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Conserved domains on  [gi|1958661309|ref|XP_038942932|]
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ethanolamine-phosphate cytidylyltransferase isoform X4 [Rattus norvegicus]

Protein Classification

nucleotidyl transferase family protein; glutamine/glutamate--tRNA ligase( domain architecture ID 10114957)

nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases| glutamine/glutamate--tRNA ligase catalyzes the attachment of glutamate or glutamine to tRNA(Glu) or tRNA(Gln); in some organisms, the non-discriminating form of glutamate--tRNA ligase aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 34-186 2.19e-98

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: 281.84  E-value: 2.19e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  34 GETVIYVAGAFDLFHIGHVDFLQEVHKLakRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYS 113
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661309 114 VTAELLNHFKVDLVCHGKTEIVPD-RDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKE 186
Cdd:cd02173    79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
 
Name Accession Description Interval E-value
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 34-186 2.19e-98

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: 281.84  E-value: 2.19e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  34 GETVIYVAGAFDLFHIGHVDFLQEVHKLakRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYS 113
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661309 114 VTAELLNHFKVDLVCHGKTEIVPD-RDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKE 186
Cdd:cd02173    79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 7-194 7.85e-84

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 252.40  E-value: 7.85e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309   7 SPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDQEVNRYKGKNYP 86
Cdd:PTZ00308  164 FPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQVVNEQKGSNYP 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  87 IMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYEEPKRRGIFCQIDSGSDLTTD 165
Cdd:PTZ00308  242 IMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTD 321

                         170       180
                  ....*....|....*....|....*....
gi 1958661309 166 LIVQRIIKNRLEYEARNQKKEAKELAFLE 194
Cdd:PTZ00308  322 SIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 36-156 1.37e-17

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: 75.53  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  36 TVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSVT 115
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958661309 116 aELLNHFKVDLVCHGkteivPDRDGSDPY--EEPKRRGIFCQI 156
Cdd:COG0615    77 -EDIEEIKPDVIVLG-----DDWKGDFDFlkEELEKRGIGCEV 113
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 37-106 4.26e-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: 66.95  E-value: 4.26e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  37 VIYVAGAFDLFHIGHVDFLQEVHKLAkrPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEV 106
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 39-130 1.17e-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: 62.34  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  39 YVAGAFDLFHIGHVDFLQEVHKLAKRPyVIAGLHFDQEVNRYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAEL 118
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 1958661309 119 LNHFKVDLVCHG 130
Cdd:pfam01467  77 LKELNPDVLVIG 88
 
Name Accession Description Interval E-value
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 34-186 2.19e-98

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: 281.84  E-value: 2.19e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  34 GETVIYVAGAFDLFHIGHVDFLQEVHKLakRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYS 113
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661309 114 VTAELLNHFKVDLVCHGKTEIVPD-RDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKE 186
Cdd:cd02173    79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 7-194 7.85e-84

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 252.40  E-value: 7.85e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309   7 SPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDQEVNRYKGKNYP 86
Cdd:PTZ00308  164 FPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVHEDQVVNEQKGSNYP 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  87 IMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYEEPKRRGIFCQIDSGSDLTTD 165
Cdd:PTZ00308  242 IMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTD 321

                         170       180
                  ....*....|....*....|....*....
gi 1958661309 166 LIVQRIIKNRLEYEARNQKKEAKELAFLE 194
Cdd:PTZ00308  322 SIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 5-189 1.33e-58

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 189.51  E-value: 1.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309   5 GQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDQEVNRYKGKN 84
Cdd:PLN02406  221 GSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLLVGIHTDQTVSAHRGAH 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  85 YPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGK-TEIVPDRDG-SDPYEEPKRRGIFCQIDSGSDL 162
Cdd:PLN02406  299 RPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGeDDPYAVPKSMGIFQVLESPLDI 378

                         170       180
                  ....*....|....*....|....*..
gi 1958661309 163 TTDLIVQRIIKNRLEYEARNQKKEAKE 189
Cdd:PLN02406  379 TTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 38-174 1.91e-38

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: 129.61  E-value: 1.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  38 IYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSVTAE 117
Cdd:cd02174     5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309 118 LLNHFKVDLVCHGKtEIVPDRDGSDPYEEPKRRGIFCQI---DSGSdlTTDlIVQRIIKN 174
Cdd:cd02174    83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 35-173 4.07e-27

