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Conserved domains on  [gi|662063701|ref|WP_030029417|]
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MULTISPECIES: glycerol-3-phosphate cytidylyltransferase [Bacillus]

Protein Classification

nucleotidyl transferase family protein; glutamine/glutamate--tRNA ligase( domain architecture ID 10114953)

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| glutamine/glutamate--tRNA ligase catalyzes the attachment of glutamate or glutamine to tRNA(Glu) or tRNA(Gln); in some organisms, the non-discriminating form of glutamate--tRNA ligase aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-128 1.64e-71

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: 209.65  E-value: 1.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   1 MRRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIED 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 662063701  81 IVKYEIDIFVMGDDWEGKFDFLKEYCEVIYLPRTEDISTTQIKSELSL 128
Cdd:cd02171   81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKK 128
 
Name Accession Description Interval E-value
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-128 1.64e-71

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: 209.65  E-value: 1.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   1 MRRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIED 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 662063701  81 IVKYEIDIFVMGDDWEGKFDFLKEYCEVIYLPRTEDISTTQIKSELSL 128
Cdd:cd02171   81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKK 128
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 1.51e-69

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: 204.95  E-value: 1.51e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   2 RRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEqKIEDI 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 662063701  82 VKYEIDIFVMGDDWEGKFDFLKEY-------CEVIYLPRTEDISTTQIKSEL 126
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 3.46e-63

glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate cytidyltransferase, also called CDP-glycerol pyrophosphorylase. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14). 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. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 130581 [Multi-domain]  Cd Length: 125  Bit Score: 188.54  E-value: 3.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701    4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIEDIVK 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 662063701   84 YEIDIFVMGDDWEGKFDFLKEYC--EVIYLPRTEDISTTQIKSEL 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-123 1.22e-28

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: 101.24  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701    5 LTYGTFDLLHYGHINLVRRAKDLGDY-LIVGLSTDEFNAlKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIEDIVK 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPH-KLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 662063701   84 YEIDIFVMGDD--------WEGKFDFLKEYCEV-----IYLPRTEDISTTQIK 123
Cdd:pfam01467  80 LNPDVLVIGADslldfwyeLDEILGNVKLVVVVrpvffIPLKPTNGISSTDIR 132
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-122 4.45e-18

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 78.29  E-value: 4.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDE-FNALKGKESYFKfEERKMLLESIRYVDLVISENTWEQKIEDI 81
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEeIMRNKGPPVMHQ-EERYEALRACKWVDEVVEGYPYTTRLEDL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 662063701  82 VKYEIDIFVMGDDWEGKFDFLKEYCEVI------YLPRTEDISTTQI 122
Cdd:PTZ00308  92 ERLECDFVVHGDDISVDLNGRNSYQEIIdagkfkVVKRTEGISTTDL 138
 
Name Accession Description Interval E-value
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-128 1.64e-71

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: 209.65  E-value: 1.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   1 MRRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIED 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 662063701  81 IVKYEIDIFVMGDDWEGKFDFLKEYCEVIYLPRTEDISTTQIKSELSL 128
Cdd:cd02171   81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKK 128
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 1.51e-69

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: 204.95  E-value: 1.51e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   2 RRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEqKIEDI 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 662063701  82 VKYEIDIFVMGDDWEGKFDFLKEY-------CEVIYLPRTEDISTTQIKSEL 126
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 3.46e-63

glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate cytidyltransferase, also called CDP-glycerol pyrophosphorylase. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14). 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. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 130581 [Multi-domain]  Cd Length: 125  Bit Score: 188.54  E-value: 3.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701    4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIEDIVK 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 662063701   84 YEIDIFVMGDDWEGKFDFLKEYC--EVIYLPRTEDISTTQIKSEL 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-125 3.52e-37

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: 123.17  E-value: 3.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   1 MRRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLVI--SENTWEQKI 78
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVIlgHPWSYFKPL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 662063701  79 EDIVKyeiDIFVMGDDWEG------KFDFLKEYCEVIYLPR--TEDISTTQIKSE 125
Cdd:cd02170   81 EELKP---DVIVLGDDQKNgvdeeeVYEELKKRGKVIEVPRkkTEGISSSDIIKR 132
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-123 1.22e-28

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: 101.24  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701    5 LTYGTFDLLHYGHINLVRRAKDLGDY-LIVGLSTDEFNAlKGKESYFKFEERKMLLESIRYVDLVISENTWEQKIEDIVK 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPH-KLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 662063701   84 YEIDIFVMGDD--------WEGKFDFLKEYCEV-----IYLPRTEDISTTQIK 123
Cdd:pfam01467  80 LNPDVLVIGADslldfwyeLDEILGNVKLVVVVrpvffIPLKPTNGISSTDIR 132
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 3-68 1.32e-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: 81.20  E-value: 1.32e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 662063701    3 RVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLESIRYVDLV 68
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 4-122 2.04e-21

