|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
52-294 |
3.10e-106 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 313.04 E-value: 3.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 52 PVDRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPW 131
Cdd:PLN02413 23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 132 TLTPEFLEKHKIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 209
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 210 LNVSFINEKKYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLElfgpdgawkqMFQERSSR 289
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLE----------KFEEGCHK 252
|
....*
gi 569010043 290 MLQAL 294
Cdd:PLN02413 253 MGTAI 257
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
55-204 |
2.08e-95 |
|
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: 279.84 E-value: 2.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 55 RPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 134
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 135 PEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 204
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
60-188 |
2.37e-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: 122.81 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 60 YADGIFDLFHSGHARALMQAKTLFPNSyLLVGVCSDDLTHKFKGfTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLE 139
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 569010043 140 KHKIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FVPTQRTEGISTSDIITR 188
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
57-189 |
5.74e-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: 87.08 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 57 VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTpE 136
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569010043 137 FLEKHKIDFVAHddipyssaGSDDVY--KHIKEAGMFVPT-------QRTEGISTSDIITRI 189
Cdd:COG0615 78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
58-125 |
2.12e-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: 83.51 E-value: 2.12e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569010043 58 RVYADGIFDLFHSGHARALMQAKTLFPnsYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV 125
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
52-294 |
3.10e-106 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 313.04 E-value: 3.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 52 PVDRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPW 131
Cdd:PLN02413 23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 132 TLTPEFLEKHKIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 209
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 210 LNVSFINEKKYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLElfgpdgawkqMFQERSSR 289
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLE----------KFEEGCHK 252
|
....*
gi 569010043 290 MLQAL 294
Cdd:PLN02413 253 MGTAI 257
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
55-204 |
2.08e-95 |
|
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: 279.84 E-value: 2.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 55 RPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 134
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 135 PEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 204
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
51-190 |
1.53e-40 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 145.70 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 51 TPVDRP--VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRD 128
Cdd:PTZ00308 4 IPPKKPgtIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569010043 129 APWTLTPEFLEKHKIDFVAH-DDIPYSSAGsDDVYKHIKEAGMFVPTQRTEGISTSDIITRIV 190
Cdd:PTZ00308 82 YPYTTRLEDLERLECDFVVHgDDISVDLNG-RNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
59-200 |
3.95e-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: 130.84 E-value: 3.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 59 VYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKG--FTVMNEAERYEALRHCRYVDEVIRDAPWTLTPE 136
Cdd:cd02173 5 VYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGsnYPIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569010043 137 FLEKHKIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRN 200
Cdd:cd02173 83 LIEHFKIDVVVHgkTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
60-188 |
2.37e-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: 122.81 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 60 YADGIFDLFHSGHARALMQAKTLFPNSyLLVGVCSDDLTHKFKGfTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLE 139
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 569010043 140 KHKIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FVPTQRTEGISTSDIITR 188
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
55-189 |
1.20e-30 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 120.56 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 55 RPVRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 134
Cdd:PLN02406 52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 569010043 135 PEFL----EKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRI 189
Cdd:PLN02406 130 EEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRM 188
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
52-211 |
1.19e-28 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 113.73 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 52 PVDRPVRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKG--FTVMNEAERYEALRHCRYVDEVIRDA 129
Cdd:PTZ00308 188 PKPGDRIVYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGsnYPIMNLNERVLGVLSCRYVDEVVIGA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 130 PWTLTPEFLEKHKIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRgyTA 207
Cdd:PTZ00308 266 PFDVTKEVIDSLHINVVVGgkFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKK--RA 343
|
....
gi 569010043 208 KELN 211
Cdd:PTZ00308 344 KEIK 347
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
56-189 |
4.29e-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: 103.91 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 56 PVRVYADGIFDLFHSGHARALMQAKTLFpnSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTP 135
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 569010043 136 EFLEKHKiDFVAHDDIPYSSAGSDDVYKHIKEAGMF--VPTQRTEGISTSDIITRI 189
Cdd:cd02170 79 PLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVieVPRKKTEGISSSDIIKRI 133
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
59-216 |
5.51e-24 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 101.68 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 59 VYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDL--THKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPE 136
Cdd:PLN02406 254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 137 FLEKHKIDFVAHDDIPYSS---AGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE--LN 211
Cdd:PLN02406 332 MITTFNISLVVHGTVAENNdflKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRyyES 411
|
....*
gi 569010043 212 VSFIN 216
Cdd:PLN02406 412 KSFVS 416
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
57-189 |
5.74e-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: 87.08 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 57 VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTpE 136
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569010043 137 FLEKHKIDFVAHddipyssaGSDDVY--KHIKEAGMFVPT-------QRTEGISTSDIITRI 189
Cdd:COG0615 78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
58-125 |
2.12e-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: 83.51 E-value: 2.12e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569010043 58 RVYADGIFDLFHSGHARALMQAKTLFPnsYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV 125
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
63-185 |
1.42e-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: 64.04 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 63 GIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHK 142
Cdd:cd02171 8 GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 569010043 143 ID-FVAHDDIpyssAGSDDVYKHIKEAgMFVPtqRTEGISTSDI 185
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 ... |
55-194 |
2.04e-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: 58.20 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 55 RPVrVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV-IRDAPW-- 131
Cdd:cd02172 4 KTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVvLFDNPTal 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569010043 132 ----TLTPEFLEKhKIDFVAHDD--IPYSSAGSDDVYKHikeAGMFVPTQrTEGISTSDIITRIVRDYD 194
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 ... |
41-189 |
1.08e-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: 50.21 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 41 KLTVAQARL-GTPVdrpvrVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFT--VMNEAERYEALR 117
Cdd:PRK11316 329 KLAVAQARArGEKI-----VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKGEGrpVNPLEQRMAVLA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569010043 118 HCRYVDEVI---RDAPWTL----TPEFLEK---HKIdfvahDDIpyssAGSDDVYKHIKEAGM--FVptqrtEGISTSDI 185
Cdd:PRK11316 402 ALEAVDWVVpfeEDTPQRLiaeiLPDLLVKggdYKP-----EEI----AGSKEVWANGGEVKVlnFE-----DGCSTTNI 467
|
....
gi 569010043 186 ITRI 189
Cdd:PRK11316 468 IKKI 471
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
63-135 |
5.12e-04 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 39.82 E-value: 5.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569010043 63 GIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRhcRYVDEVIRDAPWTLTP 135
Cdd:PRK00777 8 GTFDPLHDGHRALLRKAFEL--GKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYEIVK 76
|
|
| PPAT_CoAS |
cd02164 |
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ... |
63-118 |
8.74e-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: 8.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 569010043 63 GIFDLFHSGHARALMQAkTLFPNSYLLVGVCSDDLThKFKGFTVMNE--AERYEALRH 118
Cdd:cd02164 6 GTFDRLHDGHKILLSVA-FLLAGEKLIIGVTSDELL-KNKSLKELIEpyEERIANLHE 61
|
|
| |
