|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
21-274 |
0e+00 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 530.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 21 SDRPVRVYADGIYDLFHFGHARSLEQAKKSFPNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWV 100
Cdd:PLN02413 24 SDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 101 INQEFLDKHKIDFVAHDALPYADASGAGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRNLDRGYTRKEL 180
Cdd:PLN02413 104 ITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKDL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 181 NVSYVKEKRLRVNMRLKKLQEKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRLVAGFLEMFEEGCHKMGTAIRDRIQE 260
Cdd:PLN02413 184 GVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEGCHKMGTAIKDRIQE 263
|
250
....*....|....
gi 1954696126 261 RLRGQQSRDLLQNG 274
Cdd:PLN02413 264 RLMRQQSSGLLELL 277
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
23-174 |
2.30e-93 |
|
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: 273.29 E-value: 2.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 23 RPVRVYADGIYDLFHFGHARSLEQAKKSFPNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVIN 102
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1954696126 103 QEFLDKHKIDFVAHDALPYADASgaGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRNLDRG 174
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDAD--GEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
28-158 |
4.78e-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: 123.58 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 28 YADGIYDLFHFGHARSLEQAKKSFPNTyLLVGCCNDEITRKfKGKTVMTESERYESLRHCKWVDEVIPDAPWVINQEFLD 107
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHK-LKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 108 KHKIDFVAHDALPYADASGAGNDVYEFVKKAG-----KFKETKRTEGISTSDIIMR 158
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFWYELDEILGNVKLVVvvrpvFFIPLKPTNGISSTDIRER 134
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
26-93 |
2.85e-19 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 80.04 E-value: 2.85e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954696126 26 RVYADGIYDLFHFGHARSLEQAKKSFPntYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEV 93
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
25-159 |
8.55e-17 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 75.14 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 25 VRVYADGIYDLFHFGHARSLEQAKKsfPNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWvinqE 104
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKA--LGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEW----D 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 105 FLD---KHKIDFVAH--------DALpyadasgagNDVYEFVKKAGKFKETKRTEGISTSDIIMRI 159
Cdd:COG0615 75 KFEdieEIKPDVIVLgddwkgdfDFL---------KEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
21-274 |
0e+00 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 530.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 21 SDRPVRVYADGIYDLFHFGHARSLEQAKKSFPNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWV 100
Cdd:PLN02413 24 SDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 101 INQEFLDKHKIDFVAHDALPYADASGAGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRNLDRGYTRKEL 180
Cdd:PLN02413 104 ITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKDL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 181 NVSYVKEKRLRVNMRLKKLQEKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRLVAGFLEMFEEGCHKMGTAIRDRIQE 260
Cdd:PLN02413 184 GVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEGCHKMGTAIKDRIQE 263
|
250
....*....|....
gi 1954696126 261 RLRGQQSRDLLQNG 274
Cdd:PLN02413 264 RLMRQQSSGLLELL 277
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
23-174 |
2.30e-93 |
|
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: 273.29 E-value: 2.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 23 RPVRVYADGIYDLFHFGHARSLEQAKKSFPNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVIN 102
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1954696126 103 QEFLDKHKIDFVAHDALPYADASgaGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRNLDRG 174
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDAD--GEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
25-160 |
1.47e-43 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 152.63 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 25 VRVYADGIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVINQE 104
Cdd:PTZ00308 12 IRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 105 FLDKHKIDFVAHDALPYADASgaGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIV 160
Cdd:PTZ00308 90 DLERLECDFVVHGDDISVDLN--GRNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
28-158 |
4.78e-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: 123.58 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 28 YADGIYDLFHFGHARSLEQAKKSFPNTyLLVGCCNDEITRKfKGKTVMTESERYESLRHCKWVDEVIPDAPWVINQEFLD 107
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHK-LKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 108 KHKIDFVAHDALPYADASGAGNDVYEFVKKAG-----KFKETKRTEGISTSDIIMR 158
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFWYELDEILGNVKLVVvvrpvFFIPLKPTNGISSTDIRER 134
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
27-170 |
5.53e-35 |
|
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: 124.29 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 27 VYADGIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGKT--VMTESERYESLRHCKWVDEVIPDAPWVINQE 104
Cdd:cd02173 5 VYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNypIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 105 FLDKHKIDFVAHDALPYADASGAGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRN 170
Cdd:cd02173 83 LIEHFKIDVVVHGKTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
23-159 |
1.24e-34 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 130.19 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 23 RPVRVYADGIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVIN 102
Cdd:PLN02406 52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954696126 103 QEFL----DKHKIDFVAH--DALPYADasgaGNDVYEFVKKAGKFKETKRTEGISTSDIIMRI 159
Cdd:PLN02406 130 EEFMnklfNEYNIDYIIHgdDPCLLPD----GTDAYALAKKAGRYKQIKRTEGVSSTDIVGRM 188
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
24-159 |
3.83e-26 |
|
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.
