|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
72-314 |
1.93e-106 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 314.19 E-value: 1.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 72 PVDRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPW 151
Cdd:PLN02413 23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 152 TLTPEFLEKHKIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 229
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 230 LNVSFINEKKYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLElfgpdgawkqMFQERSSR 309
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLE----------KFEEGCHK 252
|
....*
gi 6164927 310 MLQAL 314
Cdd:PLN02413 253 MGTAI 257
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
75-224 |
4.34e-96 |
|
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: 282.53 E-value: 4.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 75 RPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 154
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 155 PEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 224
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
80-208 |
2.04e-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: 123.58 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 80 YADGIFDLFHSGHARALMQAKTLFPNSyLLVGVCSDDLTHKFKGfTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLE 159
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6164927 160 KHKIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FVPTQRTEGISTSDIITR 208
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
77-209 |
3.42e-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: 88.24 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 77 VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTpE 156
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6164927 157 FLEKHKIDFVAHddipyssaGSDDVY--KHIKEAGMFVPT-------QRTEGISTSDIITRI 209
Cdd:COG0615 78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
78-145 |
1.72e-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: 1.72e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6164927 78 RVYADGIFDLFHSGHARALMQAKTLFPnsYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV 145
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02413 |
PLN02413 |
choline-phosphate cytidylyltransferase |
72-314 |
1.93e-106 |
|
choline-phosphate cytidylyltransferase
Pssm-ID: 215229 Cd Length: 294 Bit Score: 314.19 E-value: 1.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 72 PVDRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPW 151
Cdd:PLN02413 23 PSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPW 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 152 TLTPEFLEKHKIDFVAHDDIPY--SSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE 229
Cdd:PLN02413 103 VITQEFLDKHRIDYVAHDALPYadASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNLARGYSRKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 230 LNVSFINEKKYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLElfgpdgawkqMFQERSSR 309
Cdd:PLN02413 183 LGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLE----------KFEEGCHK 252
|
....*
gi 6164927 310 MLQAL 314
Cdd:PLN02413 253 MGTAI 257
|
|
| CCT |
cd02174 |
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ... |
75-224 |
4.34e-96 |
|
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: 282.53 E-value: 4.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 75 RPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 154
Cdd:cd02174 1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 155 PEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRG 224
Cdd:cd02174 81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
71-210 |
1.91e-40 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 146.08 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 71 TPVDRP--VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRD 148
Cdd:PTZ00308 4 IPPKKPgtIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6164927 149 APWTLTPEFLEKHKIDFVAH-DDIPYSSAGsDDVYKHIKEAGMFVPTQRTEGISTSDIITRIV 210
Cdd:PTZ00308 82 YPYTTRLEDLERLECDFVVHgDDISVDLNG-RNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
|
|
| ECT |
cd02173 |
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ... |
79-220 |
3.44e-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: 131.23 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 79 VYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKG--FTVMNEAERYEALRHCRYVDEVIRDAPWTLTPE 156
Cdd:cd02173 5 VYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGsnYPIMNLHERVLSVLACRYVDEVVIGAPYVITKE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6164927 157 FLEKHKIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRN 220
Cdd:cd02173 83 LIEHFKIDVVVHgkTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
80-208 |
2.04e-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: 123.58 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 80 YADGIFDLFHSGHARALMQAKTLFPNSyLLVGVCSDDLTHKFKGfTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLE 159
Cdd:pfam01467 1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLKR-PLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6164927 160 KHKIDFVAHDDIPYSSA--GSDDVYKHIKEAGM-----FVPTQRTEGISTSDIITR 208
Cdd:pfam01467 79 ELNPDVLVIGADSLLDFwyELDEILGNVKLVVVvrpvfFIPLKPTNGISSTDIRER 134
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
75-209 |
1.42e-30 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 120.56 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 75 RPVRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLT 154
Cdd:PLN02406 52 KPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAIT 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6164927 155 PEFL----EKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRI 209
Cdd:PLN02406 130 EEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRM 188
|
|
| PTZ00308 |
PTZ00308 |
ethanolamine-phosphate cytidylyltransferase; Provisional |
72-231 |
1.37e-28 |
|
ethanolamine-phosphate cytidylyltransferase; Provisional
Pssm-ID: 140329 [Multi-domain] Cd Length: 353 Bit Score: 114.11 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 72 PVDRPVRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKG--FTVMNEAERYEALRHCRYVDEVIRDA 149
Cdd:PTZ00308 188 PKPGDRIVYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGsnYPIMNLNERVLGVLSCRYVDEVVIGA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 150 PWTLTPEFLEKHKIDFVAH--DDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRgyTA 227
Cdd:PTZ00308 266 PFDVTKEVIDSLHINVVVGgkFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKK--RA 343
|
....
