|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
101-343 |
1.18e-107 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 317.27 E-value: 1.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 101 PVDRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPW 180
Cdd:PLN02413 23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 181 TLTPEFLEKHKIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 258
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 259 LNVSFINEKKYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLElfgpdgawkqMFQERSSR 338
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLE----------KFEEGCHK 252
|
....*
gi 1126493986 339 MLQAL 343
Cdd:PLN02413 253 MGTAI 257
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
104-253 |
2.10e-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: 285.62 E-value: 2.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 104 RPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 183
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 184 PEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 253
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
109-237 |
7.07e-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: 124.74 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 109 YADGIFDLFHSGHARALMQAKTLFPNSyLLVGVCSDDLTHKfKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLE 188
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHK-LKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1126493986 189 KHKIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FVPTQRTEGISTSDIITR 237
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
106-238 |
1.16e-21 |
|
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: 89.39 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 106 VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTpE 185
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126493986 186 FLEKHKIDFVAHddipyssaGSDDVY--KHIKEAGMFVPT-------QRTEGISTSDIITRI 238
Cdd:COG0615 78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
107-174 |
1.33e-20 |
|
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: 84.28 E-value: 1.33e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126493986 107 RVYADGIFDLFHSGHARALMQAKTLFPnsYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV 174
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
101-343 |
1.18e-107 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 317.27 E-value: 1.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 101 PVDRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPW 180
Cdd:PLN02413 23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 181 TLTPEFLEKHKIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 258
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 259 LNVSFINEKKYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLElfgpdgawkqMFQERSSR 338
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLE----------KFEEGCHK 252
|
....*
gi 1126493986 339 MLQAL 343
Cdd:PLN02413 253 MGTAI 257
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
104-253 |
2.10e-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: 285.62 E-value: 2.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 104 RPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 183
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 184 PEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 253
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
100-239 |
6.73e-41 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 146.85 E-value: 6.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 100 TPVDRP--VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRD 177
Cdd:PTZ00308 4 IPPKKPgtIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126493986 178 APWTLTPEFLEKHKIDFVAH-DDIPYSSAGsDDVYKHIKEAGMFVPTQRTEGISTSDIITRIV 239
Cdd:PTZ00308 82 YPYTTRLEDLERLECDFVVHgDDISVDLNG-RNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
108-249 |
1.10e-37 |
|
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: 132.38 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 108 VYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKG--FTVMNEAERYEALRHCRYVDEVIRDAPWTLTPE 185
Cdd:cd02173 5 VYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGsnYPIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126493986 186 FLEKHKIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRN 249
Cdd:cd02173 83 LIEHFKIDVVVHgkTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
109-237 |
7.07e-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: 124.74 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 109 YADGIFDLFHSGHARALMQAKTLFPNSyLLVGVCSDDLTHKfKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLE 188
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHK-LKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1126493986 189 KHKIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FVPTQRTEGISTSDIITR 237
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
104-238 |
8.82e-31 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 120.94 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 104 RPVRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 183
Cdd:PLN02406 52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1126493986 184 PEFL----EKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRI 238
Cdd:PLN02406 130 EEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRM 188
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
101-260 |
6.44e-29 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 114.88 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 101 PVDRPVRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKG--FTVMNEAERYEALRHCRYVDEVIRDA 178
Cdd:PTZ00308 188 PKPGDRIVYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGsnYPIMNLNERVLGVLSCRYVDEVVIGA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 179 PWTLTPEFLEKHKIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRgyTA 256
Cdd:PTZ00308 266 PFDVTKEVIDSLHINVVVGgkFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKK--RA 343
|
....
