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Conserved domains on  [gi|167520029|ref|XP_001744354|]
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uncharacterized protein MONBRDRAFT_20281 [Monosiga brevicollis MX1]

Protein Classification

ethanolamine-phosphate cytidylyltransferase( domain architecture ID 11488366)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 5-356 0e+00

ethanolamine-phosphate cytidylyltransferase; Provisional


:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 605.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   5 SPKAAKRQP--TRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVT 82
Cdd:PTZ00308   1 TSPIPPKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  83 DAPYTFNLDFLEQNNCDFVVHGDDITTNADGEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRMLLMTRTHHqqddgDAKLS 162
Cdd:PTZ00308  81 GYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL-----LKSVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 163 TSKLSASDSPYTGTSQLLANSKRIVQFSTQREPKDTDVIGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRN 242
Cdd:PTZ00308 156 EVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 243 HGSNYPIMNLQERTLSILACRYVDDVVIGAPEAITEELLDYFKITKVFHGSTGVL--KPSGADPYQVAIDRGIFVHVESH 320
Cdd:PTZ00308 236 KGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLvnEEGGSDPYEVPKAMGIFKEVDSG 315

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 167520029 321 SDLTTEIIVDRIIKNRLNFAQRNAKKTQREVDRILR 356
Cdd:PTZ00308 316 CDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEI 351
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 5-356 0e+00

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 605.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   5 SPKAAKRQP--TRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVT 82
Cdd:PTZ00308   1 TSPIPPKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  83 DAPYTFNLDFLEQNNCDFVVHGDDITTNADGEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRMLLMTRTHHqqddgDAKLS 162
Cdd:PTZ00308  81 GYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL-----LKSVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 163 TSKLSASDSPYTGTSQLLANSKRIVQFSTQREPKDTDVIGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRN 242
Cdd:PTZ00308 156 EVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 243 HGSNYPIMNLQERTLSILACRYVDDVVIGAPEAITEELLDYFKITKVFHGSTGVL--KPSGADPYQVAIDRGIFVHVESH 320
Cdd:PTZ00308 236 KGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLvnEEGGSDPYEVPKAMGIFKEVDSG 315

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 167520029 321 SDLTTEIIVDRIIKNRLNFAQRNAKKTQREVDRILR 356
Cdd:PTZ00308 316 CDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEI 351
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 13-156 1.12e-86

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: 258.27  E-value: 1.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  13 PTRVYADGCFDLMHFGHANALRQAKALG--DILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFNL 90
Cdd:cd02174    2 PVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTTP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167520029  91 DFLEQNNCDFVVHGDDITTNADGEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRMLLMTRTHHQQDD 156
Cdd:cd02174   82 EFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNL 147
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 14-144 5.37e-32

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: 116.74  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  14 TRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFnLDFL 93
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDK-FEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167520029  94 EQNNCDFVVHGDDITTNADG-EDAYHIAKKSGRYKEYQRTQGVSTTDIVGRM 144
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 17-143 3.90e-28

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


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 106.63  E-value: 3.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   17 YADGCFDLMHFGHANALRQAKALGDI-LVVGIHNDEDIeKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFNLDFLEQ 95
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPP-HKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167520029   96 NNCDFVVHGDDITTNADGE-----DAYHIAKKSGR--YKEYQRTQGVSTTDIVGR 143
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYEldeilGNVKLVVVVRPvfFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 15-80 7.29e-21

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 85.05  E-value: 7.29e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167520029   15 RVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEV 80
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 5-356 0e+00

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 605.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   5 SPKAAKRQP--TRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVT 82
Cdd:PTZ00308   1 TSPIPPKKPgtIRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  83 DAPYTFNLDFLEQNNCDFVVHGDDITTNADGEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRMLLMTRTHHqqddgDAKLS 162
Cdd:PTZ00308  81 GYPYTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHL-----LKSVD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 163 TSKLSASDSPYTGTSQLLANSKRIVQFSTQREPKDTDVIGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRN 242
Cdd:PTZ00308 156 EVQLESSLFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 243 HGSNYPIMNLQERTLSILACRYVDDVVIGAPEAITEELLDYFKITKVFHGSTGVL--KPSGADPYQVAIDRGIFVHVESH 320
Cdd:PTZ00308 236 KGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFSDLvnEEGGSDPYEVPKAMGIFKEVDSG 315