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: 83.12  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701    4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDE-FNALKGKESYFKFEERKM-LLESIRYVDLVI--SENTWEQKIE 79
Cdd:TIGR02199  14 VFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDAsVKRLKGETRPINPEEDRAeVLAALSSVDYVVifDEDTPEELIG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 662063701   80 DIvkyEIDIFVMGDDWEGK----FDFLKEY-CEVIYLPRTEDISTTQI 122
Cdd:TIGR02199  94 EL---KPDILVKGGDYKVEtlvgAELVESYgGQVVLLPFVEGRSTTAI 138
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 2-122 4.34e-20

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: 4.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   2 RRVLTYGTFDLLHYGHINLVRRAKDLG--DYLIVGLSTDE-FNALKGKESYfKFEERKMLLESIRYVDLVISENTWEQKI 78
Cdd:cd02174    3 VRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEeIHKHKGPPVM-TEEERYEAVRHCKWVDEVVEGAPYVTTP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 662063701  79 EDIVKYEIDIFVMGDD----WEGK--FDFLKEYCEVIYLPRTEDISTTQI 122
Cdd:cd02174   82 EFLDKYKCDYVAHGDDiyldADGEdcYQEVKDAGRFKEVKRTEGVSTTDL 131
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-122 4.45e-18

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 78.29  E-value: 4.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDE-FNALKGKESYFKfEERKMLLESIRYVDLVISENTWEQKIEDI 81
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEeIMRNKGPPVMHQ-EERYEALRACKWVDEVVEGYPYTTRLEDL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 662063701  82 VKYEIDIFVMGDDWEGKFDFLKEYCEVI------YLPRTEDISTTQI 122
Cdd:PTZ00308  92 ERLECDFVVHGDDISVDLNGRNSYQEIIdagkfkVVKRTEGISTTDL 138
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 3-94 1.70e-15

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 71.25  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDLGDYLIVG-LSTDEFNALKGKeSYFKFEERKMLLESIRYVDLVISENTWEQKiEDI 81
Cdd:PLN02406  55 RVYMDGCFDMMHYGHANALRQARALGDELVVGvVSDEEIIANKGP-PVTPMHERMIMVSGVKWVDEVIPDAPYAIT-EEF 132

                         90
                 ....*....|....*...
gi 662063701  82 V-----KYEIDIFVMGDD 94
Cdd:PLN02406 133 MnklfnEYNIDYIIHGDD 150
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-123 4.08e-15

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. 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.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 67.08  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDLG-DYLIVGLSTDEfNALKGKESYFKFEERKMLLE----SIRYVDLV----ISENT 73
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNP-PKKKRNKDPFSLHERVEMLKeilkDRLKVVPVdfpeVKILL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 662063701  74 WEQKI-EDIVKYEIDIFVMGDDWEGKFD--------FLKEYCEVIYLPRTED---ISTTQIK 123
Cdd:cd02039   80 AVVFIlKILLKVGPDKVVVGEDFAFGKNasynkdlkELFLDIEIVEVPRVRDgkkISSTLIR 141
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 8-122 1.33e-14

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: 65.74  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   8 GTFDLLHYGHINLVRRAKDLGDYLIVGLSTDE-FNALKGKE-SYFKFEERKMLLESIRYVDLVISENTWEQKIEDIVKYE 85
Cdd:cd02173    9 GAFDLFHIGHIEFLEKARELGDYLIVGVHDDQtVNEYKGSNyPIMNLHERVLSVLACRYVDEVVIGAPYVITKELIEHFK 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 662063701  86 IDIFVMG-----DDWEGKFDFLKE------YCEViylPRTEDISTTQI 122
Cdd:cd02173   89 IDVVVHGkteetPDSLDGEDPYAVpkemgiFKEI---DSGSDLTTRDI 133
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-116 5.53e-14

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.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 62.94  E-value: 5.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNalKGKESYFKFEERKMLLESiryvdlvisentweqkiedivk 83
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPV--KVWQDPHELEERKESIEE---------------------- 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 662063701  84 yeiDIFVMGDDWEGKFD---------FLKEYCEVIYLPRTED 116
Cdd:cd02156   58 ---DISVCGEDFQQNRElyrwvkdniTLPVDPEQVELPRLNL 96
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 4-96 8.25e-14

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: 63.59  E-value: 8.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEF-NALKGKeSYFKFEERKMLLESIRYVD--LVISENTWEQKIED 80
Cdd:cd02172    7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYvNKGPGR-PIFPEDLRAEVLAALGFVDyvVLFDNPTALEIIDA 85

                         90
                 ....*....|....*.
gi 662063701  81 IvkyEIDIFVMGDDWE 96
Cdd:cd02172   86 L---QPNIYVKGGDYE 98
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
1-80 8.21e-13

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 61.00  E-value: 8.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   1 MRRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESYFKFEERKMLLEsiRYVDLVISENTWE-QKIE 79
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYEiVKID 78


