|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
86-281 |
4.65e-96 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 287.61 E-value: 4.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 86 STPFSYPINDPPEGRPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCK 165
Cdd:PLN02413 12 ASSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 166 WVDEVLENAPWVITPEFLEEHKIDFVAHDDIPYAsDDSG---DIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYV 242
Cdd:PLN02413 92 WVDEVIPDAPWVITQEFLDKHRIDYVAHDALPYA-DASGagkDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYV 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 295442802 243 MRNLARGVNRKELNVSLFKKNELDLRHHIKVLRDTLRNH 281
Cdd:PLN02413 171 MRNLARGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQ 209
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
100-249 |
9.41e-90 |
|
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: 265.97 E-value: 9.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 100 RPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVIT 179
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 180 PEFLEEHKIDFVAHDDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRNLARG 249
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
105-233 |
5.84e-34 |
|
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: 122.04 E-value: 5.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 105 YADGVFDLFHIGHMRQLEQAKKVFPNVhLIVGLPNDQLTHRLKgLTVMNDKERAEALRHCKWVDEVLENAPWVITPEFLE 184
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 295442802 185 EHKIDFVAHDDIPYAS--DDSGDIYLPVKKVG-----KFIPTKRTEGVSTSDLITR 233
Cdd:pfam01467 79 ELNPDVLVIGADSLLDfwYELDEILGNVKLVVvvrpvFFIPLKPTNGISSTDIRER 134
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
103-170 |
5.38e-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: 85.44 E-value: 5.38e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295442802 103 RVYADGVFDLFHIGHMRQLEQAKKVFPnvHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEV 170
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
102-234 |
1.20e-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: 86.31 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 102 VRVYADGVFDLFHIGHMRQLEQAKKVFPnvHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITpE 181
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 295442802 182 FLEEHKIDFVAH-DDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRI 234
Cdd:COG0615 78 DIEEIKPDVIVLgDDWKGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
86-281 |
4.65e-96 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 287.61 E-value: 4.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 86 STPFSYPINDPPEGRPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCK 165
Cdd:PLN02413 12 ASSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 166 WVDEVLENAPWVITPEFLEEHKIDFVAHDDIPYAsDDSG---DIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYV 242
Cdd:PLN02413 92 WVDEVIPDAPWVITQEFLDKHRIDYVAHDALPYA-DASGagkDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYV 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 295442802 243 MRNLARGVNRKELNVSLFKKNELDLRHHIKVLRDTLRNH 281
Cdd:PLN02413 171 MRNLARGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQ 209
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
100-249 |
9.41e-90 |
|
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: 265.97 E-value: 9.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 100 RPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVIT 179
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 180 PEFLEEHKIDFVAHDDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRNLARG 249
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
97-235 |
4.62e-35 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 131.45 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 97 PEGRP--VRVYADGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENA 174
Cdd:PTZ00308 5 PPKKPgtIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295442802 175 PWVITPEFLEEHKIDFVAH-DDIPYASDDSgDIYLPVKKVGKFIPTKRTEGVSTSDLITRII 235
Cdd:PTZ00308 83 PYTTRLEDLERLECDFVVHgDDISVDLNGR-NSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
105-233 |
5.84e-34 |
|
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: 122.04 E-value: 5.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 105 YADGVFDLFHIGHMRQLEQAKKVFPNVhLIVGLPNDQLTHRLKgLTVMNDKERAEALRHCKWVDEVLENAPWVITPEFLE 184
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 295442802 185 EHKIDFVAHDDIPYAS--DDSGDIYLPVKKVG-----KFIPTKRTEGVSTSDLITR 233
Cdd:pfam01467 79 ELNPDVLVIGADSLLDfwYELDEILGNVKLVVvvrpvFFIPLKPTNGISSTDIRER 134
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
104-245 |
1.78e-32 |
|
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: 118.90 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 104 VYADGVFDLFHIGHMRQLEQAKKVFPnvHLIVGLPNDQLTHRLKGLT--VMNDKERAEALRHCKWVDEVLENAPWVITPE 181
Cdd:cd02173 5 VYVDGAFDLFHIGHIEFLEKARELGD--YLIVGVHDDQTVNEYKGSNypIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295442802 182 FLEEHKIDFVAHDDIPYASD--DSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRN 245
Cdd:cd02173 83 LIEHFKIDVVVHGKTEETPDslDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
100-235 |
1.46e-30 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 120.56 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 100 RPVRVYADGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVIT 179
Cdd:PLN02406 52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 180 PEFL----EEHKIDFVAHDDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRII 235
Cdd:PLN02406 130 EEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRML 189
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
101-235 |
4.42e-29 |
|
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: 109.30 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 101 PVRVYADGVFDLFHIGHMRQLEQAKKVFPnvHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITP 180
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 295442802 181 EFLEEHKiDFVAHDDIPYASDDSGDIYLPVKKVGKFI--PTKRTEGVSTSDLITRII 235
Cdd:cd02170 79 PLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIevPRKKTEGISSSDIIKRIL 134
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
96-245 |
4.72e-23 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 98.32 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 96 PPEGRPVrVYADGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQLTHRLKG--LTVMNDKERAEALRHCKWVDEVLEN 173
Cdd:PTZ00308 188 PKPGDRI-VYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGsnYPIMNLNERVLGVLSCRYVDEVVIG 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295442802 174 APWVITPEFLEEHKIDFVAH--DDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRN 245
Cdd:PTZ00308 265 APFDVTKEVIDSLHINVVVGgkFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQ 338
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
103-170 |
5.38e-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: 85.44 E-value: 5.38e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295442802 103 RVYADGVFDLFHIGHMRQLEQAKKVFPnvHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEV 170
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
102-234 |
1.20e-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: 86.31 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 102 VRVYADGVFDLFHIGHMRQLEQAKKVFPnvHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITpE 181
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKALGD--ELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 295442802 182 FLEEHKIDFVAH-DDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRI 234
Cdd:COG0615 78 DIEEIKPDVIVLgDDWKGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
104-253 |
2.53e-18 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 85.50 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 104 VYADGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQL--THRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITPE 181
Cdd:PLN02406 254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295442802 182 FLEEHKIDFVAHDDIPYASD---DSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRNLARGVNRK 253
Cdd:PLN02406 332 MITTFNISLVVHGTVAENNDflkGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEK 406
|
|
| RfaE_N |
cd02172 |
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ... |
97-239 |
2.21e-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: 66.67 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 97 PEGRPVrVYADGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEV-LENAP 175
Cdd:cd02172 1 QRGKTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVvLFDNP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295442802 176 WVItpEFLEEHKIDFVA--HDDIPYASDDSGDIYLP---VKKVGKFIPTKRTEGVSTSDLITRIIRDYD 239
Cdd:cd02172 78 TAL--EIIDALQPNIYVkgGDYENPENDVTGKIAPEaeaVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
99-230 |
2.01e-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: 63.66 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295442802 99 GRPVRVYadGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVI 178
Cdd:cd02171 1 MKVVITY--GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQ 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 295442802 179 TPEFLEEHKID-FVAHDD----IPYASDDSGDIYLPvkkvgkfiptkRTEGVSTSDL 230
Cdd:cd02171 77 KIEDIKKYNVDvFVMGDDwegkFDFLKEYCEVVYLP-----------RTKGISSTQL 122
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
104-148 |
7.02e-05 |
|
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: 44.43 E-value: 7.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 295442802 104 VYADGVFDLFHIGHMRQLEQAKKVfpNVHLIVGLPNDQLTHRLKG 148
Cdd:PRK11316 343 VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKG 385
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