISHRLEYERRNQAKEKKEIEAFE 359
Cdd:PTZ00308 326 RVVKNRLAFLKRQAKKRAKEIKSQE 350
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 19-165 6.18e-90

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: 266.74  E-value: 6.18e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  19 KDVRVWCDGCYDMVHFGHANSLRQAKALG--DKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVTT 96
Cdd:cd02174    1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627729  97 LDVLDQNNCDFCVHGDDITMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLVGRMLLLTRNHFRQGSAE 165
Cdd:cd02174   81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQR 149
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 24-150 4.32e-30

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: 112.03  E-value: 4.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729   24 WCDGCYDMVHFGHANSLRQAKALGDK-VIVGIHTDEEiTKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVTTLDVLDQ 102
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442627729  103 NNCDFCVHGDDITMTAEG-----VDTYHLVKSANR--YKEVKRTAGVSTTDLVGR 150
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYeldeiLGNVKLVVVVRPvfFIPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 21-151 3.38e-29

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: 109.42  E-value: 3.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  21 VRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGapyvTTLDVL 100
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILG----EEWDKF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442627729 101 D---QNNCDFCVHGDDITMTAEGVDTYHLVKSAN-RYKEVKRTAGVSTTDLVGRM 151
Cdd:COG0615   77 EdieEIKPDVIVLGDDWKGDFDFLKEELEKRGIGcEVVYLPRTEGISSTKIKKRI 131
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 22-87 1.07e-21

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: 87.36  E-value: 1.07e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627729   22 RVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEV 87
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 16-359 4.33e-174

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 488.53  E-value: 4.33e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  16 KQRKDVRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVT 95
Cdd:PTZ00308   7 KKPGTIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  96 TLDVLDQNNCDFCVHGDDITMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLVGRMLLLTRNHFRQGSAEYDIEKEAkSP 175
Cdd:PTZ00308  87 RLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLLKSVDEVQLESSL-FP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 176 WTGCSQFLPTTQKIIQFSDGKSPNPGDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSNYPIMNL 255
Cdd:PTZ00308 166 YTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 256 HERVLSVLACKFVNEVVIGAPYCVTEELLEHFKIDVVCHGRTPIAL-ENGKIDPYAVPKTRAIFELIDSGNEMTTERIVE 334
Cdd:PTZ00308 246 NERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLVnEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVD 325

                        330       340
                 ....*....|....*....|....*
gi 442627729 335 RIISHRLEYERRNQAKEKKEIEAFE 359
Cdd:PTZ00308 326 RVVKNRLAFLKRQAKKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 16-354 2.34e-129

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 377.49  E-value: 2.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  16 KQRKDVRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVT 95
Cdd:PLN02406  49 KKKKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  96 TLD----VLDQNNCDFCVHGDDITMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLVGRMLLLTRNH-----------FR 160
Cdd:PLN02406 129 TEEfmnkLFNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsisdshnhsslQR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 161 QGSAEYDIEKEAKS-PWTGCSQFLPTTQKIIQFSDGKSPNPGDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTD 239
Cdd:PLN02406 209 QFSHGHSQFEDGGSgSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTD 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 240 PVVNSYKGSNYPIMNLHERVLSVLACKFVNEVVIGAPYCVTEELLEHFKIDVVCHGR--TPIALENGKIDPYAVPKTRAI 317
Cdd:PLN02406 289 QTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvaENNDFLKGEDDPYAVPKSMGI 368

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 442627729 318 FELIDSGNEMTTERIVERIISHRLEYERRNQAKEKKE 354
Cdd:PLN02406 369 FQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 19-165 6.18e-90

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: 266.74  E-value: 6.18e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  19 KDVRVWCDGCYDMVHFGHANSLRQAKALG--DKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVTT 96
Cdd:cd02174    1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627729  97 LDVLDQNNCDFCVHGDDITMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLVGRMLLLTRNHFRQGSAE 165
Cdd:cd02174   81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQR 149
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 201-351 3.16e-83

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: 249.87  E-value: 3.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 201 GDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSNYPIMNLHERVLSVLACKFVNEVVIGAPYCVT 280
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVIT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627729 281 EELLEHFKIDVVCHGRTPIAL-ENGKIDPYAVPKTRAIFELIDSGNEMTTERIVERIISHRLEYERRNQAKE 351
Cdd:cd02173   81 KELIEHFKIDVVVHGKTEETPdSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 22-154 5.25e-41

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: 140.89  E-value: 5.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  22 RVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVTTLDVLD 101
Cdd:cd02170    3 RVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPLEE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442627729 102 QNNcDFCVHGDDITMTAEGVDTYHLVKSANRYKEV--KRTAGVSTTDLVGRMLLL 154
Cdd:cd02170   83 LKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 1-152 1.49e-35

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 131.61  E-value: 1.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729   1 MEANGDTSACN-------GYSDKQRKDVRVWCDGCYDMVHFGHANSLRQAKAL--GDKVIVGIHTDEEITKHKGPPVFTE 71
Cdd:PLN02413   1 ARKNAGASTAAassgsatPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  72 EERVKMVKGIKWVDEVVLGAPYVTTLDVLDQNNCDFCVHgDDI---TMTAEGVDTYHLVKSANRYKEVKRTAGVSTTDLV 148
Cdd:PLN02413  81 DERYESLRHCKWVDEVIPDAPWVITQEFLDKHRIDYVAH-DALpyaDASGAGKDVYEFVKKIGKFKETKRTDGISTSDII 159


                 ....
gi 442627729 149 GRML 152
Cdd:PLN02413 160 MRIV 163
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 205-337 1.59e-32

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: 119.21  E-value: 1.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 205 VYVAGAFDLFHVGHLDFLEKAKKLG--DYLIVGLHTDPVVNSYKGSnyPIMNLHERVLSVLACKFVNEVVIGAPYCVTEE 282
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442627729 283 LLEHFKIDVVCHGRTPIALENGKiDPYAVPKTRAIFELIDSGNEMTTERIVERII 337
Cdd:cd02174   83 FLDKYKCDYVAHGDDIYLDADGE-DCYQEVKDAGRFKEVKRTEGVSTTDLIGRIL 136
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 24-150 4.32e-30

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: 112.03  E-value: 4.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729   24 WCDGCYDMVHFGHANSLRQAKALGDK-VIVGIHTDEEiTKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVTTLDVLDQ 102
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442627729  103 NNCDFCVHGDDITMTAEG-----VDTYHLVKSANR--YKEVKRTAGVSTTDLVGR 150
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYeldeiLGNVKLVVVVRPvfFIPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 21-151 3.38e-29

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: 109.42  E-value: 3.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  21 VRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGapyvTTLDVL 100
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILG----EEWDKF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442627729 101 D---QNNCDFCVHGDDITMTAEGVDTYHLVKSAN-RYKEVKRTAGVSTTDLVGRM 151
Cdd:COG0615   77 EdieEIKPDVIVLGDDWKGDFDFLKEELEKRGIGcEVVYLPRTEGISSTKIKKRI 131
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 203-295 2.69e-25

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: 99.02  E-value: 2.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 203 KIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKgsNYPIMNLHERVLSVLACKFVNEVVIGapycVTE- 281
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKG--RKPIIPEEQRKEIVEALKYVDEVILG----EEWd 74

                         90
                 ....*....|....*.
gi 442627729 282 --ELLEHFKIDVVCHG 295
Cdd:COG0615   75 kfEDIEEIKPDVIVLG 90
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 203-295 1.69e-24

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: 97.36  E-value: 1.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 203 KIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSnyPIMNLHERVLSVLACKFVNEVVIGAPYcVTEE 282
Cdd:cd02170    2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPW-SYFK 78

                         90
                 ....*....|...
gi 442627729 283 LLEHFKIDVVCHG 295
Cdd:cd02170   79 PLEELKPDVIVLG 91
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 193-350 4.65e-24

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 100.41  E-value: 4.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 193 SDGKSPNPGDKI--VYVAGAFDLFHVGHLDFLEKAKKL--GDYLIVGLHTDPVVNSYKGSNypIMNLHERVLSVLACKFV 268
Cdd:PLN02413  16 SATPSSSPSDRPvrVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 269 NEVVIGAPYCVTEELLEHFKIDVVCHGRTPIALENGKI-DPYAVPKTRAIFELIDSGNEMTTERIVERIISHRLEYERRN 347
Cdd:PLN02413  94 DEVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGkDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRN 173


                 ...
gi 442627729 348 QAK 350
Cdd:PLN02413 174 LAR 176
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 22-87 1.07e-21

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: 87.36  E-value: 1.07e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627729   22 RVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEV 87
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 204-271 6.65e-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: 79.66  E-value: 6.65e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627729  204 IVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSnyPIMNLHERVLSVLACKFVNEV 271
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 206-295 4.88e-17

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: 76.97  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  206 YVAGAFDLFHVGHLDFLEKAKKLGDY-LIVGLHTDPVVNSYKgsnYPIMNLHERVLSVLACKFVNEVVIGAPYCVTEELL 284
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77

                          90
                  ....*....|.
gi 442627729  285 EHFKIDVVCHG 295
Cdd:pfam01467  78 KELNPDVLVIG 88
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 23-113 5.32e-15

