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Conserved domains on  [gi|66826665|ref|XP_646687|]
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hypothetical protein DDB_G0270298 [Dictyostelium discoideum AX4]

Protein Classification

ethanolamine-phosphate cytidylyltransferase( domain architecture ID 11488366)

ethanolamine-phosphate cytidylyltransferase catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway

EC:  2.7.7.14
Gene Ontology:  GO:0004306|GO:0006646

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 1-360 0e+00

ethanolamine-phosphate cytidylyltransferase; Provisional


:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 635.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    1 MSTTTNKKP--IRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAE 78
Cdd:PTZ00308   1 TSPIPPKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   79 GAPYTLTEEYLDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLLCTKDHLqnvsgeqtsp 158
Cdd:PTZ00308  81 GYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL---------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  159 LGGVNPNVLHKQ-SPYTSLSHFLPTTRKIVQFSEGRSPKPNDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDR 237
Cdd:PTZ00308 151 LKSVDEVQLESSlFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  238 VVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYK 317
Cdd:PTZ00308 231 VVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMGIFK 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 66826665  318 EVKHTEGLTATEIVKRIIDNRLQYEARNRKKEAKEINFIEQSN 360
Cdd:PTZ00308 311 EVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEIKP 353
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 1-360 0e+00

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 635.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    1 MSTTTNKKP--IRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAE 78
Cdd:PTZ00308   1 TSPIPPKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   79 GAPYTLTEEYLDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLLCTKDHLqnvsgeqtsp 158
Cdd:PTZ00308  81 GYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL---------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  159 LGGVNPNVLHKQ-SPYTSLSHFLPTTRKIVQFSEGRSPKPNDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDR 237
Cdd:PTZ00308 151 LKSVDEVQLESSlFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  238 VVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYK 317
Cdd:PTZ00308 231 VVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMGIFK 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 66826665  318 EVKHTEGLTATEIVKRIIDNRLQYEARNRKKEAKEINFIEQSN 360
Cdd:PTZ00308 311 EVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEIKP 353
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 198-349 1.78e-90

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: 267.97  E-value: 1.78e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 198 NDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVT 277
Cdd:cd02173   1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVIT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66826665 278 KDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYKEVKHTEGLTATEIVKRIIDNRLQYEARNRKKE 349
Cdd:cd02173  81 KELIEHFKIDVVVHGKTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 13-139 4.73e-28

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: 106.63  E-value: 4.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    13 YVDGCFDLMHFGHANALRQARELGDI-LVVGVHTDEEiAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTLTEEYLDS 91
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 66826665    92 LNCDFCVHGED--ISVGADGKDVYE-----GIKKSGKFRFIKRTEGVSTTELVGR 139
Cdd:pfam01467  80 LNPDVLVIGADslLDFWYELDEILGnvklvVVVRPVFFIPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 200-334 6.91e-28

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: 105.96  E-value: 6.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 200 KIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVhEQKGSNfPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKD 279
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFV-ASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66826665 280 mIDSLHINVVVHGDDQVvlGPEGGVDPYKLPRELGI-YKEVKHTEGLTATEIVKRI 334
Cdd:COG0615  79 -IEEIKPDVIVLGDDWK--GDFDFLKEELEKRGIGCeVVYLPRTEGISSTKIKKRI 131
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 11-76 9.24e-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: 87.36  E-value: 9.24e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66826665    11 RVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEV 76
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 1-360 0e+00

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 635.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    1 MSTTTNKKP--IRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAE 78
Cdd:PTZ00308   1 TSPIPPKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   79 GAPYTLTEEYLDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLLCTKDHLqnvsgeqtsp 158
Cdd:PTZ00308  81 GYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL---------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  159 LGGVNPNVLHKQ-SPYTSLSHFLPTTRKIVQFSEGRSPKPNDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDR 237
Cdd:PTZ00308 151 LKSVDEVQLESSlFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  238 VVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYK 317
Cdd:PTZ00308 231 VVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMGIFK 310

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 66826665  318 EVKHTEGLTATEIVKRIIDNRLQYEARNRKKEAKEINFIEQSN 360
Cdd:PTZ00308 311 EVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEIKP 353
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 5-358 1.80e-143

