NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530413561|ref|XP_005256444|]
View 

ethanolamine-phosphate cytidylyltransferase isoform X2 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00308 super family cl31425
ethanolamine-phosphate cytidylyltransferase; Provisional
 1-358 3.21e-157

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 445.77  E-value: 3.21e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVH 80
Cdd:PTZ00308  22 MLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECDFVVH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561  81 GNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHssqemsseyreyadsfgkpphpipagdiLSS 160
Cdd:PTZ00308 102 GDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL----------------------------LKS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 161 EGCSQCPGGRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQE 240
Cdd:PTZ00308 154 VDEVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 241 VNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRRGIFRQ 319
Cdd:PTZ00308 232 VNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKE 311

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 530413561 320 IDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 358
Cdd:PTZ00308 312 VDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 1-358 3.21e-157

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 445.77  E-value: 3.21e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVH 80
Cdd:PTZ00308  22 MLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECDFVVH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561  81 GNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHssqemsseyreyadsfgkpphpipagdiLSS 160
Cdd:PTZ00308 102 GDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL----------------------------LKS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 161 EGCSQCPGGRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQE 240
Cdd:PTZ00308 154 VDEVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 241 VNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRRGIFRQ 319
Cdd:PTZ00308 232 VNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKE 311

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 530413561 320 IDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 358
Cdd:PTZ00308 312 VDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 198-350 1.69e-94

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: 278.76  E-value: 1.69e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 198 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 277
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413561 278 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 350
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 1-120 1.17e-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: 113.57  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561    1 MVHYGHSNQLRQARAMGDY-LIVGVHTDEEiAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCV 79
Cdd:pfam01467   8 PIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKELNPDVLV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530413561   80 HGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVGR 120
Cdd:pfam01467  87 IGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 1-121 4.54e-30

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: 112.12  E-value: 4.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpaaPYVTT--LETLDKYNCDFC 78
Cdd:COG0615   11 LLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVI---LGEEWdkFEDIEEIKPDVI 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530413561  79 VHGNDITLTVDG-RDTYEEVKQAGRYRECKRTQGVSTTDLVGRM 121
Cdd:COG0615   88 VLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 1-57 2.03e-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: 81.20  E-value: 2.03e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413561    1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEV 57
Cdd:TIGR00125  10 PFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 1-358 3.21e-157

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 445.77  E-value: 3.21e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVH 80
Cdd:PTZ00308  22 MLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECDFVVH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561  81 GNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHssqemsseyreyadsfgkpphpipagdiLSS 160
Cdd:PTZ00308 102 GDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL----------------------------LKS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 161 EGCSQCPGGRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQE 240
Cdd:PTZ00308 154 VDEVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 241 VNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKT-EIIPDRDGSDPYQEPKRRGIFRQ 319
Cdd:PTZ00308 232 VNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKE 311

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 530413561 320 IDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 358
Cdd:PTZ00308 312 VDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 1-353 9.96e-118

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 347.83  E-value: 9.96e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETL----DKYNCD 76
Cdd:PLN02406  64 MMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMnklfNEYNID 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561  77 FCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAH--HSSQEMSSEYREYadsfgkpphpipa 154
Cdd:PLN02406 144 YIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsiSDSHNHSSLQRQF------------- 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 155 gdilsSEGCSQCPG-GRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIA 233
Cdd:PLN02406 211 -----SHGHSQFEDgGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLLV 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 234 GLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGK-TEIIPDRDG-SDPYQEP 311
Cdd:PLN02406 284 GIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGeDDPYAVP 363

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 530413561 312 KRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKE 353
Cdd:PLN02406 364 KSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 198-350 1.69e-94

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: 278.76  E-value: 1.69e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 198 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 277
Cdd:cd02173    1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413561 278 VTAELLSHFKVDLVCHGKTEIIPD-RDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 350
Cdd:cd02173   79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 1-131 1.94e-85

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: 255.57  E-value: 1.94e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMG--DYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFC 78
Cdd:cd02174   13 LFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPEFLDKYKCDYV 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530413561  79 VHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 131
Cdd:cd02174   93 AHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 2-124 8.94e-47

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: 155.91  E-value: 8.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   2 VHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNcDFCVHG 81
Cdd:cd02170   13 IHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPLEELKP-DVIVLG 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530413561  82 NDITLTVDGRDTYEEVKQAGRYREC--KRTQGVSTTDLVGRMLLV 124
Cdd:cd02170   92 DDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 202-338 7.38e-36

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: 128.07  E-value: 7.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 202 IYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 281
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 282 LLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQI---DSGSnlTTDlIVQRIITN 338
Cdd:cd02174   83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 1-122 3.17e-32

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 122.75  E-value: 3.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAM--GDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFC 78
Cdd:PLN02413  38 LFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWVITQEFLDKHRIDYV 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530413561  79 VHgnDITLTVD----GRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 122
Cdd:PLN02413 118 AH--DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 1-120 1.17e-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: 113.57  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561    1 MVHYGHSNQLRQARAMGDY-LIVGVHTDEEiAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCV 79
Cdd:pfam01467   8 PIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKELNPDVLV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530413561   80 HGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVGR 120
Cdd:pfam01467  87 IGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 1-121 4.54e-30

