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Conserved domains on  [gi|2188917743|gb|UKH31398|]
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glycerol-3-phosphate cytidylyltransferase [Actinobacillus pleuropneumoniae serovar 11 str. 56153]

Protein Classification

nucleotidyl transferase family protein; 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; glutamate--tRNA ligase catalyzes the attachment of glutamate to tRNA(Glu)

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, ...
 1-129 1.40e-82

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: 238.15  E-value: 1.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVED 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2188917743  81 VKNHEIDVFVMGDDWEGKFDFLADYCEVVYLPRTPDISTTQVKKMLAKK 129
Cdd:cd02171    81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
 
Name Accession Description Interval E-value
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-129 1.40e-82

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: 238.15  E-value: 1.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVED 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2188917743  81 VKNHEIDVFVMGDDWEGKFDFLADYCEVVYLPRTPDISTTQVKKMLAKK 129
Cdd:cd02171    81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 5.79e-67

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: 198.79  E-value: 5.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   2 KKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEqKVEDV 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2188917743  82 KNHEIDVFVMGDDWEGKFDFLADY-------CEVVYLPRTPDISTTQVKKML 126
Cdd:COG0615    80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 6.75e-60

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: 180.83  E-value: 6.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   4 VLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKN 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2188917743  84 HEIDVFVMGDDWEGKFDFLADYC--EVVYLPRTPDISTTQVKKML 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 3.88e-27

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: 98.16  E-value: 3.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   5 LTYGTFDLLHHGHIRLLERARSLGDH-LTVAISTDQFNlGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKN 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPP-HKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2188917743  84 HEIDVFVMGDD--------WEGKFDFLADYCEVV-----YLPRTPDISTTQVKK 124
Cdd:pfam01467  80 LNPDVLVIGADslldfwyeLDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRE 133
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-126 6.99e-15

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 69.81  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKNHEID 87
Cdd:PTZ00308   18 GCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECD 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2188917743  88 VFVMGDDWEGKFDFLADYCEVV------YLPRTPDISTTQ-VKKML 126
Cdd:PTZ00308   98 FVVHGDDISVDLNGRNSYQEIIdagkfkVVKRTEGISTTDlVGRML 143
 
Name Accession Description Interval E-value
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-129 1.40e-82

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: 238.15  E-value: 1.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVED 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2188917743  81 VKNHEIDVFVMGDDWEGKFDFLADYCEVVYLPRTPDISTTQVKKMLAKK 129
Cdd:cd02171    81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 5.79e-67

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: 198.79  E-value: 5.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   2 KKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEqKVEDV 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2188917743  82 KNHEIDVFVMGDDWEGKFDFLADY-------CEVVYLPRTPDISTTQVKKML 126
Cdd:COG0615    80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 6.75e-60

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: 180.83  E-value: 6.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   4 VLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKN 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2188917743  84 HEIDVFVMGDDWEGKFDFLADYC--EVVYLPRTPDISTTQVKKML 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-124 1.95e-34

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: 116.62  E-value: 1.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIP--ETNWEQKV 78
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILghPWSYFKPL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2188917743  79 EDVKNheiDVFVMGDDWEG------KFDFLADYCEVVYLPR--TPDISTTQVKK 124
Cdd:cd02170    81 EELKP---DVIVLGDDQKNgvdeeeVYEELKKRGKVIEVPRkkTEGISSSDIIK 131
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 3.88e-27

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: 98.16  E-value: 3.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   5 LTYGTFDLLHHGHIRLLERARSLGDH-LTVAISTDQFNlGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKN 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPP-HKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2188917743  84 HEIDVFVMGDD--------WEGKFDFLADYCEVV-----YLPRTPDISTTQVKK 124
Cdd:pfam01467  80 LNPDVLVIGADslldfwyeLDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRE 133
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 3-68 2.62e-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: 78.50  E-value: 2.62e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2188917743   3 KVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEV 68
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 8-94 2.44e-17

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: 73.37  E-value: 2.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLG--DHLTVAISTDQ-FNLGKGKVcAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKNH 84
Cdd:cd02174     9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEeIHKHKGPP-VMTEEERYEAVRHCKWVDEVVEGAPYVTTPEFLDKY 87

                          90
                  ....*....|
gi 2188917743  85 EIDVFVMGDD 94
Cdd:cd02174    88 KCDYVAHGDD 97
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-125 7.30e-17