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 412.92  E-value: 1.80e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    5 TNKKPIRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTL 84
Cdd:PLN02406  49 KKKKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   85 TEEYLDSL----NCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLLCTKDH----LQNVSGEQT 156
Cdd:PLN02406 129 TEEFMNKLfneyNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsisdSHNHSSLQR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  157 SPLGGVNPNVLHKQSPYTSLSHFLPTTRKIVQFSEGRSPKPNDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDD 236
Cdd:PLN02406 209 QFSHGHSQFEDGGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTD 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  237 RVVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMIDSLHINVVVHGD-DQVVLGPEGGVDPYKLPRELGI 315
Cdd:PLN02406 289 QTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGEDDPYAVPKSMGI 368

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 66826665  316 YKEVKHTEGLTATEIVKRIIDNRLQYEARNRKKEAKEINFIEQ 358
Cdd:PLN02406 369 FQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRYYES 411
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 198-349 1.78e-90

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: 267.97  E-value: 1.78e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 198 NDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGSNFPIMNLHERVLSVLSCRYVDEVVIGAPFSVT 277
Cdd:cd02173   1 GDKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVIT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66826665 278 KDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYKEVKHTEGLTATEIVKRIIDNRLQYEARNRKKE 349
Cdd:cd02173  81 KELIEHFKIDVVVHGKTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 8-150 9.09e-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: 265.97  E-value: 9.09e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   8 KPIRVYVDGCFDLMHFGHANALRQARELG--DILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTLT 85
Cdd:cd02174   1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66826665  86 EEYLDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLLCTKDHLQN 150
Cdd:cd02174  81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 202-337 3.30e-47

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 156.96  E-value: 3.30e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 202 IYMDGGFDLFHVGHTEALKQARALG--DYLIVGVHDDRVVHEQKGsnFPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKD 279
Cdd:cd02174   5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKG--PPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66826665 280 MIDSLHINVVVHGDDQVVLgpEGGVDPYKLPRELGIYKEVKHTEGLTATEIVKRIIDN 337
Cdd:cd02174  83 FLDKYKCDYVAHGDDIYLD--ADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLD 138
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 6-151 2.05e-44

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 154.72  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    6 NKKPIRVYVDGCFDLMHFGHANALRQAREL--GDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYT 83
Cdd:PLN02413  24 SDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWV 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66826665   84 LTEEYLDSLNCDFCVHGE----DISvGAdGKDVYEGIKKSGKFRFIKRTEGVSTTELVGRMLlctKDHLQNV 151
Cdd:PLN02413 104 ITQEFLDKHRIDYVAHDAlpyaDAS-GA-GKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV---KDYNQYV 170
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 9-141 2.28e-39

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: 136.27  E-value: 2.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   9 PIRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTLTEEy 88
Cdd:cd02170   1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKP- 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66826665  89 LDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFI--KRTEGVSTTELVGRML 141
Cdd:cd02170  80 LEELKPDVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 200-336 9.73e-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: 108.53  E-value: 9.73e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 200 KIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGsnFPIMNLHERVLSVLSCRYVDEVVIGAPFSvTKD 279
Cdd:cd02170   2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWS-YFK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66826665 280 MIDSLHINVVVHGDDQVVLGPEGGVdpYKLPRELGIYKEV--KHTEGLTATEIVKRIID 336
Cdd:cd02170  79 PLEELKPDVIVLGDDQKNGVDEEEV--YEELKKRGKVIEVprKKTEGISSSDIIKRILE 135
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 13-139 4.73e-28

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: 106.63  E-value: 4.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665    13 YVDGCFDLMHFGHANALRQARELGDI-LVVGVHTDEEiAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTLTEEYLDS 91
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 66826665    92 LNCDFCVHGED--ISVGADGKDVYE-----GIKKSGKFRFIKRTEGVSTTELVGR 139
Cdd:pfam01467  80 LNPDVLVIGADslLDFWYELDEILGnvklvVVVRPVFFIPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 200-334 6.91e-28

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: 105.96  E-value: 6.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 200 KIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVhEQKGSNfPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKD 279
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFV-ASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66826665 280 mIDSLHINVVVHGDDQVvlGPEGGVDPYKLPRELGI-YKEVKHTEGLTATEIVKRI 334
Cdd:COG0615  79 -IEEIKPDVIVLGDDWK--GDFDFLKEELEKRGIGCeVVYLPRTEGISSTKIKKRI 131
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 190-345 7.70e-28

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 110.42  E-value: 7.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  190 SEGRSPKPNDKII--YMDGGFDLFHVGHTEALKQARAL--GDYLIVGVHDDRVVHEQKGSNfpIMNLHERVLSVLSCRYV 265
Cdd:PLN02413  16 SATPSSSPSDRPVrvYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  266 DEVVIGAPFSVTKDMIDSLHINVVVHGDDQVVLGPEGGVDPYKLPRELGIYKEVKHTEGLTATEIVKRIIDNRLQYEARN 345
Cdd:PLN02413  94 DEVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRN 173
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 10-140 1.14e-27

