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Conserved domains on  [gi|582517657|gb|EVY09806|]
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glycerol-3-phosphate cytidylyltransferase [Staphylococcus aureus F83251]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 6.65e-68

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: 200.72  E-value: 6.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGqKEDDV 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 582517657  82 EKFDVDVFVMGHDWEGEFDFLKDK-------CEVIYLKRTEGISTTKIKQEL 126
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
 
Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 6.65e-68

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: 200.72  E-value: 6.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGqKEDDV 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 582517657  82 EKFDVDVFVMGHDWEGEFDFLKDK-------CEVIYLKRTEGISTTKIKQEL 126
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-129 4.84e-65

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: 193.47  E-value: 4.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDD 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 582517657  81 VEKFDVDVFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTKIKQELYGK 129
Cdd:cd02171   81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 1.18e-58

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: 177.36  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657    4 VITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEK 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 582517657   84 FDVDVFVMGHDWEGEFDFLKDKC--EVIYLKRTEGISTTKIKQEL 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 5.13e-31

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: 107.41  E-value: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657    5 ITYGTYDLLHYGHIELLRRAREMGDY-LIVALSTDEFNQiKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEK 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPH-KLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 582517657   84 FDVDVFVMGHD--------WEGEFDFLKDKCEV-----IYLKRTEGISTTKIKQ 124
Cdd:pfam01467  80 LNPDVLVIGADslldfwyeLDEILGNVKLVVVVrpvffIPLKPTNGISSTDIRE 133
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-122 2.42e-16

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 73.28  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   3 RVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEfNQIKHK-KSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDV 81
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDE-EIMRNKgPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 582517657  82 EKFDVDVFVMGHD------WEGEFDFLKDKCEVIYLKRTEGISTTKI 122
Cdd:PTZ00308  92 ERLECDFVVHGDDisvdlnGRNSYQEIIDAGKFKVVKRTEGISTTDL 138
 
Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 6.65e-68

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: 200.72  E-value: 6.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGqKEDDV 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 582517657  82 EKFDVDVFVMGHDWEGEFDFLKDK-------CEVIYLKRTEGISTTKIKQEL 126
Cdd:COG0615   80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-129 4.84e-65

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: 193.47  E-value: 4.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDD 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 582517657  81 VEKFDVDVFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTKIKQELYGK 129
Cdd:cd02171   81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 1.18e-58

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: 177.36  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657    4 VITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEK 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 582517657   84 FDVDVFVMGHDWEGEFDFLKDKC--EVIYLKRTEGISTTKIKQEL 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-125 3.79e-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: 3.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQkEDD 80
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSY-FKP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 582517657  81 VEKFDVDVFVMGHDWEG------EFDFLKDKCEVIYL--KRTEGISTTKIKQE 125
Cdd:cd02170   80 LEELKPDVIVLGDDQKNgvdeeeVYEELKKRGKVIEVprKKTEGISSSDIIKR 132
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 5.13e-31

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: 107.41  E-value: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657    5 ITYGTYDLLHYGHIELLRRAREMGDY-LIVALSTDEFNQiKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEK 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPH-KLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 582517657   84 FDVDVFVMGHD--------WEGEFDFLKDKCEV-----IYLKRTEGISTTKIKQ 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 4.42e-24

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: 87.75  E-value: 4.42e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 582517657    3 RVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLV 68
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 3-122 2.06e-16

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: 70.67  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   3 RVITYGTYDLLHYGHIELLRRAREMG--DYLIVALSTDEfNQIKHK-KSYYDYEQRKMMLESIRYVDLVIPEKGWGQKED 79
Cdd:cd02174    4 RVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDE-EIHKHKgPPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 582517657  80 DVEKFDVDVFVMGHD----WEGE--FDFLKDKCEVIYLKRTEGISTTKI 122
Cdd:cd02174   83 FLDKYKCDYVAHGDDiyldADGEdcYQEVKDAGRFKEVKRTEGVSTTDL 131
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-122 2.42e-16

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 73.28  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   3 RVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEfNQIKHK-KSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDV 81
Cdd:PTZ00308  13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDE-EIMRNKgPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 582517657  82 EKFDVDVFVMGHD------WEGEFDFLKDKCEVIYLKRTEGISTTKI 122
Cdd:PTZ00308  92 ERLECDFVVHGDDisvdlnGRNSYQEIIDAGKFKVVKRTEGISTTDL 138
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-124 1.25e-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: 68.24  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   3 RVITYGTYDLLHYGHIELLRRAREMG-DYLIVALSTDEfNQIKHKKSYYDYEQRKMMLESIRY-VDLVIPEKGWGQKEDD 80
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNP-PKKKRNKDPFSLHERVEMLKEILKdRLKVVPVDFPEVKILL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 582517657  81 V--------EKFDVDVFVMGHDWEGEFD--------FLKDKCEVIYLKRTEG---ISTTKIKQ 124
Cdd:cd02039   80 AvvfilkilLKVGPDKVVVGEDFAFGKNasynkdlkELFLDIEIVEVPRVRDgkkISSTLIRE 142
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 5-92 1.41e-13

