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Conserved domains on  [gi|115533408|ref|NP_001041227|]
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ethanolamine-phosphate cytidylyltransferase [Caenorhabditis elegans]

Protein Classification

nucleotidyl transferase family protein( domain architecture ID 117)

nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 59-193 6.84e-35

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


The actual alignment was detected with superfamily member cd02173:

Pssm-ID: 469580  Cd Length: 152  Bit Score: 120.83  E-value: 6.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  59 DKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVGVPAVTNS 138
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533408 139 KF-----VNLIRASKIAVYSETH--PRRFADCTYHRIIEEVTPDYDATCEEILERITSRKIA 193
Cdd:cd02173   82 ELiehfkIDVVVHGKTEETPDSLdgEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLA 143
 
Name Accession Description Interval E-value
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 59-193 6.84e-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: 120.83  E-value: 6.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  59 DKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVGVPAVTNS 138
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533408 139 KF-----VNLIRASKIAVYSETH--PRRFADCTYHRIIEEVTPDYDATCEEILERITSRKIA 193
Cdd:cd02173   82 ELiehfkIDVVVHGKTEETPDSLdgEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLA 143
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 52-136 2.27e-31

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 117.19  E-value: 2.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  52 GRKPKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVG 131
Cdd:PTZ00308 185 NRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIG 264


                 ....*.
gi 115533408 132 VP-AVT 136
Cdd:PTZ00308 265 APfDVT 270
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 60-145 3.00e-22

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: 87.47  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGdDDVNEEKGtIFPVMNLLERTLNISSLKIVDEVFVGvpaVTNSK 139
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVAT-DEFVASKG-RKPIIPEEQRKEIVEALKYVDEVILG---EEWDK 75


                 ....*.
gi 115533408 140 FVNLIR 145
Cdd:COG0615   76 FEDIEE 81
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 61-128 5.30e-17

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: 71.95  E-value: 5.30e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533408   61 VVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGtiFPVMNLLERTLNISSLKIVDEV 128
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 66-156 2.83e-10

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: 56.17  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408   66 GAFDLFHAGHLSFLEAAKDLGDY-LIVGIVGDDDVNEEKGTIFPVMnllERTLNISSLKIVDEVFVGVPAVTNSKFVNLI 144
Cdd:pfam01467   4 GTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLKRPLFSAE---ERLEMLELAKWVDEVIVVAPWELTRELLKEL 80

                          90
                  ....*....|..
gi 115533408  145 RASKIAVYSETH 156
Cdd:pfam01467  81 NPDVLVIGADSL 92
 
Name Accession Description Interval E-value
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 59-193 6.84e-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: 120.83  E-value: 6.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  59 DKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVGVPAVTNS 138
Cdd:cd02173    2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533408 139 KF-----VNLIRASKIAVYSETH--PRRFADCTYHRIIEEVTPDYDATCEEILERITSRKIA 193
Cdd:cd02173   82 ELiehfkIDVVVHGKTEETPDSLdgEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLA 143
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 52-136 2.27e-31

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 117.19  E-value: 2.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  52 GRKPKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVG 131
Cdd:PTZ00308 185 NRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIG 264


                 ....*.
gi 115533408 132 VP-AVT 136
Cdd:PTZ00308 265 APfDVT 270
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 60-145 3.00e-22

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: 87.47  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGdDDVNEEKGtIFPVMNLLERTLNISSLKIVDEVFVGvpaVTNSK 139
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVAT-DEFVASKG-RKPIIPEEQRKEIVEALKYVDEVILG---EEWDK 75


                 ....*.
gi 115533408 140 FVNLIR 145
Cdd:COG0615   76 FEDIEE 81
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 52-133 7.02e-21

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 89.36  E-value: 7.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  52 GRKPKVTDKVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFVG 131
Cdd:PLN02406 244 GKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIG 323


                 ..
gi 115533408 132 VP 133
Cdd:PLN02406 324 AP 325
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 62-142 5.26e-19

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: 79.92  E-value: 5.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  62 VYVSGAFDLFHAGHLSFLEAAKDLG--DYLIVGIVGDDDVNEEKGTifPVMNLLERTLNISSLKIVDEVFVGVPAVTNSK 139
Cdd:cd02174    5 VYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82


                 ...
gi 115533408 140 FVN 142
Cdd:cd02174   83 FLD 85
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 60-133 3.85e-17