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: 105.19  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  10 IRVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVaegAPYTLTE--E 87
Cdd:COG0615   1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEV---ILGEEWDkfE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 66826665  88 YLDSLNCDFCVHGEDISVGADG-KDVYEGIKKSGKFRFIKRTEGVSTTELVGRM 140
Cdd:COG0615  78 DIEEIKPDVIVLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 11-76 9.24e-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: 87.36  E-value: 9.24e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66826665    11 RVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEV 76
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 203-333 7.23e-19

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: 81.60  E-value: 7.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   203 YMDGGFDLFHVGHTEALKQARALGDY-LIVGVHDDRVVHEQKGsnfPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMI 281
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLKR---PLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 66826665   282 DSLHINVVVHGDDQVV---LGPEGGVDPYKL---PRELgIYKEVKHTEGLTATEIVKR 333
Cdd:pfam01467  78 KELNPDVLVIGADSLLdfwYELDEILGNVKLvvvVRPV-FFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 201-268 2.36e-17

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: 75.42  E-value: 2.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66826665   201 IIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGsnFPIMNLHERVLSVLSCRYVDEV 268
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 8-102 4.39e-14

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: 68.60  E-value: 4.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   8 KPIrVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEgAPYTLTEE 87
Cdd:cd02172   4 KTV-VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVL-FDNPTALE 81

                        90
                ....*....|....*
gi 66826665  88 YLDSLNCDFCVHGED 102
Cdd:cd02172  82 IIDALQPNIYVKGGD 96
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 12-136 5.31e-14

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: 68.28  E-value: 5.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  12 VYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRACKWADEVAEGAPYTLTEEYLDS 91
Cdd:cd02171   4 VITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKK 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 66826665  92 LNCDFCVHGEDisvgADGKdvYEGIKKSGKFRFIKRTEGVSTTEL 136
Cdd:cd02171  84 YNVDVFVMGDD----WEGK--FDFLKEYCEVVYLPRTKGISSTQL 122
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 198-294 7.25e-14

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: 68.21  E-value: 7.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 198 NDKIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVheQKGSNFPIMNLHERVLSVLSCRYVDEVVIgAPFSVT 277
Cdd:cd02172   3 GKTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYV--NKGPGRPIFPEDLRAEVLAALGFVDYVVL-FDNPTA 79

                        90
                ....*....|....*..
gi 66826665 278 KDMIDSLHINVVVHGDD 294
Cdd:cd02172  80 LEIIDALQPNIYVKGGD 96
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 12-140 5.25e-13

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: 69.86  E-value: 5.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   12 VYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGP--PVmNEQERYKAV----RACKWADEVAEGAPYTLT 85
Cdd:PRK11316 343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPV-NPLEQRMAVlaalEAVDWVVPFEEDTPQRLI 421

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   86 EEYLDslncDFCVHG-----EDIsVGADgkdvyEGIKKSGKFRFIKRTEGVSTTELVGRM 140
Cdd:PRK11316 422 AEILP----DLLVKGgdykpEEI-AGSK-----EVWANGGEVKVLNFEDGCSTTNIIKKI 471
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 200-294 9.80e-13

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: 64.43  E-value: 9.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665 200 KIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRvVHEQKGSNfPIMNLHERVLSVLSCRYVDEVVIGAPFSVTKD 279
Cdd:cd02171   2 KVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDE-FNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQKIE 79

                        90
                ....*....|....*
gi 66826665 280 MIDSLHINVVVHGDD 294
Cdd:cd02171  80 DIKKYNVDVFVMGDD 94
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 200-275 1.32e-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: 68.70  E-value: 1.32e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66826665  200 KIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGSNFPIMNLHER--VLSVLSCryVDEVVigaPFS 275
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRmaVLAALEA--VDWVV---PFE 413
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 206-334 1.84e-10

glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate cytidyltransferase, also called CDP-glycerol pyrophosphorylase. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14). 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. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 130581 [Multi-domain]  Cd Length: 125  Bit Score: 57.95  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   206 GGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKGSNFpiMNLHERVLSVLSCRYVDEVVIGAPFSVTKDMIDSLH 285
Cdd:TIGR01518   5 GTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAY--HSYEHRKLILETIRYVDLVIPEKSWEQKKQDIIDFN 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 66826665   286 INVVVHGDDQvvlgpEGGVDPYKLPRELGIYKeVKHTEGLTATEIVKRI 334
Cdd:TIGR01518  83 IDVFVMGDDW-----EGKFDFLKDECPLKVVY-LPRTEGVSTTKIKKEI 125
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
11-96 6.79e-08