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: 63.05  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   5 ITY--GTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQiKHKKSYY---DYEQRKMMLESIRYVDLVIPEKGWGQKED 79
Cdd:cd02173    4 VVYvdGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVN-EYKGSNYpimNLHERVLSVLACRYVDEVVIGAPYVITKE 82

                         90
                 ....*....|...
gi 582517657  80 DVEKFDVDVFVMG 92
Cdd:cd02173   83 LIEHFKIDVVVHG 95
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-121 4.52e-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: 60.63  E-value: 4.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   4 VITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNqiKHKKSYYDYEQRKMMLESiryvdlvipekgwgqkeddvek 83
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPV--KVWQDPHELEERKESIEE---------------------- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 582517657  84 fdvDVFVMGHDWEGEFD---------FLKDKCEVIYLKR----TEGISTTK 121
Cdd:cd02156   58 ---DISVCGEDFQQNRElyrwvkdniTLPVDPEQVELPRlnleTTVMSKRK 105
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 4-94 5.74e-13

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 64.04  E-value: 5.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   4 VITY--GTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSY--YDYEQRKMMLESIRYVDLVIPEKGWGQKED 79
Cdd:PTZ00308 193 RIVYvdGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYpiMNLNERVLGVLSCRYVDEVVIGAPFDVTKE 272

                         90
                 ....*....|....*
gi 582517657  80 DVEKFDVDVFVMGHD 94
Cdd:PTZ00308 273 VIDSLHINVVVGGKF 287
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 3-122 1.18e-12

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 63.16  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   3 RVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDV- 81
Cdd:PLN02406  55 RVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMn 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 582517657  82 ---EKFDVDVFVMGHD------WEGEFDFLKDKCEVIYLKRTEGISTTKI 122
Cdd:PLN02406 135 klfNEYNIDYIIHGDDpcllpdGTDAYALAKKAGRYKQIKRTEGVSSTDI 184
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 8-117 5.83e-12

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 61.24  E-value: 5.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   8 GTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSY--YDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEKFD 85
Cdd:PLN02406 258 GAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRpiMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFN 337

                         90       100       110
                 ....*....|....*....|....*....|..
gi 582517657  86 VDVFVMGHDWEGEfDFLKDKCEVIYLKRTEGI 117
Cdd:PLN02406 338 ISLVVHGTVAENN-DFLKGEDDPYAVPKSMGI 368
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
1-74 3.99e-11

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 56.76  E-value: 3.99e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 582517657   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLEsiRYVDLVIPEKGW 74
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREY 72
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 4-96 5.97e-11

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: 56.27  E-value: 5.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   4 VITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKgWGQKEDDVEK 83
Cdd:cd02172    7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVVLFD-NPTALEIIDA 85

                         90
                 ....*....|...
gi 582517657  84 FDVDVFVMGHDWE 96
Cdd:cd02172   86 LQPNIYVKGGDYE 98
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 2-122 4.31e-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: 55.99  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDE-----------FNQIkhkksyydyEQRKMMLESIRYVDLVIP 70
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDAsvkrlkgegrpVNPL---------EQRMAVLAALEAVDWVVP 411

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582517657  71 ekgwgQKEDDVEKF--DV--DVFVMGHDWEGEfDFLKDKC------EVIYLKRTEGISTTKI 122
Cdd:PRK11316 412 -----FEEDTPQRLiaEIlpDLLVKGGDYKPE-EIAGSKEvwanggEVKVLNFEDGCSTTNI 467
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 3-122 1.50e-09

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 54.18  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582517657   3 RVITYGTYDLLHYGHIELLRRAREM--GDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDD 80
Cdd:PLN02413  29 RVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWVITQEF 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 582517657  81 VEKFDVDvfVMGHD----------WEGEFDFLKDKCEVIYLKRTEGISTTKI 122
Cdd:PLN02413 109 LDKHRID--YVAHDalpyadasgaGKDVYEFVKKIGKFKETKRTDGISTSDI 158
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
2-60 1.78e-08

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 51.36  E-value: 1.78e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 582517657   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQiKHKKSYYDYEQRKMMLE 60
Cdd:PRK01170   1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVR-KNKVYPIPYEDRKRKLE 58
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 8-60 1.90e-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: 44.38  E-value: 1.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 582517657   8 GTYDLLHYGHIELLRRAREMGDYLIVALSTDefnqiKHKKSYYDYEQRKMMLE 60
Cdd:cd02163    6 GSFDPITNGHLDIIERASKLFDEVIVAVAVN-----PSKKPLFSLEERVELIR 53
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 8-71 3.14e-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: 40.73  E-value: 3.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 582517657   8 GTYDLLHYGHIELLRRAREMG-DYLIVALSTDEFNQikhKKSYYD----YEQRKMMLEsiRYVDLVIPE 71
Cdd:cd02164    6 GTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLK---NKSLKEliepYEERIANLH--EFLVDLKPT 69
 
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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