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: 71.70  E-value: 7.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   3 KVLTYGTFDLLHHGHIRLLERARSLG-DHLTVAISTDQFNLGKGKvCAYTYEERAHILKAIRY-VDEVIPETNWEQK--- 77
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKRNK-DPFSLHERVEMLKEILKdRLKVVPVDFPEVKill 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2188917743  78 -----VEDVKNHEIDVFVMGDDWEGKFD--------FLADYCEVVYLPR---TPDISTTQVKKM 125
Cdd:cd02039    80 avvfiLKILLKVGPDKVVVGEDFAFGKNasynkdlkELFLDIEIVEVPRvrdGKKISSTLIREL 143
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 2-126 1.32e-16

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: 71.18  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   2 KKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQ-FNLGKGKVCAYTYEE-RAHILKAIRYVDEVI--PETNWEQK 77
Cdd:TIGR02199  12 KIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDAsVKRLKGETRPINPEEdRAEVLAALSSVDYVVifDEDTPEEL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2188917743  78 VEDVKNheiDVFVMGDDWEGK----FDFLADY-CEVVYLPRTPDISTTQ-VKKML 126
Cdd:TIGR02199  92 IGELKP---DILVKGGDYKVEtlvgAELVESYgGQVVLLPFVEGRSTTAiIEKIL 143
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 4-96 1.11e-15

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: 68.98  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   4 VLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQF-NLGKGKVcAYTYEERAHILKAIRYVDEVI--PETNWEQKVED 80
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYvNKGPGRP-IFPEDLRAEVLAALGFVDYVVlfDNPTALEIIDA 85

                          90
                  ....*....|....*.
gi 2188917743  81 VKNheiDVFVMGDDWE 96
Cdd:cd02172    86 LQP---NIYVKGGDYE 98
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-126 6.99e-15

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 69.81  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKNHEID 87
Cdd:PTZ00308   18 GCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLECD 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2188917743  88 VFVMGDDWEGKFDFLADYCEVV------YLPRTPDISTTQ-VKKML 126
Cdd:PTZ00308   98 FVVHGDDISVDLNGRNSYQEIIdagkfkVVKRTEGISTTDlVGRML 143
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 3-116 1.75e-13

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: 62.17  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   3 KVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNlgKGKVCAYTYEERAHILKAiryvdevipetnweqkvedvk 82
Cdd:cd02156     1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPV--KVWQDPHELEERKESIEE--------------------- 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2188917743  83 nheiDVFVMGDDWEGKFD---------FLADYCEVVYLPRTPD 116
Cdd:cd02156    58 ----DISVCGEDFQQNRElyrwvkdniTLPVDPEQVELPRLNL 96
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 2-94 8.48e-13

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 63.93  E-value: 8.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   2 KKVLTY--GTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKAIRYVDEVIPETNWEQKVE 79
Cdd:PLN02406   52 KPVRVYmdGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEE 131

                          90
                  ....*....|....*....
gi 2188917743  80 DVKN----HEIDVFVMGDD 94
Cdd:PLN02406  132 FMNKlfneYNIDYIIHGDD 150
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
1-75 1.25e-12

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 61.00  E-value: 1.25e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFNLGKGKVCAYTYEERAHILKaiRYVDEVIPETNWE 75
Cdd:PRK00777    1 MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREYE 73
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 8-117 8.48e-12

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 61.24  E-value: 8.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDQF---NLGKGKVCAYTYEERAHILkAIRYVDEVIPETNWEQKVEDVKNH 84
Cdd:PLN02406  258 GAFDLFHAGHVEILRLARALGDFLLVGIHTDQTvsaHRGAHRPIMNLHERSLSVL-ACRYVDEVIIGAPWEVSKDMITTF 336

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2188917743  85 EIDVFVMGDDWEGKfDFLADYCEVVYLPRTPDI 117
Cdd:PLN02406  337 NISLVVHGTVAENN-DFLKGEDDPYAVPKSMGI 368
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-94 1.07e-11

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 60.95  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDQ-FNLGKGK-VCAYTYEERAHILKAIRYVDEVIPETNWEQKVEDVKNHE 85
Cdd:PTZ00308  199 GSFDLFHIGHIRVLQKARELGDYLIVGVHEDQvVNEQKGSnYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLH 278


                  ....*....
gi 2188917743  86 IDVFVMGDD 94
Cdd:PTZ00308  279 INVVVGGKF 287
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 8-94 1.13e-11

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: 58.42  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDQ-FNLGKGK---VCayTYEERAHILKAIRYVDEVIPETNWEQKVEDVKN 83
Cdd:cd02173     9 GAFDLFHIGHIEFLEKARELGDYLIVGVHDDQtVNEYKGSnypIM--NLHERVLSVLACRYVDEVVIGAPYVITKELIEH 86

                          90
                  ....*....|.
gi 2188917743  84 HEIDVFVMGDD 94
Cdd:cd02173    87 FKIDVVVHGKT 97
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 2-95 7.62e-10