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 167520029 321 SDLTTEIIVDRIIKNRLNFAQRNAKKTQREVDRILR 356
Cdd:PTZ00308 316 CDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQEI 351
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 6-350 2.19e-128

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 374.40  E-value: 2.19e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   6 PKAAKRQPTRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAP 85
Cdd:PLN02406  46 KKKKKKKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  86 YTFNLDFL----EQNNCDFVVHGDDITTNADGEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRMLLMTR--------THHQ 153
Cdd:PLN02406 126 YAITEEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRersisdshNHSS 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 154 QDDGDAKLSTSKLSASDSPYTGTSQLLANSKRIVQFSTQREPKDTDVIGYMPGAFDLLHTGHVAALEAARQQCDYLIVGL 233
Cdd:PLN02406 206 LQRQFSHGHSQFEDGGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGI 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 234 HTDRTVNRNHGSNYPIMNLQERTLSILACRYVDDVVIGAPEAITEELLDYFKITKVFHG---STGVLKPSGADPYQVAID 310
Cdd:PLN02406 286 HTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGtvaENNDFLKGEDDPYAVPKS 365

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 167520029 311 RGIFVHVESHSDLTTEIIVDRIIKNRLNFAQRNAKKTQRE 350
Cdd:PLN02406 366 MGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 13-156 1.12e-86

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: 258.27  E-value: 1.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  13 PTRVYADGCFDLMHFGHANALRQAKALG--DILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFNL 90
Cdd:cd02174    2 PVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTTP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167520029  91 DFLEQNNCDFVVHGDDITTNADGEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRMLLMTRTHHQQDD 156
Cdd:cd02174   82 EFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNL 147
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 199-346 6.26e-71

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: 218.28  E-value: 6.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 199 DVIGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNHGSNYPIMNLQERTLSILACRYVDDVVIGAPEAITE 278
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 279 ELLDYFKITKVFHGSTGVLKPS--GADPYQVAIDRGIFVHVESHSDLTTEIIVDRIIKNRLNFAQRNAKK 346
Cdd:cd02173   82 ELIEHFKIDVVVHGKTEETPDSldGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKK 151
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 4-145 8.77e-43

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 150.48  E-value: 8.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   4 ASPKAAKRQPTRVYADGCFDLMHFGHANALRQAKAL--GDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVV 81
Cdd:PLN02413  18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVI 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167520029  82 TDAPYTFNLDFLEQNNCDFVVHgdDITTNAD----GEDAYHIAKKSGRYKEYQRTQGVSTTDIVGRML 145
Cdd:PLN02413  98 PDAPWVITQEFLDKHRIDYVAH--DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 13-147 4.11e-40

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: 138.19  E-value: 4.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  13 PTRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFNLDF 92
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 167520029  93 LEQNNcDFVVHGDDITTNADGEDAYHIAKKSGRYKE--YQRTQGVSTTDIVGRMLLM 147
Cdd:cd02170   81 EELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEvpRKKTEGISSSDIIKRILEL 136
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 203-346 1.04e-32

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


Pssm-ID: 173925  Cd Length: 150  Bit Score: 119.21  E-value: 1.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 203 YMPGAFDLLHTGHVAALEAARQ--QCDYLIVGLHTDRTVNRNHGSnyPIMNLQERTLSILACRYVDDVVIGAPEAITEEL 280
Cdd:cd02174    6 YVDGCFDLFHYGHANALRQAKKlgPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPEF 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167520029 281 LDYFKITKVFHGSTGVLKPSGADPYQVAIDRGIFVHVE-SHSDLTTEIIvDRIIKNRLNFAQRNAKK 346
Cdd:cd02174   84 LDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKrTEGVSTTDLI-GRILLDYRDYHRRNLQR 149
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 14-144 5.37e-32