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 51.37  E-value: 6.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   11 RVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVMNEQERYKAVRacKWADEVAEGAPYT---LTEE 87
Cdd:PRK00777   3 KVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYEivkIDDP 80


                 ....*....
gi 66826665   88 YLDSLNCDF 96
Cdd:PRK00777  81 YGPALEDDF 89
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
11-67 7.89e-06

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 47.12  E-value: 7.89e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 66826665   11 RVYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEEIAKNKGPPVmNEQERYKAV 67
Cdd:PRK01170   2 ITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPI-PYEDRKRKL 57
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 11-68 1.61e-04

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


Pssm-ID: 173915  Cd Length: 143  Bit Score: 41.50  E-value: 1.61e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66826665  11 RVYVDGCFDLMHFGHANALRQARELG-DILVVGVhTDEEIAKNKGPPVMNE--QERYKAVR 68
Cdd:cd02164   1 KVAVGGTFDRLHDGHKILLSVAFLLAgEKLIIGV-TSDELLKNKSLKELIEpyEERIANLH 60
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
200-332 7.84e-04

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 40.96  E-value: 7.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  200 KIIYMDGGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVheQKGSNFPImNLHERVLSVLscRYVdeVVIGAPFSVTKd 279
Cdd:PRK01170   1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYV--RKNKVYPI-PYEDRKRKLE--NFI--KKFTNKFRIRP- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 66826665  280 mIDSLHINVVVHGDDQVVLgpeggVDPYKLPRELGIyKEVKHTEGLTATEIVK 332
Cdd:PRK01170  73 -IDDRYGNTLYEEDYEIIV-----VSPETYQRALKI-NEIRIKNGLPPLKIVR 118
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 206-294 1.50e-03

FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme riboflavin kinase / FAD synthetase. These enzymes have both ATP:riboflavin 5'-phospho transferase and ATP:FMN-adenylyltransferase activity. They catalyze the 5'-phosphorylation of riboflavin to FMN and the adenylylation of FMN to FAD. This domain is thought to have the flavin mononucleotide (FMN) adenylyltransferase activity.


Pssm-ID: 429011 [Multi-domain]  Cd Length: 158  Bit Score: 38.70  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665   206 GGFDLFHVGH----TEALKQARALGDYLIVGVHDD--RVVHEQKGSNFPIMNLHERvLSVLSCRYVDEVVIgAPFS---- 275
Cdd:pfam06574  13 GNFDGVHLGHqaliAKAKEIARELGLPSVVVTFEPhpREVFNPDSAPFRLTTLEEK-IELLAELGVDYLLV-LPFTkefa 90

                          90       100
                  ....*....|....*....|....*.
gi 66826665   276 -------VTKDMIDSLHINVVVHGDD 294
Cdd:pfam06574  91 slsaeefIENVLVDGLNVKHVVVGFD 116
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 16-129 1.73e-03

FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.


Pssm-ID: 185679 [Multi-domain]  Cd Length: 180  Bit Score: 39.06  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826665  16 GCFDLMHFGH----ANALRQARELGDILVVGV---HTDEEIAKNKGPP-VMNEQERYKAVRACKwADEV---------AE 78
Cdd:cd02064   6 GNFDGVHLGHqaliKTLKKIARERGLPSAVLTfdpHPREVFLPDKAPPrLTTLEEKLELLESLG-VDYLlvlpfdkefAS 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 66826665  79 GAPYTLTEEYLDSLNCDFCVHGEDISVGADGKDVYEGIKKSGKFRFIKRTE 129
Cdd:cd02064  85 LSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTV 135
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
206-278 2.57e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 37.89  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66826665  206 GGFDLFHVGHTEALKQARALGDYLIVGVHDDRVVHEQKgsNFPIMNLHERVLSVLscRYVDEVVIGAPFSVTK 278
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYK--KHKVRPYEVRLKNLK--KFLKAVEYDREYEIVK 76
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 12-65 3.73e-03

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 36.75  E-value: 3.73e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 66826665  12 VYVDGCFDLMHFGHANALRQARELGDILVVGVHTDEeiaKNKGPPVMNEQERYK 65
Cdd:cd02156   2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNP---PVKVWQDPHELEERK 52
 
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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