                 .
gi 662063701  80 D 80
Cdd:PRK00777  79 D 79
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-94 1.77e-12

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 62.50  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   8 GTFDLLHYGHINLVRRAKDLGDYLIVGLSTDE-FNALKGKE-SYFKFEERKMLLESIRYVDLVISENTWEQKIEDIVKYE 85
Cdd:PTZ00308 199 GSFDLFHIGHIRVLQKARELGDYLIVGVHEDQvVNEQKGSNyPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLH 278


                 ....*....
gi 662063701  86 IDIFVMGDD 94
Cdd:PTZ00308 279 INVVVGGKF 287
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 2-117 2.50e-12

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 62.39  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   2 RRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNALKGKESY--FKFEERKMLLESIRYVDLVISENTWEQKIE 79
Cdd:PLN02406 252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRpiMNLHERSLSVLACRYVDEVIIGAPWEVSKD 331

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 662063701  80 DIVKYEIDIFVMGDDWEGKfDFLKEYCEVIYLPRTEDI 117
Cdd:PLN02406 332 MITTFNISLVVHGTVAENN-DFLKGEDDPYAVPKSMGI 368
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 4-122 3.61e-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: 61.77  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDE-FNALKGKESYFKFEERKM-LLESIRYVDLVI--SENTWEQKIE 79
Cdd:PRK11316 343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDAsVKRLKGEGRPVNPLEQRMaVLAALEAVDWVVpfEEDTPQRLIA 422

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 662063701  80 DIVKyeiDIFVMGDDWE-----GKfDFLKEY-CEVIYLPRTEDISTTQI 122
Cdd:PRK11316 423 EILP---DLLVKGGDYKpeeiaGS-KEVWANgGEVKVLNFEDGCSTTNI 467
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 3-122 2.13e-09

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 53.80  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDL--GDYLIVGLSTDEF-NALKGKeSYFKFEERKMLLESIRYVDLVISENTWEQKIE 79
Cdd:PLN02413  29 RVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELtHKYKGK-TVMTEDERYESLRHCKWVDEVIPDAPWVITQE 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 662063701  80 DIVKYEIDiFVMGD-----DWEGK----FDFLKEYCEVIYLPRTEDISTTQI 122
Cdd:PLN02413 108 FLDKHRID-YVAHDalpyaDASGAgkdvYEFVKKIGKFKETKRTDGISTSDI 158
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
3-60 2.24e-08

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 50.97  E-value: 2.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFNAlKGKESYFKFEERKMLLE 60
Cdd:PRK01170   2 ITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVR-KNKVYPIPYEDRKRKLE 58
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-60 3.00e-08

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 49.23  E-value: 3.00e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   1 MRRVLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEfnalkGKESYFKFEERKMLLE 60
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNP-----SKKPLFSLEERVELIR 55
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 8-60 4.74e-08

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 48.62  E-value: 4.74e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 662063701   8 GTFDLLHYGHINLVRRAKDLGDYLIVGLSTDefnalKGKESYFKFEERKMLLE 60
Cdd:cd02163    6 GSFDPITNGHLDIIERASKLFDEVIVAVAVN-----PSKKPLFSLEERVELIR 53
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 8-60 2.14e-07

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 46.88  E-value: 2.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 662063701    8 GTFDLLHYGHINLVRRAKDLGDYLIVGLSTDefnalKGKESYFKFEERKMLLE 60
Cdd:TIGR01510   6 GSFDPVTNGHLDIIKRAAALFDEVIVAVAKN-----PSKKPLFSLEERVELIK 53
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 3-86 4.24e-06

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: 43.04  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   3 RVLTYGTFDLLHYGHINLVRRAKDLG-DYLIVGLSTDEFNALKG-KESYFKFEERKMLLEsiRYVDlvisentweqKIED 80
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLKNKSlKELIEPYEERIANLH--EFLV----------DLKP 68


                 ....*.
gi 662063701  81 IVKYEI 86
Cdd:cd02164   69 TLKYEI 74
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 4-127 8.12e-03

FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.


Pssm-ID: 185679 [Multi-domain]  Cd Length: 180  Bit Score: 34.44  E-value: 8.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662063701   4 VLTYGTFDLLHYGHINLVRRAKDLGDYLIVGLSTDEFN----ALKGKESYFKF----EERKMLLES--IRYVDLV----- 68
Cdd:cd02064    2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDphprEVFLPDKAPPRlttlEEKLELLESlgVDYLLVLpfdke 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 662063701  69 ISENTWEQKIEDI-VKYEIDIFVMGDDW------EGKFDFLKEYC-----EVIYLP----RTEDISTTQIKSELS 127
Cdd:cd02064   82 FASLSAEEFVEDLlVKLNAKHVVVGFDFrfgkgrSGDAELLKELGkkygfEVTVVPpvtlDGERVSSTRIREALA 156
 
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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