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Conserved domains on  [gi|1060099114|ref|NP_001317447|]
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ethanolamine-phosphate cytidylyltransferase isoform 7 [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

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List of domain hits

 Name Accession Description Interval E-value
PTZ00308 super family cl31425
ethanolamine-phosphate cytidylyltransferase; Provisional
 14-350 1.51e-156

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 443.84  E-value: 1.51e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  14 QPGpggrrAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAA 93
Cdd:PTZ00308    8 KPG-----TIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  94 PYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSE 169
Cdd:PTZ00308   83 PYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 170 YREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGL 249
Cdd:PTZ00308  163 LFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 250 HFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHF-----------------------KEPKRR 306
Cdd:PTZ00308  227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLhinvvvggkfsdlvneeggsdpyEVPKAM 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1060099114 307 GIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 350
Cdd:PTZ00308  307 GIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 14-350 1.51e-156

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 443.84  E-value: 1.51e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  14 QPGpggrrAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAA 93
Cdd:PTZ00308    8 KPG-----TIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  94 PYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSE 169
Cdd:PTZ00308   83 PYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 170 YREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGL 249
Cdd:PTZ00308  163 LFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 250 HFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHF-----------------------KEPKRR 306
Cdd:PTZ00308  227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLhinvvvggkfsdlvneeggsdpyEVPKAM 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1060099114 307 GIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 350
Cdd:PTZ00308  307 GIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 21-163 8.35e-97

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


Pssm-ID: 173925  Cd Length: 150  Bit Score: 284.07  E-value: 8.35e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  21 RAVRVWCDGCYDMVHYGHSNQLRQARAMG--DYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTT 98
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060099114  99 LETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 163
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 26-152 2.11e-35

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 125.89  E-value: 2.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  26 WCDGCYDMVHYGHSNQLRQARAMGDY-LIVGVHTDEEiAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDK 104
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099114 105 YNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVGR 152
Cdd:pfam01467  80 LNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 23-153 1.91e-34

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: 123.29  E-value: 1.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  23 VRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpaaPYVTT--LE 100
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVI---LGEEWdkFE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060099114 101 TLDKYNCDFCVHGNDITLTVDG-RDTYEEVKQAGRYRECKRTQGVSTTDLVGRM 153
Cdd:COG0615    78 DIEEIKPDVIVLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 24-89 2.29e-24

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: 94.68  E-value: 2.29e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099114  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEV 89
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 14-350 1.51e-156

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 443.84  E-value: 1.51e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  14 QPGpggrrAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAA 93
Cdd:PTZ00308    8 KPG-----TIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  94 PYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSE 169
Cdd:PTZ00308   83 PYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 170 YREYadsfgkcpggrnpwTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGL 249
Cdd:PTZ00308  163 LFPY--------------TPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 250 HFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHF-----------------------KEPKRR 306
Cdd:PTZ00308  227 HEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLhinvvvggkfsdlvneeggsdpyEVPKAM 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1060099114 307 GIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLE 350
Cdd:PTZ00308  307 GIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 20-345 1.54e-119

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 352.06  E-value: 1.54e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  20 RRAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTL 99
Cdd:PLN02406   51 KKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 100 ETL----DKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAH--HSSQEMSSEYREY 173
Cdd:PLN02406  131 EFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsiSDSHNHSSLQRQF 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 174 ADSFGKCPG-GRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFD 252
Cdd:PLN02406  211 SHGHSQFEDgGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLLVGIHTD 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 253 QEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHF------------------------KEPKRRGI 308
Cdd:PLN02406  289 QTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFnislvvhgtvaenndflkgeddpyAVPKSMGI 368

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1060099114 309 FRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKE 345
Cdd:PLN02406  369 FQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 21-163 8.35e-97

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


Pssm-ID: 173925  Cd Length: 150  Bit Score: 284.07  E-value: 8.35e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  21 RAVRVWCDGCYDMVHYGHSNQLRQARAMG--DYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTT 98
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060099114  99 LETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 163
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 212-342 1.34e-78

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: 237.93  E-value: 1.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 212 GETVIYVAGAFDLFHIGHVDFLEKVHRLaeRPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYA 291
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1060099114 292 VTAELLSHFK-----------------------EPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKE 342
Cdd:cd02173    79 ITKELIEHFKidvvvhgkteetpdsldgedpyaVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 24-156 5.38e-54

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: 174.40  E-value: 5.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLD 103
Cdd:cd02170     3 RVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPLEE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099114 104 KYNcDFCVHGNDITLTVDGRDTYEEVKQAGRYREC--KRTQGVSTTDLVGRMLLV 156
Cdd:cd02170    83 LKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 8-154 6.33e-41

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 145.86  E-value: 6.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114   8 AAGGAEQPGPGGRRAVRVWCDGCYDMVHYGHSNQLRQARAM--GDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKW 85
Cdd:PLN02413   13 SSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKW 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060099114  86 VDEVVPAAPYVTTLETLDKYNCDFCVHgnDITLTVD----GRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 154
Cdd:PLN02413   93 VDEVIPDAPWVITQEFLDKHRIDYVAH--DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 26-152 2.11e-35

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 125.89  E-value: 2.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  26 WCDGCYDMVHYGHSNQLRQARAMGDY-LIVGVHTDEEiAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDK 104
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099114 105 YNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVGR 152
Cdd:pfam01467  80 LNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRER 134
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 23-153 1.91e-34