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: 112.12  E-value: 4.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpaaPYVTT--LETLDKYNCDFC 78
Cdd:COG0615   11 LLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVI---LGEEWdkFEDIEEIKPDVI 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530413561  79 VHGNDITLTVDG-RDTYEEVKQAGRYRECKRTQGVSTTDLVGRM 121
Cdd:COG0615   88 VLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 1-122 4.48e-27

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: 104.65  E-value: 4.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFC 78
Cdd:cd02173   13 LFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSnyPIMNLHERVLSVLACRYVDEVVIGAPYVITKELIEHFKIDVV 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530413561  79 VHG--NDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 122
Cdd:cd02173   93 VHGktEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRII 138
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 196-336 1.49e-24

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 102.94  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 196 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAP 275
Cdd:PTZ00308   8 KPGTIRVWVDGCFDMLHFGHANALRQARALGDE--LFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGYP 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530413561 276 YAVTAELLSHFKVDLVCHGKtEIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRII 336
Cdd:PTZ00308  84 YTTRLEDLERLECDFVVHGD-DISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 199-336 3.08e-21

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: 88.50  E-value: 3.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 199 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAV 278
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 279 TAELLsHFKVDLVCHGKTEIIPDrDGSDPYQEPKRRGIFRQI--DSGSNLTTDLIVQRII 336
Cdd:cd02170   77 FKPLE-ELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 190-346 6.66e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 91.55  E-value: 6.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 190 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNypIMNLHERTLSVLACRYVSE 269
Cdd:PLN02413  18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 270 VVIGAPYAVTAELLSHFKVDLVCHgktEIIPDRD----GSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEAR 345
Cdd:PLN02413  96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                 .
gi 530413561 346 N 346
Cdd:PLN02413 173 N 173
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 1-57 2.03e-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: 81.20  E-value: 2.03e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413561    1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEV 57
Cdd:TIGR00125  10 PFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-117 5.44e-17

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: 76.75  E-value: 5.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVH 80
Cdd:cd02171   12 LLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYNVDVFVM 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530413561  81 GNDITLTVDGRDTYEEVKqagrYREckRTQGVSTTDL 117
Cdd:cd02171   92 GDDWEGKFDFLKEYCEVV----YLP--RTKGISSTQL 122
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 202-337 2.63e-16

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 79.73  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 202 IYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 281
Cdd:PLN02406  56 VYMDGCFDMMHYGHANALRQARALGDE--LVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEE 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530413561 282 ----LLSHFKVDLVCHGKTE-IIPdrDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIIT 337
Cdd:PLN02406 132 fmnkLFNEYNIDYIIHGDDPcLLP--DGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLL 190
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 201-270 9.08e-15

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: 68.49  E-value: 9.08e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561  201 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 270
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 200-273 5.18e-13

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: 65.51  E-value: 5.18e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413561 200 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 273
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 203-294 2.00e-12

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: 63.88  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561  203 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 282
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 530413561  283 LSHFKVDLVCHG 294
Cdd:pfam01467  77 LKELNPDVLVIG 88
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 196-303 4.69e-11

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 60.12  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 196 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNhyKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 275
Cdd:cd02172    1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75

                         90       100
                 ....*....|....*....|....*...
gi 530413561 276 YAVTAELLSHFKVDLVCHGKTEIIPDRD 303
Cdd:cd02172   76 NPTALEIIDALQPNIYVKGGDYENPEND 103
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 1-83 6.46e-11

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 59.74  E-value: 6.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561   1 MVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpAAPYVTTLETLDKYNCDFCVH 80
Cdd:cd02172   15 LLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVV-LFDNPTALEIIDALQPNIYVK 93


                 ...
gi 530413561  81 GND 83
Cdd:cd02172   94 GGD 96
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 198-272 2.28e-08

rfaE bifunctional protein, domain II; 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 E. coli, and separate proteins in some other genome. Domain I (TIGR02198) 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. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131254 [Multi-domain]  Cd Length: 144  Bit Score: 52.69  E-value: 2.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413561  198 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLHERT--LSVLACryVSEVVI 272
Cdd:TIGR02199  10 GKKIVFTNGCFDILHAGHVSYLQQARALGDR--LVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 3-59 3.07e-08

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: 55.22  E-value: 3.07e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530413561   3 HYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQAIKWVDEVVP 59
Cdd:PRK11316 353 HAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPVNPLEQRMAVLAALEAVDWVVP 411
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 199-295 4.05e-07

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: 48.63  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413561 199 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYAV 278
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76

                         90
                 ....*....|....*..
gi 530413561 279 TAELLSHFKVDLVCHGK 295
Cdd:cd02171   77 KIEDIKKYNVDVFVMGD 93
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 198-263 5.52e-06

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: 47.90  E-value: 5.52e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530413561 198 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLhERTLSVLA 263
Cdd:PRK11316 339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
2-63 1.45e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 38.66  E-value: 1.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530413561   2 VHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVqaIKWVDEVVPAAPY 63
Cdd:PRK00777  13 LHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNL--KKFLKAVEYDREY 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH