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Conserved domains on  [gi|1376910507|ref|XP_002965656|]
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choline-phosphate cytidylyltransferase 2 [Selaginella moellendorffii]

Protein Classification

PLN02413 family protein( domain architecture ID 11476755)

PLN02413 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
89-365 0e+00

choline-phosphate cytidylyltransferase


:

Pssm-ID: 215229  Cd Length: 294  Bit Score: 548.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507  89 PHPSPPPDESSRPTRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVD 168
Cdd:PLN02413   15 GSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 169 EVVEDAPWVITQEFLDKHRIDYVAHDALPYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRNL 248
Cdd:PLN02413   95 EVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 249 ARGYSRKELGVSYVKEKQLQVNMGMRKLRQKVKEQQERVGQRLNTVARTAGMHHSEWVENADRWVSGFLEKFEEGCHVME 328
Cdd:PLN02413  175 ARGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEGCHKMG 254
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1376910507 329 KAIKTRIQTGLMTPRLRKRSTVKLLTNSGSGKALPHN 365
Cdd:PLN02413  255 TAIKDRIQERLMRQQSSGLLELLQNGDVDSDDDDDEY 291
 
Name Accession Description Interval E-value
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
89-365 0e+00

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 548.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507  89 PHPSPPPDESSRPTRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVD 168
Cdd:PLN02413   15 GSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 169 EVVEDAPWVITQEFLDKHRIDYVAHDALPYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRNL 248
Cdd:PLN02413   95 EVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 249 ARGYSRKELGVSYVKEKQLQVNMGMRKLRQKVKEQQERVGQRLNTVARTAGMHHSEWVENADRWVSGFLEKFEEGCHVME 328
Cdd:PLN02413  175 ARGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEGCHKMG 254
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1376910507 329 KAIKTRIQTGLMTPRLRKRSTVKLLTNSGSGKALPHN 365
Cdd:PLN02413  255 TAIKDRIQERLMRQQSSGLLELLQNGDVDSDDDDDEY 291
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
100-251 1.15e-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: 268.67  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 100 RPTRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEVVEDAPWVIT 179
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376910507 180 QEFLDKHRIDYVAHDALPYADTSGasKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRNLARG 251
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADG--EDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
105-235 1.81e-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: 126.28  E-value: 1.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 105 YADGIYDLFHFGHARSLEQAKKLFPNTyLLVGCCSDALTHKYKgKTVMSEAERYESLRHCRWVDEVVEDAPWVITQEFLD 184
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1376910507 185 KHRIDYVAHDALPYADTSGASKDVYHFVKAAG-----KFMETKRTDGVSTSDLIMR 235
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 1.61e-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: 86.98  E-value: 1.61e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376910507 103 RVYADGIYDLFHFGHARSLEQAKKLFPntYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEV 170
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
102-236 3.62e-19

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: 82.46  E-value: 3.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 102 TRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEVVEDAPWVITqE 181
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376910507 182 FLDKHRIDYVAH--------DALpyadtsgasKDVYHFVKAAGKFMETKRTDGVSTSDLIMRI 236
Cdd:COG0615    78 DIEEIKPDVIVLgddwkgdfDFL---------KEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
 
Name Accession Description Interval E-value
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
89-365 0e+00

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 548.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507  89 PHPSPPPDESSRPTRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVD 168
Cdd:PLN02413   15 GSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 169 EVVEDAPWVITQEFLDKHRIDYVAHDALPYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRNL 248
Cdd:PLN02413   95 EVIPDAPWVITQEFLDKHRIDYVAHDALPYADASGAGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMRNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 249 ARGYSRKELGVSYVKEKQLQVNMGMRKLRQKVKEQQERVGQRLNTVARTAGMHHSEWVENADRWVSGFLEKFEEGCHVME 328
Cdd:PLN02413  175 ARGYSRKDLGVSYVKEKRLRVNMGLKKLREKVKEQQEKVGEKIQTVAKTAGMHRNEWVENADRWVAGFLEKFEEGCHKMG 254
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1376910507 329 KAIKTRIQTGLMTPRLRKRSTVKLLTNSGSGKALPHN 365
Cdd:PLN02413  255 TAIKDRIQERLMRQQSSGLLELLQNGDVDSDDDDDEY 291
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
100-251 1.15e-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: 268.67  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 100 RPTRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEVVEDAPWVIT 179
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376910507 180 QEFLDKHRIDYVAHDALPYADTSGasKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRNLARG 251
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADG--EDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRRNLQRG 150
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
91-237 1.06e-42

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 151.86  E-value: 1.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507  91 PSPPPDESSRPTRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEV 170
Cdd:PTZ00308    1 TSPIPPKKPGTIRVWVDGCFDMLHFGHANALRQARAL--GDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376910507 171 VEDAPWVITQEFLDKHRIDYVAHDALPYADTSGasKDVYHFVKAAGKFMETKRTDGVSTSDLIMRII 237
Cdd:PTZ00308   79 VEGYPYTTRLEDLERLECDFVVHGDDISVDLNG--RNSYQEIIDAGKFKVVKRTEGISTTDLVGRML 143
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
101-247 1.99e-36