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: 100.44  E-value: 4.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  35 ETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSV 114
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661309 115 TaELLNHFKVDLVCHGKTEIVPDrDGSDPYEEPKRRGIFCQIDSGSD--LTTDLIVQRIIK 173
Cdd:cd02170    77 F-KPLEELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVPRKKTegISSSDIIKRILE 135
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 32-172 1.24e-25

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 101.40  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  32 QPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYViaGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAP 111
Cdd:PTZ00308    8 KPGTIRVWVDGCFDMLHFGHANALRQARALGDELFV--GCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGYP 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661309 112 YSVTAELLNHFKVDLVCHGKtEIVPDRDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRII 172
Cdd:PTZ00308   84 YTTRLEDLERLECDFVVHGD-DISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 26-182 1.34e-23

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 95.01  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  26 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKNypIMNLHERTLSVLACRYVSE 105
Cdd:PLN02413   18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309 106 VVIGAPYSVTAELLNHFKVDLVCHgktEIVPDRD----GSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRIIKNRLEYEAR 181
Cdd:PLN02413   96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172


                  .
gi 1958661309 182 N 182
Cdd:PLN02413  173 N 173
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 36-156 1.37e-17

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: 75.53  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  36 TVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSVT 115
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILGEEWDKF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958661309 116 aELLNHFKVDLVCHGkteivPDRDGSDPY--EEPKRRGIFCQI 156
Cdd:COG0615    77 -EDIEEIKPDVIVLG-----DDWKGDFDFlkEELEKRGIGCEV 113
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 38-172 1.05e-16

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 77.42  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  38 IYVAGAFDLFHIGHVDFLQEVHKLAKRPYViaGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSVTAE 117
Cdd:PLN02406   56 VYMDGCFDMMHYGHANALRQARALGDELVV--GVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEE 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309 118 ----LLNHFKVDLVCHGKTE-IVPdrDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRII 172
Cdd:PLN02406  132 fmnkLFNEYNIDYIIHGDDPcLLP--DGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRML 189
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 37-106 4.26e-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: 66.95  E-value: 4.26e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  37 VIYVAGAFDLFHIGHVDFLQEVHKLAkrPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEV 106
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 32-139 8.72e-13

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: 63.20  E-value: 8.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  32 QPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNryKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 111
Cdd:cd02172     1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75

                          90       100
                  ....*....|....*....|....*...
gi 1958661309 112 YSVTAELLNHFKVDLVCHGKTEIVPDRD 139
Cdd:cd02172    76 NPTALEIIDALQPNIYVKGGDYENPEND 103
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 39-130 1.17e-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: 62.34  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  39 YVAGAFDLFHIGHVDFLQEVHKLAKRPyVIAGLHFDQEVNRYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAEL 118
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76

                          90
                  ....*....|..
gi 1958661309 119 LNHFKVDLVCHG 130
Cdd:pfam01467  77 LKELNPDVLVIG 88
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 34-108 2.32e-10

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: 56.54  E-value: 2.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661309  34 GETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNRYKGKNYPIMNLHERT--LSVLACryVSEVVI 108
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 ...
 34-99 6.15e-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: 51.75  E-value: 6.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661309  34 GETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNRYKGKNYPIMNLhERTLSVLA 99
Cdd:PRK11316  339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 35-131 2.77e-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: 47.86  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661309  35 ETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSV 114
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76

                          90
                  ....*....|....*..
gi 1958661309 115 TAELLNHFKVDLVCHGK 131
Cdd:cd02171    77 KIEDIKKYNVDVFVMGD 93
PRK07143 PRK07143
hypothetical protein; Provisional
 21-93 4.14e-03

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 37.29  E-value: 4.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661309  21 KIIQFAsgKEPQPGETVIYVAGAFDLFHIGHvdflQEVHKLAKRP-YVIAGLHFDQEVNRYKGKNYPIMNLHER 93
Cdd:PRK07143    3 KVYTFP--LKNFKFEKPTFVLGGFESFHLGH----LELFKKAKESnDEIVIVIFKNPENLPKNTNKKFSDLNSR 70
 
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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