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: 116.74  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  14 TRVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFnLDFL 93
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDK-FEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167520029  94 EQNNCDFVVHGDDITTNADG-EDAYHIAKKSGRYKEYQRTQGVSTTDIVGRM 144
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFlKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 17-143 3.90e-28

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


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 106.63  E-value: 3.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029   17 YADGCFDLMHFGHANALRQAKALGDI-LVVGIHNDEDIeKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFNLDFLEQ 95
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPP-HKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167520029   96 NNCDFVVHGDDITTNADGE-----DAYHIAKKSGR--YKEYQRTQGVSTTDIVGR 143
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYEldeilGNVKLVVVVRPvfFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 15-80 7.29e-21

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 85.05  E-value: 7.29e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167520029   15 RVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEV 80
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 200-293 4.05e-20

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: 85.16  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 200 VIGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTvNRNHGSNyPIMNLQERtLSIL-ACRYVDDVVIGAPEAITE 278
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEF-VASKGRK-PIIPEEQR-KEIVeALKYVDEVILGEEWDKFE 77

                         90
                 ....*....|....*
gi 167520029 279 ELLDYfKITKVFHGS 293
Cdd:COG0615   78 DIEEI-KPDVIVLGD 91
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 206-334 2.22e-19

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: 83.11  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 206 GAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNHGSnyPIMNLQERTLSILACRYVDDVVIGAPEAITEELL---- 281
Cdd:cd02170    8 GTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSYFKPLEelkp 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167520029 282 DYfkitkVFHGSTGVLKPSGADPYQVAIDRGIFVHVESHSD--LTTEIIVDRIIK 334
Cdd:cd02170   86 DV-----IVLGDDQKNGVDEEEVYEELKKRGKVIEVPRKKTegISSSDIIKRILE 135
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 190-343 2.79e-18

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 83.84  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 190 STQREPKDTDVIGYMPGAFDLLHTGHVAALEAARQQC--DYLIVGLHTDRTVNRNHGSNypIMNLQERTLSILACRYVDD 267
Cdd:PLN02413  18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFpnTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167520029 268 VVIGAPEAITEELLDYFKITKVFHGSTGVLKPSGA--DPYQVAIDRGIFVHVESHSDLTTEIIVDRIIKNRLNFAQRN 343
Cdd:PLN02413  96 VIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAgkDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRN 173
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 201-268 4.38e-17

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 74.65  E-value: 4.38e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167520029  201 IGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNHGSnyPIMNLQERTLSILACRYVDDV 268
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 201-285 2.18e-15

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: 72.34  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  201 IGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNHGSNYPIMNLQERT--LSILACryVDDVVIgAPEAITE 278
Cdd:TIGR02199  13 IVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAevLAALSS--VDYVVI-FDEDTPE 89


                  ....*..
gi 167520029  279 ELLDYFK 285
Cdd:TIGR02199  90 ELIGELK 96
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 20-140 1.52e-14

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 69.44  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  20 GCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDAPYTFNLDFLEQNNCD 99
Cdd:cd02171    8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYNVD 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 167520029 100 FVVHGDdittnaDGEDAYHIAKKSGRYKEYQRTQGVSTTDI 140
Cdd:cd02171   88 VFVMGD------DWEGKFDFLKEYCEVVYLPRTKGISSTQL 122
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 206-282 2.00e-14