gi 1126493986 257 KELN 260
Cdd:PTZ00308 344 KEIK 347
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
105-238 |
1.62e-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: 105.07 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 105 PVRVYADGIFDLFHSGHARALMQAKTLFpnSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTP 184
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1126493986 185 EFLEKHKiDFVAHDDIPYSSAGSDDVYKHIKEAGMF--VPTQRTEGISTSDIITRI 238
Cdd:cd02170 79 PLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVieVPRKKTEGISSSDIIKRI 133
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
108-265 |
4.53e-24 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 102.45 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 108 VYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDL--THKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPE 185
Cdd:PLN02406 254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 186 FLEKHKIDFVAHDDIPYSS---AGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE--LN 260
Cdd:PLN02406 332 MITTFNISLVVHGTVAENNdflKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRyyES 411
|
....*
gi 1126493986 261 VSFIN 265
Cdd:PLN02406 412 KSFVS 416
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
106-238 |
1.16e-21 |
|
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: 89.39 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 106 VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTpE 185
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126493986 186 FLEKHKIDFVAHddipyssaGSDDVY--KHIKEAGMFVPT-------QRTEGISTSDIITRI 238
Cdd:COG0615 78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
107-174 |
1.33e-20 |
|
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: 84.28 E-value: 1.33e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126493986 107 RVYADGIFDLFHSGHARALMQAKTLFPnsYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV 174
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
112-234 |
4.74e-13 |
|
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.
Pssm-ID: 173922 [Multi-domain] Cd Length: 129 Bit Score: 65.58 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 112 GIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHK 191
Cdd:cd02171 8 GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1126493986 192 ID-FVAHDDIpyssAGSDDVYKHIKEAgMFVPtqRTEGISTSDI 234
Cdd:cd02171 86 VDvFVMGDDW----EGKFDFLKEYCEV-VYLP--RTKGISSTQL 122
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
104-243 |
1.96e-10 |
|
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: 58.58 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 104 RPVrVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV-IRDAPW-- 180
Cdd:cd02172 4 KTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVvLFDNPTal 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126493986 181 ----TLTPEFLEKhKIDFVAHDD--IPYSSAGSDDVYKHikeAGMFVPTQrTEGISTSDIITRIVRDYD 243
Cdd:cd02172 81 eiidALQPNIYVK-GGDYENPENdvTGKIAPEAEAVKAY---GGKIVFTG-EIVFSSSALINRIFDELD 144
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
90-238 |
1.74e-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: 49.44 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 90 KLTIAQARL-GTPVdrpvrVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFT--VMNEAERYEALR 166
Cdd:PRK11316 329 KLAVAQARArGEKI-----VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKGEGrpVNPLEQRMAVLA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 167 HCRYVDEVI---RDAPWTL----TPEFLEK---HKIdfvahDDIpyssAGSDDVYKHIKEAGM--FVptqrtEGISTSDI 234
Cdd:PRK11316 402 ALEAVDWVVpfeEDTPQRLiaeiLPDLLVKggdYKP-----EEI----AGSKEVWANGGEVKVlnFE-----DGCSTTNI 467
|
....
gi 1126493986 235 ITRI 238
Cdd:PRK11316 468 IKKI 471
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
112-204 |
4.40e-04 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 40.20 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126493986 112 GIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRhcRYVDEVIRDAPW----------- 180
Cdd:PRK00777 8 GTFDPLHDGHRALLRKAFEL--GKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYeivkiddpygp 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1126493986 181 TLTPEF---------------------------LEKHKIDFV-AHDDIPYSS 204
Cdd:PRK00777 84 ALEDDFdaivvspetypgalkineirrerglkpLEIVVIDFVlAEDGKPISS 135
|
|
| PPAT_CoAS |
cd02164 |
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ... |
112-167 |
9.15e-03 |
|
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.
Pssm-ID: 173915 Cd Length: 143 Bit Score: 36.10 E-value: 9.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1126493986 112 GIFDLFHSGHARALMQAkTLFPNSYLLVGVCSDDLThKFKGFTVMNE--AERYEALRH 167
Cdd:cd02164 6 GTFDRLHDGHKILLSVA-FLLAGEKLIIGVTSDELL-KNKSLKELIEpyEERIANLHE 61
|
|
| |