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: 71.29  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  23 VWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLgAPYVTTLDVLDQ 102
Cdd:cd02172    7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVL-FDNPTALEIIDA 85

                         90
                 ....*....|.
gi 442627729 103 NNCDFCVHGDD 113
Cdd:cd02172   86 LQPNIYVKGGD 96
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 201-295 8.05e-15

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: 70.91  E-value: 8.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 201 GDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNsyKGSNYPIMNLHERVLSVLACKFVNEVVIgAPYCVT 280
Cdd:cd02172    3 GKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FDNPTA 79

                         90
                 ....*....|....*
gi 442627729 281 EELLEHFKIDVVCHG 295
Cdd:cd02172   80 LEIIDALQPNIYVKG 94
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 27-147 1.94e-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: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729  27 GCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIKWVDEVVLGAPYVTTLDVLDQNNCD 106
Cdd:cd02171    8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYNVD 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442627729 107 FCVHGDDitmtAEGvdTYHLVKSANRYKEVKRTAGVSTTDL 147
Cdd:cd02171   88 VFVMGDD----WEG--KFDFLKEYCEVVYLPRTKGISSTQL 122
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 201-272 4.06e-12

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: 67.16  E-value: 4.06e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627729 201 GDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKGSNYPIMNLHER--VLSVLACkfVNEVV 272
Cdd:PRK11316 339 GEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRmaVLAALEA--VDWVV 410
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 203-295 4.72e-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: 62.50  E-value: 4.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 203 KIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPvVNSYKGSNyPIMNLHERVLSVLACKFVNEVVIGAPYCVTEE 282
Cdd:cd02171    2 KVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDE-FNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQKIE 79

                         90
                 ....*....|...
gi 442627729 283 LLEHFKIDVVCHG 295
Cdd:cd02171   80 DIKKYNVDVFVMG 92
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 16-88 1.24e-09

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: 59.46  E-value: 1.24e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627729  16 KQRKDVRVWCDGCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGP--PVFTEEERVKMVKGIKWVDEVV 88
Cdd:PRK11316 336 RARGEKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPVNPLEQRMAVLAALEAVDWVV 410
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
205-281 2.44e-08

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 52.53  E-value: 2.44e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627729 205 VYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNSYKgsNYPIMNLHERVLSVLacKFVNEVVIGAPYCVTE 281
Cdd:PRK00777   4 VAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYK--KHKVRPYEVRLKNLK--KFLKAVEYDREYEIVK 76
PRK07143 PRK07143
hypothetical protein; Provisional
 188-273 1.20e-07

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 52.31  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 188 KIIQFSdgKSPNPGDKIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPvVNSYKGSNYPIMNLHERVLSVLACKF 267
Cdd:PRK07143   3 KVYTFP--LKNFKFEKPTFVLGGFESFHLGHLELFKKAKESNDEIVIVIFKNP-ENLPKNTNKKFSDLNSRLQTLANLGF 79


                 ....*.
gi 442627729 268 VNEVVI 273
Cdd:PRK07143  80 KNIILL 85
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
27-93 1.52e-05

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 44.44  E-value: 1.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627729  27 GCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKgiKWVDEVVLGAPY 93
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREY 72
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 204-296 3.47e-05

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: 43.20  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627729 204 IVYVAGAFDLFHVGHLDFLEKAK-KLGDYLIVGlhtdPVVNSYK-GSNYPIMNLHERVLSVLAC--KFVNEVVIGAPYC- 278
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALeEALDEVIII----IVSNPPKkKRNKDPFSLHERVEMLKEIlkDRLKVVPVDFPEVk 76

                         90       100
                 ....*....|....*....|....
gi 442627729 279 ------VTEELLEHFKIDVVCHGR 296
Cdd:cd02039   77 illavvFILKILLKVGPDKVVVGE 100
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
203-252 6.74e-05

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 44.42  E-value: 6.74e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 442627729 203 KIVYVAGAFDLFHVGHLDFLEKAKKLGDYLIVGLHTDPVVNsyKGSNYPI 252
Cdd:PRK01170   1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVR--KNKVYPI 48
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 27-79 1.65e-04

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 41.68  E-value: 1.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442627729  27 GCYDMVHFGHANSLRQAKALGDKVIVGIhtdeEITKHKgPPVFTEEERVKMVK 79
Cdd:cd02163    6 GSFDPITNGHLDIIERASKLFDEVIVAV----AVNPSK-KPLFSLEERVELIR 53
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
27-82 4.56e-03

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 38.65  E-value: 4.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442627729  27 GCYDMVHFGHANSLRQAKALGDKVIVGIHTDEEITKHKGPPVFTEEERVKMVKGIK 82
Cdd:PRK01170   7 GTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPIPYEDRKRKLENFIK 62
 
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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