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: 129.30  E-value: 1.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 101 PTRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKT--VMSEAERYESLRHCRWVDEVVEDAPWVI 178
Cdd:cd02173     2 DKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNypIMNLHERVLSVLACRYVDEVVIGAPYVI 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376910507 179 TQEFLDKHRIDYVAHDALPYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRN 247
Cdd:cd02173    80 TKELIEHFKIDVVVHGKTEETPDSLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARN 148
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
105-235 1.81e-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: 126.28  E-value: 1.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 105 YADGIYDLFHFGHARSLEQAKKLFPNTyLLVGCCSDALTHKYKgKTVMSEAERYESLRHCRWVDEVVEDAPWVITQEFLD 184
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1376910507 185 KHRIDYVAHDALPYADTSGASKDVYHFVKAAG-----KFMETKRTDGVSTSDLIMR 235
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFWYELDEILGNVKLVVvvrpvFFIPLKPTNGISSTDIRER 134
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
91-237 9.93e-30

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 118.25  E-value: 9.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507  91 PSPPPDESS-------RPTRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRH 163
Cdd:PLN02406   36 PYAWPDLGIfkkkkkkKPVRVYMDGCFDMMHYGHANALRQARAL--GDELVVGVVSDEEIIANKGPPVTPMHERMIMVSG 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376910507 164 CRWVDEVVEDAPWVITQEFL----DKHRIDYVAHDALPYADTSGAskDVYHFVKAAGKFMETKRTDGVSTSDLIMRII 237
Cdd:PLN02406  114 VKWVDEVIPDAPYAITEEFMnklfNEYNIDYIIHGDDPCLLPDGT--DAYALAKKAGRYKQIKRTEGVSSTDIVGRML 189
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
92-247 2.66e-25

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 104.87  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507  92 SPPPDEssrpTRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKT--VMSEAERYESLRHCRWVDE 169
Cdd:PTZ00308  187 SPKPGD----RIVYVDGSFDLFHIGHIRVLQKAREL--GDYLIVGVHEDQVVNEQKGSNypIMNLNERVLGVLSCRYVDE 260
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376910507 170 VVEDAPWVITQEFLDKHRIDYVAHDALPYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRN 247
Cdd:PTZ00308  261 VVIGAPFDVTKEVIDSLHINVVVGGKFSDLVNEEGGSDPYEVPKAMGIFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQ 338
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
101-238 1.26e-23

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: 94.67  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 101 PTRVYADGIYDLFHFGHARSLEQAKKLFpnTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEVVEDAPWVITQ 180
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLG--DYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFK 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 181 EFLDKHRiDYVAHDalPYADTSGASKDVYHFVKAAGKFMET--KRTDGVSTSDLIMRIIK 238
Cdd:cd02170    79 PLEELKP-DVIVLG--DDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILE 135
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
103-170 1.61e-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: 86.98  E-value: 1.61e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376910507 103 RVYADGIYDLFHFGHARSLEQAKKLFPntYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEV 170
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD--ELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
102-236 3.62e-19

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: 82.46  E-value: 3.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 102 TRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEVVEDAPWVITqE 181
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKAL--GDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWDKF-E 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376910507 182 FLDKHRIDYVAH--------DALpyadtsgasKDVYHFVKAAGKFMETKRTDGVSTSDLIMRI 236
Cdd:COG0615    78 DIEEIKPDVIVLgddwkgdfDFL---------KEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
104-255 7.04e-19

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 87.43  E-value: 7.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 104 VYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDAL--THKYKGKTVMSEAERYESLRHCRWVDEVVEDAPWVITQE 181
Cdd:PLN02406  254 VYIDGAFDLFHAGHVEILRLARAL--GDFLLVGIHTDQTvsAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376910507 182 FLDKHRIDYVAHDAL-PYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYNEYVMRNLARGYSRK 255
Cdd:PLN02406  332 MITTFNISLVVHGTVaENNDFLKGEDDPYAVPKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESEK 406
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
104-241 1.40e-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: 58.97  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376910507 104 VYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKTVMSEAERYESLRHCRWVDEVV-EDAPWVItqEF 182
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSL--GDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVlFDNPTAL--EI 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376910507 183 LDKHRID-YV-AHD-ALPYADTSGASKDVYHFVKAAGKFMETKRTDGVSTSDLIMRIIKDYN 241
Cdd:cd02172    83 IDALQPNiYVkGGDyENPENDVTGKIAPEAEAVKAYGGKIVFTGEIVFSSSALINRIFDELD 144
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
104-175 1.20e-03

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: 40.58  E-value: 1.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376910507 104 VYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCSDALTHKYKGKT--VMSEAERYESLRHCRWVDEVV---EDAP 175
Cdd:PRK11316  343 VMTNGCFDILHAGHVSYLANARKL--GDRLIVAVNSDASVKRLKGEGrpVNPLEQRMAVLAALEAVDWVVpfeEDTP 417
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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