Pssm-ID: 173921 [Multi-domain] Cd Length: 136 Bit Score: 100.44 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 24 PVRVYADGIYDLFHFGHARSLEQAKKSFpnTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVINQ 103
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 104 EFLDKHKiDFVAH--DALPYADASgagnDVYEFVKKAGKFKET--KRTEGISTSDIIMRI 159
Cdd:cd02170 79 PLEELKP-DVIVLgdDQKNGVDEE----EVYEELKKRGKVIEVprKKTEGISSSDIIKRI 133
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
27-170 |
6.88e-25 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 102.56 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 27 VYADGIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGKT--VMTESERYESLRHCKWVDEVIPDAPWVINQE 104
Cdd:PTZ00308 195 VYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGSNypIMNLNERVLGVLSCRYVDEVVIGAPFDVTKE 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 105 FLDKHKIDFVAHDALPYADASGAGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRN 170
Cdd:PTZ00308 273 VIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQ 338
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
27-185 |
2.13e-20 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 90.90 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 27 VYADGIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGK--TVMTESERYESLRHCKWVDEVIPDAPWVINQE 104
Cdd:PLN02406 254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTVSAHRGAhrPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 105 FLDKHKIDFVAHDAL-PYADASGAGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYNQYVMRNLDRGYTRKE--LN 181
Cdd:PLN02406 332 MITTFNISLVVHGTVaENNDFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRyyES 411
|
....
gi 1954696126 182 VSYV 185
Cdd:PLN02406 412 KSFV 415
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
26-93 |
2.85e-19 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 80.04 E-value: 2.85e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954696126 26 RVYADGIYDLFHFGHARSLEQAKKSFPntYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEV 93
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
25-159 |
8.55e-17 |
|
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440380 [Multi-domain] Cd Length: 131 Bit Score: 75.14 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 25 VRVYADGIYDLFHFGHARSLEQAKKsfPNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWvinqE 104
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKA--LGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEW----D 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954696126 105 FLD---KHKIDFVAH--------DALpyadasgagNDVYEFVKKAGKFKETKRTEGISTSDIIMRI 159
Cdd:COG0615 75 KFEdieEIKPDVIVLgddwkgdfDFL---------KEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
31-155 |
4.18e-12 |
|
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: 62.50 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 31 GIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVINQEFLDKHK 110
Cdd:cd02171 8 GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1954696126 111 ID-FVAHDalpyaDASGAgndvYEFVKKAGKFKETKRTEGISTSDI 155
Cdd:cd02171 86 VDvFVMGD-----DWEGK----FDFLKEYCEVVYLPRTKGISSTQL 122
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
20-164 |
2.22e-08 |
|
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: 52.42 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954696126 20 QSDRPVrVYADGIYDLFHFGHARSLEQAKKSfpNTYLLVGCCNDEITRKFKGKTVMTESERYESLRHCKWVDEV-IPDAP 98
Cdd:cd02172 1 QRGKTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVvLFDNP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954696126 99 WVInqEFLDKHKIDFVA--HD-ALPYADASGAGNDVYEFVKKAGKFKETKRTEGISTSDIIMRIVKDYN 164
Cdd:cd02172 78 TAL--EIIDALQPNIYVkgGDyENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
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