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: 123.29  E-value: 1.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  23 VRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpaaPYVTT--LE 100
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVI---LGEEWdkFE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060099114 101 TLDKYNCDFCVHGNDITLTVDG-RDTYEEVKQAGRYRECKRTQGVSTTDLVGRM 153
Cdd:COG0615    78 DIEEIKPDVIVLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 25-154 1.01e-30

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: 114.28  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETL 102
Cdd:cd02173     5 VYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSnyPIMNLHERVLSVLACRYVDEVVIGAPYVITKELI 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060099114 103 DKYNCDFCVHG--NDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 154
Cdd:cd02173    85 EHFKIDVVVHGktEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRII 138
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 24-89 2.29e-24

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: 94.68  E-value: 2.29e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099114  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEV 89
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 216-330 2.89e-24

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: 96.87  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 216 IYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAVTAE 295
Cdd:cd02174     5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099114 296 LLSHFK---------------------EPKRRGIFRQI---DSGSnlTTDlIVQRIITN 330
Cdd:cd02174    83 FLDKYKcdyvahgddiyldadgedcyqEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 4-175 1.39e-21

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 95.13  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114   4 NGRGaaggaeqPGPGGRRavrVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQ 81
Cdd:PLN02406  243 NGKG-------PGPDARI---VYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAhrPIMNLHERSLSVL 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  82 AIKWVDEVVPAAPYVTTLETLDKYNCDFCVHG---NDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTK 158
Cdd:PLN02406  313 ACRYVDEVIIGAPWEVSKDMITTFNISLVVHGtvaENNDFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHE 392

                         170
                  ....*....|....*....
gi 1060099114 159 AHHSSQE--MSSEYREYAD 175
Cdd:PLN02406  393 AYQKRNEkkAESEKRYYES 411
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 29-149 3.41e-19

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: 82.53  E-value: 3.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCD 108
Cdd:cd02171     8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYNVD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1060099114 109 FCVHGNDITLTVDGRDTYEEVKqagrYREckRTQGVSTTDL 149
Cdd:cd02171    88 VFVMGDDWEGKFDFLKEYCEVV----YLP--RTKGISSTQL 122
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 213-328 3.54e-17

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: 77.33  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 213 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYAV 292
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1060099114 293 TAELLS--------------------HFKEPKRRGIFRQI--DSGSNLTTDLIVQRII 328
Cdd:cd02170    77 FKPLEElkpdvivlgddqkngvdeeeVYEELKKRGKVIEVprKKTEGISSSDIIKRIL 134
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 25-115 1.30e-15

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


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 73.22  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpAAPYVTTLETLDK 104
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVV-LFDNPTALEIIDA 85

                          90
                  ....*....|.
gi 1060099114 105 YNCDFCVHGND 115
Cdd:cd02172    86 LQPNIYVKGGD 96
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 215-284 6.03e-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: 68.87  E-value: 6.03e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 215 VIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDQEVNHYKGKnyPIMNLHERTLSVLACRYVSEV 284
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 204-338 1.89e-14

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 73.06  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 204 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNypIMNLHERTLSVLACRYVSE 283
Cdd:PLN02413   18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060099114 284 VVIGAPYAVTAELL--------SHFKEP---------------KRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARN 338
Cdd:PLN02413   96 VIPDAPWVITQEFLdkhridyvAHDALPyadasgagkdvyefvKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRN 173
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 214-287 3.67e-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: 65.90  E-value: 3.67e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1060099114 214 TVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVVIG 287
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATD-EFVASKGRK-PIIPEEQRKEIVEALKYVDEVILG 70
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 217-297 1.92e-11

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: 61.18  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099114 217 YVAGAFDLFHIGHVDFLEKVHRLAERPyIIAGLHFDQEVNHYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAEL 296
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76


                  .
gi 1060099114 297 L 297
Cdd:pfam01467  77 L 77
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 25-91 2.74e-11

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: 64.46  E-value: 2.74e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099114  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQAIKWVDEVVP 91
Cdd:PRK11316  343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPVNPLEQRMAVLAALEAVDWVVP 411
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 210-286 2.43e-09

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: 55.11  E-value: 2.43e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060099114 210 QPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNhyKGKNYPIMNLHERTLSVLACRYVSEVVI 286
Cdd:cd02172     1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL 73
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 212-286 2.64e-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: 52.31  E-value: 2.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060099114 212 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLHERT--LSVLACryVSEVVI 286
Cdd:TIGR02199  10 GKKIVFTNGCFDILHAGHVSYLQQARALGDR--LVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI 82
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 213-285 4.56e-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: 48.25  E-value: 4.56e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060099114 213 ETVIYVAGAFDLFHIGHVDFLEKVHRLAErpYIIAGLHFDqEVNHYKGKNyPIMNLHERTLSVLACRYVSEVV 285
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVI 69
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 212-277 6.21e-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: 6.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099114 212 GETVIYVAGAFDLFHIGHVDFLEKVHRLAERpyIIAGLHFDQEVNHYKGKNYPIMNLhERTLSVLA 277
Cdd:PRK11316  339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
29-95 1.09e-04

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 42.13  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1060099114  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVqaIKWVDEVVPAAPY 95
Cdd:PRK00777    8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNL--KKFLKAVEYDREY 72
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
29-81 5.27e-03

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 38.26  E-value: 5.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1060099114  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVfTQEERYKMVQ 81
Cdd:PRK01170    7 GTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPI-PYEDRKRKLE 58
 
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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