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


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 69.75  E-value: 2.00e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167520029 206 GAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNHGSnyPIMNLQERTLSILACRYVDDVVIgAPEAITEELLD 282
Cdd:cd02172   11 GVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGR--PIFPEDLRAEVLAALGFVDYVVL-FDNPTALEIID 84
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 16-141 7.25e-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: 65.13  E-value: 7.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  16 VYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKAVKWVDEVVTDaPYTFNLDFLEQ 95
Cdd:cd02172    7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVLF-DNPTALEIIDA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 167520029  96 NNCDFVVHGDDIttnADGEDAYHiaKKSGRYKEYQRTQG---VSTTDIV 141
Cdd:cd02172   86 LQPNIYVKGGDY---ENPENDVT--GKIAPEAEAVKAYGgkiVFTGEIV 129
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 203-292 8.62e-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: 61.95  E-value: 8.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  203 YMPGAFDLLHTGHVAALEAARQQCDY-LIVGLHTDRTVNRNhgsNYPIMNLQERTLSILACRYVDDVVIGAPEAITEELL 281
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKL---KRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELL 77

                          90
                  ....*....|.
gi 167520029  282 DYFKITKVFHG 292
Cdd:pfam01467  78 KELNPDVLVIG 88
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 16-81 7.88e-10

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 59.84  E-value: 7.88e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167520029  16 VYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGP--PVLTQEERYKLVKAVKWVDEVV 81
Cdd:PRK11316 343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPVNPLEQRMAVLAALEAVDWVV 410
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 206-269 9.17e-10

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 59.84  E-value: 9.17e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167520029 206 GAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNHGSNYPIMNLQER--TLSILACryVDDVV 269
Cdd:PRK11316 347 GCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRmaVLAALEA--VDWVV 410
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 200-285 2.68e-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: 49.02  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029 200 VIGYmpGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRtVNRNHGSNyPIMNLQERTLSILACRYVDDVVigaPEAITEE 279
Cdd:cd02171    4 VITY--GTFDLLHIGHLNLLERAKALGDKLIVAVSTDE-FNAGKGKK-AVIPYEQRAEILESIRYVDLVI---PETNWEQ 76


                 ....*.
gi 167520029 280 LLDYFK 285
Cdd:cd02171   77 KIEDIK 82
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
20-87 2.76e-06

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 46.75  E-value: 2.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167520029  20 GCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVLTQEERYKLVKavKWVDEVVTDAPYT 87
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYE 73
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
15-69 2.75e-04

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 42.50  E-value: 2.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167520029  15 RVYADGCFDLMHFGHANALRQAKALGDILVVGIHNDEDIEKNKGPPVlTQEERYK 69
Cdd:PRK01170   2 ITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPI-PYEDRKR 55
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
201-255 3.57e-03

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 39.03  E-value: 3.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167520029 201 IGYMPGAFDLLHTGHVAALEAARQQCDYLIVGLHTDRTVNRNhgSNYPImNLQER 255
Cdd:PRK01170   2 ITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKN--KVYPI-PYEDR 53
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 20-74 6.60e-03

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


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 35.98  E-value: 6.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167520029  20 GCFDLMHFGHANALRQAKALGDILVVGIhnDEDIEKNKGPPVLTQEERYKLVKAV 74
Cdd:cd02156    6 GEPGYLHIGHAKLICRAKGIADQCVVRI--DDNPPVKVWQDPHELEERKESIEED 58
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 20-106 8.46e-03

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


Pssm-ID: 185679 [Multi-domain]  Cd Length: 180  Bit Score: 36.75  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167520029  20 GCFDLMHFGH----ANALRQAKALGDILVVGI---HNDEDIEKNKGPPVLT-QEERYKLVKAVKwVDEVVTdAPYTFNL- 90
Cdd:cd02064    6 GNFDGVHLGHqaliKTLKKIARERGLPSAVLTfdpHPREVFLPDKAPPRLTtLEEKLELLESLG-VDYLLV-LPFDKEFa 83

                         90       100
                 ....*....|....*....|....*
gi 167520029  91 ---------DFLEQNNCDFVVHGDD 106
Cdd:cd02064   84 slsaeefveDLLVKLNAKHVVVGFD 108
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 201-233 9.08e-03

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 36.33  E-value: 9.08e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 167520029 201 IGYMPGAFDLLHTGHVAALEAARQQCDYLIVGL 233
Cdd:COG1056    4 RGLFIGRFQPFHLGHLAVIKWALEEVDELIIGI 36
 
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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