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: 74.63  E-value: 3.85e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGtiFPVMNLLERTLNISSLKIVDEVFVGVP 133
Cdd:cd02170    2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHP 73
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 61-128 5.30e-17

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: 71.95  E-value: 5.30e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533408   61 VVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGtiFPVMNLLERTLNISSLKIVDEV 128
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKALKYVDEV 66
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 62-142 2.87e-15

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 73.56  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  62 VYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTifPVMNLLERTLNISSLKIVDEVFVGVPAVTNSKFV 141
Cdd:PLN02406  56 VYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFM 133


                 .
gi 115533408 142 N 142
Cdd:PLN02406 134 N 134
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 60-152 3.04e-14

rfaE bifunctional protein, domain II; 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 E. coli, and separate proteins in some other genome. Domain I (TIGR02198) 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. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131254 [Multi-domain]  Cd Length: 144  Bit Score: 66.94  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408   60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVFV---GVPavt 136
Cdd:TIGR02199  12 KIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDYVVIfdeDTP--- 88

                          90
                  ....*....|....*.
gi 115533408  137 nskfVNLIRASKIAVY 152
Cdd:TIGR02199  89 ----EELIGELKPDIL 100
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 53-141 1.48e-13

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 68.27  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  53 RKPKVTDkvVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTifPVMNLLERTLNISSLKIVDEVFVGV 132
Cdd:PTZ00308   7 KKPGTIR--VWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVVEGY 82


                 ....*....
gi 115533408 133 PAVTNSKFV 141
Cdd:PTZ00308  83 PYTTRLEDL 91
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 60-166 9.46e-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: 63.20  E-value: 9.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNeeKGTIFPVMNLLERTLNISSLKIVDEVFVgvpaVTNSK 139
Cdd:cd02172    5 TVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL----FDNPT 78

                         90       100
                 ....*....|....*....|....*..
gi 115533408 140 FVNLIRASKIAVYSETHPRRFADCTYH 166
Cdd:cd02172   79 ALEIIDALQPNIYVKGGDYENPENDVT 105
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 60-175 2.65e-12

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: 64.85  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFPVMNLLERTLNISSLKIVDEVfvgVPavtnsk 139
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVLAALEAVDWV---VP------ 411

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 115533408 140 fvnliraskiavysethprrFADCTYHRIIEEVTPD 175
Cdd:PRK11316 412 --------------------FEEDTPQRLIAEILPD 427
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 60-128 6.56e-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: 60.58  E-value: 6.56e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGiVGDDDVNEEKGTIfPVMNLLERTLNISSLKIVDEV 128
Cdd:cd02171    2 KVVITYGTFDLLHIGHLNLLERAKALGDKLIVA-VSTDEFNAGKGKK-AVIPYEQRAEILESIRYVDLV 68
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 62-142 8.54e-11

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 59.96  E-value: 8.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408  62 VYVSGAFDLFHAGHLSFLEAAKDL--GDYLIVGIVGDDDVNEEKGTIfpVMNLLERTLNISSLKIVDEVFVGVPAVTNSK 139
Cdd:PLN02413  30 VYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDEVIPDAPWVITQE 107


                 ...
gi 115533408 140 FVN 142
Cdd:PLN02413 108 FLD 110
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 66-156 2.83e-10

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: 56.17  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533408   66 GAFDLFHAGHLSFLEAAKDLGDY-LIVGIVGDDDVNEEKGTIFPVMnllERTLNISSLKIVDEVFVGVPAVTNSKFVNLI 144
Cdd:pfam01467   4 GTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPHKLKRPLFSAE---ERLEMLELAKWVDEVIVVAPWELTRELLKEL 80

                          90
                  ....*....|..
gi 115533408  145 RASKIAVYSETH 156
Cdd:pfam01467  81 NPDVLVIGADSL 92
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
60-104 3.37e-04

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 39.43  E-value: 3.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 115533408  60 KVVyVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKG 104
Cdd:PRK00777   3 KVA-VGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKK 46
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
60-108 8.14e-04

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 39.42  E-value: 8.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 115533408  60 KVVYVSGAFDLFHAGHLSFLEAAKDLGDYLIVGIVGDDDVNEEKGTIFP 108
Cdd:PRK01170   1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPIP 49
 
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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