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: 55.61  E-value: 7.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   2 KKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQF--NLgKGK---VcaYTYEERAHILKAIRYVDEVIP--ETNW 74
Cdd:PRK11316  341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASvkRL-KGEgrpV--NPLEQRMAVLAALEAVDWVVPfeEDTP 417

                          90       100
                  ....*....|....*....|.
gi 2188917743  75 EQKVEDVKNheiDVFVMGDDW 95
Cdd:PRK11316  418 QRLIAEILP---DLLVKGGDY 435
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 3-87 3.25e-09

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 53.41  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   3 KVLTYGTFDLLHHGHIRLLERARSL--GDHLTVAISTDQF-NLGKGKVcAYTYEERAHILKAIRYVDEVIPETNWEQKVE 79
Cdd:PLN02413   29 RVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELtHKYKGKT-VMTEDERYESLRHCKWVDEVIPDAPWVITQE 107


                  ....*...
gi 2188917743  80 DVKNHEID 87
Cdd:PLN02413  108 FLDKHRID 115
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-107 8.00e-07

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: 45.76  E-value: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDqfnlgKGKVCAYTYEERAHILKAIryvdevipetnweqkVED 80
Cdd:COG0669     1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVN-----PSKKPLFSLEERVELIREA---------------LAD 60

                          90       100
                  ....*....|....*....|....*..
gi 2188917743  81 VKNHEIDVFvmgddwEGkfdFLADYCE 107
Cdd:COG0669    61 LPNVEVDSF------DG---LLVDFAR 78
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
2-55 1.18e-06

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 46.35  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2188917743   2 KKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFnLGKGKVCAYTYEER 55
Cdd:PRK01170    1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEY-VRKNKVYPIPYEDR 53
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 8-107 4.21e-06

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: 43.61  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDqfnlgKGKVCAYTYEERAHILkairyvdevipetnwEQKVEDVKNHEID 87
Cdd:cd02163     6 GSFDPITNGHLDIIERASKLFDEVIVAVAVN-----PSKKPLFSLEERVELI---------------REATKHLPNVEVD 65

                          90       100
                  ....*....|....*....|
gi 2188917743  88 VFVmgddwegkfDFLADYCE 107
Cdd:cd02163    66 GFD---------GLLVDFAR 76
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 8-130 6.47e-06

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: 43.03  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   8 GTFDLLHHGHIRLLERARSLGDHLTVAISTDqfnlgKGKVCAYTYEERAHILK-AIRYVDEVIPETNWEQKVEDVKNHEI 86
Cdd:TIGR01510   6 GSFDPVTNGHLDIIKRAAALFDEVIVAVAKN-----PSKKPLFSLEERVELIKdATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2188917743  87 DVFVMG----DDWEGKFDF------LADYCEVVYLPRTPD---ISTTQVKKMLAKKD 130
Cdd:TIGR01510  81 TFIVRGlraaTDFEYELQMalmnkhLAPEIETVFLMASPEyafVSSSLVKEIASFGG 137
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 3-69 2.23e-05

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: 41.50  E-value: 2.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2188917743   3 KVLTYGTFDLLHHGHIRLLERARSLG-DHLTVAISTDQFNLGKG-KVCAYTYEERahilkaIRYVDEVI 69
Cdd:cd02164     1 KVAVGGTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLKNKSlKELIEPYEER------IANLHEFL 63
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-128 5.39e-04

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 37.87  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188917743   1 MKKVLTYGTFDLLHHGHIRLLERARSLGDHLTVAISTDQFnlgkgkvcAY------TYEERAH-ILKAIRYVD----EVI 69
Cdd:COG1056     2 MKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIGSAQE--------SHtprnpfTAGERIEmIRAALKEEGlsrvYIV 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2188917743  70 P---ETNWEQKVEDVKN--HEIDVFVMGDDWEGKFDFLADYcEVVYLP--RTPDISTTQVKKMLAK 128
Cdd:COG1056    74 PipdINNNSLWVSHVKSlvPPFDVVYSNNPLVGRLFKEAGY-EVLLPPlfEREEYSGTEIRRLMLE 138
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 1-38 3.11e-03

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;


Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 36.56  E-value: 3.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2188917743   1 MKKV-LTYGTFDLLHHGHIRLLERARSLGDHLTVAISTD 38
Cdd:PRK08099   51 MKKIgVVFGKFYPLHTGHIYLIQRACSQVDELHIIICYD 89
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 5-38 4.66e-03

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase


Pssm-ID: 173918  Cd Length: 158  Bit Score: 35.16  E-value: 4.66e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2188917743   5 LTYGTFDLLHHGHIRLLERARSLGDHLTVAISTD 38
Cdd:cd02167     3 IVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSD 36
 
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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