gi 6164927 228 KELN 231
Cdd:PTZ00308 344 KEIK 347
|
|
| cytidylyltransferase |
cd02170 |
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
76-209 |
4.72e-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: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 76 PVRVYADGIFDLFHSGHARALMQAKTLFpnSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTP 155
Cdd:cd02170 1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6164927 156 EFLEKHKiDFVAHDDIPYSSAGSDDVYKHIKEAGMF--VPTQRTEGISTSDIITRI 209
Cdd:cd02170 79 PLEELKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVieVPRKKTEGISSSDIIKRI 133
|
|
| PLN02406 |
PLN02406 |
ethanolamine-phosphate cytidylyltransferase |
6-236 |
7.44e-25 |
|
ethanolamine-phosphate cytidylyltransferase
Pssm-ID: 215227 [Multi-domain] Cd Length: 418 Bit Score: 104.76 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 6 TDAESETGI-PKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADESSCQCQAPHEKLT---IAQARLGT-PVDRPVRVY 80
Cdd:PLN02406 176 TEGVSSTDIvGRMLLCVRERSISDSHNHSSLQRQFSHGHSQFEDGGSGSGTRVSHFLPTsrrIVQFSNGKgPGPDARIVY 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 81 ADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDL--THKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFL 158
Cdd:PLN02406 256 IDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMI 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 159 EKHKIDFVAHDDIPYSS---AGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKE--LNVS 233
Cdd:PLN02406 334 TTFNISLVVHGTVAENNdflKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEKRyyESKS 413
|
...
gi 6164927 234 FIN 236
Cdd:PLN02406 414 FVS 416
|
|
| TagD |
COG0615 |
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ... |
77-209 |
3.42e-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: 88.24 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 77 VRVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTpE 156
Cdd:COG0615 1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6164927 157 FLEKHKIDFVAHddipyssaGSDDVY--KHIKEAGMFVPT-------QRTEGISTSDIITRI 209
Cdd:COG0615 78 DIEEIKPDVIVL--------GDDWKGdfDFLKEELEKRGIgcevvylPRTEGISSTKIKKRI 131
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
78-145 |
1.72e-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: 1.72e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6164927 78 RVYADGIFDLFHSGHARALMQAKTLFPnsYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV 145
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| G3P_Cytidylyltransferase |
cd02171 |
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ... |
83-205 |
9.03e-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: 64.81 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 83 GIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHK 162
Cdd:cd02171 8 GTFDLLHIGHLNLLERAKAL--GDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6164927 163 ID-FVAHDDIpyssAGSDDVYKHIKEAgMFVPtqRTEGISTSDI 205
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 ... |
75-214 |
2.55e-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: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 75 RPVrVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEV-IRDAPW-- 151
Cdd:cd02172 4 KTV-VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVvLFDNPTal 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6164927 152 ----TLTPEFLEKhKIDFVAHDD--IPYSSAGSDDVYKHikeAGMFVPTQrTEGISTSDIITRIVRDYD 214
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 ... |
61-209 |
1.81e-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: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 61 KLTIAQARL-GTPVdrpvrVYADGIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFT--VMNEAERYEALR 137
Cdd:PRK11316 329 KLAVAQARArGEKI-----VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKGEGrpVNPLEQRMAVLA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6164927 138 HCRYVDEVI---RDAPWTL----TPEFLEK---HKIdfvahDDIpyssAGSDDVYKHIKEAGM--FVptqrtEGISTSDI 205
Cdd:PRK11316 402 ALEAVDWVVpfeEDTPQRLiaeiLPDLLVKggdYKP-----EEI----AGSKEVWANGGEVKVlnFE-----DGCSTTNI 467
|
....
gi 6164927 206 ITRI 209
Cdd:PRK11316 468 IKKI 471
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
83-155 |
6.47e-04 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 39.82 E-value: 6.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6164927 83 GIFDLFHSGHARALMQAKTLfpNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRhcRYVDEVIRDAPWTLTP 155
Cdd:PRK00777 8 GTFDPLHDGHRALLRKAFEL--GKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYEIVK 76
|
|
| |
